data_9I6A
# 
_entry.id   9I6A 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_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   9I6A         pdb_00009i6a 10.2210/pdb9i6a/pdb 
WWPDB D_1292145041 ?            ?                   
# 
_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       2025-02-12 
# 
_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                        9I6A 
_pdbx_database_status.recvd_initial_deposition_date   2025-01-29 
_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              lsi10@cam.ac.uk 
_pdbx_contact_author.name_first         Itzhaki 
_pdbx_contact_author.name_last          Laura 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-6504-2576 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Eapen, R.'         1  0000-0001-7269-3633 
'Okoye, C.'         2  ?                   
'Stubbs, C.'        3  ?                   
'Schimpl, M.'       4  0000-0003-2284-5250 
'Tischer, T.'       5  ?                   
'Fisher, E.J.'      6  ?                   
'Zacharopoulou, M.' 7  ?                   
'Ferrer, F.'        8  ?                   
'Barford, D.'       9  ?                   
'Spring, D.'        10 ?                   
'Lindon, C.'        11 ?                   
'Phillips, C.'      12 ?                   
'Itzhaki, L.S.'     13 0000-0001-6504-2576 
# 
_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                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To be published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'Development of D-box peptides to inhibit the Anaphase Promoting Complex/Cyclosome' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Eapen, R.'         1  0000-0001-7269-3633 
primary 'Okoye, C.'         2  ?                   
primary 'Stubbs, C.'        3  ?                   
primary 'Schimpl, M.'       4  0000-0003-2284-5250 
primary 'Tischer, T.'       5  ?                   
primary 'Fisher, E.J.'      6  ?                   
primary 'Zacharopoulou, M.' 7  ?                   
primary 'Ferrer, F.'        8  ?                   
primary 'Barford, D.'       9  ?                   
primary 'Spring, D.'        10 ?                   
primary 'Lindon, C.'        11 ?                   
primary 'Phillips, C.'      12 ?                   
primary 'Itzhaki, L.S.'     13 0000-0001-6504-2576 
# 
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 'Cell division cycle protein 20 homolog' 54796.508 1  ? ? ? ?                                           
2 polymer syn ALA-PRO-0JY-GLY                          957.064   1  ? ? ? 'D-box peptide with non-natural amino acid' 
3 water   nat water                                    18.015    72 ? ? ? ?                                           
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        p55CDC 
# 
loop_
_entity_poly.entity_id 
_entity_poly.type 
_entity_poly.nstd_linkage 
_entity_poly.nstd_monomer 
_entity_poly.pdbx_seq_one_letter_code 
_entity_poly.pdbx_seq_one_letter_code_can 
_entity_poly.pdbx_strand_id 
_entity_poly.pdbx_target_identifier 
1 'polypeptide(L)' no no  
;MAQFAFESDLHSLLQLDAPIPNAPPARWQRKAKEAAGPAPSPMRAANRSHSAGRTPGRTPGKSSSKVQTTPSKPGGDRYI
PHRSAAQMEVASFLLSKENQPENSQTPTKKEHQKAWALNLNGFDVEEAKILRLSGKPQNAPEGYQNRLKVLYSQKATPGS
SRKTCRYIPSLPDRILDAPEIRNDYYLNLVDWSSGNVLAVALDNSVYLWSASSGDILQLLQMEQPGEYISSVAWIKEGNY
LAVGTSSAEVQLWDVQQQKRLRNMTSHSARVGSLSWNSYILSSGSRSGHIHHHDVRVAEHHVATLSGHSQEVCGLRWAPD
GRHLASGGNDNLVNVWPSAPGEGGWVPLQTFTQHQGAVKAVAWCPWQSNVLATGGGTSDRHIRIWNVCSGACLSAVDAHS
QVCSILWSPHYKELISGHGFAQNQLVIWKYPTMAKVAELKGHTSRVLSLTMSPDGATVASAAADETLRLWRCFELDPARR
REREKASAAKSSLIHQGIR
;
;MAQFAFESDLHSLLQLDAPIPNAPPARWQRKAKEAAGPAPSPMRAANRSHSAGRTPGRTPGKSSSKVQTTPSKPGGDRYI
PHRSAAQMEVASFLLSKENQPENSQTPTKKEHQKAWALNLNGFDVEEAKILRLSGKPQNAPEGYQNRLKVLYSQKATPGS
SRKTCRYIPSLPDRILDAPEIRNDYYLNLVDWSSGNVLAVALDNSVYLWSASSGDILQLLQMEQPGEYISSVAWIKEGNY
LAVGTSSAEVQLWDVQQQKRLRNMTSHSARVGSLSWNSYILSSGSRSGHIHHHDVRVAEHHVATLSGHSQEVCGLRWAPD
GRHLASGGNDNLVNVWPSAPGEGGWVPLQTFTQHQGAVKAVAWCPWQSNVLATGGGTSDRHIRIWNVCSGACLSAVDAHS
QVCSILWSPHYKELISGHGFAQNQLVIWKYPTMAKVAELKGHTSRVLSLTMSPDGATVASAAADETLRLWRCFELDPARR
REREKASAAKSSLIHQGIR
;
A ? 
2 'polypeptide(L)' no yes 'RAP(0JY)GDISN' RAPXGDISN B ? 
# 
_pdbx_entity_nonpoly.entity_id   3 
_pdbx_entity_nonpoly.name        water 
_pdbx_entity_nonpoly.comp_id     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   ALA n 
1 3   GLN n 
1 4   PHE n 
1 5   ALA n 
1 6   PHE n 
1 7   GLU n 
1 8   SER n 
1 9   ASP n 
1 10  LEU n 
1 11  HIS n 
1 12  SER n 
1 13  LEU n 
1 14  LEU n 
1 15  GLN n 
1 16  LEU n 
1 17  ASP n 
1 18  ALA n 
1 19  PRO n 
1 20  ILE n 
1 21  PRO n 
1 22  ASN n 
1 23  ALA n 
1 24  PRO n 
1 25  PRO n 
1 26  ALA n 
1 27  ARG n 
1 28  TRP n 
1 29  GLN n 
1 30  ARG n 
1 31  LYS n 
1 32  ALA n 
1 33  LYS n 
1 34  GLU n 
1 35  ALA n 
1 36  ALA n 
1 37  GLY n 
1 38  PRO n 
1 39  ALA n 
1 40  PRO n 
1 41  SER n 
1 42  PRO n 
1 43  MET n 
1 44  ARG n 
1 45  ALA n 
1 46  ALA n 
1 47  ASN n 
1 48  ARG n 
1 49  SER n 
1 50  HIS n 
1 51  SER n 
1 52  ALA n 
1 53  GLY n 
1 54  ARG n 
1 55  THR n 
1 56  PRO n 
1 57  GLY n 
1 58  ARG n 
1 59  THR n 
1 60  PRO n 
1 61  GLY n 
1 62  LYS n 
1 63  SER n 
1 64  SER n 
1 65  SER n 
1 66  LYS n 
1 67  VAL n 
1 68  GLN n 
1 69  THR n 
1 70  THR n 
1 71  PRO n 
1 72  SER n 
1 73  LYS n 
1 74  PRO n 
1 75  GLY n 
1 76  GLY n 
1 77  ASP n 
1 78  ARG n 
1 79  TYR n 
1 80  ILE n 
1 81  PRO n 
1 82  HIS n 
1 83  ARG n 
1 84  SER n 
1 85  ALA n 
1 86  ALA n 
1 87  GLN n 
1 88  MET n 
1 89  GLU n 
1 90  VAL n 
1 91  ALA n 
1 92  SER n 
1 93  PHE n 
1 94  LEU n 
1 95  LEU n 
1 96  SER n 
1 97  LYS n 
1 98  GLU n 
1 99  ASN n 
1 100 GLN n 
1 101 PRO n 
1 102 GLU n 
1 103 ASN n 
1 104 SER n 
1 105 GLN n 
1 106 THR n 
1 107 PRO n 
1 108 THR n 
1 109 LYS n 
1 110 LYS n 
1 111 GLU n 
1 112 HIS n 
1 113 GLN n 
1 114 LYS n 
1 115 ALA n 
1 116 TRP n 
1 117 ALA n 
1 118 LEU n 
1 119 ASN n 
1 120 LEU n 
1 121 ASN n 
1 122 GLY n 
1 123 PHE n 
1 124 ASP n 
1 125 VAL n 
1 126 GLU n 
1 127 GLU n 
1 128 ALA n 
1 129 LYS n 
1 130 ILE n 
1 131 LEU n 
1 132 ARG n 
1 133 LEU n 
1 134 SER n 
1 135 GLY n 
1 136 LYS n 
1 137 PRO n 
1 138 GLN n 
1 139 ASN n 
1 140 ALA n 
1 141 PRO n 
1 142 GLU n 
1 143 GLY n 
1 144 TYR n 
1 145 GLN n 
1 146 ASN n 
1 147 ARG n 
1 148 LEU n 
1 149 LYS n 
1 150 VAL n 
1 151 LEU n 
1 152 TYR n 
1 153 SER n 
1 154 GLN n 
1 155 LYS n 
1 156 ALA n 
1 157 THR n 
1 158 PRO n 
1 159 GLY n 
1 160 SER n 
1 161 SER n 
1 162 ARG n 
1 163 LYS n 
1 164 THR n 
1 165 CYS n 
1 166 ARG n 
1 167 TYR n 
1 168 ILE n 
1 169 PRO n 
1 170 SER n 
1 171 LEU n 
1 172 PRO n 
1 173 ASP n 
1 174 ARG n 
1 175 ILE n 
1 176 LEU n 
1 177 ASP n 
1 178 ALA n 
1 179 PRO n 
1 180 GLU n 
1 181 ILE n 
1 182 ARG n 
1 183 ASN n 
1 184 ASP n 
1 185 TYR n 
1 186 TYR n 
1 187 LEU n 
1 188 ASN n 
1 189 LEU n 
1 190 VAL n 
1 191 ASP n 
1 192 TRP n 
1 193 SER n 
1 194 SER n 
1 195 GLY n 
1 196 ASN n 
1 197 VAL n 
1 198 LEU n 
1 199 ALA n 
1 200 VAL n 
1 201 ALA n 
1 202 LEU n 
1 203 ASP n 
1 204 ASN n 
1 205 SER n 
1 206 VAL n 
1 207 TYR n 
1 208 LEU n 
1 209 TRP n 
1 210 SER n 
1 211 ALA n 
1 212 SER n 
1 213 SER n 
1 214 GLY n 
1 215 ASP n 
1 216 ILE n 
1 217 LEU n 
1 218 GLN n 
1 219 LEU n 
1 220 LEU n 
1 221 GLN n 
1 222 MET n 
1 223 GLU n 
1 224 GLN n 
1 225 PRO n 
1 226 GLY n 
1 227 GLU n 
1 228 TYR n 
1 229 ILE n 
1 230 SER n 
1 231 SER n 
1 232 VAL n 
1 233 ALA n 
1 234 TRP n 
1 235 ILE n 
1 236 LYS n 
1 237 GLU n 
1 238 GLY n 
1 239 ASN n 
1 240 TYR n 
1 241 LEU n 
1 242 ALA n 
1 243 VAL n 
1 244 GLY n 
1 245 THR n 
1 246 SER n 
1 247 SER n 
1 248 ALA n 
1 249 GLU n 
1 250 VAL n 
1 251 GLN n 
1 252 LEU n 
1 253 TRP n 
1 254 ASP n 
1 255 VAL n 
1 256 GLN n 
1 257 GLN n 
1 258 GLN n 
1 259 LYS n 
1 260 ARG n 
1 261 LEU n 
1 262 ARG n 
1 263 ASN n 
1 264 MET n 
1 265 THR n 
1 266 SER n 
1 267 HIS n 
1 268 SER n 
1 269 ALA n 
1 270 ARG n 
1 271 VAL n 
1 272 GLY n 
1 273 SER n 
1 274 LEU n 
1 275 SER n 
1 276 TRP n 
1 277 ASN n 
1 278 SER n 
1 279 TYR n 
1 280 ILE n 
1 281 LEU n 
1 282 SER n 
1 283 SER n 
1 284 GLY n 
1 285 SER n 
1 286 ARG n 
1 287 SER n 
1 288 GLY n 
1 289 HIS n 
1 290 ILE n 
1 291 HIS n 
1 292 HIS n 
1 293 HIS n 
1 294 ASP n 
1 295 VAL n 
1 296 ARG n 
1 297 VAL n 
1 298 ALA n 
1 299 GLU n 
1 300 HIS n 
1 301 HIS n 
1 302 VAL n 
1 303 ALA n 
1 304 THR n 
1 305 LEU n 
1 306 SER n 
1 307 GLY n 
1 308 HIS n 
1 309 SER n 
1 310 GLN n 
1 311 GLU n 
1 312 VAL n 
1 313 CYS n 
1 314 GLY n 
1 315 LEU n 
1 316 ARG n 
1 317 TRP n 
1 318 ALA n 
1 319 PRO n 
1 320 ASP n 
1 321 GLY n 
1 322 ARG n 
1 323 HIS n 
1 324 LEU n 
1 325 ALA n 
1 326 SER n 
1 327 GLY n 
1 328 GLY n 
1 329 ASN n 
1 330 ASP n 
1 331 ASN n 
1 332 LEU n 
1 333 VAL n 
1 334 ASN n 
1 335 VAL n 
1 336 TRP n 
1 337 PRO n 
1 338 SER n 
1 339 ALA n 
1 340 PRO n 
1 341 GLY n 
1 342 GLU n 
1 343 GLY n 
1 344 GLY n 
1 345 TRP n 
1 346 VAL n 
1 347 PRO n 
1 348 LEU n 
1 349 GLN n 
1 350 THR n 
1 351 PHE n 
1 352 THR n 
1 353 GLN n 
1 354 HIS n 
1 355 GLN n 
1 356 GLY n 
1 357 ALA n 
1 358 VAL n 
1 359 LYS n 
1 360 ALA n 
1 361 VAL n 
1 362 ALA n 
1 363 TRP n 
1 364 CYS n 
1 365 PRO n 
1 366 TRP n 
1 367 GLN n 
1 368 SER n 
1 369 ASN n 
1 370 VAL n 
1 371 LEU n 
1 372 ALA n 
1 373 THR n 
1 374 GLY n 
1 375 GLY n 
1 376 GLY n 
1 377 THR n 
1 378 SER n 
1 379 ASP n 
1 380 ARG n 
1 381 HIS n 
1 382 ILE n 
1 383 ARG n 
1 384 ILE n 
1 385 TRP n 
1 386 ASN n 
1 387 VAL n 
1 388 CYS n 
1 389 SER n 
1 390 GLY n 
1 391 ALA n 
1 392 CYS n 
1 393 LEU n 
1 394 SER n 
1 395 ALA n 
1 396 VAL n 
1 397 ASP n 
1 398 ALA n 
1 399 HIS n 
1 400 SER n 
1 401 GLN n 
1 402 VAL n 
1 403 CYS n 
1 404 SER n 
1 405 ILE n 
1 406 LEU n 
1 407 TRP n 
1 408 SER n 
1 409 PRO n 
1 410 HIS n 
1 411 TYR n 
1 412 LYS n 
1 413 GLU n 
1 414 LEU n 
1 415 ILE n 
1 416 SER n 
1 417 GLY n 
1 418 HIS n 
1 419 GLY n 
1 420 PHE n 
1 421 ALA n 
1 422 GLN n 
1 423 ASN n 
1 424 GLN n 
1 425 LEU n 
1 426 VAL n 
1 427 ILE n 
1 428 TRP n 
1 429 LYS n 
1 430 TYR n 
1 431 PRO n 
1 432 THR n 
1 433 MET n 
1 434 ALA n 
1 435 LYS n 
1 436 VAL n 
1 437 ALA n 
1 438 GLU n 
1 439 LEU n 
1 440 LYS n 
1 441 GLY n 
1 442 HIS n 
1 443 THR n 
1 444 SER n 
1 445 ARG n 
1 446 VAL n 
1 447 LEU n 
1 448 SER n 
1 449 LEU n 
1 450 THR n 
1 451 MET n 
1 452 SER n 
1 453 PRO n 
1 454 ASP n 
1 455 GLY n 
1 456 ALA n 
1 457 THR n 
1 458 VAL n 
1 459 ALA n 
1 460 SER n 
1 461 ALA n 
1 462 ALA n 
1 463 ALA n 
1 464 ASP n 
1 465 GLU n 
1 466 THR n 
1 467 LEU n 
1 468 ARG n 
1 469 LEU n 
1 470 TRP n 
1 471 ARG n 
1 472 CYS n 
1 473 PHE n 
1 474 GLU n 
1 475 LEU n 
1 476 ASP n 
1 477 PRO n 
1 478 ALA n 
1 479 ARG n 
1 480 ARG n 
1 481 ARG n 
1 482 GLU n 
1 483 ARG n 
1 484 GLU n 
1 485 LYS n 
1 486 ALA n 
1 487 SER n 
1 488 ALA n 
1 489 ALA n 
1 490 LYS n 
1 491 SER n 
1 492 SER n 
1 493 LEU n 
1 494 ILE n 
1 495 HIS n 
1 496 GLN n 
1 497 GLY n 
1 498 ILE n 
1 499 ARG n 
2 1   ARG n 
2 2   ALA n 
2 3   PRO n 
2 4   0JY n 
2 5   GLY n 
2 6   ASP n 
2 7   ILE n 
2 8   SER n 
2 9   ASN 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                   499 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 CDC20 
_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      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_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      'Spodoptera frugiperda' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     7108 
_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            Sf21 
_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_src_syn.entity_id              2 
_pdbx_entity_src_syn.pdbx_src_id            1 
_pdbx_entity_src_syn.pdbx_alt_source_flag   sample 
_pdbx_entity_src_syn.pdbx_beg_seq_num       1 
_pdbx_entity_src_syn.pdbx_end_seq_num       9 
_pdbx_entity_src_syn.organism_scientific    'Homo sapiens' 
_pdbx_entity_src_syn.organism_common_name   ? 
_pdbx_entity_src_syn.ncbi_taxonomy_id       9606 
_pdbx_entity_src_syn.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 
0JY non-polymer         . 4-methyl-L-leucine ? 'C7 H15 N O2'    145.200 
ALA 'L-peptide linking' y ALANINE            ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE           ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE         ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'    ? 'C4 H7 N O4'     133.103 
CYS 'L-peptide linking' y CYSTEINE           ? 'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE          ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'    ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE            ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE          ? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER              ? 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE         ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE            ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE             ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE         ? 'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking' y PHENYLALANINE      ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE            ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE             ? 'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE          ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN         ? 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE           ? 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE             ? 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   ?   ?   ?   A . n 
A 1 2   ALA 2   2   ?   ?   ?   A . n 
A 1 3   GLN 3   3   ?   ?   ?   A . n 
A 1 4   PHE 4   4   ?   ?   ?   A . n 
A 1 5   ALA 5   5   ?   ?   ?   A . n 
A 1 6   PHE 6   6   ?   ?   ?   A . n 
A 1 7   GLU 7   7   ?   ?   ?   A . n 
A 1 8   SER 8   8   ?   ?   ?   A . n 
A 1 9   ASP 9   9   ?   ?   ?   A . n 
A 1 10  LEU 10  10  ?   ?   ?   A . n 
A 1 11  HIS 11  11  ?   ?   ?   A . n 
A 1 12  SER 12  12  ?   ?   ?   A . n 
A 1 13  LEU 13  13  ?   ?   ?   A . n 
A 1 14  LEU 14  14  ?   ?   ?   A . n 
A 1 15  GLN 15  15  ?   ?   ?   A . n 
A 1 16  LEU 16  16  ?   ?   ?   A . n 
A 1 17  ASP 17  17  ?   ?   ?   A . n 
A 1 18  ALA 18  18  ?   ?   ?   A . n 
A 1 19  PRO 19  19  ?   ?   ?   A . n 
A 1 20  ILE 20  20  ?   ?   ?   A . n 
A 1 21  PRO 21  21  ?   ?   ?   A . n 
A 1 22  ASN 22  22  ?   ?   ?   A . n 
A 1 23  ALA 23  23  ?   ?   ?   A . n 
A 1 24  PRO 24  24  ?   ?   ?   A . n 
A 1 25  PRO 25  25  ?   ?   ?   A . n 
A 1 26  ALA 26  26  ?   ?   ?   A . n 
A 1 27  ARG 27  27  ?   ?   ?   A . n 
A 1 28  TRP 28  28  ?   ?   ?   A . n 
A 1 29  GLN 29  29  ?   ?   ?   A . n 
A 1 30  ARG 30  30  ?   ?   ?   A . n 
A 1 31  LYS 31  31  ?   ?   ?   A . n 
A 1 32  ALA 32  32  ?   ?   ?   A . n 
A 1 33  LYS 33  33  ?   ?   ?   A . n 
A 1 34  GLU 34  34  ?   ?   ?   A . n 
A 1 35  ALA 35  35  ?   ?   ?   A . n 
A 1 36  ALA 36  36  ?   ?   ?   A . n 
A 1 37  GLY 37  37  ?   ?   ?   A . n 
A 1 38  PRO 38  38  ?   ?   ?   A . n 
A 1 39  ALA 39  39  ?   ?   ?   A . n 
A 1 40  PRO 40  40  ?   ?   ?   A . n 
A 1 41  SER 41  41  ?   ?   ?   A . n 
A 1 42  PRO 42  42  ?   ?   ?   A . n 
A 1 43  MET 43  43  ?   ?   ?   A . n 
A 1 44  ARG 44  44  ?   ?   ?   A . n 
A 1 45  ALA 45  45  ?   ?   ?   A . n 
A 1 46  ALA 46  46  ?   ?   ?   A . n 
A 1 47  ASN 47  47  ?   ?   ?   A . n 
A 1 48  ARG 48  48  ?   ?   ?   A . n 
A 1 49  SER 49  49  ?   ?   ?   A . n 
A 1 50  HIS 50  50  ?   ?   ?   A . n 
A 1 51  SER 51  51  ?   ?   ?   A . n 
A 1 52  ALA 52  52  ?   ?   ?   A . n 
A 1 53  GLY 53  53  ?   ?   ?   A . n 
A 1 54  ARG 54  54  ?   ?   ?   A . n 
A 1 55  THR 55  55  ?   ?   ?   A . n 
A 1 56  PRO 56  56  ?   ?   ?   A . n 
A 1 57  GLY 57  57  ?   ?   ?   A . n 
A 1 58  ARG 58  58  ?   ?   ?   A . n 
A 1 59  THR 59  59  ?   ?   ?   A . n 
A 1 60  PRO 60  60  ?   ?   ?   A . n 
A 1 61  GLY 61  61  ?   ?   ?   A . n 
A 1 62  LYS 62  62  ?   ?   ?   A . n 
A 1 63  SER 63  63  ?   ?   ?   A . n 
A 1 64  SER 64  64  ?   ?   ?   A . n 
A 1 65  SER 65  65  ?   ?   ?   A . n 
A 1 66  LYS 66  66  ?   ?   ?   A . n 
A 1 67  VAL 67  67  ?   ?   ?   A . n 
A 1 68  GLN 68  68  ?   ?   ?   A . n 
A 1 69  THR 69  69  ?   ?   ?   A . n 
A 1 70  THR 70  70  ?   ?   ?   A . n 
A 1 71  PRO 71  71  ?   ?   ?   A . n 
A 1 72  SER 72  72  ?   ?   ?   A . n 
A 1 73  LYS 73  73  ?   ?   ?   A . n 
A 1 74  PRO 74  74  ?   ?   ?   A . n 
A 1 75  GLY 75  75  ?   ?   ?   A . n 
A 1 76  GLY 76  76  ?   ?   ?   A . n 
A 1 77  ASP 77  77  ?   ?   ?   A . n 
A 1 78  ARG 78  78  ?   ?   ?   A . n 
A 1 79  TYR 79  79  ?   ?   ?   A . n 
A 1 80  ILE 80  80  ?   ?   ?   A . n 
A 1 81  PRO 81  81  ?   ?   ?   A . n 
A 1 82  HIS 82  82  ?   ?   ?   A . n 
A 1 83  ARG 83  83  ?   ?   ?   A . n 
A 1 84  SER 84  84  ?   ?   ?   A . n 
A 1 85  ALA 85  85  ?   ?   ?   A . n 
A 1 86  ALA 86  86  ?   ?   ?   A . n 
A 1 87  GLN 87  87  ?   ?   ?   A . n 
A 1 88  MET 88  88  ?   ?   ?   A . n 
A 1 89  GLU 89  89  ?   ?   ?   A . n 
A 1 90  VAL 90  90  ?   ?   ?   A . n 
A 1 91  ALA 91  91  ?   ?   ?   A . n 
A 1 92  SER 92  92  ?   ?   ?   A . n 
A 1 93  PHE 93  93  ?   ?   ?   A . n 
A 1 94  LEU 94  94  ?   ?   ?   A . n 
A 1 95  LEU 95  95  ?   ?   ?   A . n 
A 1 96  SER 96  96  ?   ?   ?   A . n 
A 1 97  LYS 97  97  ?   ?   ?   A . n 
A 1 98  GLU 98  98  ?   ?   ?   A . n 
A 1 99  ASN 99  99  ?   ?   ?   A . n 
A 1 100 GLN 100 100 ?   ?   ?   A . n 
A 1 101 PRO 101 101 ?   ?   ?   A . n 
A 1 102 GLU 102 102 ?   ?   ?   A . n 
A 1 103 ASN 103 103 ?   ?   ?   A . n 
A 1 104 SER 104 104 ?   ?   ?   A . n 
A 1 105 GLN 105 105 ?   ?   ?   A . n 
A 1 106 THR 106 106 ?   ?   ?   A . n 
A 1 107 PRO 107 107 ?   ?   ?   A . n 
A 1 108 THR 108 108 ?   ?   ?   A . n 
A 1 109 LYS 109 109 ?   ?   ?   A . n 
A 1 110 LYS 110 110 ?   ?   ?   A . n 
A 1 111 GLU 111 111 ?   ?   ?   A . n 
A 1 112 HIS 112 112 ?   ?   ?   A . n 
A 1 113 GLN 113 113 ?   ?   ?   A . n 
A 1 114 LYS 114 114 ?   ?   ?   A . n 
A 1 115 ALA 115 115 ?   ?   ?   A . n 
A 1 116 TRP 116 116 ?   ?   ?   A . n 
A 1 117 ALA 117 117 ?   ?   ?   A . n 
A 1 118 LEU 118 118 ?   ?   ?   A . n 
A 1 119 ASN 119 119 ?   ?   ?   A . n 
A 1 120 LEU 120 120 ?   ?   ?   A . n 
A 1 121 ASN 121 121 ?   ?   ?   A . n 
A 1 122 GLY 122 122 ?   ?   ?   A . n 
A 1 123 PHE 123 123 ?   ?   ?   A . n 
A 1 124 ASP 124 124 ?   ?   ?   A . n 
A 1 125 VAL 125 125 ?   ?   ?   A . n 
A 1 126 GLU 126 126 ?   ?   ?   A . n 
A 1 127 GLU 127 127 ?   ?   ?   A . n 
A 1 128 ALA 128 128 ?   ?   ?   A . n 
A 1 129 LYS 129 129 ?   ?   ?   A . n 
A 1 130 ILE 130 130 ?   ?   ?   A . n 
A 1 131 LEU 131 131 ?   ?   ?   A . n 
A 1 132 ARG 132 132 ?   ?   ?   A . n 
A 1 133 LEU 133 133 ?   ?   ?   A . n 
A 1 134 SER 134 134 ?   ?   ?   A . n 
A 1 135 GLY 135 135 ?   ?   ?   A . n 
A 1 136 LYS 136 136 ?   ?   ?   A . n 
A 1 137 PRO 137 137 ?   ?   ?   A . n 
A 1 138 GLN 138 138 ?   ?   ?   A . n 
A 1 139 ASN 139 139 ?   ?   ?   A . n 
A 1 140 ALA 140 140 ?   ?   ?   A . n 
A 1 141 PRO 141 141 ?   ?   ?   A . n 
A 1 142 GLU 142 142 ?   ?   ?   A . n 
A 1 143 GLY 143 143 ?   ?   ?   A . n 
A 1 144 TYR 144 144 ?   ?   ?   A . n 
A 1 145 GLN 145 145 ?   ?   ?   A . n 
A 1 146 ASN 146 146 ?   ?   ?   A . n 
A 1 147 ARG 147 147 ?   ?   ?   A . n 
A 1 148 LEU 148 148 ?   ?   ?   A . n 
A 1 149 LYS 149 149 ?   ?   ?   A . n 
A 1 150 VAL 150 150 ?   ?   ?   A . n 
A 1 151 LEU 151 151 ?   ?   ?   A . n 
A 1 152 TYR 152 152 ?   ?   ?   A . n 
A 1 153 SER 153 153 ?   ?   ?   A . n 
A 1 154 GLN 154 154 ?   ?   ?   A . n 
A 1 155 LYS 155 155 ?   ?   ?   A . n 
A 1 156 ALA 156 156 ?   ?   ?   A . n 
A 1 157 THR 157 157 ?   ?   ?   A . n 
A 1 158 PRO 158 158 ?   ?   ?   A . n 
A 1 159 GLY 159 159 ?   ?   ?   A . n 
A 1 160 SER 160 160 ?   ?   ?   A . n 
A 1 161 SER 161 161 ?   ?   ?   A . n 
A 1 162 ARG 162 162 ?   ?   ?   A . n 
A 1 163 LYS 163 163 ?   ?   ?   A . n 
A 1 164 THR 164 164 ?   ?   ?   A . n 
A 1 165 CYS 165 165 ?   ?   ?   A . n 
A 1 166 ARG 166 166 ?   ?   ?   A . n 
A 1 167 TYR 167 167 ?   ?   ?   A . n 
A 1 168 ILE 168 168 168 ILE ILE A . n 
A 1 169 PRO 169 169 169 PRO PRO A . n 
A 1 170 SER 170 170 170 SER SER A . n 
A 1 171 LEU 171 171 171 LEU LEU A . n 
A 1 172 PRO 172 172 172 PRO PRO A . n 
A 1 173 ASP 173 173 173 ASP ASP A . n 
A 1 174 ARG 174 174 174 ARG ARG A . n 
A 1 175 ILE 175 175 175 ILE ILE A . n 
A 1 176 LEU 176 176 176 LEU LEU A . n 
A 1 177 ASP 177 177 177 ASP ASP A . n 
A 1 178 ALA 178 178 178 ALA ALA A . n 
A 1 179 PRO 179 179 179 PRO PRO A . n 
A 1 180 GLU 180 180 180 GLU GLU A . n 
A 1 181 ILE 181 181 181 ILE ILE A . n 
A 1 182 ARG 182 182 182 ARG ARG A . n 
A 1 183 ASN 183 183 183 ASN ASN A . n 
A 1 184 ASP 184 184 184 ASP ASP A . n 
A 1 185 TYR 185 185 185 TYR TYR A . n 
A 1 186 TYR 186 186 186 TYR TYR A . n 
A 1 187 LEU 187 187 187 LEU LEU A . n 
A 1 188 ASN 188 188 188 ASN ASN A . n 
A 1 189 LEU 189 189 189 LEU LEU A . n 
A 1 190 VAL 190 190 190 VAL VAL A . n 
A 1 191 ASP 191 191 191 ASP ASP A . n 
A 1 192 TRP 192 192 192 TRP TRP A . n 
A 1 193 SER 193 193 193 SER SER A . n 
A 1 194 SER 194 194 194 SER SER A . n 
A 1 195 GLY 195 195 195 GLY GLY A . n 
A 1 196 ASN 196 196 196 ASN ASN A . n 
A 1 197 VAL 197 197 197 VAL VAL A . n 
A 1 198 LEU 198 198 198 LEU LEU A . n 
A 1 199 ALA 199 199 199 ALA ALA A . n 
A 1 200 VAL 200 200 200 VAL VAL A . n 
A 1 201 ALA 201 201 201 ALA ALA A . n 
A 1 202 LEU 202 202 202 LEU LEU A . n 
A 1 203 ASP 203 203 203 ASP ASP A . n 
A 1 204 ASN 204 204 204 ASN ASN A . n 
A 1 205 SER 205 205 205 SER SER A . n 
A 1 206 VAL 206 206 206 VAL VAL A . n 
A 1 207 TYR 207 207 207 TYR TYR A . n 
A 1 208 LEU 208 208 208 LEU LEU A . n 
A 1 209 TRP 209 209 209 TRP TRP A . n 
A 1 210 SER 210 210 210 SER SER A . n 
A 1 211 ALA 211 211 211 ALA ALA A . n 
A 1 212 SER 212 212 212 SER SER A . n 
A 1 213 SER 213 213 213 SER SER A . n 
A 1 214 GLY 214 214 214 GLY GLY A . n 
A 1 215 ASP 215 215 215 ASP ASP A . n 
A 1 216 ILE 216 216 216 ILE ILE A . n 
A 1 217 LEU 217 217 217 LEU LEU A . n 
A 1 218 GLN 218 218 218 GLN GLN A . n 
A 1 219 LEU 219 219 219 LEU LEU A . n 
A 1 220 LEU 220 220 220 LEU LEU A . n 
A 1 221 GLN 221 221 221 GLN GLN A . n 
A 1 222 MET 222 222 222 MET MET A . n 
A 1 223 GLU 223 223 223 GLU GLU A . n 
A 1 224 GLN 224 224 224 GLN GLN A . n 
A 1 225 PRO 225 225 225 PRO PRO A . n 
A 1 226 GLY 226 226 226 GLY GLY A . n 
A 1 227 GLU 227 227 227 GLU GLU A . n 
A 1 228 TYR 228 228 228 TYR TYR A . n 
A 1 229 ILE 229 229 229 ILE ILE A . n 
A 1 230 SER 230 230 230 SER SER A . n 
A 1 231 SER 231 231 231 SER SER A . n 
A 1 232 VAL 232 232 232 VAL VAL A . n 
A 1 233 ALA 233 233 233 ALA ALA A . n 
A 1 234 TRP 234 234 234 TRP TRP A . n 
A 1 235 ILE 235 235 235 ILE ILE A . n 
A 1 236 LYS 236 236 236 LYS LYS A . n 
A 1 237 GLU 237 237 237 GLU GLU A . n 
A 1 238 GLY 238 238 238 GLY GLY A . n 
A 1 239 ASN 239 239 239 ASN ASN A . n 
A 1 240 TYR 240 240 240 TYR TYR A . n 
A 1 241 LEU 241 241 241 LEU LEU A . n 
A 1 242 ALA 242 242 242 ALA ALA A . n 
A 1 243 VAL 243 243 243 VAL VAL A . n 
A 1 244 GLY 244 244 244 GLY GLY A . n 
A 1 245 THR 245 245 245 THR THR A . n 
A 1 246 SER 246 246 246 SER SER A . n 
A 1 247 SER 247 247 247 SER SER A . n 
A 1 248 ALA 248 248 248 ALA ALA A . n 
A 1 249 GLU 249 249 249 GLU GLU A . n 
A 1 250 VAL 250 250 250 VAL VAL A . n 
A 1 251 GLN 251 251 251 GLN GLN A . n 
A 1 252 LEU 252 252 252 LEU LEU A . n 
A 1 253 TRP 253 253 253 TRP TRP A . n 
A 1 254 ASP 254 254 254 ASP ASP A . n 
A 1 255 VAL 255 255 255 VAL VAL A . n 
A 1 256 GLN 256 256 256 GLN GLN A . n 
A 1 257 GLN 257 257 257 GLN GLN A . n 
A 1 258 GLN 258 258 258 GLN GLN A . n 
A 1 259 LYS 259 259 259 LYS LYS A . n 
A 1 260 ARG 260 260 260 ARG ARG A . n 
A 1 261 LEU 261 261 261 LEU LEU A . n 
A 1 262 ARG 262 262 262 ARG ARG A . n 
A 1 263 ASN 263 263 263 ASN ASN A . n 
A 1 264 MET 264 264 264 MET MET A . n 
A 1 265 THR 265 265 265 THR THR A . n 
A 1 266 SER 266 266 266 SER SER A . n 
A 1 267 HIS 267 267 267 HIS HIS A . n 
A 1 268 SER 268 268 268 SER SER A . n 
A 1 269 ALA 269 269 269 ALA ALA A . n 
A 1 270 ARG 270 270 270 ARG ARG A . n 
A 1 271 VAL 271 271 271 VAL VAL A . n 
A 1 272 GLY 272 272 272 GLY GLY A . n 
A 1 273 SER 273 273 273 SER SER A . n 
A 1 274 LEU 274 274 274 LEU LEU A . n 
A 1 275 SER 275 275 275 SER SER A . n 
A 1 276 TRP 276 276 276 TRP TRP A . n 
A 1 277 ASN 277 277 277 ASN ASN A . n 
A 1 278 SER 278 278 278 SER SER A . n 
A 1 279 TYR 279 279 279 TYR TYR A . n 
A 1 280 ILE 280 280 280 ILE ILE A . n 
A 1 281 LEU 281 281 281 LEU LEU A . n 
A 1 282 SER 282 282 282 SER SER A . n 
A 1 283 SER 283 283 283 SER SER A . n 
A 1 284 GLY 284 284 284 GLY GLY A . n 
A 1 285 SER 285 285 285 SER SER A . n 
A 1 286 ARG 286 286 286 ARG ARG A . n 
A 1 287 SER 287 287 287 SER SER A . n 
A 1 288 GLY 288 288 288 GLY GLY A . n 
A 1 289 HIS 289 289 289 HIS HIS A . n 
A 1 290 ILE 290 290 290 ILE ILE A . n 
A 1 291 HIS 291 291 291 HIS HIS A . n 
A 1 292 HIS 292 292 292 HIS HIS A . n 
A 1 293 HIS 293 293 293 HIS HIS A . n 
A 1 294 ASP 294 294 294 ASP ASP A . n 
A 1 295 VAL 295 295 295 VAL VAL A . n 
A 1 296 ARG 296 296 296 ARG ARG A . n 
A 1 297 VAL 297 297 297 VAL VAL A . n 
A 1 298 ALA 298 298 298 ALA ALA A . n 
A 1 299 GLU 299 299 299 GLU GLU A . n 
A 1 300 HIS 300 300 300 HIS HIS A . n 
A 1 301 HIS 301 301 301 HIS HIS A . n 
A 1 302 VAL 302 302 302 VAL VAL A . n 
A 1 303 ALA 303 303 303 ALA ALA A . n 
A 1 304 THR 304 304 304 THR THR A . n 
A 1 305 LEU 305 305 305 LEU LEU A . n 
A 1 306 SER 306 306 306 SER SER A . n 
A 1 307 GLY 307 307 307 GLY GLY A . n 
A 1 308 HIS 308 308 308 HIS HIS A . n 
A 1 309 SER 309 309 309 SER SER A . n 
A 1 310 GLN 310 310 310 GLN GLN A . n 
A 1 311 GLU 311 311 311 GLU GLU A . n 
A 1 312 VAL 312 312 312 VAL VAL A . n 
A 1 313 CYS 313 313 313 CYS CYS A . n 
A 1 314 GLY 314 314 314 GLY GLY A . n 
A 1 315 LEU 315 315 315 LEU LEU A . n 
A 1 316 ARG 316 316 316 ARG ARG A . n 
A 1 317 TRP 317 317 317 TRP TRP A . n 
A 1 318 ALA 318 318 318 ALA ALA A . n 
A 1 319 PRO 319 319 319 PRO PRO A . n 
A 1 320 ASP 320 320 320 ASP ASP A . n 
A 1 321 GLY 321 321 321 GLY GLY A . n 
A 1 322 ARG 322 322 322 ARG ARG A . n 
A 1 323 HIS 323 323 323 HIS HIS A . n 
A 1 324 LEU 324 324 324 LEU LEU A . n 
A 1 325 ALA 325 325 325 ALA ALA A . n 
A 1 326 SER 326 326 326 SER SER A . n 
A 1 327 GLY 327 327 327 GLY GLY A . n 
A 1 328 GLY 328 328 328 GLY GLY A . n 
A 1 329 ASN 329 329 329 ASN ASN A . n 
A 1 330 ASP 330 330 330 ASP ASP A . n 
A 1 331 ASN 331 331 331 ASN ASN A . n 
A 1 332 LEU 332 332 332 LEU LEU A . n 
A 1 333 VAL 333 333 333 VAL VAL A . n 
A 1 334 ASN 334 334 334 ASN ASN A . n 
A 1 335 VAL 335 335 335 VAL VAL A . n 
A 1 336 TRP 336 336 336 TRP TRP A . n 
A 1 337 PRO 337 337 337 PRO PRO A . n 
A 1 338 SER 338 338 338 SER SER A . n 
A 1 339 ALA 339 339 339 ALA ALA A . n 
A 1 340 PRO 340 340 340 PRO PRO A . n 
A 1 341 GLY 341 341 ?   ?   ?   A . n 
A 1 342 GLU 342 342 ?   ?   ?   A . n 
A 1 343 GLY 343 343 ?   ?   ?   A . n 
A 1 344 GLY 344 344 344 GLY GLY A . n 
A 1 345 TRP 345 345 345 TRP TRP A . n 
A 1 346 VAL 346 346 346 VAL VAL A . n 
A 1 347 PRO 347 347 347 PRO PRO A . n 
A 1 348 LEU 348 348 348 LEU LEU A . n 
A 1 349 GLN 349 349 349 GLN GLN A . n 
A 1 350 THR 350 350 350 THR THR A . n 
A 1 351 PHE 351 351 351 PHE PHE A . n 
A 1 352 THR 352 352 352 THR THR A . n 
A 1 353 GLN 353 353 353 GLN GLN A . n 
A 1 354 HIS 354 354 354 HIS HIS A . n 
A 1 355 GLN 355 355 355 GLN GLN A . n 
A 1 356 GLY 356 356 356 GLY GLY A . n 
A 1 357 ALA 357 357 357 ALA ALA A . n 
A 1 358 VAL 358 358 358 VAL VAL A . n 
A 1 359 LYS 359 359 359 LYS LYS A . n 
A 1 360 ALA 360 360 360 ALA ALA A . n 
A 1 361 VAL 361 361 361 VAL VAL A . n 
A 1 362 ALA 362 362 362 ALA ALA A . n 
A 1 363 TRP 363 363 363 TRP TRP A . n 
A 1 364 CYS 364 364 364 CYS CYS A . n 
A 1 365 PRO 365 365 365 PRO PRO A . n 
A 1 366 TRP 366 366 366 TRP TRP A . n 
A 1 367 GLN 367 367 367 GLN GLN A . n 
A 1 368 SER 368 368 368 SER SER A . n 
A 1 369 ASN 369 369 369 ASN ASN A . n 
A 1 370 VAL 370 370 370 VAL VAL A . n 
A 1 371 LEU 371 371 371 LEU LEU A . n 
A 1 372 ALA 372 372 372 ALA ALA A . n 
A 1 373 THR 373 373 373 THR THR A . n 
A 1 374 GLY 374 374 374 GLY GLY A . n 
A 1 375 GLY 375 375 375 GLY GLY A . n 
A 1 376 GLY 376 376 376 GLY GLY A . n 
A 1 377 THR 377 377 377 THR THR A . n 
A 1 378 SER 378 378 378 SER SER A . n 
A 1 379 ASP 379 379 379 ASP ASP A . n 
A 1 380 ARG 380 380 380 ARG ARG A . n 
A 1 381 HIS 381 381 381 HIS HIS A . n 
A 1 382 ILE 382 382 382 ILE ILE A . n 
A 1 383 ARG 383 383 383 ARG ARG A . n 
A 1 384 ILE 384 384 384 ILE ILE A . n 
A 1 385 TRP 385 385 385 TRP TRP A . n 
A 1 386 ASN 386 386 386 ASN ASN A . n 
A 1 387 VAL 387 387 387 VAL VAL A . n 
A 1 388 CYS 388 388 388 CYS CYS A . n 
A 1 389 SER 389 389 389 SER SER A . n 
A 1 390 GLY 390 390 390 GLY GLY A . n 
A 1 391 ALA 391 391 391 ALA ALA A . n 
A 1 392 CYS 392 392 392 CYS CYS A . n 
A 1 393 LEU 393 393 393 LEU LEU A . n 
A 1 394 SER 394 394 394 SER SER A . n 
A 1 395 ALA 395 395 395 ALA ALA A . n 
A 1 396 VAL 396 396 396 VAL VAL A . n 
A 1 397 ASP 397 397 397 ASP ASP A . n 
A 1 398 ALA 398 398 398 ALA ALA A . n 
A 1 399 HIS 399 399 399 HIS HIS A . n 
A 1 400 SER 400 400 400 SER SER A . n 
A 1 401 GLN 401 401 401 GLN GLN A . n 
A 1 402 VAL 402 402 402 VAL VAL A . n 
A 1 403 CYS 403 403 403 CYS CYS A . n 
A 1 404 SER 404 404 404 SER SER A . n 
A 1 405 ILE 405 405 405 ILE ILE A . n 
A 1 406 LEU 406 406 406 LEU LEU A . n 
A 1 407 TRP 407 407 407 TRP TRP A . n 
A 1 408 SER 408 408 408 SER SER A . n 
A 1 409 PRO 409 409 409 PRO PRO A . n 
A 1 410 HIS 410 410 410 HIS HIS A . n 
A 1 411 TYR 411 411 411 TYR TYR A . n 
A 1 412 LYS 412 412 412 LYS LYS A . n 
A 1 413 GLU 413 413 413 GLU GLU A . n 
A 1 414 LEU 414 414 414 LEU LEU A . n 
A 1 415 ILE 415 415 415 ILE ILE A . n 
A 1 416 SER 416 416 416 SER SER A . n 
A 1 417 GLY 417 417 417 GLY GLY A . n 
A 1 418 HIS 418 418 418 HIS HIS A . n 
A 1 419 GLY 419 419 419 GLY GLY A . n 
A 1 420 PHE 420 420 420 PHE PHE A . n 
A 1 421 ALA 421 421 421 ALA ALA A . n 
A 1 422 GLN 422 422 422 GLN GLN A . n 
A 1 423 ASN 423 423 423 ASN ASN A . n 
A 1 424 GLN 424 424 424 GLN GLN A . n 
A 1 425 LEU 425 425 425 LEU LEU A . n 
A 1 426 VAL 426 426 426 VAL VAL A . n 
A 1 427 ILE 427 427 427 ILE ILE A . n 
A 1 428 TRP 428 428 428 TRP TRP A . n 
A 1 429 LYS 429 429 429 LYS LYS A . n 
A 1 430 TYR 430 430 430 TYR TYR A . n 
A 1 431 PRO 431 431 431 PRO PRO A . n 
A 1 432 THR 432 432 432 THR THR A . n 
A 1 433 MET 433 433 433 MET MET A . n 
A 1 434 ALA 434 434 434 ALA ALA A . n 
A 1 435 LYS 435 435 435 LYS LYS A . n 
A 1 436 VAL 436 436 436 VAL VAL A . n 
A 1 437 ALA 437 437 437 ALA ALA A . n 
A 1 438 GLU 438 438 438 GLU GLU A . n 
A 1 439 LEU 439 439 439 LEU LEU A . n 
A 1 440 LYS 440 440 440 LYS LYS A . n 
A 1 441 GLY 441 441 441 GLY GLY A . n 
A 1 442 HIS 442 442 442 HIS HIS A . n 
A 1 443 THR 443 443 443 THR THR A . n 
A 1 444 SER 444 444 444 SER SER A . n 
A 1 445 ARG 445 445 445 ARG ARG A . n 
A 1 446 VAL 446 446 446 VAL VAL A . n 
A 1 447 LEU 447 447 447 LEU LEU A . n 
A 1 448 SER 448 448 448 SER SER A . n 
A 1 449 LEU 449 449 449 LEU LEU A . n 
A 1 450 THR 450 450 450 THR THR A . n 
A 1 451 MET 451 451 451 MET MET A . n 
A 1 452 SER 452 452 452 SER SER A . n 
A 1 453 PRO 453 453 453 PRO PRO A . n 
A 1 454 ASP 454 454 454 ASP ASP A . n 
A 1 455 GLY 455 455 455 GLY GLY A . n 
A 1 456 ALA 456 456 456 ALA ALA A . n 
A 1 457 THR 457 457 457 THR THR A . n 
A 1 458 VAL 458 458 458 VAL VAL A . n 
A 1 459 ALA 459 459 459 ALA ALA A . n 
A 1 460 SER 460 460 460 SER SER A . n 
A 1 461 ALA 461 461 461 ALA ALA A . n 
A 1 462 ALA 462 462 462 ALA ALA A . n 
A 1 463 ALA 463 463 463 ALA ALA A . n 
A 1 464 ASP 464 464 464 ASP ASP A . n 
A 1 465 GLU 465 465 465 GLU GLU A . n 
A 1 466 THR 466 466 466 THR THR A . n 
A 1 467 LEU 467 467 467 LEU LEU A . n 
A 1 468 ARG 468 468 468 ARG ARG A . n 
A 1 469 LEU 469 469 469 LEU LEU A . n 
A 1 470 TRP 470 470 470 TRP TRP A . n 
A 1 471 ARG 471 471 471 ARG ARG A . n 
A 1 472 CYS 472 472 472 CYS CYS A . n 
A 1 473 PHE 473 473 473 PHE PHE A . n 
A 1 474 GLU 474 474 474 GLU GLU A . n 
A 1 475 LEU 475 475 ?   ?   ?   A . n 
A 1 476 ASP 476 476 ?   ?   ?   A . n 
A 1 477 PRO 477 477 ?   ?   ?   A . n 
A 1 478 ALA 478 478 ?   ?   ?   A . n 
A 1 479 ARG 479 479 ?   ?   ?   A . n 
A 1 480 ARG 480 480 ?   ?   ?   A . n 
A 1 481 ARG 481 481 ?   ?   ?   A . n 
A 1 482 GLU 482 482 ?   ?   ?   A . n 
A 1 483 ARG 483 483 ?   ?   ?   A . n 
A 1 484 GLU 484 484 ?   ?   ?   A . n 
A 1 485 LYS 485 485 ?   ?   ?   A . n 
A 1 486 ALA 486 486 ?   ?   ?   A . n 
A 1 487 SER 487 487 ?   ?   ?   A . n 
A 1 488 ALA 488 488 ?   ?   ?   A . n 
A 1 489 ALA 489 489 ?   ?   ?   A . n 
A 1 490 LYS 490 490 ?   ?   ?   A . n 
A 1 491 SER 491 491 ?   ?   ?   A . n 
A 1 492 SER 492 492 ?   ?   ?   A . n 
A 1 493 LEU 493 493 ?   ?   ?   A . n 
A 1 494 ILE 494 494 ?   ?   ?   A . n 
A 1 495 HIS 495 495 ?   ?   ?   A . n 
A 1 496 GLN 496 496 ?   ?   ?   A . n 
A 1 497 GLY 497 497 ?   ?   ?   A . n 
A 1 498 ILE 498 498 ?   ?   ?   A . n 
A 1 499 ARG 499 499 ?   ?   ?   A . n 
B 2 1   ARG 1   1   ?   ?   ?   B . n 
B 2 2   ALA 2   2   2   ALA ALA B . n 
B 2 3   PRO 3   3   3   PRO PRO B . n 
B 2 4   0JY 4   4   4   0JY 0JY B . n 
B 2 5   GLY 5   5   5   GLY GLY B . n 
B 2 6   ASP 6   6   ?   ?   ?   B . n 
B 2 7   ILE 7   7   ?   ?   ?   B . n 
B 2 8   SER 8   8   ?   ?   ?   B . n 
B 2 9   ASN 9   9   ?   ?   ?   B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        0JY 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   0JY 
_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 
C 3 HOH 1  501 29 HOH HOH A . 
C 3 HOH 2  502 43 HOH HOH A . 
C 3 HOH 3  503 23 HOH HOH A . 
C 3 HOH 4  504 24 HOH HOH A . 
C 3 HOH 5  505 27 HOH HOH A . 
C 3 HOH 6  506 50 HOH HOH A . 
C 3 HOH 7  507 58 HOH HOH A . 
C 3 HOH 8  508 55 HOH HOH A . 
C 3 HOH 9  509 47 HOH HOH A . 
C 3 HOH 10 510 46 HOH HOH A . 
C 3 HOH 11 511 54 HOH HOH A . 
C 3 HOH 12 512 13 HOH HOH A . 
C 3 HOH 13 513 12 HOH HOH A . 
C 3 HOH 14 514 51 HOH HOH A . 
C 3 HOH 15 515 9  HOH HOH A . 
C 3 HOH 16 516 48 HOH HOH A . 
C 3 HOH 17 517 18 HOH HOH A . 
C 3 HOH 18 518 32 HOH HOH A . 
C 3 HOH 19 519 49 HOH HOH A . 
C 3 HOH 20 520 3  HOH HOH A . 
C 3 HOH 21 521 37 HOH HOH A . 
C 3 HOH 22 522 7  HOH HOH A . 
C 3 HOH 23 523 52 HOH HOH A . 
C 3 HOH 24 524 57 HOH HOH A . 
C 3 HOH 25 525 44 HOH HOH A . 
C 3 HOH 26 526 42 HOH HOH A . 
C 3 HOH 27 527 68 HOH HOH A . 
C 3 HOH 28 528 26 HOH HOH A . 
C 3 HOH 29 529 71 HOH HOH A . 
C 3 HOH 30 530 41 HOH HOH A . 
C 3 HOH 31 531 25 HOH HOH A . 
C 3 HOH 32 532 10 HOH HOH A . 
C 3 HOH 33 533 14 HOH HOH A . 
C 3 HOH 34 534 39 HOH HOH A . 
C 3 HOH 35 535 8  HOH HOH A . 
C 3 HOH 36 536 30 HOH HOH A . 
C 3 HOH 37 537 17 HOH HOH A . 
C 3 HOH 38 538 45 HOH HOH A . 
C 3 HOH 39 539 15 HOH HOH A . 
C 3 HOH 40 540 34 HOH HOH A . 
C 3 HOH 41 541 69 HOH HOH A . 
C 3 HOH 42 542 5  HOH HOH A . 
C 3 HOH 43 543 6  HOH HOH A . 
C 3 HOH 44 544 53 HOH HOH A . 
C 3 HOH 45 545 70 HOH HOH A . 
C 3 HOH 46 546 28 HOH HOH A . 
C 3 HOH 47 547 60 HOH HOH A . 
C 3 HOH 48 548 33 HOH HOH A . 
C 3 HOH 49 549 21 HOH HOH A . 
C 3 HOH 50 550 72 HOH HOH A . 
C 3 HOH 51 551 61 HOH HOH A . 
C 3 HOH 52 552 38 HOH HOH A . 
C 3 HOH 53 553 40 HOH HOH A . 
C 3 HOH 54 554 66 HOH HOH A . 
C 3 HOH 55 555 22 HOH HOH A . 
C 3 HOH 56 556 63 HOH HOH A . 
C 3 HOH 57 557 65 HOH HOH A . 
C 3 HOH 58 558 31 HOH HOH A . 
C 3 HOH 59 559 19 HOH HOH A . 
C 3 HOH 60 560 11 HOH HOH A . 
C 3 HOH 61 561 36 HOH HOH A . 
C 3 HOH 62 562 20 HOH HOH A . 
C 3 HOH 63 563 4  HOH HOH A . 
C 3 HOH 64 564 67 HOH HOH A . 
C 3 HOH 65 565 1  HOH HOH A . 
C 3 HOH 66 566 16 HOH HOH A . 
C 3 HOH 67 567 35 HOH HOH A . 
C 3 HOH 68 568 56 HOH HOH A . 
C 3 HOH 69 569 59 HOH HOH A . 
C 3 HOH 70 570 62 HOH HOH A . 
C 3 HOH 71 571 64 HOH HOH A . 
C 3 HOH 72 572 2  HOH HOH A . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A LYS 236 ? CG  ? A LYS 236 CG  
2  1 Y 1 A LYS 236 ? CD  ? A LYS 236 CD  
3  1 Y 1 A LYS 236 ? CE  ? A LYS 236 CE  
4  1 Y 1 A LYS 236 ? NZ  ? A LYS 236 NZ  
5  1 Y 1 A GLU 237 ? CG  ? A GLU 237 CG  
6  1 Y 1 A GLU 237 ? CD  ? A GLU 237 CD  
7  1 Y 1 A GLU 237 ? OE1 ? A GLU 237 OE1 
8  1 Y 1 A GLU 237 ? OE2 ? A GLU 237 OE2 
9  1 Y 1 A LYS 412 ? CG  ? A LYS 412 CG  
10 1 Y 1 A LYS 412 ? CD  ? A LYS 412 CD  
11 1 Y 1 A LYS 412 ? CE  ? A LYS 412 CE  
12 1 Y 1 A LYS 412 ? NZ  ? A LYS 412 NZ  
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? BUSTER  ? ? ? '2.10.3 (20-MAY-2020)' 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .                      2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .                      3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER  ? ? ? .                      4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   109.60 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9I6A 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     35.003 
_cell.length_a_esd                 ? 
_cell.length_b                     86.869 
_cell.length_b_esd                 ? 
_cell.length_c                     48.027 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        2 
_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                         9I6A 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 1 21 1' 
_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                   9I6A 
_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             ? 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          ? 
_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' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              6.5 
_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    '10 % MPD, 12-14 % PEG 6000, 0.1 M MES pH 6.5' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER2 XE 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2019-10-24 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.9795 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'DIAMOND BEAMLINE I04' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.9795 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   I04 
_diffrn_source.pdbx_synchrotron_site       Diamond 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9I6A 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.915 
_reflns.d_resolution_low                               45.243 
_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                                     14979 
_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                           71.8 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                5.1 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          7.6 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.147 
_reflns.pdbx_Rpim_I_all                                0.064 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       76640 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   ? 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.132 
_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                                    1.915 
_reflns_shell.d_res_low                                     2.094 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           3657 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             750 
_reflns_shell.percent_possible_obs                          15.4 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               4.9 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     1.5 
_reflns_shell.pdbx_Rrim_I_all                               1.299 
_reflns_shell.pdbx_Rpim_I_all                               0.573 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  ? 
_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                                  1.161 
_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]                            -3.09080 
_refine.aniso_B[1][2]                            0.00000 
_refine.aniso_B[1][3]                            0.90190 
_refine.aniso_B[2][2]                            6.37390 
_refine.aniso_B[2][3]                            0.00000 
_refine.aniso_B[3][3]                            -3.28310 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               29.97 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.907 
_refine.correlation_coeff_Fo_to_Fc_free          0.883 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9I6A 
_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                            1.915 
_refine.ls_d_res_low                             45.24 
_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                     14966 
_refine.ls_number_reflns_R_free                  774 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    71.8 
_refine.ls_percent_reflns_R_free                 5.170 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2078 
_refine.ls_R_factor_R_free                       0.2307 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2065 
_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                    ? 
_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                          0.000 
_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       ? 
_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                  ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_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   0.199 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.193 
_refine.pdbx_overall_SU_R_Blow_DPI               0.288 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            ? 
_refine.overall_SU_R_Cruickshank_DPI             0.301 
_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_analyze.entry_id                        9I6A 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.Luzzati_coordinate_error_free   ? 
_refine_analyze.Luzzati_coordinate_error_obs    0.32 
_refine_analyze.Luzzati_d_res_low_free          ? 
_refine_analyze.Luzzati_d_res_low_obs           ? 
_refine_analyze.Luzzati_sigma_a_free            ? 
_refine_analyze.Luzzati_sigma_a_free_details    ? 
_refine_analyze.Luzzati_sigma_a_obs             ? 
_refine_analyze.Luzzati_sigma_a_obs_details     ? 
_refine_analyze.number_disordered_residues      ? 
_refine_analyze.occupancy_sum_hydrogen          ? 
_refine_analyze.occupancy_sum_non_hydrogen      ? 
_refine_analyze.RG_d_res_high                   ? 
_refine_analyze.RG_d_res_low                    ? 
_refine_analyze.RG_free                         ? 
_refine_analyze.RG_work                         ? 
_refine_analyze.RG_free_work_ratio              ? 
_refine_analyze.pdbx_Luzzati_d_res_high_obs     ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.915 
_refine_hist.d_res_low                        45.24 
_refine_hist.number_atoms_solvent             72 
_refine_hist.number_atoms_total               2437 
_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        2356 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         9 
_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' ? 0.008 ? 2429 ? t_bond_d                  2.00  HARMONIC     
'X-RAY DIFFRACTION' ? 1.00  ? 3321 ? t_angle_deg               2.00  HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? 784  ? t_dihedral_angle_d        2.00  SINUSOIDAL   
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_incorr_chiral_ct        ?     ?            
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_pseud_angle             ?     ?            
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_trig_c_planes           ?     ?            
'X-RAY DIFFRACTION' ? ?     ? 411  ? t_gen_planes              5.00  HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? 2429 ? t_it                      10.00 HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_nbd                     ?     ?            
'X-RAY DIFFRACTION' ? 4.20  ? ?    ? t_omega_torsion           ?     ?            
'X-RAY DIFFRACTION' ? 15.86 ? ?    ? t_other_torsion           ?     ?            
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_improper_torsion        ?     ?            
'X-RAY DIFFRACTION' ? ?     ? 309  ? t_chiral_improper_torsion 5.00  SEMIHARMONIC 
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_sum_occupancies         ?     ?            
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_utility_distance        ?     ?            
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_utility_angle           ?     ?            
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_utility_torsion         ?     ?            
'X-RAY DIFFRACTION' ? ?     ? 2161 ? t_ideal_dist_contact      4.00  SEMIHARMONIC 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.92 
_refine_ls_shell.d_res_low                        2.05 
_refine_ls_shell.number_reflns_all                394 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             ? 
_refine_ls_shell.number_reflns_R_work             372 
_refine_ls_shell.percent_reflns_obs               10.57 
_refine_ls_shell.percent_reflns_R_free            5.58 
_refine_ls_shell.R_factor_all                     0.2068 
_refine_ls_shell.R_factor_obs                     ? 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.R_factor_R_work                  0.2066 
_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   39 
_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                  0.2109 
# 
_struct.entry_id                     9I6A 
_struct.title                        'Crystal structure of human Cdc20 bound to synthetic D-box peptide D7' 
_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        9I6A 
_struct_keywords.text            'APC/C, degron, D-box, LIGASE' 
_struct_keywords.pdbx_keywords   LIGASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP CDC20_HUMAN Q12834 ? 1 
;MAQFAFESDLHSLLQLDAPIPNAPPARWQRKAKEAAGPAPSPMRAANRSHSAGRTPGRTPGKSSSKVQTTPSKPGGDRYI
PHRSAAQMEVASFLLSKENQPENSQTPTKKEHQKAWALNLNGFDVEEAKILRLSGKPQNAPEGYQNRLKVLYSQKATPGS
SRKTCRYIPSLPDRILDAPEIRNDYYLNLVDWSSGNVLAVALDNSVYLWSASSGDILQLLQMEQPGEYISSVAWIKEGNY
LAVGTSSAEVQLWDVQQQKRLRNMTSHSARVGSLSWNSYILSSGSRSGHIHHHDVRVAEHHVATLSGHSQEVCGLRWAPD
GRHLASGGNDNLVNVWPSAPGEGGWVPLQTFTQHQGAVKAVAWCPWQSNVLATGGGTSDRHIRIWNVCSGACLSAVDAHS
QVCSILWSPHYKELISGHGFAQNQLVIWKYPTMAKVAELKGHTSRVLSLTMSPDGATVASAAADETLRLWRCFELDPARR
REREKASAAKSSLIHQGIR
;
1 
2 PDB 9I6A        9I6A   ? 2 ? 1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 9I6A A 1 ? 499 ? Q12834 1 ? 499 ? 1 499 
2 2 9I6A B 1 ? 9   ? 9I6A   1 ? 9   ? 1 9   
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 580   ? 
1 MORE         -3    ? 
1 'SSA (A^2)'  11620 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_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 ? B PRO 3 C ? ? ? 1_555 B 0JY 4 N ? ? B PRO 3 B 0JY 4 1_555 ? ? ? ? ? ? ? 1.337 ? ? 
covale2 covale both ? B 0JY 4 C ? ? ? 1_555 B GLY 5 N ? ? B 0JY 4 B GLY 5 1_555 ? ? ? ? ? ? ? 1.324 ? ? 
# 
_struct_conn_type.id          covale 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
_pdbx_modification_feature.ordinal                            1 
_pdbx_modification_feature.label_comp_id                      0JY 
_pdbx_modification_feature.label_asym_id                      B 
_pdbx_modification_feature.label_seq_id                       4 
_pdbx_modification_feature.label_alt_id                       ? 
_pdbx_modification_feature.modified_residue_label_comp_id     . 
_pdbx_modification_feature.modified_residue_label_asym_id     . 
_pdbx_modification_feature.modified_residue_label_seq_id      . 
_pdbx_modification_feature.modified_residue_label_alt_id      . 
_pdbx_modification_feature.auth_comp_id                       0JY 
_pdbx_modification_feature.auth_asym_id                       B 
_pdbx_modification_feature.auth_seq_id                        4 
_pdbx_modification_feature.PDB_ins_code                       ? 
_pdbx_modification_feature.symmetry                           1_555 
_pdbx_modification_feature.modified_residue_auth_comp_id      . 
_pdbx_modification_feature.modified_residue_auth_asym_id      . 
_pdbx_modification_feature.modified_residue_auth_seq_id       . 
_pdbx_modification_feature.modified_residue_PDB_ins_code      . 
_pdbx_modification_feature.modified_residue_symmetry          . 
_pdbx_modification_feature.comp_id_linking_atom               . 
_pdbx_modification_feature.modified_residue_id_linking_atom   . 
_pdbx_modification_feature.modified_residue_id                LEU 
_pdbx_modification_feature.ref_pcm_id                         1 
_pdbx_modification_feature.ref_comp_id                        0JY 
_pdbx_modification_feature.type                               Methylation 
_pdbx_modification_feature.category                           'Named protein modification' 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 PHE 420 A . ? PHE 420 A ALA 421 A ? ALA 421 A 1 3.81 
2 TYR 430 A . ? TYR 430 A PRO 431 A ? PRO 431 A 1 7.00 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 4 ? 
AA3 ? 4 ? 
AA4 ? 4 ? 
AA5 ? 4 ? 
AA6 ? 4 ? 
AA7 ? 4 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA5 2 3 ? anti-parallel 
AA5 3 4 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA6 2 3 ? anti-parallel 
AA6 3 4 ? anti-parallel 
AA7 1 2 ? anti-parallel 
AA7 2 3 ? anti-parallel 
AA7 3 4 ? 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 ARG A 174 ? ASP A 177 ? ARG A 174 ASP A 177 
AA1 2 THR A 466 ? TRP A 470 ? THR A 466 TRP A 470 
AA1 3 VAL A 458 ? ALA A 462 ? VAL A 458 ALA A 462 
AA1 4 VAL A 446 ? MET A 451 ? VAL A 446 MET A 451 
AA2 1 VAL A 190 ? TRP A 192 ? VAL A 190 TRP A 192 
AA2 2 VAL A 197 ? LEU A 202 ? VAL A 197 LEU A 202 
AA2 3 SER A 205 ? SER A 210 ? SER A 205 SER A 210 
AA2 4 ILE A 216 ? GLN A 221 ? ILE A 216 GLN A 221 
AA3 1 ILE A 229 ? TRP A 234 ? ILE A 229 TRP A 234 
AA3 2 TYR A 240 ? THR A 245 ? TYR A 240 THR A 245 
AA3 3 GLU A 249 ? ASP A 254 ? GLU A 249 ASP A 254 
AA3 4 LYS A 259 ? THR A 265 ? LYS A 259 THR A 265 
AA4 1 VAL A 271 ? ASN A 277 ? VAL A 271 ASN A 277 
AA4 2 ILE A 280 ? SER A 285 ? ILE A 280 SER A 285 
AA4 3 HIS A 289 ? ASP A 294 ? HIS A 289 ASP A 294 
AA4 4 HIS A 301 ? SER A 306 ? HIS A 301 SER A 306 
AA5 1 VAL A 312 ? TRP A 317 ? VAL A 312 TRP A 317 
AA5 2 HIS A 323 ? GLY A 328 ? HIS A 323 GLY A 328 
AA5 3 VAL A 333 ? PRO A 337 ? VAL A 333 PRO A 337 
AA5 4 GLN A 349 ? PHE A 351 ? GLN A 349 PHE A 351 
AA6 1 VAL A 358 ? TRP A 363 ? VAL A 358 TRP A 363 
AA6 2 VAL A 370 ? GLY A 375 ? VAL A 370 GLY A 375 
AA6 3 HIS A 381 ? ASN A 386 ? HIS A 381 ASN A 386 
AA6 4 CYS A 392 ? ASP A 397 ? CYS A 392 ASP A 397 
AA7 1 VAL A 402 ? SER A 408 ? VAL A 402 SER A 408 
AA7 2 GLU A 413 ? HIS A 418 ? GLU A 413 HIS A 418 
AA7 3 LEU A 425 ? LYS A 429 ? LEU A 425 LYS A 429 
AA7 4 ALA A 434 ? LEU A 439 ? ALA A 434 LEU A 439 
# 
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 ARG A 174 ? N ARG A 174 O LEU A 469 ? O LEU A 469 
AA1 2 3 O TRP A 470 ? O TRP A 470 N VAL A 458 ? N VAL A 458 
AA1 3 4 O ALA A 461 ? O ALA A 461 N LEU A 447 ? N LEU A 447 
AA2 1 2 N ASP A 191 ? N ASP A 191 O ALA A 199 ? O ALA A 199 
AA2 2 3 N VAL A 200 ? N VAL A 200 O TYR A 207 ? O TYR A 207 
AA2 3 4 N LEU A 208 ? N LEU A 208 O LEU A 217 ? O LEU A 217 
AA3 1 2 N ALA A 233 ? N ALA A 233 O ALA A 242 ? O ALA A 242 
AA3 2 3 N VAL A 243 ? N VAL A 243 O GLN A 251 ? O GLN A 251 
AA3 3 4 N ASP A 254 ? N ASP A 254 O LYS A 259 ? O LYS A 259 
AA4 1 2 N SER A 275 ? N SER A 275 O SER A 282 ? O SER A 282 
AA4 2 3 N LEU A 281 ? N LEU A 281 O HIS A 293 ? O HIS A 293 
AA4 3 4 N ILE A 290 ? N ILE A 290 O LEU A 305 ? O LEU A 305 
AA5 1 2 N ARG A 316 ? N ARG A 316 O ALA A 325 ? O ALA A 325 
AA5 2 3 N LEU A 324 ? N LEU A 324 O TRP A 336 ? O TRP A 336 
AA5 3 4 N VAL A 335 ? N VAL A 335 O GLN A 349 ? O GLN A 349 
AA6 1 2 N ALA A 362 ? N ALA A 362 O ALA A 372 ? O ALA A 372 
AA6 2 3 N LEU A 371 ? N LEU A 371 O TRP A 385 ? O TRP A 385 
AA6 3 4 N ILE A 382 ? N ILE A 382 O VAL A 396 ? O VAL A 396 
AA7 1 2 N LEU A 406 ? N LEU A 406 O ILE A 415 ? O ILE A 415 
AA7 2 3 N LEU A 414 ? N LEU A 414 O TRP A 428 ? O TRP A 428 
AA7 3 4 N ILE A 427 ? N ILE A 427 O VAL A 436 ? O VAL A 436 
# 
_pdbx_entry_details.entry_id                   9I6A 
_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   Y 
# 
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 ASP A 203 ? ? 57.90   -108.04 
2 1 SER A 266 ? ? -173.89 -37.15  
3 1 SER A 278 ? ? 61.97   -128.55 
4 1 GLN A 355 ? ? -106.22 48.72   
# 
_pdbx_refine_tls.id               1 
_pdbx_refine_tls.pdbx_refine_id   'X-RAY DIFFRACTION' 
_pdbx_refine_tls.details          ? 
_pdbx_refine_tls.method           refined 
_pdbx_refine_tls.origin_x         -1.4037 
_pdbx_refine_tls.origin_y         -15.5029 
_pdbx_refine_tls.origin_z         14.7136 
_pdbx_refine_tls.T[1][1]          -0.1446 
_pdbx_refine_tls.T[1][1]_esd      ? 
_pdbx_refine_tls.T[1][2]          -0.0294 
_pdbx_refine_tls.T[1][2]_esd      ? 
_pdbx_refine_tls.T[1][3]          0.0058 
_pdbx_refine_tls.T[1][3]_esd      ? 
_pdbx_refine_tls.T[2][2]          0.0027 
_pdbx_refine_tls.T[2][2]_esd      ? 
_pdbx_refine_tls.T[2][3]          -0.0117 
_pdbx_refine_tls.T[2][3]_esd      ? 
_pdbx_refine_tls.T[3][3]          -0.1163 
_pdbx_refine_tls.T[3][3]_esd      ? 
_pdbx_refine_tls.L[1][1]          1.1271 
_pdbx_refine_tls.L[1][1]_esd      ? 
_pdbx_refine_tls.L[1][2]          -0.2656 
_pdbx_refine_tls.L[1][2]_esd      ? 
_pdbx_refine_tls.L[1][3]          -0.1579 
_pdbx_refine_tls.L[1][3]_esd      ? 
_pdbx_refine_tls.L[2][2]          0.9059 
_pdbx_refine_tls.L[2][2]_esd      ? 
_pdbx_refine_tls.L[2][3]          -0.1113 
_pdbx_refine_tls.L[2][3]_esd      ? 
_pdbx_refine_tls.L[3][3]          2.9423 
_pdbx_refine_tls.L[3][3]_esd      ? 
_pdbx_refine_tls.S[1][1]          -0.0706 
_pdbx_refine_tls.S[1][1]_esd      ? 
_pdbx_refine_tls.S[1][2]          -0.0081 
_pdbx_refine_tls.S[1][2]_esd      ? 
_pdbx_refine_tls.S[1][3]          0.0024 
_pdbx_refine_tls.S[1][3]_esd      ? 
_pdbx_refine_tls.S[2][1]          0.0257 
_pdbx_refine_tls.S[2][1]_esd      ? 
_pdbx_refine_tls.S[2][2]          0.0269 
_pdbx_refine_tls.S[2][2]_esd      ? 
_pdbx_refine_tls.S[2][3]          -0.0325 
_pdbx_refine_tls.S[2][3]_esd      ? 
_pdbx_refine_tls.S[3][1]          0.0009 
_pdbx_refine_tls.S[3][1]_esd      ? 
_pdbx_refine_tls.S[3][2]          0.0706 
_pdbx_refine_tls.S[3][2]_esd      ? 
_pdbx_refine_tls.S[3][3]          0.0437 
_pdbx_refine_tls.S[3][3]_esd      ? 
# 
_pdbx_refine_tls_group.id                  1 
_pdbx_refine_tls_group.pdbx_refine_id      'X-RAY DIFFRACTION' 
_pdbx_refine_tls_group.refine_tls_id       1 
_pdbx_refine_tls_group.beg_label_asym_id   ? 
_pdbx_refine_tls_group.beg_label_seq_id    ? 
_pdbx_refine_tls_group.beg_auth_asym_id    ? 
_pdbx_refine_tls_group.beg_auth_seq_id     ? 
_pdbx_refine_tls_group.beg_PDB_ins_code    ? 
_pdbx_refine_tls_group.end_label_asym_id   ? 
_pdbx_refine_tls_group.end_label_seq_id    ? 
_pdbx_refine_tls_group.end_auth_asym_id    ? 
_pdbx_refine_tls_group.end_auth_seq_id     ? 
_pdbx_refine_tls_group.end_PDB_ins_code    ? 
_pdbx_refine_tls_group.selection           ? 
_pdbx_refine_tls_group.selection_details   '{ A|* }' 
# 
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 ALA 2   ? A ALA 2   
3   1 Y 1 A GLN 3   ? A GLN 3   
4   1 Y 1 A PHE 4   ? A PHE 4   
5   1 Y 1 A ALA 5   ? A ALA 5   
6   1 Y 1 A PHE 6   ? A PHE 6   
7   1 Y 1 A GLU 7   ? A GLU 7   
8   1 Y 1 A SER 8   ? A SER 8   
9   1 Y 1 A ASP 9   ? A ASP 9   
10  1 Y 1 A LEU 10  ? A LEU 10  
11  1 Y 1 A HIS 11  ? A HIS 11  
12  1 Y 1 A SER 12  ? A SER 12  
13  1 Y 1 A LEU 13  ? A LEU 13  
14  1 Y 1 A LEU 14  ? A LEU 14  
15  1 Y 1 A GLN 15  ? A GLN 15  
16  1 Y 1 A LEU 16  ? A LEU 16  
17  1 Y 1 A ASP 17  ? A ASP 17  
18  1 Y 1 A ALA 18  ? A ALA 18  
19  1 Y 1 A PRO 19  ? A PRO 19  
20  1 Y 1 A ILE 20  ? A ILE 20  
21  1 Y 1 A PRO 21  ? A PRO 21  
22  1 Y 1 A ASN 22  ? A ASN 22  
23  1 Y 1 A ALA 23  ? A ALA 23  
24  1 Y 1 A PRO 24  ? A PRO 24  
25  1 Y 1 A PRO 25  ? A PRO 25  
26  1 Y 1 A ALA 26  ? A ALA 26  
27  1 Y 1 A ARG 27  ? A ARG 27  
28  1 Y 1 A TRP 28  ? A TRP 28  
29  1 Y 1 A GLN 29  ? A GLN 29  
30  1 Y 1 A ARG 30  ? A ARG 30  
31  1 Y 1 A LYS 31  ? A LYS 31  
32  1 Y 1 A ALA 32  ? A ALA 32  
33  1 Y 1 A LYS 33  ? A LYS 33  
34  1 Y 1 A GLU 34  ? A GLU 34  
35  1 Y 1 A ALA 35  ? A ALA 35  
36  1 Y 1 A ALA 36  ? A ALA 36  
37  1 Y 1 A GLY 37  ? A GLY 37  
38  1 Y 1 A PRO 38  ? A PRO 38  
39  1 Y 1 A ALA 39  ? A ALA 39  
40  1 Y 1 A PRO 40  ? A PRO 40  
41  1 Y 1 A SER 41  ? A SER 41  
42  1 Y 1 A PRO 42  ? A PRO 42  
43  1 Y 1 A MET 43  ? A MET 43  
44  1 Y 1 A ARG 44  ? A ARG 44  
45  1 Y 1 A ALA 45  ? A ALA 45  
46  1 Y 1 A ALA 46  ? A ALA 46  
47  1 Y 1 A ASN 47  ? A ASN 47  
48  1 Y 1 A ARG 48  ? A ARG 48  
49  1 Y 1 A SER 49  ? A SER 49  
50  1 Y 1 A HIS 50  ? A HIS 50  
51  1 Y 1 A SER 51  ? A SER 51  
52  1 Y 1 A ALA 52  ? A ALA 52  
53  1 Y 1 A GLY 53  ? A GLY 53  
54  1 Y 1 A ARG 54  ? A ARG 54  
55  1 Y 1 A THR 55  ? A THR 55  
56  1 Y 1 A PRO 56  ? A PRO 56  
57  1 Y 1 A GLY 57  ? A GLY 57  
58  1 Y 1 A ARG 58  ? A ARG 58  
59  1 Y 1 A THR 59  ? A THR 59  
60  1 Y 1 A PRO 60  ? A PRO 60  
61  1 Y 1 A GLY 61  ? A GLY 61  
62  1 Y 1 A LYS 62  ? A LYS 62  
63  1 Y 1 A SER 63  ? A SER 63  
64  1 Y 1 A SER 64  ? A SER 64  
65  1 Y 1 A SER 65  ? A SER 65  
66  1 Y 1 A LYS 66  ? A LYS 66  
67  1 Y 1 A VAL 67  ? A VAL 67  
68  1 Y 1 A GLN 68  ? A GLN 68  
69  1 Y 1 A THR 69  ? A THR 69  
70  1 Y 1 A THR 70  ? A THR 70  
71  1 Y 1 A PRO 71  ? A PRO 71  
72  1 Y 1 A SER 72  ? A SER 72  
73  1 Y 1 A LYS 73  ? A LYS 73  
74  1 Y 1 A PRO 74  ? A PRO 74  
75  1 Y 1 A GLY 75  ? A GLY 75  
76  1 Y 1 A GLY 76  ? A GLY 76  
77  1 Y 1 A ASP 77  ? A ASP 77  
78  1 Y 1 A ARG 78  ? A ARG 78  
79  1 Y 1 A TYR 79  ? A TYR 79  
80  1 Y 1 A ILE 80  ? A ILE 80  
81  1 Y 1 A PRO 81  ? A PRO 81  
82  1 Y 1 A HIS 82  ? A HIS 82  
83  1 Y 1 A ARG 83  ? A ARG 83  
84  1 Y 1 A SER 84  ? A SER 84  
85  1 Y 1 A ALA 85  ? A ALA 85  
86  1 Y 1 A ALA 86  ? A ALA 86  
87  1 Y 1 A GLN 87  ? A GLN 87  
88  1 Y 1 A MET 88  ? A MET 88  
89  1 Y 1 A GLU 89  ? A GLU 89  
90  1 Y 1 A VAL 90  ? A VAL 90  
91  1 Y 1 A ALA 91  ? A ALA 91  
92  1 Y 1 A SER 92  ? A SER 92  
93  1 Y 1 A PHE 93  ? A PHE 93  
94  1 Y 1 A LEU 94  ? A LEU 94  
95  1 Y 1 A LEU 95  ? A LEU 95  
96  1 Y 1 A SER 96  ? A SER 96  
97  1 Y 1 A LYS 97  ? A LYS 97  
98  1 Y 1 A GLU 98  ? A GLU 98  
99  1 Y 1 A ASN 99  ? A ASN 99  
100 1 Y 1 A GLN 100 ? A GLN 100 
101 1 Y 1 A PRO 101 ? A PRO 101 
102 1 Y 1 A GLU 102 ? A GLU 102 
103 1 Y 1 A ASN 103 ? A ASN 103 
104 1 Y 1 A SER 104 ? A SER 104 
105 1 Y 1 A GLN 105 ? A GLN 105 
106 1 Y 1 A THR 106 ? A THR 106 
107 1 Y 1 A PRO 107 ? A PRO 107 
108 1 Y 1 A THR 108 ? A THR 108 
109 1 Y 1 A LYS 109 ? A LYS 109 
110 1 Y 1 A LYS 110 ? A LYS 110 
111 1 Y 1 A GLU 111 ? A GLU 111 
112 1 Y 1 A HIS 112 ? A HIS 112 
113 1 Y 1 A GLN 113 ? A GLN 113 
114 1 Y 1 A LYS 114 ? A LYS 114 
115 1 Y 1 A ALA 115 ? A ALA 115 
116 1 Y 1 A TRP 116 ? A TRP 116 
117 1 Y 1 A ALA 117 ? A ALA 117 
118 1 Y 1 A LEU 118 ? A LEU 118 
119 1 Y 1 A ASN 119 ? A ASN 119 
120 1 Y 1 A LEU 120 ? A LEU 120 
121 1 Y 1 A ASN 121 ? A ASN 121 
122 1 Y 1 A GLY 122 ? A GLY 122 
123 1 Y 1 A PHE 123 ? A PHE 123 
124 1 Y 1 A ASP 124 ? A ASP 124 
125 1 Y 1 A VAL 125 ? A VAL 125 
126 1 Y 1 A GLU 126 ? A GLU 126 
127 1 Y 1 A GLU 127 ? A GLU 127 
128 1 Y 1 A ALA 128 ? A ALA 128 
129 1 Y 1 A LYS 129 ? A LYS 129 
130 1 Y 1 A ILE 130 ? A ILE 130 
131 1 Y 1 A LEU 131 ? A LEU 131 
132 1 Y 1 A ARG 132 ? A ARG 132 
133 1 Y 1 A LEU 133 ? A LEU 133 
134 1 Y 1 A SER 134 ? A SER 134 
135 1 Y 1 A GLY 135 ? A GLY 135 
136 1 Y 1 A LYS 136 ? A LYS 136 
137 1 Y 1 A PRO 137 ? A PRO 137 
138 1 Y 1 A GLN 138 ? A GLN 138 
139 1 Y 1 A ASN 139 ? A ASN 139 
140 1 Y 1 A ALA 140 ? A ALA 140 
141 1 Y 1 A PRO 141 ? A PRO 141 
142 1 Y 1 A GLU 142 ? A GLU 142 
143 1 Y 1 A GLY 143 ? A GLY 143 
144 1 Y 1 A TYR 144 ? A TYR 144 
145 1 Y 1 A GLN 145 ? A GLN 145 
146 1 Y 1 A ASN 146 ? A ASN 146 
147 1 Y 1 A ARG 147 ? A ARG 147 
148 1 Y 1 A LEU 148 ? A LEU 148 
149 1 Y 1 A LYS 149 ? A LYS 149 
150 1 Y 1 A VAL 150 ? A VAL 150 
151 1 Y 1 A LEU 151 ? A LEU 151 
152 1 Y 1 A TYR 152 ? A TYR 152 
153 1 Y 1 A SER 153 ? A SER 153 
154 1 Y 1 A GLN 154 ? A GLN 154 
155 1 Y 1 A LYS 155 ? A LYS 155 
156 1 Y 1 A ALA 156 ? A ALA 156 
157 1 Y 1 A THR 157 ? A THR 157 
158 1 Y 1 A PRO 158 ? A PRO 158 
159 1 Y 1 A GLY 159 ? A GLY 159 
160 1 Y 1 A SER 160 ? A SER 160 
161 1 Y 1 A SER 161 ? A SER 161 
162 1 Y 1 A ARG 162 ? A ARG 162 
163 1 Y 1 A LYS 163 ? A LYS 163 
164 1 Y 1 A THR 164 ? A THR 164 
165 1 Y 1 A CYS 165 ? A CYS 165 
166 1 Y 1 A ARG 166 ? A ARG 166 
167 1 Y 1 A TYR 167 ? A TYR 167 
168 1 Y 1 A GLY 341 ? A GLY 341 
169 1 Y 1 A GLU 342 ? A GLU 342 
170 1 Y 1 A GLY 343 ? A GLY 343 
171 1 Y 1 A LEU 475 ? A LEU 475 
172 1 Y 1 A ASP 476 ? A ASP 476 
173 1 Y 1 A PRO 477 ? A PRO 477 
174 1 Y 1 A ALA 478 ? A ALA 478 
175 1 Y 1 A ARG 479 ? A ARG 479 
176 1 Y 1 A ARG 480 ? A ARG 480 
177 1 Y 1 A ARG 481 ? A ARG 481 
178 1 Y 1 A GLU 482 ? A GLU 482 
179 1 Y 1 A ARG 483 ? A ARG 483 
180 1 Y 1 A GLU 484 ? A GLU 484 
181 1 Y 1 A LYS 485 ? A LYS 485 
182 1 Y 1 A ALA 486 ? A ALA 486 
183 1 Y 1 A SER 487 ? A SER 487 
184 1 Y 1 A ALA 488 ? A ALA 488 
185 1 Y 1 A ALA 489 ? A ALA 489 
186 1 Y 1 A LYS 490 ? A LYS 490 
187 1 Y 1 A SER 491 ? A SER 491 
188 1 Y 1 A SER 492 ? A SER 492 
189 1 Y 1 A LEU 493 ? A LEU 493 
190 1 Y 1 A ILE 494 ? A ILE 494 
191 1 Y 1 A HIS 495 ? A HIS 495 
192 1 Y 1 A GLN 496 ? A GLN 496 
193 1 Y 1 A GLY 497 ? A GLY 497 
194 1 Y 1 A ILE 498 ? A ILE 498 
195 1 Y 1 A ARG 499 ? A ARG 499 
196 1 Y 1 B ARG 1   ? B ARG 1   
197 1 Y 1 B ASP 6   ? B ASP 6   
198 1 Y 1 B ILE 7   ? B ILE 7   
199 1 Y 1 B SER 8   ? B SER 8   
200 1 Y 1 B ASN 9   ? B ASN 9   
# 
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 
0JY O    O N N 1   
0JY C    C N N 2   
0JY CA   C N S 3   
0JY N    N N N 4   
0JY CB   C N N 5   
0JY CAI  C N N 6   
0JY CAB  C N N 7   
0JY CAC  C N N 8   
0JY CAA  C N N 9   
0JY HA   H N N 10  
0JY H2   H N N 11  
0JY H    H N N 12  
0JY H6   H N N 13  
0JY H7   H N N 14  
0JY H8   H N N 15  
0JY H9   H N N 16  
0JY H10  H N N 17  
0JY H11  H N N 18  
0JY H12  H N N 19  
0JY H13  H N N 20  
0JY H14  H N N 21  
0JY H15  H N N 22  
0JY H16  H N N 23  
0JY OXT  O N N 24  
0JY HXT  H N N 25  
ALA N    N N N 26  
ALA CA   C N S 27  
ALA C    C N N 28  
ALA O    O N N 29  
ALA CB   C N N 30  
ALA OXT  O N N 31  
ALA H    H N N 32  
ALA H2   H N N 33  
ALA HA   H N N 34  
ALA HB1  H N N 35  
ALA HB2  H N N 36  
ALA HB3  H N N 37  
ALA HXT  H N N 38  
ARG N    N N N 39  
ARG CA   C N S 40  
ARG C    C N N 41  
ARG O    O N N 42  
ARG CB   C N N 43  
ARG CG   C N N 44  
ARG CD   C N N 45  
ARG NE   N N N 46  
ARG CZ   C N N 47  
ARG NH1  N N N 48  
ARG NH2  N N N 49  
ARG OXT  O N N 50  
ARG H    H N N 51  
ARG H2   H N N 52  
ARG HA   H N N 53  
ARG HB2  H N N 54  
ARG HB3  H N N 55  
ARG HG2  H N N 56  
ARG HG3  H N N 57  
ARG HD2  H N N 58  
ARG HD3  H N N 59  
ARG HE   H N N 60  
ARG HH11 H N N 61  
ARG HH12 H N N 62  
ARG HH21 H N N 63  
ARG HH22 H N N 64  
ARG HXT  H N N 65  
ASN N    N N N 66  
ASN CA   C N S 67  
ASN C    C N N 68  
ASN O    O N N 69  
ASN CB   C N N 70  
ASN CG   C N N 71  
ASN OD1  O N N 72  
ASN ND2  N N N 73  
ASN OXT  O N N 74  
ASN H    H N N 75  
ASN H2   H N N 76  
ASN HA   H N N 77  
ASN HB2  H N N 78  
ASN HB3  H N N 79  
ASN HD21 H N N 80  
ASN HD22 H N N 81  
ASN HXT  H N N 82  
ASP N    N N N 83  
ASP CA   C N S 84  
ASP C    C N N 85  
ASP O    O N N 86  
ASP CB   C N N 87  
ASP CG   C N N 88  
ASP OD1  O N N 89  
ASP OD2  O N N 90  
ASP OXT  O N N 91  
ASP H    H N N 92  
ASP H2   H N N 93  
ASP HA   H N N 94  
ASP HB2  H N N 95  
ASP HB3  H N N 96  
ASP HD2  H N N 97  
ASP HXT  H N N 98  
CYS N    N N N 99  
CYS CA   C N R 100 
CYS C    C N N 101 
CYS O    O N N 102 
CYS CB   C N N 103 
CYS SG   S N N 104 
CYS OXT  O N N 105 
CYS H    H N N 106 
CYS H2   H N N 107 
CYS HA   H N N 108 
CYS HB2  H N N 109 
CYS HB3  H N N 110 
CYS HG   H N N 111 
CYS HXT  H N N 112 
GLN N    N N N 113 
GLN CA   C N S 114 
GLN C    C N N 115 
GLN O    O N N 116 
GLN CB   C N N 117 
GLN CG   C N N 118 
GLN CD   C N N 119 
GLN OE1  O N N 120 
GLN NE2  N N N 121 
GLN OXT  O N N 122 
GLN H    H N N 123 
GLN H2   H N N 124 
GLN HA   H N N 125 
GLN HB2  H N N 126 
GLN HB3  H N N 127 
GLN HG2  H N N 128 
GLN HG3  H N N 129 
GLN HE21 H N N 130 
GLN HE22 H N N 131 
GLN HXT  H N N 132 
GLU N    N N N 133 
GLU CA   C N S 134 
GLU C    C N N 135 
GLU O    O N N 136 
GLU CB   C N N 137 
GLU CG   C N N 138 
GLU CD   C N N 139 
GLU OE1  O N N 140 
GLU OE2  O N N 141 
GLU OXT  O N N 142 
GLU H    H N N 143 
GLU H2   H N N 144 
GLU HA   H N N 145 
GLU HB2  H N N 146 
GLU HB3  H N N 147 
GLU HG2  H N N 148 
GLU HG3  H N N 149 
GLU HE2  H N N 150 
GLU HXT  H N N 151 
GLY N    N N N 152 
GLY CA   C N N 153 
GLY C    C N N 154 
GLY O    O N N 155 
GLY OXT  O N N 156 
GLY H    H N N 157 
GLY H2   H N N 158 
GLY HA2  H N N 159 
GLY HA3  H N N 160 
GLY HXT  H N N 161 
HIS N    N N N 162 
HIS CA   C N S 163 
HIS C    C N N 164 
HIS O    O N N 165 
HIS CB   C N N 166 
HIS CG   C Y N 167 
HIS ND1  N Y N 168 
HIS CD2  C Y N 169 
HIS CE1  C Y N 170 
HIS NE2  N Y N 171 
HIS OXT  O N N 172 
HIS H    H N N 173 
HIS H2   H N N 174 
HIS HA   H N N 175 
HIS HB2  H N N 176 
HIS HB3  H N N 177 
HIS HD1  H N N 178 
HIS HD2  H N N 179 
HIS HE1  H N N 180 
HIS HE2  H N N 181 
HIS HXT  H N N 182 
HOH O    O N N 183 
HOH H1   H N N 184 
HOH H2   H N N 185 
ILE N    N N N 186 
ILE CA   C N S 187 
ILE C    C N N 188 
ILE O    O N N 189 
ILE CB   C N S 190 
ILE CG1  C N N 191 
ILE CG2  C N N 192 
ILE CD1  C N N 193 
ILE OXT  O N N 194 
ILE H    H N N 195 
ILE H2   H N N 196 
ILE HA   H N N 197 
ILE HB   H N N 198 
ILE HG12 H N N 199 
ILE HG13 H N N 200 
ILE HG21 H N N 201 
ILE HG22 H N N 202 
ILE HG23 H N N 203 
ILE HD11 H N N 204 
ILE HD12 H N N 205 
ILE HD13 H N N 206 
ILE HXT  H N N 207 
LEU N    N N N 208 
LEU CA   C N S 209 
LEU C    C N N 210 
LEU O    O N N 211 
LEU CB   C N N 212 
LEU CG   C N N 213 
LEU CD1  C N N 214 
LEU CD2  C N N 215 
LEU OXT  O N N 216 
LEU H    H N N 217 
LEU H2   H N N 218 
LEU HA   H N N 219 
LEU HB2  H N N 220 
LEU HB3  H N N 221 
LEU HG   H N N 222 
LEU HD11 H N N 223 
LEU HD12 H N N 224 
LEU HD13 H N N 225 
LEU HD21 H N N 226 
LEU HD22 H N N 227 
LEU HD23 H N N 228 
LEU HXT  H N N 229 
LYS N    N N N 230 
LYS CA   C N S 231 
LYS C    C N N 232 
LYS O    O N N 233 
LYS CB   C N N 234 
LYS CG   C N N 235 
LYS CD   C N N 236 
LYS CE   C N N 237 
LYS NZ   N N N 238 
LYS OXT  O N N 239 
LYS H    H N N 240 
LYS H2   H N N 241 
LYS HA   H N N 242 
LYS HB2  H N N 243 
LYS HB3  H N N 244 
LYS HG2  H N N 245 
LYS HG3  H N N 246 
LYS HD2  H N N 247 
LYS HD3  H N N 248 
LYS HE2  H N N 249 
LYS HE3  H N N 250 
LYS HZ1  H N N 251 
LYS HZ2  H N N 252 
LYS HZ3  H N N 253 
LYS HXT  H N N 254 
MET N    N N N 255 
MET CA   C N S 256 
MET C    C N N 257 
MET O    O N N 258 
MET CB   C N N 259 
MET CG   C N N 260 
MET SD   S N N 261 
MET CE   C N N 262 
MET OXT  O N N 263 
MET H    H N N 264 
MET H2   H N N 265 
MET HA   H N N 266 
MET HB2  H N N 267 
MET HB3  H N N 268 
MET HG2  H N N 269 
MET HG3  H N N 270 
MET HE1  H N N 271 
MET HE2  H N N 272 
MET HE3  H N N 273 
MET HXT  H N N 274 
PHE N    N N N 275 
PHE CA   C N S 276 
PHE C    C N N 277 
PHE O    O N N 278 
PHE CB   C N N 279 
PHE CG   C Y N 280 
PHE CD1  C Y N 281 
PHE CD2  C Y N 282 
PHE CE1  C Y N 283 
PHE CE2  C Y N 284 
PHE CZ   C Y N 285 
PHE OXT  O N N 286 
PHE H    H N N 287 
PHE H2   H N N 288 
PHE HA   H N N 289 
PHE HB2  H N N 290 
PHE HB3  H N N 291 
PHE HD1  H N N 292 
PHE HD2  H N N 293 
PHE HE1  H N N 294 
PHE HE2  H N N 295 
PHE HZ   H N N 296 
PHE HXT  H N N 297 
PRO N    N N N 298 
PRO CA   C N S 299 
PRO C    C N N 300 
PRO O    O N N 301 
PRO CB   C N N 302 
PRO CG   C N N 303 
PRO CD   C N N 304 
PRO OXT  O N N 305 
PRO H    H N N 306 
PRO HA   H N N 307 
PRO HB2  H N N 308 
PRO HB3  H N N 309 
PRO HG2  H N N 310 
PRO HG3  H N N 311 
PRO HD2  H N N 312 
PRO HD3  H N N 313 
PRO HXT  H N N 314 
SER N    N N N 315 
SER CA   C N S 316 
SER C    C N N 317 
SER O    O N N 318 
SER CB   C N N 319 
SER OG   O N N 320 
SER OXT  O N N 321 
SER H    H N N 322 
SER H2   H N N 323 
SER HA   H N N 324 
SER HB2  H N N 325 
SER HB3  H N N 326 
SER HG   H N N 327 
SER HXT  H N N 328 
THR N    N N N 329 
THR CA   C N S 330 
THR C    C N N 331 
THR O    O N N 332 
THR CB   C N R 333 
THR OG1  O N N 334 
THR CG2  C N N 335 
THR OXT  O N N 336 
THR H    H N N 337 
THR H2   H N N 338 
THR HA   H N N 339 
THR HB   H N N 340 
THR HG1  H N N 341 
THR HG21 H N N 342 
THR HG22 H N N 343 
THR HG23 H N N 344 
THR HXT  H N N 345 
TRP N    N N N 346 
TRP CA   C N S 347 
TRP C    C N N 348 
TRP O    O N N 349 
TRP CB   C N N 350 
TRP CG   C Y N 351 
TRP CD1  C Y N 352 
TRP CD2  C Y N 353 
TRP NE1  N Y N 354 
TRP CE2  C Y N 355 
TRP CE3  C Y N 356 
TRP CZ2  C Y N 357 
TRP CZ3  C Y N 358 
TRP CH2  C Y N 359 
TRP OXT  O N N 360 
TRP H    H N N 361 
TRP H2   H N N 362 
TRP HA   H N N 363 
TRP HB2  H N N 364 
TRP HB3  H N N 365 
TRP HD1  H N N 366 
TRP HE1  H N N 367 
TRP HE3  H N N 368 
TRP HZ2  H N N 369 
TRP HZ3  H N N 370 
TRP HH2  H N N 371 
TRP HXT  H N N 372 
TYR N    N N N 373 
TYR CA   C N S 374 
TYR C    C N N 375 
TYR O    O N N 376 
TYR CB   C N N 377 
TYR CG   C Y N 378 
TYR CD1  C Y N 379 
TYR CD2  C Y N 380 
TYR CE1  C Y N 381 
TYR CE2  C Y N 382 
TYR CZ   C Y N 383 
TYR OH   O N N 384 
TYR OXT  O N N 385 
TYR H    H N N 386 
TYR H2   H N N 387 
TYR HA   H N N 388 
TYR HB2  H N N 389 
TYR HB3  H N N 390 
TYR HD1  H N N 391 
TYR HD2  H N N 392 
TYR HE1  H N N 393 
TYR HE2  H N N 394 
TYR HH   H N N 395 
TYR HXT  H N N 396 
VAL N    N N N 397 
VAL CA   C N S 398 
VAL C    C N N 399 
VAL O    O N N 400 
VAL CB   C N N 401 
VAL CG1  C N N 402 
VAL CG2  C N N 403 
VAL OXT  O N N 404 
VAL H    H N N 405 
VAL H2   H N N 406 
VAL HA   H N N 407 
VAL HB   H N N 408 
VAL HG11 H N N 409 
VAL HG12 H N N 410 
VAL HG13 H N N 411 
VAL HG21 H N N 412 
VAL HG22 H N N 413 
VAL HG23 H N N 414 
VAL HXT  H N N 415 
# 
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 
0JY O   C    doub N N 1   
0JY C   CA   sing N N 2   
0JY CA  N    sing N N 3   
0JY CA  CB   sing N N 4   
0JY CAC CAI  sing N N 5   
0JY CB  CAI  sing N N 6   
0JY CAI CAB  sing N N 7   
0JY CAI CAA  sing N N 8   
0JY CA  HA   sing N N 9   
0JY N   H2   sing N N 10  
0JY N   H    sing N N 11  
0JY CB  H6   sing N N 12  
0JY CB  H7   sing N N 13  
0JY CAB H8   sing N N 14  
0JY CAB H9   sing N N 15  
0JY CAB H10  sing N N 16  
0JY CAC H11  sing N N 17  
0JY CAC H12  sing N N 18  
0JY CAC H13  sing N N 19  
0JY CAA H14  sing N N 20  
0JY CAA H15  sing N N 21  
0JY CAA H16  sing N N 22  
0JY C   OXT  sing N N 23  
0JY OXT HXT  sing N N 24  
ALA N   CA   sing N N 25  
ALA N   H    sing N N 26  
ALA N   H2   sing N N 27  
ALA CA  C    sing N N 28  
ALA CA  CB   sing N N 29  
ALA CA  HA   sing N N 30  
ALA C   O    doub N N 31  
ALA C   OXT  sing N N 32  
ALA CB  HB1  sing N N 33  
ALA CB  HB2  sing N N 34  
ALA CB  HB3  sing N N 35  
ALA OXT HXT  sing N N 36  
ARG N   CA   sing N N 37  
ARG N   H    sing N N 38  
ARG N   H2   sing N N 39  
ARG CA  C    sing N N 40  
ARG CA  CB   sing N N 41  
ARG CA  HA   sing N N 42  
ARG C   O    doub N N 43  
ARG C   OXT  sing N N 44  
ARG CB  CG   sing N N 45  
ARG CB  HB2  sing N N 46  
ARG CB  HB3  sing N N 47  
ARG CG  CD   sing N N 48  
ARG CG  HG2  sing N N 49  
ARG CG  HG3  sing N N 50  
ARG CD  NE   sing N N 51  
ARG CD  HD2  sing N N 52  
ARG CD  HD3  sing N N 53  
ARG NE  CZ   sing N N 54  
ARG NE  HE   sing N N 55  
ARG CZ  NH1  sing N N 56  
ARG CZ  NH2  doub N N 57  
ARG NH1 HH11 sing N N 58  
ARG NH1 HH12 sing N N 59  
ARG NH2 HH21 sing N N 60  
ARG NH2 HH22 sing N N 61  
ARG OXT HXT  sing N N 62  
ASN N   CA   sing N N 63  
ASN N   H    sing N N 64  
ASN N   H2   sing N N 65  
ASN CA  C    sing N N 66  
ASN CA  CB   sing N N 67  
ASN CA  HA   sing N N 68  
ASN C   O    doub N N 69  
ASN C   OXT  sing N N 70  
ASN CB  CG   sing N N 71  
ASN CB  HB2  sing N N 72  
ASN CB  HB3  sing N N 73  
ASN CG  OD1  doub N N 74  
ASN CG  ND2  sing N N 75  
ASN ND2 HD21 sing N N 76  
ASN ND2 HD22 sing N N 77  
ASN OXT HXT  sing N N 78  
ASP N   CA   sing N N 79  
ASP N   H    sing N N 80  
ASP N   H2   sing N N 81  
ASP CA  C    sing N N 82  
ASP CA  CB   sing N N 83  
ASP CA  HA   sing N N 84  
ASP C   O    doub N N 85  
ASP C   OXT  sing N N 86  
ASP CB  CG   sing N N 87  
ASP CB  HB2  sing N N 88  
ASP CB  HB3  sing N N 89  
ASP CG  OD1  doub N N 90  
ASP CG  OD2  sing N N 91  
ASP OD2 HD2  sing N N 92  
ASP OXT HXT  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 
HIS N   CA   sing N N 153 
HIS N   H    sing N N 154 
HIS N   H2   sing N N 155 
HIS CA  C    sing N N 156 
HIS CA  CB   sing N N 157 
HIS CA  HA   sing N N 158 
HIS C   O    doub N N 159 
HIS C   OXT  sing N N 160 
HIS CB  CG   sing N N 161 
HIS CB  HB2  sing N N 162 
HIS CB  HB3  sing N N 163 
HIS CG  ND1  sing Y N 164 
HIS CG  CD2  doub Y N 165 
HIS ND1 CE1  doub Y N 166 
HIS ND1 HD1  sing N N 167 
HIS CD2 NE2  sing Y N 168 
HIS CD2 HD2  sing N N 169 
HIS CE1 NE2  sing Y N 170 
HIS CE1 HE1  sing N N 171 
HIS NE2 HE2  sing N N 172 
HIS OXT HXT  sing N N 173 
HOH O   H1   sing N N 174 
HOH O   H2   sing N N 175 
ILE N   CA   sing N N 176 
ILE N   H    sing N N 177 
ILE N   H2   sing N N 178 
ILE CA  C    sing N N 179 
ILE CA  CB   sing N N 180 
ILE CA  HA   sing N N 181 
ILE C   O    doub N N 182 
ILE C   OXT  sing N N 183 
ILE CB  CG1  sing N N 184 
ILE CB  CG2  sing N N 185 
ILE CB  HB   sing N N 186 
ILE CG1 CD1  sing N N 187 
ILE CG1 HG12 sing N N 188 
ILE CG1 HG13 sing N N 189 
ILE CG2 HG21 sing N N 190 
ILE CG2 HG22 sing N N 191 
ILE CG2 HG23 sing N N 192 
ILE CD1 HD11 sing N N 193 
ILE CD1 HD12 sing N N 194 
ILE CD1 HD13 sing N N 195 
ILE OXT HXT  sing N N 196 
LEU N   CA   sing N N 197 
LEU N   H    sing N N 198 
LEU N   H2   sing N N 199 
LEU CA  C    sing N N 200 
LEU CA  CB   sing N N 201 
LEU CA  HA   sing N N 202 
LEU C   O    doub N N 203 
LEU C   OXT  sing N N 204 
LEU CB  CG   sing N N 205 
LEU CB  HB2  sing N N 206 
LEU CB  HB3  sing N N 207 
LEU CG  CD1  sing N N 208 
LEU CG  CD2  sing N N 209 
LEU CG  HG   sing N N 210 
LEU CD1 HD11 sing N N 211 
LEU CD1 HD12 sing N N 212 
LEU CD1 HD13 sing N N 213 
LEU CD2 HD21 sing N N 214 
LEU CD2 HD22 sing N N 215 
LEU CD2 HD23 sing N N 216 
LEU OXT HXT  sing N N 217 
LYS N   CA   sing N N 218 
LYS N   H    sing N N 219 
LYS N   H2   sing N N 220 
LYS CA  C    sing N N 221 
LYS CA  CB   sing N N 222 
LYS CA  HA   sing N N 223 
LYS C   O    doub N N 224 
LYS C   OXT  sing N N 225 
LYS CB  CG   sing N N 226 
LYS CB  HB2  sing N N 227 
LYS CB  HB3  sing N N 228 
LYS CG  CD   sing N N 229 
LYS CG  HG2  sing N N 230 
LYS CG  HG3  sing N N 231 
LYS CD  CE   sing N N 232 
LYS CD  HD2  sing N N 233 
LYS CD  HD3  sing N N 234 
LYS CE  NZ   sing N N 235 
LYS CE  HE2  sing N N 236 
LYS CE  HE3  sing N N 237 
LYS NZ  HZ1  sing N N 238 
LYS NZ  HZ2  sing N N 239 
LYS NZ  HZ3  sing N N 240 
LYS OXT HXT  sing N N 241 
MET N   CA   sing N N 242 
MET N   H    sing N N 243 
MET N   H2   sing N N 244 
MET CA  C    sing N N 245 
MET CA  CB   sing N N 246 
MET CA  HA   sing N N 247 
MET C   O    doub N N 248 
MET C   OXT  sing N N 249 
MET CB  CG   sing N N 250 
MET CB  HB2  sing N N 251 
MET CB  HB3  sing N N 252 
MET CG  SD   sing N N 253 
MET CG  HG2  sing N N 254 
MET CG  HG3  sing N N 255 
MET SD  CE   sing N N 256 
MET CE  HE1  sing N N 257 
MET CE  HE2  sing N N 258 
MET CE  HE3  sing N N 259 
MET OXT HXT  sing N N 260 
PHE N   CA   sing N N 261 
PHE N   H    sing N N 262 
PHE N   H2   sing N N 263 
PHE CA  C    sing N N 264 
PHE CA  CB   sing N N 265 
PHE CA  HA   sing N N 266 
PHE C   O    doub N N 267 
PHE C   OXT  sing N N 268 
PHE CB  CG   sing N N 269 
PHE CB  HB2  sing N N 270 
PHE CB  HB3  sing N N 271 
PHE CG  CD1  doub Y N 272 
PHE CG  CD2  sing Y N 273 
PHE CD1 CE1  sing Y N 274 
PHE CD1 HD1  sing N N 275 
PHE CD2 CE2  doub Y N 276 
PHE CD2 HD2  sing N N 277 
PHE CE1 CZ   doub Y N 278 
PHE CE1 HE1  sing N N 279 
PHE CE2 CZ   sing Y N 280 
PHE CE2 HE2  sing N N 281 
PHE CZ  HZ   sing N N 282 
PHE OXT HXT  sing N N 283 
PRO N   CA   sing N N 284 
PRO N   CD   sing N N 285 
PRO N   H    sing N N 286 
PRO CA  C    sing N N 287 
PRO CA  CB   sing N N 288 
PRO CA  HA   sing N N 289 
PRO C   O    doub N N 290 
PRO C   OXT  sing N N 291 
PRO CB  CG   sing N N 292 
PRO CB  HB2  sing N N 293 
PRO CB  HB3  sing N N 294 
PRO CG  CD   sing N N 295 
PRO CG  HG2  sing N N 296 
PRO CG  HG3  sing N N 297 
PRO CD  HD2  sing N N 298 
PRO CD  HD3  sing N N 299 
PRO OXT HXT  sing N N 300 
SER N   CA   sing N N 301 
SER N   H    sing N N 302 
SER N   H2   sing N N 303 
SER CA  C    sing N N 304 
SER CA  CB   sing N N 305 
SER CA  HA   sing N N 306 
SER C   O    doub N N 307 
SER C   OXT  sing N N 308 
SER CB  OG   sing N N 309 
SER CB  HB2  sing N N 310 
SER CB  HB3  sing N N 311 
SER OG  HG   sing N N 312 
SER OXT HXT  sing N N 313 
THR N   CA   sing N N 314 
THR N   H    sing N N 315 
THR N   H2   sing N N 316 
THR CA  C    sing N N 317 
THR CA  CB   sing N N 318 
THR CA  HA   sing N N 319 
THR C   O    doub N N 320 
THR C   OXT  sing N N 321 
THR CB  OG1  sing N N 322 
THR CB  CG2  sing N N 323 
THR CB  HB   sing N N 324 
THR OG1 HG1  sing N N 325 
THR CG2 HG21 sing N N 326 
THR CG2 HG22 sing N N 327 
THR CG2 HG23 sing N N 328 
THR OXT HXT  sing N N 329 
TRP N   CA   sing N N 330 
TRP N   H    sing N N 331 
TRP N   H2   sing N N 332 
TRP CA  C    sing N N 333 
TRP CA  CB   sing N N 334 
TRP CA  HA   sing N N 335 
TRP C   O    doub N N 336 
TRP C   OXT  sing N N 337 
TRP CB  CG   sing N N 338 
TRP CB  HB2  sing N N 339 
TRP CB  HB3  sing N N 340 
TRP CG  CD1  doub Y N 341 
TRP CG  CD2  sing Y N 342 
TRP CD1 NE1  sing Y N 343 
TRP CD1 HD1  sing N N 344 
TRP CD2 CE2  doub Y N 345 
TRP CD2 CE3  sing Y N 346 
TRP NE1 CE2  sing Y N 347 
TRP NE1 HE1  sing N N 348 
TRP CE2 CZ2  sing Y N 349 
TRP CE3 CZ3  doub Y N 350 
TRP CE3 HE3  sing N N 351 
TRP CZ2 CH2  doub Y N 352 
TRP CZ2 HZ2  sing N N 353 
TRP CZ3 CH2  sing Y N 354 
TRP CZ3 HZ3  sing N N 355 
TRP CH2 HH2  sing N N 356 
TRP OXT HXT  sing N N 357 
TYR N   CA   sing N N 358 
TYR N   H    sing N N 359 
TYR N   H2   sing N N 360 
TYR CA  C    sing N N 361 
TYR CA  CB   sing N N 362 
TYR CA  HA   sing N N 363 
TYR C   O    doub N N 364 
TYR C   OXT  sing N N 365 
TYR CB  CG   sing N N 366 
TYR CB  HB2  sing N N 367 
TYR CB  HB3  sing N N 368 
TYR CG  CD1  doub Y N 369 
TYR CG  CD2  sing Y N 370 
TYR CD1 CE1  sing Y N 371 
TYR CD1 HD1  sing N N 372 
TYR CD2 CE2  doub Y N 373 
TYR CD2 HD2  sing N N 374 
TYR CE1 CZ   doub Y N 375 
TYR CE1 HE1  sing N N 376 
TYR CE2 CZ   sing Y N 377 
TYR CE2 HE2  sing N N 378 
TYR CZ  OH   sing N N 379 
TYR OH  HH   sing N N 380 
TYR OXT HXT  sing N N 381 
VAL N   CA   sing N N 382 
VAL N   H    sing N N 383 
VAL N   H2   sing N N 384 
VAL CA  C    sing N N 385 
VAL CA  CB   sing N N 386 
VAL CA  HA   sing N N 387 
VAL C   O    doub N N 388 
VAL C   OXT  sing N N 389 
VAL CB  CG1  sing N N 390 
VAL CB  CG2  sing N N 391 
VAL CB  HB   sing N N 392 
VAL CG1 HG11 sing N N 393 
VAL CG1 HG12 sing N N 394 
VAL CG1 HG13 sing N N 395 
VAL CG2 HG21 sing N N 396 
VAL CG2 HG22 sing N N 397 
VAL CG2 HG23 sing N N 398 
VAL OXT HXT  sing N N 399 
# 
_pdbx_audit_support.funding_organization   'Biotechnology and Biological Sciences Research Council (BBSRC)' 
_pdbx_audit_support.country                'United Kingdom' 
_pdbx_audit_support.grant_number           BB/R004137/1 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   4GGC 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9I6A 
_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]   0.028569 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.010173 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.011512 
_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]   0.022102 
_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   . ILE A 1 168 ? -16.178 2.109   5.281  1.00 39.18 ? 168 ILE A N   1 
ATOM   2    C CA  . ILE A 1 168 ? -15.195 1.641   6.259  1.00 39.43 ? 168 ILE A CA  1 
ATOM   3    C C   . ILE A 1 168 ? -14.764 2.796   7.141  1.00 39.25 ? 168 ILE A C   1 
ATOM   4    O O   . ILE A 1 168 ? -14.253 3.803   6.643  1.00 39.23 ? 168 ILE A O   1 
ATOM   5    C CB  . ILE A 1 168 ? -13.968 1.043   5.541  1.00 39.80 ? 168 ILE A CB  1 
ATOM   6    C CG1 . ILE A 1 168 ? -14.380 -0.004  4.493  1.00 40.76 ? 168 ILE A CG1 1 
ATOM   7    C CG2 . ILE A 1 168 ? -12.956 0.504   6.536  1.00 39.63 ? 168 ILE A CG2 1 
ATOM   8    C CD1 . ILE A 1 168 ? -13.332 -0.312  3.561  1.00 41.44 ? 168 ILE A CD1 1 
ATOM   9    N N   . PRO A 1 169 ? -14.955 2.673   8.457  1.00 39.03 ? 169 PRO A N   1 
ATOM   10   C CA  . PRO A 1 169 ? -14.546 3.769   9.348  1.00 38.49 ? 169 PRO A CA  1 
ATOM   11   C C   . PRO A 1 169 ? -13.035 3.956   9.324  1.00 37.32 ? 169 PRO A C   1 
ATOM   12   O O   . PRO A 1 169 ? -12.295 2.978   9.285  1.00 37.26 ? 169 PRO A O   1 
ATOM   13   C CB  . PRO A 1 169 ? -15.024 3.312   10.736 1.00 39.39 ? 169 PRO A CB  1 
ATOM   14   C CG  . PRO A 1 169 ? -16.010 2.212   10.480 1.00 40.16 ? 169 PRO A CG  1 
ATOM   15   C CD  . PRO A 1 169 ? -15.568 1.558   9.202  1.00 38.71 ? 169 PRO A CD  1 
ATOM   16   N N   . SER A 1 170 ? -12.579 5.205   9.324  1.00 36.06 ? 170 SER A N   1 
ATOM   17   C CA  . SER A 1 170 ? -11.144 5.494   9.362  1.00 35.52 ? 170 SER A CA  1 
ATOM   18   C C   . SER A 1 170 ? -10.577 5.455   10.805 1.00 34.53 ? 170 SER A C   1 
ATOM   19   O O   . SER A 1 170 ? -9.361  5.398   10.986 1.00 34.16 ? 170 SER A O   1 
ATOM   20   C CB  . SER A 1 170 ? -10.849 6.836   8.702  1.00 37.14 ? 170 SER A CB  1 
ATOM   21   O OG  . SER A 1 170 ? -11.548 7.884   9.355  1.00 40.65 ? 170 SER A OG  1 
ATOM   22   N N   . LEU A 1 171 ? -11.459 5.441   11.821 1.00 33.80 ? 171 LEU A N   1 
ATOM   23   C CA  . LEU A 1 171 ? -11.085 5.369   13.220 1.00 34.14 ? 171 LEU A CA  1 
ATOM   24   C C   . LEU A 1 171 ? -11.461 4.001   13.809 1.00 34.07 ? 171 LEU A C   1 
ATOM   25   O O   . LEU A 1 171 ? -12.463 3.390   13.409 1.00 35.21 ? 171 LEU A O   1 
ATOM   26   C CB  . LEU A 1 171 ? -11.809 6.472   14.010 1.00 34.42 ? 171 LEU A CB  1 
ATOM   27   C CG  . LEU A 1 171 ? -11.574 7.906   13.530 1.00 36.11 ? 171 LEU A CG  1 
ATOM   28   C CD1 . LEU A 1 171 ? -12.408 8.869   14.324 1.00 35.99 ? 171 LEU A CD1 1 
ATOM   29   C CD2 . LEU A 1 171 ? -10.093 8.281   13.614 1.00 37.01 ? 171 LEU A CD2 1 
ATOM   30   N N   . PRO A 1 172 ? -10.664 3.497   14.752 1.00 32.63 ? 172 PRO A N   1 
ATOM   31   C CA  . PRO A 1 172 ? -11.044 2.237   15.413 1.00 32.43 ? 172 PRO A CA  1 
ATOM   32   C C   . PRO A 1 172 ? -12.308 2.457   16.274 1.00 32.83 ? 172 PRO A C   1 
ATOM   33   O O   . PRO A 1 172 ? -12.577 3.579   16.653 1.00 32.82 ? 172 PRO A O   1 
ATOM   34   C CB  . PRO A 1 172 ? -9.827  1.929   16.294 1.00 32.78 ? 172 PRO A CB  1 
ATOM   35   C CG  . PRO A 1 172 ? -9.142  3.220   16.484 1.00 33.11 ? 172 PRO A CG  1 
ATOM   36   C CD  . PRO A 1 172 ? -9.455  4.101   15.346 1.00 31.64 ? 172 PRO A CD  1 
ATOM   37   N N   . ASP A 1 173 ? -13.097 1.423   16.557 1.00 32.88 ? 173 ASP A N   1 
ATOM   38   C CA  . ASP A 1 173 ? -14.245 1.561   17.468 1.00 33.71 ? 173 ASP A CA  1 
ATOM   39   C C   . ASP A 1 173 ? -13.776 1.596   18.933 1.00 33.84 ? 173 ASP A C   1 
ATOM   40   O O   . ASP A 1 173 ? -14.460 2.162   19.766 1.00 34.44 ? 173 ASP A O   1 
ATOM   41   C CB  . ASP A 1 173 ? -15.319 0.488   17.240 1.00 36.67 ? 173 ASP A CB  1 
ATOM   42   C CG  . ASP A 1 173 ? -16.281 0.834   16.108 1.00 44.69 ? 173 ASP A CG  1 
ATOM   43   O OD1 . ASP A 1 173 ? -15.809 1.314   15.050 1.00 45.85 ? 173 ASP A OD1 1 
ATOM   44   O OD2 . ASP A 1 173 ? -17.507 0.600   16.270 1.00 47.73 ? 173 ASP A OD2 1 
ATOM   45   N N   . ARG A 1 174 ? -12.622 1.007   19.254 1.00 33.37 ? 174 ARG A N   1 
ATOM   46   C CA  . ARG A 1 174 ? -12.061 1.035   20.608 1.00 33.72 ? 174 ARG A CA  1 
ATOM   47   C C   . ARG A 1 174 ? -10.533 1.062   20.551 1.00 32.52 ? 174 ARG A C   1 
ATOM   48   O O   . ARG A 1 174 ? -9.934  0.554   19.605 1.00 31.71 ? 174 ARG A O   1 
ATOM   49   C CB  . ARG A 1 174 ? -12.462 -0.225  21.410 1.00 36.35 ? 174 ARG A CB  1 
ATOM   50   C CG  . ARG A 1 174 ? -13.892 -0.280  21.897 1.00 41.91 ? 174 ARG A CG  1 
ATOM   51   C CD  . ARG A 1 174 ? -13.948 -0.387  23.397 1.00 47.36 ? 174 ARG A CD  1 
ATOM   52   N NE  . ARG A 1 174 ? -15.177 -1.053  23.826 1.00 52.08 ? 174 ARG A NE  1 
ATOM   53   C CZ  . ARG A 1 174 ? -15.424 -1.437  25.073 1.00 55.59 ? 174 ARG A CZ  1 
ATOM   54   N NH1 . ARG A 1 174 ? -14.537 -1.205  26.035 1.00 55.63 ? 174 ARG A NH1 1 
ATOM   55   N NH2 . ARG A 1 174 ? -16.566 -2.045  25.371 1.00 56.23 ? 174 ARG A NH2 1 
ATOM   56   N N   . ILE A 1 175 ? -9.897  1.606   21.585 1.00 31.99 ? 175 ILE A N   1 
ATOM   57   C CA  . ILE A 1 175 ? -8.448  1.548   21.729 1.00 32.68 ? 175 ILE A CA  1 
ATOM   58   C C   . ILE A 1 175 ? -8.195  1.102   23.142 1.00 33.34 ? 175 ILE A C   1 
ATOM   59   O O   . ILE A 1 175 ? -8.624  1.774   24.083 1.00 33.75 ? 175 ILE A O   1 
ATOM   60   C CB  . ILE A 1 175 ? -7.702  2.863   21.459 1.00 34.05 ? 175 ILE A CB  1 
ATOM   61   C CG1 . ILE A 1 175 ? -7.988  3.367   20.035 1.00 35.77 ? 175 ILE A CG1 1 
ATOM   62   C CG2 . ILE A 1 175 ? -6.191  2.658   21.678 1.00 34.49 ? 175 ILE A CG2 1 
ATOM   63   C CD1 . ILE A 1 175 ? -7.421  4.714   19.741 1.00 37.06 ? 175 ILE A CD1 1 
ATOM   64   N N   . LEU A 1 176 ? -7.567  -0.056  23.297 1.00 33.01 ? 176 LEU A N   1 
ATOM   65   C CA  . LEU A 1 176 ? -7.242  -0.607  24.598 1.00 32.85 ? 176 LEU A CA  1 
ATOM   66   C C   . LEU A 1 176 ? -5.757  -0.350  24.855 1.00 31.89 ? 176 LEU A C   1 
ATOM   67   O O   . LEU A 1 176 ? -4.934  -0.487  23.945 1.00 31.25 ? 176 LEU A O   1 
ATOM   68   C CB  . LEU A 1 176 ? -7.504  -2.135  24.601 1.00 33.55 ? 176 LEU A CB  1 
ATOM   69   C CG  . LEU A 1 176 ? -8.877  -2.623  24.122 1.00 35.50 ? 176 LEU A CG  1 
ATOM   70   C CD1 . LEU A 1 176 ? -8.935  -4.137  24.098 1.00 35.98 ? 176 LEU A CD1 1 
ATOM   71   C CD2 . LEU A 1 176 ? -9.998  -2.080  24.987 1.00 36.49 ? 176 LEU A CD2 1 
ATOM   72   N N   . ASP A 1 177 ? -5.403  0.010   26.091 1.00 32.16 ? 177 ASP A N   1 
ATOM   73   C CA  . ASP A 1 177 ? -3.994  0.180   26.432 1.00 32.32 ? 177 ASP A CA  1 
ATOM   74   C C   . ASP A 1 177 ? -3.368  -1.225  26.493 1.00 31.61 ? 177 ASP A C   1 
ATOM   75   O O   . ASP A 1 177 ? -3.976  -2.173  26.956 1.00 31.47 ? 177 ASP A O   1 
ATOM   76   C CB  . ASP A 1 177 ? -3.801  0.945   27.754 1.00 35.47 ? 177 ASP A CB  1 
ATOM   77   C CG  . ASP A 1 177 ? -2.416  1.574   27.908 1.00 43.26 ? 177 ASP A CG  1 
ATOM   78   O OD1 . ASP A 1 177 ? -1.521  1.263   27.080 1.00 44.92 ? 177 ASP A OD1 1 
ATOM   79   O OD2 . ASP A 1 177 ? -2.224  2.383   28.858 1.00 46.42 ? 177 ASP A OD2 1 
ATOM   80   N N   . ALA A 1 178 ? -2.191  -1.369  25.941 1.00 30.98 ? 178 ALA A N   1 
ATOM   81   C CA  . ALA A 1 178 ? -1.436  -2.620  25.963 1.00 30.23 ? 178 ALA A CA  1 
ATOM   82   C C   . ALA A 1 178 ? -0.048  -2.288  26.527 1.00 29.40 ? 178 ALA A C   1 
ATOM   83   O O   . ALA A 1 178 ? 0.960   -2.390  25.831 1.00 29.35 ? 178 ALA A O   1 
ATOM   84   C CB  . ALA A 1 178 ? -1.331  -3.189  24.551 1.00 30.36 ? 178 ALA A CB  1 
ATOM   85   N N   . PRO A 1 179 ? 0.023   -1.837  27.796 1.00 29.06 ? 179 PRO A N   1 
ATOM   86   C CA  . PRO A 1 179 ? 1.325   -1.476  28.362 1.00 29.15 ? 179 PRO A CA  1 
ATOM   87   C C   . PRO A 1 179 ? 2.253   -2.668  28.407 1.00 29.21 ? 179 PRO A C   1 
ATOM   88   O O   . PRO A 1 179 ? 1.803   -3.784  28.654 1.00 28.92 ? 179 PRO A O   1 
ATOM   89   C CB  . PRO A 1 179 ? 0.976   -0.957  29.757 1.00 29.45 ? 179 PRO A CB  1 
ATOM   90   C CG  . PRO A 1 179 ? -0.319  -1.610  30.081 1.00 29.83 ? 179 PRO A CG  1 
ATOM   91   C CD  . PRO A 1 179 ? -1.054  -1.686  28.789 1.00 28.20 ? 179 PRO A CD  1 
ATOM   92   N N   . GLU A 1 180 ? 3.528   -2.439  28.082 1.00 29.40 ? 180 GLU A N   1 
ATOM   93   C CA  . GLU A 1 180 ? 4.561   -3.464  28.114 1.00 30.19 ? 180 GLU A CA  1 
ATOM   94   C C   . GLU A 1 180 ? 4.399   -4.571  27.097 1.00 30.24 ? 180 GLU A C   1 
ATOM   95   O O   . GLU A 1 180 ? 5.030   -5.612  27.250 1.00 31.11 ? 180 GLU A O   1 
ATOM   96   C CB  . GLU A 1 180 ? 4.702   -4.074  29.508 1.00 33.67 ? 180 GLU A CB  1 
ATOM   97   C CG  . GLU A 1 180 ? 5.040   -3.090  30.606 1.00 41.56 ? 180 GLU A CG  1 
ATOM   98   C CD  . GLU A 1 180 ? 5.531   -3.816  31.840 1.00 54.51 ? 180 GLU A CD  1 
ATOM   99   O OE1 . GLU A 1 180 ? 6.687   -4.304  31.813 1.00 57.32 ? 180 GLU A OE1 1 
ATOM   100  O OE2 . GLU A 1 180 ? 4.750   -3.941  32.813 1.00 58.41 ? 180 GLU A OE2 1 
ATOM   101  N N   . ILE A 1 181 ? 3.622   -4.360  26.017 1.00 29.15 ? 181 ILE A N   1 
ATOM   102  C CA  . ILE A 1 181 ? 3.526   -5.359  24.959 1.00 28.72 ? 181 ILE A CA  1 
ATOM   103  C C   . ILE A 1 181 ? 4.931   -5.547  24.351 1.00 29.26 ? 181 ILE A C   1 
ATOM   104  O O   . ILE A 1 181 ? 5.681   -4.577  24.178 1.00 29.07 ? 181 ILE A O   1 
ATOM   105  C CB  . ILE A 1 181 ? 2.472   -5.021  23.891 1.00 27.93 ? 181 ILE A CB  1 
ATOM   106  C CG1 . ILE A 1 181 ? 2.235   -6.236  22.983 1.00 28.53 ? 181 ILE A CG1 1 
ATOM   107  C CG2 . ILE A 1 181 ? 2.893   -3.818  23.099 1.00 28.16 ? 181 ILE A CG2 1 
ATOM   108  C CD1 . ILE A 1 181 ? 0.939   -6.179  22.190 1.00 29.72 ? 181 ILE A CD1 1 
ATOM   109  N N   . ARG A 1 182 ? 5.334   -6.797  24.228 1.00 29.28 ? 182 ARG A N   1 
ATOM   110  C CA  . ARG A 1 182 ? 6.666   -7.121  23.773 1.00 29.66 ? 182 ARG A CA  1 
ATOM   111  C C   . ARG A 1 182 ? 6.842   -6.789  22.314 1.00 29.27 ? 182 ARG A C   1 
ATOM   112  O O   . ARG A 1 182 ? 6.148   -7.348  21.468 1.00 29.05 ? 182 ARG A O   1 
ATOM   113  C CB  . ARG A 1 182 ? 6.954   -8.589  24.034 1.00 31.69 ? 182 ARG A CB  1 
ATOM   114  C CG  . ARG A 1 182 ? 8.418   -8.842  24.106 1.00 36.76 ? 182 ARG A CG  1 
ATOM   115  C CD  . ARG A 1 182 ? 8.715   -10.157 24.756 1.00 40.40 ? 182 ARG A CD  1 
ATOM   116  N NE  . ARG A 1 182 ? 10.163  -10.332 24.839 1.00 41.84 ? 182 ARG A NE  1 
ATOM   117  C CZ  . ARG A 1 182 ? 10.886  -10.082 25.919 1.00 39.39 ? 182 ARG A CZ  1 
ATOM   118  N NH1 . ARG A 1 182 ? 10.300  -9.694  27.043 1.00 36.86 ? 182 ARG A NH1 1 
ATOM   119  N NH2 . ARG A 1 182 ? 12.192  -10.266 25.899 1.00 39.01 ? 182 ARG A NH2 1 
ATOM   120  N N   . ASN A 1 183 ? 7.760   -5.867  22.012 1.00 29.03 ? 183 ASN A N   1 
ATOM   121  C CA  . ASN A 1 183 ? 8.011   -5.475  20.634 1.00 29.39 ? 183 ASN A CA  1 
ATOM   122  C C   . ASN A 1 183 ? 8.950   -6.465  19.969 1.00 30.01 ? 183 ASN A C   1 
ATOM   123  O O   . ASN A 1 183 ? 10.104  -6.135  19.657 1.00 30.41 ? 183 ASN A O   1 
ATOM   124  C CB  . ASN A 1 183 ? 8.559   -4.050  20.535 1.00 30.02 ? 183 ASN A CB  1 
ATOM   125  C CG  . ASN A 1 183 ? 8.592   -3.539  19.115 1.00 32.93 ? 183 ASN A CG  1 
ATOM   126  O OD1 . ASN A 1 183 ? 8.038   -4.144  18.183 1.00 33.29 ? 183 ASN A OD1 1 
ATOM   127  N ND2 . ASN A 1 183 ? 9.209   -2.403  18.919 1.00 33.67 ? 183 ASN A ND2 1 
ATOM   128  N N   . ASP A 1 184 ? 8.463   -7.701  19.809 1.00 29.64 ? 184 ASP A N   1 
ATOM   129  C CA  . ASP A 1 184 ? 9.201   -8.789  19.200 1.00 30.02 ? 184 ASP A CA  1 
ATOM   130  C C   . ASP A 1 184 ? 8.323   -9.284  18.090 1.00 30.30 ? 184 ASP A C   1 
ATOM   131  O O   . ASP A 1 184 ? 7.260   -9.855  18.343 1.00 30.73 ? 184 ASP A O   1 
ATOM   132  C CB  . ASP A 1 184 ? 9.453   -9.900  20.211 1.00 32.00 ? 184 ASP A CB  1 
ATOM   133  C CG  . ASP A 1 184 ? 10.425  -10.944 19.717 1.00 37.33 ? 184 ASP A CG  1 
ATOM   134  O OD1 . ASP A 1 184 ? 10.234  -11.447 18.589 1.00 37.73 ? 184 ASP A OD1 1 
ATOM   135  O OD2 . ASP A 1 184 ? 11.375  -11.268 20.462 1.00 39.95 ? 184 ASP A OD2 1 
ATOM   136  N N   . TYR A 1 185 ? 8.767   -9.059  16.859 1.00 29.19 ? 185 TYR A N   1 
ATOM   137  C CA  . TYR A 1 185 ? 8.057   -9.386  15.643 1.00 29.25 ? 185 TYR A CA  1 
ATOM   138  C C   . TYR A 1 185 ? 7.604   -10.825 15.534 1.00 28.86 ? 185 TYR A C   1 
ATOM   139  O O   . TYR A 1 185 ? 6.569   -11.083 14.941 1.00 29.30 ? 185 TYR A O   1 
ATOM   140  C CB  . TYR A 1 185 ? 8.948   -9.023  14.435 1.00 29.61 ? 185 TYR A CB  1 
ATOM   141  C CG  . TYR A 1 185 ? 8.272   -9.167  13.093 1.00 31.45 ? 185 TYR A CG  1 
ATOM   142  C CD1 . TYR A 1 185 ? 7.396   -8.201  12.627 1.00 32.76 ? 185 TYR A CD1 1 
ATOM   143  C CD2 . TYR A 1 185 ? 8.530   -10.259 12.277 1.00 32.72 ? 185 TYR A CD2 1 
ATOM   144  C CE1 . TYR A 1 185 ? 6.780   -8.324  11.392 1.00 33.75 ? 185 TYR A CE1 1 
ATOM   145  C CE2 . TYR A 1 185 ? 7.915   -10.395 11.042 1.00 33.58 ? 185 TYR A CE2 1 
ATOM   146  C CZ  . TYR A 1 185 ? 7.033   -9.430  10.609 1.00 34.77 ? 185 TYR A CZ  1 
ATOM   147  O OH  . TYR A 1 185 ? 6.414   -9.565  9.394  1.00 37.15 ? 185 TYR A OH  1 
ATOM   148  N N   . TYR A 1 186 ? 8.373   -11.771 16.053 1.00 27.75 ? 186 TYR A N   1 
ATOM   149  C CA  . TYR A 1 186 ? 8.093   -13.202 15.859 1.00 27.07 ? 186 TYR A CA  1 
ATOM   150  C C   . TYR A 1 186 ? 7.037   -13.800 16.787 1.00 25.18 ? 186 TYR A C   1 
ATOM   151  O O   . TYR A 1 186 ? 6.593   -14.937 16.567 1.00 25.04 ? 186 TYR A O   1 
ATOM   152  C CB  . TYR A 1 186 ? 9.396   -13.998 15.950 1.00 27.67 ? 186 TYR A CB  1 
ATOM   153  C CG  . TYR A 1 186 ? 10.439  -13.451 14.999 1.00 29.55 ? 186 TYR A CG  1 
ATOM   154  C CD1 . TYR A 1 186 ? 10.362  -13.702 13.635 1.00 30.64 ? 186 TYR A CD1 1 
ATOM   155  C CD2 . TYR A 1 186 ? 11.415  -12.569 15.440 1.00 30.72 ? 186 TYR A CD2 1 
ATOM   156  C CE1 . TYR A 1 186 ? 11.264  -13.139 12.745 1.00 31.71 ? 186 TYR A CE1 1 
ATOM   157  C CE2 . TYR A 1 186 ? 12.330  -12.010 14.561 1.00 31.83 ? 186 TYR A CE2 1 
ATOM   158  C CZ  . TYR A 1 186 ? 12.265  -12.313 13.214 1.00 32.76 ? 186 TYR A CZ  1 
ATOM   159  O OH  . TYR A 1 186 ? 13.187  -11.781 12.338 1.00 33.89 ? 186 TYR A OH  1 
ATOM   160  N N   . LEU A 1 187 ? 6.621   -13.042 17.796 1.00 22.83 ? 187 LEU A N   1 
ATOM   161  C CA  . LEU A 1 187 ? 5.636   -13.534 18.743 1.00 21.84 ? 187 LEU A CA  1 
ATOM   162  C C   . LEU A 1 187 ? 4.197   -13.336 18.285 1.00 21.75 ? 187 LEU A C   1 
ATOM   163  O O   . LEU A 1 187 ? 3.912   -12.428 17.515 1.00 22.56 ? 187 LEU A O   1 
ATOM   164  C CB  . LEU A 1 187 ? 5.859   -12.880 20.097 1.00 20.92 ? 187 LEU A CB  1 
ATOM   165  C CG  . LEU A 1 187 ? 7.264   -12.994 20.669 1.00 21.33 ? 187 LEU A CG  1 
ATOM   166  C CD1 . LEU A 1 187 ? 7.329   -12.335 22.014 1.00 21.81 ? 187 LEU A CD1 1 
ATOM   167  C CD2 . LEU A 1 187 ? 7.769   -14.458 20.679 1.00 20.80 ? 187 LEU A CD2 1 
ATOM   168  N N   . ASN A 1 188 ? 3.282   -14.158 18.790 1.00 20.37 ? 188 ASN A N   1 
ATOM   169  C CA  . ASN A 1 188 ? 1.880   -14.072 18.419 1.00 19.59 ? 188 ASN A CA  1 
ATOM   170  C C   . ASN A 1 188 ? 1.132   -13.872 19.707 1.00 19.27 ? 188 ASN A C   1 
ATOM   171  O O   . ASN A 1 188 ? 0.703   -14.819 20.357 1.00 18.23 ? 188 ASN A O   1 
ATOM   172  C CB  . ASN A 1 188 ? 1.481   -15.338 17.699 1.00 20.10 ? 188 ASN A CB  1 
ATOM   173  C CG  . ASN A 1 188 ? 2.098   -15.378 16.318 1.00 23.42 ? 188 ASN A CG  1 
ATOM   174  O OD1 . ASN A 1 188 ? 1.518   -14.898 15.346 1.00 24.95 ? 188 ASN A OD1 1 
ATOM   175  N ND2 . ASN A 1 188 ? 3.292   -15.931 16.192 1.00 23.01 ? 188 ASN A ND2 1 
ATOM   176  N N   . LEU A 1 189 ? 1.032   -12.615 20.108 1.00 19.67 ? 189 LEU A N   1 
ATOM   177  C CA  . LEU A 1 189 ? 0.575   -12.243 21.426 1.00 19.98 ? 189 LEU A CA  1 
ATOM   178  C C   . LEU A 1 189 ? -0.888  -11.969 21.598 1.00 20.32 ? 189 LEU A C   1 
ATOM   179  O O   . LEU A 1 189 ? -1.281  -11.675 22.721 1.00 20.19 ? 189 LEU A O   1 
ATOM   180  C CB  . LEU A 1 189 ? 1.370   -11.024 21.886 1.00 20.77 ? 189 LEU A CB  1 
ATOM   181  C CG  . LEU A 1 189 ? 2.890   -11.218 21.841 1.00 22.35 ? 189 LEU A CG  1 
ATOM   182  C CD1 . LEU A 1 189 ? 3.606   -9.907  22.048 1.00 22.63 ? 189 LEU A CD1 1 
ATOM   183  C CD2 . LEU A 1 189 ? 3.327   -12.271 22.832 1.00 23.02 ? 189 LEU A CD2 1 
ATOM   184  N N   . VAL A 1 190 ? -1.700  -12.030 20.528 1.00 20.63 ? 190 VAL A N   1 
ATOM   185  C CA  . VAL A 1 190 ? -3.118  -11.754 20.679 1.00 21.46 ? 190 VAL A CA  1 
ATOM   186  C C   . VAL A 1 190 ? -3.961  -12.771 19.950 1.00 20.99 ? 190 VAL A C   1 
ATOM   187  O O   . VAL A 1 190 ? -3.574  -13.282 18.895 1.00 20.10 ? 190 VAL A O   1 
ATOM   188  C CB  . VAL A 1 190 ? -3.514  -10.300 20.294 1.00 23.26 ? 190 VAL A CB  1 
ATOM   189  C CG1 . VAL A 1 190 ? -2.760  -9.263  21.126 1.00 24.31 ? 190 VAL A CG1 1 
ATOM   190  C CG2 . VAL A 1 190 ? -3.310  -10.043 18.808 1.00 24.04 ? 190 VAL A CG2 1 
ATOM   191  N N   . ASP A 1 191 ? -5.140  -13.036 20.498 1.00 20.75 ? 191 ASP A N   1 
ATOM   192  C CA  . ASP A 1 191 ? -6.079  -13.932 19.874 1.00 21.40 ? 191 ASP A CA  1 
ATOM   193  C C   . ASP A 1 191 ? -7.474  -13.654 20.372 1.00 21.60 ? 191 ASP A C   1 
ATOM   194  O O   . ASP A 1 191 ? -7.660  -13.393 21.542 1.00 21.88 ? 191 ASP A O   1 
ATOM   195  C CB  . ASP A 1 191 ? -5.701  -15.413 20.044 1.00 23.19 ? 191 ASP A CB  1 
ATOM   196  C CG  . ASP A 1 191 ? -6.366  -16.318 19.005 1.00 27.98 ? 191 ASP A CG  1 
ATOM   197  O OD1 . ASP A 1 191 ? -6.853  -15.796 17.982 1.00 28.17 ? 191 ASP A OD1 1 
ATOM   198  O OD2 . ASP A 1 191 ? -6.414  -17.540 19.225 1.00 31.19 ? 191 ASP A OD2 1 
ATOM   199  N N   . TRP A 1 192 ? -8.447  -13.670 19.476 1.00 21.44 ? 192 TRP A N   1 
ATOM   200  C CA  . TRP A 1 192 ? -9.825  -13.386 19.820 1.00 22.19 ? 192 TRP A CA  1 
ATOM   201  C C   . TRP A 1 192 ? -10.588 -14.703 19.785 1.00 23.07 ? 192 TRP A C   1 
ATOM   202  O O   . TRP A 1 192 ? -10.584 -15.399 18.772 1.00 23.57 ? 192 TRP A O   1 
ATOM   203  C CB  . TRP A 1 192 ? -10.381 -12.401 18.805 1.00 22.00 ? 192 TRP A CB  1 
ATOM   204  C CG  . TRP A 1 192 ? -11.505 -11.559 19.308 1.00 22.45 ? 192 TRP A CG  1 
ATOM   205  C CD1 . TRP A 1 192 ? -12.494 -11.924 20.176 1.00 23.31 ? 192 TRP A CD1 1 
ATOM   206  C CD2 . TRP A 1 192 ? -11.714 -10.176 19.019 1.00 22.43 ? 192 TRP A CD2 1 
ATOM   207  N NE1 . TRP A 1 192 ? -13.334 -10.858 20.407 1.00 23.44 ? 192 TRP A NE1 1 
ATOM   208  C CE2 . TRP A 1 192 ? -12.892 -9.782  19.682 1.00 23.17 ? 192 TRP A CE2 1 
ATOM   209  C CE3 . TRP A 1 192 ? -11.053 -9.249  18.216 1.00 23.15 ? 192 TRP A CE3 1 
ATOM   210  C CZ2 . TRP A 1 192 ? -13.400 -8.493  19.582 1.00 23.90 ? 192 TRP A CZ2 1 
ATOM   211  C CZ3 . TRP A 1 192 ? -11.578 -7.983  18.098 1.00 23.96 ? 192 TRP A CZ3 1 
ATOM   212  C CH2 . TRP A 1 192 ? -12.733 -7.616  18.778 1.00 23.84 ? 192 TRP A CH2 1 
ATOM   213  N N   . SER A 1 193 ? -11.188 -15.074 20.900 1.00 22.64 ? 193 SER A N   1 
ATOM   214  C CA  . SER A 1 193 ? -11.869 -16.356 21.015 1.00 22.82 ? 193 SER A CA  1 
ATOM   215  C C   . SER A 1 193 ? -13.219 -16.366 20.364 1.00 24.35 ? 193 SER A C   1 
ATOM   216  O O   . SER A 1 193 ? -13.859 -15.317 20.257 1.00 25.03 ? 193 SER A O   1 
ATOM   217  C CB  . SER A 1 193 ? -12.046 -16.723 22.488 1.00 21.62 ? 193 SER A CB  1 
ATOM   218  O OG  . SER A 1 193 ? -13.189 -16.115 23.055 1.00 23.20 ? 193 SER A OG  1 
ATOM   219  N N   . SER A 1 194 ? -13.720 -17.572 20.091 1.00 24.80 ? 194 SER A N   1 
ATOM   220  C CA  . SER A 1 194 ? -15.065 -17.767 19.600 1.00 25.75 ? 194 SER A CA  1 
ATOM   221  C C   . SER A 1 194 ? -16.119 -17.320 20.625 1.00 26.71 ? 194 SER A C   1 
ATOM   222  O O   . SER A 1 194 ? -17.258 -17.098 20.236 1.00 27.63 ? 194 SER A O   1 
ATOM   223  C CB  . SER A 1 194 ? -15.284 -19.221 19.194 1.00 27.26 ? 194 SER A CB  1 
ATOM   224  O OG  . SER A 1 194 ? -15.265 -20.078 20.319 1.00 30.19 ? 194 SER A OG  1 
ATOM   225  N N   . GLY A 1 195 ? -15.737 -17.180 21.900 1.00 26.56 ? 195 GLY A N   1 
ATOM   226  C CA  . GLY A 1 195 ? -16.585 -16.673 22.977 1.00 26.66 ? 195 GLY A CA  1 
ATOM   227  C C   . GLY A 1 195 ? -16.504 -15.160 23.142 1.00 26.64 ? 195 GLY A C   1 
ATOM   228  O O   . GLY A 1 195 ? -17.016 -14.605 24.114 1.00 26.97 ? 195 GLY A O   1 
ATOM   229  N N   . ASN A 1 196 ? -15.859 -14.474 22.193 1.00 26.27 ? 196 ASN A N   1 
ATOM   230  C CA  . ASN A 1 196 ? -15.734 -13.017 22.177 1.00 25.69 ? 196 ASN A CA  1 
ATOM   231  C C   . ASN A 1 196 ? -14.830 -12.459 23.296 1.00 23.54 ? 196 ASN A C   1 
ATOM   232  O O   . ASN A 1 196 ? -15.028 -11.340 23.772 1.00 23.03 ? 196 ASN A O   1 
ATOM   233  C CB  . ASN A 1 196 ? -17.106 -12.334 22.156 1.00 26.87 ? 196 ASN A CB  1 
ATOM   234  C CG  . ASN A 1 196 ? -17.080 -10.999 21.478 1.00 30.86 ? 196 ASN A CG  1 
ATOM   235  O OD1 . ASN A 1 196 ? -16.203 -10.725 20.654 1.00 32.42 ? 196 ASN A OD1 1 
ATOM   236  N ND2 . ASN A 1 196 ? -18.029 -10.134 21.821 1.00 32.16 ? 196 ASN A ND2 1 
ATOM   237  N N   . VAL A 1 197 ? -13.790 -13.211 23.645 1.00 22.26 ? 197 VAL A N   1 
ATOM   238  C CA  . VAL A 1 197 ? -12.818 -12.769 24.644 1.00 22.10 ? 197 VAL A CA  1 
ATOM   239  C C   . VAL A 1 197 ? -11.461 -12.619 23.968 1.00 22.22 ? 197 VAL A C   1 
ATOM   240  O O   . VAL A 1 197 ? -10.979 -13.538 23.307 1.00 22.19 ? 197 VAL A O   1 
ATOM   241  C CB  . VAL A 1 197 ? -12.757 -13.730 25.854 1.00 22.70 ? 197 VAL A CB  1 
ATOM   242  C CG1 . VAL A 1 197 ? -11.681 -13.306 26.860 1.00 22.85 ? 197 VAL A CG1 1 
ATOM   243  C CG2 . VAL A 1 197 ? -14.128 -13.839 26.546 1.00 22.37 ? 197 VAL A CG2 1 
ATOM   244  N N   . LEU A 1 198 ? -10.874 -11.448 24.087 1.00 21.95 ? 198 LEU A N   1 
ATOM   245  C CA  . LEU A 1 198 ? -9.566  -11.168 23.521 1.00 22.03 ? 198 LEU A CA  1 
ATOM   246  C C   . LEU A 1 198 ? -8.522  -11.533 24.544 1.00 21.68 ? 198 LEU A C   1 
ATOM   247  O O   . LEU A 1 198 ? -8.575  -11.052 25.671 1.00 21.68 ? 198 LEU A O   1 
ATOM   248  C CB  . LEU A 1 198 ? -9.477  -9.661  23.253 1.00 22.32 ? 198 LEU A CB  1 
ATOM   249  C CG  . LEU A 1 198 ? -8.528  -9.161  22.180 1.00 23.84 ? 198 LEU A CG  1 
ATOM   250  C CD1 . LEU A 1 198 ? -8.726  -9.907  20.871 1.00 23.08 ? 198 LEU A CD1 1 
ATOM   251  C CD2 . LEU A 1 198 ? -8.712  -7.658  21.990 1.00 24.45 ? 198 LEU A CD2 1 
ATOM   252  N N   . ALA A 1 199 ? -7.572  -12.358 24.163 1.00 21.35 ? 199 ALA A N   1 
ATOM   253  C CA  . ALA A 1 199 ? -6.463  -12.721 25.030 1.00 21.47 ? 199 ALA A CA  1 
ATOM   254  C C   . ALA A 1 199 ? -5.293  -11.899 24.558 1.00 21.12 ? 199 ALA A C   1 
ATOM   255  O O   . ALA A 1 199 ? -4.985  -11.874 23.356 1.00 21.31 ? 199 ALA A O   1 
ATOM   256  C CB  . ALA A 1 199 ? -6.154  -14.204 24.904 1.00 22.04 ? 199 ALA A CB  1 
ATOM   257  N N   . VAL A 1 200 ? -4.702  -11.151 25.474 1.00 20.69 ? 200 VAL A N   1 
ATOM   258  C CA  . VAL A 1 200 ? -3.600  -10.264 25.156 1.00 21.78 ? 200 VAL A CA  1 
ATOM   259  C C   . VAL A 1 200 ? -2.422  -10.548 26.066 1.00 22.38 ? 200 VAL A C   1 
ATOM   260  O O   . VAL A 1 200 ? -2.538  -10.392 27.291 1.00 22.66 ? 200 VAL A O   1 
ATOM   261  C CB  . VAL A 1 200 ? -4.044  -8.786  25.310 1.00 22.60 ? 200 VAL A CB  1 
ATOM   262  C CG1 . VAL A 1 200 ? -2.920  -7.848  24.904 1.00 23.13 ? 200 VAL A CG1 1 
ATOM   263  C CG2 . VAL A 1 200 ? -5.320  -8.498  24.509 1.00 22.96 ? 200 VAL A CG2 1 
ATOM   264  N N   . ALA A 1 201 ? -1.287  -10.943 25.493 1.00 22.06 ? 201 ALA A N   1 
ATOM   265  C CA  . ALA A 1 201 ? -0.097  -11.198 26.307 1.00 22.53 ? 201 ALA A CA  1 
ATOM   266  C C   . ALA A 1 201 ? 0.706   -9.921  26.430 1.00 22.78 ? 201 ALA A C   1 
ATOM   267  O O   . ALA A 1 201 ? 1.159   -9.380  25.426 1.00 22.49 ? 201 ALA A O   1 
ATOM   268  C CB  . ALA A 1 201 ? 0.744   -12.273 25.675 1.00 22.58 ? 201 ALA A CB  1 
ATOM   269  N N   . LEU A 1 202 ? 0.873   -9.434  27.656 1.00 22.56 ? 202 LEU A N   1 
ATOM   270  C CA  . LEU A 1 202 ? 1.630   -8.225  27.935 1.00 23.36 ? 202 LEU A CA  1 
ATOM   271  C C   . LEU A 1 202 ? 2.794   -8.596  28.831 1.00 23.90 ? 202 LEU A C   1 
ATOM   272  O O   . LEU A 1 202 ? 2.615   -8.808  30.025 1.00 24.07 ? 202 LEU A O   1 
ATOM   273  C CB  . LEU A 1 202 ? 0.757   -7.172  28.619 1.00 23.65 ? 202 LEU A CB  1 
ATOM   274  C CG  . LEU A 1 202 ? -0.458  -6.694  27.828 1.00 25.53 ? 202 LEU A CG  1 
ATOM   275  C CD1 . LEU A 1 202 ? -1.225  -5.655  28.619 1.00 26.18 ? 202 LEU A CD1 1 
ATOM   276  C CD2 . LEU A 1 202 ? -0.045  -6.092  26.496 1.00 26.55 ? 202 LEU A CD2 1 
ATOM   277  N N   . ASP A 1 203 ? 3.983   -8.701  28.232 1.00 23.47 ? 203 ASP A N   1 
ATOM   278  C CA  . ASP A 1 203 ? 5.203   -9.107  28.891 1.00 23.62 ? 203 ASP A CA  1 
ATOM   279  C C   . ASP A 1 203 ? 5.034   -10.498 29.522 1.00 23.23 ? 203 ASP A C   1 
ATOM   280  O O   . ASP A 1 203 ? 4.941   -11.471 28.775 1.00 22.28 ? 203 ASP A O   1 
ATOM   281  C CB  . ASP A 1 203 ? 5.737   -8.032  29.847 1.00 26.18 ? 203 ASP A CB  1 
ATOM   282  C CG  . ASP A 1 203 ? 7.031   -8.454  30.508 1.00 32.40 ? 203 ASP A CG  1 
ATOM   283  O OD1 . ASP A 1 203 ? 7.849   -9.132  29.834 1.00 32.56 ? 203 ASP A OD1 1 
ATOM   284  O OD2 . ASP A 1 203 ? 7.216   -8.132  31.707 1.00 35.76 ? 203 ASP A OD2 1 
ATOM   285  N N   . ASN A 1 204 ? 4.950   -10.606 30.858 1.00 23.50 ? 204 ASN A N   1 
ATOM   286  C CA  . ASN A 1 204 ? 4.818   -11.892 31.510 1.00 24.10 ? 204 ASN A CA  1 
ATOM   287  C C   . ASN A 1 204 ? 3.403   -12.240 31.931 1.00 25.11 ? 204 ASN A C   1 
ATOM   288  O O   . ASN A 1 204 ? 3.223   -13.198 32.677 1.00 25.99 ? 204 ASN A O   1 
ATOM   289  C CB  . ASN A 1 204 ? 5.758   -11.966 32.711 1.00 25.15 ? 204 ASN A CB  1 
ATOM   290  C CG  . ASN A 1 204 ? 5.399   -11.043 33.844 1.00 29.29 ? 204 ASN A CG  1 
ATOM   291  O OD1 . ASN A 1 204 ? 4.605   -10.110 33.686 1.00 30.92 ? 204 ASN A OD1 1 
ATOM   292  N ND2 . ASN A 1 204 ? 5.988   -11.274 35.022 1.00 29.18 ? 204 ASN A ND2 1 
ATOM   293  N N   . SER A 1 205 ? 2.406   -11.469 31.506 1.00 24.49 ? 205 SER A N   1 
ATOM   294  C CA  . SER A 1 205 ? 1.040   -11.712 31.927 1.00 24.01 ? 205 SER A CA  1 
ATOM   295  C C   . SER A 1 205 ? 0.139   -11.872 30.743 1.00 23.32 ? 205 SER A C   1 
ATOM   296  O O   . SER A 1 205 ? 0.438   -11.371 29.669 1.00 23.50 ? 205 SER A O   1 
ATOM   297  C CB  . SER A 1 205 ? 0.547   -10.538 32.758 1.00 25.58 ? 205 SER A CB  1 
ATOM   298  O OG  . SER A 1 205 ? 1.234   -10.443 33.995 1.00 30.03 ? 205 SER A OG  1 
ATOM   299  N N   . VAL A 1 206 ? -0.979  -12.544 30.940 1.00 22.27 ? 206 VAL A N   1 
ATOM   300  C CA  . VAL A 1 206 ? -1.998  -12.658 29.915 1.00 21.86 ? 206 VAL A CA  1 
ATOM   301  C C   . VAL A 1 206 ? -3.228  -12.013 30.497 1.00 21.44 ? 206 VAL A C   1 
ATOM   302  O O   . VAL A 1 206 ? -3.636  -12.320 31.622 1.00 20.45 ? 206 VAL A O   1 
ATOM   303  C CB  . VAL A 1 206 ? -2.290  -14.106 29.446 1.00 22.32 ? 206 VAL A CB  1 
ATOM   304  C CG1 . VAL A 1 206 ? -3.467  -14.144 28.472 1.00 22.20 ? 206 VAL A CG1 1 
ATOM   305  C CG2 . VAL A 1 206 ? -1.049  -14.733 28.819 1.00 23.20 ? 206 VAL A CG2 1 
ATOM   306  N N   . TYR A 1 207 ? -3.789  -11.085 29.744 1.00 21.42 ? 207 TYR A N   1 
ATOM   307  C CA  . TYR A 1 207 ? -5.011  -10.412 30.118 1.00 22.20 ? 207 TYR A CA  1 
ATOM   308  C C   . TYR A 1 207 ? -6.116  -10.875 29.197 1.00 22.65 ? 207 TYR A C   1 
ATOM   309  O O   . TYR A 1 207 ? -5.899  -11.118 28.017 1.00 22.00 ? 207 TYR A O   1 
ATOM   310  C CB  . TYR A 1 207 ? -4.849  -8.888  30.004 1.00 22.66 ? 207 TYR A CB  1 
ATOM   311  C CG  . TYR A 1 207 ? -3.988  -8.319  31.098 1.00 24.53 ? 207 TYR A CG  1 
ATOM   312  C CD1 . TYR A 1 207 ? -2.605  -8.286  30.976 1.00 26.45 ? 207 TYR A CD1 1 
ATOM   313  C CD2 . TYR A 1 207 ? -4.544  -7.906  32.299 1.00 25.48 ? 207 TYR A CD2 1 
ATOM   314  C CE1 . TYR A 1 207 ? -1.799  -7.850  32.024 1.00 27.88 ? 207 TYR A CE1 1 
ATOM   315  C CE2 . TYR A 1 207 ? -3.752  -7.447  33.337 1.00 27.41 ? 207 TYR A CE2 1 
ATOM   316  C CZ  . TYR A 1 207 ? -2.378  -7.443  33.204 1.00 29.44 ? 207 TYR A CZ  1 
ATOM   317  O OH  . TYR A 1 207 ? -1.601  -6.962  34.224 1.00 33.56 ? 207 TYR A OH  1 
ATOM   318  N N   . LEU A 1 208 ? -7.299  -10.995 29.745 1.00 23.23 ? 208 LEU A N   1 
ATOM   319  C CA  . LEU A 1 208 ? -8.477  -11.343 28.992 1.00 24.39 ? 208 LEU A CA  1 
ATOM   320  C C   . LEU A 1 208 ? -9.379  -10.144 29.038 1.00 26.64 ? 208 LEU A C   1 
ATOM   321  O O   . LEU A 1 208 ? -9.561  -9.539  30.098 1.00 26.98 ? 208 LEU A O   1 
ATOM   322  C CB  . LEU A 1 208 ? -9.193  -12.535 29.617 1.00 23.96 ? 208 LEU A CB  1 
ATOM   323  C CG  . LEU A 1 208 ? -8.417  -13.836 29.692 1.00 24.77 ? 208 LEU A CG  1 
ATOM   324  C CD1 . LEU A 1 208 ? -9.331  -14.965 30.157 1.00 25.38 ? 208 LEU A CD1 1 
ATOM   325  C CD2 . LEU A 1 208 ? -7.733  -14.194 28.328 1.00 24.76 ? 208 LEU A CD2 1 
ATOM   326  N N   . TRP A 1 209 ? -9.930  -9.788  27.895 1.00 27.56 ? 209 TRP A N   1 
ATOM   327  C CA  . TRP A 1 209 ? -10.841 -8.675  27.810 1.00 29.89 ? 209 TRP A CA  1 
ATOM   328  C C   . TRP A 1 209 ? -12.097 -9.159  27.108 1.00 31.03 ? 209 TRP A C   1 
ATOM   329  O O   . TRP A 1 209 ? -12.018 -9.630  25.970 1.00 30.55 ? 209 TRP A O   1 
ATOM   330  C CB  . TRP A 1 209 ? -10.181 -7.513  27.056 1.00 30.60 ? 209 TRP A CB  1 
ATOM   331  C CG  . TRP A 1 209 ? -11.080 -6.345  26.829 1.00 32.51 ? 209 TRP A CG  1 
ATOM   332  C CD1 . TRP A 1 209 ? -11.412 -5.370  27.722 1.00 33.63 ? 209 TRP A CD1 1 
ATOM   333  C CD2 . TRP A 1 209 ? -11.754 -6.023  25.615 1.00 33.44 ? 209 TRP A CD2 1 
ATOM   334  N NE1 . TRP A 1 209 ? -12.263 -4.467  27.139 1.00 34.04 ? 209 TRP A NE1 1 
ATOM   335  C CE2 . TRP A 1 209 ? -12.484 -4.840  25.841 1.00 34.25 ? 209 TRP A CE2 1 
ATOM   336  C CE3 . TRP A 1 209 ? -11.785 -6.603  24.343 1.00 34.19 ? 209 TRP A CE3 1 
ATOM   337  C CZ2 . TRP A 1 209 ? -13.253 -4.241  24.851 1.00 35.15 ? 209 TRP A CZ2 1 
ATOM   338  C CZ3 . TRP A 1 209 ? -12.549 -6.006  23.367 1.00 35.16 ? 209 TRP A CZ3 1 
ATOM   339  C CH2 . TRP A 1 209 ? -13.276 -4.843  23.626 1.00 35.25 ? 209 TRP A CH2 1 
ATOM   340  N N   . SER A 1 210 ? -13.237 -9.121  27.801 1.00 32.08 ? 210 SER A N   1 
ATOM   341  C CA  . SER A 1 210 ? -14.492 -9.529  27.187 1.00 34.54 ? 210 SER A CA  1 
ATOM   342  C C   . SER A 1 210 ? -14.965 -8.382  26.337 1.00 36.41 ? 210 SER A C   1 
ATOM   343  O O   . SER A 1 210 ? -15.167 -7.283  26.853 1.00 36.75 ? 210 SER A O   1 
ATOM   344  C CB  . SER A 1 210 ? -15.538 -9.862  28.244 1.00 37.83 ? 210 SER A CB  1 
ATOM   345  O OG  . SER A 1 210 ? -16.858 -9.839  27.717 1.00 43.03 ? 210 SER A OG  1 
ATOM   346  N N   . ALA A 1 211 ? -15.136 -8.621  25.041 1.00 37.41 ? 211 ALA A N   1 
ATOM   347  C CA  . ALA A 1 211 ? -15.621 -7.578  24.139 1.00 38.80 ? 211 ALA A CA  1 
ATOM   348  C C   . ALA A 1 211 ? -17.069 -7.178  24.424 1.00 40.43 ? 211 ALA A C   1 
ATOM   349  O O   . ALA A 1 211 ? -17.465 -6.063  24.085 1.00 41.58 ? 211 ALA A O   1 
ATOM   350  C CB  . ALA A 1 211 ? -15.441 -7.995  22.686 1.00 38.51 ? 211 ALA A CB  1 
ATOM   351  N N   . SER A 1 212 ? -17.837 -8.038  25.104 1.00 40.36 ? 212 SER A N   1 
ATOM   352  C CA  . SER A 1 212 ? -19.217 -7.728  25.412 1.00 41.38 ? 212 SER A CA  1 
ATOM   353  C C   . SER A 1 212 ? -19.354 -6.824  26.652 1.00 42.13 ? 212 SER A C   1 
ATOM   354  O O   . SER A 1 212 ? -20.084 -5.829  26.624 1.00 42.62 ? 212 SER A O   1 
ATOM   355  C CB  . SER A 1 212 ? -20.016 -9.020  25.563 1.00 43.11 ? 212 SER A CB  1 
ATOM   356  O OG  . SER A 1 212 ? -20.182 -9.470  26.902 1.00 45.62 ? 212 SER A OG  1 
ATOM   357  N N   . SER A 1 213 ? -18.661 -7.171  27.736 1.00 41.65 ? 213 SER A N   1 
ATOM   358  C CA  . SER A 1 213 ? -18.794 -6.426  28.990 1.00 41.97 ? 213 SER A CA  1 
ATOM   359  C C   . SER A 1 213 ? -17.694 -5.429  29.275 1.00 41.89 ? 213 SER A C   1 
ATOM   360  O O   . SER A 1 213 ? -17.846 -4.600  30.174 1.00 41.95 ? 213 SER A O   1 
ATOM   361  C CB  . SER A 1 213 ? -18.851 -7.397  30.156 1.00 43.20 ? 213 SER A CB  1 
ATOM   362  O OG  . SER A 1 213 ? -17.635 -8.124  30.196 1.00 46.45 ? 213 SER A OG  1 
ATOM   363  N N   . GLY A 1 214 ? -16.568 -5.568  28.587 1.00 41.27 ? 214 GLY A N   1 
ATOM   364  C CA  . GLY A 1 214 ? -15.397 -4.752  28.857 1.00 41.01 ? 214 GLY A CA  1 
ATOM   365  C C   . GLY A 1 214 ? -14.649 -5.204  30.099 1.00 40.71 ? 214 GLY A C   1 
ATOM   366  O O   . GLY A 1 214 ? -13.695 -4.542  30.501 1.00 41.46 ? 214 GLY A O   1 
ATOM   367  N N   . ASP A 1 215 ? -15.060 -6.327  30.727 1.00 39.54 ? 215 ASP A N   1 
ATOM   368  C CA  . ASP A 1 215 ? -14.385 -6.824  31.915 1.00 39.07 ? 215 ASP A CA  1 
ATOM   369  C C   . ASP A 1 215 ? -12.984 -7.277  31.565 1.00 37.13 ? 215 ASP A C   1 
ATOM   370  O O   . ASP A 1 215 ? -12.764 -7.847  30.496 1.00 36.95 ? 215 ASP A O   1 
ATOM   371  C CB  . ASP A 1 215 ? -15.159 -7.981  32.545 1.00 42.34 ? 215 ASP A CB  1 
ATOM   372  C CG  . ASP A 1 215 ? -16.415 -7.535  33.258 1.00 50.75 ? 215 ASP A CG  1 
ATOM   373  O OD1 . ASP A 1 215 ? -16.363 -6.500  33.962 1.00 52.20 ? 215 ASP A OD1 1 
ATOM   374  O OD2 . ASP A 1 215 ? -17.455 -8.217  33.110 1.00 54.52 ? 215 ASP A OD2 1 
ATOM   375  N N   . ILE A 1 216 ? -12.030 -6.989  32.445 1.00 35.15 ? 216 ILE A N   1 
ATOM   376  C CA  . ILE A 1 216 ? -10.649 -7.401  32.233 1.00 34.01 ? 216 ILE A CA  1 
ATOM   377  C C   . ILE A 1 216 ? -10.245 -8.329  33.343 1.00 32.32 ? 216 ILE A C   1 
ATOM   378  O O   . ILE A 1 216 ? -10.594 -8.098  34.490 1.00 32.53 ? 216 ILE A O   1 
ATOM   379  C CB  . ILE A 1 216 ? -9.705  -6.192  32.182 1.00 34.36 ? 216 ILE A CB  1 
ATOM   380  C CG1 . ILE A 1 216 ? -10.103 -5.233  31.051 1.00 35.19 ? 216 ILE A CG1 1 
ATOM   381  C CG2 . ILE A 1 216 ? -8.242  -6.623  32.091 1.00 34.35 ? 216 ILE A CG2 1 
ATOM   382  C CD1 . ILE A 1 216 ? -9.656  -3.839  31.285 1.00 35.91 ? 216 ILE A CD1 1 
ATOM   383  N N   . LEU A 1 217 ? -9.546  -9.396  32.996 1.00 30.38 ? 217 LEU A N   1 
ATOM   384  C CA  . LEU A 1 217 ? -9.060  -10.367 33.949 1.00 29.20 ? 217 LEU A CA  1 
ATOM   385  C C   . LEU A 1 217 ? -7.580  -10.595 33.671 1.00 28.43 ? 217 LEU A C   1 
ATOM   386  O O   . LEU A 1 217 ? -7.212  -10.891 32.533 1.00 28.35 ? 217 LEU A O   1 
ATOM   387  C CB  . LEU A 1 217 ? -9.810  -11.708 33.753 1.00 29.07 ? 217 LEU A CB  1 
ATOM   388  C CG  . LEU A 1 217 ? -9.300  -12.866 34.619 1.00 30.91 ? 217 LEU A CG  1 
ATOM   389  C CD1 . LEU A 1 217 ? -9.779  -12.707 36.068 1.00 30.93 ? 217 LEU A CD1 1 
ATOM   390  C CD2 . LEU A 1 217 ? -9.694  -14.227 34.049 1.00 31.46 ? 217 LEU A CD2 1 
ATOM   391  N N   . GLN A 1 218 ? -6.731  -10.492 34.693 1.00 27.54 ? 218 GLN A N   1 
ATOM   392  C CA  . GLN A 1 218 ? -5.341  -10.879 34.537 1.00 27.38 ? 218 GLN A CA  1 
ATOM   393  C C   . GLN A 1 218 ? -5.386  -12.398 34.770 1.00 27.12 ? 218 GLN A C   1 
ATOM   394  O O   . GLN A 1 218 ? -5.514  -12.842 35.906 1.00 27.33 ? 218 GLN A O   1 
ATOM   395  C CB  . GLN A 1 218 ? -4.449  -10.209 35.572 1.00 28.99 ? 218 GLN A CB  1 
ATOM   396  C CG  . GLN A 1 218 ? -2.979  -10.439 35.247 1.00 31.87 ? 218 GLN A CG  1 
ATOM   397  C CD  . GLN A 1 218 ? -2.041  -9.930  36.305 1.00 34.60 ? 218 GLN A CD  1 
ATOM   398  O OE1 . GLN A 1 218 ? -2.433  -9.542  37.392 1.00 37.52 ? 218 GLN A OE1 1 
ATOM   399  N NE2 . GLN A 1 218 ? -0.767  -9.946  36.008 1.00 34.38 ? 218 GLN A NE2 1 
ATOM   400  N N   . LEU A 1 219 ? -5.398  -13.178 33.701 1.00 26.40 ? 219 LEU A N   1 
ATOM   401  C CA  . LEU A 1 219 ? -5.546  -14.624 33.790 1.00 26.21 ? 219 LEU A CA  1 
ATOM   402  C C   . LEU A 1 219 ? -4.373  -15.257 34.487 1.00 26.93 ? 219 LEU A C   1 
ATOM   403  O O   . LEU A 1 219 ? -4.559  -16.168 35.289 1.00 26.92 ? 219 LEU A O   1 
ATOM   404  C CB  . LEU A 1 219 ? -5.701  -15.225 32.380 1.00 25.43 ? 219 LEU A CB  1 
ATOM   405  C CG  . LEU A 1 219 ? -5.743  -16.743 32.281 1.00 25.99 ? 219 LEU A CG  1 
ATOM   406  C CD1 . LEU A 1 219 ? -6.983  -17.287 32.968 1.00 26.61 ? 219 LEU A CD1 1 
ATOM   407  C CD2 . LEU A 1 219 ? -5.669  -17.200 30.810 1.00 25.98 ? 219 LEU A CD2 1 
ATOM   408  N N   . LEU A 1 220 ? -3.166  -14.836 34.123 1.00 27.07 ? 220 LEU A N   1 
ATOM   409  C CA  . LEU A 1 220 ? -1.969  -15.443 34.656 1.00 28.16 ? 220 LEU A CA  1 
ATOM   410  C C   . LEU A 1 220 ? -0.800  -14.502 34.626 1.00 29.26 ? 220 LEU A C   1 
ATOM   411  O O   . LEU A 1 220 ? -0.798  -13.507 33.911 1.00 29.60 ? 220 LEU A O   1 
ATOM   412  C CB  . LEU A 1 220 ? -1.630  -16.687 33.812 1.00 28.56 ? 220 LEU A CB  1 
ATOM   413  C CG  . LEU A 1 220 ? -1.199  -16.422 32.339 1.00 30.63 ? 220 LEU A CG  1 
ATOM   414  C CD1 . LEU A 1 220 ? 0.316   -16.340 32.196 1.00 31.19 ? 220 LEU A CD1 1 
ATOM   415  C CD2 . LEU A 1 220 ? -1.698  -17.501 31.434 1.00 31.27 ? 220 LEU A CD2 1 
ATOM   416  N N   . GLN A 1 221 ? 0.220   -14.847 35.373 1.00 29.85 ? 221 GLN A N   1 
ATOM   417  C CA  . GLN A 1 221 ? 1.481   -14.151 35.347 1.00 30.68 ? 221 GLN A CA  1 
ATOM   418  C C   . GLN A 1 221 ? 2.529   -15.225 35.471 1.00 30.74 ? 221 GLN A C   1 
ATOM   419  O O   . GLN A 1 221 ? 2.387   -16.142 36.296 1.00 30.96 ? 221 GLN A O   1 
ATOM   420  C CB  . GLN A 1 221 ? 1.606   -13.126 36.474 1.00 32.88 ? 221 GLN A CB  1 
ATOM   421  C CG  . GLN A 1 221 ? 2.910   -12.342 36.399 1.00 39.37 ? 221 GLN A CG  1 
ATOM   422  C CD  . GLN A 1 221 ? 2.980   -11.234 37.411 1.00 46.72 ? 221 GLN A CD  1 
ATOM   423  O OE1 . GLN A 1 221 ? 2.478   -10.127 37.178 1.00 50.07 ? 221 GLN A OE1 1 
ATOM   424  N NE2 . GLN A 1 221 ? 3.595   -11.506 38.559 1.00 47.28 ? 221 GLN A NE2 1 
ATOM   425  N N   . MET A 1 222 ? 3.579   -15.151 34.633 1.00 30.03 ? 222 MET A N   1 
ATOM   426  C CA  . MET A 1 222 ? 4.715   -16.071 34.697 1.00 30.62 ? 222 MET A CA  1 
ATOM   427  C C   . MET A 1 222 ? 5.360   -15.988 36.066 1.00 31.22 ? 222 MET A C   1 
ATOM   428  O O   . MET A 1 222 ? 5.384   -14.909 36.660 1.00 30.79 ? 222 MET A O   1 
ATOM   429  C CB  . MET A 1 222 ? 5.756   -15.715 33.637 1.00 31.48 ? 222 MET A CB  1 
ATOM   430  C CG  . MET A 1 222 ? 5.210   -15.697 32.224 1.00 33.96 ? 222 MET A CG  1 
ATOM   431  S SD  . MET A 1 222 ? 5.275   -17.324 31.458 1.00 39.65 ? 222 MET A SD  1 
ATOM   432  C CE  . MET A 1 222 ? 3.772   -18.046 32.021 1.00 36.20 ? 222 MET A CE  1 
ATOM   433  N N   . GLU A 1 223 ? 5.817   -17.117 36.584 1.00 32.28 ? 223 GLU A N   1 
ATOM   434  C CA  . GLU A 1 223 ? 6.357   -17.149 37.931 1.00 34.48 ? 223 GLU A CA  1 
ATOM   435  C C   . GLU A 1 223 ? 7.865   -16.902 38.024 1.00 35.03 ? 223 GLU A C   1 
ATOM   436  O O   . GLU A 1 223 ? 8.301   -16.412 39.051 1.00 35.72 ? 223 GLU A O   1 
ATOM   437  C CB  . GLU A 1 223 ? 5.965   -18.456 38.633 1.00 38.34 ? 223 GLU A CB  1 
ATOM   438  C CG  . GLU A 1 223 ? 4.458   -18.652 38.704 1.00 45.76 ? 223 GLU A CG  1 
ATOM   439  C CD  . GLU A 1 223 ? 3.879   -18.628 40.106 1.00 56.40 ? 223 GLU A CD  1 
ATOM   440  O OE1 . GLU A 1 223 ? 4.566   -19.094 41.045 1.00 58.13 ? 223 GLU A OE1 1 
ATOM   441  O OE2 . GLU A 1 223 ? 2.728   -18.159 40.265 1.00 60.14 ? 223 GLU A OE2 1 
ATOM   442  N N   . GLN A 1 224 ? 8.650   -17.215 36.989 1.00 34.85 ? 224 GLN A N   1 
ATOM   443  C CA  . GLN A 1 224 ? 10.103  -17.051 37.069 1.00 35.39 ? 224 GLN A CA  1 
ATOM   444  C C   . GLN A 1 224 ? 10.623  -15.747 36.445 1.00 33.98 ? 224 GLN A C   1 
ATOM   445  O O   . GLN A 1 224 ? 10.111  -15.283 35.430 1.00 33.26 ? 224 GLN A O   1 
ATOM   446  C CB  . GLN A 1 224 ? 10.848  -18.248 36.427 1.00 39.11 ? 224 GLN A CB  1 
ATOM   447  C CG  . GLN A 1 224 ? 10.159  -19.613 36.500 1.00 44.84 ? 224 GLN A CG  1 
ATOM   448  C CD  . GLN A 1 224 ? 9.950   -20.122 37.892 1.00 50.11 ? 224 GLN A CD  1 
ATOM   449  O OE1 . GLN A 1 224 ? 8.812   -20.310 38.337 1.00 51.83 ? 224 GLN A OE1 1 
ATOM   450  N NE2 . GLN A 1 224 ? 11.035  -20.396 38.589 1.00 51.09 ? 224 GLN A NE2 1 
ATOM   451  N N   . PRO A 1 225 ? 11.706  -15.193 37.009 1.00 33.00 ? 225 PRO A N   1 
ATOM   452  C CA  . PRO A 1 225 ? 12.293  -13.980 36.428 1.00 32.61 ? 225 PRO A CA  1 
ATOM   453  C C   . PRO A 1 225 ? 12.765  -14.200 34.986 1.00 32.49 ? 225 PRO A C   1 
ATOM   454  O O   . PRO A 1 225 ? 13.198  -15.291 34.607 1.00 32.69 ? 225 PRO A O   1 
ATOM   455  C CB  . PRO A 1 225 ? 13.449  -13.666 37.384 1.00 33.65 ? 225 PRO A CB  1 
ATOM   456  C CG  . PRO A 1 225 ? 13.026  -14.300 38.695 1.00 33.84 ? 225 PRO A CG  1 
ATOM   457  C CD  . PRO A 1 225 ? 12.398  -15.591 38.246 1.00 32.09 ? 225 PRO A CD  1 
ATOM   458  N N   . GLY A 1 226 ? 12.593  -13.180 34.161 1.00 31.64 ? 226 GLY A N   1 
ATOM   459  C CA  . GLY A 1 226 ? 12.964  -13.245 32.754 1.00 31.68 ? 226 GLY A CA  1 
ATOM   460  C C   . GLY A 1 226 ? 11.955  -13.934 31.857 1.00 31.81 ? 226 GLY A C   1 
ATOM   461  O O   . GLY A 1 226 ? 12.052  -13.834 30.628 1.00 32.94 ? 226 GLY A O   1 
ATOM   462  N N   . GLU A 1 227 ? 10.981  -14.648 32.443 1.00 30.92 ? 227 GLU A N   1 
ATOM   463  C CA  . GLU A 1 227 ? 9.974   -15.341 31.646 1.00 30.46 ? 227 GLU A CA  1 
ATOM   464  C C   . GLU A 1 227 ? 8.973   -14.380 31.049 1.00 28.41 ? 227 GLU A C   1 
ATOM   465  O O   . GLU A 1 227 ? 8.512   -13.447 31.714 1.00 28.24 ? 227 GLU A O   1 
ATOM   466  C CB  . GLU A 1 227 ? 9.189   -16.343 32.484 1.00 33.66 ? 227 GLU A CB  1 
ATOM   467  C CG  . GLU A 1 227 ? 9.912   -17.629 32.782 1.00 40.59 ? 227 GLU A CG  1 
ATOM   468  C CD  . GLU A 1 227 ? 8.958   -18.625 33.408 1.00 49.86 ? 227 GLU A CD  1 
ATOM   469  O OE1 . GLU A 1 227 ? 8.138   -18.210 34.260 1.00 51.06 ? 227 GLU A OE1 1 
ATOM   470  O OE2 . GLU A 1 227 ? 9.041   -19.825 33.061 1.00 52.79 ? 227 GLU A OE2 1 
ATOM   471  N N   . TYR A 1 228 ? 8.593   -14.651 29.825 1.00 26.35 ? 228 TYR A N   1 
ATOM   472  C CA  . TYR A 1 228 ? 7.577   -13.874 29.156 1.00 25.64 ? 228 TYR A CA  1 
ATOM   473  C C   . TYR A 1 228 ? 6.708   -14.762 28.286 1.00 24.64 ? 228 TYR A C   1 
ATOM   474  O O   . TYR A 1 228 ? 7.096   -15.886 27.939 1.00 25.59 ? 228 TYR A O   1 
ATOM   475  C CB  . TYR A 1 228 ? 8.199   -12.731 28.357 1.00 25.63 ? 228 TYR A CB  1 
ATOM   476  C CG  . TYR A 1 228 ? 9.135   -13.179 27.260 1.00 25.97 ? 228 TYR A CG  1 
ATOM   477  C CD1 . TYR A 1 228 ? 8.656   -13.488 25.995 1.00 26.87 ? 228 TYR A CD1 1 
ATOM   478  C CD2 . TYR A 1 228 ? 10.508  -13.199 27.457 1.00 25.97 ? 228 TYR A CD2 1 
ATOM   479  C CE1 . TYR A 1 228 ? 9.517   -13.838 24.965 1.00 27.54 ? 228 TYR A CE1 1 
ATOM   480  C CE2 . TYR A 1 228 ? 11.378  -13.557 26.439 1.00 26.64 ? 228 TYR A CE2 1 
ATOM   481  C CZ  . TYR A 1 228 ? 10.876  -13.880 25.195 1.00 27.87 ? 228 TYR A CZ  1 
ATOM   482  O OH  . TYR A 1 228 ? 11.708  -14.225 24.170 1.00 29.69 ? 228 TYR A OH  1 
ATOM   483  N N   . ILE A 1 229 ? 5.523   -14.272 27.951 1.00 22.28 ? 229 ILE A N   1 
ATOM   484  C CA  . ILE A 1 229 ? 4.613   -15.008 27.109 1.00 20.88 ? 229 ILE A CA  1 
ATOM   485  C C   . ILE A 1 229 ? 5.028   -14.781 25.672 1.00 20.19 ? 229 ILE A C   1 
ATOM   486  O O   . ILE A 1 229 ? 5.224   -13.643 25.254 1.00 19.98 ? 229 ILE A O   1 
ATOM   487  C CB  . ILE A 1 229 ? 3.171   -14.545 27.322 1.00 20.94 ? 229 ILE A CB  1 
ATOM   488  C CG1 . ILE A 1 229 ? 2.767   -14.558 28.801 1.00 21.53 ? 229 ILE A CG1 1 
ATOM   489  C CG2 . ILE A 1 229 ? 2.237   -15.341 26.446 1.00 21.34 ? 229 ILE A CG2 1 
ATOM   490  C CD1 . ILE A 1 229 ? 2.765   -15.800 29.414 1.00 23.30 ? 229 ILE A CD1 1 
ATOM   491  N N   . SER A 1 230 ? 5.189   -15.853 24.922 1.00 19.89 ? 230 SER A N   1 
ATOM   492  C CA  . SER A 1 230 ? 5.600   -15.769 23.521 1.00 19.63 ? 230 SER A CA  1 
ATOM   493  C C   . SER A 1 230 ? 4.487   -16.099 22.538 1.00 19.03 ? 230 SER A C   1 
ATOM   494  O O   . SER A 1 230 ? 4.629   -15.793 21.341 1.00 19.53 ? 230 SER A O   1 
ATOM   495  C CB  . SER A 1 230 ? 6.843   -16.614 23.264 1.00 21.93 ? 230 SER A CB  1 
ATOM   496  O OG  . SER A 1 230 ? 6.771   -17.879 23.899 1.00 25.98 ? 230 SER A OG  1 
ATOM   497  N N   . SER A 1 231 ? 3.371   -16.664 23.005 1.00 17.68 ? 231 SER A N   1 
ATOM   498  C CA  . SER A 1 231 ? 2.226   -16.904 22.135 1.00 18.33 ? 231 SER A CA  1 
ATOM   499  C C   . SER A 1 231 ? 0.970   -17.206 22.910 1.00 18.34 ? 231 SER A C   1 
ATOM   500  O O   . SER A 1 231 ? 1.034   -17.711 24.023 1.00 18.69 ? 231 SER A O   1 
ATOM   501  C CB  . SER A 1 231 ? 2.495   -18.039 21.161 1.00 20.00 ? 231 SER A CB  1 
ATOM   502  O OG  . SER A 1 231 ? 2.966   -19.205 21.817 1.00 22.17 ? 231 SER A OG  1 
ATOM   503  N N   . VAL A 1 232 ? -0.171  -16.915 22.322 1.00 17.51 ? 232 VAL A N   1 
ATOM   504  C CA  . VAL A 1 232 ? -1.456  -17.272 22.888 1.00 17.48 ? 232 VAL A CA  1 
ATOM   505  C C   . VAL A 1 232 ? -2.323  -17.763 21.746 1.00 17.94 ? 232 VAL A C   1 
ATOM   506  O O   . VAL A 1 232 ? -2.222  -17.257 20.617 1.00 17.70 ? 232 VAL A O   1 
ATOM   507  C CB  . VAL A 1 232 ? -2.170  -16.141 23.667 1.00 17.94 ? 232 VAL A CB  1 
ATOM   508  C CG1 . VAL A 1 232 ? -1.347  -15.660 24.867 1.00 17.80 ? 232 VAL A CG1 1 
ATOM   509  C CG2 . VAL A 1 232 ? -2.539  -14.983 22.753 1.00 17.81 ? 232 VAL A CG2 1 
ATOM   510  N N   . ALA A 1 233 ? -3.170  -18.751 22.017 1.00 17.80 ? 233 ALA A N   1 
ATOM   511  C CA  . ALA A 1 233 ? -4.137  -19.215 21.039 1.00 18.72 ? 233 ALA A CA  1 
ATOM   512  C C   . ALA A 1 233 ? -5.292  -19.885 21.717 1.00 18.68 ? 233 ALA A C   1 
ATOM   513  O O   . ALA A 1 233 ? -5.093  -20.808 22.488 1.00 18.33 ? 233 ALA A O   1 
ATOM   514  C CB  . ALA A 1 233 ? -3.521  -20.154 20.026 1.00 18.81 ? 233 ALA A CB  1 
ATOM   515  N N   . TRP A 1 234 ? -6.499  -19.491 21.349 1.00 18.44 ? 234 TRP A N   1 
ATOM   516  C CA  . TRP A 1 234 ? -7.695  -20.078 21.894 1.00 19.70 ? 234 TRP A CA  1 
ATOM   517  C C   . TRP A 1 234 ? -8.050  -21.347 21.195 1.00 21.38 ? 234 TRP A C   1 
ATOM   518  O O   . TRP A 1 234 ? -8.011  -21.374 19.977 1.00 22.96 ? 234 TRP A O   1 
ATOM   519  C CB  . TRP A 1 234 ? -8.856  -19.138 21.653 1.00 19.48 ? 234 TRP A CB  1 
ATOM   520  C CG  . TRP A 1 234 ? -8.829  -17.911 22.495 1.00 20.28 ? 234 TRP A CG  1 
ATOM   521  C CD1 . TRP A 1 234 ? -8.520  -16.652 22.091 1.00 20.94 ? 234 TRP A CD1 1 
ATOM   522  C CD2 . TRP A 1 234 ? -9.210  -17.812 23.868 1.00 20.78 ? 234 TRP A CD2 1 
ATOM   523  N NE1 . TRP A 1 234 ? -8.724  -15.768 23.107 1.00 20.97 ? 234 TRP A NE1 1 
ATOM   524  C CE2 . TRP A 1 234 ? -9.127  -16.454 24.224 1.00 21.52 ? 234 TRP A CE2 1 
ATOM   525  C CE3 . TRP A 1 234 ? -9.678  -18.728 24.810 1.00 21.91 ? 234 TRP A CE3 1 
ATOM   526  C CZ2 . TRP A 1 234 ? -9.499  -15.989 25.483 1.00 22.40 ? 234 TRP A CZ2 1 
ATOM   527  C CZ3 . TRP A 1 234 ? -10.028 -18.274 26.068 1.00 23.33 ? 234 TRP A CZ3 1 
ATOM   528  C CH2 . TRP A 1 234 ? -9.914  -16.924 26.405 1.00 23.23 ? 234 TRP A CH2 1 
ATOM   529  N N   . ILE A 1 235 ? -8.531  -22.348 21.923 1.00 21.17 ? 235 ILE A N   1 
ATOM   530  C CA  . ILE A 1 235 ? -9.073  -23.561 21.300 1.00 22.67 ? 235 ILE A CA  1 
ATOM   531  C C   . ILE A 1 235 ? -10.384 -23.163 20.554 1.00 24.71 ? 235 ILE A C   1 
ATOM   532  O O   . ILE A 1 235 ? -10.987 -22.138 20.895 1.00 24.68 ? 235 ILE A O   1 
ATOM   533  C CB  . ILE A 1 235 ? -9.362  -24.607 22.412 1.00 22.62 ? 235 ILE A CB  1 
ATOM   534  C CG1 . ILE A 1 235 ? -9.443  -26.035 21.860 1.00 22.64 ? 235 ILE A CG1 1 
ATOM   535  C CG2 . ILE A 1 235 ? -10.598 -24.245 23.232 1.00 22.62 ? 235 ILE A CG2 1 
ATOM   536  C CD1 . ILE A 1 235 ? -9.522  -27.122 22.986 1.00 22.95 ? 235 ILE A CD1 1 
ATOM   537  N N   . LYS A 1 236 ? -10.829 -23.951 19.554 1.00 26.12 ? 236 LYS A N   1 
ATOM   538  C CA  . LYS A 1 236 ? -12.035 -23.602 18.790 1.00 27.86 ? 236 LYS A CA  1 
ATOM   539  C C   . LYS A 1 236 ? -13.262 -23.255 19.644 1.00 28.76 ? 236 LYS A C   1 
ATOM   540  O O   . LYS A 1 236 ? -13.910 -22.261 19.358 1.00 29.31 ? 236 LYS A O   1 
ATOM   541  C CB  . LYS A 1 236 ? -12.405 -24.667 17.742 1.00 30.15 ? 236 LYS A CB  1 
ATOM   542  N N   . GLU A 1 237 ? -13.541 -24.000 20.709 1.00 29.33 ? 237 GLU A N   1 
ATOM   543  C CA  . GLU A 1 237 ? -14.689 -23.707 21.580 1.00 30.37 ? 237 GLU A CA  1 
ATOM   544  C C   . GLU A 1 237 ? -14.517 -22.461 22.492 1.00 30.75 ? 237 GLU A C   1 
ATOM   545  O O   . GLU A 1 237 ? -15.483 -22.021 23.119 1.00 31.23 ? 237 GLU A O   1 
ATOM   546  C CB  . GLU A 1 237 ? -15.063 -24.940 22.417 1.00 32.96 ? 237 GLU A CB  1 
ATOM   547  N N   . GLY A 1 238 ? -13.304 -21.919 22.566 1.00 30.03 ? 238 GLY A N   1 
ATOM   548  C CA  . GLY A 1 238 ? -13.012 -20.726 23.344 1.00 30.04 ? 238 GLY A CA  1 
ATOM   549  C C   . GLY A 1 238 ? -12.968 -20.888 24.853 1.00 29.72 ? 238 GLY A C   1 
ATOM   550  O O   . GLY A 1 238 ? -12.925 -19.882 25.568 1.00 29.87 ? 238 GLY A O   1 
ATOM   551  N N   . ASN A 1 239 ? -12.960 -22.122 25.355 1.00 29.20 ? 239 ASN A N   1 
ATOM   552  C CA  . ASN A 1 239 ? -12.936 -22.342 26.804 1.00 29.67 ? 239 ASN A CA  1 
ATOM   553  C C   . ASN A 1 239 ? -11.549 -22.652 27.374 1.00 29.22 ? 239 ASN A C   1 
ATOM   554  O O   . ASN A 1 239 ? -11.356 -22.615 28.594 1.00 30.29 ? 239 ASN A O   1 
ATOM   555  C CB  . ASN A 1 239 ? -13.951 -23.384 27.236 1.00 32.32 ? 239 ASN A CB  1 
ATOM   556  C CG  . ASN A 1 239 ? -13.910 -24.681 26.471 1.00 37.84 ? 239 ASN A CG  1 
ATOM   557  O OD1 . ASN A 1 239 ? -13.374 -24.782 25.349 1.00 39.43 ? 239 ASN A OD1 1 
ATOM   558  N ND2 . ASN A 1 239 ? -14.516 -25.706 27.070 1.00 38.59 ? 239 ASN A ND2 1 
ATOM   559  N N   . TYR A 1 240 ? -10.586 -22.910 26.522 1.00 27.90 ? 240 TYR A N   1 
ATOM   560  C CA  . TYR A 1 240 ? -9.215  -23.160 26.908 1.00 27.20 ? 240 TYR A CA  1 
ATOM   561  C C   . TYR A 1 240 ? -8.311  -22.254 26.113 1.00 25.43 ? 240 TYR A C   1 
ATOM   562  O O   . TYR A 1 240 ? -8.565  -21.980 24.930 1.00 24.88 ? 240 TYR A O   1 
ATOM   563  C CB  . TYR A 1 240 ? -8.822  -24.618 26.650 1.00 28.20 ? 240 TYR A CB  1 
ATOM   564  C CG  . TYR A 1 240 ? -9.715  -25.602 27.371 1.00 30.66 ? 240 TYR A CG  1 
ATOM   565  C CD1 . TYR A 1 240 ? -9.612  -25.791 28.737 1.00 31.87 ? 240 TYR A CD1 1 
ATOM   566  C CD2 . TYR A 1 240 ? -10.693 -26.307 26.690 1.00 32.97 ? 240 TYR A CD2 1 
ATOM   567  C CE1 . TYR A 1 240 ? -10.445 -26.674 29.407 1.00 33.27 ? 240 TYR A CE1 1 
ATOM   568  C CE2 . TYR A 1 240 ? -11.522 -27.208 27.346 1.00 34.25 ? 240 TYR A CE2 1 
ATOM   569  C CZ  . TYR A 1 240 ? -11.386 -27.397 28.705 1.00 35.04 ? 240 TYR A CZ  1 
ATOM   570  O OH  . TYR A 1 240 ? -12.217 -28.285 29.351 1.00 37.25 ? 240 TYR A OH  1 
ATOM   571  N N   . LEU A 1 241 ? -7.243  -21.794 26.757 1.00 23.40 ? 241 LEU A N   1 
ATOM   572  C CA  . LEU A 1 241 ? -6.289  -20.921 26.106 1.00 22.43 ? 241 LEU A CA  1 
ATOM   573  C C   . LEU A 1 241 ? -4.942  -21.562 26.185 1.00 21.69 ? 241 LEU A C   1 
ATOM   574  O O   . LEU A 1 241 ? -4.526  -21.989 27.262 1.00 21.47 ? 241 LEU A O   1 
ATOM   575  C CB  . LEU A 1 241 ? -6.242  -19.557 26.822 1.00 22.26 ? 241 LEU A CB  1 
ATOM   576  C CG  . LEU A 1 241 ? -5.301  -18.522 26.204 1.00 22.29 ? 241 LEU A CG  1 
ATOM   577  C CD1 . LEU A 1 241 ? -5.818  -18.071 24.846 1.00 22.75 ? 241 LEU A CD1 1 
ATOM   578  C CD2 . LEU A 1 241 ? -5.096  -17.349 27.136 1.00 21.62 ? 241 LEU A CD2 1 
ATOM   579  N N   . ALA A 1 242 ? -4.267  -21.668 25.059 1.00 20.52 ? 242 ALA A N   1 
ATOM   580  C CA  . ALA A 1 242 ? -2.899  -22.177 25.041 1.00 20.18 ? 242 ALA A CA  1 
ATOM   581  C C   . ALA A 1 242 ? -1.997  -20.978 25.151 1.00 19.80 ? 242 ALA A C   1 
ATOM   582  O O   . ALA A 1 242 ? -2.250  -19.941 24.538 1.00 19.63 ? 242 ALA A O   1 
ATOM   583  C CB  . ALA A 1 242 ? -2.610  -22.926 23.751 1.00 19.55 ? 242 ALA A CB  1 
ATOM   584  N N   . VAL A 1 243 ? -0.958  -21.106 25.930 1.00 19.78 ? 243 VAL A N   1 
ATOM   585  C CA  . VAL A 1 243 ? -0.014  -20.032 26.173 1.00 20.84 ? 243 VAL A CA  1 
ATOM   586  C C   . VAL A 1 243 ? 1.387   -20.580 26.026 1.00 21.94 ? 243 VAL A C   1 
ATOM   587  O O   . VAL A 1 243 ? 1.796   -21.435 26.796 1.00 23.18 ? 243 VAL A O   1 
ATOM   588  C CB  . VAL A 1 243 ? -0.206  -19.494 27.605 1.00 21.98 ? 243 VAL A CB  1 
ATOM   589  C CG1 . VAL A 1 243 ? 0.809   -18.413 27.913 1.00 22.11 ? 243 VAL A CG1 1 
ATOM   590  C CG2 . VAL A 1 243 ? -1.636  -18.999 27.822 1.00 22.72 ? 243 VAL A CG2 1 
ATOM   591  N N   . GLY A 1 244 ? 2.112   -20.088 25.054 1.00 21.68 ? 244 GLY A N   1 
ATOM   592  C CA  . GLY A 1 244 ? 3.490   -20.489 24.842 1.00 22.34 ? 244 GLY A CA  1 
ATOM   593  C C   . GLY A 1 244 ? 4.374   -19.544 25.610 1.00 22.76 ? 244 GLY A C   1 
ATOM   594  O O   . GLY A 1 244 ? 4.068   -18.354 25.706 1.00 23.21 ? 244 GLY A O   1 
ATOM   595  N N   . THR A 1 245 ? 5.464   -20.054 26.174 1.00 22.63 ? 245 THR A N   1 
ATOM   596  C CA  . THR A 1 245 ? 6.341   -19.205 26.982 1.00 23.37 ? 245 THR A CA  1 
ATOM   597  C C   . THR A 1 245 ? 7.764   -19.210 26.468 1.00 25.13 ? 245 THR A C   1 
ATOM   598  O O   . THR A 1 245 ? 8.165   -20.108 25.730 1.00 25.22 ? 245 THR A O   1 
ATOM   599  C CB  . THR A 1 245 ? 6.298   -19.632 28.475 1.00 23.51 ? 245 THR A CB  1 
ATOM   600  O OG1 . THR A 1 245 ? 7.166   -20.756 28.651 1.00 24.11 ? 245 THR A OG1 1 
ATOM   601  C CG2 . THR A 1 245 ? 4.888   -19.935 28.974 1.00 22.84 ? 245 THR A CG2 1 
ATOM   602  N N   . SER A 1 246 ? 8.531   -18.218 26.901 1.00 26.33 ? 246 SER A N   1 
ATOM   603  C CA  . SER A 1 246 ? 9.953   -18.083 26.640 1.00 27.45 ? 246 SER A CA  1 
ATOM   604  C C   . SER A 1 246 ? 10.721  -19.235 27.282 1.00 28.24 ? 246 SER A C   1 
ATOM   605  O O   . SER A 1 246 ? 11.830  -19.492 26.855 1.00 29.10 ? 246 SER A O   1 
ATOM   606  C CB  . SER A 1 246 ? 10.449  -16.780 27.238 1.00 28.48 ? 246 SER A CB  1 
ATOM   607  O OG  . SER A 1 246 ? 10.154  -16.770 28.622 1.00 30.40 ? 246 SER A OG  1 
ATOM   608  N N   . SER A 1 247 ? 10.174  -19.901 28.318 1.00 27.91 ? 247 SER A N   1 
ATOM   609  C CA  . SER A 1 247 ? 10.830  -21.061 28.913 1.00 28.23 ? 247 SER A CA  1 
ATOM   610  C C   . SER A 1 247 ? 10.430  -22.370 28.206 1.00 28.42 ? 247 SER A C   1 
ATOM   611  O O   . SER A 1 247 ? 10.544  -23.455 28.783 1.00 29.30 ? 247 SER A O   1 
ATOM   612  C CB  . SER A 1 247 ? 10.551  -21.150 30.409 1.00 29.72 ? 247 SER A CB  1 
ATOM   613  O OG  . SER A 1 247 ? 9.172   -20.963 30.666 1.00 33.21 ? 247 SER A OG  1 
ATOM   614  N N   . ALA A 1 248 ? 9.994   -22.274 26.933 1.00 27.61 ? 248 ALA A N   1 
ATOM   615  C CA  . ALA A 1 248 ? 9.653   -23.413 26.091 1.00 26.78 ? 248 ALA A CA  1 
ATOM   616  C C   . ALA A 1 248 ? 8.463   -24.226 26.576 1.00 25.49 ? 248 ALA A C   1 
ATOM   617  O O   . ALA A 1 248 ? 8.375   -25.417 26.267 1.00 26.34 ? 248 ALA A O   1 
ATOM   618  C CB  . ALA A 1 248 ? 10.872  -24.318 25.902 1.00 26.71 ? 248 ALA A CB  1 
ATOM   619  N N   . GLU A 1 249 ? 7.564   -23.613 27.315 1.00 23.60 ? 249 GLU A N   1 
ATOM   620  C CA  . GLU A 1 249 ? 6.372   -24.309 27.790 1.00 23.51 ? 249 GLU A CA  1 
ATOM   621  C C   . GLU A 1 249 ? 5.174   -23.989 26.935 1.00 23.13 ? 249 GLU A C   1 
ATOM   622  O O   . GLU A 1 249 ? 5.061   -22.894 26.395 1.00 22.97 ? 249 GLU A O   1 
ATOM   623  C CB  . GLU A 1 249 ? 6.040   -23.876 29.212 1.00 25.84 ? 249 GLU A CB  1 
ATOM   624  C CG  . GLU A 1 249 ? 7.161   -24.138 30.189 1.00 31.24 ? 249 GLU A CG  1 
ATOM   625  C CD  . GLU A 1 249 ? 7.016   -23.291 31.433 1.00 39.62 ? 249 GLU A CD  1 
ATOM   626  O OE1 . GLU A 1 249 ? 7.315   -23.809 32.535 1.00 43.88 ? 249 GLU A OE1 1 
ATOM   627  O OE2 . GLU A 1 249 ? 6.595   -22.116 31.308 1.00 40.01 ? 249 GLU A OE2 1 
ATOM   628  N N   . VAL A 1 250 ? 4.269   -24.930 26.832 1.00 23.07 ? 250 VAL A N   1 
ATOM   629  C CA  . VAL A 1 250 ? 3.003   -24.729 26.174 1.00 23.58 ? 250 VAL A CA  1 
ATOM   630  C C   . VAL A 1 250 ? 2.000   -25.010 27.268 1.00 24.13 ? 250 VAL A C   1 
ATOM   631  O O   . VAL A 1 250 ? 1.796   -26.166 27.642 1.00 24.50 ? 250 VAL A O   1 
ATOM   632  C CB  . VAL A 1 250 ? 2.795   -25.669 24.985 1.00 24.65 ? 250 VAL A CB  1 
ATOM   633  C CG1 . VAL A 1 250 ? 1.430   -25.423 24.364 1.00 25.13 ? 250 VAL A CG1 1 
ATOM   634  C CG2 . VAL A 1 250 ? 3.907   -25.519 23.944 1.00 24.95 ? 250 VAL A CG2 1 
ATOM   635  N N   . GLN A 1 251 ? 1.481   -23.967 27.881 1.00 24.17 ? 251 GLN A N   1 
ATOM   636  C CA  . GLN A 1 251 ? 0.534   -24.119 28.974 1.00 24.83 ? 251 GLN A CA  1 
ATOM   637  C C   . GLN A 1 251 ? -0.869  -24.145 28.440 1.00 25.80 ? 251 GLN A C   1 
ATOM   638  O O   . GLN A 1 251 ? -1.155  -23.556 27.399 1.00 26.98 ? 251 GLN A O   1 
ATOM   639  C CB  . GLN A 1 251 ? 0.688   -22.989 29.984 1.00 26.53 ? 251 GLN A CB  1 
ATOM   640  C CG  . GLN A 1 251 ? 2.135   -22.753 30.380 1.00 29.07 ? 251 GLN A CG  1 
ATOM   641  C CD  . GLN A 1 251 ? 2.290   -21.812 31.543 1.00 30.85 ? 251 GLN A CD  1 
ATOM   642  O OE1 . GLN A 1 251 ? 1.344   -21.141 31.982 1.00 29.35 ? 251 GLN A OE1 1 
ATOM   643  N NE2 . GLN A 1 251 ? 3.511   -21.752 32.068 1.00 31.70 ? 251 GLN A NE2 1 
ATOM   644  N N   . LEU A 1 252 ? -1.733  -24.864 29.113 1.00 25.30 ? 252 LEU A N   1 
ATOM   645  C CA  . LEU A 1 252 ? -3.127  -24.933 28.733 1.00 25.03 ? 252 LEU A CA  1 
ATOM   646  C C   . LEU A 1 252 ? -3.905  -24.423 29.914 1.00 23.10 ? 252 LEU A C   1 
ATOM   647  O O   . LEU A 1 252 ? -3.793  -24.986 30.993 1.00 23.15 ? 252 LEU A O   1 
ATOM   648  C CB  . LEU A 1 252 ? -3.534  -26.365 28.391 1.00 25.91 ? 252 LEU A CB  1 
ATOM   649  C CG  . LEU A 1 252 ? -4.979  -26.496 27.932 1.00 28.44 ? 252 LEU A CG  1 
ATOM   650  C CD1 . LEU A 1 252 ? -5.184  -25.777 26.626 1.00 29.43 ? 252 LEU A CD1 1 
ATOM   651  C CD2 . LEU A 1 252 ? -5.390  -27.937 27.808 1.00 29.21 ? 252 LEU A CD2 1 
ATOM   652  N N   . TRP A 1 253 ? -4.654  -23.340 29.728 1.00 21.75 ? 253 TRP A N   1 
ATOM   653  C CA  . TRP A 1 253 ? -5.434  -22.721 30.789 1.00 22.18 ? 253 TRP A CA  1 
ATOM   654  C C   . TRP A 1 253 ? -6.922  -22.879 30.557 1.00 23.69 ? 253 TRP A C   1 
ATOM   655  O O   . TRP A 1 253 ? -7.418  -22.599 29.470 1.00 23.73 ? 253 TRP A O   1 
ATOM   656  C CB  . TRP A 1 253 ? -5.092  -21.213 30.878 1.00 21.08 ? 253 TRP A CB  1 
ATOM   657  C CG  . TRP A 1 253 ? -3.759  -20.955 31.504 1.00 20.17 ? 253 TRP A CG  1 
ATOM   658  C CD1 . TRP A 1 253 ? -2.533  -21.134 30.932 1.00 21.05 ? 253 TRP A CD1 1 
ATOM   659  C CD2 . TRP A 1 253 ? -3.519  -20.592 32.864 1.00 19.34 ? 253 TRP A CD2 1 
ATOM   660  N NE1 . TRP A 1 253 ? -1.542  -20.902 31.856 1.00 21.00 ? 253 TRP A NE1 1 
ATOM   661  C CE2 . TRP A 1 253 ? -2.120  -20.542 33.046 1.00 20.16 ? 253 TRP A CE2 1 
ATOM   662  C CE3 . TRP A 1 253 ? -4.348  -20.231 33.928 1.00 18.79 ? 253 TRP A CE3 1 
ATOM   663  C CZ2 . TRP A 1 253 ? -1.538  -20.179 34.261 1.00 20.05 ? 253 TRP A CZ2 1 
ATOM   664  C CZ3 . TRP A 1 253 ? -3.769  -19.904 35.144 1.00 19.89 ? 253 TRP A CZ3 1 
ATOM   665  C CH2 . TRP A 1 253 ? -2.384  -19.878 35.302 1.00 19.97 ? 253 TRP A CH2 1 
ATOM   666  N N   . ASP A 1 254 ? -7.641  -23.271 31.590 1.00 24.37 ? 254 ASP A N   1 
ATOM   667  C CA  . ASP A 1 254 ? -9.084  -23.339 31.543 1.00 25.18 ? 254 ASP A CA  1 
ATOM   668  C C   . ASP A 1 254 ? -9.437  -21.926 31.991 1.00 25.79 ? 254 ASP A C   1 
ATOM   669  O O   . ASP A 1 254 ? -9.155  -21.564 33.133 1.00 26.54 ? 254 ASP A O   1 
ATOM   670  C CB  . ASP A 1 254 ? -9.557  -24.387 32.549 1.00 28.25 ? 254 ASP A CB  1 
ATOM   671  C CG  . ASP A 1 254 ? -11.055 -24.577 32.636 1.00 33.97 ? 254 ASP A CG  1 
ATOM   672  O OD1 . ASP A 1 254 ? -11.793 -23.574 32.484 1.00 34.98 ? 254 ASP A OD1 1 
ATOM   673  O OD2 . ASP A 1 254 ? -11.493 -25.724 32.902 1.00 35.48 ? 254 ASP A OD2 1 
ATOM   674  N N   . VAL A 1 255 ? -9.970  -21.099 31.086 1.00 24.84 ? 255 VAL A N   1 
ATOM   675  C CA  . VAL A 1 255 ? -10.275 -19.714 31.417 1.00 24.47 ? 255 VAL A CA  1 
ATOM   676  C C   . VAL A 1 255 ? -11.533 -19.554 32.270 1.00 26.09 ? 255 VAL A C   1 
ATOM   677  O O   . VAL A 1 255 ? -11.608 -18.554 32.993 1.00 26.07 ? 255 VAL A O   1 
ATOM   678  C CB  . VAL A 1 255 ? -10.319 -18.812 30.198 1.00 23.66 ? 255 VAL A CB  1 
ATOM   679  C CG1 . VAL A 1 255 ? -9.023  -18.944 29.415 1.00 24.17 ? 255 VAL A CG1 1 
ATOM   680  C CG2 . VAL A 1 255 ? -11.518 -19.161 29.331 1.00 23.20 ? 255 VAL A CG2 1 
ATOM   681  N N   . GLN A 1 256 ? -12.495 -20.502 32.219 1.00 26.79 ? 256 GLN A N   1 
ATOM   682  C CA  . GLN A 1 256 ? -13.655 -20.386 33.110 1.00 28.82 ? 256 GLN A CA  1 
ATOM   683  C C   . GLN A 1 256 ? -13.238 -20.715 34.545 1.00 29.55 ? 256 GLN A C   1 
ATOM   684  O O   . GLN A 1 256 ? -13.712 -20.085 35.487 1.00 29.96 ? 256 GLN A O   1 
ATOM   685  C CB  . GLN A 1 256 ? -14.855 -21.225 32.651 1.00 32.02 ? 256 GLN A CB  1 
ATOM   686  C CG  . GLN A 1 256 ? -16.044 -20.368 32.165 1.00 37.73 ? 256 GLN A CG  1 
ATOM   687  C CD  . GLN A 1 256 ? -17.033 -19.952 33.259 1.00 43.98 ? 256 GLN A CD  1 
ATOM   688  O OE1 . GLN A 1 256 ? -18.261 -20.127 33.130 1.00 45.73 ? 256 GLN A OE1 1 
ATOM   689  N NE2 . GLN A 1 256 ? -16.544 -19.388 34.364 1.00 44.77 ? 256 GLN A NE2 1 
ATOM   690  N N   . GLN A 1 257 ? -12.353 -21.700 34.721 1.00 29.58 ? 257 GLN A N   1 
ATOM   691  C CA  . GLN A 1 257 ? -11.850 -22.035 36.055 1.00 29.91 ? 257 GLN A CA  1 
ATOM   692  C C   . GLN A 1 257 ? -10.696 -21.117 36.467 1.00 29.00 ? 257 GLN A C   1 
ATOM   693  O O   . GLN A 1 257 ? -10.342 -21.108 37.633 1.00 29.31 ? 257 GLN A O   1 
ATOM   694  C CB  . GLN A 1 257 ? -11.353 -23.483 36.103 1.00 31.50 ? 257 GLN A CB  1 
ATOM   695  C CG  . GLN A 1 257 ? -12.444 -24.520 35.968 1.00 34.64 ? 257 GLN A CG  1 
ATOM   696  C CD  . GLN A 1 257 ? -11.889 -25.870 36.335 1.00 37.81 ? 257 GLN A CD  1 
ATOM   697  O OE1 . GLN A 1 257 ? -11.937 -26.283 37.487 1.00 39.80 ? 257 GLN A OE1 1 
ATOM   698  N NE2 . GLN A 1 257 ? -11.310 -26.569 35.378 1.00 37.85 ? 257 GLN A NE2 1 
ATOM   699  N N   . GLN A 1 258 ? -10.069 -20.406 35.513 1.00 28.04 ? 258 GLN A N   1 
ATOM   700  C CA  . GLN A 1 258 ? -8.889  -19.567 35.703 1.00 28.55 ? 258 GLN A CA  1 
ATOM   701  C C   . GLN A 1 258 ? -7.780  -20.383 36.352 1.00 28.32 ? 258 GLN A C   1 
ATOM   702  O O   . GLN A 1 258 ? -7.293  -20.042 37.426 1.00 28.52 ? 258 GLN A O   1 
ATOM   703  C CB  . GLN A 1 258 ? -9.219  -18.308 36.502 1.00 31.37 ? 258 GLN A CB  1 
ATOM   704  C CG  . GLN A 1 258 ? -10.341 -17.510 35.852 1.00 35.79 ? 258 GLN A CG  1 
ATOM   705  C CD  . GLN A 1 258 ? -10.727 -16.302 36.652 1.00 40.00 ? 258 GLN A CD  1 
ATOM   706  O OE1 . GLN A 1 258 ? -9.932  -15.759 37.431 1.00 40.37 ? 258 GLN A OE1 1 
ATOM   707  N NE2 . GLN A 1 258 ? -11.954 -15.843 36.450 1.00 41.38 ? 258 GLN A NE2 1 
ATOM   708  N N   . LYS A 1 259 ? -7.521  -21.554 35.780 1.00 27.77 ? 259 LYS A N   1 
ATOM   709  C CA  . LYS A 1 259 ? -6.518  -22.460 36.295 1.00 27.53 ? 259 LYS A CA  1 
ATOM   710  C C   . LYS A 1 259 ? -5.729  -23.097 35.183 1.00 27.17 ? 259 LYS A C   1 
ATOM   711  O O   . LYS A 1 259 ? -6.250  -23.345 34.102 1.00 26.43 ? 259 LYS A O   1 
ATOM   712  C CB  . LYS A 1 259 ? -7.114  -23.509 37.245 1.00 29.69 ? 259 LYS A CB  1 
ATOM   713  C CG  . LYS A 1 259 ? -7.597  -24.815 36.615 1.00 34.19 ? 259 LYS A CG  1 
ATOM   714  C CD  . LYS A 1 259 ? -8.144  -25.801 37.665 1.00 38.00 ? 259 LYS A CD  1 
ATOM   715  C CE  . LYS A 1 259 ? -7.251  -25.957 38.877 1.00 41.72 ? 259 LYS A CE  1 
ATOM   716  N NZ  . LYS A 1 259 ? -8.043  -26.019 40.149 1.00 43.75 ? 259 LYS A NZ  1 
ATOM   717  N N   . ARG A 1 260 ? -4.466  -23.351 35.453 1.00 27.64 ? 260 ARG A N   1 
ATOM   718  C CA  . ARG A 1 260 ? -3.590  -23.986 34.506 1.00 28.90 ? 260 ARG A CA  1 
ATOM   719  C C   . ARG A 1 260 ? -3.857  -25.469 34.604 1.00 30.15 ? 260 ARG A C   1 
ATOM   720  O O   . ARG A 1 260 ? -3.670  -26.057 35.665 1.00 30.26 ? 260 ARG A O   1 
ATOM   721  C CB  . ARG A 1 260 ? -2.134  -23.697 34.858 1.00 30.33 ? 260 ARG A CB  1 
ATOM   722  C CG  . ARG A 1 260 ? -1.193  -24.141 33.761 1.00 33.79 ? 260 ARG A CG  1 
ATOM   723  C CD  . ARG A 1 260 ? 0.243   -23.803 34.071 1.00 37.85 ? 260 ARG A CD  1 
ATOM   724  N NE  . ARG A 1 260 ? 0.780   -24.685 35.104 1.00 43.42 ? 260 ARG A NE  1 
ATOM   725  C CZ  . ARG A 1 260 ? 1.911   -24.468 35.763 1.00 48.20 ? 260 ARG A CZ  1 
ATOM   726  N NH1 . ARG A 1 260 ? 2.633   -23.383 35.517 1.00 48.93 ? 260 ARG A NH1 1 
ATOM   727  N NH2 . ARG A 1 260 ? 2.325   -25.329 36.684 1.00 49.84 ? 260 ARG A NH2 1 
ATOM   728  N N   . LEU A 1 261 ? -4.332  -26.066 33.522 1.00 30.44 ? 261 LEU A N   1 
ATOM   729  C CA  . LEU A 1 261 ? -4.567  -27.501 33.493 1.00 31.18 ? 261 LEU A CA  1 
ATOM   730  C C   . LEU A 1 261 ? -3.263  -28.233 33.183 1.00 31.90 ? 261 LEU A C   1 
ATOM   731  O O   . LEU A 1 261 ? -3.008  -29.288 33.751 1.00 32.75 ? 261 LEU A O   1 
ATOM   732  C CB  . LEU A 1 261 ? -5.606  -27.833 32.426 1.00 31.11 ? 261 LEU A CB  1 
ATOM   733  C CG  . LEU A 1 261 ? -6.959  -27.159 32.592 1.00 32.25 ? 261 LEU A CG  1 
ATOM   734  C CD1 . LEU A 1 261 ? -7.880  -27.612 31.523 1.00 32.56 ? 261 LEU A CD1 1 
ATOM   735  C CD2 . LEU A 1 261 ? -7.581  -27.474 33.941 1.00 32.70 ? 261 LEU A CD2 1 
ATOM   736  N N   . ARG A 1 262 ? -2.448  -27.694 32.265 1.00 31.35 ? 262 ARG A N   1 
ATOM   737  C CA  . ARG A 1 262 ? -1.217  -28.356 31.863 1.00 31.59 ? 262 ARG A CA  1 
ATOM   738  C C   . ARG A 1 262 ? -0.067  -27.411 31.660 1.00 31.16 ? 262 ARG A C   1 
ATOM   739  O O   . ARG A 1 262 ? -0.274  -26.261 31.303 1.00 31.42 ? 262 ARG A O   1 
ATOM   740  C CB  . ARG A 1 262 ? -1.444  -29.097 30.545 1.00 33.40 ? 262 ARG A CB  1 
ATOM   741  C CG  . ARG A 1 262 ? -2.583  -30.090 30.608 1.00 36.46 ? 262 ARG A CG  1 
ATOM   742  C CD  . ARG A 1 262 ? -2.526  -31.047 29.469 1.00 38.27 ? 262 ARG A CD  1 
ATOM   743  N NE  . ARG A 1 262 ? -1.373  -31.923 29.622 1.00 39.13 ? 262 ARG A NE  1 
ATOM   744  C CZ  . ARG A 1 262 ? -1.139  -32.984 28.871 1.00 39.21 ? 262 ARG A CZ  1 
ATOM   745  N NH1 . ARG A 1 262 ? -1.983  -33.317 27.902 1.00 38.39 ? 262 ARG A NH1 1 
ATOM   746  N NH2 . ARG A 1 262 ? -0.066  -33.732 29.087 1.00 38.20 ? 262 ARG A NH2 1 
ATOM   747  N N   . ASN A 1 263 ? 1.149   -27.906 31.854 1.00 30.71 ? 263 ASN A N   1 
ATOM   748  C CA  . ASN A 1 263 ? 2.358   -27.160 31.582 1.00 31.48 ? 263 ASN A CA  1 
ATOM   749  C C   . ASN A 1 263 ? 3.178   -28.093 30.747 1.00 32.09 ? 263 ASN A C   1 
ATOM   750  O O   . ASN A 1 263 ? 3.968   -28.862 31.279 1.00 32.75 ? 263 ASN A O   1 
ATOM   751  C CB  . ASN A 1 263 ? 3.104   -26.780 32.849 1.00 32.67 ? 263 ASN A CB  1 
ATOM   752  C CG  . ASN A 1 263 ? 4.168   -25.740 32.577 1.00 36.94 ? 263 ASN A CG  1 
ATOM   753  O OD1 . ASN A 1 263 ? 4.096   -24.976 31.603 1.00 37.28 ? 263 ASN A OD1 1 
ATOM   754  N ND2 . ASN A 1 263 ? 5.186   -25.684 33.428 1.00 38.20 ? 263 ASN A ND2 1 
ATOM   755  N N   . MET A 1 264 ? 2.943   -28.078 29.434 1.00 31.59 ? 264 MET A N   1 
ATOM   756  C CA  . MET A 1 264 ? 3.553   -29.021 28.520 1.00 31.60 ? 264 MET A CA  1 
ATOM   757  C C   . MET A 1 264 ? 4.927   -28.639 28.060 1.00 32.22 ? 264 MET A C   1 
ATOM   758  O O   . MET A 1 264 ? 5.128   -27.576 27.479 1.00 32.56 ? 264 MET A O   1 
ATOM   759  C CB  . MET A 1 264 ? 2.629   -29.278 27.329 1.00 31.11 ? 264 MET A CB  1 
ATOM   760  C CG  . MET A 1 264 ? 1.260   -29.732 27.766 1.00 31.84 ? 264 MET A CG  1 
ATOM   761  S SD  . MET A 1 264 ? 0.109   -30.017 26.420 1.00 32.63 ? 264 MET A SD  1 
ATOM   762  C CE  . MET A 1 264 ? -0.138  -28.393 25.867 1.00 31.56 ? 264 MET A CE  1 
ATOM   763  N N   . THR A 1 265 ? 5.883   -29.529 28.308 1.00 32.06 ? 265 THR A N   1 
ATOM   764  C CA  . THR A 1 265 ? 7.246   -29.320 27.868 1.00 32.46 ? 265 THR A CA  1 
ATOM   765  C C   . THR A 1 265 ? 7.609   -30.350 26.841 1.00 32.93 ? 265 THR A C   1 
ATOM   766  O O   . THR A 1 265 ? 7.221   -31.524 26.927 1.00 34.76 ? 265 THR A O   1 
ATOM   767  C CB  . THR A 1 265 ? 8.222   -29.334 29.023 1.00 33.41 ? 265 THR A CB  1 
ATOM   768  O OG1 . THR A 1 265 ? 8.099   -30.576 29.734 1.00 34.37 ? 265 THR A OG1 1 
ATOM   769  C CG2 . THR A 1 265 ? 8.032   -28.140 29.935 1.00 33.66 ? 265 THR A CG2 1 
ATOM   770  N N   . SER A 1 266 ? 8.375   -29.911 25.882 1.00 31.21 ? 266 SER A N   1 
ATOM   771  C CA  . SER A 1 266 ? 8.861   -30.717 24.784 1.00 30.53 ? 266 SER A CA  1 
ATOM   772  C C   . SER A 1 266 ? 9.842   -29.909 23.951 1.00 29.64 ? 266 SER A C   1 
ATOM   773  O O   . SER A 1 266 ? 10.832  -30.458 23.488 1.00 30.15 ? 266 SER A O   1 
ATOM   774  C CB  . SER A 1 266 ? 7.705   -31.214 23.920 1.00 31.32 ? 266 SER A CB  1 
ATOM   775  O OG  . SER A 1 266 ? 6.920   -30.161 23.389 1.00 32.85 ? 266 SER A OG  1 
ATOM   776  N N   . HIS A 1 267 ? 9.583   -28.604 23.778 1.00 28.68 ? 267 HIS A N   1 
ATOM   777  C CA  . HIS A 1 267 ? 10.432  -27.732 22.988 1.00 28.47 ? 267 HIS A CA  1 
ATOM   778  C C   . HIS A 1 267 ? 11.753  -27.389 23.653 1.00 28.63 ? 267 HIS A C   1 
ATOM   779  O O   . HIS A 1 267 ? 11.863  -27.460 24.869 1.00 27.86 ? 267 HIS A O   1 
ATOM   780  C CB  . HIS A 1 267 ? 9.678   -26.455 22.606 1.00 28.05 ? 267 HIS A CB  1 
ATOM   781  C CG  . HIS A 1 267 ? 8.734   -26.640 21.461 1.00 28.03 ? 267 HIS A CG  1 
ATOM   782  N ND1 . HIS A 1 267 ? 9.192   -26.939 20.199 1.00 29.31 ? 267 HIS A ND1 1 
ATOM   783  C CD2 . HIS A 1 267 ? 7.383   -26.566 21.431 1.00 28.42 ? 267 HIS A CD2 1 
ATOM   784  C CE1 . HIS A 1 267 ? 8.115   -27.029 19.438 1.00 29.66 ? 267 HIS A CE1 1 
ATOM   785  N NE2 . HIS A 1 267 ? 7.004   -26.806 20.138 1.00 28.92 ? 267 HIS A NE2 1 
ATOM   786  N N   . SER A 1 268 ? 12.757  -27.003 22.852 1.00 28.70 ? 268 SER A N   1 
ATOM   787  C CA  . SER A 1 268 ? 14.050  -26.589 23.404 1.00 29.17 ? 268 SER A CA  1 
ATOM   788  C C   . SER A 1 268 ? 14.206  -25.049 23.465 1.00 28.55 ? 268 SER A C   1 
ATOM   789  O O   . SER A 1 268 ? 15.222  -24.562 23.951 1.00 29.67 ? 268 SER A O   1 
ATOM   790  C CB  . SER A 1 268 ? 15.184  -27.160 22.563 1.00 31.32 ? 268 SER A CB  1 
ATOM   791  O OG  . SER A 1 268 ? 15.094  -26.640 21.246 1.00 36.03 ? 268 SER A OG  1 
ATOM   792  N N   . ALA A 1 269 ? 13.238  -24.289 22.952 1.00 26.63 ? 269 ALA A N   1 
ATOM   793  C CA  . ALA A 1 269 ? 13.325  -22.832 22.912 1.00 25.79 ? 269 ALA A CA  1 
ATOM   794  C C   . ALA A 1 269 ? 11.908  -22.222 22.988 1.00 24.87 ? 269 ALA A C   1 
ATOM   795  O O   . ALA A 1 269 ? 10.928  -22.964 22.957 1.00 24.69 ? 269 ALA A O   1 
ATOM   796  C CB  . ALA A 1 269 ? 14.062  -22.397 21.634 1.00 25.41 ? 269 ALA A CB  1 
ATOM   797  N N   . ARG A 1 270 ? 11.770  -20.885 23.085 1.00 24.36 ? 270 ARG A N   1 
ATOM   798  C CA  . ARG A 1 270 ? 10.467  -20.254 23.209 1.00 24.90 ? 270 ARG A CA  1 
ATOM   799  C C   . ARG A 1 270 ? 9.460   -20.703 22.183 1.00 24.82 ? 270 ARG A C   1 
ATOM   800  O O   . ARG A 1 270 ? 9.823   -21.081 21.055 1.00 25.07 ? 270 ARG A O   1 
ATOM   801  C CB  . ARG A 1 270 ? 10.570  -18.729 23.209 1.00 26.37 ? 270 ARG A CB  1 
ATOM   802  C CG  . ARG A 1 270 ? 11.012  -18.156 21.896 1.00 29.22 ? 270 ARG A CG  1 
ATOM   803  C CD  . ARG A 1 270 ? 10.869  -16.662 21.942 1.00 30.89 ? 270 ARG A CD  1 
ATOM   804  N NE  . ARG A 1 270 ? 11.025  -16.049 20.621 1.00 30.65 ? 270 ARG A NE  1 
ATOM   805  C CZ  . ARG A 1 270 ? 11.222  -14.750 20.423 1.00 32.01 ? 270 ARG A CZ  1 
ATOM   806  N NH1 . ARG A 1 270 ? 11.360  -14.274 19.192 1.00 30.57 ? 270 ARG A NH1 1 
ATOM   807  N NH2 . ARG A 1 270 ? 11.295  -13.916 21.458 1.00 31.84 ? 270 ARG A NH2 1 
ATOM   808  N N   . VAL A 1 271 ? 8.196   -20.720 22.598 1.00 23.45 ? 271 VAL A N   1 
ATOM   809  C CA  . VAL A 1 271 ? 7.129   -21.121 21.706 1.00 23.09 ? 271 VAL A CA  1 
ATOM   810  C C   . VAL A 1 271 ? 6.426   -19.859 21.235 1.00 22.24 ? 271 VAL A C   1 
ATOM   811  O O   . VAL A 1 271 ? 5.595   -19.303 21.958 1.00 22.17 ? 271 VAL A O   1 
ATOM   812  C CB  . VAL A 1 271 ? 6.192   -22.073 22.441 1.00 23.89 ? 271 VAL A CB  1 
ATOM   813  C CG1 . VAL A 1 271 ? 4.960   -22.377 21.591 1.00 24.68 ? 271 VAL A CG1 1 
ATOM   814  C CG2 . VAL A 1 271 ? 6.937   -23.350 22.814 1.00 23.94 ? 271 VAL A CG2 1 
ATOM   815  N N   . GLY A 1 272 ? 6.805   -19.393 20.054 1.00 20.86 ? 272 GLY A N   1 
ATOM   816  C CA  . GLY A 1 272 ? 6.286   -18.149 19.503 1.00 21.07 ? 272 GLY A CA  1 
ATOM   817  C C   . GLY A 1 272 ? 5.017   -18.250 18.678 1.00 21.04 ? 272 GLY A C   1 
ATOM   818  O O   . GLY A 1 272 ? 4.397   -17.225 18.388 1.00 21.25 ? 272 GLY A O   1 
ATOM   819  N N   . SER A 1 273 ? 4.627   -19.462 18.282 1.00 20.14 ? 273 SER A N   1 
ATOM   820  C CA  . SER A 1 273 ? 3.430   -19.633 17.481 1.00 20.01 ? 273 SER A CA  1 
ATOM   821  C C   . SER A 1 273 ? 2.623   -20.838 17.922 1.00 19.50 ? 273 SER A C   1 
ATOM   822  O O   . SER A 1 273 ? 3.162   -21.814 18.459 1.00 18.58 ? 273 SER A O   1 
ATOM   823  C CB  . SER A 1 273 ? 3.785   -19.703 16.000 1.00 21.40 ? 273 SER A CB  1 
ATOM   824  O OG  . SER A 1 273 ? 4.697   -20.762 15.785 1.00 22.96 ? 273 SER A OG  1 
ATOM   825  N N   . LEU A 1 274 ? 1.306   -20.725 17.770 1.00 19.39 ? 274 LEU A N   1 
ATOM   826  C CA  . LEU A 1 274 ? 0.368   -21.764 18.184 1.00 19.18 ? 274 LEU A CA  1 
ATOM   827  C C   . LEU A 1 274 ? -0.807  -21.797 17.244 1.00 19.44 ? 274 LEU A C   1 
ATOM   828  O O   . LEU A 1 274 ? -1.275  -20.747 16.798 1.00 19.07 ? 274 LEU A O   1 
ATOM   829  C CB  . LEU A 1 274 ? -0.196  -21.444 19.570 1.00 18.64 ? 274 LEU A CB  1 
ATOM   830  C CG  . LEU A 1 274 ? 0.765   -21.470 20.751 1.00 19.66 ? 274 LEU A CG  1 
ATOM   831  C CD1 . LEU A 1 274 ? 0.123   -20.821 21.979 1.00 19.89 ? 274 LEU A CD1 1 
ATOM   832  C CD2 . LEU A 1 274 ? 1.194   -22.899 21.067 1.00 19.59 ? 274 LEU A CD2 1 
ATOM   833  N N   . SER A 1 275 ? -1.359  -22.986 17.046 1.00 19.59 ? 275 SER A N   1 
ATOM   834  C CA  . SER A 1 275 ? -2.556  -23.139 16.249 1.00 20.48 ? 275 SER A CA  1 
ATOM   835  C C   . SER A 1 275 ? -3.250  -24.420 16.632 1.00 22.19 ? 275 SER A C   1 
ATOM   836  O O   . SER A 1 275 ? -2.618  -25.467 16.707 1.00 23.16 ? 275 SER A O   1 
ATOM   837  C CB  . SER A 1 275 ? -2.224  -23.146 14.760 1.00 19.96 ? 275 SER A CB  1 
ATOM   838  O OG  . SER A 1 275 ? -3.399  -23.331 13.994 1.00 19.72 ? 275 SER A OG  1 
ATOM   839  N N   . TRP A 1 276 ? -4.548  -24.349 16.846 1.00 22.37 ? 276 TRP A N   1 
ATOM   840  C CA  . TRP A 1 276 ? -5.339  -25.514 17.201 1.00 23.05 ? 276 TRP A CA  1 
ATOM   841  C C   . TRP A 1 276 ? -5.999  -26.161 15.991 1.00 23.92 ? 276 TRP A C   1 
ATOM   842  O O   . TRP A 1 276 ? -6.399  -25.480 15.064 1.00 22.83 ? 276 TRP A O   1 
ATOM   843  C CB  . TRP A 1 276 ? -6.459  -25.095 18.138 1.00 22.43 ? 276 TRP A CB  1 
ATOM   844  C CG  . TRP A 1 276 ? -6.015  -24.727 19.517 1.00 23.01 ? 276 TRP A CG  1 
ATOM   845  C CD1 . TRP A 1 276 ? -5.706  -23.482 19.971 1.00 24.14 ? 276 TRP A CD1 1 
ATOM   846  C CD2 . TRP A 1 276 ? -5.988  -25.589 20.659 1.00 23.09 ? 276 TRP A CD2 1 
ATOM   847  N NE1 . TRP A 1 276 ? -5.435  -23.524 21.318 1.00 24.54 ? 276 TRP A NE1 1 
ATOM   848  C CE2 . TRP A 1 276 ? -5.614  -24.808 21.767 1.00 24.29 ? 276 TRP A CE2 1 
ATOM   849  C CE3 . TRP A 1 276 ? -6.207  -26.954 20.845 1.00 23.63 ? 276 TRP A CE3 1 
ATOM   850  C CZ2 . TRP A 1 276 ? -5.472  -25.346 23.043 1.00 25.16 ? 276 TRP A CZ2 1 
ATOM   851  C CZ3 . TRP A 1 276 ? -6.069  -27.486 22.106 1.00 24.89 ? 276 TRP A CZ3 1 
ATOM   852  C CH2 . TRP A 1 276 ? -5.703  -26.687 23.192 1.00 25.38 ? 276 TRP A CH2 1 
ATOM   853  N N   . ASN A 1 277 ? -6.195  -27.475 16.070 1.00 25.51 ? 277 ASN A N   1 
ATOM   854  C CA  . ASN A 1 277 ? -6.957  -28.298 15.147 1.00 27.07 ? 277 ASN A CA  1 
ATOM   855  C C   . ASN A 1 277 ? -7.705  -29.269 16.043 1.00 28.48 ? 277 ASN A C   1 
ATOM   856  O O   . ASN A 1 277 ? -7.138  -30.298 16.427 1.00 29.14 ? 277 ASN A O   1 
ATOM   857  C CB  . ASN A 1 277 ? -6.065  -29.067 14.211 1.00 28.96 ? 277 ASN A CB  1 
ATOM   858  C CG  . ASN A 1 277 ? -6.838  -29.954 13.268 1.00 33.15 ? 277 ASN A CG  1 
ATOM   859  O OD1 . ASN A 1 277 ? -8.057  -29.820 13.080 1.00 34.68 ? 277 ASN A OD1 1 
ATOM   860  N ND2 . ASN A 1 277 ? -6.145  -30.895 12.669 1.00 34.99 ? 277 ASN A ND2 1 
ATOM   861  N N   . SER A 1 278 ? -8.932  -28.901 16.452 1.00 28.43 ? 278 SER A N   1 
ATOM   862  C CA  . SER A 1 278 ? -9.724  -29.684 17.390 1.00 29.38 ? 278 SER A CA  1 
ATOM   863  C C   . SER A 1 278 ? -8.939  -29.755 18.745 1.00 30.72 ? 278 SER A C   1 
ATOM   864  O O   . SER A 1 278 ? -8.472  -28.714 19.216 1.00 30.27 ? 278 SER A O   1 
ATOM   865  C CB  . SER A 1 278 ? -10.089 -31.039 16.790 1.00 30.65 ? 278 SER A CB  1 
ATOM   866  O OG  . SER A 1 278 ? -10.938 -31.748 17.669 1.00 34.55 ? 278 SER A OG  1 
ATOM   867  N N   . TYR A 1 279 ? -8.728  -30.940 19.315 1.00 31.59 ? 279 TYR A N   1 
ATOM   868  C CA  . TYR A 1 279 ? -7.967  -31.130 20.545 1.00 32.35 ? 279 TYR A CA  1 
ATOM   869  C C   . TYR A 1 279 ? -6.438  -31.189 20.301 1.00 31.19 ? 279 TYR A C   1 
ATOM   870  O O   . TYR A 1 279 ? -5.673  -31.364 21.253 1.00 31.79 ? 279 TYR A O   1 
ATOM   871  C CB  . TYR A 1 279 ? -8.451  -32.403 21.254 1.00 34.01 ? 279 TYR A CB  1 
ATOM   872  C CG  . TYR A 1 279 ? -8.411  -33.634 20.364 1.00 37.18 ? 279 TYR A CG  1 
ATOM   873  C CD1 . TYR A 1 279 ? -7.202  -34.215 20.000 1.00 39.04 ? 279 TYR A CD1 1 
ATOM   874  C CD2 . TYR A 1 279 ? -9.580  -34.211 19.883 1.00 38.98 ? 279 TYR A CD2 1 
ATOM   875  C CE1 . TYR A 1 279 ? -7.154  -35.322 19.163 1.00 40.37 ? 279 TYR A CE1 1 
ATOM   876  C CE2 . TYR A 1 279 ? -9.547  -35.351 19.084 1.00 40.21 ? 279 TYR A CE2 1 
ATOM   877  C CZ  . TYR A 1 279 ? -8.329  -35.907 18.732 1.00 41.80 ? 279 TYR A CZ  1 
ATOM   878  O OH  . TYR A 1 279 ? -8.267  -37.024 17.927 1.00 44.58 ? 279 TYR A OH  1 
ATOM   879  N N   . ILE A 1 280 ? -5.992  -31.080 19.045 1.00 29.62 ? 280 ILE A N   1 
ATOM   880  C CA  . ILE A 1 280 ? -4.572  -31.063 18.737 1.00 28.51 ? 280 ILE A CA  1 
ATOM   881  C C   . ILE A 1 280 ? -4.138  -29.623 18.746 1.00 27.99 ? 280 ILE A C   1 
ATOM   882  O O   . ILE A 1 280 ? -4.709  -28.792 18.045 1.00 28.49 ? 280 ILE A O   1 
ATOM   883  C CB  . ILE A 1 280 ? -4.258  -31.701 17.370 1.00 28.79 ? 280 ILE A CB  1 
ATOM   884  C CG1 . ILE A 1 280 ? -4.543  -33.202 17.399 1.00 29.46 ? 280 ILE A CG1 1 
ATOM   885  C CG2 . ILE A 1 280 ? -2.806  -31.407 16.929 1.00 29.40 ? 280 ILE A CG2 1 
ATOM   886  C CD1 . ILE A 1 280 ? -3.677  -33.996 18.331 1.00 30.52 ? 280 ILE A CD1 1 
ATOM   887  N N   . LEU A 1 281 ? -3.118  -29.329 19.526 1.00 26.60 ? 281 LEU A N   1 
ATOM   888  C CA  . LEU A 1 281 ? -2.538  -28.012 19.578 1.00 25.51 ? 281 LEU A CA  1 
ATOM   889  C C   . LEU A 1 281 ? -1.185  -28.128 18.955 1.00 24.93 ? 281 LEU A C   1 
ATOM   890  O O   . LEU A 1 281 ? -0.372  -28.923 19.397 1.00 25.65 ? 281 LEU A O   1 
ATOM   891  C CB  . LEU A 1 281 ? -2.381  -27.566 21.024 1.00 25.53 ? 281 LEU A CB  1 
ATOM   892  C CG  . LEU A 1 281 ? -1.607  -26.280 21.273 1.00 26.07 ? 281 LEU A CG  1 
ATOM   893  C CD1 . LEU A 1 281 ? -2.231  -25.080 20.514 1.00 25.46 ? 281 LEU A CD1 1 
ATOM   894  C CD2 . LEU A 1 281 ? -1.556  -26.018 22.740 1.00 26.78 ? 281 LEU A CD2 1 
ATOM   895  N N   . SER A 1 282 ? -0.912  -27.294 17.988 1.00 23.53 ? 282 SER A N   1 
ATOM   896  C CA  . SER A 1 282 ? 0.385   -27.262 17.345 1.00 22.58 ? 282 SER A CA  1 
ATOM   897  C C   . SER A 1 282 ? 1.146   -26.070 17.873 1.00 21.02 ? 282 SER A C   1 
ATOM   898  O O   . SER A 1 282 ? 0.591   -24.977 18.007 1.00 20.26 ? 282 SER A O   1 
ATOM   899  C CB  . SER A 1 282 ? 0.230   -27.194 15.831 1.00 22.87 ? 282 SER A CB  1 
ATOM   900  O OG  . SER A 1 282 ? -0.448  -28.347 15.366 1.00 23.53 ? 282 SER A OG  1 
ATOM   901  N N   . SER A 1 283 ? 2.425   -26.276 18.145 1.00 20.28 ? 283 SER A N   1 
ATOM   902  C CA  . SER A 1 283 ? 3.273   -25.228 18.666 1.00 20.59 ? 283 SER A CA  1 
ATOM   903  C C   . SER A 1 283 ? 4.506   -25.095 17.839 1.00 21.80 ? 283 SER A C   1 
ATOM   904  O O   . SER A 1 283 ? 5.103   -26.092 17.457 1.00 21.82 ? 283 SER A O   1 
ATOM   905  C CB  . SER A 1 283 ? 3.667   -25.534 20.107 1.00 20.89 ? 283 SER A CB  1 
ATOM   906  O OG  . SER A 1 283 ? 4.313   -26.793 20.197 1.00 21.00 ? 283 SER A OG  1 
ATOM   907  N N   . GLY A 1 284 ? 4.906   -23.859 17.595 1.00 22.59 ? 284 GLY A N   1 
ATOM   908  C CA  . GLY A 1 284 ? 6.099   -23.557 16.820 1.00 23.76 ? 284 GLY A CA  1 
ATOM   909  C C   . GLY A 1 284 ? 7.095   -22.885 17.729 1.00 24.77 ? 284 GLY A C   1 
ATOM   910  O O   . GLY A 1 284 ? 6.717   -22.055 18.562 1.00 24.69 ? 284 GLY A O   1 
ATOM   911  N N   . SER A 1 285 ? 8.358   -23.226 17.565 1.00 25.18 ? 285 SER A N   1 
ATOM   912  C CA  . SER A 1 285 ? 9.411   -22.739 18.411 1.00 26.41 ? 285 SER A CA  1 
ATOM   913  C C   . SER A 1 285 ? 10.512  -21.984 17.693 1.00 26.80 ? 285 SER A C   1 
ATOM   914  O O   . SER A 1 285 ? 10.724  -22.168 16.492 1.00 25.81 ? 285 SER A O   1 
ATOM   915  C CB  . SER A 1 285 ? 10.024  -23.925 19.147 1.00 29.07 ? 285 SER A CB  1 
ATOM   916  O OG  . SER A 1 285 ? 11.060  -23.547 20.036 1.00 32.85 ? 285 SER A OG  1 
ATOM   917  N N   . ARG A 1 286 ? 11.264  -21.171 18.461 1.00 27.76 ? 286 ARG A N   1 
ATOM   918  C CA  . ARG A 1 286 ? 12.450  -20.476 17.971 1.00 28.75 ? 286 ARG A CA  1 
ATOM   919  C C   . ARG A 1 286 ? 13.488  -21.496 17.452 1.00 28.81 ? 286 ARG A C   1 
ATOM   920  O O   . ARG A 1 286 ? 14.274  -21.158 16.587 1.00 29.34 ? 286 ARG A O   1 
ATOM   921  C CB  . ARG A 1 286 ? 13.035  -19.586 19.081 1.00 31.42 ? 286 ARG A CB  1 
ATOM   922  C CG  . ARG A 1 286 ? 14.196  -18.675 18.655 1.00 36.45 ? 286 ARG A CG  1 
ATOM   923  C CD  . ARG A 1 286 ? 14.524  -17.587 19.688 1.00 42.17 ? 286 ARG A CD  1 
ATOM   924  N NE  . ARG A 1 286 ? 14.642  -18.145 21.037 1.00 47.93 ? 286 ARG A NE  1 
ATOM   925  C CZ  . ARG A 1 286 ? 14.560  -17.439 22.163 1.00 50.50 ? 286 ARG A CZ  1 
ATOM   926  N NH1 . ARG A 1 286 ? 14.626  -18.048 23.342 1.00 47.89 ? 286 ARG A NH1 1 
ATOM   927  N NH2 . ARG A 1 286 ? 14.414  -16.119 22.118 1.00 51.43 ? 286 ARG A NH2 1 
ATOM   928  N N   . SER A 1 287 ? 13.441  -22.752 17.906 1.00 28.84 ? 287 SER A N   1 
ATOM   929  C CA  . SER A 1 287 ? 14.323  -23.818 17.429 1.00 29.70 ? 287 SER A CA  1 
ATOM   930  C C   . SER A 1 287 ? 14.056  -24.238 15.970 1.00 29.93 ? 287 SER A C   1 
ATOM   931  O O   . SER A 1 287 ? 14.886  -24.911 15.365 1.00 30.90 ? 287 SER A O   1 
ATOM   932  C CB  . SER A 1 287 ? 14.114  -25.051 18.293 1.00 31.52 ? 287 SER A CB  1 
ATOM   933  O OG  . SER A 1 287 ? 12.765  -25.469 18.156 1.00 34.49 ? 287 SER A OG  1 
ATOM   934  N N   . GLY A 1 288 ? 12.885  -23.917 15.448 1.00 28.63 ? 288 GLY A N   1 
ATOM   935  C CA  . GLY A 1 288 ? 12.508  -24.318 14.103 1.00 28.26 ? 288 GLY A CA  1 
ATOM   936  C C   . GLY A 1 288 ? 11.589  -25.519 14.055 1.00 27.81 ? 288 GLY A C   1 
ATOM   937  O O   . GLY A 1 288 ? 11.107  -25.880 12.981 1.00 27.95 ? 288 GLY A O   1 
ATOM   938  N N   . HIS A 1 289 ? 11.321  -26.138 15.209 1.00 27.01 ? 289 HIS A N   1 
ATOM   939  C CA  . HIS A 1 289 ? 10.463  -27.308 15.258 1.00 26.96 ? 289 HIS A CA  1 
ATOM   940  C C   . HIS A 1 289 ? 9.029   -26.961 15.557 1.00 26.46 ? 289 HIS A C   1 
ATOM   941  O O   . HIS A 1 289 ? 8.720   -25.974 16.224 1.00 26.35 ? 289 HIS A O   1 
ATOM   942  C CB  . HIS A 1 289 ? 10.966  -28.317 16.301 1.00 27.64 ? 289 HIS A CB  1 
ATOM   943  C CG  . HIS A 1 289 ? 12.375  -28.757 16.075 1.00 30.44 ? 289 HIS A CG  1 
ATOM   944  N ND1 . HIS A 1 289 ? 12.723  -29.534 14.974 1.00 32.63 ? 289 HIS A ND1 1 
ATOM   945  C CD2 . HIS A 1 289 ? 13.482  -28.523 16.818 1.00 31.18 ? 289 HIS A CD2 1 
ATOM   946  C CE1 . HIS A 1 289 ? 14.026  -29.751 15.089 1.00 33.26 ? 289 HIS A CE1 1 
ATOM   947  N NE2 . HIS A 1 289 ? 14.525  -29.174 16.189 1.00 32.76 ? 289 HIS A NE2 1 
ATOM   948  N N   . ILE A 1 290 ? 8.148   -27.798 15.070 1.00 25.79 ? 290 ILE A N   1 
ATOM   949  C CA  . ILE A 1 290 ? 6.734   -27.692 15.340 1.00 25.43 ? 290 ILE A CA  1 
ATOM   950  C C   . ILE A 1 290 ? 6.372   -28.962 16.061 1.00 25.56 ? 290 ILE A C   1 
ATOM   951  O O   . ILE A 1 290 ? 6.772   -30.031 15.615 1.00 25.97 ? 290 ILE A O   1 
ATOM   952  C CB  . ILE A 1 290 ? 5.926   -27.576 14.030 1.00 25.56 ? 290 ILE A CB  1 
ATOM   953  C CG1 . ILE A 1 290 ? 6.160   -26.228 13.347 1.00 25.70 ? 290 ILE A CG1 1 
ATOM   954  C CG2 . ILE A 1 290 ? 4.432   -27.820 14.278 1.00 25.89 ? 290 ILE A CG2 1 
ATOM   955  C CD1 . ILE A 1 290 ? 5.759   -26.255 11.891 1.00 26.17 ? 290 ILE A CD1 1 
ATOM   956  N N   . HIS A 1 291 ? 5.604   -28.869 17.155 1.00 25.24 ? 291 HIS A N   1 
ATOM   957  C CA  . HIS A 1 291 ? 5.158   -30.053 17.852 1.00 25.43 ? 291 HIS A CA  1 
ATOM   958  C C   . HIS A 1 291 ? 3.651   -30.119 17.821 1.00 26.99 ? 291 HIS A C   1 
ATOM   959  O O   . HIS A 1 291 ? 2.989   -29.094 17.981 1.00 27.59 ? 291 HIS A O   1 
ATOM   960  C CB  . HIS A 1 291 ? 5.629   -30.032 19.318 1.00 24.97 ? 291 HIS A CB  1 
ATOM   961  C CG  . HIS A 1 291 ? 7.108   -30.205 19.500 1.00 25.30 ? 291 HIS A CG  1 
ATOM   962  N ND1 . HIS A 1 291 ? 7.683   -30.127 20.744 1.00 25.96 ? 291 HIS A ND1 1 
ATOM   963  C CD2 . HIS A 1 291 ? 8.077   -30.462 18.590 1.00 25.87 ? 291 HIS A CD2 1 
ATOM   964  C CE1 . HIS A 1 291 ? 8.976   -30.310 20.556 1.00 26.39 ? 291 HIS A CE1 1 
ATOM   965  N NE2 . HIS A 1 291 ? 9.258   -30.516 19.277 1.00 26.46 ? 291 HIS A NE2 1 
ATOM   966  N N   . HIS A 1 292 ? 3.093   -31.327 17.656 1.00 26.91 ? 292 HIS A N   1 
ATOM   967  C CA  . HIS A 1 292 ? 1.653   -31.508 17.811 1.00 26.54 ? 292 HIS A CA  1 
ATOM   968  C C   . HIS A 1 292 ? 1.470   -32.027 19.224 1.00 25.62 ? 292 HIS A C   1 
ATOM   969  O O   . HIS A 1 292 ? 2.168   -32.950 19.648 1.00 25.56 ? 292 HIS A O   1 
ATOM   970  C CB  . HIS A 1 292 ? 1.071   -32.531 16.846 1.00 27.91 ? 292 HIS A CB  1 
ATOM   971  C CG  . HIS A 1 292 ? 1.025   -32.070 15.428 1.00 30.70 ? 292 HIS A CG  1 
ATOM   972  N ND1 . HIS A 1 292 ? 0.786   -30.753 15.106 1.00 32.55 ? 292 HIS A ND1 1 
ATOM   973  C CD2 . HIS A 1 292 ? 1.184   -32.778 14.287 1.00 31.94 ? 292 HIS A CD2 1 
ATOM   974  C CE1 . HIS A 1 292 ? 0.833   -30.691 13.784 1.00 33.01 ? 292 HIS A CE1 1 
ATOM   975  N NE2 . HIS A 1 292 ? 1.064   -31.884 13.248 1.00 33.01 ? 292 HIS A NE2 1 
ATOM   976  N N   . HIS A 1 293 ? 0.524   -31.448 19.940 1.00 24.99 ? 293 HIS A N   1 
ATOM   977  C CA  . HIS A 1 293 ? 0.209   -31.839 21.303 1.00 25.88 ? 293 HIS A CA  1 
ATOM   978  C C   . HIS A 1 293 ? -1.228  -32.321 21.358 1.00 26.82 ? 293 HIS A C   1 
ATOM   979  O O   . HIS A 1 293 ? -2.134  -31.582 20.969 1.00 26.32 ? 293 HIS A O   1 
ATOM   980  C CB  . HIS A 1 293 ? 0.332   -30.649 22.271 1.00 25.57 ? 293 HIS A CB  1 
ATOM   981  C CG  . HIS A 1 293 ? 1.641   -29.946 22.220 1.00 26.26 ? 293 HIS A CG  1 
ATOM   982  N ND1 . HIS A 1 293 ? 2.713   -30.368 22.975 1.00 27.80 ? 293 HIS A ND1 1 
ATOM   983  C CD2 . HIS A 1 293 ? 2.004   -28.856 21.516 1.00 27.00 ? 293 HIS A CD2 1 
ATOM   984  C CE1 . HIS A 1 293 ? 3.690   -29.522 22.710 1.00 28.18 ? 293 HIS A CE1 1 
ATOM   985  N NE2 . HIS A 1 293 ? 3.311   -28.603 21.829 1.00 28.10 ? 293 HIS A NE2 1 
ATOM   986  N N   . ASP A 1 294 ? -1.442  -33.547 21.854 1.00 27.60 ? 294 ASP A N   1 
ATOM   987  C CA  . ASP A 1 294 ? -2.791  -34.030 22.087 1.00 28.60 ? 294 ASP A CA  1 
ATOM   988  C C   . ASP A 1 294 ? -2.996  -33.622 23.525 1.00 29.10 ? 294 ASP A C   1 
ATOM   989  O O   . ASP A 1 294 ? -2.453  -34.249 24.429 1.00 29.57 ? 294 ASP A O   1 
ATOM   990  C CB  . ASP A 1 294 ? -2.908  -35.544 21.926 1.00 29.82 ? 294 ASP A CB  1 
ATOM   991  C CG  . ASP A 1 294 ? -4.322  -36.070 22.166 1.00 34.62 ? 294 ASP A CG  1 
ATOM   992  O OD1 . ASP A 1 294 ? -5.147  -35.335 22.783 1.00 33.94 ? 294 ASP A OD1 1 
ATOM   993  O OD2 . ASP A 1 294 ? -4.605  -37.219 21.750 1.00 37.44 ? 294 ASP A OD2 1 
ATOM   994  N N   . VAL A 1 295 ? -3.713  -32.529 23.737 1.00 28.92 ? 295 VAL A N   1 
ATOM   995  C CA  . VAL A 1 295 ? -3.873  -31.959 25.074 1.00 29.14 ? 295 VAL A CA  1 
ATOM   996  C C   . VAL A 1 295 ? -4.725  -32.787 26.022 1.00 29.48 ? 295 VAL A C   1 
ATOM   997  O O   . VAL A 1 295 ? -4.744  -32.500 27.221 1.00 29.82 ? 295 VAL A O   1 
ATOM   998  C CB  . VAL A 1 295 ? -4.388  -30.512 24.996 1.00 29.74 ? 295 VAL A CB  1 
ATOM   999  C CG1 . VAL A 1 295 ? -3.501  -29.680 24.057 1.00 29.77 ? 295 VAL A CG1 1 
ATOM   1000 C CG2 . VAL A 1 295 ? -5.853  -30.479 24.553 1.00 29.78 ? 295 VAL A CG2 1 
ATOM   1001 N N   . ARG A 1 296 ? -5.387  -33.826 25.521 1.00 29.39 ? 296 ARG A N   1 
ATOM   1002 C CA  . ARG A 1 296 ? -6.206  -34.681 26.350 1.00 29.83 ? 296 ARG A CA  1 
ATOM   1003 C C   . ARG A 1 296 ? -5.413  -35.789 27.048 1.00 30.13 ? 296 ARG A C   1 
ATOM   1004 O O   . ARG A 1 296 ? -5.946  -36.411 27.968 1.00 29.93 ? 296 ARG A O   1 
ATOM   1005 C CB  . ARG A 1 296 ? -7.294  -35.340 25.508 1.00 31.29 ? 296 ARG A CB  1 
ATOM   1006 C CG  . ARG A 1 296 ? -8.055  -34.424 24.554 1.00 34.83 ? 296 ARG A CG  1 
ATOM   1007 C CD  . ARG A 1 296 ? -8.815  -35.273 23.545 1.00 37.86 ? 296 ARG A CD  1 
ATOM   1008 N NE  . ARG A 1 296 ? -7.896  -36.045 22.700 1.00 41.17 ? 296 ARG A NE  1 
ATOM   1009 C CZ  . ARG A 1 296 ? -8.251  -37.095 21.965 1.00 42.84 ? 296 ARG A CZ  1 
ATOM   1010 N NH1 . ARG A 1 296 ? -7.348  -37.732 21.227 1.00 41.44 ? 296 ARG A NH1 1 
ATOM   1011 N NH2 . ARG A 1 296 ? -9.514  -37.513 21.956 1.00 42.22 ? 296 ARG A NH2 1 
ATOM   1012 N N   . VAL A 1 297 ? -4.184  -36.090 26.586 1.00 30.00 ? 297 VAL A N   1 
ATOM   1013 C CA  . VAL A 1 297 ? -3.442  -37.225 27.111 1.00 30.99 ? 297 VAL A CA  1 
ATOM   1014 C C   . VAL A 1 297 ? -2.140  -36.875 27.856 1.00 32.29 ? 297 VAL A C   1 
ATOM   1015 O O   . VAL A 1 297 ? -1.546  -35.835 27.617 1.00 32.58 ? 297 VAL A O   1 
ATOM   1016 C CB  . VAL A 1 297 ? -3.176  -38.249 25.981 1.00 31.64 ? 297 VAL A CB  1 
ATOM   1017 C CG1 . VAL A 1 297 ? -4.482  -38.653 25.300 1.00 32.41 ? 297 VAL A CG1 1 
ATOM   1018 C CG2 . VAL A 1 297 ? -2.182  -37.717 24.954 1.00 31.90 ? 297 VAL A CG2 1 
ATOM   1019 N N   . ALA A 1 298 ? -1.690  -37.770 28.729 1.00 32.93 ? 298 ALA A N   1 
ATOM   1020 C CA  . ALA A 1 298 ? -0.465  -37.630 29.524 1.00 33.79 ? 298 ALA A CA  1 
ATOM   1021 C C   . ALA A 1 298 ? 0.786   -37.319 28.671 1.00 34.69 ? 298 ALA A C   1 
ATOM   1022 O O   . ALA A 1 298 ? 1.431   -36.316 28.935 1.00 34.93 ? 298 ALA A O   1 
ATOM   1023 C CB  . ALA A 1 298 ? -0.250  -38.874 30.374 1.00 33.59 ? 298 ALA A CB  1 
ATOM   1024 N N   . GLU A 1 299 ? 1.109   -38.131 27.650 1.00 34.82 ? 299 GLU A N   1 
ATOM   1025 C CA  . GLU A 1 299 ? 2.256   -37.857 26.787 1.00 35.47 ? 299 GLU A CA  1 
ATOM   1026 C C   . GLU A 1 299 ? 1.717   -37.086 25.635 1.00 34.77 ? 299 GLU A C   1 
ATOM   1027 O O   . GLU A 1 299 ? 1.328   -37.662 24.625 1.00 35.12 ? 299 GLU A O   1 
ATOM   1028 C CB  . GLU A 1 299 ? 2.935   -39.149 26.304 1.00 39.57 ? 299 GLU A CB  1 
ATOM   1029 C CG  . GLU A 1 299 ? 3.682   -39.895 27.397 1.00 46.97 ? 299 GLU A CG  1 
ATOM   1030 C CD  . GLU A 1 299 ? 4.689   -39.058 28.164 1.00 56.49 ? 299 GLU A CD  1 
ATOM   1031 O OE1 . GLU A 1 299 ? 5.357   -38.202 27.538 1.00 58.03 ? 299 GLU A OE1 1 
ATOM   1032 O OE2 . GLU A 1 299 ? 4.807   -39.257 29.395 1.00 59.80 ? 299 GLU A OE2 1 
ATOM   1033 N N   . HIS A 1 300 ? 1.612   -35.780 25.818 1.00 33.63 ? 300 HIS A N   1 
ATOM   1034 C CA  . HIS A 1 300 ? 1.002   -34.879 24.861 1.00 33.46 ? 300 HIS A CA  1 
ATOM   1035 C C   . HIS A 1 300 ? 1.742   -34.797 23.528 1.00 33.52 ? 300 HIS A C   1 
ATOM   1036 O O   . HIS A 1 300 ? 1.116   -34.592 22.504 1.00 32.96 ? 300 HIS A O   1 
ATOM   1037 C CB  . HIS A 1 300 ? 0.914   -33.478 25.478 1.00 34.27 ? 300 HIS A CB  1 
ATOM   1038 C CG  . HIS A 1 300 ? 2.254   -32.965 25.899 1.00 37.40 ? 300 HIS A CG  1 
ATOM   1039 N ND1 . HIS A 1 300 ? 3.099   -32.341 25.000 1.00 39.43 ? 300 HIS A ND1 1 
ATOM   1040 C CD2 . HIS A 1 300 ? 2.880   -33.058 27.098 1.00 38.74 ? 300 HIS A CD2 1 
ATOM   1041 C CE1 . HIS A 1 300 ? 4.201   -32.067 25.678 1.00 40.27 ? 300 HIS A CE1 1 
ATOM   1042 N NE2 . HIS A 1 300 ? 4.114   -32.479 26.945 1.00 40.06 ? 300 HIS A NE2 1 
ATOM   1043 N N   . HIS A 1 301 ? 3.065   -34.909 23.548 1.00 33.62 ? 301 HIS A N   1 
ATOM   1044 C CA  . HIS A 1 301 ? 3.881   -34.749 22.361 1.00 33.42 ? 301 HIS A CA  1 
ATOM   1045 C C   . HIS A 1 301 ? 3.750   -35.933 21.424 1.00 33.78 ? 301 HIS A C   1 
ATOM   1046 O O   . HIS A 1 301 ? 4.434   -36.931 21.586 1.00 33.68 ? 301 HIS A O   1 
ATOM   1047 C CB  . HIS A 1 301 ? 5.332   -34.503 22.766 1.00 34.19 ? 301 HIS A CB  1 
ATOM   1048 C CG  . HIS A 1 301 ? 6.226   -34.122 21.625 1.00 37.87 ? 301 HIS A CG  1 
ATOM   1049 N ND1 . HIS A 1 301 ? 7.600   -34.239 21.724 1.00 39.76 ? 301 HIS A ND1 1 
ATOM   1050 C CD2 . HIS A 1 301 ? 5.914   -33.638 20.396 1.00 38.97 ? 301 HIS A CD2 1 
ATOM   1051 C CE1 . HIS A 1 301 ? 8.078   -33.825 20.561 1.00 40.46 ? 301 HIS A CE1 1 
ATOM   1052 N NE2 . HIS A 1 301 ? 7.099   -33.467 19.727 1.00 40.32 ? 301 HIS A NE2 1 
ATOM   1053 N N   . VAL A 1 302 ? 2.864   -35.821 20.430 1.00 34.06 ? 302 VAL A N   1 
ATOM   1054 C CA  . VAL A 1 302 ? 2.577   -36.925 19.509 1.00 34.00 ? 302 VAL A CA  1 
ATOM   1055 C C   . VAL A 1 302 ? 3.221   -36.789 18.127 1.00 34.27 ? 302 VAL A C   1 
ATOM   1056 O O   . VAL A 1 302 ? 3.110   -37.709 17.310 1.00 34.87 ? 302 VAL A O   1 
ATOM   1057 C CB  . VAL A 1 302 ? 1.053   -37.119 19.394 1.00 34.24 ? 302 VAL A CB  1 
ATOM   1058 C CG1 . VAL A 1 302 ? 0.452   -37.486 20.759 1.00 34.42 ? 302 VAL A CG1 1 
ATOM   1059 C CG2 . VAL A 1 302 ? 0.393   -35.859 18.847 1.00 34.48 ? 302 VAL A CG2 1 
ATOM   1060 N N   . ALA A 1 303 ? 3.852   -35.652 17.834 1.00 33.43 ? 303 ALA A N   1 
ATOM   1061 C CA  . ALA A 1 303 ? 4.527   -35.465 16.547 1.00 33.13 ? 303 ALA A CA  1 
ATOM   1062 C C   . ALA A 1 303 ? 5.483   -34.303 16.591 1.00 32.48 ? 303 ALA A C   1 
ATOM   1063 O O   . ALA A 1 303 ? 5.265   -33.340 17.320 1.00 32.72 ? 303 ALA A O   1 
ATOM   1064 C CB  . ALA A 1 303 ? 3.517   -35.259 15.416 1.00 33.37 ? 303 ALA A CB  1 
ATOM   1065 N N   . THR A 1 304 ? 6.536   -34.396 15.791 1.00 31.60 ? 304 THR A N   1 
ATOM   1066 C CA  . THR A 1 304 ? 7.529   -33.351 15.596 1.00 31.09 ? 304 THR A CA  1 
ATOM   1067 C C   . THR A 1 304 ? 7.633   -33.149 14.097 1.00 29.28 ? 304 THR A C   1 
ATOM   1068 O O   . THR A 1 304 ? 7.910   -34.100 13.372 1.00 29.26 ? 304 THR A O   1 
ATOM   1069 C CB  . THR A 1 304 ? 8.884   -33.781 16.169 1.00 32.90 ? 304 THR A CB  1 
ATOM   1070 O OG1 . THR A 1 304 ? 8.728   -33.993 17.568 1.00 34.13 ? 304 THR A OG1 1 
ATOM   1071 C CG2 . THR A 1 304 ? 9.968   -32.747 15.929 1.00 33.32 ? 304 THR A CG2 1 
ATOM   1072 N N   . LEU A 1 305 ? 7.356   -31.933 13.634 1.00 27.91 ? 305 LEU A N   1 
ATOM   1073 C CA  . LEU A 1 305 ? 7.388   -31.542 12.224 1.00 27.13 ? 305 LEU A CA  1 
ATOM   1074 C C   . LEU A 1 305 ? 8.580   -30.630 12.117 1.00 27.34 ? 305 LEU A C   1 
ATOM   1075 O O   . LEU A 1 305 ? 8.610   -29.576 12.753 1.00 27.22 ? 305 LEU A O   1 
ATOM   1076 C CB  . LEU A 1 305 ? 6.115   -30.773 11.851 1.00 26.70 ? 305 LEU A CB  1 
ATOM   1077 C CG  . LEU A 1 305 ? 4.862   -31.581 11.531 1.00 27.80 ? 305 LEU A CG  1 
ATOM   1078 C CD1 . LEU A 1 305 ? 4.438   -32.470 12.691 1.00 28.32 ? 305 LEU A CD1 1 
ATOM   1079 C CD2 . LEU A 1 305 ? 3.693   -30.669 11.189 1.00 27.81 ? 305 LEU A CD2 1 
ATOM   1080 N N   . SER A 1 306 ? 9.602   -31.060 11.388 1.00 27.67 ? 306 SER A N   1 
ATOM   1081 C CA  . SER A 1 306 ? 10.840  -30.313 11.301 1.00 28.89 ? 306 SER A CA  1 
ATOM   1082 C C   . SER A 1 306 ? 11.114  -29.928 9.889  1.00 29.41 ? 306 SER A C   1 
ATOM   1083 O O   . SER A 1 306 ? 11.690  -30.706 9.141  1.00 30.09 ? 306 SER A O   1 
ATOM   1084 C CB  . SER A 1 306 ? 12.001  -31.133 11.853 1.00 31.45 ? 306 SER A CB  1 
ATOM   1085 O OG  . SER A 1 306 ? 11.771  -31.399 13.225 1.00 36.22 ? 306 SER A OG  1 
ATOM   1086 N N   . GLY A 1 307 ? 10.708  -28.722 9.532  1.00 28.41 ? 307 GLY A N   1 
ATOM   1087 C CA  . GLY A 1 307 ? 10.938  -28.186 8.201  1.00 27.63 ? 307 GLY A CA  1 
ATOM   1088 C C   . GLY A 1 307 ? 11.483  -26.774 8.218  1.00 26.16 ? 307 GLY A C   1 
ATOM   1089 O O   . GLY A 1 307 ? 11.573  -26.150 7.166  1.00 25.86 ? 307 GLY A O   1 
ATOM   1090 N N   . HIS A 1 308 ? 11.854  -26.255 9.397  1.00 24.95 ? 308 HIS A N   1 
ATOM   1091 C CA  . HIS A 1 308 ? 12.416  -24.920 9.506  1.00 25.12 ? 308 HIS A CA  1 
ATOM   1092 C C   . HIS A 1 308 ? 13.723  -24.952 10.250 1.00 26.55 ? 308 HIS A C   1 
ATOM   1093 O O   . HIS A 1 308 ? 13.883  -25.720 11.198 1.00 26.17 ? 308 HIS A O   1 
ATOM   1094 C CB  . HIS A 1 308 ? 11.475  -23.959 10.231 1.00 24.28 ? 308 HIS A CB  1 
ATOM   1095 C CG  . HIS A 1 308 ? 10.195  -23.700 9.517  1.00 24.47 ? 308 HIS A CG  1 
ATOM   1096 N ND1 . HIS A 1 308 ? 10.084  -22.683 8.596  1.00 26.03 ? 308 HIS A ND1 1 
ATOM   1097 C CD2 . HIS A 1 308 ? 8.988   -24.297 9.660  1.00 24.82 ? 308 HIS A CD2 1 
ATOM   1098 C CE1 . HIS A 1 308 ? 8.828   -22.711 8.179  1.00 26.12 ? 308 HIS A CE1 1 
ATOM   1099 N NE2 . HIS A 1 308 ? 8.132   -23.667 8.792  1.00 25.83 ? 308 HIS A NE2 1 
ATOM   1100 N N   . SER A 1 309 ? 14.661  -24.105 9.832  1.00 27.64 ? 309 SER A N   1 
ATOM   1101 C CA  . SER A 1 309 ? 15.949  -24.009 10.516 1.00 28.76 ? 309 SER A CA  1 
ATOM   1102 C C   . SER A 1 309 ? 16.045  -22.759 11.407 1.00 29.05 ? 309 SER A C   1 
ATOM   1103 O O   . SER A 1 309 ? 17.055  -22.563 12.062 1.00 29.95 ? 309 SER A O   1 
ATOM   1104 C CB  . SER A 1 309 ? 17.092  -24.021 9.511  1.00 30.38 ? 309 SER A CB  1 
ATOM   1105 O OG  . SER A 1 309 ? 16.923  -22.954 8.596  1.00 33.63 ? 309 SER A OG  1 
ATOM   1106 N N   . GLN A 1 310 ? 15.049  -21.880 11.366 1.00 28.54 ? 310 GLN A N   1 
ATOM   1107 C CA  . GLN A 1 310 ? 14.970  -20.675 12.182 1.00 28.50 ? 310 GLN A CA  1 
ATOM   1108 C C   . GLN A 1 310 ? 13.566  -20.636 12.811 1.00 28.55 ? 310 GLN A C   1 
ATOM   1109 O O   . GLN A 1 310 ? 12.736  -21.497 12.517 1.00 28.65 ? 310 GLN A O   1 
ATOM   1110 C CB  . GLN A 1 310 ? 15.259  -19.425 11.338 1.00 29.67 ? 310 GLN A CB  1 
ATOM   1111 C CG  . GLN A 1 310 ? 16.650  -19.415 10.682 1.00 34.31 ? 310 GLN A CG  1 
ATOM   1112 C CD  . GLN A 1 310 ? 17.779  -19.333 11.686 1.00 39.78 ? 310 GLN A CD  1 
ATOM   1113 O OE1 . GLN A 1 310 ? 17.640  -18.788 12.789 1.00 42.71 ? 310 GLN A OE1 1 
ATOM   1114 N NE2 . GLN A 1 310 ? 18.933  -19.866 11.336 1.00 40.22 ? 310 GLN A NE2 1 
ATOM   1115 N N   . GLU A 1 311 ? 13.296  -19.656 13.667 1.00 28.38 ? 311 GLU A N   1 
ATOM   1116 C CA  . GLU A 1 311 ? 12.032  -19.542 14.390 1.00 28.09 ? 311 GLU A CA  1 
ATOM   1117 C C   . GLU A 1 311 ? 10.765  -19.707 13.566 1.00 27.49 ? 311 GLU A C   1 
ATOM   1118 O O   . GLU A 1 311 ? 10.596  -19.070 12.533 1.00 27.87 ? 311 GLU A O   1 
ATOM   1119 C CB  . GLU A 1 311 ? 11.968  -18.205 15.148 1.00 30.33 ? 311 GLU A CB  1 
ATOM   1120 C CG  . GLU A 1 311 ? 10.737  -18.070 16.032 1.00 34.23 ? 311 GLU A CG  1 
ATOM   1121 C CD  . GLU A 1 311 ? 10.870  -17.188 17.260 1.00 37.12 ? 311 GLU A CD  1 
ATOM   1122 O OE1 . GLU A 1 311 ? 10.159  -17.455 18.255 1.00 33.77 ? 311 GLU A OE1 1 
ATOM   1123 O OE2 . GLU A 1 311 ? 11.678  -16.233 17.230 1.00 39.90 ? 311 GLU A OE2 1 
ATOM   1124 N N   . VAL A 1 312 ? 9.846   -20.525 14.062 1.00 26.16 ? 312 VAL A N   1 
ATOM   1125 C CA  . VAL A 1 312 ? 8.540   -20.676 13.451 1.00 25.53 ? 312 VAL A CA  1 
ATOM   1126 C C   . VAL A 1 312 ? 7.687   -19.562 14.030 1.00 24.77 ? 312 VAL A C   1 
ATOM   1127 O O   . VAL A 1 312 ? 7.280   -19.633 15.191 1.00 24.55 ? 312 VAL A O   1 
ATOM   1128 C CB  . VAL A 1 312 ? 7.934   -22.056 13.768 1.00 26.69 ? 312 VAL A CB  1 
ATOM   1129 C CG1 . VAL A 1 312 ? 6.568   -22.206 13.117 1.00 27.54 ? 312 VAL A CG1 1 
ATOM   1130 C CG2 . VAL A 1 312 ? 8.875   -23.168 13.336 1.00 27.21 ? 312 VAL A CG2 1 
ATOM   1131 N N   . CYS A 1 313 ? 7.431   -18.529 13.246 1.00 24.47 ? 313 CYS A N   1 
ATOM   1132 C CA  . CYS A 1 313 ? 6.658   -17.365 13.689 1.00 25.14 ? 313 CYS A CA  1 
ATOM   1133 C C   . CYS A 1 313 ? 5.189   -17.333 13.188 1.00 25.23 ? 313 CYS A C   1 
ATOM   1134 O O   . CYS A 1 313 ? 4.387   -16.524 13.659 1.00 24.97 ? 313 CYS A O   1 
ATOM   1135 C CB  . CYS A 1 313 ? 7.391   -16.089 13.313 1.00 26.01 ? 313 CYS A CB  1 
ATOM   1136 S SG  . CYS A 1 313 ? 8.038   -16.101 11.625 1.00 29.91 ? 313 CYS A SG  1 
ATOM   1137 N N   . GLY A 1 314 ? 4.866   -18.178 12.220 1.00 24.54 ? 314 GLY A N   1 
ATOM   1138 C CA  . GLY A 1 314 ? 3.512   -18.265 11.699 1.00 24.18 ? 314 GLY A CA  1 
ATOM   1139 C C   . GLY A 1 314 ? 3.106   -19.716 11.715 1.00 23.45 ? 314 GLY A C   1 
ATOM   1140 O O   . GLY A 1 314 ? 3.879   -20.574 11.276 1.00 22.79 ? 314 GLY A O   1 
ATOM   1141 N N   . LEU A 1 315 ? 1.933   -20.012 12.266 1.00 23.01 ? 315 LEU A N   1 
ATOM   1142 C CA  . LEU A 1 315 ? 1.471   -21.380 12.358 1.00 23.50 ? 315 LEU A CA  1 
ATOM   1143 C C   . LEU A 1 315 ? -0.031  -21.323 12.312 1.00 23.71 ? 315 LEU A C   1 
ATOM   1144 O O   . LEU A 1 315 ? -0.637  -20.645 13.133 1.00 23.79 ? 315 LEU A O   1 
ATOM   1145 C CB  . LEU A 1 315 ? 1.960   -21.992 13.672 1.00 23.75 ? 315 LEU A CB  1 
ATOM   1146 C CG  . LEU A 1 315 ? 1.829   -23.508 13.816 1.00 24.63 ? 315 LEU A CG  1 
ATOM   1147 C CD1 . LEU A 1 315 ? 2.603   -24.233 12.732 1.00 25.15 ? 315 LEU A CD1 1 
ATOM   1148 C CD2 . LEU A 1 315 ? 2.342   -23.950 15.167 1.00 24.79 ? 315 LEU A CD2 1 
ATOM   1149 N N   . ARG A 1 316 ? -0.633  -21.966 11.307 1.00 23.12 ? 316 ARG A N   1 
ATOM   1150 C CA  . ARG A 1 316 ? -2.074  -21.897 11.138 1.00 22.69 ? 316 ARG A CA  1 
ATOM   1151 C C   . ARG A 1 316 ? -2.630  -23.127 10.476 1.00 22.56 ? 316 ARG A C   1 
ATOM   1152 O O   . ARG A 1 316 ? -2.316  -23.426 9.317  1.00 22.15 ? 316 ARG A O   1 
ATOM   1153 C CB  . ARG A 1 316 ? -2.458  -20.660 10.305 1.00 23.54 ? 316 ARG A CB  1 
ATOM   1154 C CG  . ARG A 1 316 ? -3.831  -20.091 10.641 1.00 26.87 ? 316 ARG A CG  1 
ATOM   1155 C CD  . ARG A 1 316 ? -3.793  -19.051 11.770 1.00 30.25 ? 316 ARG A CD  1 
ATOM   1156 N NE  . ARG A 1 316 ? -2.902  -17.952 11.420 1.00 32.05 ? 316 ARG A NE  1 
ATOM   1157 C CZ  . ARG A 1 316 ? -1.929  -17.485 12.190 1.00 34.77 ? 316 ARG A CZ  1 
ATOM   1158 N NH1 . ARG A 1 316 ? -1.780  -17.934 13.430 1.00 32.73 ? 316 ARG A NH1 1 
ATOM   1159 N NH2 . ARG A 1 316 ? -1.115  -16.538 11.737 1.00 35.92 ? 316 ARG A NH2 1 
ATOM   1160 N N   . TRP A 1 317 ? -3.498  -23.819 11.193 1.00 22.58 ? 317 TRP A N   1 
ATOM   1161 C CA  . TRP A 1 317 ? -4.213  -24.948 10.645 1.00 23.80 ? 317 TRP A CA  1 
ATOM   1162 C C   . TRP A 1 317 ? -5.287  -24.400 9.738  1.00 24.08 ? 317 TRP A C   1 
ATOM   1163 O O   . TRP A 1 317 ? -5.847  -23.325 9.998  1.00 23.35 ? 317 TRP A O   1 
ATOM   1164 C CB  . TRP A 1 317 ? -4.883  -25.745 11.751 1.00 24.57 ? 317 TRP A CB  1 
ATOM   1165 C CG  . TRP A 1 317 ? -4.011  -26.798 12.360 1.00 25.72 ? 317 TRP A CG  1 
ATOM   1166 C CD1 . TRP A 1 317 ? -3.349  -26.722 13.545 1.00 26.88 ? 317 TRP A CD1 1 
ATOM   1167 C CD2 . TRP A 1 317 ? -3.725  -28.098 11.821 1.00 26.21 ? 317 TRP A CD2 1 
ATOM   1168 N NE1 . TRP A 1 317 ? -2.711  -27.914 13.808 1.00 27.56 ? 317 TRP A NE1 1 
ATOM   1169 C CE2 . TRP A 1 317 ? -2.913  -28.771 12.757 1.00 27.22 ? 317 TRP A CE2 1 
ATOM   1170 C CE3 . TRP A 1 317 ? -4.133  -28.785 10.675 1.00 27.12 ? 317 TRP A CE3 1 
ATOM   1171 C CZ2 . TRP A 1 317 ? -2.489  -30.087 12.570 1.00 28.08 ? 317 TRP A CZ2 1 
ATOM   1172 C CZ3 . TRP A 1 317 ? -3.677  -30.077 10.469 1.00 28.23 ? 317 TRP A CZ3 1 
ATOM   1173 C CH2 . TRP A 1 317 ? -2.874  -30.718 11.412 1.00 28.43 ? 317 TRP A CH2 1 
ATOM   1174 N N   . ALA A 1 318 ? -5.555  -25.118 8.650  1.00 24.62 ? 318 ALA A N   1 
ATOM   1175 C CA  . ALA A 1 318 ? -6.623  -24.719 7.749  1.00 25.91 ? 318 ALA A CA  1 
ATOM   1176 C C   . ALA A 1 318 ? -7.964  -24.979 8.454  1.00 27.06 ? 318 ALA A C   1 
ATOM   1177 O O   . ALA A 1 318 ? -8.078  -25.908 9.244  1.00 26.23 ? 318 ALA A O   1 
ATOM   1178 C CB  . ALA A 1 318 ? -6.543  -25.520 6.466  1.00 25.54 ? 318 ALA A CB  1 
ATOM   1179 N N   . PRO A 1 319 ? -8.979  -24.147 8.199  1.00 28.78 ? 319 PRO A N   1 
ATOM   1180 C CA  . PRO A 1 319 ? -10.290 -24.363 8.824  1.00 29.86 ? 319 PRO A CA  1 
ATOM   1181 C C   . PRO A 1 319 ? -10.866 -25.762 8.616  1.00 30.84 ? 319 PRO A C   1 
ATOM   1182 O O   . PRO A 1 319 ? -11.555 -26.236 9.494  1.00 31.59 ? 319 PRO A O   1 
ATOM   1183 C CB  . PRO A 1 319 ? -11.162 -23.296 8.167  1.00 30.53 ? 319 PRO A CB  1 
ATOM   1184 C CG  . PRO A 1 319 ? -10.203 -22.212 7.816  1.00 30.79 ? 319 PRO A CG  1 
ATOM   1185 C CD  . PRO A 1 319 ? -8.986  -22.950 7.340  1.00 28.92 ? 319 PRO A CD  1 
ATOM   1186 N N   . ASP A 1 320 ? -10.540 -26.448 7.507  1.00 31.05 ? 320 ASP A N   1 
ATOM   1187 C CA  . ASP A 1 320 ? -11.026 -27.820 7.295  1.00 31.28 ? 320 ASP A CA  1 
ATOM   1188 C C   . ASP A 1 320 ? -10.130 -28.924 7.918  1.00 31.67 ? 320 ASP A C   1 
ATOM   1189 O O   . ASP A 1 320 ? -10.429 -30.113 7.788  1.00 32.08 ? 320 ASP A O   1 
ATOM   1190 C CB  . ASP A 1 320 ? -11.264 -28.089 5.816  1.00 31.85 ? 320 ASP A CB  1 
ATOM   1191 C CG  . ASP A 1 320 ? -10.023 -28.091 4.942  1.00 36.82 ? 320 ASP A CG  1 
ATOM   1192 O OD1 . ASP A 1 320 ? -8.908  -27.927 5.481  1.00 37.37 ? 320 ASP A OD1 1 
ATOM   1193 O OD2 . ASP A 1 320 ? -10.164 -28.269 3.720  1.00 39.42 ? 320 ASP A OD2 1 
ATOM   1194 N N   . GLY A 1 321 ? -9.013  -28.522 8.511  1.00 30.98 ? 321 GLY A N   1 
ATOM   1195 C CA  . GLY A 1 321 ? -8.068  -29.426 9.141  1.00 31.41 ? 321 GLY A CA  1 
ATOM   1196 C C   . GLY A 1 321 ? -7.252  -30.282 8.201  1.00 32.07 ? 321 GLY A C   1 
ATOM   1197 O O   . GLY A 1 321 ? -6.528  -31.151 8.663  1.00 32.60 ? 321 GLY A O   1 
ATOM   1198 N N   . ARG A 1 322 ? -7.361  -30.073 6.883  1.00 31.72 ? 322 ARG A N   1 
ATOM   1199 C CA  . ARG A 1 322 ? -6.637  -30.893 5.914  1.00 31.65 ? 322 ARG A CA  1 
ATOM   1200 C C   . ARG A 1 322 ? -5.167  -30.497 5.721  1.00 30.57 ? 322 ARG A C   1 
ATOM   1201 O O   . ARG A 1 322 ? -4.400  -31.266 5.149  1.00 31.03 ? 322 ARG A O   1 
ATOM   1202 C CB  . ARG A 1 322 ? -7.358  -30.869 4.572  1.00 33.76 ? 322 ARG A CB  1 
ATOM   1203 C CG  . ARG A 1 322 ? -8.759  -31.472 4.604  1.00 37.44 ? 322 ARG A CG  1 
ATOM   1204 C CD  . ARG A 1 322 ? -9.513  -31.320 3.277  1.00 41.60 ? 322 ARG A CD  1 
ATOM   1205 N NE  . ARG A 1 322 ? -8.703  -31.598 2.078  1.00 46.03 ? 322 ARG A NE  1 
ATOM   1206 C CZ  . ARG A 1 322 ? -8.239  -30.660 1.250  1.00 48.97 ? 322 ARG A CZ  1 
ATOM   1207 N NH1 . ARG A 1 322 ? -8.499  -29.376 1.476  1.00 48.95 ? 322 ARG A NH1 1 
ATOM   1208 N NH2 . ARG A 1 322 ? -7.520  -31.000 0.189  1.00 48.63 ? 322 ARG A NH2 1 
ATOM   1209 N N   . HIS A 1 323 ? -4.786  -29.292 6.129  1.00 28.98 ? 323 HIS A N   1 
ATOM   1210 C CA  . HIS A 1 323 ? -3.410  -28.819 5.988  1.00 28.54 ? 323 HIS A CA  1 
ATOM   1211 C C   . HIS A 1 323 ? -3.037  -27.921 7.162  1.00 27.79 ? 323 HIS A C   1 
ATOM   1212 O O   . HIS A 1 323 ? -3.894  -27.284 7.754  1.00 27.79 ? 323 HIS A O   1 
ATOM   1213 C CB  . HIS A 1 323 ? -3.243  -27.981 4.693  1.00 28.94 ? 323 HIS A CB  1 
ATOM   1214 C CG  . HIS A 1 323 ? -3.593  -28.688 3.423  1.00 30.39 ? 323 HIS A CG  1 
ATOM   1215 N ND1 . HIS A 1 323 ? -4.871  -28.639 2.889  1.00 31.72 ? 323 HIS A ND1 1 
ATOM   1216 C CD2 . HIS A 1 323 ? -2.804  -29.405 2.590  1.00 31.73 ? 323 HIS A CD2 1 
ATOM   1217 C CE1 . HIS A 1 323 ? -4.824  -29.347 1.773  1.00 32.15 ? 323 HIS A CE1 1 
ATOM   1218 N NE2 . HIS A 1 323 ? -3.603  -29.836 1.557  1.00 32.33 ? 323 HIS A NE2 1 
ATOM   1219 N N   . LEU A 1 324 ? -1.748  -27.841 7.469  1.00 27.20 ? 324 LEU A N   1 
ATOM   1220 C CA  . LEU A 1 324 ? -1.214  -26.939 8.493  1.00 26.32 ? 324 LEU A CA  1 
ATOM   1221 C C   . LEU A 1 324 ? -0.159  -26.127 7.791  1.00 25.51 ? 324 LEU A C   1 
ATOM   1222 O O   . LEU A 1 324 ? 0.751   -26.711 7.239  1.00 25.23 ? 324 LEU A O   1 
ATOM   1223 C CB  . LEU A 1 324 ? -0.543  -27.713 9.639  1.00 26.33 ? 324 LEU A CB  1 
ATOM   1224 C CG  . LEU A 1 324 ? 0.305   -26.887 10.625 1.00 27.83 ? 324 LEU A CG  1 
ATOM   1225 C CD1 . LEU A 1 324 ? -0.535  -25.843 11.346 1.00 27.86 ? 324 LEU A CD1 1 
ATOM   1226 C CD2 . LEU A 1 324 ? 0.992   -27.775 11.638 1.00 28.94 ? 324 LEU A CD2 1 
ATOM   1227 N N   . ALA A 1 325 ? -0.231  -24.799 7.866  1.00 25.19 ? 325 ALA A N   1 
ATOM   1228 C CA  . ALA A 1 325 ? 0.778   -23.952 7.257  1.00 25.18 ? 325 ALA A CA  1 
ATOM   1229 C C   . ALA A 1 325 ? 1.692   -23.402 8.321  1.00 24.14 ? 325 ALA A C   1 
ATOM   1230 O O   . ALA A 1 325 ? 1.247   -23.119 9.429  1.00 23.64 ? 325 ALA A O   1 
ATOM   1231 C CB  . ALA A 1 325 ? 0.124   -22.810 6.495  1.00 25.80 ? 325 ALA A CB  1 
ATOM   1232 N N   . SER A 1 326 ? 2.978   -23.267 7.990  1.00 22.76 ? 326 SER A N   1 
ATOM   1233 C CA  . SER A 1 326 ? 3.933   -22.677 8.902  1.00 22.54 ? 326 SER A CA  1 
ATOM   1234 C C   . SER A 1 326 ? 4.844   -21.744 8.164  1.00 23.51 ? 326 SER A C   1 
ATOM   1235 O O   . SER A 1 326 ? 5.222   -22.008 7.042  1.00 24.09 ? 326 SER A O   1 
ATOM   1236 C CB  . SER A 1 326 ? 4.753   -23.730 9.626  1.00 22.79 ? 326 SER A CB  1 
ATOM   1237 O OG  . SER A 1 326 ? 5.597   -24.436 8.734  1.00 24.18 ? 326 SER A OG  1 
ATOM   1238 N N   . GLY A 1 327 ? 5.151   -20.637 8.781  1.00 23.57 ? 327 GLY A N   1 
ATOM   1239 C CA  . GLY A 1 327 ? 6.057   -19.650 8.244  1.00 24.91 ? 327 GLY A CA  1 
ATOM   1240 C C   . GLY A 1 327 ? 7.190   -19.453 9.223  1.00 26.18 ? 327 GLY A C   1 
ATOM   1241 O O   . GLY A 1 327 ? 6.980   -19.490 10.443 1.00 26.44 ? 327 GLY A O   1 
ATOM   1242 N N   . GLY A 1 328 ? 8.386   -19.259 8.699  1.00 26.32 ? 328 GLY A N   1 
ATOM   1243 C CA  . GLY A 1 328 ? 9.544   -19.097 9.551  1.00 27.20 ? 328 GLY A CA  1 
ATOM   1244 C C   . GLY A 1 328 ? 10.436  -17.915 9.278  1.00 28.35 ? 328 GLY A C   1 
ATOM   1245 O O   . GLY A 1 328 ? 10.349  -17.271 8.235  1.00 29.19 ? 328 GLY A O   1 
ATOM   1246 N N   . ASN A 1 329 ? 11.333  -17.654 10.226 1.00 28.31 ? 329 ASN A N   1 
ATOM   1247 C CA  . ASN A 1 329 ? 12.379  -16.651 10.076 1.00 28.59 ? 329 ASN A CA  1 
ATOM   1248 C C   . ASN A 1 329 ? 13.483  -17.165 9.114  1.00 28.91 ? 329 ASN A C   1 
ATOM   1249 O O   . ASN A 1 329 ? 14.463  -16.478 8.900  1.00 29.99 ? 329 ASN A O   1 
ATOM   1250 C CB  . ASN A 1 329 ? 12.958  -16.279 11.444 1.00 29.08 ? 329 ASN A CB  1 
ATOM   1251 C CG  . ASN A 1 329 ? 13.854  -15.075 11.425 1.00 31.48 ? 329 ASN A CG  1 
ATOM   1252 O OD1 . ASN A 1 329 ? 13.628  -14.112 10.686 1.00 33.00 ? 329 ASN A OD1 1 
ATOM   1253 N ND2 . ASN A 1 329 ? 14.903  -15.110 12.230 1.00 31.76 ? 329 ASN A ND2 1 
ATOM   1254 N N   . ASP A 1 330 ? 13.336  -18.368 8.548  1.00 28.61 ? 330 ASP A N   1 
ATOM   1255 C CA  . ASP A 1 330 ? 14.239  -18.892 7.522  1.00 29.27 ? 330 ASP A CA  1 
ATOM   1256 C C   . ASP A 1 330 ? 13.668  -18.599 6.106  1.00 29.76 ? 330 ASP A C   1 
ATOM   1257 O O   . ASP A 1 330 ? 14.162  -19.154 5.127  1.00 30.11 ? 330 ASP A O   1 
ATOM   1258 C CB  . ASP A 1 330 ? 14.471  -20.399 7.701  1.00 29.87 ? 330 ASP A CB  1 
ATOM   1259 C CG  . ASP A 1 330 ? 13.203  -21.241 7.767  1.00 33.27 ? 330 ASP A CG  1 
ATOM   1260 O OD1 . ASP A 1 330 ? 12.088  -20.659 7.784  1.00 33.36 ? 330 ASP A OD1 1 
ATOM   1261 O OD2 . ASP A 1 330 ? 13.322  -22.476 7.803  1.00 35.13 ? 330 ASP A OD2 1 
ATOM   1262 N N   . ASN A 1 331 ? 12.631  -17.727 6.017  1.00 29.45 ? 331 ASN A N   1 
ATOM   1263 C CA  . ASN A 1 331 ? 11.985  -17.300 4.792  1.00 29.65 ? 331 ASN A CA  1 
ATOM   1264 C C   . ASN A 1 331 ? 11.217  -18.416 4.114  1.00 28.48 ? 331 ASN A C   1 
ATOM   1265 O O   . ASN A 1 331 ? 10.981  -18.330 2.906  1.00 28.89 ? 331 ASN A O   1 
ATOM   1266 C CB  . ASN A 1 331 ? 13.015  -16.679 3.825  1.00 32.13 ? 331 ASN A CB  1 
ATOM   1267 C CG  . ASN A 1 331 ? 13.897  -15.612 4.439  1.00 36.96 ? 331 ASN A CG  1 
ATOM   1268 O OD1 . ASN A 1 331 ? 13.672  -15.139 5.542  1.00 37.89 ? 331 ASN A OD1 1 
ATOM   1269 N ND2 . ASN A 1 331 ? 14.888  -15.158 3.689  1.00 39.65 ? 331 ASN A ND2 1 
ATOM   1270 N N   . LEU A 1 332 ? 10.828  -19.462 4.860  1.00 26.58 ? 332 LEU A N   1 
ATOM   1271 C CA  . LEU A 1 332 ? 10.104  -20.561 4.259  1.00 25.36 ? 332 LEU A CA  1 
ATOM   1272 C C   . LEU A 1 332 ? 8.664   -20.593 4.666  1.00 24.65 ? 332 LEU A C   1 
ATOM   1273 O O   . LEU A 1 332 ? 8.330   -20.239 5.789  1.00 24.57 ? 332 LEU A O   1 
ATOM   1274 C CB  . LEU A 1 332 ? 10.729  -21.899 4.669  1.00 24.85 ? 332 LEU A CB  1 
ATOM   1275 C CG  . LEU A 1 332 ? 12.137  -22.198 4.208  1.00 25.69 ? 332 LEU A CG  1 
ATOM   1276 C CD1 . LEU A 1 332 ? 12.570  -23.543 4.718  1.00 26.43 ? 332 LEU A CD1 1 
ATOM   1277 C CD2 . LEU A 1 332 ? 12.217  -22.211 2.728  1.00 25.43 ? 332 LEU A CD2 1 
ATOM   1278 N N   . VAL A 1 333 ? 7.819   -21.113 3.776  1.00 23.42 ? 333 VAL A N   1 
ATOM   1279 C CA  . VAL A 1 333 ? 6.460   -21.454 4.123  1.00 23.22 ? 333 VAL A CA  1 
ATOM   1280 C C   . VAL A 1 333 ? 6.368   -22.959 3.885  1.00 23.31 ? 333 VAL A C   1 
ATOM   1281 O O   . VAL A 1 333 ? 6.701   -23.427 2.797  1.00 23.13 ? 333 VAL A O   1 
ATOM   1282 C CB  . VAL A 1 333 ? 5.375   -20.722 3.315  1.00 22.90 ? 333 VAL A CB  1 
ATOM   1283 C CG1 . VAL A 1 333 ? 3.997   -21.298 3.612  1.00 22.65 ? 333 VAL A CG1 1 
ATOM   1284 C CG2 . VAL A 1 333 ? 5.400   -19.232 3.608  1.00 22.66 ? 333 VAL A CG2 1 
ATOM   1285 N N   . ASN A 1 334 ? 5.952   -23.716 4.885  1.00 22.45 ? 334 ASN A N   1 
ATOM   1286 C CA  . ASN A 1 334 ? 5.727   -25.137 4.710  1.00 22.50 ? 334 ASN A CA  1 
ATOM   1287 C C   . ASN A 1 334 ? 4.242   -25.399 4.820  1.00 23.36 ? 334 ASN A C   1 
ATOM   1288 O O   . ASN A 1 334 ? 3.553   -24.795 5.648  1.00 22.84 ? 334 ASN A O   1 
ATOM   1289 C CB  . ASN A 1 334 ? 6.476   -25.950 5.745  1.00 22.68 ? 334 ASN A CB  1 
ATOM   1290 C CG  . ASN A 1 334 ? 7.963   -25.999 5.478  1.00 23.69 ? 334 ASN A CG  1 
ATOM   1291 O OD1 . ASN A 1 334 ? 8.418   -26.456 4.422  1.00 24.45 ? 334 ASN A OD1 1 
ATOM   1292 N ND2 . ASN A 1 334 ? 8.748   -25.544 6.431  1.00 22.35 ? 334 ASN A ND2 1 
ATOM   1293 N N   . VAL A 1 335 ? 3.736   -26.280 3.966  1.00 23.74 ? 335 VAL A N   1 
ATOM   1294 C CA  . VAL A 1 335 ? 2.354   -26.710 4.072  1.00 24.70 ? 335 VAL A CA  1 
ATOM   1295 C C   . VAL A 1 335 ? 2.457   -28.176 4.414  1.00 24.49 ? 335 VAL A C   1 
ATOM   1296 O O   . VAL A 1 335 ? 3.015   -28.954 3.657  1.00 23.79 ? 335 VAL A O   1 
ATOM   1297 C CB  . VAL A 1 335 ? 1.502   -26.455 2.818  1.00 25.82 ? 335 VAL A CB  1 
ATOM   1298 C CG1 . VAL A 1 335 ? 0.088   -26.983 3.034  1.00 26.20 ? 335 VAL A CG1 1 
ATOM   1299 C CG2 . VAL A 1 335 ? 1.475   -24.961 2.486  1.00 25.98 ? 335 VAL A CG2 1 
ATOM   1300 N N   . TRP A 1 336 ? 1.987   -28.529 5.577  1.00 24.18 ? 336 TRP A N   1 
ATOM   1301 C CA  . TRP A 1 336 ? 2.082   -29.859 6.109  1.00 25.32 ? 336 TRP A CA  1 
ATOM   1302 C C   . TRP A 1 336 ? 0.785   -30.604 5.923  1.00 28.30 ? 336 TRP A C   1 
ATOM   1303 O O   . TRP A 1 336 ? -0.290  -30.008 6.019  1.00 28.04 ? 336 TRP A O   1 
ATOM   1304 C CB  . TRP A 1 336 ? 2.373   -29.755 7.634  1.00 24.21 ? 336 TRP A CB  1 
ATOM   1305 C CG  . TRP A 1 336 ? 3.606   -28.972 7.963  1.00 23.91 ? 336 TRP A CG  1 
ATOM   1306 C CD1 . TRP A 1 336 ? 3.683   -27.637 8.233  1.00 24.44 ? 336 TRP A CD1 1 
ATOM   1307 C CD2 . TRP A 1 336 ? 4.943   -29.479 8.059  1.00 23.81 ? 336 TRP A CD2 1 
ATOM   1308 N NE1 . TRP A 1 336 ? 4.984   -27.284 8.499  1.00 24.65 ? 336 TRP A NE1 1 
ATOM   1309 C CE2 . TRP A 1 336 ? 5.777   -28.400 8.408  1.00 24.39 ? 336 TRP A CE2 1 
ATOM   1310 C CE3 . TRP A 1 336 ? 5.512   -30.748 7.912  1.00 24.59 ? 336 TRP A CE3 1 
ATOM   1311 C CZ2 . TRP A 1 336 ? 7.147   -28.551 8.613  1.00 25.07 ? 336 TRP A CZ2 1 
ATOM   1312 C CZ3 . TRP A 1 336 ? 6.873   -30.894 8.111  1.00 25.64 ? 336 TRP A CZ3 1 
ATOM   1313 C CH2 . TRP A 1 336 ? 7.676   -29.799 8.433  1.00 25.56 ? 336 TRP A CH2 1 
ATOM   1314 N N   . PRO A 1 337 ? 0.859   -31.939 5.790  1.00 31.16 ? 337 PRO A N   1 
ATOM   1315 C CA  . PRO A 1 337 ? -0.375  -32.736 5.795  1.00 33.26 ? 337 PRO A CA  1 
ATOM   1316 C C   . PRO A 1 337 ? -0.937  -32.817 7.219  1.00 35.85 ? 337 PRO A C   1 
ATOM   1317 O O   . PRO A 1 337 ? -0.285  -32.422 8.199  1.00 35.66 ? 337 PRO A O   1 
ATOM   1318 C CB  . PRO A 1 337 ? 0.107   -34.107 5.341  1.00 33.85 ? 337 PRO A CB  1 
ATOM   1319 C CG  . PRO A 1 337 ? 1.496   -34.190 5.884  1.00 34.02 ? 337 PRO A CG  1 
ATOM   1320 C CD  . PRO A 1 337 ? 2.056   -32.799 5.752  1.00 31.65 ? 337 PRO A CD  1 
ATOM   1321 N N   . SER A 1 338 ? -2.171  -33.291 7.338  1.00 37.84 ? 338 SER A N   1 
ATOM   1322 C CA  . SER A 1 338 ? -2.810  -33.435 8.650  1.00 39.85 ? 338 SER A CA  1 
ATOM   1323 C C   . SER A 1 338 ? -2.388  -34.713 9.375  1.00 42.20 ? 338 SER A C   1 
ATOM   1324 O O   . SER A 1 338 ? -2.649  -34.843 10.564 1.00 42.76 ? 338 SER A O   1 
ATOM   1325 C CB  . SER A 1 338 ? -4.324  -33.414 8.506  1.00 41.30 ? 338 SER A CB  1 
ATOM   1326 O OG  . SER A 1 338 ? -4.768  -34.535 7.762  1.00 43.94 ? 338 SER A OG  1 
ATOM   1327 N N   . ALA A 1 339 ? -1.755  -35.664 8.669  1.00 43.61 ? 339 ALA A N   1 
ATOM   1328 C CA  . ALA A 1 339 ? -1.295  -36.931 9.230  1.00 45.39 ? 339 ALA A CA  1 
ATOM   1329 C C   . ALA A 1 339 ? -0.034  -37.391 8.499  1.00 46.91 ? 339 ALA A C   1 
ATOM   1330 O O   . ALA A 1 339 ? 0.179   -37.032 7.338  1.00 47.03 ? 339 ALA A O   1 
ATOM   1331 C CB  . ALA A 1 339 ? -2.390  -37.980 9.084  1.00 45.46 ? 339 ALA A CB  1 
ATOM   1332 N N   . PRO A 1 340 ? 0.814   -38.201 9.151  1.00 47.86 ? 340 PRO A N   1 
ATOM   1333 C CA  . PRO A 1 340 ? 2.017   -38.682 8.462  1.00 48.58 ? 340 PRO A CA  1 
ATOM   1334 C C   . PRO A 1 340 ? 1.724   -39.875 7.544  1.00 49.83 ? 340 PRO A C   1 
ATOM   1335 O O   . PRO A 1 340 ? 0.695   -40.552 7.668  1.00 50.44 ? 340 PRO A O   1 
ATOM   1336 C CB  . PRO A 1 340 ? 2.968   -39.018 9.615  1.00 49.05 ? 340 PRO A CB  1 
ATOM   1337 C CG  . PRO A 1 340 ? 2.082   -39.342 10.775 1.00 49.33 ? 340 PRO A CG  1 
ATOM   1338 C CD  . PRO A 1 340 ? 0.719   -38.737 10.527 1.00 47.67 ? 340 PRO A CD  1 
ATOM   1339 N N   . GLY A 1 344 ? 6.273   -40.114 5.975  1.00 45.35 ? 344 GLY A N   1 
ATOM   1340 C CA  . GLY A 1 344 ? 6.298   -39.568 7.324  1.00 45.61 ? 344 GLY A CA  1 
ATOM   1341 C C   . GLY A 1 344 ? 5.903   -38.111 7.377  1.00 45.28 ? 344 GLY A C   1 
ATOM   1342 O O   . GLY A 1 344 ? 5.083   -37.657 6.572  1.00 45.63 ? 344 GLY A O   1 
ATOM   1343 N N   . TRP A 1 345 ? 6.499   -37.359 8.310  1.00 44.42 ? 345 TRP A N   1 
ATOM   1344 C CA  . TRP A 1 345 ? 6.197   -35.932 8.466  1.00 43.93 ? 345 TRP A CA  1 
ATOM   1345 C C   . TRP A 1 345 ? 7.007   -35.022 7.547  1.00 43.56 ? 345 TRP A C   1 
ATOM   1346 O O   . TRP A 1 345 ? 7.932   -34.339 7.989  1.00 43.91 ? 345 TRP A O   1 
ATOM   1347 C CB  . TRP A 1 345 ? 6.357   -35.489 9.921  1.00 43.44 ? 345 TRP A CB  1 
ATOM   1348 C CG  . TRP A 1 345 ? 5.213   -35.865 10.801 1.00 43.49 ? 345 TRP A CG  1 
ATOM   1349 C CD1 . TRP A 1 345 ? 5.247   -36.711 11.870 1.00 44.56 ? 345 TRP A CD1 1 
ATOM   1350 C CD2 . TRP A 1 345 ? 3.865   -35.383 10.712 1.00 43.14 ? 345 TRP A CD2 1 
ATOM   1351 N NE1 . TRP A 1 345 ? 4.003   -36.784 12.454 1.00 44.68 ? 345 TRP A NE1 1 
ATOM   1352 C CE2 . TRP A 1 345 ? 3.139   -35.970 11.768 1.00 44.00 ? 345 TRP A CE2 1 
ATOM   1353 C CE3 . TRP A 1 345 ? 3.201   -34.517 9.842  1.00 43.35 ? 345 TRP A CE3 1 
ATOM   1354 C CZ2 . TRP A 1 345 ? 1.788   -35.710 11.976 1.00 44.22 ? 345 TRP A CZ2 1 
ATOM   1355 C CZ3 . TRP A 1 345 ? 1.864   -34.266 10.051 1.00 44.04 ? 345 TRP A CZ3 1 
ATOM   1356 C CH2 . TRP A 1 345 ? 1.169   -34.868 11.099 1.00 44.08 ? 345 TRP A CH2 1 
ATOM   1357 N N   . VAL A 1 346 ? 6.646   -35.000 6.271  1.00 42.51 ? 346 VAL A N   1 
ATOM   1358 C CA  . VAL A 1 346 ? 7.318   -34.172 5.290  1.00 41.63 ? 346 VAL A CA  1 
ATOM   1359 C C   . VAL A 1 346 ? 6.307   -33.185 4.699  1.00 39.84 ? 346 VAL A C   1 
ATOM   1360 O O   . VAL A 1 346 ? 5.144   -33.539 4.494  1.00 40.11 ? 346 VAL A O   1 
ATOM   1361 C CB  . VAL A 1 346 ? 7.949   -35.100 4.225  1.00 42.75 ? 346 VAL A CB  1 
ATOM   1362 C CG1 . VAL A 1 346 ? 8.260   -34.372 2.921  1.00 43.19 ? 346 VAL A CG1 1 
ATOM   1363 C CG2 . VAL A 1 346 ? 9.194   -35.785 4.784  1.00 43.35 ? 346 VAL A CG2 1 
ATOM   1364 N N   . PRO A 1 347 ? 6.716   -31.933 4.443  1.00 37.59 ? 347 PRO A N   1 
ATOM   1365 C CA  . PRO A 1 347 ? 5.777   -30.974 3.853  1.00 35.80 ? 347 PRO A CA  1 
ATOM   1366 C C   . PRO A 1 347 ? 5.251   -31.394 2.481  1.00 33.85 ? 347 PRO A C   1 
ATOM   1367 O O   . PRO A 1 347 ? 5.977   -31.958 1.678  1.00 33.24 ? 347 PRO A O   1 
ATOM   1368 C CB  . PRO A 1 347 ? 6.621   -29.703 3.693  1.00 36.65 ? 347 PRO A CB  1 
ATOM   1369 C CG  . PRO A 1 347 ? 7.763   -29.866 4.601  1.00 37.64 ? 347 PRO A CG  1 
ATOM   1370 C CD  . PRO A 1 347 ? 8.043   -31.331 4.672  1.00 36.62 ? 347 PRO A CD  1 
ATOM   1371 N N   . LEU A 1 348 ? 3.982   -31.098 2.227  1.00 32.58 ? 348 LEU A N   1 
ATOM   1372 C CA  . LEU A 1 348 ? 3.326   -31.248 0.936  1.00 32.00 ? 348 LEU A CA  1 
ATOM   1373 C C   . LEU A 1 348 ? 3.810   -30.121 -0.010 1.00 31.38 ? 348 LEU A C   1 
ATOM   1374 O O   . LEU A 1 348 ? 3.819   -30.296 -1.223 1.00 31.41 ? 348 LEU A O   1 
ATOM   1375 C CB  . LEU A 1 348 ? 1.813   -31.118 1.120  1.00 31.73 ? 348 LEU A CB  1 
ATOM   1376 C CG  . LEU A 1 348 ? 1.161   -32.236 1.878  1.00 33.01 ? 348 LEU A CG  1 
ATOM   1377 C CD1 . LEU A 1 348 ? -0.287  -31.928 2.125  1.00 32.85 ? 348 LEU A CD1 1 
ATOM   1378 C CD2 . LEU A 1 348 ? 1.302   -33.565 1.125  1.00 34.48 ? 348 LEU A CD2 1 
ATOM   1379 N N   . GLN A 1 349 ? 4.118   -28.933 0.552  1.00 30.28 ? 349 GLN A N   1 
ATOM   1380 C CA  . GLN A 1 349 ? 4.644   -27.802 -0.193 1.00 29.60 ? 349 GLN A CA  1 
ATOM   1381 C C   . GLN A 1 349 ? 5.656   -27.074 0.657  1.00 29.24 ? 349 GLN A C   1 
ATOM   1382 O O   . GLN A 1 349 ? 5.504   -26.980 1.868  1.00 28.92 ? 349 GLN A O   1 
ATOM   1383 C CB  . GLN A 1 349 ? 3.563   -26.781 -0.577 1.00 29.62 ? 349 GLN A CB  1 
ATOM   1384 C CG  . GLN A 1 349 ? 2.412   -27.316 -1.395 1.00 31.82 ? 349 GLN A CG  1 
ATOM   1385 C CD  . GLN A 1 349 ? 2.770   -27.637 -2.831 1.00 32.61 ? 349 GLN A CD  1 
ATOM   1386 O OE1 . GLN A 1 349 ? 3.895   -27.417 -3.303 1.00 32.24 ? 349 GLN A OE1 1 
ATOM   1387 N NE2 . GLN A 1 349 ? 1.808   -28.177 -3.548 1.00 32.24 ? 349 GLN A NE2 1 
ATOM   1388 N N   . THR A 1 350 ? 6.686   -26.534 0.009  1.00 28.68 ? 350 THR A N   1 
ATOM   1389 C CA  . THR A 1 350 ? 7.659   -25.676 0.650  1.00 27.47 ? 350 THR A CA  1 
ATOM   1390 C C   . THR A 1 350 ? 7.866   -24.517 -0.281 1.00 27.11 ? 350 THR A C   1 
ATOM   1391 O O   . THR A 1 350 ? 8.499   -24.652 -1.326 1.00 27.26 ? 350 THR A O   1 
ATOM   1392 C CB  . THR A 1 350 ? 8.944   -26.378 0.992  1.00 28.11 ? 350 THR A CB  1 
ATOM   1393 O OG1 . THR A 1 350 ? 8.645   -27.396 1.934  1.00 28.50 ? 350 THR A OG1 1 
ATOM   1394 C CG2 . THR A 1 350 ? 9.943   -25.432 1.626  1.00 28.80 ? 350 THR A CG2 1 
ATOM   1395 N N   . PHE A 1 351 ? 7.296   -23.380 0.076  1.00 26.31 ? 351 PHE A N   1 
ATOM   1396 C CA  . PHE A 1 351 ? 7.406   -22.182 -0.712 1.00 25.56 ? 351 PHE A CA  1 
ATOM   1397 C C   . PHE A 1 351 ? 8.591   -21.378 -0.220 1.00 25.04 ? 351 PHE A C   1 
ATOM   1398 O O   . PHE A 1 351 ? 8.628   -20.961 0.948  1.00 24.44 ? 351 PHE A O   1 
ATOM   1399 C CB  . PHE A 1 351 ? 6.121   -21.383 -0.585 1.00 24.84 ? 351 PHE A CB  1 
ATOM   1400 C CG  . PHE A 1 351 ? 4.887   -22.141 -1.000 1.00 25.01 ? 351 PHE A CG  1 
ATOM   1401 C CD1 . PHE A 1 351 ? 4.866   -22.881 -2.173 1.00 25.33 ? 351 PHE A CD1 1 
ATOM   1402 C CD2 . PHE A 1 351 ? 3.735   -22.091 -0.228 1.00 25.80 ? 351 PHE A CD2 1 
ATOM   1403 C CE1 . PHE A 1 351 ? 3.718   -23.550 -2.566 1.00 26.23 ? 351 PHE A CE1 1 
ATOM   1404 C CE2 . PHE A 1 351 ? 2.591   -22.762 -0.617 1.00 26.17 ? 351 PHE A CE2 1 
ATOM   1405 C CZ  . PHE A 1 351 ? 2.582   -23.477 -1.787 1.00 26.05 ? 351 PHE A CZ  1 
ATOM   1406 N N   . THR A 1 352 ? 9.552   -21.146 -1.112 1.00 24.50 ? 352 THR A N   1 
ATOM   1407 C CA  . THR A 1 352 ? 10.773  -20.397 -0.811 1.00 25.83 ? 352 THR A CA  1 
ATOM   1408 C C   . THR A 1 352 ? 10.781  -18.941 -1.361 1.00 26.02 ? 352 THR A C   1 
ATOM   1409 O O   . THR A 1 352 ? 11.774  -18.239 -1.201 1.00 26.35 ? 352 THR A O   1 
ATOM   1410 C CB  . THR A 1 352 ? 11.942  -21.135 -1.463 1.00 27.72 ? 352 THR A CB  1 
ATOM   1411 O OG1 . THR A 1 352 ? 11.720  -21.147 -2.882 1.00 29.43 ? 352 THR A OG1 1 
ATOM   1412 C CG2 . THR A 1 352 ? 12.069  -22.564 -0.952 1.00 28.39 ? 352 THR A CG2 1 
ATOM   1413 N N   . GLN A 1 353 ? 9.722   -18.525 -2.045 1.00 25.52 ? 353 GLN A N   1 
ATOM   1414 C CA  . GLN A 1 353 ? 9.635   -17.252 -2.761 1.00 25.36 ? 353 GLN A CA  1 
ATOM   1415 C C   . GLN A 1 353 ? 9.672   -16.007 -1.875 1.00 25.37 ? 353 GLN A C   1 
ATOM   1416 O O   . GLN A 1 353 ? 10.106  -14.964 -2.357 1.00 25.07 ? 353 GLN A O   1 
ATOM   1417 C CB  . GLN A 1 353 ? 8.406   -17.224 -3.685 1.00 25.47 ? 353 GLN A CB  1 
ATOM   1418 C CG  . GLN A 1 353 ? 8.435   -18.313 -4.746 1.00 27.16 ? 353 GLN A CG  1 
ATOM   1419 C CD  . GLN A 1 353 ? 7.770   -19.622 -4.354 1.00 31.02 ? 353 GLN A CD  1 
ATOM   1420 O OE1 . GLN A 1 353 ? 7.684   -20.004 -3.194 1.00 31.08 ? 353 GLN A OE1 1 
ATOM   1421 N NE2 . GLN A 1 353 ? 7.279   -20.353 -5.328 1.00 33.30 ? 353 GLN A NE2 1 
ATOM   1422 N N   . HIS A 1 354 ? 9.237   -16.097 -0.613 1.00 25.64 ? 354 HIS A N   1 
ATOM   1423 C CA  . HIS A 1 354 ? 9.352   -14.948 0.280  1.00 26.17 ? 354 HIS A CA  1 
ATOM   1424 C C   . HIS A 1 354 ? 10.841  -14.742 0.611  1.00 27.00 ? 354 HIS A C   1 
ATOM   1425 O O   . HIS A 1 354 ? 11.565  -15.694 0.890  1.00 27.01 ? 354 HIS A O   1 
ATOM   1426 C CB  . HIS A 1 354 ? 8.544   -15.124 1.563  1.00 25.86 ? 354 HIS A CB  1 
ATOM   1427 C CG  . HIS A 1 354 ? 7.064   -14.980 1.390  1.00 27.33 ? 354 HIS A CG  1 
ATOM   1428 N ND1 . HIS A 1 354 ? 6.468   -13.738 1.188  1.00 29.44 ? 354 HIS A ND1 1 
ATOM   1429 C CD2 . HIS A 1 354 ? 6.093   -15.917 1.468  1.00 27.52 ? 354 HIS A CD2 1 
ATOM   1430 C CE1 . HIS A 1 354 ? 5.161   -13.971 1.143  1.00 29.26 ? 354 HIS A CE1 1 
ATOM   1431 N NE2 . HIS A 1 354 ? 4.895   -15.268 1.285  1.00 28.51 ? 354 HIS A NE2 1 
ATOM   1432 N N   . GLN A 1 355 ? 11.300  -13.513 0.515  1.00 27.72 ? 355 GLN A N   1 
ATOM   1433 C CA  . GLN A 1 355 ? 12.688  -13.165 0.772  1.00 29.01 ? 355 GLN A CA  1 
ATOM   1434 C C   . GLN A 1 355 ? 12.764  -12.446 2.112  1.00 29.16 ? 355 GLN A C   1 
ATOM   1435 O O   . GLN A 1 355 ? 13.276  -11.344 2.204  1.00 29.93 ? 355 GLN A O   1 
ATOM   1436 C CB  . GLN A 1 355 ? 13.207  -12.273 -0.364 1.00 31.20 ? 355 GLN A CB  1 
ATOM   1437 C CG  . GLN A 1 355 ? 12.950  -12.827 -1.769 1.00 36.81 ? 355 GLN A CG  1 
ATOM   1438 C CD  . GLN A 1 355 ? 13.773  -14.057 -2.079 1.00 43.92 ? 355 GLN A CD  1 
ATOM   1439 O OE1 . GLN A 1 355 ? 14.995  -13.988 -2.317 1.00 45.19 ? 355 GLN A OE1 1 
ATOM   1440 N NE2 . GLN A 1 355 ? 13.117  -15.211 -2.120 1.00 44.99 ? 355 GLN A NE2 1 
ATOM   1441 N N   . GLY A 1 356 ? 12.139  -13.025 3.120  1.00 28.60 ? 356 GLY A N   1 
ATOM   1442 C CA  . GLY A 1 356 ? 12.091  -12.473 4.465  1.00 28.01 ? 356 GLY A CA  1 
ATOM   1443 C C   . GLY A 1 356 ? 11.220  -13.322 5.363  1.00 27.75 ? 356 GLY A C   1 
ATOM   1444 O O   . GLY A 1 356 ? 10.489  -14.192 4.885  1.00 28.10 ? 356 GLY A O   1 
ATOM   1445 N N   . ALA A 1 357 ? 11.267  -13.084 6.671  1.00 26.56 ? 357 ALA A N   1 
ATOM   1446 C CA  . ALA A 1 357 ? 10.484  -13.872 7.629  1.00 26.44 ? 357 ALA A CA  1 
ATOM   1447 C C   . ALA A 1 357 ? 9.004   -13.959 7.269  1.00 26.11 ? 357 ALA A C   1 
ATOM   1448 O O   . ALA A 1 357 ? 8.458   -13.000 6.733  1.00 26.44 ? 357 ALA A O   1 
ATOM   1449 C CB  . ALA A 1 357 ? 10.640  -13.309 9.025  1.00 26.41 ? 357 ALA A CB  1 
ATOM   1450 N N   . VAL A 1 358 ? 8.398   -15.126 7.447  1.00 24.75 ? 358 VAL A N   1 
ATOM   1451 C CA  . VAL A 1 358 ? 6.993   -15.288 7.122  1.00 24.40 ? 358 VAL A CA  1 
ATOM   1452 C C   . VAL A 1 358 ? 6.178   -15.475 8.377  1.00 24.94 ? 358 VAL A C   1 
ATOM   1453 O O   . VAL A 1 358 ? 6.032   -16.599 8.864  1.00 25.58 ? 358 VAL A O   1 
ATOM   1454 C CB  . VAL A 1 358 ? 6.714   -16.405 6.103  1.00 24.22 ? 358 VAL A CB  1 
ATOM   1455 C CG1 . VAL A 1 358 ? 5.224   -16.417 5.757  1.00 24.39 ? 358 VAL A CG1 1 
ATOM   1456 C CG2 . VAL A 1 358 ? 7.562   -16.218 4.834  1.00 23.81 ? 358 VAL A CG2 1 
ATOM   1457 N N   . LYS A 1 359 ? 5.645   -14.389 8.905  1.00 24.32 ? 359 LYS A N   1 
ATOM   1458 C CA  . LYS A 1 359 ? 4.815   -14.443 10.094 1.00 24.76 ? 359 LYS A CA  1 
ATOM   1459 C C   . LYS A 1 359 ? 3.339   -14.502 9.711  1.00 25.78 ? 359 LYS A C   1 
ATOM   1460 O O   . LYS A 1 359 ? 2.555   -15.155 10.385 1.00 26.03 ? 359 LYS A O   1 
ATOM   1461 C CB  . LYS A 1 359 ? 5.085   -13.221 10.985 1.00 25.33 ? 359 LYS A CB  1 
ATOM   1462 C CG  . LYS A 1 359 ? 4.293   -13.258 12.277 1.00 25.44 ? 359 LYS A CG  1 
ATOM   1463 C CD  . LYS A 1 359 ? 4.388   -11.977 13.019 1.00 26.50 ? 359 LYS A CD  1 
ATOM   1464 C CE  . LYS A 1 359 ? 3.589   -12.094 14.290 1.00 28.11 ? 359 LYS A CE  1 
ATOM   1465 N NZ  . LYS A 1 359 ? 3.853   -10.964 15.189 1.00 28.75 ? 359 LYS A NZ  1 
ATOM   1466 N N   . ALA A 1 360 ? 2.957   -13.812 8.638  1.00 25.93 ? 360 ALA A N   1 
ATOM   1467 C CA  . ALA A 1 360 ? 1.580   -13.753 8.204  1.00 26.13 ? 360 ALA A CA  1 
ATOM   1468 C C   . ALA A 1 360 ? 1.203   -15.011 7.477  1.00 26.12 ? 360 ALA A C   1 
ATOM   1469 O O   . ALA A 1 360 ? 1.820   -15.364 6.473  1.00 27.00 ? 360 ALA A O   1 
ATOM   1470 C CB  . ALA A 1 360 ? 1.365   -12.547 7.320  1.00 26.44 ? 360 ALA A CB  1 
ATOM   1471 N N   . VAL A 1 361 ? 0.208   -15.711 7.998  1.00 24.75 ? 361 VAL A N   1 
ATOM   1472 C CA  . VAL A 1 361 ? -0.239  -16.970 7.451  1.00 24.37 ? 361 VAL A CA  1 
ATOM   1473 C C   . VAL A 1 361 ? -1.740  -17.052 7.738  1.00 22.35 ? 361 VAL A C   1 
ATOM   1474 O O   . VAL A 1 361 ? -2.125  -17.079 8.904  1.00 20.77 ? 361 VAL A O   1 
ATOM   1475 C CB  . VAL A 1 361 ? 0.476   -18.156 8.146  1.00 26.44 ? 361 VAL A CB  1 
ATOM   1476 C CG1 . VAL A 1 361 ? -0.025  -19.470 7.598  1.00 27.40 ? 361 VAL A CG1 1 
ATOM   1477 C CG2 . VAL A 1 361 ? 1.995   -18.083 8.022  1.00 27.95 ? 361 VAL A CG2 1 
ATOM   1478 N N   . ALA A 1 362 ? -2.579  -17.087 6.703  1.00 21.02 ? 362 ALA A N   1 
ATOM   1479 C CA  . ALA A 1 362 ? -4.028  -17.197 6.916  1.00 20.87 ? 362 ALA A CA  1 
ATOM   1480 C C   . ALA A 1 362 ? -4.676  -17.914 5.768  1.00 21.48 ? 362 ALA A C   1 
ATOM   1481 O O   . ALA A 1 362 ? -4.344  -17.663 4.616  1.00 21.56 ? 362 ALA A O   1 
ATOM   1482 C CB  . ALA A 1 362 ? -4.655  -15.835 7.086  1.00 19.91 ? 362 ALA A CB  1 
ATOM   1483 N N   . TRP A 1 363 ? -5.571  -18.823 6.076  1.00 21.52 ? 363 TRP A N   1 
ATOM   1484 C CA  . TRP A 1 363 ? -6.272  -19.599 5.073  1.00 22.33 ? 363 TRP A CA  1 
ATOM   1485 C C   . TRP A 1 363 ? -7.513  -18.905 4.660  1.00 22.97 ? 363 TRP A C   1 
ATOM   1486 O O   . TRP A 1 363 ? -8.205  -18.299 5.487  1.00 23.57 ? 363 TRP A O   1 
ATOM   1487 C CB  . TRP A 1 363 ? -6.667  -20.969 5.624  1.00 22.35 ? 363 TRP A CB  1 
ATOM   1488 C CG  . TRP A 1 363 ? -5.498  -21.835 5.931  1.00 23.58 ? 363 TRP A CG  1 
ATOM   1489 C CD1 . TRP A 1 363 ? -4.804  -21.897 7.102  1.00 24.77 ? 363 TRP A CD1 1 
ATOM   1490 C CD2 . TRP A 1 363 ? -4.836  -22.717 5.021  1.00 24.09 ? 363 TRP A CD2 1 
ATOM   1491 N NE1 . TRP A 1 363 ? -3.751  -22.766 6.978  1.00 25.40 ? 363 TRP A NE1 1 
ATOM   1492 C CE2 . TRP A 1 363 ? -3.754  -23.296 5.713  1.00 24.85 ? 363 TRP A CE2 1 
ATOM   1493 C CE3 . TRP A 1 363 ? -5.047  -23.063 3.686  1.00 24.20 ? 363 TRP A CE3 1 
ATOM   1494 C CZ2 . TRP A 1 363 ? -2.924  -24.239 5.130  1.00 25.07 ? 363 TRP A CZ2 1 
ATOM   1495 C CZ3 . TRP A 1 363 ? -4.215  -23.990 3.102  1.00 25.08 ? 363 TRP A CZ3 1 
ATOM   1496 C CH2 . TRP A 1 363 ? -3.140  -24.532 3.805  1.00 25.44 ? 363 TRP A CH2 1 
ATOM   1497 N N   . CYS A 1 364 ? -7.854  -19.061 3.392  1.00 22.92 ? 364 CYS A N   1 
ATOM   1498 C CA  . CYS A 1 364 ? -9.095  -18.542 2.884  1.00 23.89 ? 364 CYS A CA  1 
ATOM   1499 C C   . CYS A 1 364 ? -10.249 -19.362 3.482  1.00 24.44 ? 364 CYS A C   1 
ATOM   1500 O O   . CYS A 1 364 ? -10.288 -20.575 3.326  1.00 24.27 ? 364 CYS A O   1 
ATOM   1501 C CB  . CYS A 1 364 ? -9.123  -18.590 1.364  1.00 24.96 ? 364 CYS A CB  1 
ATOM   1502 S SG  . CYS A 1 364 ? -10.666 -17.966 0.662  1.00 29.14 ? 364 CYS A SG  1 
ATOM   1503 N N   . PRO A 1 365 ? -11.173 -18.715 4.189  1.00 25.23 ? 365 PRO A N   1 
ATOM   1504 C CA  . PRO A 1 365 ? -12.297 -19.446 4.791  1.00 26.07 ? 365 PRO A CA  1 
ATOM   1505 C C   . PRO A 1 365 ? -13.249 -20.080 3.785  1.00 27.84 ? 365 PRO A C   1 
ATOM   1506 O O   . PRO A 1 365 ? -13.873 -21.084 4.103  1.00 28.23 ? 365 PRO A O   1 
ATOM   1507 C CB  . PRO A 1 365 ? -13.032 -18.367 5.583  1.00 26.22 ? 365 PRO A CB  1 
ATOM   1508 C CG  . PRO A 1 365 ? -12.054 -17.288 5.760  1.00 26.43 ? 365 PRO A CG  1 
ATOM   1509 C CD  . PRO A 1 365 ? -11.233 -17.286 4.518  1.00 24.79 ? 365 PRO A CD  1 
ATOM   1510 N N   . TRP A 1 366 ? -13.344 -19.528 2.574  1.00 28.78 ? 366 TRP A N   1 
ATOM   1511 C CA  . TRP A 1 366 ? -14.266 -20.063 1.569  1.00 29.87 ? 366 TRP A CA  1 
ATOM   1512 C C   . TRP A 1 366 ? -13.582 -20.886 0.452  1.00 30.52 ? 366 TRP A C   1 
ATOM   1513 O O   . TRP A 1 366 ? -14.241 -21.254 -0.530 1.00 30.95 ? 366 TRP A O   1 
ATOM   1514 C CB  . TRP A 1 366 ? -15.138 -18.937 0.982  1.00 30.01 ? 366 TRP A CB  1 
ATOM   1515 C CG  . TRP A 1 366 ? -14.362 -17.877 0.264  1.00 31.04 ? 366 TRP A CG  1 
ATOM   1516 C CD1 . TRP A 1 366 ? -14.041 -17.843 -1.063 1.00 31.98 ? 366 TRP A CD1 1 
ATOM   1517 C CD2 . TRP A 1 366 ? -13.829 -16.684 0.837  1.00 31.68 ? 366 TRP A CD2 1 
ATOM   1518 N NE1 . TRP A 1 366 ? -13.326 -16.702 -1.348 1.00 32.43 ? 366 TRP A NE1 1 
ATOM   1519 C CE2 . TRP A 1 366 ? -13.173 -15.977 -0.195 1.00 32.41 ? 366 TRP A CE2 1 
ATOM   1520 C CE3 . TRP A 1 366 ? -13.846 -16.140 2.120  1.00 32.84 ? 366 TRP A CE3 1 
ATOM   1521 C CZ2 . TRP A 1 366 ? -12.526 -14.767 0.031  1.00 33.09 ? 366 TRP A CZ2 1 
ATOM   1522 C CZ3 . TRP A 1 366 ? -13.159 -14.968 2.348  1.00 33.84 ? 366 TRP A CZ3 1 
ATOM   1523 C CH2 . TRP A 1 366 ? -12.528 -14.286 1.310  1.00 33.63 ? 366 TRP A CH2 1 
ATOM   1524 N N   . GLN A 1 367 ? -12.277 -21.152 0.584  1.00 30.22 ? 367 GLN A N   1 
ATOM   1525 C CA  . GLN A 1 367 ? -11.528 -21.962 -0.388 1.00 31.12 ? 367 GLN A CA  1 
ATOM   1526 C C   . GLN A 1 367 ? -10.496 -22.734 0.397  1.00 31.84 ? 367 GLN A C   1 
ATOM   1527 O O   . GLN A 1 367 ? -9.480  -22.178 0.814  1.00 31.36 ? 367 GLN A O   1 
ATOM   1528 C CB  . GLN A 1 367 ? -10.812 -21.106 -1.406 1.00 32.33 ? 367 GLN A CB  1 
ATOM   1529 C CG  . GLN A 1 367 ? -11.696 -20.540 -2.464 1.00 36.79 ? 367 GLN A CG  1 
ATOM   1530 C CD  . GLN A 1 367 ? -10.994 -19.345 -2.976 1.00 42.81 ? 367 GLN A CD  1 
ATOM   1531 O OE1 . GLN A 1 367 ? -10.701 -18.408 -2.221 1.00 45.34 ? 367 GLN A OE1 1 
ATOM   1532 N NE2 . GLN A 1 367 ? -10.659 -19.372 -4.247 1.00 43.61 ? 367 GLN A NE2 1 
ATOM   1533 N N   . SER A 1 368 ? -10.766 -24.016 0.584  1.00 32.39 ? 368 SER A N   1 
ATOM   1534 C CA  . SER A 1 368 ? -9.984  -24.941 1.376  1.00 33.32 ? 368 SER A CA  1 
ATOM   1535 C C   . SER A 1 368 ? -8.476  -24.917 1.144  1.00 32.30 ? 368 SER A C   1 
ATOM   1536 O O   . SER A 1 368 ? -7.706  -24.949 2.109  1.00 32.58 ? 368 SER A O   1 
ATOM   1537 C CB  . SER A 1 368 ? -10.504 -26.356 1.170  1.00 36.69 ? 368 SER A CB  1 
ATOM   1538 O OG  . SER A 1 368 ? -10.520 -26.671 -0.213 1.00 42.19 ? 368 SER A OG  1 
ATOM   1539 N N   . ASN A 1 369 ? -8.059  -24.873 -0.114 1.00 30.34 ? 369 ASN A N   1 
ATOM   1540 C CA  . ASN A 1 369 ? -6.651  -24.941 -0.456 1.00 28.90 ? 369 ASN A CA  1 
ATOM   1541 C C   . ASN A 1 369 ? -5.981  -23.598 -0.701 1.00 26.53 ? 369 ASN A C   1 
ATOM   1542 O O   . ASN A 1 369 ? -4.820  -23.592 -1.070 1.00 25.77 ? 369 ASN A O   1 
ATOM   1543 C CB  . ASN A 1 369 ? -6.473  -25.815 -1.685 1.00 30.28 ? 369 ASN A CB  1 
ATOM   1544 C CG  . ASN A 1 369 ? -7.026  -27.188 -1.501 1.00 33.99 ? 369 ASN A CG  1 
ATOM   1545 O OD1 . ASN A 1 369 ? -6.878  -27.787 -0.451 1.00 34.54 ? 369 ASN A OD1 1 
ATOM   1546 N ND2 . ASN A 1 369 ? -7.692  -27.711 -2.524 1.00 36.65 ? 369 ASN A ND2 1 
ATOM   1547 N N   . VAL A 1 370 ? -6.678  -22.472 -0.486 1.00 24.97 ? 370 VAL A N   1 
ATOM   1548 C CA  . VAL A 1 370 ? -6.082  -21.174 -0.729 1.00 23.72 ? 370 VAL A CA  1 
ATOM   1549 C C   . VAL A 1 370 ? -5.483  -20.603 0.540  1.00 23.60 ? 370 VAL A C   1 
ATOM   1550 O O   . VAL A 1 370 ? -6.149  -20.495 1.580  1.00 23.68 ? 370 VAL A O   1 
ATOM   1551 C CB  . VAL A 1 370 ? -7.052  -20.225 -1.438 1.00 23.65 ? 370 VAL A CB  1 
ATOM   1552 C CG1 . VAL A 1 370 ? -6.473  -18.821 -1.530 1.00 23.41 ? 370 VAL A CG1 1 
ATOM   1553 C CG2 . VAL A 1 370 ? -7.405  -20.763 -2.824 1.00 23.53 ? 370 VAL A CG2 1 
ATOM   1554 N N   . LEU A 1 371 ? -4.198  -20.257 0.459  1.00 22.60 ? 371 LEU A N   1 
ATOM   1555 C CA  . LEU A 1 371 ? -3.439  -19.757 1.590  1.00 21.92 ? 371 LEU A CA  1 
ATOM   1556 C C   . LEU A 1 371 ? -2.853  -18.410 1.290  1.00 21.81 ? 371 LEU A C   1 
ATOM   1557 O O   . LEU A 1 371 ? -2.299  -18.227 0.213  1.00 22.26 ? 371 LEU A O   1 
ATOM   1558 C CB  . LEU A 1 371 ? -2.288  -20.728 1.875  1.00 21.31 ? 371 LEU A CB  1 
ATOM   1559 C CG  . LEU A 1 371 ? -1.342  -20.348 3.023  1.00 21.82 ? 371 LEU A CG  1 
ATOM   1560 C CD1 . LEU A 1 371 ? -2.049  -20.464 4.374  1.00 21.75 ? 371 LEU A CD1 1 
ATOM   1561 C CD2 . LEU A 1 371 ? -0.069  -21.197 3.006  1.00 21.70 ? 371 LEU A CD2 1 
ATOM   1562 N N   . ALA A 1 372 ? -2.889  -17.488 2.254  1.00 20.67 ? 372 ALA A N   1 
ATOM   1563 C CA  . ALA A 1 372 ? -2.234  -16.203 2.095  1.00 20.35 ? 372 ALA A CA  1 
ATOM   1564 C C   . ALA A 1 372 ? -1.068  -16.150 3.080  1.00 19.48 ? 372 ALA A C   1 
ATOM   1565 O O   . ALA A 1 372 ? -1.220  -16.518 4.257  1.00 19.47 ? 372 ALA A O   1 
ATOM   1566 C CB  . ALA A 1 372 ? -3.206  -15.074 2.378  1.00 20.30 ? 372 ALA A CB  1 
ATOM   1567 N N   . THR A 1 373 ? 0.084   -15.714 2.607  1.00 18.48 ? 373 THR A N   1 
ATOM   1568 C CA  . THR A 1 373 ? 1.256   -15.543 3.454  1.00 19.97 ? 373 THR A CA  1 
ATOM   1569 C C   . THR A 1 373 ? 1.848   -14.144 3.224  1.00 21.62 ? 373 THR A C   1 
ATOM   1570 O O   . THR A 1 373 ? 1.660   -13.560 2.165  1.00 21.16 ? 373 THR A O   1 
ATOM   1571 C CB  . THR A 1 373 ? 2.314   -16.599 3.182  1.00 19.82 ? 373 THR A CB  1 
ATOM   1572 O OG1 . THR A 1 373 ? 2.690   -16.484 1.811  1.00 20.89 ? 373 THR A OG1 1 
ATOM   1573 C CG2 . THR A 1 373 ? 1.834   -18.006 3.471  1.00 19.62 ? 373 THR A CG2 1 
ATOM   1574 N N   . GLY A 1 374 ? 2.566   -13.631 4.217  1.00 22.32 ? 374 GLY A N   1 
ATOM   1575 C CA  . GLY A 1 374 ? 3.195   -12.328 4.108  1.00 22.99 ? 374 GLY A CA  1 
ATOM   1576 C C   . GLY A 1 374 ? 4.592   -12.332 4.679  1.00 23.84 ? 374 GLY A C   1 
ATOM   1577 O O   . GLY A 1 374 ? 4.846   -12.908 5.747  1.00 23.29 ? 374 GLY A O   1 
ATOM   1578 N N   . GLY A 1 375 ? 5.499   -11.683 3.967  1.00 24.38 ? 375 GLY A N   1 
ATOM   1579 C CA  . GLY A 1 375 ? 6.890   -11.618 4.383  1.00 25.35 ? 375 GLY A CA  1 
ATOM   1580 C C   . GLY A 1 375 ? 7.246   -10.355 5.142  1.00 26.70 ? 375 GLY A C   1 
ATOM   1581 O O   . GLY A 1 375 ? 6.528   -9.351  5.078  1.00 27.42 ? 375 GLY A O   1 
ATOM   1582 N N   . GLY A 1 376 ? 8.387   -10.403 5.827  1.00 26.62 ? 376 GLY A N   1 
ATOM   1583 C CA  . GLY A 1 376 ? 8.903   -9.315  6.640  1.00 27.14 ? 376 GLY A CA  1 
ATOM   1584 C C   . GLY A 1 376 ? 9.466   -8.168  5.842  1.00 28.04 ? 376 GLY A C   1 
ATOM   1585 O O   . GLY A 1 376 ? 9.215   -8.061  4.643  1.00 29.31 ? 376 GLY A O   1 
ATOM   1586 N N   . THR A 1 377 ? 10.257  -7.319  6.492  1.00 27.88 ? 377 THR A N   1 
ATOM   1587 C CA  . THR A 1 377 ? 10.815  -6.094  5.925  1.00 28.37 ? 377 THR A CA  1 
ATOM   1588 C C   . THR A 1 377 ? 11.619  -6.288  4.644  1.00 29.41 ? 377 THR A C   1 
ATOM   1589 O O   . THR A 1 377 ? 11.584  -5.423  3.761  1.00 30.16 ? 377 THR A O   1 
ATOM   1590 C CB  . THR A 1 377 ? 11.635  -5.368  6.978  1.00 28.75 ? 377 THR A CB  1 
ATOM   1591 O OG1 . THR A 1 377 ? 10.807  -5.176  8.128  1.00 29.51 ? 377 THR A OG1 1 
ATOM   1592 C CG2 . THR A 1 377 ? 12.117  -4.014  6.499  1.00 29.08 ? 377 THR A CG2 1 
ATOM   1593 N N   . SER A 1 378 ? 12.359  -7.397  4.542  1.00 28.83 ? 378 SER A N   1 
ATOM   1594 C CA  . SER A 1 378 ? 13.154  -7.647  3.338  1.00 28.86 ? 378 SER A CA  1 
ATOM   1595 C C   . SER A 1 378 ? 12.325  -8.274  2.199  1.00 27.81 ? 378 SER A C   1 
ATOM   1596 O O   . SER A 1 378 ? 12.868  -8.524  1.129  1.00 27.95 ? 378 SER A O   1 
ATOM   1597 C CB  . SER A 1 378 ? 14.329  -8.553  3.663  1.00 29.89 ? 378 SER A CB  1 
ATOM   1598 O OG  . SER A 1 378 ? 13.832  -9.777  4.171  1.00 30.98 ? 378 SER A OG  1 
ATOM   1599 N N   . ASP A 1 379 ? 11.040  -8.559  2.434  1.00 26.74 ? 379 ASP A N   1 
ATOM   1600 C CA  . ASP A 1 379 ? 10.198  -9.189  1.432  1.00 26.85 ? 379 ASP A CA  1 
ATOM   1601 C C   . ASP A 1 379 ? 9.066   -8.262  1.045  1.00 27.34 ? 379 ASP A C   1 
ATOM   1602 O O   . ASP A 1 379 ? 8.913   -7.949  -0.122 1.00 27.22 ? 379 ASP A O   1 
ATOM   1603 C CB  . ASP A 1 379 ? 9.670   -10.543 1.945  1.00 27.50 ? 379 ASP A CB  1 
ATOM   1604 C CG  . ASP A 1 379 ? 8.756   -11.201 0.941  1.00 30.11 ? 379 ASP A CG  1 
ATOM   1605 O OD1 . ASP A 1 379 ? 9.262   -11.643 -0.120 1.00 29.53 ? 379 ASP A OD1 1 
ATOM   1606 O OD2 . ASP A 1 379 ? 7.536   -11.242 1.191  1.00 32.00 ? 379 ASP A OD2 1 
ATOM   1607 N N   . ARG A 1 380 ? 8.251   -7.867  2.024  1.00 28.16 ? 380 ARG A N   1 
ATOM   1608 C CA  . ARG A 1 380 ? 7.143   -6.930  1.899  1.00 29.64 ? 380 ARG A CA  1 
ATOM   1609 C C   . ARG A 1 380 ? 5.981   -7.396  1.033  1.00 29.41 ? 380 ARG A C   1 
ATOM   1610 O O   . ARG A 1 380 ? 5.125   -6.574  0.693  1.00 30.05 ? 380 ARG A O   1 
ATOM   1611 C CB  . ARG A 1 380 ? 7.634   -5.563  1.392  1.00 32.23 ? 380 ARG A CB  1 
ATOM   1612 C CG  . ARG A 1 380 ? 8.890   -5.010  2.060  1.00 36.72 ? 380 ARG A CG  1 
ATOM   1613 C CD  . ARG A 1 380 ? 9.430   -3.774  1.338  1.00 41.55 ? 380 ARG A CD  1 
ATOM   1614 N NE  . ARG A 1 380 ? 9.269   -3.837  -0.123 1.00 46.34 ? 380 ARG A NE  1 
ATOM   1615 C CZ  . ARG A 1 380 ? 10.178  -4.323  -0.962 1.00 49.48 ? 380 ARG A CZ  1 
ATOM   1616 N NH1 . ARG A 1 380 ? 11.339  -4.777  -0.504 1.00 49.23 ? 380 ARG A NH1 1 
ATOM   1617 N NH2 . ARG A 1 380 ? 9.932   -4.362  -2.266 1.00 49.62 ? 380 ARG A NH2 1 
ATOM   1618 N N   . HIS A 1 381 ? 5.942   -8.683  0.677  1.00 27.64 ? 381 HIS A N   1 
ATOM   1619 C CA  . HIS A 1 381 ? 4.888   -9.174  -0.179 1.00 26.82 ? 381 HIS A CA  1 
ATOM   1620 C C   . HIS A 1 381 ? 3.867   -10.061 0.497  1.00 25.16 ? 381 HIS A C   1 
ATOM   1621 O O   . HIS A 1 381 ? 4.190   -10.842 1.369  1.00 24.23 ? 381 HIS A O   1 
ATOM   1622 C CB  . HIS A 1 381 ? 5.462   -9.917  -1.393 1.00 27.85 ? 381 HIS A CB  1 
ATOM   1623 C CG  . HIS A 1 381 ? 6.022   -9.013  -2.447 1.00 30.02 ? 381 HIS A CG  1 
ATOM   1624 N ND1 . HIS A 1 381 ? 7.089   -8.178  -2.183 1.00 31.92 ? 381 HIS A ND1 1 
ATOM   1625 C CD2 . HIS A 1 381 ? 5.670   -8.873  -3.747 1.00 31.39 ? 381 HIS A CD2 1 
ATOM   1626 C CE1 . HIS A 1 381 ? 7.345   -7.546  -3.316 1.00 32.60 ? 381 HIS A CE1 1 
ATOM   1627 N NE2 . HIS A 1 381 ? 6.510   -7.924  -4.284 1.00 32.63 ? 381 HIS A NE2 1 
ATOM   1628 N N   . ILE A 1 382 ? 2.635   -9.961  0.015  1.00 24.15 ? 382 ILE A N   1 
ATOM   1629 C CA  . ILE A 1 382 ? 1.556   -10.855 0.313  1.00 23.46 ? 382 ILE A CA  1 
ATOM   1630 C C   . ILE A 1 382 ? 1.532   -11.827 -0.876 1.00 22.69 ? 382 ILE A C   1 
ATOM   1631 O O   . ILE A 1 382 ? 1.607   -11.414 -2.038 1.00 21.94 ? 382 ILE A O   1 
ATOM   1632 C CB  . ILE A 1 382 ? 0.238   -10.090 0.427  1.00 24.21 ? 382 ILE A CB  1 
ATOM   1633 C CG1 . ILE A 1 382 ? 0.234   -9.274  1.729  1.00 24.79 ? 382 ILE A CG1 1 
ATOM   1634 C CG2 . ILE A 1 382 ? -0.960  -11.036 0.358  1.00 24.78 ? 382 ILE A CG2 1 
ATOM   1635 C CD1 . ILE A 1 382 ? -0.733  -8.151  1.735  1.00 25.80 ? 382 ILE A CD1 1 
ATOM   1636 N N   . ARG A 1 383 ? 1.505   -13.118 -0.581 1.00 22.27 ? 383 ARG A N   1 
ATOM   1637 C CA  . ARG A 1 383 ? 1.424   -14.137 -1.615 1.00 22.46 ? 383 ARG A CA  1 
ATOM   1638 C C   . ARG A 1 383 ? 0.224   -14.999 -1.363 1.00 22.71 ? 383 ARG A C   1 
ATOM   1639 O O   . ARG A 1 383 ? -0.060  -15.359 -0.221 1.00 23.33 ? 383 ARG A O   1 
ATOM   1640 C CB  . ARG A 1 383 ? 2.709   -14.968 -1.699 1.00 22.43 ? 383 ARG A CB  1 
ATOM   1641 C CG  . ARG A 1 383 ? 3.799   -14.212 -2.403 1.00 21.08 ? 383 ARG A CG  1 
ATOM   1642 C CD  . ARG A 1 383 ? 5.110   -14.939 -2.375 1.00 23.28 ? 383 ARG A CD  1 
ATOM   1643 N NE  . ARG A 1 383 ? 6.109   -14.238 -3.177 1.00 26.13 ? 383 ARG A NE  1 
ATOM   1644 C CZ  . ARG A 1 383 ? 6.286   -14.413 -4.483 1.00 27.90 ? 383 ARG A CZ  1 
ATOM   1645 N NH1 . ARG A 1 383 ? 7.227   -13.733 -5.126 1.00 25.33 ? 383 ARG A NH1 1 
ATOM   1646 N NH2 . ARG A 1 383 ? 5.527   -15.276 -5.157 1.00 27.98 ? 383 ARG A NH2 1 
ATOM   1647 N N   . ILE A 1 384 ? -0.512  -15.286 -2.413 1.00 22.16 ? 384 ILE A N   1 
ATOM   1648 C CA  . ILE A 1 384 ? -1.693  -16.136 -2.320 1.00 21.90 ? 384 ILE A CA  1 
ATOM   1649 C C   . ILE A 1 384 ? -1.338  -17.406 -3.038 1.00 22.10 ? 384 ILE A C   1 
ATOM   1650 O O   . ILE A 1 384 ? -0.830  -17.352 -4.151 1.00 22.26 ? 384 ILE A O   1 
ATOM   1651 C CB  . ILE A 1 384 ? -2.905  -15.465 -2.994 1.00 22.04 ? 384 ILE A CB  1 
ATOM   1652 C CG1 . ILE A 1 384 ? -3.127  -14.042 -2.471 1.00 22.35 ? 384 ILE A CG1 1 
ATOM   1653 C CG2 . ILE A 1 384 ? -4.153  -16.340 -2.863 1.00 21.81 ? 384 ILE A CG2 1 
ATOM   1654 C CD1 . ILE A 1 384 ? -3.419  -13.963 -1.080 1.00 23.40 ? 384 ILE A CD1 1 
ATOM   1655 N N   . TRP A 1 385 ? -1.571  -18.541 -2.416 1.00 22.09 ? 385 TRP A N   1 
ATOM   1656 C CA  . TRP A 1 385 ? -1.203  -19.828 -2.992 1.00 22.86 ? 385 TRP A CA  1 
ATOM   1657 C C   . TRP A 1 385 ? -2.370  -20.750 -3.074 1.00 24.16 ? 385 TRP A C   1 
ATOM   1658 O O   . TRP A 1 385 ? -3.312  -20.642 -2.279 1.00 23.96 ? 385 TRP A O   1 
ATOM   1659 C CB  . TRP A 1 385 ? -0.202  -20.532 -2.067 1.00 22.73 ? 385 TRP A CB  1 
ATOM   1660 C CG  . TRP A 1 385 ? 0.901   -19.681 -1.539 1.00 23.42 ? 385 TRP A CG  1 
ATOM   1661 C CD1 . TRP A 1 385 ? 0.924   -19.010 -0.355 1.00 24.64 ? 385 TRP A CD1 1 
ATOM   1662 C CD2 . TRP A 1 385 ? 2.190   -19.521 -2.118 1.00 23.62 ? 385 TRP A CD2 1 
ATOM   1663 N NE1 . TRP A 1 385 ? 2.149   -18.422 -0.171 1.00 25.03 ? 385 TRP A NE1 1 
ATOM   1664 C CE2 . TRP A 1 385 ? 2.941   -18.704 -1.253 1.00 24.60 ? 385 TRP A CE2 1 
ATOM   1665 C CE3 . TRP A 1 385 ? 2.796   -20.019 -3.271 1.00 24.26 ? 385 TRP A CE3 1 
ATOM   1666 C CZ2 . TRP A 1 385 ? 4.254   -18.349 -1.524 1.00 25.30 ? 385 TRP A CZ2 1 
ATOM   1667 C CZ3 . TRP A 1 385 ? 4.092   -19.647 -3.548 1.00 25.57 ? 385 TRP A CZ3 1 
ATOM   1668 C CH2 . TRP A 1 385 ? 4.800   -18.807 -2.691 1.00 25.54 ? 385 TRP A CH2 1 
ATOM   1669 N N   . ASN A 1 386 ? -2.267  -21.730 -3.964 1.00 24.85 ? 386 ASN A N   1 
ATOM   1670 C CA  . ASN A 1 386 ? -3.141  -22.874 -3.965 1.00 26.82 ? 386 ASN A CA  1 
ATOM   1671 C C   . ASN A 1 386 ? -2.195  -23.968 -3.468 1.00 27.87 ? 386 ASN A C   1 
ATOM   1672 O O   . ASN A 1 386 ? -1.232  -24.298 -4.159 1.00 28.20 ? 386 ASN A O   1 
ATOM   1673 C CB  . ASN A 1 386 ? -3.666  -23.219 -5.337 1.00 28.85 ? 386 ASN A CB  1 
ATOM   1674 C CG  . ASN A 1 386 ? -4.602  -24.397 -5.247 1.00 34.66 ? 386 ASN A CG  1 
ATOM   1675 O OD1 . ASN A 1 386 ? -4.205  -25.516 -4.885 1.00 35.41 ? 386 ASN A OD1 1 
ATOM   1676 N ND2 . ASN A 1 386 ? -5.879  -24.154 -5.507 1.00 36.55 ? 386 ASN A ND2 1 
ATOM   1677 N N   . VAL A 1 387 ? -2.436  -24.511 -2.285 1.00 28.06 ? 387 VAL A N   1 
ATOM   1678 C CA  . VAL A 1 387 ? -1.537  -25.501 -1.684 1.00 29.31 ? 387 VAL A CA  1 
ATOM   1679 C C   . VAL A 1 387 ? -1.592  -26.888 -2.336 1.00 30.93 ? 387 VAL A C   1 
ATOM   1680 O O   . VAL A 1 387 ? -0.692  -27.700 -2.111 1.00 31.40 ? 387 VAL A O   1 
ATOM   1681 C CB  . VAL A 1 387 ? -1.731  -25.593 -0.160 1.00 30.12 ? 387 VAL A CB  1 
ATOM   1682 C CG1 . VAL A 1 387 ? -1.671  -24.201 0.474  1.00 30.12 ? 387 VAL A CG1 1 
ATOM   1683 C CG2 . VAL A 1 387 ? -3.044  -26.292 0.181  1.00 30.70 ? 387 VAL A CG2 1 
ATOM   1684 N N   . CYS A 1 388 ? -2.608  -27.158 -3.150 1.00 31.59 ? 388 CYS A N   1 
ATOM   1685 C CA  . CYS A 1 388 ? -2.729  -28.442 -3.829 1.00 32.91 ? 388 CYS A CA  1 
ATOM   1686 C C   . CYS A 1 388 ? -1.850  -28.418 -5.079 1.00 32.47 ? 388 CYS A C   1 
ATOM   1687 O O   . CYS A 1 388 ? -0.996  -29.283 -5.238 1.00 33.07 ? 388 CYS A O   1 
ATOM   1688 C CB  . CYS A 1 388 ? -4.193  -28.731 -4.157 1.00 35.64 ? 388 CYS A CB  1 
ATOM   1689 S SG  . CYS A 1 388 ? -4.495  -30.363 -4.884 1.00 45.49 ? 388 CYS A SG  1 
ATOM   1690 N N   . SER A 1 389 ? -2.019  -27.410 -5.935 1.00 31.36 ? 389 SER A N   1 
ATOM   1691 C CA  . SER A 1 389 ? -1.205  -27.288 -7.147 1.00 31.25 ? 389 SER A CA  1 
ATOM   1692 C C   . SER A 1 389 ? 0.177   -26.679 -6.895 1.00 31.08 ? 389 SER A C   1 
ATOM   1693 O O   . SER A 1 389 ? 1.056   -26.795 -7.741 1.00 31.66 ? 389 SER A O   1 
ATOM   1694 C CB  . SER A 1 389 ? -1.932  -26.432 -8.172 1.00 31.62 ? 389 SER A CB  1 
ATOM   1695 O OG  . SER A 1 389 ? -2.116  -25.137 -7.630 1.00 33.44 ? 389 SER A OG  1 
ATOM   1696 N N   . GLY A 1 390 ? 0.338   -25.991 -5.774 1.00 30.34 ? 390 GLY A N   1 
ATOM   1697 C CA  . GLY A 1 390 ? 1.559   -25.270 -5.440 1.00 30.17 ? 390 GLY A CA  1 
ATOM   1698 C C   . GLY A 1 390 ? 1.659   -23.912 -6.118 1.00 29.68 ? 390 GLY A C   1 
ATOM   1699 O O   . GLY A 1 390 ? 2.653   -23.204 -5.949 1.00 29.97 ? 390 GLY A O   1 
ATOM   1700 N N   . ALA A 1 391 ? 0.641   -23.533 -6.894 1.00 28.77 ? 391 ALA A N   1 
ATOM   1701 C CA  . ALA A 1 391 ? 0.663   -22.303 -7.657 1.00 28.93 ? 391 ALA A CA  1 
ATOM   1702 C C   . ALA A 1 391 ? 0.612   -21.074 -6.802 1.00 28.69 ? 391 ALA A C   1 
ATOM   1703 O O   . ALA A 1 391 ? -0.147  -21.033 -5.842 1.00 29.02 ? 391 ALA A O   1 
ATOM   1704 C CB  . ALA A 1 391 ? -0.500  -22.286 -8.640 1.00 28.90 ? 391 ALA A CB  1 
ATOM   1705 N N   . CYS A 1 392 ? 1.400   -20.064 -7.152 1.00 28.49 ? 392 CYS A N   1 
ATOM   1706 C CA  . CYS A 1 392 ? 1.304   -18.768 -6.503 1.00 28.99 ? 392 CYS A CA  1 
ATOM   1707 C C   . CYS A 1 392 ? 0.302   -18.016 -7.362 1.00 28.12 ? 392 CYS A C   1 
ATOM   1708 O O   . CYS A 1 392 ? 0.582   -17.677 -8.506 1.00 28.12 ? 392 CYS A O   1 
ATOM   1709 C CB  . CYS A 1 392 ? 2.639   -18.040 -6.453 1.00 30.81 ? 392 CYS A CB  1 
ATOM   1710 S SG  . CYS A 1 392 ? 2.505   -16.350 -5.815 1.00 37.78 ? 392 CYS A SG  1 
ATOM   1711 N N   . LEU A 1 393 ? -0.888  -17.836 -6.847 1.00 27.54 ? 393 LEU A N   1 
ATOM   1712 C CA  . LEU A 1 393 ? -1.975  -17.176 -7.560 1.00 27.44 ? 393 LEU A CA  1 
ATOM   1713 C C   . LEU A 1 393 ? -1.768  -15.665 -7.663 1.00 27.32 ? 393 LEU A C   1 
ATOM   1714 O O   . LEU A 1 393 ? -2.207  -15.047 -8.632 1.00 27.83 ? 393 LEU A O   1 
ATOM   1715 C CB  . LEU A 1 393 ? -3.291  -17.472 -6.822 1.00 27.41 ? 393 LEU A CB  1 
ATOM   1716 C CG  . LEU A 1 393 ? -3.569  -18.950 -6.527 1.00 28.19 ? 393 LEU A CG  1 
ATOM   1717 C CD1 . LEU A 1 393 ? -4.841  -19.125 -5.716 1.00 28.65 ? 393 LEU A CD1 1 
ATOM   1718 C CD2 . LEU A 1 393 ? -3.603  -19.771 -7.785 1.00 28.31 ? 393 LEU A CD2 1 
ATOM   1719 N N   . SER A 1 394 ? -1.087  -15.076 -6.682 1.00 26.04 ? 394 SER A N   1 
ATOM   1720 C CA  . SER A 1 394 ? -0.860  -13.648 -6.655 1.00 26.18 ? 394 SER A CA  1 
ATOM   1721 C C   . SER A 1 394 ? 0.333   -13.313 -5.765 1.00 26.60 ? 394 SER A C   1 
ATOM   1722 O O   . SER A 1 394 ? 0.545   -13.952 -4.743 1.00 26.78 ? 394 SER A O   1 
ATOM   1723 C CB  . SER A 1 394 ? -2.097  -12.951 -6.097 1.00 27.27 ? 394 SER A CB  1 
ATOM   1724 O OG  . SER A 1 394 ? -1.881  -11.554 -6.085 1.00 29.19 ? 394 SER A OG  1 
ATOM   1725 N N   . ALA A 1 395 ? 1.081   -12.300 -6.129 1.00 27.23 ? 395 ALA A N   1 
ATOM   1726 C CA  . ALA A 1 395 ? 2.204   -11.810 -5.343 1.00 28.60 ? 395 ALA A CA  1 
ATOM   1727 C C   . ALA A 1 395 ? 2.058   -10.301 -5.385 1.00 29.65 ? 395 ALA A C   1 
ATOM   1728 O O   . ALA A 1 395 ? 2.136   -9.705  -6.459 1.00 29.97 ? 395 ALA A O   1 
ATOM   1729 C CB  . ALA A 1 395 ? 3.522   -12.231 -5.979 1.00 28.94 ? 395 ALA A CB  1 
ATOM   1730 N N   . VAL A 1 396 ? 1.757   -9.687  -4.243 1.00 29.71 ? 396 VAL A N   1 
ATOM   1731 C CA  . VAL A 1 396 ? 1.507   -8.254  -4.182 1.00 30.47 ? 396 VAL A CA  1 
ATOM   1732 C C   . VAL A 1 396 ? 2.469   -7.545  -3.253 1.00 30.76 ? 396 VAL A C   1 
ATOM   1733 O O   . VAL A 1 396 ? 2.633   -7.961  -2.115 1.00 30.84 ? 396 VAL A O   1 
ATOM   1734 C CB  . VAL A 1 396 ? 0.036   -8.015  -3.762 1.00 32.16 ? 396 VAL A CB  1 
ATOM   1735 C CG1 . VAL A 1 396 ? -0.216  -6.551  -3.448 1.00 33.31 ? 396 VAL A CG1 1 
ATOM   1736 C CG2 . VAL A 1 396 ? -0.916  -8.489  -4.852 1.00 32.83 ? 396 VAL A CG2 1 
ATOM   1737 N N   . ASP A 1 397 ? 3.046   -6.435  -3.708 1.00 31.11 ? 397 ASP A N   1 
ATOM   1738 C CA  . ASP A 1 397 ? 3.956   -5.622  -2.911 1.00 31.94 ? 397 ASP A CA  1 
ATOM   1739 C C   . ASP A 1 397 ? 3.161   -4.739  -1.964 1.00 31.84 ? 397 ASP A C   1 
ATOM   1740 O O   . ASP A 1 397 ? 2.443   -3.852  -2.408 1.00 32.33 ? 397 ASP A O   1 
ATOM   1741 C CB  . ASP A 1 397 ? 4.807   -4.723  -3.834 1.00 33.93 ? 397 ASP A CB  1 
ATOM   1742 C CG  . ASP A 1 397 ? 6.050   -4.129  -3.185 1.00 38.93 ? 397 ASP A CG  1 
ATOM   1743 O OD1 . ASP A 1 397 ? 6.132   -4.128  -1.946 1.00 38.62 ? 397 ASP A OD1 1 
ATOM   1744 O OD2 . ASP A 1 397 ? 6.947   -3.671  -3.926 1.00 42.27 ? 397 ASP A OD2 1 
ATOM   1745 N N   . ALA A 1 398 ? 3.295   -4.968  -0.670 1.00 31.23 ? 398 ALA A N   1 
ATOM   1746 C CA  . ALA A 1 398 ? 2.645   -4.132  0.335  1.00 31.47 ? 398 ALA A CA  1 
ATOM   1747 C C   . ALA A 1 398 ? 3.525   -2.948  0.791  1.00 31.86 ? 398 ALA A C   1 
ATOM   1748 O O   . ALA A 1 398 ? 3.075   -2.143  1.604  1.00 32.08 ? 398 ALA A O   1 
ATOM   1749 C CB  . ALA A 1 398 ? 2.235   -4.970  1.534  1.00 31.29 ? 398 ALA A CB  1 
ATOM   1750 N N   . HIS A 1 399 ? 4.782   -2.867  0.301  1.00 31.76 ? 399 HIS A N   1 
ATOM   1751 C CA  . HIS A 1 399 ? 5.732   -1.797  0.607  1.00 32.19 ? 399 HIS A CA  1 
ATOM   1752 C C   . HIS A 1 399 ? 6.112   -1.683  2.073  1.00 31.57 ? 399 HIS A C   1 
ATOM   1753 O O   . HIS A 1 399 ? 6.593   -0.644  2.519  1.00 31.92 ? 399 HIS A O   1 
ATOM   1754 C CB  . HIS A 1 399 ? 5.217   -0.464  0.076  1.00 33.58 ? 399 HIS A CB  1 
ATOM   1755 C CG  . HIS A 1 399 ? 4.975   -0.512  -1.393 1.00 36.55 ? 399 HIS A CG  1 
ATOM   1756 N ND1 . HIS A 1 399 ? 6.017   -0.426  -2.290 1.00 38.96 ? 399 HIS A ND1 1 
ATOM   1757 C CD2 . HIS A 1 399 ? 3.820   -0.705  -2.071 1.00 37.96 ? 399 HIS A CD2 1 
ATOM   1758 C CE1 . HIS A 1 399 ? 5.464   -0.531  -3.485 1.00 39.54 ? 399 HIS A CE1 1 
ATOM   1759 N NE2 . HIS A 1 399 ? 4.142   -0.702  -3.399 1.00 39.38 ? 399 HIS A NE2 1 
ATOM   1760 N N   . SER A 1 400 ? 5.968   -2.764  2.798  1.00 30.46 ? 400 SER A N   1 
ATOM   1761 C CA  . SER A 1 400 ? 6.248   -2.803  4.207  1.00 29.88 ? 400 SER A CA  1 
ATOM   1762 C C   . SER A 1 400 ? 6.195   -4.243  4.669  1.00 29.19 ? 400 SER A C   1 
ATOM   1763 O O   . SER A 1 400 ? 5.576   -5.090  4.020  1.00 29.66 ? 400 SER A O   1 
ATOM   1764 C CB  . SER A 1 400 ? 5.163   -2.016  4.936  1.00 31.07 ? 400 SER A CB  1 
ATOM   1765 O OG  . SER A 1 400 ? 5.320   -2.093  6.341  1.00 32.46 ? 400 SER A OG  1 
ATOM   1766 N N   . GLN A 1 401 ? 6.741   -4.514  5.856  1.00 28.04 ? 401 GLN A N   1 
ATOM   1767 C CA  . GLN A 1 401 ? 6.637   -5.831  6.451  1.00 27.61 ? 401 GLN A CA  1 
ATOM   1768 C C   . GLN A 1 401 ? 5.155   -6.207  6.654  1.00 27.55 ? 401 GLN A C   1 
ATOM   1769 O O   . GLN A 1 401 ? 4.298   -5.345  6.857  1.00 27.92 ? 401 GLN A O   1 
ATOM   1770 C CB  . GLN A 1 401 ? 7.397   -5.906  7.772  1.00 28.36 ? 401 GLN A CB  1 
ATOM   1771 C CG  . GLN A 1 401 ? 7.001   -4.872  8.771  1.00 30.14 ? 401 GLN A CG  1 
ATOM   1772 C CD  . GLN A 1 401 ? 7.642   -5.095  10.113 1.00 35.89 ? 401 GLN A CD  1 
ATOM   1773 O OE1 . GLN A 1 401 ? 6.994   -4.890  11.137 1.00 36.26 ? 401 GLN A OE1 1 
ATOM   1774 N NE2 . GLN A 1 401 ? 8.916   -5.484  10.166 1.00 37.30 ? 401 GLN A NE2 1 
ATOM   1775 N N   . VAL A 1 402 ? 4.863   -7.477  6.480  1.00 26.53 ? 402 VAL A N   1 
ATOM   1776 C CA  . VAL A 1 402 ? 3.514   -7.978  6.604  1.00 26.52 ? 402 VAL A CA  1 
ATOM   1777 C C   . VAL A 1 402 ? 3.488   -8.873  7.822  1.00 27.03 ? 402 VAL A C   1 
ATOM   1778 O O   . VAL A 1 402 ? 3.879   -10.033 7.743  1.00 28.11 ? 402 VAL A O   1 
ATOM   1779 C CB  . VAL A 1 402 ? 3.083   -8.754  5.343  1.00 26.65 ? 402 VAL A CB  1 
ATOM   1780 C CG1 . VAL A 1 402 ? 1.603   -9.078  5.426  1.00 27.17 ? 402 VAL A CG1 1 
ATOM   1781 C CG2 . VAL A 1 402 ? 3.393   -7.973  4.073  1.00 26.04 ? 402 VAL A CG2 1 
ATOM   1782 N N   . CYS A 1 403 ? 3.071   -8.338  8.955  1.00 26.13 ? 403 CYS A N   1 
ATOM   1783 C CA  . CYS A 1 403 ? 3.067   -9.086  10.210 1.00 25.90 ? 403 CYS A CA  1 
ATOM   1784 C C   . CYS A 1 403 ? 1.947   -10.051 10.314 1.00 25.02 ? 403 CYS A C   1 
ATOM   1785 O O   . CYS A 1 403 ? 2.063   -11.021 11.054 1.00 25.27 ? 403 CYS A O   1 
ATOM   1786 C CB  . CYS A 1 403 ? 3.045   -8.134  11.398 1.00 26.61 ? 403 CYS A CB  1 
ATOM   1787 S SG  . CYS A 1 403 ? 1.476   -7.245  11.587 1.00 30.41 ? 403 CYS A SG  1 
ATOM   1788 N N   . SER A 1 404 ? 0.829   -9.755  9.655  1.00 23.83 ? 404 SER A N   1 
ATOM   1789 C CA  . SER A 1 404 ? -0.358  -10.537 9.833  1.00 23.28 ? 404 SER A CA  1 
ATOM   1790 C C   . SER A 1 404 ? -1.306  -10.365 8.676  1.00 21.13 ? 404 SER A C   1 
ATOM   1791 O O   . SER A 1 404 ? -1.369  -9.291  8.099  1.00 20.08 ? 404 SER A O   1 
ATOM   1792 C CB  . SER A 1 404 ? -1.021  -10.038 11.108 1.00 26.58 ? 404 SER A CB  1 
ATOM   1793 O OG  . SER A 1 404 ? -1.964  -10.961 11.608 1.00 32.37 ? 404 SER A OG  1 
ATOM   1794 N N   . ILE A 1 405 ? -2.046  -11.425 8.332  1.00 20.19 ? 405 ILE A N   1 
ATOM   1795 C CA  . ILE A 1 405 ? -3.097  -11.409 7.325  1.00 19.21 ? 405 ILE A CA  1 
ATOM   1796 C C   . ILE A 1 405 ? -4.322  -12.086 7.895  1.00 19.19 ? 405 ILE A C   1 
ATOM   1797 O O   . ILE A 1 405 ? -4.201  -13.112 8.548  1.00 18.92 ? 405 ILE A O   1 
ATOM   1798 C CB  . ILE A 1 405 ? -2.700  -12.114 6.012  1.00 19.13 ? 405 ILE A CB  1 
ATOM   1799 C CG1 . ILE A 1 405 ? -1.560  -11.410 5.340  1.00 19.21 ? 405 ILE A CG1 1 
ATOM   1800 C CG2 . ILE A 1 405 ? -3.893  -12.238 5.045  1.00 19.51 ? 405 ILE A CG2 1 
ATOM   1801 C CD1 . ILE A 1 405 ? -0.895  -12.293 4.362  1.00 20.19 ? 405 ILE A CD1 1 
ATOM   1802 N N   . LEU A 1 406 ? -5.493  -11.538 7.619  1.00 19.11 ? 406 LEU A N   1 
ATOM   1803 C CA  . LEU A 1 406 ? -6.770  -12.128 7.977  1.00 19.89 ? 406 LEU A CA  1 
ATOM   1804 C C   . LEU A 1 406 ? -7.644  -12.037 6.746  1.00 20.70 ? 406 LEU A C   1 
ATOM   1805 O O   . LEU A 1 406 ? -7.495  -11.119 5.934  1.00 21.54 ? 406 LEU A O   1 
ATOM   1806 C CB  . LEU A 1 406 ? -7.459  -11.352 9.098  1.00 20.49 ? 406 LEU A CB  1 
ATOM   1807 C CG  . LEU A 1 406 ? -6.760  -11.307 10.450 1.00 22.04 ? 406 LEU A CG  1 
ATOM   1808 C CD1 . LEU A 1 406 ? -7.463  -10.345 11.364 1.00 22.79 ? 406 LEU A CD1 1 
ATOM   1809 C CD2 . LEU A 1 406 ? -6.718  -12.688 11.094 1.00 21.78 ? 406 LEU A CD2 1 
ATOM   1810 N N   . TRP A 1 407 ? -8.546  -12.970 6.596  1.00 20.15 ? 407 TRP A N   1 
ATOM   1811 C CA  . TRP A 1 407 ? -9.508  -12.953 5.510  1.00 21.14 ? 407 TRP A CA  1 
ATOM   1812 C C   . TRP A 1 407 ? -10.850 -12.652 6.139  1.00 22.54 ? 407 TRP A C   1 
ATOM   1813 O O   . TRP A 1 407 ? -11.168 -13.204 7.189  1.00 21.31 ? 407 TRP A O   1 
ATOM   1814 C CB  . TRP A 1 407 ? -9.644  -14.338 4.867  1.00 20.59 ? 407 TRP A CB  1 
ATOM   1815 C CG  . TRP A 1 407 ? -8.443  -14.854 4.161  1.00 20.27 ? 407 TRP A CG  1 
ATOM   1816 C CD1 . TRP A 1 407 ? -7.357  -15.439 4.727  1.00 21.18 ? 407 TRP A CD1 1 
ATOM   1817 C CD2 . TRP A 1 407 ? -8.268  -14.964 2.746  1.00 20.14 ? 407 TRP A CD2 1 
ATOM   1818 N NE1 . TRP A 1 407 ? -6.481  -15.850 3.753  1.00 21.13 ? 407 TRP A NE1 1 
ATOM   1819 C CE2 . TRP A 1 407 ? -7.010  -15.553 2.526  1.00 20.65 ? 407 TRP A CE2 1 
ATOM   1820 C CE3 . TRP A 1 407 ? -9.029  -14.568 1.641  1.00 20.52 ? 407 TRP A CE3 1 
ATOM   1821 C CZ2 . TRP A 1 407 ? -6.502  -15.772 1.254  1.00 20.98 ? 407 TRP A CZ2 1 
ATOM   1822 C CZ3 . TRP A 1 407 ? -8.539  -14.811 0.379  1.00 21.35 ? 407 TRP A CZ3 1 
ATOM   1823 C CH2 . TRP A 1 407 ? -7.282  -15.392 0.194  1.00 21.76 ? 407 TRP A CH2 1 
ATOM   1824 N N   . SER A 1 408 ? -11.661 -11.846 5.471  1.00 24.58 ? 408 SER A N   1 
ATOM   1825 C CA  . SER A 1 408 ? -13.016 -11.610 5.934  1.00 27.01 ? 408 SER A CA  1 
ATOM   1826 C C   . SER A 1 408 ? -13.857 -12.622 5.210  1.00 30.13 ? 408 SER A C   1 
ATOM   1827 O O   . SER A 1 408 ? -13.934 -12.565 3.989  1.00 30.77 ? 408 SER A O   1 
ATOM   1828 C CB  . SER A 1 408 ? -13.480 -10.202 5.573  1.00 27.50 ? 408 SER A CB  1 
ATOM   1829 O OG  . SER A 1 408 ? -14.884 -10.060 5.712  1.00 28.71 ? 408 SER A OG  1 
ATOM   1830 N N   . PRO A 1 409 ? -14.547 -13.515 5.921  1.00 32.03 ? 409 PRO A N   1 
ATOM   1831 C CA  . PRO A 1 409 ? -15.455 -14.449 5.225  1.00 33.57 ? 409 PRO A CA  1 
ATOM   1832 C C   . PRO A 1 409 ? -16.707 -13.773 4.658  1.00 35.25 ? 409 PRO A C   1 
ATOM   1833 O O   . PRO A 1 409 ? -17.308 -14.303 3.727  1.00 36.89 ? 409 PRO A O   1 
ATOM   1834 C CB  . PRO A 1 409 ? -15.828 -15.476 6.294  1.00 34.23 ? 409 PRO A CB  1 
ATOM   1835 C CG  . PRO A 1 409 ? -15.061 -15.102 7.529  1.00 34.42 ? 409 PRO A CG  1 
ATOM   1836 C CD  . PRO A 1 409 ? -14.594 -13.682 7.379  1.00 32.16 ? 409 PRO A CD  1 
ATOM   1837 N N   . HIS A 1 410 ? -17.056 -12.576 5.144  1.00 34.64 ? 410 HIS A N   1 
ATOM   1838 C CA  . HIS A 1 410 ? -18.250 -11.881 4.667  1.00 34.62 ? 410 HIS A CA  1 
ATOM   1839 C C   . HIS A 1 410 ? -18.021 -11.014 3.429  1.00 34.78 ? 410 HIS A C   1 
ATOM   1840 O O   . HIS A 1 410 ? -18.788 -11.107 2.469  1.00 34.78 ? 410 HIS A O   1 
ATOM   1841 C CB  . HIS A 1 410 ? -18.870 -11.074 5.813  1.00 34.39 ? 410 HIS A CB  1 
ATOM   1842 C CG  . HIS A 1 410 ? -19.101 -11.933 7.012  1.00 35.36 ? 410 HIS A CG  1 
ATOM   1843 N ND1 . HIS A 1 410 ? -19.955 -13.020 6.956  1.00 37.02 ? 410 HIS A ND1 1 
ATOM   1844 C CD2 . HIS A 1 410 ? -18.456 -11.949 8.198  1.00 36.06 ? 410 HIS A CD2 1 
ATOM   1845 C CE1 . HIS A 1 410 ? -19.866 -13.607 8.134  1.00 37.61 ? 410 HIS A CE1 1 
ATOM   1846 N NE2 . HIS A 1 410 ? -18.980 -12.998 8.916  1.00 37.43 ? 410 HIS A NE2 1 
ATOM   1847 N N   . TYR A 1 411 ? -16.978 -10.182 3.434  1.00 34.48 ? 411 TYR A N   1 
ATOM   1848 C CA  . TYR A 1 411 ? -16.737 -9.251  2.335  1.00 34.48 ? 411 TYR A CA  1 
ATOM   1849 C C   . TYR A 1 411 ? -15.882 -9.757  1.186  1.00 34.81 ? 411 TYR A C   1 
ATOM   1850 O O   . TYR A 1 411 ? -15.800 -9.075  0.155  1.00 36.07 ? 411 TYR A O   1 
ATOM   1851 C CB  . TYR A 1 411 ? -16.141 -7.957  2.865  1.00 34.29 ? 411 TYR A CB  1 
ATOM   1852 C CG  . TYR A 1 411 ? -17.154 -7.119  3.598  1.00 35.03 ? 411 TYR A CG  1 
ATOM   1853 C CD1 . TYR A 1 411 ? -17.944 -6.200  2.921  1.00 36.29 ? 411 TYR A CD1 1 
ATOM   1854 C CD2 . TYR A 1 411 ? -17.381 -7.298  4.952  1.00 35.68 ? 411 TYR A CD2 1 
ATOM   1855 C CE1 . TYR A 1 411 ? -18.888 -5.432  3.589  1.00 36.95 ? 411 TYR A CE1 1 
ATOM   1856 C CE2 . TYR A 1 411 ? -18.339 -6.555  5.624  1.00 36.36 ? 411 TYR A CE2 1 
ATOM   1857 C CZ  . TYR A 1 411 ? -19.079 -5.612  4.941  1.00 37.69 ? 411 TYR A CZ  1 
ATOM   1858 O OH  . TYR A 1 411 ? -20.024 -4.869  5.601  1.00 40.01 ? 411 TYR A OH  1 
ATOM   1859 N N   . LYS A 1 412 ? -15.237 -10.913 1.328  1.00 33.58 ? 412 LYS A N   1 
ATOM   1860 C CA  . LYS A 1 412 ? -14.332 -11.416 0.275  1.00 33.12 ? 412 LYS A CA  1 
ATOM   1861 C C   . LYS A 1 412 ? -13.174 -10.444 0.100  1.00 31.71 ? 412 LYS A C   1 
ATOM   1862 O O   . LYS A 1 412 ? -12.913 -9.901  -0.983 1.00 32.04 ? 412 LYS A O   1 
ATOM   1863 C CB  . LYS A 1 412 ? -15.041 -11.752 -1.060 1.00 35.07 ? 412 LYS A CB  1 
ATOM   1864 N N   . GLU A 1 413 ? -12.566 -10.152 1.234  1.00 30.01 ? 413 GLU A N   1 
ATOM   1865 C CA  . GLU A 1 413 ? -11.462 -9.239  1.361  1.00 29.02 ? 413 GLU A CA  1 
ATOM   1866 C C   . GLU A 1 413 ? -10.420 -9.838  2.268  1.00 27.86 ? 413 GLU A C   1 
ATOM   1867 O O   . GLU A 1 413 ? -10.681 -10.781 2.999  1.00 27.68 ? 413 GLU A O   1 
ATOM   1868 C CB  . GLU A 1 413 ? -11.939 -7.893  1.942  1.00 30.84 ? 413 GLU A CB  1 
ATOM   1869 C CG  . GLU A 1 413 ? -12.848 -7.102  1.014  1.00 34.05 ? 413 GLU A CG  1 
ATOM   1870 C CD  . GLU A 1 413 ? -13.535 -5.904  1.641  1.00 37.23 ? 413 GLU A CD  1 
ATOM   1871 O OE1 . GLU A 1 413 ? -13.515 -5.776  2.887  1.00 39.41 ? 413 GLU A OE1 1 
ATOM   1872 O OE2 . GLU A 1 413 ? -14.116 -5.099  0.883  1.00 36.85 ? 413 GLU A OE2 1 
ATOM   1873 N N   . LEU A 1 414 ? -9.232  -9.277  2.214  1.00 27.19 ? 414 LEU A N   1 
ATOM   1874 C CA  . LEU A 1 414 ? -8.129  -9.619  3.083  1.00 26.96 ? 414 LEU A CA  1 
ATOM   1875 C C   . LEU A 1 414 ? -7.760  -8.351  3.814  1.00 25.30 ? 414 LEU A C   1 
ATOM   1876 O O   . LEU A 1 414 ? -7.929  -7.261  3.288  1.00 25.59 ? 414 LEU A O   1 
ATOM   1877 C CB  . LEU A 1 414 ? -6.900  -10.032 2.261  1.00 28.57 ? 414 LEU A CB  1 
ATOM   1878 C CG  . LEU A 1 414 ? -6.935  -11.378 1.632  1.00 31.92 ? 414 LEU A CG  1 
ATOM   1879 C CD1 . LEU A 1 414 ? -7.481  -11.282 0.243  1.00 33.13 ? 414 LEU A CD1 1 
ATOM   1880 C CD2 . LEU A 1 414 ? -5.547  -11.949 1.578  1.00 33.13 ? 414 LEU A CD2 1 
ATOM   1881 N N   . ILE A 1 415 ? -7.201  -8.485  5.001  1.00 23.46 ? 415 ILE A N   1 
ATOM   1882 C CA  . ILE A 1 415 ? -6.659  -7.364  5.737  1.00 22.28 ? 415 ILE A CA  1 
ATOM   1883 C C   . ILE A 1 415 ? -5.272  -7.752  6.221  1.00 21.55 ? 415 ILE A C   1 
ATOM   1884 O O   . ILE A 1 415 ? -5.057  -8.858  6.699  1.00 21.63 ? 415 ILE A O   1 
ATOM   1885 C CB  . ILE A 1 415 ? -7.590  -6.845  6.848  1.00 22.44 ? 415 ILE A CB  1 
ATOM   1886 C CG1 . ILE A 1 415 ? -7.015  -5.577  7.510  1.00 23.24 ? 415 ILE A CG1 1 
ATOM   1887 C CG2 . ILE A 1 415 ? -7.874  -7.928  7.847  1.00 22.33 ? 415 ILE A CG2 1 
ATOM   1888 C CD1 . ILE A 1 415 ? -8.006  -4.891  8.458  1.00 24.41 ? 415 ILE A CD1 1 
ATOM   1889 N N   . SER A 1 416 ? -4.319  -6.874  6.038  1.00 21.20 ? 416 SER A N   1 
ATOM   1890 C CA  . SER A 1 416 ? -2.935  -7.130  6.438  1.00 20.94 ? 416 SER A CA  1 
ATOM   1891 C C   . SER A 1 416 ? -2.446  -6.039  7.364  1.00 21.04 ? 416 SER A C   1 
ATOM   1892 O O   . SER A 1 416 ? -2.902  -4.914  7.250  1.00 21.87 ? 416 SER A O   1 
ATOM   1893 C CB  . SER A 1 416 ? -2.043  -7.211  5.205  1.00 21.25 ? 416 SER A CB  1 
ATOM   1894 O OG  . SER A 1 416 ? -2.199  -6.037  4.420  1.00 22.59 ? 416 SER A OG  1 
ATOM   1895 N N   . GLY A 1 417 ? -1.508  -6.365  8.252  1.00 20.13 ? 417 GLY A N   1 
ATOM   1896 C CA  . GLY A 1 417 ? -0.921  -5.406  9.172  1.00 20.48 ? 417 GLY A CA  1 
ATOM   1897 C C   . GLY A 1 417 ? 0.509   -5.115  8.779  1.00 21.56 ? 417 GLY A C   1 
ATOM   1898 O O   . GLY A 1 417 ? 1.217   -6.003  8.293  1.00 21.56 ? 417 GLY A O   1 
ATOM   1899 N N   . HIS A 1 418 ? 0.945   -3.859  8.955  1.00 22.32 ? 418 HIS A N   1 
ATOM   1900 C CA  . HIS A 1 418 ? 2.252   -3.439  8.473  1.00 23.24 ? 418 HIS A CA  1 
ATOM   1901 C C   . HIS A 1 418 ? 3.063   -2.586  9.438  1.00 24.07 ? 418 HIS A C   1 
ATOM   1902 O O   . HIS A 1 418 ? 2.592   -2.206  10.506 1.00 23.48 ? 418 HIS A O   1 
ATOM   1903 C CB  . HIS A 1 418 ? 2.085   -2.715  7.129  1.00 24.43 ? 418 HIS A CB  1 
ATOM   1904 C CG  . HIS A 1 418 ? 1.347   -3.530  6.127  1.00 27.61 ? 418 HIS A CG  1 
ATOM   1905 N ND1 . HIS A 1 418 ? 1.991   -4.486  5.363  1.00 30.19 ? 418 HIS A ND1 1 
ATOM   1906 C CD2 . HIS A 1 418 ? 0.021   -3.581  5.874  1.00 29.17 ? 418 HIS A CD2 1 
ATOM   1907 C CE1 . HIS A 1 418 ? 1.049   -5.044  4.620  1.00 31.09 ? 418 HIS A CE1 1 
ATOM   1908 N NE2 . HIS A 1 418 ? -0.154  -4.525  4.889  1.00 30.90 ? 418 HIS A NE2 1 
ATOM   1909 N N   . GLY A 1 419 ? 4.327   -2.377  9.089  1.00 24.64 ? 419 GLY A N   1 
ATOM   1910 C CA  . GLY A 1 419 ? 5.232   -1.590  9.898  1.00 26.34 ? 419 GLY A CA  1 
ATOM   1911 C C   . GLY A 1 419 ? 5.648   -0.321  9.190  1.00 28.67 ? 419 GLY A C   1 
ATOM   1912 O O   . GLY A 1 419 ? 4.826   0.365   8.573  1.00 28.91 ? 419 GLY A O   1 
ATOM   1913 N N   . PHE A 1 420 ? 6.953   -0.019  9.231  1.00 29.79 ? 420 PHE A N   1 
ATOM   1914 C CA  . PHE A 1 420 ? 7.548   1.146   8.596  1.00 31.11 ? 420 PHE A CA  1 
ATOM   1915 C C   . PHE A 1 420 ? 7.111   1.262   7.126  1.00 31.96 ? 420 PHE A C   1 
ATOM   1916 O O   . PHE A 1 420 ? 7.091   0.248   6.456  1.00 32.12 ? 420 PHE A O   1 
ATOM   1917 C CB  . PHE A 1 420 ? 9.076   1.043   8.690  1.00 31.33 ? 420 PHE A CB  1 
ATOM   1918 C CG  . PHE A 1 420 ? 9.766   2.337   8.346  1.00 32.19 ? 420 PHE A CG  1 
ATOM   1919 C CD1 . PHE A 1 420 ? 9.817   3.374   9.259  1.00 33.15 ? 420 PHE A CD1 1 
ATOM   1920 C CD2 . PHE A 1 420 ? 10.277  2.551   7.080  1.00 32.76 ? 420 PHE A CD2 1 
ATOM   1921 C CE1 . PHE A 1 420 ? 10.393  4.584   8.924  1.00 33.71 ? 420 PHE A CE1 1 
ATOM   1922 C CE2 . PHE A 1 420 ? 10.853  3.759   6.746  1.00 33.65 ? 420 PHE A CE2 1 
ATOM   1923 C CZ  . PHE A 1 420 ? 10.913  4.765   7.668  1.00 33.66 ? 420 PHE A CZ  1 
ATOM   1924 N N   . ALA A 1 421 ? 6.663   2.443   6.657  1.00 32.35 ? 421 ALA A N   1 
ATOM   1925 C CA  . ALA A 1 421 ? 6.635   3.671   7.443  1.00 33.14 ? 421 ALA A CA  1 
ATOM   1926 C C   . ALA A 1 421 ? 5.251   4.054   7.945  1.00 33.78 ? 421 ALA A C   1 
ATOM   1927 O O   . ALA A 1 421 ? 5.161   4.853   8.872  1.00 34.06 ? 421 ALA A O   1 
ATOM   1928 C CB  . ALA A 1 421 ? 7.213   4.809   6.627  1.00 33.27 ? 421 ALA A CB  1 
ATOM   1929 N N   . GLN A 1 422 ? 4.172   3.525   7.337  1.00 33.72 ? 422 GLN A N   1 
ATOM   1930 C CA  . GLN A 1 422 ? 2.824   3.978   7.694  1.00 34.02 ? 422 GLN A CA  1 
ATOM   1931 C C   . GLN A 1 422 ? 2.187   3.307   8.898  1.00 32.80 ? 422 GLN A C   1 
ATOM   1932 O O   . GLN A 1 422 ? 1.193   3.837   9.401  1.00 33.24 ? 422 GLN A O   1 
ATOM   1933 C CB  . GLN A 1 422 ? 1.876   3.890   6.499  1.00 36.88 ? 422 GLN A CB  1 
ATOM   1934 C CG  . GLN A 1 422 ? 2.329   4.707   5.284  1.00 43.38 ? 422 GLN A CG  1 
ATOM   1935 C CD  . GLN A 1 422 ? 2.369   6.194   5.554  1.00 52.27 ? 422 GLN A CD  1 
ATOM   1936 O OE1 . GLN A 1 422 ? 1.527   6.758   6.280  1.00 54.75 ? 422 GLN A OE1 1 
ATOM   1937 N NE2 . GLN A 1 422 ? 3.353   6.875   4.957  1.00 54.11 ? 422 GLN A NE2 1 
ATOM   1938 N N   . ASN A 1 423 ? 2.708   2.137   9.344  1.00 31.05 ? 423 ASN A N   1 
ATOM   1939 C CA  . ASN A 1 423 ? 2.182   1.374   10.486 1.00 30.30 ? 423 ASN A CA  1 
ATOM   1940 C C   . ASN A 1 423 ? 0.678   1.163   10.372 1.00 29.54 ? 423 ASN A C   1 
ATOM   1941 O O   . ASN A 1 423 ? -0.077  1.305   11.351 1.00 29.72 ? 423 ASN A O   1 
ATOM   1942 C CB  . ASN A 1 423 ? 2.514   2.051   11.810 1.00 30.62 ? 423 ASN A CB  1 
ATOM   1943 C CG  . ASN A 1 423 ? 3.976   2.266   11.997 1.00 32.58 ? 423 ASN A CG  1 
ATOM   1944 O OD1 . ASN A 1 423 ? 4.778   1.355   11.807 1.00 33.03 ? 423 ASN A OD1 1 
ATOM   1945 N ND2 . ASN A 1 423 ? 4.355   3.472   12.378 1.00 33.03 ? 423 ASN A ND2 1 
ATOM   1946 N N   . GLN A 1 424 ? 0.250   0.832   9.168  1.00 28.02 ? 424 GLN A N   1 
ATOM   1947 C CA  . GLN A 1 424 ? -1.153  0.733   8.884  1.00 27.68 ? 424 GLN A CA  1 
ATOM   1948 C C   . GLN A 1 424 ? -1.657  -0.682  8.622  1.00 26.94 ? 424 GLN A C   1 
ATOM   1949 O O   . GLN A 1 424 ? -0.877  -1.629  8.481  1.00 26.66 ? 424 GLN A O   1 
ATOM   1950 C CB  . GLN A 1 424 ? -1.450  1.672   7.693  1.00 29.01 ? 424 GLN A CB  1 
ATOM   1951 C CG  . GLN A 1 424 ? -1.330  1.059   6.298  1.00 31.70 ? 424 GLN A CG  1 
ATOM   1952 C CD  . GLN A 1 424 ? 0.054   0.995   5.717  1.00 34.71 ? 424 GLN A CD  1 
ATOM   1953 O OE1 . GLN A 1 424 ? 1.030   0.639   6.392  1.00 34.48 ? 424 GLN A OE1 1 
ATOM   1954 N NE2 . GLN A 1 424 ? 0.148   1.322   4.419  1.00 34.93 ? 424 GLN A NE2 1 
ATOM   1955 N N   . LEU A 1 425 ? -2.990  -0.811  8.560  1.00 25.91 ? 425 LEU A N   1 
ATOM   1956 C CA  . LEU A 1 425 ? -3.612  -2.027  8.104  1.00 24.93 ? 425 LEU A CA  1 
ATOM   1957 C C   . LEU A 1 425 ? -4.100  -1.743  6.697  1.00 24.61 ? 425 LEU A C   1 
ATOM   1958 O O   . LEU A 1 425 ? -4.562  -0.636  6.424  1.00 24.61 ? 425 LEU A O   1 
ATOM   1959 C CB  . LEU A 1 425 ? -4.796  -2.439  8.962  1.00 24.76 ? 425 LEU A CB  1 
ATOM   1960 C CG  . LEU A 1 425 ? -4.612  -2.498  10.477 1.00 25.48 ? 425 LEU A CG  1 
ATOM   1961 C CD1 . LEU A 1 425 ? -5.791  -3.220  11.115 1.00 24.88 ? 425 LEU A CD1 1 
ATOM   1962 C CD2 . LEU A 1 425 ? -3.301  -3.146  10.878 1.00 26.12 ? 425 LEU A CD2 1 
ATOM   1963 N N   . VAL A 1 426 ? -3.998  -2.725  5.790  1.00 23.70 ? 426 VAL A N   1 
ATOM   1964 C CA  . VAL A 1 426 ? -4.506  -2.541  4.448  1.00 23.66 ? 426 VAL A CA  1 
ATOM   1965 C C   . VAL A 1 426 ? -5.603  -3.546  4.216  1.00 24.46 ? 426 VAL A C   1 
ATOM   1966 O O   . VAL A 1 426 ? -5.420  -4.733  4.486  1.00 23.82 ? 426 VAL A O   1 
ATOM   1967 C CB  . VAL A 1 426 ? -3.410  -2.640  3.357  1.00 24.00 ? 426 VAL A CB  1 
ATOM   1968 C CG1 . VAL A 1 426 ? -4.008  -2.509  1.960  1.00 23.99 ? 426 VAL A CG1 1 
ATOM   1969 C CG2 . VAL A 1 426 ? -2.334  -1.597  3.572  1.00 24.17 ? 426 VAL A CG2 1 
ATOM   1970 N N   . ILE A 1 427 ? -6.738  -3.080  3.679  1.00 25.15 ? 427 ILE A N   1 
ATOM   1971 C CA  . ILE A 1 427 ? -7.814  -3.965  3.290  1.00 25.74 ? 427 ILE A CA  1 
ATOM   1972 C C   . ILE A 1 427 ? -7.707  -4.109  1.779  1.00 25.84 ? 427 ILE A C   1 
ATOM   1973 O O   . ILE A 1 427 ? -7.580  -3.103  1.072  1.00 26.11 ? 427 ILE A O   1 
ATOM   1974 C CB  . ILE A 1 427 ? -9.190  -3.437  3.735  1.00 26.23 ? 427 ILE A CB  1 
ATOM   1975 C CG1 . ILE A 1 427 ? -9.240  -3.364  5.265  1.00 26.83 ? 427 ILE A CG1 1 
ATOM   1976 C CG2 . ILE A 1 427 ? -10.318 -4.301  3.157  1.00 26.81 ? 427 ILE A CG2 1 
ATOM   1977 C CD1 . ILE A 1 427 ? -10.507 -2.795  5.838  1.00 28.05 ? 427 ILE A CD1 1 
ATOM   1978 N N   . TRP A 1 428 ? -7.679  -5.358  1.296  1.00 25.37 ? 428 TRP A N   1 
ATOM   1979 C CA  . TRP A 1 428 ? -7.556  -5.669  -0.124 1.00 26.10 ? 428 TRP A CA  1 
ATOM   1980 C C   . TRP A 1 428 ? -8.793  -6.432  -0.585 1.00 27.36 ? 428 TRP A C   1 
ATOM   1981 O O   . TRP A 1 428 ? -9.268  -7.307  0.126  1.00 27.14 ? 428 TRP A O   1 
ATOM   1982 C CB  . TRP A 1 428 ? -6.349  -6.583  -0.380 1.00 25.48 ? 428 TRP A CB  1 
ATOM   1983 C CG  . TRP A 1 428 ? -5.080  -6.198  0.294  1.00 25.70 ? 428 TRP A CG  1 
ATOM   1984 C CD1 . TRP A 1 428 ? -4.698  -6.519  1.560  1.00 26.35 ? 428 TRP A CD1 1 
ATOM   1985 C CD2 . TRP A 1 428 ? -3.956  -5.557  -0.314 1.00 26.29 ? 428 TRP A CD2 1 
ATOM   1986 N NE1 . TRP A 1 428 ? -3.431  -6.058  1.803  1.00 26.66 ? 428 TRP A NE1 1 
ATOM   1987 C CE2 . TRP A 1 428 ? -2.941  -5.484  0.658  1.00 27.09 ? 428 TRP A CE2 1 
ATOM   1988 C CE3 . TRP A 1 428 ? -3.703  -5.046  -1.596 1.00 27.68 ? 428 TRP A CE3 1 
ATOM   1989 C CZ2 . TRP A 1 428 ? -1.704  -4.908  0.399  1.00 28.28 ? 428 TRP A CZ2 1 
ATOM   1990 C CZ3 . TRP A 1 428 ? -2.481  -4.447  -1.844 1.00 28.78 ? 428 TRP A CZ3 1 
ATOM   1991 C CH2 . TRP A 1 428 ? -1.495  -4.391  -0.855 1.00 28.81 ? 428 TRP A CH2 1 
ATOM   1992 N N   . LYS A 1 429 ? -9.262  -6.165  -1.788 1.00 28.65 ? 429 LYS A N   1 
ATOM   1993 C CA  . LYS A 1 429 ? -10.394 -6.886  -2.356 1.00 30.29 ? 429 LYS A CA  1 
ATOM   1994 C C   . LYS A 1 429 ? -9.892  -8.187  -2.933 1.00 31.55 ? 429 LYS A C   1 
ATOM   1995 O O   . LYS A 1 429 ? -8.873  -8.186  -3.579 1.00 32.03 ? 429 LYS A O   1 
ATOM   1996 C CB  . LYS A 1 429 ? -11.070 -6.073  -3.455 1.00 32.52 ? 429 LYS A CB  1 
ATOM   1997 C CG  . LYS A 1 429 ? -12.338 -6.743  -3.992 1.00 38.53 ? 429 LYS A CG  1 
ATOM   1998 C CD  . LYS A 1 429 ? -13.447 -6.818  -2.932 1.00 43.68 ? 429 LYS A CD  1 
ATOM   1999 C CE  . LYS A 1 429 ? -14.666 -7.564  -3.419 1.00 47.93 ? 429 LYS A CE  1 
ATOM   2000 N NZ  . LYS A 1 429 ? -14.506 -9.028  -3.239 1.00 50.78 ? 429 LYS A NZ  1 
ATOM   2001 N N   . TYR A 1 430 ? -10.567 -9.300  -2.673 1.00 32.00 ? 430 TYR A N   1 
ATOM   2002 C CA  . TYR A 1 430 ? -10.176 -10.591 -3.218 1.00 32.62 ? 430 TYR A CA  1 
ATOM   2003 C C   . TYR A 1 430 ? -11.217 -11.015 -4.250 1.00 33.56 ? 430 TYR A C   1 
ATOM   2004 O O   . TYR A 1 430 ? -12.410 -10.812 -4.008 1.00 33.81 ? 430 TYR A O   1 
ATOM   2005 C CB  . TYR A 1 430 ? -10.107 -11.625 -2.106 1.00 32.39 ? 430 TYR A CB  1 
ATOM   2006 C CG  . TYR A 1 430 ? -9.401  -12.880 -2.549 1.00 33.10 ? 430 TYR A CG  1 
ATOM   2007 C CD1 . TYR A 1 430 ? -8.020  -12.914 -2.680 1.00 33.98 ? 430 TYR A CD1 1 
ATOM   2008 C CD2 . TYR A 1 430 ? -10.114 -14.019 -2.886 1.00 33.77 ? 430 TYR A CD2 1 
ATOM   2009 C CE1 . TYR A 1 430 ? -7.365  -14.055 -3.107 1.00 34.80 ? 430 TYR A CE1 1 
ATOM   2010 C CE2 . TYR A 1 430 ? -9.469  -15.170 -3.309 1.00 34.68 ? 430 TYR A CE2 1 
ATOM   2011 C CZ  . TYR A 1 430 ? -8.093  -15.180 -3.429 1.00 35.67 ? 430 TYR A CZ  1 
ATOM   2012 O OH  . TYR A 1 430 ? -7.431  -16.297 -3.868 1.00 36.96 ? 430 TYR A OH  1 
ATOM   2013 N N   . PRO A 1 431 ? -10.814 -11.562 -5.420 1.00 33.52 ? 431 PRO A N   1 
ATOM   2014 C CA  . PRO A 1 431 ? -9.458  -11.956 -5.824 1.00 33.49 ? 431 PRO A CA  1 
ATOM   2015 C C   . PRO A 1 431 ? -8.616  -10.944 -6.586 1.00 33.84 ? 431 PRO A C   1 
ATOM   2016 O O   . PRO A 1 431 ? -7.487  -11.262 -6.944 1.00 33.22 ? 431 PRO A O   1 
ATOM   2017 C CB  . PRO A 1 431 ? -9.729  -13.179 -6.699 1.00 34.41 ? 431 PRO A CB  1 
ATOM   2018 C CG  . PRO A 1 431 ? -10.999 -12.801 -7.426 1.00 34.89 ? 431 PRO A CG  1 
ATOM   2019 C CD  . PRO A 1 431 ? -11.815 -12.012 -6.409 1.00 33.13 ? 431 PRO A CD  1 
ATOM   2020 N N   . THR A 1 432 ? -9.135  -9.741  -6.838 1.00 34.41 ? 432 THR A N   1 
ATOM   2021 C CA  . THR A 1 432 ? -8.401  -8.733  -7.613 1.00 34.94 ? 432 THR A CA  1 
ATOM   2022 C C   . THR A 1 432 ? -7.177  -8.173  -6.936 1.00 34.83 ? 432 THR A C   1 
ATOM   2023 O O   . THR A 1 432 ? -6.344  -7.568  -7.608 1.00 34.79 ? 432 THR A O   1 
ATOM   2024 C CB  . THR A 1 432 ? -9.313  -7.571  -7.976 1.00 36.16 ? 432 THR A CB  1 
ATOM   2025 O OG1 . THR A 1 432 ? -9.697  -6.898  -6.766 1.00 37.39 ? 432 THR A OG1 1 
ATOM   2026 C CG2 . THR A 1 432 ? -10.525 -8.020  -8.758 1.00 36.11 ? 432 THR A CG2 1 
ATOM   2027 N N   . MET A 1 433 ? -7.108  -8.298  -5.604 1.00 34.53 ? 433 MET A N   1 
ATOM   2028 C CA  . MET A 1 433 ? -6.039  -7.767  -4.761 1.00 34.60 ? 433 MET A CA  1 
ATOM   2029 C C   . MET A 1 433 ? -5.905  -6.258  -4.869 1.00 35.10 ? 433 MET A C   1 
ATOM   2030 O O   . MET A 1 433 ? -4.814  -5.730  -4.678 1.00 35.60 ? 433 MET A O   1 
ATOM   2031 C CB  . MET A 1 433 ? -4.700  -8.481  -5.005 1.00 35.01 ? 433 MET A CB  1 
ATOM   2032 C CG  . MET A 1 433 ? -4.677  -9.922  -4.511 1.00 37.06 ? 433 MET A CG  1 
ATOM   2033 S SD  . MET A 1 433 ? -5.121  -10.141 -2.751 1.00 40.47 ? 433 MET A SD  1 
ATOM   2034 C CE  . MET A 1 433 ? -3.748  -9.265  -1.947 1.00 36.42 ? 433 MET A CE  1 
ATOM   2035 N N   . ALA A 1 434 ? -6.999  -5.560  -5.188 1.00 34.90 ? 434 ALA A N   1 
ATOM   2036 C CA  . ALA A 1 434 ? -6.978  -4.109  -5.278 1.00 35.06 ? 434 ALA A CA  1 
ATOM   2037 C C   . ALA A 1 434 ? -7.049  -3.548  -3.868 1.00 35.68 ? 434 ALA A C   1 
ATOM   2038 O O   . ALA A 1 434 ? -7.749  -4.097  -3.016 1.00 35.56 ? 434 ALA A O   1 
ATOM   2039 C CB  . ALA A 1 434 ? -8.172  -3.619  -6.085 1.00 34.80 ? 434 ALA A CB  1 
ATOM   2040 N N   . LYS A 1 435 ? -6.344  -2.453  -3.621 1.00 36.08 ? 435 LYS A N   1 
ATOM   2041 C CA  . LYS A 1 435 ? -6.374  -1.798  -2.321 1.00 37.25 ? 435 LYS A CA  1 
ATOM   2042 C C   . LYS A 1 435 ? -7.755  -1.156  -2.131 1.00 37.79 ? 435 LYS A C   1 
ATOM   2043 O O   . LYS A 1 435 ? -8.213  -0.413  -2.989 1.00 38.40 ? 435 LYS A O   1 
ATOM   2044 C CB  . LYS A 1 435 ? -5.266  -0.733  -2.235 1.00 39.14 ? 435 LYS A CB  1 
ATOM   2045 C CG  . LYS A 1 435 ? -5.119  -0.127  -0.840 1.00 43.65 ? 435 LYS A CG  1 
ATOM   2046 C CD  . LYS A 1 435 ? -3.830  0.690   -0.665 1.00 48.43 ? 435 LYS A CD  1 
ATOM   2047 C CE  . LYS A 1 435 ? -2.577  -0.145  -0.799 1.00 52.34 ? 435 LYS A CE  1 
ATOM   2048 N NZ  . LYS A 1 435 ? -1.366  0.615   -0.366 1.00 54.59 ? 435 LYS A NZ  1 
ATOM   2049 N N   . VAL A 1 436 ? -8.420  -1.458  -1.037 1.00 37.60 ? 436 VAL A N   1 
ATOM   2050 C CA  . VAL A 1 436 ? -9.740  -0.921  -0.738 1.00 37.93 ? 436 VAL A CA  1 
ATOM   2051 C C   . VAL A 1 436 ? -9.624  0.237   0.243  1.00 37.10 ? 436 VAL A C   1 
ATOM   2052 O O   . VAL A 1 436 ? -10.264 1.274   0.049  1.00 38.06 ? 436 VAL A O   1 
ATOM   2053 C CB  . VAL A 1 436 ? -10.653 -2.039  -0.174 1.00 39.54 ? 436 VAL A CB  1 
ATOM   2054 C CG1 . VAL A 1 436 ? -11.945 -1.478  0.409  1.00 40.42 ? 436 VAL A CG1 1 
ATOM   2055 C CG2 . VAL A 1 436 ? -10.960 -3.060  -1.248 1.00 40.49 ? 436 VAL A CG2 1 
ATOM   2056 N N   . ALA A 1 437 ? -8.824  0.060   1.297  1.00 34.89 ? 437 ALA A N   1 
ATOM   2057 C CA  . ALA A 1 437 ? -8.698  1.045   2.356  1.00 34.14 ? 437 ALA A CA  1 
ATOM   2058 C C   . ALA A 1 437 ? -7.393  0.881   3.135  1.00 33.25 ? 437 ALA A C   1 
ATOM   2059 O O   . ALA A 1 437 ? -6.780  -0.194  3.149  1.00 33.09 ? 437 ALA A O   1 
ATOM   2060 C CB  . ALA A 1 437 ? -9.883  0.902   3.321  1.00 34.11 ? 437 ALA A CB  1 
ATOM   2061 N N   . GLU A 1 438 ? -6.984  1.949   3.802  1.00 32.53 ? 438 GLU A N   1 
ATOM   2062 C CA  . GLU A 1 438 ? -5.838  1.910   4.673  1.00 32.76 ? 438 GLU A CA  1 
ATOM   2063 C C   . GLU A 1 438 ? -6.307  2.392   6.027  1.00 32.24 ? 438 GLU A C   1 
ATOM   2064 O O   . GLU A 1 438 ? -6.941  3.439   6.130  1.00 33.07 ? 438 GLU A O   1 
ATOM   2065 C CB  . GLU A 1 438 ? -4.700  2.773   4.124  1.00 35.68 ? 438 GLU A CB  1 
ATOM   2066 C CG  . GLU A 1 438 ? -4.009  2.125   2.945  1.00 41.86 ? 438 GLU A CG  1 
ATOM   2067 C CD  . GLU A 1 438 ? -2.693  2.779   2.587  1.00 50.74 ? 438 GLU A CD  1 
ATOM   2068 O OE1 . GLU A 1 438 ? -2.730  3.840   1.919  1.00 53.35 ? 438 GLU A OE1 1 
ATOM   2069 O OE2 . GLU A 1 438 ? -1.628  2.234   2.966  1.00 51.59 ? 438 GLU A OE2 1 
ATOM   2070 N N   . LEU A 1 439 ? -6.033  1.627   7.061  1.00 31.09 ? 439 LEU A N   1 
ATOM   2071 C CA  . LEU A 1 439 ? -6.396  2.004   8.418  1.00 30.54 ? 439 LEU A CA  1 
ATOM   2072 C C   . LEU A 1 439 ? -5.170  2.512   9.140  1.00 29.97 ? 439 LEU A C   1 
ATOM   2073 O O   . LEU A 1 439 ? -4.290  1.746   9.538  1.00 29.90 ? 439 LEU A O   1 
ATOM   2074 C CB  . LEU A 1 439 ? -7.066  0.847   9.157  1.00 30.82 ? 439 LEU A CB  1 
ATOM   2075 C CG  . LEU A 1 439 ? -8.302  0.280   8.455  1.00 32.50 ? 439 LEU A CG  1 
ATOM   2076 C CD1 . LEU A 1 439 ? -8.826  -0.945  9.182  1.00 32.60 ? 439 LEU A CD1 1 
ATOM   2077 C CD2 . LEU A 1 439 ? -9.389  1.333   8.305  1.00 33.49 ? 439 LEU A CD2 1 
ATOM   2078 N N   . LYS A 1 440 ? -5.091  3.834   9.237  1.00 29.77 ? 440 LYS A N   1 
ATOM   2079 C CA  . LYS A 1 440 ? -3.999  4.561   9.860  1.00 29.83 ? 440 LYS A CA  1 
ATOM   2080 C C   . LYS A 1 440 ? -4.366  4.993   11.278 1.00 29.98 ? 440 LYS A C   1 
ATOM   2081 O O   . LYS A 1 440 ? -5.539  5.257   11.584 1.00 30.54 ? 440 LYS A O   1 
ATOM   2082 C CB  . LYS A 1 440 ? -3.609  5.755   8.981  1.00 30.73 ? 440 LYS A CB  1 
ATOM   2083 C CG  . LYS A 1 440 ? -3.077  5.322   7.620  1.00 34.47 ? 440 LYS A CG  1 
ATOM   2084 C CD  . LYS A 1 440 ? -2.935  6.494   6.632  1.00 38.46 ? 440 LYS A CD  1 
ATOM   2085 C CE  . LYS A 1 440 ? -1.866  6.247   5.602  1.00 42.40 ? 440 LYS A CE  1 
ATOM   2086 N NZ  . LYS A 1 440 ? -2.278  6.744   4.258  1.00 46.04 ? 440 LYS A NZ  1 
ATOM   2087 N N   . GLY A 1 441 ? -3.365  5.009   12.144 1.00 29.23 ? 441 GLY A N   1 
ATOM   2088 C CA  . GLY A 1 441 ? -3.569  5.382   13.531 1.00 29.83 ? 441 GLY A CA  1 
ATOM   2089 C C   . GLY A 1 441 ? -2.449  4.940   14.447 1.00 29.79 ? 441 GLY A C   1 
ATOM   2090 O O   . GLY A 1 441 ? -2.054  5.686   15.334 1.00 30.47 ? 441 GLY A O   1 
ATOM   2091 N N   . HIS A 1 442 ? -1.925  3.734   14.247 1.00 29.53 ? 442 HIS A N   1 
ATOM   2092 C CA  . HIS A 1 442 ? -0.812  3.241   15.055 1.00 29.50 ? 442 HIS A CA  1 
ATOM   2093 C C   . HIS A 1 442 ? 0.426   4.108   14.818 1.00 29.45 ? 442 HIS A C   1 
ATOM   2094 O O   . HIS A 1 442 ? 0.681   4.515   13.690 1.00 29.12 ? 442 HIS A O   1 
ATOM   2095 C CB  . HIS A 1 442 ? -0.493  1.766   14.744 1.00 29.83 ? 442 HIS A CB  1 
ATOM   2096 C CG  . HIS A 1 442 ? -1.440  0.790   15.369 1.00 31.64 ? 442 HIS A CG  1 
ATOM   2097 N ND1 . HIS A 1 442 ? -1.533  0.655   16.746 1.00 33.77 ? 442 HIS A ND1 1 
ATOM   2098 C CD2 . HIS A 1 442 ? -2.290  -0.088  14.790 1.00 32.14 ? 442 HIS A CD2 1 
ATOM   2099 C CE1 . HIS A 1 442 ? -2.426  -0.301  16.956 1.00 33.81 ? 442 HIS A CE1 1 
ATOM   2100 N NE2 . HIS A 1 442 ? -2.917  -0.766  15.811 1.00 33.58 ? 442 HIS A NE2 1 
ATOM   2101 N N   . THR A 1 443 ? 1.182   4.396   15.881 1.00 29.53 ? 443 THR A N   1 
ATOM   2102 C CA  . THR A 1 443 ? 2.395   5.206   15.753 1.00 30.17 ? 443 THR A CA  1 
ATOM   2103 C C   . THR A 1 443 ? 3.700   4.380   15.712 1.00 29.34 ? 443 THR A C   1 
ATOM   2104 O O   . THR A 1 443 ? 4.768   4.949   15.551 1.00 29.24 ? 443 THR A O   1 
ATOM   2105 C CB  . THR A 1 443 ? 2.434   6.263   16.829 1.00 32.16 ? 443 THR A CB  1 
ATOM   2106 O OG1 . THR A 1 443 ? 2.395   5.598   18.080 1.00 33.91 ? 443 THR A OG1 1 
ATOM   2107 C CG2 . THR A 1 443 ? 1.272   7.224   16.721 1.00 32.62 ? 443 THR A CG2 1 
ATOM   2108 N N   . SER A 1 444 ? 3.601   3.053   15.820 1.00 28.47 ? 444 SER A N   1 
ATOM   2109 C CA  . SER A 1 444 ? 4.716   2.119   15.713 1.00 28.22 ? 444 SER A CA  1 
ATOM   2110 C C   . SER A 1 444 ? 4.213   0.842   15.018 1.00 27.42 ? 444 SER A C   1 
ATOM   2111 O O   . SER A 1 444 ? 3.001   0.651   14.855 1.00 26.68 ? 444 SER A O   1 
ATOM   2112 C CB  . SER A 1 444 ? 5.328   1.818   17.081 1.00 29.79 ? 444 SER A CB  1 
ATOM   2113 O OG  . SER A 1 444 ? 6.007   2.964   17.570 1.00 31.78 ? 444 SER A OG  1 
ATOM   2114 N N   . ARG A 1 445 ? 5.132   -0.031  14.602 1.00 27.05 ? 445 ARG A N   1 
ATOM   2115 C CA  . ARG A 1 445 ? 4.786   -1.207  13.823 1.00 26.98 ? 445 ARG A CA  1 
ATOM   2116 C C   . ARG A 1 445 ? 3.698   -2.065  14.415 1.00 26.74 ? 445 ARG A C   1 
ATOM   2117 O O   . ARG A 1 445 ? 3.622   -2.261  15.632 1.00 26.46 ? 445 ARG A O   1 
ATOM   2118 C CB  . ARG A 1 445 ? 6.017   -2.066  13.495 1.00 28.43 ? 445 ARG A CB  1 
ATOM   2119 C CG  . ARG A 1 445 ? 6.597   -2.821  14.667 1.00 31.92 ? 445 ARG A CG  1 
ATOM   2120 C CD  . ARG A 1 445 ? 7.819   -3.622  14.260 1.00 35.68 ? 445 ARG A CD  1 
ATOM   2121 N NE  . ARG A 1 445 ? 8.397   -4.303  15.418 1.00 38.89 ? 445 ARG A NE  1 
ATOM   2122 C CZ  . ARG A 1 445 ? 9.380   -5.192  15.360 1.00 41.55 ? 445 ARG A CZ  1 
ATOM   2123 N NH1 . ARG A 1 445 ? 9.834   -5.757  16.469 1.00 41.11 ? 445 ARG A NH1 1 
ATOM   2124 N NH2 . ARG A 1 445 ? 9.923   -5.517  14.193 1.00 42.33 ? 445 ARG A NH2 1 
ATOM   2125 N N   . VAL A 1 446 ? 2.818   -2.534  13.541 1.00 25.80 ? 446 VAL A N   1 
ATOM   2126 C CA  . VAL A 1 446 ? 1.783   -3.457  13.946 1.00 25.93 ? 446 VAL A CA  1 
ATOM   2127 C C   . VAL A 1 446 ? 2.472   -4.814  14.159 1.00 26.38 ? 446 VAL A C   1 
ATOM   2128 O O   . VAL A 1 446 ? 3.361   -5.202  13.396 1.00 26.30 ? 446 VAL A O   1 
ATOM   2129 C CB  . VAL A 1 446 ? 0.675   -3.533  12.881 1.00 26.04 ? 446 VAL A CB  1 
ATOM   2130 C CG1 . VAL A 1 446 ? -0.365  -4.570  13.255 1.00 25.43 ? 446 VAL A CG1 1 
ATOM   2131 C CG2 . VAL A 1 446 ? 0.031   -2.163  12.693 1.00 26.44 ? 446 VAL A CG2 1 
ATOM   2132 N N   . LEU A 1 447 ? 2.109   -5.498  15.221 1.00 26.46 ? 447 LEU A N   1 
ATOM   2133 C CA  . LEU A 1 447 ? 2.690   -6.783  15.570 1.00 27.44 ? 447 LEU A CA  1 
ATOM   2134 C C   . LEU A 1 447 ? 1.763   -7.928  15.197 1.00 27.58 ? 447 LEU A C   1 
ATOM   2135 O O   . LEU A 1 447 ? 2.221   -8.907  14.620 1.00 28.44 ? 447 LEU A O   1 
ATOM   2136 C CB  . LEU A 1 447 ? 2.973   -6.807  17.070 1.00 27.70 ? 447 LEU A CB  1 
ATOM   2137 C CG  . LEU A 1 447 ? 3.983   -5.798  17.517 1.00 29.02 ? 447 LEU A CG  1 
ATOM   2138 C CD1 . LEU A 1 447 ? 3.955   -5.657  19.026 1.00 30.27 ? 447 LEU A CD1 1 
ATOM   2139 C CD2 . LEU A 1 447 ? 5.354   -6.211  17.068 1.00 29.45 ? 447 LEU A CD2 1 
ATOM   2140 N N   . SER A 1 448 ? 0.468   -7.804  15.497 1.00 26.86 ? 448 SER A N   1 
ATOM   2141 C CA  . SER A 1 448 ? -0.478  -8.867  15.175 1.00 27.48 ? 448 SER A CA  1 
ATOM   2142 C C   . SER A 1 448 ? -1.863  -8.363  14.911 1.00 25.55 ? 448 SER A C   1 
ATOM   2143 O O   . SER A 1 448 ? -2.259  -7.328  15.432 1.00 25.52 ? 448 SER A O   1 
ATOM   2144 C CB  . SER A 1 448 ? -0.549  -9.866  16.322 1.00 31.58 ? 448 SER A CB  1 
ATOM   2145 O OG  . SER A 1 448 ? 0.663   -10.595 16.402 1.00 37.63 ? 448 SER A OG  1 
ATOM   2146 N N   . LEU A 1 449 ? -2.612  -9.123  14.140 1.00 23.88 ? 449 LEU A N   1 
ATOM   2147 C CA  . LEU A 1 449 ? -4.009  -8.887  13.893 1.00 23.08 ? 449 LEU A CA  1 
ATOM   2148 C C   . LEU A 1 449 ? -4.763  -10.094 14.363 1.00 21.97 ? 449 LEU A C   1 
ATOM   2149 O O   . LEU A 1 449 ? -4.316  -11.230 14.174 1.00 22.62 ? 449 LEU A O   1 
ATOM   2150 C CB  . LEU A 1 449 ? -4.306  -8.749  12.398 1.00 23.24 ? 449 LEU A CB  1 
ATOM   2151 C CG  . LEU A 1 449 ? -3.672  -7.609  11.642 1.00 24.93 ? 449 LEU A CG  1 
ATOM   2152 C CD1 . LEU A 1 449 ? -4.243  -7.548  10.237 1.00 25.20 ? 449 LEU A CD1 1 
ATOM   2153 C CD2 . LEU A 1 449 ? -3.906  -6.289  12.353 1.00 25.44 ? 449 LEU A CD2 1 
ATOM   2154 N N   . THR A 1 450 ? -5.960  -9.867  14.867 1.00 20.14 ? 450 THR A N   1 
ATOM   2155 C CA  . THR A 1 450 ? -6.852  -10.961 15.210 1.00 19.35 ? 450 THR A CA  1 
ATOM   2156 C C   . THR A 1 450 ? -8.274  -10.535 14.920 1.00 18.80 ? 450 THR A C   1 
ATOM   2157 O O   . THR A 1 450 ? -8.613  -9.363  15.040 1.00 18.10 ? 450 THR A O   1 
ATOM   2158 C CB  . THR A 1 450 ? -6.600  -11.495 16.593 1.00 20.36 ? 450 THR A CB  1 
ATOM   2159 O OG1 . THR A 1 450 ? -7.363  -12.695 16.748 1.00 22.17 ? 450 THR A OG1 1 
ATOM   2160 C CG2 . THR A 1 450 ? -6.930  -10.483 17.670 1.00 20.25 ? 450 THR A CG2 1 
ATOM   2161 N N   . MET A 1 451 ? -9.094  -11.472 14.506 1.00 18.87 ? 451 MET A N   1 
ATOM   2162 C CA  . MET A 1 451 ? -10.458 -11.181 14.125 1.00 19.59 ? 451 MET A CA  1 
ATOM   2163 C C   . MET A 1 451 ? -11.451 -11.568 15.168 1.00 20.85 ? 451 MET A C   1 
ATOM   2164 O O   . MET A 1 451 ? -11.291 -12.597 15.792 1.00 21.17 ? 451 MET A O   1 
ATOM   2165 C CB  . MET A 1 451 ? -10.772 -11.868 12.798 1.00 19.92 ? 451 MET A CB  1 
ATOM   2166 C CG  . MET A 1 451 ? -12.134 -11.499 12.268 1.00 23.72 ? 451 MET A CG  1 
ATOM   2167 S SD  . MET A 1 451 ? -12.330 -11.994 10.570 1.00 30.91 ? 451 MET A SD  1 
ATOM   2168 C CE  . MET A 1 451 ? -11.408 -10.754 9.773  1.00 28.65 ? 451 MET A CE  1 
ATOM   2169 N N   . SER A 1 452 ? -12.501 -10.763 15.348 1.00 21.74 ? 452 SER A N   1 
ATOM   2170 C CA  . SER A 1 452 ? -13.590 -11.090 16.260 1.00 22.66 ? 452 SER A CA  1 
ATOM   2171 C C   . SER A 1 452 ? -14.332 -12.333 15.738 1.00 24.65 ? 452 SER A C   1 
ATOM   2172 O O   . SER A 1 452 ? -14.289 -12.624 14.543 1.00 25.17 ? 452 SER A O   1 
ATOM   2173 C CB  . SER A 1 452 ? -14.551 -9.909  16.370 1.00 23.00 ? 452 SER A CB  1 
ATOM   2174 O OG  . SER A 1 452 ? -15.236 -9.710  15.147 1.00 24.90 ? 452 SER A OG  1 
ATOM   2175 N N   . PRO A 1 453 ? -15.040 -13.063 16.613 1.00 25.98 ? 453 PRO A N   1 
ATOM   2176 C CA  . PRO A 1 453 ? -15.765 -14.261 16.146 1.00 26.64 ? 453 PRO A CA  1 
ATOM   2177 C C   . PRO A 1 453 ? -16.825 -13.971 15.092 1.00 26.97 ? 453 PRO A C   1 
ATOM   2178 O O   . PRO A 1 453 ? -17.026 -14.799 14.201 1.00 28.02 ? 453 PRO A O   1 
ATOM   2179 C CB  . PRO A 1 453 ? -16.382 -14.852 17.425 1.00 27.24 ? 453 PRO A CB  1 
ATOM   2180 C CG  . PRO A 1 453 ? -16.232 -13.822 18.476 1.00 27.41 ? 453 PRO A CG  1 
ATOM   2181 C CD  . PRO A 1 453 ? -15.213 -12.827 18.062 1.00 25.48 ? 453 PRO A CD  1 
ATOM   2182 N N   . ASP A 1 454 ? -17.476 -12.801 15.164 1.00 26.07 ? 454 ASP A N   1 
ATOM   2183 C CA  . ASP A 1 454 ? -18.486 -12.474 14.158 1.00 25.99 ? 454 ASP A CA  1 
ATOM   2184 C C   . ASP A 1 454 ? -17.889 -11.972 12.826 1.00 24.73 ? 454 ASP A C   1 
ATOM   2185 O O   . ASP A 1 454 ? -18.613 -11.860 11.842 1.00 24.14 ? 454 ASP A O   1 
ATOM   2186 C CB  . ASP A 1 454 ? -19.535 -11.511 14.714 1.00 28.21 ? 454 ASP A CB  1 
ATOM   2187 C CG  . ASP A 1 454 ? -19.035 -10.136 15.070 1.00 34.05 ? 454 ASP A CG  1 
ATOM   2188 O OD1 . ASP A 1 454 ? -17.805 -9.919  15.012 1.00 34.41 ? 454 ASP A OD1 1 
ATOM   2189 O OD2 . ASP A 1 454 ? -19.876 -9.268  15.415 1.00 37.10 ? 454 ASP A OD2 1 
ATOM   2190 N N   . GLY A 1 455 ? -16.579 -11.718 12.795 1.00 24.09 ? 455 GLY A N   1 
ATOM   2191 C CA  . GLY A 1 455 ? -15.895 -11.273 11.589 1.00 23.77 ? 455 GLY A CA  1 
ATOM   2192 C C   . GLY A 1 455 ? -15.955 -9.778  11.337 1.00 23.97 ? 455 GLY A C   1 
ATOM   2193 O O   . GLY A 1 455 ? -15.328 -9.298  10.391 1.00 24.89 ? 455 GLY A O   1 
ATOM   2194 N N   . ALA A 1 456 ? -16.670 -9.014  12.177 1.00 23.42 ? 456 ALA A N   1 
ATOM   2195 C CA  . ALA A 1 456 ? -16.827 -7.572  11.958 1.00 23.55 ? 456 ALA A CA  1 
ATOM   2196 C C   . ALA A 1 456 ? -15.637 -6.723  12.359 1.00 23.25 ? 456 ALA A C   1 
ATOM   2197 O O   . ALA A 1 456 ? -15.394 -5.671  11.770 1.00 23.86 ? 456 ALA A O   1 
ATOM   2198 C CB  . ALA A 1 456 ? -18.051 -7.073  12.711 1.00 23.48 ? 456 ALA A CB  1 
ATOM   2199 N N   . THR A 1 457 ? -14.952 -7.134  13.398 1.00 22.63 ? 457 THR A N   1 
ATOM   2200 C CA  . THR A 1 457 ? -13.893 -6.346  13.991 1.00 22.81 ? 457 THR A CA  1 
ATOM   2201 C C   . THR A 1 457 ? -12.544 -7.003  13.937 1.00 22.47 ? 457 THR A C   1 
ATOM   2202 O O   . THR A 1 457 ? -12.416 -8.199  14.175 1.00 23.28 ? 457 THR A O   1 
ATOM   2203 C CB  . THR A 1 457 ? -14.281 -6.032  15.462 1.00 24.78 ? 457 THR A CB  1 
ATOM   2204 O OG1 . THR A 1 457 ? -15.598 -5.475  15.495 1.00 26.56 ? 457 THR A OG1 1 
ATOM   2205 C CG2 . THR A 1 457 ? -13.321 -5.084  16.138 1.00 24.85 ? 457 THR A CG2 1 
ATOM   2206 N N   . VAL A 1 458 ? -11.517 -6.206  13.691 1.00 21.27 ? 458 VAL A N   1 
ATOM   2207 C CA  . VAL A 1 458 ? -10.147 -6.659  13.685 1.00 20.51 ? 458 VAL A CA  1 
ATOM   2208 C C   . VAL A 1 458 ? -9.413  -5.930  14.785 1.00 20.27 ? 458 VAL A C   1 
ATOM   2209 O O   . VAL A 1 458 ? -9.423  -4.706  14.803 1.00 20.78 ? 458 VAL A O   1 
ATOM   2210 C CB  . VAL A 1 458 ? -9.484  -6.353  12.331 1.00 21.17 ? 458 VAL A CB  1 
ATOM   2211 C CG1 . VAL A 1 458 ? -7.968  -6.593  12.385 1.00 21.77 ? 458 VAL A CG1 1 
ATOM   2212 C CG2 . VAL A 1 458 ? -10.145 -7.155  11.218 1.00 21.37 ? 458 VAL A CG2 1 
ATOM   2213 N N   . ALA A 1 459 ? -8.747  -6.655  15.668 1.00 19.35 ? 459 ALA A N   1 
ATOM   2214 C CA  . ALA A 1 459 ? -7.913  -6.058  16.679 1.00 19.96 ? 459 ALA A CA  1 
ATOM   2215 C C   . ALA A 1 459 ? -6.492  -6.077  16.153 1.00 20.50 ? 459 ALA A C   1 
ATOM   2216 O O   . ALA A 1 459 ? -6.006  -7.112  15.712 1.00 20.75 ? 459 ALA A O   1 
ATOM   2217 C CB  . ALA A 1 459 ? -7.987  -6.869  17.964 1.00 21.07 ? 459 ALA A CB  1 
ATOM   2218 N N   . SER A 1 460 ? -5.837  -4.939  16.165 1.00 20.55 ? 460 SER A N   1 
ATOM   2219 C CA  . SER A 1 460 ? -4.434  -4.851  15.805 1.00 20.87 ? 460 SER A CA  1 
ATOM   2220 C C   . SER A 1 460 ? -3.638  -4.490  17.047 1.00 20.74 ? 460 SER A C   1 
ATOM   2221 O O   . SER A 1 460 ? -3.894  -3.470  17.660 1.00 21.77 ? 460 SER A O   1 
ATOM   2222 C CB  . SER A 1 460 ? -4.213  -3.780  14.743 1.00 21.92 ? 460 SER A CB  1 
ATOM   2223 O OG  . SER A 1 460 ? -4.778  -2.547  15.154 1.00 23.53 ? 460 SER A OG  1 
ATOM   2224 N N   . ALA A 1 461 ? -2.675  -5.298  17.398 1.00 20.52 ? 461 ALA A N   1 
ATOM   2225 C CA  . ALA A 1 461 ? -1.758  -5.016  18.509 1.00 21.28 ? 461 ALA A CA  1 
ATOM   2226 C C   . ALA A 1 461 ? -0.512  -4.413  17.885 1.00 21.43 ? 461 ALA A C   1 
ATOM   2227 O O   . ALA A 1 461 ? -0.028  -4.938  16.892 1.00 21.60 ? 461 ALA A O   1 
ATOM   2228 C CB  . ALA A 1 461 ? -1.402  -6.310  19.231 1.00 21.39 ? 461 ALA A CB  1 
ATOM   2229 N N   . ALA A 1 462 ? -0.012  -3.317  18.427 1.00 21.90 ? 462 ALA A N   1 
ATOM   2230 C CA  . ALA A 1 462 ? 1.151   -2.648  17.867 1.00 22.66 ? 462 ALA A CA  1 
ATOM   2231 C C   . ALA A 1 462 ? 2.185   -2.278  18.923 1.00 23.69 ? 462 ALA A C   1 
ATOM   2232 O O   . ALA A 1 462 ? 1.879   -2.235  20.112 1.00 24.44 ? 462 ALA A O   1 
ATOM   2233 C CB  . ALA A 1 462 ? 0.705   -1.416  17.071 1.00 22.54 ? 462 ALA A CB  1 
ATOM   2234 N N   . ALA A 1 463 ? 3.420   -2.049  18.490 1.00 24.31 ? 463 ALA A N   1 
ATOM   2235 C CA  . ALA A 1 463 ? 4.537   -1.675  19.346 1.00 25.97 ? 463 ALA A CA  1 
ATOM   2236 C C   . ALA A 1 463 ? 4.358   -0.306  20.022 1.00 27.03 ? 463 ALA A C   1 
ATOM   2237 O O   . ALA A 1 463 ? 5.188   0.072   20.845 1.00 28.05 ? 463 ALA A O   1 
ATOM   2238 C CB  . ALA A 1 463 ? 5.816   -1.699  18.535 1.00 25.92 ? 463 ALA A CB  1 
ATOM   2239 N N   . ASP A 1 464 ? 3.292   0.441   19.676 1.00 26.73 ? 464 ASP A N   1 
ATOM   2240 C CA  . ASP A 1 464 ? 2.955   1.695   20.341 1.00 26.76 ? 464 ASP A CA  1 
ATOM   2241 C C   . ASP A 1 464 ? 2.134   1.459   21.628 1.00 26.57 ? 464 ASP A C   1 
ATOM   2242 O O   . ASP A 1 464 ? 1.557   2.410   22.162 1.00 26.93 ? 464 ASP A O   1 
ATOM   2243 C CB  . ASP A 1 464 ? 2.170   2.593   19.393 1.00 28.82 ? 464 ASP A CB  1 
ATOM   2244 C CG  . ASP A 1 464 ? 0.861   2.006   18.901 1.00 33.62 ? 464 ASP A CG  1 
ATOM   2245 O OD1 . ASP A 1 464 ? 0.394   1.013   19.485 1.00 34.04 ? 464 ASP A OD1 1 
ATOM   2246 O OD2 . ASP A 1 464 ? 0.283   2.569   17.964 1.00 36.52 ? 464 ASP A OD2 1 
ATOM   2247 N N   . GLU A 1 465 ? 2.041   0.194   22.089 1.00 25.65 ? 465 GLU A N   1 
ATOM   2248 C CA  . GLU A 1 465 ? 1.372   -0.212  23.309 1.00 25.20 ? 465 GLU A CA  1 
ATOM   2249 C C   . GLU A 1 465 ? -0.115  0.020   23.279 1.00 24.58 ? 465 GLU A C   1 
ATOM   2250 O O   . GLU A 1 465 ? -0.712  0.322   24.305 1.00 24.18 ? 465 GLU A O   1 
ATOM   2251 C CB  . GLU A 1 465 ? 2.025   0.416   24.535 1.00 26.72 ? 465 GLU A CB  1 
ATOM   2252 C CG  . GLU A 1 465 ? 3.484   0.031   24.627 1.00 31.76 ? 465 GLU A CG  1 
ATOM   2253 C CD  . GLU A 1 465 ? 4.169   0.611   25.837 1.00 39.22 ? 465 GLU A CD  1 
ATOM   2254 O OE1 . GLU A 1 465 ? 4.524   -0.176  26.736 1.00 41.29 ? 465 GLU A OE1 1 
ATOM   2255 O OE2 . GLU A 1 465 ? 4.315   1.851   25.912 1.00 45.58 ? 465 GLU A OE2 1 
ATOM   2256 N N   . THR A 1 466 ? -0.732  -0.196  22.123 1.00 24.13 ? 466 THR A N   1 
ATOM   2257 C CA  . THR A 1 466 ? -2.185  -0.130  22.009 1.00 24.22 ? 466 THR A CA  1 
ATOM   2258 C C   . THR A 1 466 ? -2.710  -1.330  21.226 1.00 25.17 ? 466 THR A C   1 
ATOM   2259 O O   . THR A 1 466 ? -2.005  -1.897  20.385 1.00 24.62 ? 466 THR A O   1 
ATOM   2260 C CB  . THR A 1 466 ? -2.649  1.146   21.282 1.00 24.53 ? 466 THR A CB  1 
ATOM   2261 O OG1 . THR A 1 466 ? -2.293  1.078   19.893 1.00 25.00 ? 466 THR A OG1 1 
ATOM   2262 C CG2 . THR A 1 466 ? -2.154  2.422   21.931 1.00 23.77 ? 466 THR A CG2 1 
ATOM   2263 N N   . LEU A 1 467 ? -3.969  -1.679  21.485 1.00 25.93 ? 467 LEU A N   1 
ATOM   2264 C CA  . LEU A 1 467 ? -4.709  -2.611  20.681 1.00 27.24 ? 467 LEU A CA  1 
ATOM   2265 C C   . LEU A 1 467 ? -5.825  -1.797  20.111 1.00 26.78 ? 467 LEU A C   1 
ATOM   2266 O O   . LEU A 1 467 ? -6.688  -1.350  20.863 1.00 27.18 ? 467 LEU A O   1 
ATOM   2267 C CB  . LEU A 1 467 ? -5.293  -3.774  21.464 1.00 29.13 ? 467 LEU A CB  1 
ATOM   2268 C CG  . LEU A 1 467 ? -4.576  -5.075  21.192 1.00 33.03 ? 467 LEU A CG  1 
ATOM   2269 C CD1 . LEU A 1 467 ? -3.297  -5.124  22.010 1.00 34.32 ? 467 LEU A CD1 1 
ATOM   2270 C CD2 . LEU A 1 467 ? -5.454  -6.250  21.527 1.00 34.34 ? 467 LEU A CD2 1 
ATOM   2271 N N   . ARG A 1 468 ? -5.809  -1.580  18.803 1.00 25.99 ? 468 ARG A N   1 
ATOM   2272 C CA  . ARG A 1 468 ? -6.868  -0.829  18.151 1.00 26.13 ? 468 ARG A CA  1 
ATOM   2273 C C   . ARG A 1 468 ? -7.869  -1.810  17.583 1.00 25.86 ? 468 ARG A C   1 
ATOM   2274 O O   . ARG A 1 468 ? -7.485  -2.753  16.895 1.00 26.24 ? 468 ARG A O   1 
ATOM   2275 C CB  . ARG A 1 468 ? -6.298  0.101   17.068 1.00 27.80 ? 468 ARG A CB  1 
ATOM   2276 C CG  . ARG A 1 468 ? -5.666  1.360   17.661 1.00 32.26 ? 468 ARG A CG  1 
ATOM   2277 C CD  . ARG A 1 468 ? -4.983  2.211   16.621 1.00 35.75 ? 468 ARG A CD  1 
ATOM   2278 N NE  . ARG A 1 468 ? -4.480  3.449   17.214 1.00 39.87 ? 468 ARG A NE  1 
ATOM   2279 C CZ  . ARG A 1 468 ? -4.893  4.664   16.871 1.00 43.08 ? 468 ARG A CZ  1 
ATOM   2280 N NH1 . ARG A 1 468 ? -4.375  5.735   17.456 1.00 43.62 ? 468 ARG A NH1 1 
ATOM   2281 N NH2 . ARG A 1 468 ? -5.839  4.818   15.947 1.00 42.35 ? 468 ARG A NH2 1 
ATOM   2282 N N   . LEU A 1 469 ? -9.150  -1.606  17.871 1.00 25.27 ? 469 LEU A N   1 
ATOM   2283 C CA  . LEU A 1 469 ? -10.213 -2.497  17.405 1.00 24.90 ? 469 LEU A CA  1 
ATOM   2284 C C   . LEU A 1 469 ? -10.967 -1.837  16.298 1.00 24.80 ? 469 LEU A C   1 
ATOM   2285 O O   . LEU A 1 469 ? -11.717 -0.926  16.549 1.00 25.23 ? 469 LEU A O   1 
ATOM   2286 C CB  . LEU A 1 469 ? -11.154 -2.822  18.557 1.00 24.78 ? 469 LEU A CB  1 
ATOM   2287 C CG  . LEU A 1 469 ? -10.795 -4.058  19.383 1.00 26.19 ? 469 LEU A CG  1 
ATOM   2288 C CD1 . LEU A 1 469 ? -9.372  -4.019  19.911 1.00 26.87 ? 469 LEU A CD1 1 
ATOM   2289 C CD2 . LEU A 1 469 ? -11.728 -4.195  20.520 1.00 26.43 ? 469 LEU A CD2 1 
ATOM   2290 N N   . TRP A 1 470 ? -10.759 -2.269  15.074 1.00 24.39 ? 470 TRP A N   1 
ATOM   2291 C CA  . TRP A 1 470 ? -11.362 -1.655  13.910 1.00 24.28 ? 470 TRP A CA  1 
ATOM   2292 C C   . TRP A 1 470 ? -12.591 -2.422  13.466 1.00 25.89 ? 470 TRP A C   1 
ATOM   2293 O O   . TRP A 1 470 ? -12.452 -3.564  13.051 1.00 25.85 ? 470 TRP A O   1 
ATOM   2294 C CB  . TRP A 1 470 ? -10.352 -1.678  12.767 1.00 23.89 ? 470 TRP A CB  1 
ATOM   2295 C CG  . TRP A 1 470 ? -8.973  -1.206  13.118 1.00 24.20 ? 470 TRP A CG  1 
ATOM   2296 C CD1 . TRP A 1 470 ? -7.962  -1.947  13.662 1.00 24.87 ? 470 TRP A CD1 1 
ATOM   2297 C CD2 . TRP A 1 470 ? -8.439  0.105   12.895 1.00 24.37 ? 470 TRP A CD2 1 
ATOM   2298 N NE1 . TRP A 1 470 ? -6.835  -1.177  13.801 1.00 25.24 ? 470 TRP A NE1 1 
ATOM   2299 C CE2 . TRP A 1 470 ? -7.093  0.086   13.322 1.00 25.19 ? 470 TRP A CE2 1 
ATOM   2300 C CE3 . TRP A 1 470 ? -8.964  1.291   12.366 1.00 24.71 ? 470 TRP A CE3 1 
ATOM   2301 C CZ2 . TRP A 1 470 ? -6.265  1.205   13.230 1.00 25.60 ? 470 TRP A CZ2 1 
ATOM   2302 C CZ3 . TRP A 1 470 ? -8.149  2.406   12.304 1.00 25.66 ? 470 TRP A CZ3 1 
ATOM   2303 C CH2 . TRP A 1 470 ? -6.815  2.353   12.721 1.00 25.77 ? 470 TRP A CH2 1 
ATOM   2304 N N   . ARG A 1 471 ? -13.778 -1.810  13.503 1.00 26.86 ? 471 ARG A N   1 
ATOM   2305 C CA  . ARG A 1 471 ? -14.985 -2.442  12.999 1.00 28.56 ? 471 ARG A CA  1 
ATOM   2306 C C   . ARG A 1 471 ? -14.987 -2.147  11.491 1.00 30.12 ? 471 ARG A C   1 
ATOM   2307 O O   . ARG A 1 471 ? -15.785 -1.359  10.987 1.00 31.23 ? 471 ARG A O   1 
ATOM   2308 C CB  . ARG A 1 471 ? -16.207 -1.855  13.701 1.00 30.26 ? 471 ARG A CB  1 
ATOM   2309 C CG  . ARG A 1 471 ? -17.544 -2.434  13.270 1.00 34.25 ? 471 ARG A CG  1 
ATOM   2310 C CD  . ARG A 1 471 ? -18.599 -2.170  14.329 1.00 38.83 ? 471 ARG A CD  1 
ATOM   2311 N NE  . ARG A 1 471 ? -18.618 -3.283  15.272 1.00 42.63 ? 471 ARG A NE  1 
ATOM   2312 C CZ  . ARG A 1 471 ? -19.415 -4.342  15.164 1.00 45.29 ? 471 ARG A CZ  1 
ATOM   2313 N NH1 . ARG A 1 471 ? -20.310 -4.411  14.185 1.00 46.29 ? 471 ARG A NH1 1 
ATOM   2314 N NH2 . ARG A 1 471 ? -19.337 -5.329  16.046 1.00 44.88 ? 471 ARG A NH2 1 
ATOM   2315 N N   . CYS A 1 472 ? -14.026 -2.729  10.778 1.00 30.24 ? 472 CYS A N   1 
ATOM   2316 C CA  . CYS A 1 472 ? -13.846 -2.485  9.353  1.00 31.08 ? 472 CYS A CA  1 
ATOM   2317 C C   . CYS A 1 472 ? -14.605 -3.441  8.444  1.00 32.51 ? 472 CYS A C   1 
ATOM   2318 O O   . CYS A 1 472 ? -14.581 -3.244  7.235  1.00 32.91 ? 472 CYS A O   1 
ATOM   2319 C CB  . CYS A 1 472 ? -12.364 -2.481  9.017  1.00 30.83 ? 472 CYS A CB  1 
ATOM   2320 S SG  . CYS A 1 472 ? -11.517 -4.016  9.453  1.00 30.56 ? 472 CYS A SG  1 
ATOM   2321 N N   . PHE A 1 473 ? -15.213 -4.500  9.000  1.00 33.16 ? 473 PHE A N   1 
ATOM   2322 C CA  . PHE A 1 473 ? -16.004 -5.422  8.214  1.00 34.39 ? 473 PHE A CA  1 
ATOM   2323 C C   . PHE A 1 473 ? -17.428 -5.476  8.767  1.00 37.43 ? 473 PHE A C   1 
ATOM   2324 O O   . PHE A 1 473 ? -17.936 -6.558  9.056  1.00 38.51 ? 473 PHE A O   1 
ATOM   2325 C CB  . PHE A 1 473 ? -15.379 -6.811  8.161  1.00 32.96 ? 473 PHE A CB  1 
ATOM   2326 C CG  . PHE A 1 473 ? -13.977 -6.863  7.632  1.00 32.08 ? 473 PHE A CG  1 
ATOM   2327 C CD1 . PHE A 1 473 ? -13.698 -6.499  6.326  1.00 32.22 ? 473 PHE A CD1 1 
ATOM   2328 C CD2 . PHE A 1 473 ? -12.942 -7.336  8.420  1.00 31.85 ? 473 PHE A CD2 1 
ATOM   2329 C CE1 . PHE A 1 473 ? -12.399 -6.577  5.835  1.00 32.53 ? 473 PHE A CE1 1 
ATOM   2330 C CE2 . PHE A 1 473 ? -11.651 -7.408  7.927  1.00 32.42 ? 473 PHE A CE2 1 
ATOM   2331 C CZ  . PHE A 1 473 ? -11.386 -7.039  6.636  1.00 31.88 ? 473 PHE A CZ  1 
ATOM   2332 N N   . GLU A 1 474 ? -18.065 -4.303  8.902  1.00 38.62 ? 474 GLU A N   1 
ATOM   2333 C CA  . GLU A 1 474 ? -19.461 -4.123  9.312  1.00 40.60 ? 474 GLU A CA  1 
ATOM   2334 C C   . GLU A 1 474 ? -19.872 -2.661  9.205  1.00 42.23 ? 474 GLU A C   1 
ATOM   2335 O O   . GLU A 1 474 ? -19.043 -1.774  9.408  1.00 43.20 ? 474 GLU A O   1 
ATOM   2336 C CB  . GLU A 1 474 ? -19.751 -4.648  10.721 1.00 43.15 ? 474 GLU A CB  1 
ATOM   2337 C CG  . GLU A 1 474 ? -20.408 -6.018  10.754 1.00 48.76 ? 474 GLU A CG  1 
ATOM   2338 C CD  . GLU A 1 474 ? -21.915 -6.070  10.608 1.00 56.18 ? 474 GLU A CD  1 
ATOM   2339 O OE1 . GLU A 1 474 ? -22.507 -5.072  10.137 1.00 56.80 ? 474 GLU A OE1 1 
ATOM   2340 O OE2 . GLU A 1 474 ? -22.504 -7.112  10.974 1.00 58.96 ? 474 GLU A OE2 1 
ATOM   2341 N N   . ALA B 2 2   ? -3.309  1.240   33.359 1.00 46.40 ? 2   ALA B N   1 
ATOM   2342 C CA  . ALA B 2 2   ? -4.204  0.088   33.459 1.00 47.13 ? 2   ALA B CA  1 
ATOM   2343 C C   . ALA B 2 2   ? -4.126  -0.771  32.206 1.00 47.71 ? 2   ALA B C   1 
ATOM   2344 O O   . ALA B 2 2   ? -4.403  -0.290  31.100 1.00 48.03 ? 2   ALA B O   1 
ATOM   2345 C CB  . ALA B 2 2   ? -5.637  0.551   33.666 1.00 47.29 ? 2   ALA B CB  1 
ATOM   2346 N N   . PRO B 2 3   ? -3.759  -2.051  32.358 1.00 47.33 ? 3   PRO B N   1 
ATOM   2347 C CA  . PRO B 2 3   ? -3.701  -2.926  31.186 1.00 47.29 ? 3   PRO B CA  1 
ATOM   2348 C C   . PRO B 2 3   ? -5.099  -3.179  30.623 1.00 47.84 ? 3   PRO B C   1 
ATOM   2349 O O   . PRO B 2 3   ? -6.039  -3.454  31.363 1.00 47.51 ? 3   PRO B O   1 
ATOM   2350 C CB  . PRO B 2 3   ? -3.045  -4.207  31.718 1.00 47.74 ? 3   PRO B CB  1 
ATOM   2351 C CG  . PRO B 2 3   ? -2.546  -3.873  33.090 1.00 48.15 ? 3   PRO B CG  1 
ATOM   2352 C CD  . PRO B 2 3   ? -3.406  -2.769  33.592 1.00 46.71 ? 3   PRO B CD  1 
HETATM 2353 O O   . 0JY B 2 4   ? -8.701  -2.394  28.270 1.00 49.59 ? 4   0JY B O   1 
HETATM 2354 C C   . 0JY B 2 4   ? -7.596  -2.205  28.778 1.00 49.54 ? 4   0JY B C   1 
HETATM 2355 C CA  . 0JY B 2 4   ? -6.446  -3.185  28.508 1.00 49.00 ? 4   0JY B CA  1 
HETATM 2356 N N   . 0JY B 2 4   ? -5.236  -2.982  29.308 1.00 48.27 ? 4   0JY B N   1 
HETATM 2357 C CB  . 0JY B 2 4   ? -6.942  -4.648  28.526 1.00 48.76 ? 4   0JY B CB  1 
HETATM 2358 C CAI . 0JY B 2 4   ? -6.202  -5.688  27.662 1.00 48.63 ? 4   0JY B CAI 1 
HETATM 2359 C CAB . 0JY B 2 4   ? -6.892  -7.042  27.776 1.00 48.54 ? 4   0JY B CAB 1 
HETATM 2360 C CAC . 0JY B 2 4   ? -6.197  -5.260  26.197 1.00 48.63 ? 4   0JY B CAC 1 
HETATM 2361 C CAA . 0JY B 2 4   ? -4.758  -5.850  28.126 1.00 48.71 ? 4   0JY B CAA 1 
ATOM   2362 N N   . GLY B 2 5   ? -7.321  -1.144  29.520 1.00 49.89 ? 5   GLY B N   1 
ATOM   2363 C CA  . GLY B 2 5   ? -8.321  -0.123  29.804 1.00 50.81 ? 5   GLY B CA  1 
ATOM   2364 C C   . GLY B 2 5   ? -8.467  0.866   28.661 1.00 51.37 ? 5   GLY B C   1 
ATOM   2365 O O   . GLY B 2 5   ? -7.574  0.988   27.814 1.00 51.41 ? 5   GLY B O   1 
HETATM 2366 O O   . HOH C 3 .   ? -13.607 -17.705 25.319 1.00 25.50 ? 501 HOH A O   1 
HETATM 2367 O O   . HOH C 3 .   ? 5.014   -23.055 -5.757 1.00 23.92 ? 502 HOH A O   1 
HETATM 2368 O O   . HOH C 3 .   ? 1.381   -15.391 12.964 1.00 22.26 ? 503 HOH A O   1 
HETATM 2369 O O   . HOH C 3 .   ? -1.442  -13.210 17.711 1.00 29.75 ? 504 HOH A O   1 
HETATM 2370 O O   . HOH C 3 .   ? 5.086   -11.315 26.079 1.00 21.51 ? 505 HOH A O   1 
HETATM 2371 O O   . HOH C 3 .   ? -19.162 -10.118 0.197  1.00 44.29 ? 506 HOH A O   1 
HETATM 2372 O O   . HOH C 3 .   ? 4.869   -9.396  18.938 1.00 28.98 ? 507 HOH A O   1 
HETATM 2373 O O   . HOH C 3 .   ? -6.857  -20.082 18.162 1.00 35.49 ? 508 HOH A O   1 
HETATM 2374 O O   . HOH C 3 .   ? 6.381   -27.053 -3.078 1.00 29.75 ? 509 HOH A O   1 
HETATM 2375 O O   . HOH C 3 .   ? 12.875  -18.331 1.094  1.00 31.41 ? 510 HOH A O   1 
HETATM 2376 O O   . HOH C 3 .   ? 9.204   -27.060 11.751 1.00 29.61 ? 511 HOH A O   1 
HETATM 2377 O O   . HOH C 3 .   ? -7.532  5.327   9.170  1.00 24.98 ? 512 HOH A O   1 
HETATM 2378 O O   . HOH C 3 .   ? -8.708  -17.713 7.950  1.00 22.40 ? 513 HOH A O   1 
HETATM 2379 O O   . HOH C 3 .   ? -2.242  3.416   18.505 1.00 44.96 ? 514 HOH A O   1 
HETATM 2380 O O   . HOH C 3 .   ? 5.803   -11.744 7.982  1.00 17.16 ? 515 HOH A O   1 
HETATM 2381 O O   . HOH C 3 .   ? 3.596   0.810   6.022  1.00 35.64 ? 516 HOH A O   1 
HETATM 2382 O O   . HOH C 3 .   ? -3.855  -14.754 10.538 1.00 23.62 ? 517 HOH A O   1 
HETATM 2383 O O   . HOH C 3 .   ? -13.812 1.100   13.369 1.00 30.61 ? 518 HOH A O   1 
HETATM 2384 O O   . HOH C 3 .   ? 4.394   -5.202  10.909 1.00 30.42 ? 519 HOH A O   1 
HETATM 2385 O O   . HOH C 3 .   ? 8.323   -19.557 17.610 1.00 32.25 ? 520 HOH A O   1 
HETATM 2386 O O   . HOH C 3 .   ? 11.973  -27.216 19.967 1.00 33.29 ? 521 HOH A O   1 
HETATM 2387 O O   . HOH C 3 .   ? 8.792   -18.337 1.295  1.00 19.82 ? 522 HOH A O   1 
HETATM 2388 O O   . HOH C 3 .   ? 2.044   -9.916  18.565 1.00 30.27 ? 523 HOH A O   1 
HETATM 2389 O O   . HOH C 3 .   ? 15.392  -23.555 6.512  1.00 47.11 ? 524 HOH A O   1 
HETATM 2390 O O   . HOH C 3 .   ? 0.303   -31.393 10.582 1.00 27.43 ? 525 HOH A O   1 
HETATM 2391 O O   . HOH C 3 .   ? 7.073   -27.191 24.769 1.00 26.52 ? 526 HOH A O   1 
HETATM 2392 O O   . HOH C 3 .   ? -9.631  -26.414 18.536 1.00 29.43 ? 527 HOH A O   1 
HETATM 2393 O O   . HOH C 3 .   ? -17.355 -11.182 25.459 1.00 36.78 ? 528 HOH A O   1 
HETATM 2394 O O   . HOH C 3 .   ? -12.645 0.783   10.795 1.00 34.62 ? 529 HOH A O   1 
HETATM 2395 O O   . HOH C 3 .   ? -7.263  -15.452 37.621 1.00 44.26 ? 530 HOH A O   1 
HETATM 2396 O O   . HOH C 3 .   ? 7.867   -12.335 -2.330 1.00 24.31 ? 531 HOH A O   1 
HETATM 2397 O O   . HOH C 3 .   ? 8.298   -13.173 34.409 1.00 24.00 ? 532 HOH A O   1 
HETATM 2398 O O   . HOH C 3 .   ? -7.007  -27.143 3.663  1.00 24.66 ? 533 HOH A O   1 
HETATM 2399 O O   . HOH C 3 .   ? 12.376  -18.945 -4.341 1.00 39.01 ? 534 HOH A O   1 
HETATM 2400 O O   . HOH C 3 .   ? -0.653  4.708   11.215 1.00 28.88 ? 535 HOH A O   1 
HETATM 2401 O O   . HOH C 3 .   ? -5.310  -21.383 13.887 1.00 58.08 ? 536 HOH A O   1 
HETATM 2402 O O   . HOH C 3 .   ? -2.683  1.721   12.056 1.00 23.61 ? 537 HOH A O   1 
HETATM 2403 O O   . HOH C 3 .   ? -4.033  -33.903 4.464  1.00 44.57 ? 538 HOH A O   1 
HETATM 2404 O O   . HOH C 3 .   ? 5.420   -32.201 29.355 1.00 41.09 ? 539 HOH A O   1 
HETATM 2405 O O   . HOH C 3 .   ? 0.005   -18.306 16.752 1.00 25.93 ? 540 HOH A O   1 
HETATM 2406 O O   . HOH C 3 .   ? 7.433   2.089   11.961 1.00 30.78 ? 541 HOH A O   1 
HETATM 2407 O O   . HOH C 3 .   ? -8.632  -36.088 28.510 1.00 26.79 ? 542 HOH A O   1 
HETATM 2408 O O   . HOH C 3 .   ? 3.931   -9.153  25.405 1.00 20.19 ? 543 HOH A O   1 
HETATM 2409 O O   . HOH C 3 .   ? -17.373 -7.443  16.351 1.00 37.84 ? 544 HOH A O   1 
HETATM 2410 O O   . HOH C 3 .   ? -6.827  -27.297 42.336 1.00 38.70 ? 545 HOH A O   1 
HETATM 2411 O O   . HOH C 3 .   ? 14.475  -14.282 24.785 1.00 40.02 ? 546 HOH A O   1 
HETATM 2412 O O   . HOH C 3 .   ? 11.037  -10.869 34.739 1.00 32.21 ? 547 HOH A O   1 
HETATM 2413 O O   . HOH C 3 .   ? 9.590   -4.980  24.004 1.00 33.58 ? 548 HOH A O   1 
HETATM 2414 O O   . HOH C 3 .   ? -6.351  -18.947 8.814  1.00 20.45 ? 549 HOH A O   1 
HETATM 2415 O O   . HOH C 3 .   ? -7.484  -9.586  37.296 1.00 39.63 ? 550 HOH A O   1 
HETATM 2416 O O   . HOH C 3 .   ? 8.726   -1.953  10.372 1.00 36.49 ? 551 HOH A O   1 
HETATM 2417 O O   . HOH C 3 .   ? 5.155   -35.881 25.862 1.00 29.47 ? 552 HOH A O   1 
HETATM 2418 O O   . HOH C 3 .   ? -9.535  -24.705 -2.574 1.00 48.31 ? 553 HOH A O   1 
HETATM 2419 O O   . HOH C 3 .   ? 1.502   -4.492  31.426 1.00 36.49 ? 554 HOH A O   1 
HETATM 2420 O O   . HOH C 3 .   ? -5.603  -21.660 16.912 1.00 28.15 ? 555 HOH A O   1 
HETATM 2421 O O   . HOH C 3 .   ? -3.341  -22.547 38.013 1.00 35.11 ? 556 HOH A O   1 
HETATM 2422 O O   . HOH C 3 .   ? -9.754  -26.149 15.886 1.00 35.14 ? 557 HOH A O   1 
HETATM 2423 O O   . HOH C 3 .   ? 1.762   -7.344  32.428 1.00 42.38 ? 558 HOH A O   1 
HETATM 2424 O O   . HOH C 3 .   ? 1.106   -17.694 14.016 1.00 27.08 ? 559 HOH A O   1 
HETATM 2425 O O   . HOH C 3 .   ? -1.438  -13.906 9.878  1.00 29.47 ? 560 HOH A O   1 
HETATM 2426 O O   . HOH C 3 .   ? 2.172   -20.501 34.826 1.00 36.11 ? 561 HOH A O   1 
HETATM 2427 O O   . HOH C 3 .   ? 11.659  -8.299  16.388 1.00 34.05 ? 562 HOH A O   1 
HETATM 2428 O O   . HOH C 3 .   ? 0.722   -31.833 31.837 1.00 34.89 ? 563 HOH A O   1 
HETATM 2429 O O   . HOH C 3 .   ? 16.214  -21.154 4.055  1.00 48.66 ? 564 HOH A O   1 
HETATM 2430 O O   . HOH C 3 .   ? -9.966  -14.874 9.469  1.00 37.12 ? 565 HOH A O   1 
HETATM 2431 O O   . HOH C 3 .   ? 14.638  -26.498 6.679  1.00 36.18 ? 566 HOH A O   1 
HETATM 2432 O O   . HOH C 3 .   ? -0.419  -17.071 37.492 1.00 31.47 ? 567 HOH A O   1 
HETATM 2433 O O   . HOH C 3 .   ? -8.797  -26.147 12.322 1.00 27.95 ? 568 HOH A O   1 
HETATM 2434 O O   . HOH C 3 .   ? -15.537 -3.523  3.984  1.00 40.25 ? 569 HOH A O   1 
HETATM 2435 O O   . HOH C 3 .   ? -14.518 6.503   11.743 1.00 42.99 ? 570 HOH A O   1 
HETATM 2436 O O   . HOH C 3 .   ? 8.031   -3.665  28.925 1.00 49.71 ? 571 HOH A O   1 
HETATM 2437 O O   . HOH C 3 .   ? 0.038   -27.973 35.574 1.00 37.54 ? 572 HOH A 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   . ILE A 168 ? 0.5230 0.5877 0.3779 0.1761  -0.0186 0.0477  168 ILE A N   
2    C CA  . ILE A 168 ? 0.5277 0.5791 0.3914 0.1555  -0.0157 0.0404  168 ILE A CA  
3    C C   . ILE A 168 ? 0.5498 0.5518 0.3897 0.1619  -0.0127 0.0394  168 ILE A C   
4    O O   . ILE A 168 ? 0.5721 0.5316 0.3869 0.1645  -0.0120 0.0449  168 ILE A O   
5    C CB  . ILE A 168 ? 0.5324 0.5778 0.4021 0.1308  -0.0156 0.0408  168 ILE A CB  
6    C CG1 . ILE A 168 ? 0.5243 0.6124 0.4119 0.1255  -0.0188 0.0417  168 ILE A CG1 
7    C CG2 . ILE A 168 ? 0.5298 0.5662 0.4096 0.1110  -0.0131 0.0337  168 ILE A CG2 
8    C CD1 . ILE A 168 ? 0.5368 0.6151 0.4228 0.1087  -0.0185 0.0441  168 ILE A CD1 
9    N N   . PRO A 169 ? 0.5442 0.5492 0.3897 0.1639  -0.0107 0.0324  169 PRO A N   
10   C CA  . PRO A 169 ? 0.5619 0.5181 0.3825 0.1695  -0.0083 0.0299  169 PRO A CA  
11   C C   . PRO A 169 ? 0.5620 0.4813 0.3745 0.1455  -0.0076 0.0288  169 PRO A C   
12   O O   . PRO A 169 ? 0.5480 0.4868 0.3808 0.1241  -0.0080 0.0261  169 PRO A O   
13   C CB  . PRO A 169 ? 0.5622 0.5392 0.3954 0.1731  -0.0065 0.0218  169 PRO A CB  
14   C CG  . PRO A 169 ? 0.5428 0.5793 0.4038 0.1762  -0.0077 0.0222  169 PRO A CG  
15   C CD  . PRO A 169 ? 0.5159 0.5668 0.3881 0.1609  -0.0105 0.0264  169 PRO A CD  
16   N N   . SER A 170 ? 0.5738 0.4402 0.3559 0.1489  -0.0065 0.0312  170 SER A N   
17   C CA  . SER A 170 ? 0.5816 0.4130 0.3549 0.1248  -0.0058 0.0302  170 SER A CA  
18   C C   . SER A 170 ? 0.5727 0.3923 0.3471 0.1143  -0.0053 0.0202  170 SER A C   
19   O O   . SER A 170 ? 0.5723 0.3775 0.3479 0.0913  -0.0054 0.0177  170 SER A O   
20   C CB  . SER A 170 ? 0.6314 0.4092 0.3704 0.1294  -0.0047 0.0373  170 SER A CB  
21   O OG  . SER A 170 ? 0.6960 0.4402 0.4085 0.1519  -0.0037 0.0358  170 SER A OG  
22   N N   . LEU A 171 ? 0.5598 0.3896 0.3347 0.1311  -0.0047 0.0145  171 LEU A N   
23   C CA  . LEU A 171 ? 0.5667 0.3890 0.3416 0.1245  -0.0043 0.0050  171 LEU A CA  
24   C C   . LEU A 171 ? 0.5374 0.4130 0.3442 0.1213  -0.0042 0.0008  171 LEU A C   
25   O O   . LEU A 171 ? 0.5336 0.4479 0.3564 0.1331  -0.0039 0.0039  171 LEU A O   
26   C CB  . LEU A 171 ? 0.5909 0.3797 0.3373 0.1476  -0.0027 0.0016  171 LEU A CB  
27   C CG  . LEU A 171 ? 0.6448 0.3734 0.3539 0.1541  -0.0023 0.0056  171 LEU A CG  
28   C CD1 . LEU A 171 ? 0.6626 0.3611 0.3438 0.1805  -0.0004 0.0016  171 LEU A CD1 
29   C CD2 . LEU A 171 ? 0.6724 0.3632 0.3706 0.1256  -0.0034 0.0033  171 LEU A CD2 
30   N N   . PRO A 172 ? 0.5154 0.3937 0.3309 0.1048  -0.0046 -0.0059 172 PRO A N   
31   C CA  . PRO A 172 ? 0.4890 0.4125 0.3308 0.1028  -0.0038 -0.0094 172 PRO A CA  
32   C C   . PRO A 172 ? 0.4923 0.4263 0.3290 0.1259  -0.0014 -0.0123 172 PRO A C   
33   O O   . PRO A 172 ? 0.5118 0.4121 0.3229 0.1406  -0.0006 -0.0142 172 PRO A O   
34   C CB  . PRO A 172 ? 0.4955 0.4099 0.3401 0.0826  -0.0050 -0.0156 172 PRO A CB  
35   C CG  . PRO A 172 ? 0.5260 0.3898 0.3422 0.0795  -0.0062 -0.0179 172 PRO A CG  
36   C CD  . PRO A 172 ? 0.5208 0.3609 0.3206 0.0884  -0.0058 -0.0109 172 PRO A CD  
37   N N   . ASP A 173 ? 0.4700 0.4496 0.3295 0.1297  0.0002  -0.0124 173 ASP A N   
38   C CA  . ASP A 173 ? 0.4763 0.4714 0.3332 0.1501  0.0034  -0.0151 173 ASP A CA  
39   C C   . ASP A 173 ? 0.4853 0.4663 0.3342 0.1459  0.0047  -0.0231 173 ASP A C   
40   O O   . ASP A 173 ? 0.4997 0.4742 0.3345 0.1640  0.0074  -0.0267 173 ASP A O   
41   C CB  . ASP A 173 ? 0.4864 0.5369 0.3699 0.1542  0.0050  -0.0119 173 ASP A CB  
42   C CG  . ASP A 173 ? 0.5825 0.6487 0.4667 0.1702  0.0041  -0.0054 173 ASP A CG  
43   O OD1 . ASP A 173 ? 0.6076 0.6518 0.4827 0.1671  0.0013  -0.0012 173 ASP A OD1 
44   O OD2 . ASP A 173 ? 0.6053 0.7086 0.4996 0.1854  0.0062  -0.0041 173 ASP A OD2 
45   N N   . ARG A 174 ? 0.4780 0.4552 0.3346 0.1236  0.0027  -0.0260 174 ARG A N   
46   C CA  . ARG A 174 ? 0.4897 0.4538 0.3378 0.1183  0.0029  -0.0335 174 ARG A CA  
47   C C   . ARG A 174 ? 0.4830 0.4241 0.3284 0.0954  -0.0012 -0.0358 174 ARG A C   
48   O O   . ARG A 174 ? 0.4651 0.4153 0.3246 0.0813  -0.0029 -0.0312 174 ARG A O   
49   C CB  . ARG A 174 ? 0.5021 0.5077 0.3715 0.1158  0.0056  -0.0343 174 ARG A CB  
50   C CG  . ARG A 174 ? 0.5629 0.5948 0.4346 0.1364  0.0105  -0.0337 174 ARG A CG  
51   C CD  . ARG A 174 ? 0.6337 0.6673 0.4984 0.1400  0.0132  -0.0397 174 ARG A CD  
52   N NE  . ARG A 174 ? 0.6747 0.7505 0.5537 0.1511  0.0188  -0.0372 174 ARG A NE  
53   C CZ  . ARG A 174 ? 0.7150 0.8041 0.5932 0.1540  0.0227  -0.0404 174 ARG A CZ  
54   N NH1 . ARG A 174 ? 0.7292 0.7925 0.5920 0.1479  0.0209  -0.0467 174 ARG A NH1 
55   N NH2 . ARG A 174 ? 0.7047 0.8347 0.5970 0.1625  0.0284  -0.0371 174 ARG A NH2 
56   N N   . ILE A 175 ? 0.4911 0.4055 0.3190 0.0915  -0.0028 -0.0431 175 ILE A N   
57   C CA  . ILE A 175 ? 0.5046 0.4050 0.3323 0.0690  -0.0070 -0.0461 175 ILE A CA  
58   C C   . ILE A 175 ? 0.5098 0.4196 0.3375 0.0664  -0.0075 -0.0528 175 ILE A C   
59   O O   . ILE A 175 ? 0.5277 0.4193 0.3352 0.0785  -0.0066 -0.0590 175 ILE A O   
60   C CB  . ILE A 175 ? 0.5466 0.3986 0.3485 0.0622  -0.0100 -0.0486 175 ILE A CB  
61   C CG1 . ILE A 175 ? 0.5736 0.4134 0.3721 0.0663  -0.0090 -0.0407 175 ILE A CG1 
62   C CG2 . ILE A 175 ? 0.5519 0.4001 0.3585 0.0369  -0.0144 -0.0517 175 ILE A CG2 
63   C CD1 . ILE A 175 ? 0.6167 0.4048 0.3865 0.0613  -0.0107 -0.0419 175 ILE A CD1 
64   N N   . LEU A 176 ? 0.4890 0.4273 0.3381 0.0528  -0.0085 -0.0514 176 LEU A N   
65   C CA  . LEU A 176 ? 0.4826 0.4326 0.3328 0.0497  -0.0092 -0.0565 176 LEU A CA  
66   C C   . LEU A 176 ? 0.4776 0.4119 0.3224 0.0307  -0.0152 -0.0609 176 LEU A C   
67   O O   . LEU A 176 ? 0.4656 0.4013 0.3206 0.0166  -0.0173 -0.0572 176 LEU A O   
68   C CB  . LEU A 176 ? 0.4689 0.4605 0.3452 0.0476  -0.0064 -0.0511 176 LEU A CB  
69   C CG  . LEU A 176 ? 0.4815 0.4974 0.3698 0.0606  -0.0010 -0.0455 176 LEU A CG  
70   C CD1 . LEU A 176 ? 0.4685 0.5187 0.3799 0.0535  0.0012  -0.0408 176 LEU A CD1 
71   C CD2 . LEU A 176 ? 0.4992 0.5135 0.3738 0.0797  0.0029  -0.0487 176 LEU A CD2 
72   N N   . ASP A 177 ? 0.4903 0.4122 0.3193 0.0299  -0.0178 -0.0689 177 ASP A N   
73   C CA  . ASP A 177 ? 0.4963 0.4098 0.3218 0.0108  -0.0242 -0.0736 177 ASP A CA  
74   C C   . ASP A 177 ? 0.4659 0.4179 0.3171 0.0020  -0.0249 -0.0692 177 ASP A C   
75   O O   . ASP A 177 ? 0.4525 0.4290 0.3141 0.0110  -0.0214 -0.0664 177 ASP A O   
76   C CB  . ASP A 177 ? 0.5525 0.4428 0.3524 0.0123  -0.0277 -0.0843 177 ASP A CB  
77   C CG  . ASP A 177 ? 0.6605 0.5325 0.4508 -0.0089 -0.0352 -0.0903 177 ASP A CG  
78   O OD1 . ASP A 177 ? 0.6719 0.5560 0.4790 -0.0249 -0.0374 -0.0855 177 ASP A OD1 
79   O OD2 . ASP A 177 ? 0.7171 0.5639 0.4827 -0.0100 -0.0389 -0.1002 177 ASP A OD2 
80   N N   . ALA A 178 ? 0.4528 0.4100 0.3141 -0.0149 -0.0288 -0.0676 178 ALA A N   
81   C CA  . ALA A 178 ? 0.4250 0.4156 0.3081 -0.0225 -0.0299 -0.0637 178 ALA A CA  
82   C C   . ALA A 178 ? 0.4164 0.4057 0.2949 -0.0384 -0.0371 -0.0694 178 ALA A C   
83   O O   . ALA A 178 ? 0.4088 0.4074 0.2988 -0.0523 -0.0395 -0.0668 178 ALA A O   
84   C CB  . ALA A 178 ? 0.4157 0.4200 0.3181 -0.0267 -0.0271 -0.0555 178 ALA A CB  
85   N N   . PRO A 179 ? 0.4215 0.4003 0.2823 -0.0369 -0.0408 -0.0775 179 PRO A N   
86   C CA  . PRO A 179 ? 0.4240 0.4035 0.2798 -0.0531 -0.0487 -0.0838 179 PRO A CA  
87   C C   . PRO A 179 ? 0.4045 0.4226 0.2826 -0.0589 -0.0509 -0.0792 179 PRO A C   
88   O O   . PRO A 179 ? 0.3902 0.4296 0.2792 -0.0474 -0.0471 -0.0742 179 PRO A O   
89   C CB  . PRO A 179 ? 0.4411 0.4047 0.2732 -0.0462 -0.0514 -0.0932 179 PRO A CB  
90   C CG  . PRO A 179 ? 0.4426 0.4146 0.2763 -0.0256 -0.0442 -0.0893 179 PRO A CG  
91   C CD  . PRO A 179 ? 0.4189 0.3884 0.2640 -0.0203 -0.0379 -0.0815 179 PRO A CD  
92   N N   . GLU A 180 ? 0.4016 0.4287 0.2867 -0.0766 -0.0563 -0.0802 180 GLU A N   
93   C CA  . GLU A 180 ? 0.3923 0.4573 0.2976 -0.0816 -0.0590 -0.0763 180 GLU A CA  
94   C C   . GLU A 180 ? 0.3788 0.4643 0.3059 -0.0750 -0.0528 -0.0662 180 GLU A C   
95   O O   . GLU A 180 ? 0.3753 0.4904 0.3166 -0.0731 -0.0536 -0.0625 180 GLU A O   
96   C CB  . GLU A 180 ? 0.4323 0.5142 0.3330 -0.0742 -0.0628 -0.0796 180 GLU A CB  
97   C CG  . GLU A 180 ? 0.5446 0.6108 0.4235 -0.0818 -0.0703 -0.0907 180 GLU A CG  
98   C CD  . GLU A 180 ? 0.7002 0.7923 0.5784 -0.0772 -0.0755 -0.0928 180 GLU A CD  
99   O OE1 . GLU A 180 ? 0.7205 0.8438 0.6137 -0.0852 -0.0804 -0.0906 180 GLU A OE1 
100  O OE2 . GLU A 180 ? 0.7577 0.8409 0.6206 -0.0644 -0.0742 -0.0958 180 GLU A OE2 
101  N N   . ILE A 181 ? 0.3696 0.4396 0.2983 -0.0716 -0.0468 -0.0619 181 ILE A N   
102  C CA  . ILE A 181 ? 0.3519 0.4398 0.2996 -0.0674 -0.0415 -0.0534 181 ILE A CA  
103  C C   . ILE A 181 ? 0.3464 0.4565 0.3088 -0.0808 -0.0443 -0.0512 181 ILE A C   
104  O O   . ILE A 181 ? 0.3479 0.4508 0.3057 -0.0960 -0.0482 -0.0545 181 ILE A O   
105  C CB  . ILE A 181 ? 0.3488 0.4179 0.2947 -0.0621 -0.0357 -0.0498 181 ILE A CB  
106  C CG1 . ILE A 181 ? 0.3440 0.4326 0.3076 -0.0561 -0.0305 -0.0422 181 ILE A CG1 
107  C CG2 . ILE A 181 ? 0.3608 0.4097 0.2996 -0.0747 -0.0372 -0.0508 181 ILE A CG2 
108  C CD1 . ILE A 181 ? 0.3635 0.4400 0.3256 -0.0471 -0.0251 -0.0389 181 ILE A CD1 
109  N N   . ARG A 182 ? 0.3323 0.4701 0.3103 -0.0752 -0.0427 -0.0462 182 ARG A N   
110  C CA  . ARG A 182 ? 0.3232 0.4879 0.3158 -0.0842 -0.0448 -0.0439 182 ARG A CA  
111  C C   . ARG A 182 ? 0.3170 0.4785 0.3168 -0.0920 -0.0410 -0.0398 182 ARG A C   
112  O O   . ARG A 182 ? 0.3139 0.4715 0.3182 -0.0837 -0.0350 -0.0350 182 ARG A O   
113  C CB  . ARG A 182 ? 0.3363 0.5274 0.3404 -0.0723 -0.0433 -0.0394 182 ARG A CB  
114  C CG  . ARG A 182 ? 0.3858 0.6090 0.4019 -0.0790 -0.0477 -0.0388 182 ARG A CG  
115  C CD  . ARG A 182 ? 0.4228 0.6681 0.4439 -0.0651 -0.0479 -0.0357 182 ARG A CD  
116  N NE  . ARG A 182 ? 0.4255 0.7058 0.4584 -0.0702 -0.0527 -0.0353 182 ARG A NE  
117  C CZ  . ARG A 182 ? 0.3897 0.6872 0.4199 -0.0740 -0.0606 -0.0394 182 ARG A CZ  
118  N NH1 . ARG A 182 ? 0.3685 0.6491 0.3830 -0.0723 -0.0643 -0.0444 182 ARG A NH1 
119  N NH2 . ARG A 182 ? 0.3683 0.7025 0.4115 -0.0784 -0.0649 -0.0385 182 ARG A NH2 
120  N N   . ASN A 183 ? 0.3134 0.4764 0.3133 -0.1091 -0.0443 -0.0416 183 ASN A N   
121  C CA  . ASN A 183 ? 0.3171 0.4773 0.3224 -0.1180 -0.0403 -0.0370 183 ASN A CA  
122  C C   . ASN A 183 ? 0.3062 0.5028 0.3313 -0.1171 -0.0379 -0.0317 183 ASN A C   
123  O O   . ASN A 183 ? 0.3016 0.5185 0.3352 -0.1311 -0.0397 -0.0310 183 ASN A O   
124  C CB  . ASN A 183 ? 0.3340 0.4774 0.3292 -0.1381 -0.0437 -0.0403 183 ASN A CB  
125  C CG  . ASN A 183 ? 0.3740 0.5070 0.3701 -0.1461 -0.0386 -0.0346 183 ASN A CG  
126  O OD1 . ASN A 183 ? 0.3762 0.5107 0.3781 -0.1355 -0.0327 -0.0290 183 ASN A OD1 
127  N ND2 . ASN A 183 ? 0.3902 0.5106 0.3785 -0.1655 -0.0407 -0.0360 183 ASN A ND2 
128  N N   . ASP A 184 ? 0.2964 0.5017 0.3280 -0.1006 -0.0338 -0.0282 184 ASP A N   
129  C CA  . ASP A 184 ? 0.2860 0.5212 0.3332 -0.0951 -0.0307 -0.0235 184 ASP A CA  
130  C C   . ASP A 184 ? 0.2940 0.5161 0.3410 -0.0866 -0.0238 -0.0194 184 ASP A C   
131  O O   . ASP A 184 ? 0.3060 0.5140 0.3476 -0.0749 -0.0218 -0.0195 184 ASP A O   
132  C CB  . ASP A 184 ? 0.3036 0.5577 0.3545 -0.0824 -0.0328 -0.0238 184 ASP A CB  
133  C CG  . ASP A 184 ? 0.3557 0.6419 0.4209 -0.0758 -0.0304 -0.0195 184 ASP A CG  
134  O OD1 . ASP A 184 ? 0.3598 0.6446 0.4291 -0.0711 -0.0242 -0.0157 184 ASP A OD1 
135  O OD2 . ASP A 184 ? 0.3778 0.6912 0.4491 -0.0741 -0.0348 -0.0201 184 ASP A OD2 
136  N N   . TYR A 185 ? 0.2761 0.5043 0.3288 -0.0933 -0.0202 -0.0158 185 TYR A N   
137  C CA  . TYR A 185 ? 0.2807 0.4981 0.3324 -0.0876 -0.0142 -0.0122 185 TYR A CA  
138  C C   . TYR A 185 ? 0.2729 0.4957 0.3279 -0.0718 -0.0107 -0.0109 185 TYR A C   
139  O O   . TYR A 185 ? 0.2855 0.4920 0.3355 -0.0660 -0.0075 -0.0100 185 TYR A O   
140  C CB  . TYR A 185 ? 0.2785 0.5098 0.3368 -0.0977 -0.0109 -0.0083 185 TYR A CB  
141  C CG  . TYR A 185 ? 0.3068 0.5264 0.3618 -0.0936 -0.0052 -0.0046 185 TYR A CG  
142  C CD1 . TYR A 185 ? 0.3366 0.5283 0.3798 -0.0978 -0.0048 -0.0038 185 TYR A CD1 
143  C CD2 . TYR A 185 ? 0.3150 0.5512 0.3771 -0.0847 -0.0004 -0.0022 185 TYR A CD2 
144  C CE1 . TYR A 185 ? 0.3531 0.5365 0.3926 -0.0935 -0.0003 -0.0003 185 TYR A CE1 
145  C CE2 . TYR A 185 ? 0.3307 0.5568 0.3883 -0.0814 0.0042  0.0004  185 TYR A CE2 
146  C CZ  . TYR A 185 ? 0.3577 0.5589 0.4046 -0.0860 0.0039  0.0014  185 TYR A CZ  
147  O OH  . TYR A 185 ? 0.3920 0.5855 0.4340 -0.0821 0.0077  0.0041  185 TYR A OH  
148  N N   . TYR A 186 ? 0.2491 0.4940 0.3114 -0.0648 -0.0113 -0.0107 186 TYR A N   
149  C CA  . TYR A 186 ? 0.2394 0.4865 0.3027 -0.0501 -0.0074 -0.0090 186 TYR A CA  
150  C C   . TYR A 186 ? 0.2239 0.4538 0.2791 -0.0412 -0.0080 -0.0104 186 TYR A C   
151  O O   . TYR A 186 ? 0.2246 0.4491 0.2776 -0.0312 -0.0042 -0.0091 186 TYR A O   
152  C CB  . TYR A 186 ? 0.2339 0.5109 0.3065 -0.0440 -0.0070 -0.0073 186 TYR A CB  
153  C CG  . TYR A 186 ? 0.2474 0.5460 0.3294 -0.0532 -0.0053 -0.0054 186 TYR A CG  
154  C CD1 . TYR A 186 ? 0.2615 0.5586 0.3439 -0.0517 0.0007  -0.0031 186 TYR A CD1 
155  C CD2 . TYR A 186 ? 0.2531 0.5719 0.3420 -0.0657 -0.0098 -0.0061 186 TYR A CD2 
156  C CE1 . TYR A 186 ? 0.2661 0.5828 0.3561 -0.0609 0.0031  -0.0006 186 TYR A CE1 
157  C CE2 . TYR A 186 ? 0.2575 0.5968 0.3550 -0.0767 -0.0076 -0.0037 186 TYR A CE2 
158  C CZ  . TYR A 186 ? 0.2692 0.6081 0.3675 -0.0737 -0.0007 -0.0005 186 TYR A CZ  
159  O OH  . TYR A 186 ? 0.2735 0.6343 0.3798 -0.0844 0.0023  0.0026  186 TYR A OH  
160  N N   . LEU A 187 ? 0.1993 0.4194 0.2487 -0.0452 -0.0122 -0.0132 187 LEU A N   
161  C CA  . LEU A 187 ? 0.1939 0.4004 0.2356 -0.0373 -0.0123 -0.0141 187 LEU A CA  
162  C C   . LEU A 187 ? 0.2018 0.3869 0.2375 -0.0368 -0.0093 -0.0143 187 LEU A C   
163  O O   . LEU A 187 ? 0.2152 0.3923 0.2499 -0.0433 -0.0091 -0.0146 187 LEU A O   
164  C CB  . LEU A 187 ? 0.1834 0.3912 0.2202 -0.0401 -0.0179 -0.0173 187 LEU A CB  
165  C CG  . LEU A 187 ? 0.1781 0.4111 0.2211 -0.0414 -0.0223 -0.0176 187 LEU A CG  
166  C CD1 . LEU A 187 ? 0.1870 0.4188 0.2227 -0.0446 -0.0285 -0.0217 187 LEU A CD1 
167  C CD2 . LEU A 187 ? 0.1650 0.4130 0.2124 -0.0283 -0.0197 -0.0136 187 LEU A CD2 
168  N N   . ASN A 188 ? 0.1885 0.3655 0.2197 -0.0293 -0.0071 -0.0137 188 ASN A N   
169  C CA  . ASN A 188 ? 0.1848 0.3475 0.2121 -0.0286 -0.0044 -0.0137 188 ASN A CA  
170  C C   . ASN A 188 ? 0.1851 0.3414 0.2055 -0.0254 -0.0056 -0.0152 188 ASN A C   
171  O O   . ASN A 188 ? 0.1731 0.3287 0.1910 -0.0199 -0.0033 -0.0136 188 ASN A O   
172  C CB  . ASN A 188 ? 0.1912 0.3526 0.2200 -0.0245 0.0001  -0.0116 188 ASN A CB  
173  C CG  . ASN A 188 ? 0.2299 0.3965 0.2635 -0.0272 0.0015  -0.0109 188 ASN A CG  
174  O OD1 . ASN A 188 ? 0.2509 0.4126 0.2844 -0.0307 0.0024  -0.0110 188 ASN A OD1 
175  N ND2 . ASN A 188 ? 0.2196 0.3979 0.2569 -0.0245 0.0020  -0.0098 188 ASN A ND2 
176  N N   . LEU A 189 ? 0.1939 0.3440 0.2095 -0.0289 -0.0088 -0.0182 189 LEU A N   
177  C CA  . LEU A 189 ? 0.2023 0.3472 0.2095 -0.0256 -0.0105 -0.0206 189 LEU A CA  
178  C C   . LEU A 189 ? 0.2116 0.3469 0.2134 -0.0211 -0.0078 -0.0210 189 LEU A C   
179  O O   . LEU A 189 ? 0.2137 0.3458 0.2076 -0.0172 -0.0084 -0.0231 189 LEU A O   
180  C CB  . LEU A 189 ? 0.2150 0.3569 0.2171 -0.0319 -0.0160 -0.0248 189 LEU A CB  
181  C CG  . LEU A 189 ? 0.2273 0.3853 0.2364 -0.0374 -0.0193 -0.0246 189 LEU A CG  
182  C CD1 . LEU A 189 ? 0.2337 0.3878 0.2383 -0.0478 -0.0246 -0.0289 189 LEU A CD1 
183  C CD2 . LEU A 189 ? 0.2313 0.4024 0.2409 -0.0305 -0.0201 -0.0232 189 LEU A CD2 
184  N N   . VAL A 190 ? 0.2150 0.3482 0.2207 -0.0211 -0.0048 -0.0192 190 VAL A N   
185  C CA  . VAL A 190 ? 0.2280 0.3574 0.2301 -0.0160 -0.0023 -0.0194 190 VAL A CA  
186  C C   . VAL A 190 ? 0.2173 0.3539 0.2263 -0.0157 0.0017  -0.0163 190 VAL A C   
187  O O   . VAL A 190 ? 0.2034 0.3423 0.2181 -0.0195 0.0022  -0.0149 190 VAL A O   
188  C CB  . VAL A 190 ? 0.2569 0.3744 0.2523 -0.0151 -0.0042 -0.0216 190 VAL A CB  
189  C CG1 . VAL A 190 ? 0.2774 0.3836 0.2627 -0.0170 -0.0083 -0.0258 190 VAL A CG1 
190  C CG2 . VAL A 190 ? 0.2660 0.3817 0.2658 -0.0194 -0.0044 -0.0196 190 VAL A CG2 
191  N N   . ASP A 191 ? 0.2132 0.3541 0.2211 -0.0117 0.0047  -0.0156 191 ASP A N   
192  C CA  . ASP A 191 ? 0.2167 0.3656 0.2308 -0.0135 0.0083  -0.0132 191 ASP A CA  
193  C C   . ASP A 191 ? 0.2167 0.3737 0.2301 -0.0089 0.0109  -0.0130 191 ASP A C   
194  O O   . ASP A 191 ? 0.2222 0.3791 0.2299 -0.0042 0.0119  -0.0136 191 ASP A O   
195  C CB  . ASP A 191 ? 0.2386 0.3882 0.2544 -0.0172 0.0109  -0.0108 191 ASP A CB  
196  C CG  . ASP A 191 ? 0.2962 0.4495 0.3172 -0.0225 0.0133  -0.0096 191 ASP A CG  
197  O OD1 . ASP A 191 ? 0.2961 0.4536 0.3208 -0.0235 0.0120  -0.0107 191 ASP A OD1 
198  O OD2 . ASP A 191 ? 0.3383 0.4890 0.3579 -0.0256 0.0164  -0.0077 191 ASP A OD2 
199  N N   . TRP A 192 ? 0.2097 0.3759 0.2288 -0.0096 0.0118  -0.0122 192 TRP A N   
200  C CA  . TRP A 192 ? 0.2142 0.3941 0.2348 -0.0045 0.0143  -0.0116 192 TRP A CA  
201  C C   . TRP A 192 ? 0.2184 0.4120 0.2462 -0.0119 0.0183  -0.0091 192 TRP A C   
202  O O   . TRP A 192 ? 0.2224 0.4177 0.2552 -0.0194 0.0177  -0.0088 192 TRP A O   
203  C CB  . TRP A 192 ? 0.2103 0.3935 0.2321 0.0005  0.0119  -0.0122 192 TRP A CB  
204  C CG  . TRP A 192 ? 0.2136 0.4066 0.2328 0.0115  0.0133  -0.0125 192 TRP A CG  
205  C CD1 . TRP A 192 ? 0.2177 0.4281 0.2398 0.0144  0.0177  -0.0114 192 TRP A CD1 
206  C CD2 . TRP A 192 ? 0.2186 0.4033 0.2301 0.0223  0.0110  -0.0137 192 TRP A CD2 
207  N NE1 . TRP A 192 ? 0.2187 0.4354 0.2366 0.0276  0.0182  -0.0122 192 TRP A NE1 
208  C CE2 . TRP A 192 ? 0.2235 0.4229 0.2340 0.0332  0.0140  -0.0136 192 TRP A CE2 
209  C CE3 . TRP A 192 ? 0.2364 0.4024 0.2407 0.0238  0.0072  -0.0143 192 TRP A CE3 
210  C CZ2 . TRP A 192 ? 0.2378 0.4314 0.2390 0.0476  0.0130  -0.0145 192 TRP A CZ2 
211  C CZ3 . TRP A 192 ? 0.2526 0.4107 0.2471 0.0363  0.0062  -0.0146 192 TRP A CZ3 
212  C CH2 . TRP A 192 ? 0.2475 0.4184 0.2400 0.0490  0.0090  -0.0149 192 TRP A CH2 
213  N N   . SER A 193 ? 0.2108 0.4123 0.2373 -0.0108 0.0225  -0.0074 193 SER A N   
214  C CA  . SER A 193 ? 0.2080 0.4197 0.2393 -0.0202 0.0270  -0.0044 193 SER A CA  
215  C C   . SER A 193 ? 0.2164 0.4515 0.2573 -0.0230 0.0282  -0.0039 193 SER A C   
216  O O   . SER A 193 ? 0.2201 0.4676 0.2631 -0.0136 0.0270  -0.0050 193 SER A O   
217  C CB  . SER A 193 ? 0.1942 0.4074 0.2198 -0.0184 0.0319  -0.0018 193 SER A CB  
218  O OG  . SER A 193 ? 0.2069 0.4397 0.2347 -0.0119 0.0349  -0.0013 193 SER A OG  
219  N N   . SER A 194 ? 0.2183 0.4603 0.2639 -0.0357 0.0310  -0.0021 194 SER A N   
220  C CA  . SER A 194 ? 0.2178 0.4870 0.2738 -0.0416 0.0322  -0.0015 194 SER A CA  
221  C C   . SER A 194 ? 0.2208 0.5140 0.2802 -0.0351 0.0368  0.0008  194 SER A C   
222  O O   . SER A 194 ? 0.2195 0.5415 0.2888 -0.0352 0.0372  0.0011  194 SER A O   
223  C CB  . SER A 194 ? 0.2371 0.5041 0.2946 -0.0592 0.0344  -0.0006 194 SER A CB  
224  O OG  . SER A 194 ? 0.2786 0.5380 0.3304 -0.0649 0.0404  0.0032  194 SER A OG  
225  N N   . GLY A 195 ? 0.2249 0.5084 0.2759 -0.0287 0.0403  0.0023  195 GLY A N   
226  C CA  . GLY A 195 ? 0.2195 0.5228 0.2705 -0.0199 0.0452  0.0041  195 GLY A CA  
227  C C   . GLY A 195 ? 0.2216 0.5231 0.2674 -0.0012 0.0422  0.0008  195 GLY A C   
228  O O   . GLY A 195 ? 0.2235 0.5357 0.2654 0.0094  0.0461  0.0011  195 GLY A O   
229  N N   . ASN A 196 ? 0.2226 0.5089 0.2666 0.0029  0.0358  -0.0025 196 ASN A N   
230  C CA  . ASN A 196 ? 0.2204 0.4987 0.2569 0.0191  0.0326  -0.0056 196 ASN A CA  
231  C C   . ASN A 196 ? 0.2061 0.4606 0.2277 0.0264  0.0325  -0.0080 196 ASN A C   
232  O O   . ASN A 196 ? 0.2041 0.4544 0.2166 0.0405  0.0323  -0.0106 196 ASN A O   
233  C CB  . ASN A 196 ? 0.2240 0.5311 0.2657 0.0310  0.0349  -0.0049 196 ASN A CB  
234  C CG  . ASN A 196 ? 0.2798 0.5775 0.3153 0.0453  0.0302  -0.0074 196 ASN A CG  
235  O OD1 . ASN A 196 ? 0.3083 0.5837 0.3398 0.0423  0.0251  -0.0087 196 ASN A OD1 
236  N ND2 . ASN A 196 ? 0.2917 0.6053 0.3248 0.0620  0.0325  -0.0075 196 ASN A ND2 
237  N N   . VAL A 197 ? 0.1968 0.4344 0.2147 0.0174  0.0319  -0.0075 197 VAL A N   
238  C CA  . VAL A 197 ? 0.2060 0.4231 0.2104 0.0224  0.0304  -0.0101 197 VAL A CA  
239  C C   . VAL A 197 ? 0.2157 0.4108 0.2178 0.0174  0.0243  -0.0122 197 VAL A C   
240  O O   . VAL A 197 ? 0.2139 0.4070 0.2224 0.0074  0.0235  -0.0103 197 VAL A O   
241  C CB  . VAL A 197 ? 0.2139 0.4340 0.2145 0.0186  0.0352  -0.0070 197 VAL A CB  
242  C CG1 . VAL A 197 ? 0.2270 0.4280 0.2132 0.0235  0.0325  -0.0099 197 VAL A CG1 
243  C CG2 . VAL A 197 ? 0.2006 0.4456 0.2038 0.0229  0.0423  -0.0042 197 VAL A CG2 
244  N N   . LEU A 198 ? 0.2210 0.3998 0.2132 0.0241  0.0202  -0.0164 198 LEU A N   
245  C CA  . LEU A 198 ? 0.2288 0.3893 0.2187 0.0187  0.0147  -0.0184 198 LEU A CA  
246  C C   . LEU A 198 ? 0.2295 0.3817 0.2127 0.0159  0.0134  -0.0194 198 LEU A C   
247  O O   . LEU A 198 ? 0.2343 0.3828 0.2067 0.0223  0.0137  -0.0220 198 LEU A O   
248  C CB  . LEU A 198 ? 0.2409 0.3861 0.2211 0.0258  0.0112  -0.0223 198 LEU A CB  
249  C CG  . LEU A 198 ? 0.2651 0.3954 0.2453 0.0198  0.0065  -0.0230 198 LEU A CG  
250  C CD1 . LEU A 198 ? 0.2473 0.3890 0.2406 0.0136  0.0070  -0.0192 198 LEU A CD1 
251  C CD2 . LEU A 198 ? 0.2830 0.3954 0.2505 0.0277  0.0043  -0.0259 198 LEU A CD2 
252  N N   . ALA A 199 ? 0.2242 0.3742 0.2126 0.0078  0.0118  -0.0176 199 ALA A N   
253  C CA  . ALA A 199 ? 0.2294 0.3742 0.2122 0.0062  0.0096  -0.0181 199 ALA A CA  
254  C C   . ALA A 199 ? 0.2292 0.3633 0.2102 0.0028  0.0036  -0.0216 199 ALA A C   
255  O O   . ALA A 199 ? 0.2295 0.3624 0.2178 -0.0020 0.0024  -0.0208 199 ALA A O   
256  C CB  . ALA A 199 ? 0.2331 0.3826 0.2217 0.0012  0.0122  -0.0133 199 ALA A CB  
257  N N   . VAL A 200 ? 0.2297 0.3564 0.2002 0.0046  -0.0001 -0.0259 200 VAL A N   
258  C CA  . VAL A 200 ? 0.2477 0.3645 0.2153 -0.0009 -0.0059 -0.0297 200 VAL A CA  
259  C C   . VAL A 200 ? 0.2552 0.3758 0.2192 -0.0036 -0.0100 -0.0312 200 VAL A C   
260  O O   . VAL A 200 ? 0.2626 0.3823 0.2160 0.0011  -0.0107 -0.0338 200 VAL A O   
261  C CB  . VAL A 200 ? 0.2679 0.3682 0.2227 0.0028  -0.0076 -0.0349 200 VAL A CB  
262  C CG1 . VAL A 200 ? 0.2803 0.3676 0.2309 -0.0059 -0.0134 -0.0386 200 VAL A CG1 
263  C CG2 . VAL A 200 ? 0.2717 0.3715 0.2291 0.0089  -0.0036 -0.0328 200 VAL A CG2 
264  N N   . ALA A 201 ? 0.2462 0.3733 0.2187 -0.0102 -0.0128 -0.0297 201 ALA A N   
265  C CA  . ALA A 201 ? 0.2500 0.3855 0.2205 -0.0121 -0.0174 -0.0310 201 ALA A CA  
266  C C   . ALA A 201 ? 0.2575 0.3862 0.2219 -0.0197 -0.0239 -0.0372 201 ALA A C   
267  O O   . ALA A 201 ? 0.2532 0.3785 0.2229 -0.0275 -0.0252 -0.0375 201 ALA A O   
268  C CB  . ALA A 201 ? 0.2423 0.3910 0.2247 -0.0137 -0.0169 -0.0262 201 ALA A CB  
269  N N   . LEU A 202 ? 0.2599 0.3854 0.2116 -0.0184 -0.0278 -0.0423 202 LEU A N   
270  C CA  . LEU A 202 ? 0.2760 0.3927 0.2188 -0.0275 -0.0346 -0.0494 202 LEU A CA  
271  C C   . LEU A 202 ? 0.2769 0.4116 0.2197 -0.0304 -0.0407 -0.0511 202 LEU A C   
272  O O   . LEU A 202 ? 0.2817 0.4188 0.2140 -0.0237 -0.0420 -0.0530 202 LEU A O   
273  C CB  . LEU A 202 ? 0.2935 0.3879 0.2173 -0.0231 -0.0346 -0.0557 202 LEU A CB  
274  C CG  . LEU A 202 ? 0.3234 0.4014 0.2454 -0.0174 -0.0289 -0.0543 202 LEU A CG  
275  C CD1 . LEU A 202 ? 0.3457 0.4023 0.2468 -0.0105 -0.0289 -0.0609 202 LEU A CD1 
276  C CD2 . LEU A 202 ? 0.3372 0.4065 0.2653 -0.0270 -0.0298 -0.0530 202 LEU A CD2 
277  N N   . ASP A 203 ? 0.2624 0.4124 0.2171 -0.0396 -0.0443 -0.0499 203 ASP A N   
278  C CA  . ASP A 203 ? 0.2550 0.4289 0.2135 -0.0422 -0.0505 -0.0505 203 ASP A CA  
279  C C   . ASP A 203 ? 0.2449 0.4327 0.2051 -0.0282 -0.0476 -0.0444 203 ASP A C   
280  O O   . ASP A 203 ? 0.2272 0.4211 0.1983 -0.0230 -0.0423 -0.0375 203 ASP A O   
281  C CB  . ASP A 203 ? 0.2935 0.4631 0.2382 -0.0511 -0.0589 -0.0596 203 ASP A CB  
282  C CG  . ASP A 203 ? 0.3604 0.5603 0.3104 -0.0540 -0.0663 -0.0603 203 ASP A CG  
283  O OD1 . ASP A 203 ? 0.3488 0.5725 0.3159 -0.0549 -0.0660 -0.0548 203 ASP A OD1 
284  O OD2 . ASP A 203 ? 0.4071 0.6083 0.3434 -0.0540 -0.0724 -0.0663 203 ASP A OD2 
285  N N   . ASN A 204 ? 0.2519 0.4418 0.1991 -0.0220 -0.0505 -0.0467 204 ASN A N   
286  C CA  . ASN A 204 ? 0.2565 0.4569 0.2024 -0.0090 -0.0475 -0.0401 204 ASN A CA  
287  C C   . ASN A 204 ? 0.2780 0.4619 0.2141 0.0004  -0.0400 -0.0374 204 ASN A C   
288  O O   . ASN A 204 ? 0.2893 0.4783 0.2198 0.0101  -0.0374 -0.0321 204 ASN A O   
289  C CB  . ASN A 204 ? 0.2662 0.4848 0.2045 -0.0070 -0.0556 -0.0426 204 ASN A CB  
290  C CG  . ASN A 204 ? 0.3287 0.5362 0.2480 -0.0083 -0.0598 -0.0508 204 ASN A CG  
291  O OD1 . ASN A 204 ? 0.3593 0.5445 0.2709 -0.0124 -0.0578 -0.0562 204 ASN A OD1 
292  N ND2 . ASN A 204 ? 0.3255 0.5480 0.2351 -0.0038 -0.0660 -0.0522 204 ASN A ND2 
293  N N   . SER A 205 ? 0.2773 0.4428 0.2104 -0.0022 -0.0363 -0.0405 205 SER A N   
294  C CA  . SER A 205 ? 0.2775 0.4324 0.2026 0.0063  -0.0291 -0.0383 205 SER A CA  
295  C C   . SER A 205 ? 0.2677 0.4151 0.2032 0.0055  -0.0223 -0.0346 205 SER A C   
296  O O   . SER A 205 ? 0.2683 0.4123 0.2125 -0.0017 -0.0237 -0.0360 205 SER A O   
297  C CB  . SER A 205 ? 0.3074 0.4491 0.2154 0.0073  -0.0313 -0.0465 205 SER A CB  
298  O OG  . SER A 205 ? 0.3657 0.5144 0.2610 0.0088  -0.0375 -0.0505 205 SER A OG  
299  N N   . VAL A 206 ? 0.2554 0.4013 0.1895 0.0122  -0.0149 -0.0298 206 VAL A N   
300  C CA  . VAL A 206 ? 0.2487 0.3901 0.1917 0.0114  -0.0087 -0.0269 206 VAL A CA  
301  C C   . VAL A 206 ? 0.2487 0.3843 0.1818 0.0173  -0.0050 -0.0295 206 VAL A C   
302  O O   . VAL A 206 ? 0.2384 0.3773 0.1614 0.0236  -0.0023 -0.0284 206 VAL A O   
303  C CB  . VAL A 206 ? 0.2498 0.3968 0.2016 0.0120  -0.0028 -0.0187 206 VAL A CB  
304  C CG1 . VAL A 206 ? 0.2462 0.3909 0.2062 0.0102  0.0028  -0.0169 206 VAL A CG1 
305  C CG2 . VAL A 206 ? 0.2564 0.4086 0.2166 0.0088  -0.0061 -0.0164 206 VAL A CG2 
306  N N   . TYR A 207 ? 0.2507 0.3779 0.1855 0.0164  -0.0046 -0.0328 207 TYR A N   
307  C CA  . TYR A 207 ? 0.2648 0.3877 0.1912 0.0242  -0.0006 -0.0352 207 TYR A CA  
308  C C   . TYR A 207 ? 0.2637 0.3944 0.2025 0.0250  0.0057  -0.0300 207 TYR A C   
309  O O   . TYR A 207 ? 0.2513 0.3826 0.2020 0.0189  0.0050  -0.0277 207 TYR A O   
310  C CB  . TYR A 207 ? 0.2802 0.3851 0.1957 0.0247  -0.0052 -0.0432 207 TYR A CB  
311  C CG  . TYR A 207 ? 0.3118 0.4086 0.2115 0.0237  -0.0113 -0.0500 207 TYR A CG  
312  C CD1 . TYR A 207 ? 0.3351 0.4323 0.2376 0.0135  -0.0185 -0.0520 207 TYR A CD1 
313  C CD2 . TYR A 207 ? 0.3311 0.4237 0.2134 0.0329  -0.0099 -0.0543 207 TYR A CD2 
314  C CE1 . TYR A 207 ? 0.3589 0.4530 0.2476 0.0114  -0.0250 -0.0584 207 TYR A CE1 
315  C CE2 . TYR A 207 ? 0.3629 0.4490 0.2294 0.0316  -0.0161 -0.0612 207 TYR A CE2 
316  C CZ  . TYR A 207 ? 0.3869 0.4745 0.2571 0.0202  -0.0240 -0.0632 207 TYR A CZ  
317  O OH  . TYR A 207 ? 0.4456 0.5292 0.3002 0.0176  -0.0311 -0.0706 207 TYR A OH  
318  N N   . LEU A 208 ? 0.2693 0.4081 0.2051 0.0324  0.0118  -0.0283 208 LEU A N   
319  C CA  . LEU A 208 ? 0.2763 0.4269 0.2234 0.0331  0.0175  -0.0241 208 LEU A CA  
320  C C   . LEU A 208 ? 0.3081 0.4560 0.2480 0.0433  0.0187  -0.0283 208 LEU A C   
321  O O   . LEU A 208 ? 0.3189 0.4622 0.2441 0.0519  0.0194  -0.0323 208 LEU A O   
322  C CB  . LEU A 208 ? 0.2645 0.4309 0.2148 0.0326  0.0246  -0.0176 208 LEU A CB  
323  C CG  . LEU A 208 ? 0.2739 0.4397 0.2275 0.0249  0.0246  -0.0125 208 LEU A CG  
324  C CD1 . LEU A 208 ? 0.2770 0.4550 0.2325 0.0229  0.0328  -0.0054 208 LEU A CD1 
325  C CD2 . LEU A 208 ? 0.2715 0.4322 0.2369 0.0165  0.0210  -0.0117 208 LEU A CD2 
326  N N   . TRP A 209 ? 0.3162 0.4663 0.2647 0.0437  0.0189  -0.0275 209 TRP A N   
327  C CA  . TRP A 209 ? 0.3487 0.4966 0.2903 0.0558  0.0203  -0.0306 209 TRP A CA  
328  C C   . TRP A 209 ? 0.3501 0.5223 0.3065 0.0576  0.0254  -0.0254 209 TRP A C   
329  O O   . TRP A 209 ? 0.3381 0.5152 0.3074 0.0493  0.0239  -0.0223 209 TRP A O   
330  C CB  . TRP A 209 ? 0.3684 0.4917 0.3025 0.0557  0.0142  -0.0350 209 TRP A CB  
331  C CG  . TRP A 209 ? 0.3981 0.5143 0.3227 0.0697  0.0154  -0.0375 209 TRP A CG  
332  C CD1 . TRP A 209 ? 0.4233 0.5259 0.3285 0.0827  0.0164  -0.0431 209 TRP A CD1 
333  C CD2 . TRP A 209 ? 0.4058 0.5269 0.3379 0.0737  0.0158  -0.0345 209 TRP A CD2 
334  N NE1 . TRP A 209 ? 0.4318 0.5297 0.3318 0.0958  0.0177  -0.0434 209 TRP A NE1 
335  C CE2 . TRP A 209 ? 0.4248 0.5349 0.3415 0.0906  0.0171  -0.0378 209 TRP A CE2 
336  C CE3 . TRP A 209 ? 0.4060 0.5385 0.3545 0.0654  0.0149  -0.0296 209 TRP A CE3 
337  C CZ2 . TRP A 209 ? 0.4353 0.5472 0.3532 0.1002  0.0175  -0.0355 209 TRP A CZ2 
338  C CZ3 . TRP A 209 ? 0.4168 0.5523 0.3668 0.0737  0.0149  -0.0278 209 TRP A CZ3 
339  C CH2 . TRP A 209 ? 0.4259 0.5520 0.3612 0.0913  0.0161  -0.0302 209 TRP A CH2 
340  N N   . SER A 210 ? 0.3579 0.5482 0.3127 0.0676  0.0315  -0.0244 210 SER A N   
341  C CA  . SER A 210 ? 0.3745 0.5934 0.3443 0.0689  0.0361  -0.0197 210 SER A CA  
342  C C   . SER A 210 ? 0.4004 0.6151 0.3679 0.0803  0.0336  -0.0220 210 SER A C   
343  O O   . SER A 210 ? 0.4139 0.6164 0.3658 0.0951  0.0338  -0.0263 210 SER A O   
344  C CB  . SER A 210 ? 0.4080 0.6516 0.3777 0.0756  0.0441  -0.0174 210 SER A CB  
345  O OG  . SER A 210 ? 0.4597 0.7335 0.4417 0.0811  0.0481  -0.0143 210 SER A OG  
346  N N   . ALA A 211 ? 0.4060 0.6287 0.3866 0.0742  0.0313  -0.0191 211 ALA A N   
347  C CA  . ALA A 211 ? 0.4255 0.6452 0.4034 0.0857  0.0288  -0.0199 211 ALA A CA  
348  C C   . ALA A 211 ? 0.4365 0.6835 0.4160 0.1024  0.0339  -0.0187 211 ALA A C   
349  O O   . ALA A 211 ? 0.4569 0.6959 0.4269 0.1185  0.0326  -0.0203 211 ALA A O   
350  C CB  . ALA A 211 ? 0.4163 0.6399 0.4070 0.0751  0.0250  -0.0169 211 ALA A CB  
351  N N   . SER A 212 ? 0.4218 0.7000 0.4117 0.0997  0.0401  -0.0158 212 SER A N   
352  C CA  . SER A 212 ? 0.4226 0.7335 0.4163 0.1150  0.0457  -0.0142 212 SER A CA  
353  C C   . SER A 212 ? 0.4426 0.7418 0.4164 0.1335  0.0494  -0.0185 212 SER A C   
354  O O   . SER A 212 ? 0.4501 0.7535 0.4158 0.1543  0.0509  -0.0201 212 SER A O   
355  C CB  . SER A 212 ? 0.4243 0.7758 0.4380 0.1021  0.0512  -0.0088 212 SER A CB  
356  O OG  . SER A 212 ? 0.4549 0.8142 0.4644 0.1010  0.0579  -0.0079 212 SER A OG  
357  N N   . SER A 213 ? 0.4447 0.7288 0.4090 0.1273  0.0510  -0.0206 213 SER A N   
358  C CA  . SER A 213 ? 0.4588 0.7329 0.4028 0.1437  0.0547  -0.0253 213 SER A CA  
359  C C   . SER A 213 ? 0.4816 0.7084 0.4015 0.1480  0.0488  -0.0328 213 SER A C   
360  O O   . SER A 213 ? 0.4937 0.7071 0.3931 0.1639  0.0510  -0.0383 213 SER A O   
361  C CB  . SER A 213 ? 0.4683 0.7589 0.4143 0.1358  0.0609  -0.0227 213 SER A CB  
362  O OG  . SER A 213 ? 0.5164 0.7860 0.4626 0.1174  0.0564  -0.0224 213 SER A OG  
363  N N   . GLY A 214 ? 0.4812 0.6838 0.4029 0.1329  0.0417  -0.0334 214 GLY A N   
364  C CA  . GLY A 214 ? 0.4990 0.6593 0.4001 0.1317  0.0356  -0.0403 214 GLY A CA  
365  C C   . GLY A 214 ? 0.5005 0.6537 0.3927 0.1246  0.0356  -0.0431 214 GLY A C   
366  O O   . GLY A 214 ? 0.5264 0.6482 0.4007 0.1230  0.0304  -0.0497 214 GLY A O   
367  N N   . ASP A 215 ? 0.4723 0.6543 0.3756 0.1198  0.0413  -0.0381 215 ASP A N   
368  C CA  . ASP A 215 ? 0.4712 0.6481 0.3652 0.1143  0.0416  -0.0395 215 ASP A CA  
369  C C   . ASP A 215 ? 0.4514 0.6106 0.3488 0.0973  0.0342  -0.0397 215 ASP A C   
370  O O   . ASP A 215 ? 0.4417 0.6061 0.3560 0.0862  0.0322  -0.0352 215 ASP A O   
371  C CB  . ASP A 215 ? 0.4978 0.7081 0.4027 0.1118  0.0500  -0.0324 215 ASP A CB  
372  C CG  . ASP A 215 ? 0.5996 0.8305 0.4981 0.1294  0.0582  -0.0328 215 ASP A CG  
373  O OD1 . ASP A 215 ? 0.6315 0.8441 0.5080 0.1443  0.0576  -0.0403 215 ASP A OD1 
374  O OD2 . ASP A 215 ? 0.6304 0.8960 0.5452 0.1282  0.0653  -0.0259 215 ASP A OD2 
375  N N   . ILE A 216 ? 0.4384 0.5779 0.3191 0.0958  0.0299  -0.0452 216 ILE A N   
376  C CA  . ILE A 216 ? 0.4271 0.5543 0.3109 0.0809  0.0228  -0.0454 216 ILE A CA  
377  C C   . ILE A 216 ? 0.4036 0.5404 0.2840 0.0774  0.0242  -0.0430 216 ILE A C   
378  O O   . ILE A 216 ? 0.4108 0.5491 0.2759 0.0868  0.0272  -0.0457 216 ILE A O   
379  C CB  . ILE A 216 ? 0.4474 0.5433 0.3149 0.0798  0.0147  -0.0543 216 ILE A CB  
380  C CG1 . ILE A 216 ? 0.4623 0.5446 0.3302 0.0841  0.0137  -0.0557 216 ILE A CG1 
381  C CG2 . ILE A 216 ? 0.4479 0.5376 0.3195 0.0646  0.0075  -0.0546 216 ILE A CG2 
382  C CD1 . ILE A 216 ? 0.4906 0.5390 0.3349 0.0882  0.0088  -0.0649 216 ILE A CD1 
383  N N   . LEU A 217 ? 0.3728 0.5156 0.2660 0.0654  0.0225  -0.0374 217 LEU A N   
384  C CA  . LEU A 217 ? 0.3568 0.5066 0.2460 0.0624  0.0234  -0.0336 217 LEU A CA  
385  C C   . LEU A 217 ? 0.3497 0.4895 0.2411 0.0526  0.0151  -0.0348 217 LEU A C   
386  O O   . LEU A 217 ? 0.3440 0.4832 0.2501 0.0445  0.0130  -0.0323 217 LEU A O   
387  C CB  . LEU A 217 ? 0.3437 0.5134 0.2473 0.0581  0.0314  -0.0234 217 LEU A CB  
388  C CG  . LEU A 217 ? 0.3674 0.5409 0.2662 0.0547  0.0330  -0.0174 217 LEU A CG  
389  C CD1 . LEU A 217 ? 0.3716 0.5507 0.2529 0.0645  0.0377  -0.0180 217 LEU A CD1 
390  C CD2 . LEU A 217 ? 0.3664 0.5497 0.2795 0.0458  0.0388  -0.0078 217 LEU A CD2 
391  N N   . GLN A 218 ? 0.3447 0.4797 0.2220 0.0535  0.0104  -0.0383 218 GLN A N   
392  C CA  . GLN A 218 ? 0.3421 0.4751 0.2233 0.0450  0.0029  -0.0381 218 GLN A CA  
393  C C   . GLN A 218 ? 0.3321 0.4782 0.2200 0.0442  0.0080  -0.0280 218 GLN A C   
394  O O   . GLN A 218 ? 0.3371 0.4883 0.2132 0.0497  0.0106  -0.0254 218 GLN A O   
395  C CB  . GLN A 218 ? 0.3706 0.4966 0.2342 0.0460  -0.0047 -0.0459 218 GLN A CB  
396  C CG  . GLN A 218 ? 0.4040 0.5325 0.2744 0.0366  -0.0132 -0.0463 218 GLN A CG  
397  C CD  . GLN A 218 ? 0.4445 0.5715 0.2988 0.0360  -0.0216 -0.0537 218 GLN A CD  
398  O OE1 . GLN A 218 ? 0.4889 0.6120 0.3248 0.0431  -0.0211 -0.0581 218 GLN A OE1 
399  N NE2 . GLN A 218 ? 0.4376 0.5701 0.2986 0.0273  -0.0296 -0.0551 218 GLN A NE2 
400  N N   . LEU A 219 ? 0.3164 0.4658 0.2208 0.0379  0.0102  -0.0221 219 LEU A N   
401  C CA  . LEU A 219 ? 0.3104 0.4663 0.2191 0.0365  0.0157  -0.0125 219 LEU A CA  
402  C C   . LEU A 219 ? 0.3220 0.4781 0.2232 0.0379  0.0113  -0.0100 219 LEU A C   
403  O O   . LEU A 219 ? 0.3237 0.4823 0.2168 0.0416  0.0159  -0.0032 219 LEU A O   
404  C CB  . LEU A 219 ? 0.2948 0.4505 0.2207 0.0289  0.0178  -0.0086 219 LEU A CB  
405  C CG  . LEU A 219 ? 0.3007 0.4569 0.2297 0.0257  0.0230  0.0005  219 LEU A CG  
406  C CD1 . LEU A 219 ? 0.3083 0.4705 0.2323 0.0268  0.0321  0.0062  219 LEU A CD1 
407  C CD2 . LEU A 219 ? 0.2967 0.4500 0.2405 0.0181  0.0230  0.0018  219 LEU A CD2 
408  N N   . LEU A 220 ? 0.3232 0.4778 0.2277 0.0348  0.0028  -0.0146 220 LEU A N   
409  C CA  . LEU A 220 ? 0.3368 0.4963 0.2368 0.0370  -0.0023 -0.0122 220 LEU A CA  
410  C C   . LEU A 220 ? 0.3497 0.5122 0.2498 0.0334  -0.0126 -0.0203 220 LEU A C   
411  O O   . LEU A 220 ? 0.3539 0.5111 0.2597 0.0273  -0.0155 -0.0267 220 LEU A O   
412  C CB  . LEU A 220 ? 0.3383 0.4977 0.2491 0.0350  0.0006  -0.0043 220 LEU A CB  
413  C CG  . LEU A 220 ? 0.3593 0.5178 0.2868 0.0276  -0.0020 -0.0069 220 LEU A CG  
414  C CD1 . LEU A 220 ? 0.3622 0.5294 0.2935 0.0271  -0.0102 -0.0090 220 LEU A CD1 
415  C CD2 . LEU A 220 ? 0.3663 0.5197 0.3021 0.0253  0.0047  -0.0003 220 LEU A CD2 
416  N N   . GLN A 221 ? 0.3563 0.5279 0.2500 0.0367  -0.0182 -0.0195 221 GLN A N   
417  C CA  . GLN A 221 ? 0.3633 0.5434 0.2591 0.0316  -0.0286 -0.0262 221 GLN A CA  
418  C C   . GLN A 221 ? 0.3581 0.5526 0.2574 0.0364  -0.0313 -0.0195 221 GLN A C   
419  O O   . GLN A 221 ? 0.3638 0.5598 0.2527 0.0459  -0.0281 -0.0126 221 GLN A O   
420  C CB  . GLN A 221 ? 0.3971 0.5763 0.2760 0.0319  -0.0348 -0.0351 221 GLN A CB  
421  C CG  . GLN A 221 ? 0.4753 0.6637 0.3568 0.0230  -0.0460 -0.0429 221 GLN A CG  
422  C CD  . GLN A 221 ? 0.5763 0.7593 0.4394 0.0209  -0.0526 -0.0535 221 GLN A CD  
423  O OE1 . GLN A 221 ? 0.6266 0.7918 0.4840 0.0155  -0.0526 -0.0613 221 GLN A OE1 
424  N NE2 . GLN A 221 ? 0.5829 0.7795 0.4340 0.0258  -0.0584 -0.0542 221 GLN A NE2 
425  N N   . MET A 222 ? 0.3409 0.5461 0.2541 0.0309  -0.0364 -0.0208 222 MET A N   
426  C CA  . MET A 222 ? 0.3411 0.5639 0.2585 0.0372  -0.0398 -0.0152 222 MET A CA  
427  C C   . MET A 222 ? 0.3486 0.5855 0.2521 0.0430  -0.0472 -0.0170 222 MET A C   
428  O O   . MET A 222 ? 0.3455 0.5829 0.2413 0.0369  -0.0531 -0.0259 222 MET A O   
429  C CB  . MET A 222 ? 0.3416 0.5782 0.2763 0.0291  -0.0447 -0.0181 222 MET A CB  
430  C CG  . MET A 222 ? 0.3730 0.5969 0.3204 0.0229  -0.0383 -0.0171 222 MET A CG  
431  S SD  . MET A 222 ? 0.4436 0.6657 0.3974 0.0326  -0.0308 -0.0067 222 MET A SD  
432  C CE  . MET A 222 ? 0.4119 0.6112 0.3522 0.0384  -0.0216 -0.0011 222 MET A CE  
433  N N   . GLU A 223 ? 0.3609 0.6066 0.2589 0.0554  -0.0468 -0.0086 223 GLU A N   
434  C CA  . GLU A 223 ? 0.3891 0.6490 0.2721 0.0630  -0.0536 -0.0090 223 GLU A CA  
435  C C   . GLU A 223 ? 0.3833 0.6739 0.2739 0.0619  -0.0652 -0.0125 223 GLU A C   
436  O O   . GLU A 223 ? 0.3911 0.6951 0.2708 0.0620  -0.0736 -0.0177 223 GLU A O   
437  C CB  . GLU A 223 ? 0.4455 0.6973 0.3138 0.0782  -0.0470 0.0027  223 GLU A CB  
438  C CG  . GLU A 223 ? 0.5507 0.7770 0.4110 0.0773  -0.0357 0.0060  223 GLU A CG  
439  C CD  . GLU A 223 ? 0.6941 0.9167 0.5322 0.0839  -0.0343 0.0074  223 GLU A CD  
440  O OE1 . GLU A 223 ? 0.7163 0.9507 0.5416 0.0944  -0.0390 0.0115  223 GLU A OE1 
441  O OE2 . GLU A 223 ? 0.7475 0.9569 0.5806 0.0797  -0.0282 0.0047  223 GLU A OE2 
442  N N   . GLN A 224 ? 0.3706 0.6744 0.2793 0.0606  -0.0659 -0.0102 224 GLN A N   
443  C CA  . GLN A 224 ? 0.3626 0.7017 0.2805 0.0601  -0.0763 -0.0126 224 GLN A CA  
444  C C   . GLN A 224 ? 0.3362 0.6866 0.2681 0.0403  -0.0830 -0.0233 224 GLN A C   
445  O O   . GLN A 224 ? 0.3299 0.6631 0.2709 0.0299  -0.0778 -0.0257 224 GLN A O   
446  C CB  . GLN A 224 ? 0.4015 0.7546 0.3297 0.0732  -0.0735 -0.0030 224 GLN A CB  
447  C CG  . GLN A 224 ? 0.4861 0.8152 0.4025 0.0896  -0.0633 0.0086  224 GLN A CG  
448  C CD  . GLN A 224 ? 0.5613 0.8873 0.4555 0.1025  -0.0643 0.0136  224 GLN A CD  
449  O OE1 . GLN A 224 ? 0.5968 0.8958 0.4767 0.1032  -0.0572 0.0163  224 GLN A OE1 
450  N NE2 . GLN A 224 ? 0.5652 0.9203 0.4559 0.1134  -0.0728 0.0158  224 GLN A NE2 
451  N N   . PRO A 225 ? 0.3132 0.6940 0.2467 0.0347  -0.0946 -0.0292 225 PRO A N   
452  C CA  . PRO A 225 ? 0.3005 0.6921 0.2464 0.0136  -0.1010 -0.0389 225 PRO A CA  
453  C C   . PRO A 225 ? 0.2882 0.6896 0.2566 0.0093  -0.0966 -0.0350 225 PRO A C   
454  O O   . PRO A 225 ? 0.2830 0.6991 0.2598 0.0235  -0.0930 -0.0262 225 PRO A O   
455  C CB  . PRO A 225 ? 0.3021 0.7307 0.2457 0.0108  -0.1144 -0.0439 225 PRO A CB  
456  C CG  . PRO A 225 ? 0.3135 0.7368 0.2355 0.0280  -0.1149 -0.0403 225 PRO A CG  
457  C CD  . PRO A 225 ? 0.2970 0.7030 0.2194 0.0459  -0.1029 -0.0277 225 PRO A CD  
458  N N   . GLY A 226 ? 0.2792 0.6681 0.2549 -0.0090 -0.0957 -0.0413 226 GLY A N   
459  C CA  . GLY A 226 ? 0.2709 0.6668 0.2662 -0.0149 -0.0910 -0.0382 226 GLY A CA  
460  C C   . GLY A 226 ? 0.2816 0.6490 0.2781 -0.0061 -0.0790 -0.0315 226 GLY A C   
461  O O   . GLY A 226 ? 0.2918 0.6583 0.3016 -0.0122 -0.0744 -0.0300 226 GLY A O   
462  N N   . GLU A 227 ? 0.2825 0.6274 0.2648 0.0076  -0.0736 -0.0272 227 GLU A N   
463  C CA  . GLU A 227 ? 0.2854 0.6040 0.2681 0.0143  -0.0627 -0.0213 227 GLU A CA  
464  C C   . GLU A 227 ? 0.2689 0.5602 0.2504 0.0017  -0.0589 -0.0264 227 GLU A C   
465  O O   . GLU A 227 ? 0.2745 0.5534 0.2449 -0.0051 -0.0622 -0.0330 227 GLU A O   
466  C CB  . GLU A 227 ? 0.3364 0.6391 0.3036 0.0299  -0.0577 -0.0151 227 GLU A CB  
467  C CG  . GLU A 227 ? 0.4191 0.7379 0.3851 0.0470  -0.0575 -0.0067 227 GLU A CG  
468  C CD  . GLU A 227 ? 0.5501 0.8447 0.4995 0.0599  -0.0503 0.0006  227 GLU A CD  
469  O OE1 . GLU A 227 ? 0.5743 0.8552 0.5106 0.0576  -0.0501 -0.0019 227 GLU A OE1 
470  O OE2 . GLU A 227 ? 0.5897 0.8784 0.5378 0.0722  -0.0446 0.0088  227 GLU A OE2 
471  N N   . TYR A 228 ? 0.2432 0.5238 0.2340 0.0005  -0.0519 -0.0232 228 TYR A N   
472  C CA  . TYR A 228 ? 0.2430 0.4984 0.2327 -0.0084 -0.0477 -0.0264 228 TYR A CA  
473  C C   . TYR A 228 ? 0.2346 0.4743 0.2273 -0.0018 -0.0383 -0.0204 228 TYR A C   
474  O O   . TYR A 228 ? 0.2425 0.4901 0.2399 0.0072  -0.0352 -0.0144 228 TYR A O   
475  C CB  . TYR A 228 ? 0.2380 0.4990 0.2369 -0.0245 -0.0514 -0.0315 228 TYR A CB  
476  C CG  . TYR A 228 ? 0.2299 0.5115 0.2453 -0.0257 -0.0500 -0.0275 228 TYR A CG  
477  C CD1 . TYR A 228 ? 0.2428 0.5131 0.2650 -0.0253 -0.0427 -0.0240 228 TYR A CD1 
478  C CD2 . TYR A 228 ? 0.2159 0.5307 0.2403 -0.0283 -0.0563 -0.0279 228 TYR A CD2 
479  C CE1 . TYR A 228 ? 0.2405 0.5296 0.2764 -0.0263 -0.0410 -0.0209 228 TYR A CE1 
480  C CE2 . TYR A 228 ? 0.2119 0.5486 0.2518 -0.0289 -0.0543 -0.0243 228 TYR A CE2 
481  C CZ  . TYR A 228 ? 0.2304 0.5531 0.2754 -0.0275 -0.0463 -0.0208 228 TYR A CZ  
482  O OH  . TYR A 228 ? 0.2419 0.5856 0.3005 -0.0273 -0.0437 -0.0176 228 TYR A OH  
483  N N   . ILE A 229 ? 0.2134 0.4308 0.2021 -0.0056 -0.0341 -0.0222 229 ILE A N   
484  C CA  . ILE A 229 ? 0.1994 0.4032 0.1909 -0.0019 -0.0260 -0.0176 229 ILE A CA  
485  C C   . ILE A 229 ? 0.1853 0.3927 0.1893 -0.0088 -0.0249 -0.0176 229 ILE A C   
486  O O   . ILE A 229 ? 0.1821 0.3884 0.1888 -0.0190 -0.0279 -0.0219 229 ILE A O   
487  C CB  . ILE A 229 ? 0.2093 0.3935 0.1928 -0.0027 -0.0223 -0.0193 229 ILE A CB  
488  C CG1 . ILE A 229 ? 0.2221 0.4040 0.1919 0.0034  -0.0233 -0.0201 229 ILE A CG1 
489  C CG2 . ILE A 229 ? 0.2164 0.3905 0.2039 -0.0005 -0.0147 -0.0148 229 ILE A CG2 
490  C CD1 . ILE A 229 ? 0.2451 0.4299 0.2101 0.0128  -0.0203 -0.0138 229 ILE A CD1 
491  N N   . SER A 230 ? 0.1788 0.3887 0.1884 -0.0031 -0.0204 -0.0127 230 SER A N   
492  C CA  . SER A 230 ? 0.1704 0.3848 0.1907 -0.0080 -0.0185 -0.0124 230 SER A CA  
493  C C   . SER A 230 ? 0.1688 0.3654 0.1889 -0.0085 -0.0123 -0.0110 230 SER A C   
494  O O   . SER A 230 ? 0.1726 0.3701 0.1994 -0.0138 -0.0109 -0.0114 230 SER A O   
495  C CB  . SER A 230 ? 0.1906 0.4251 0.2175 -0.0012 -0.0188 -0.0092 230 SER A CB  
496  O OG  . SER A 230 ? 0.2455 0.4765 0.2649 0.0120  -0.0163 -0.0047 230 SER A OG  
497  N N   . SER A 231 ? 0.1591 0.3413 0.1715 -0.0041 -0.0086 -0.0093 231 SER A N   
498  C CA  . SER A 231 ? 0.1717 0.3404 0.1845 -0.0064 -0.0035 -0.0086 231 SER A CA  
499  C C   . SER A 231 ? 0.1779 0.3357 0.1830 -0.0043 -0.0004 -0.0075 231 SER A C   
500  O O   . SER A 231 ? 0.1848 0.3427 0.1828 0.0012  -0.0003 -0.0054 231 SER A O   
501  C CB  . SER A 231 ? 0.1925 0.3595 0.2078 -0.0031 0.0005  -0.0059 231 SER A CB  
502  O OG  . SER A 231 ? 0.2222 0.3888 0.2315 0.0061  0.0020  -0.0022 231 SER A OG  
503  N N   . VAL A 232 ? 0.1693 0.3201 0.1758 -0.0083 0.0022  -0.0084 232 VAL A N   
504  C CA  . VAL A 232 ? 0.1727 0.3174 0.1742 -0.0073 0.0062  -0.0068 232 VAL A CA  
505  C C   . VAL A 232 ? 0.1784 0.3190 0.1843 -0.0116 0.0100  -0.0060 232 VAL A C   
506  O O   . VAL A 232 ? 0.1730 0.3150 0.1847 -0.0151 0.0086  -0.0080 232 VAL A O   
507  C CB  . VAL A 232 ? 0.1797 0.3248 0.1773 -0.0069 0.0047  -0.0097 232 VAL A CB  
508  C CG1 . VAL A 232 ? 0.1791 0.3274 0.1700 -0.0036 0.0004  -0.0116 232 VAL A CG1 
509  C CG2 . VAL A 232 ? 0.1771 0.3208 0.1790 -0.0106 0.0030  -0.0131 232 VAL A CG2 
510  N N   . ALA A 233 ? 0.1795 0.3152 0.1817 -0.0123 0.0148  -0.0030 233 ALA A N   
511  C CA  . ALA A 233 ? 0.1907 0.3242 0.1964 -0.0183 0.0179  -0.0030 233 ALA A CA  
512  C C   . ALA A 233 ? 0.1919 0.3242 0.1938 -0.0211 0.0227  -0.0001 233 ALA A C   
513  O O   . ALA A 233 ? 0.1927 0.3170 0.1867 -0.0194 0.0256  0.0037  233 ALA A O   
514  C CB  . ALA A 233 ? 0.1946 0.3203 0.1999 -0.0197 0.0189  -0.0028 233 ALA A CB  
515  N N   . TRP A 234 ? 0.1841 0.3252 0.1915 -0.0256 0.0239  -0.0012 234 TRP A N   
516  C CA  . TRP A 234 ? 0.1990 0.3443 0.2051 -0.0302 0.0289  0.0017  234 TRP A CA  
517  C C   . TRP A 234 ? 0.2235 0.3605 0.2283 -0.0395 0.0321  0.0030  234 TRP A C   
518  O O   . TRP A 234 ? 0.2422 0.3787 0.2513 -0.0433 0.0300  0.0000  234 TRP A O   
519  C CB  . TRP A 234 ? 0.1879 0.3503 0.2019 -0.0307 0.0285  -0.0002 234 TRP A CB  
520  C CG  . TRP A 234 ? 0.1968 0.3650 0.2089 -0.0216 0.0267  -0.0017 234 TRP A CG  
521  C CD1 . TRP A 234 ? 0.2045 0.3731 0.2181 -0.0163 0.0221  -0.0054 234 TRP A CD1 
522  C CD2 . TRP A 234 ? 0.2038 0.3762 0.2098 -0.0171 0.0298  0.0002  234 TRP A CD2 
523  N NE1 . TRP A 234 ? 0.2058 0.3769 0.2140 -0.0088 0.0220  -0.0067 234 TRP A NE1 
524  C CE2 . TRP A 234 ? 0.2131 0.3878 0.2168 -0.0085 0.0266  -0.0035 234 TRP A CE2 
525  C CE3 . TRP A 234 ? 0.2193 0.3929 0.2202 -0.0197 0.0355  0.0049  234 TRP A CE3 
526  C CZ2 . TRP A 234 ? 0.2253 0.4043 0.2216 -0.0016 0.0287  -0.0036 234 TRP A CZ2 
527  C CZ3 . TRP A 234 ? 0.2372 0.4173 0.2318 -0.0130 0.0379  0.0058  234 TRP A CZ3 
528  C CH2 . TRP A 234 ? 0.2359 0.4188 0.2280 -0.0035 0.0343  0.0011  234 TRP A CH2 
529  N N   . ILE A 235 ? 0.2253 0.3558 0.2232 -0.0443 0.0374  0.0074  235 ILE A N   
530  C CA  . ILE A 235 ? 0.2488 0.3691 0.2435 -0.0561 0.0409  0.0083  235 ILE A CA  
531  C C   . ILE A 235 ? 0.2636 0.4050 0.2701 -0.0652 0.0404  0.0056  235 ILE A C   
532  O O   . ILE A 235 ? 0.2537 0.4159 0.2683 -0.0608 0.0395  0.0051  235 ILE A O   
533  C CB  . ILE A 235 ? 0.2561 0.3642 0.2392 -0.0599 0.0473  0.0146  235 ILE A CB  
534  C CG1 . ILE A 235 ? 0.2677 0.3520 0.2404 -0.0706 0.0508  0.0158  235 ILE A CG1 
535  C CG2 . ILE A 235 ? 0.2474 0.3762 0.2357 -0.0642 0.0512  0.0174  235 ILE A CG2 
536  C CD1 . ILE A 235 ? 0.2835 0.3482 0.2402 -0.0733 0.0576  0.0234  235 ILE A CD1 
537  N N   . LYS A 236 ? 0.2832 0.4197 0.2897 -0.0769 0.0408  0.0035  236 LYS A N   
538  C CA  . LYS A 236 ? 0.2935 0.4535 0.3116 -0.0855 0.0393  0.0007  236 LYS A CA  
539  C C   . LYS A 236 ? 0.2937 0.4794 0.3195 -0.0883 0.0428  0.0039  236 LYS A C   
540  O O   . LYS A 236 ? 0.2887 0.4994 0.3256 -0.0840 0.0402  0.0021  236 LYS A O   
541  C CB  . LYS A 236 ? 0.3267 0.4774 0.3414 -0.1003 0.0394  -0.0023 236 LYS A CB  
542  N N   . GLU A 237 ? 0.3051 0.4849 0.3242 -0.0935 0.0490  0.0091  237 GLU A N   
543  C CA  . GLU A 237 ? 0.3072 0.5136 0.3333 -0.0959 0.0536  0.0128  237 GLU A CA  
544  C C   . GLU A 237 ? 0.3072 0.5260 0.3353 -0.0786 0.0530  0.0134  237 GLU A C   
545  O O   . GLU A 237 ? 0.3028 0.5468 0.3371 -0.0771 0.0564  0.0154  237 GLU A O   
546  C CB  . GLU A 237 ? 0.3468 0.5420 0.3634 -0.1086 0.0613  0.0189  237 GLU A CB  
547  N N   . GLY A 238 ? 0.3057 0.5074 0.3278 -0.0662 0.0488  0.0114  238 GLY A N   
548  C CA  . GLY A 238 ? 0.3041 0.5121 0.3253 -0.0512 0.0471  0.0105  238 GLY A CA  
549  C C   . GLY A 238 ? 0.3040 0.5096 0.3156 -0.0466 0.0521  0.0150  238 GLY A C   
550  O O   . GLY A 238 ? 0.3040 0.5170 0.3138 -0.0349 0.0512  0.0136  238 GLY A O   
551  N N   . ASN A 239 ? 0.3043 0.4974 0.3077 -0.0552 0.0574  0.0204  239 ASN A N   
552  C CA  . ASN A 239 ? 0.3148 0.5054 0.3072 -0.0508 0.0626  0.0258  239 ASN A CA  
553  C C   . ASN A 239 ? 0.3222 0.4875 0.3005 -0.0426 0.0603  0.0273  239 ASN A C   
554  O O   . ASN A 239 ? 0.3396 0.5035 0.3076 -0.0357 0.0628  0.0309  239 ASN A O   
555  C CB  . ASN A 239 ? 0.3472 0.5432 0.3376 -0.0645 0.0711  0.0324  239 ASN A CB  
556  C CG  . ASN A 239 ? 0.4250 0.6011 0.4117 -0.0798 0.0726  0.0342  239 ASN A CG  
557  O OD1 . ASN A 239 ? 0.4480 0.6125 0.4375 -0.0814 0.0672  0.0294  239 ASN A OD1 
558  N ND2 . ASN A 239 ? 0.4387 0.6098 0.4177 -0.0920 0.0805  0.0412  239 ASN A ND2 
559  N N   . TYR A 240 ? 0.3112 0.4597 0.2890 -0.0421 0.0554  0.0246  240 TYR A N   
560  C CA  . TYR A 240 ? 0.3123 0.4420 0.2793 -0.0332 0.0523  0.0256  240 TYR A CA  
561  C C   . TYR A 240 ? 0.2869 0.4183 0.2612 -0.0268 0.0445  0.0189  240 TYR A C   
562  O O   . TYR A 240 ? 0.2750 0.4110 0.2594 -0.0317 0.0422  0.0148  240 TYR A O   
563  C CB  . TYR A 240 ? 0.3368 0.4416 0.2932 -0.0389 0.0555  0.0301  240 TYR A CB  
564  C CG  . TYR A 240 ? 0.3732 0.4717 0.3202 -0.0482 0.0640  0.0375  240 TYR A CG  
565  C CD1 . TYR A 240 ? 0.3936 0.4893 0.3281 -0.0420 0.0678  0.0438  240 TYR A CD1 
566  C CD2 . TYR A 240 ? 0.4017 0.4990 0.3522 -0.0643 0.0682  0.0381  240 TYR A CD2 
567  C CE1 . TYR A 240 ? 0.4163 0.5064 0.3413 -0.0515 0.0764  0.0516  240 TYR A CE1 
568  C CE2 . TYR A 240 ? 0.4226 0.5143 0.3643 -0.0755 0.0764  0.0453  240 TYR A CE2 
569  C CZ  . TYR A 240 ? 0.4384 0.5257 0.3671 -0.0690 0.0809  0.0526  240 TYR A CZ  
570  O OH  . TYR A 240 ? 0.4715 0.5531 0.3908 -0.0812 0.0899  0.0607  240 TYR A OH  
571  N N   . LEU A 241 ? 0.2640 0.3925 0.2327 -0.0165 0.0404  0.0181  241 LEU A N   
572  C CA  . LEU A 241 ? 0.2488 0.3796 0.2237 -0.0118 0.0333  0.0124  241 LEU A CA  
573  C C   . LEU A 241 ? 0.2455 0.3648 0.2138 -0.0064 0.0309  0.0142  241 LEU A C   
574  O O   . LEU A 241 ? 0.2478 0.3628 0.2053 -0.0003 0.0318  0.0183  241 LEU A O   
575  C CB  . LEU A 241 ? 0.2430 0.3847 0.2179 -0.0053 0.0295  0.0084  241 LEU A CB  
576  C CG  . LEU A 241 ? 0.2413 0.3842 0.2215 -0.0029 0.0223  0.0026  241 LEU A CG  
577  C CD1 . LEU A 241 ? 0.2425 0.3885 0.2334 -0.0082 0.0216  -0.0004 241 LEU A CD1 
578  C CD2 . LEU A 241 ? 0.2332 0.3804 0.2078 0.0030  0.0186  -0.0013 241 LEU A CD2 
579  N N   . ALA A 242 ? 0.2300 0.3457 0.2039 -0.0074 0.0281  0.0117  242 ALA A N   
580  C CA  . ALA A 242 ? 0.2293 0.3387 0.1986 -0.0002 0.0256  0.0129  242 ALA A CA  
581  C C   . ALA A 242 ? 0.2179 0.3412 0.1933 0.0039  0.0188  0.0085  242 ALA A C   
582  O O   . ALA A 242 ? 0.2104 0.3410 0.1946 -0.0005 0.0161  0.0038  242 ALA A O   
583  C CB  . ALA A 242 ? 0.2240 0.3234 0.1953 -0.0028 0.0269  0.0122  242 ALA A CB  
584  N N   . VAL A 243 ? 0.2183 0.3449 0.1882 0.0118  0.0158  0.0101  243 VAL A N   
585  C CA  . VAL A 243 ? 0.2255 0.3663 0.2000 0.0139  0.0087  0.0058  243 VAL A CA  
586  C C   . VAL A 243 ? 0.2374 0.3839 0.2123 0.0208  0.0060  0.0075  243 VAL A C   
587  O O   . VAL A 243 ? 0.2573 0.4009 0.2225 0.0294  0.0069  0.0123  243 VAL A O   
588  C CB  . VAL A 243 ? 0.2412 0.3866 0.2073 0.0171  0.0068  0.0054  243 VAL A CB  
589  C CG1 . VAL A 243 ? 0.2377 0.3962 0.2064 0.0174  -0.0012 0.0001  243 VAL A CG1 
590  C CG2 . VAL A 243 ? 0.2521 0.3942 0.2171 0.0126  0.0106  0.0041  243 VAL A CG2 
591  N N   . GLY A 244 ? 0.2276 0.3832 0.2130 0.0180  0.0029  0.0041  244 GLY A N   
592  C CA  . GLY A 244 ? 0.2312 0.3984 0.2193 0.0249  0.0003  0.0053  244 GLY A CA  
593  C C   . GLY A 244 ? 0.2288 0.4159 0.2200 0.0247  -0.0071 0.0024  244 GLY A C   
594  O O   . GLY A 244 ? 0.2327 0.4223 0.2270 0.0161  -0.0103 -0.0025 244 GLY A O   
595  N N   . THR A 245 ? 0.2234 0.4241 0.2125 0.0342  -0.0101 0.0051  245 THR A N   
596  C CA  . THR A 245 ? 0.2246 0.4472 0.2161 0.0330  -0.0181 0.0019  245 THR A CA  
597  C C   . THR A 245 ? 0.2347 0.4829 0.2373 0.0353  -0.0220 0.0018  245 THR A C   
598  O O   . THR A 245 ? 0.2348 0.4836 0.2399 0.0433  -0.0180 0.0054  245 THR A O   
599  C CB  . THR A 245 ? 0.2311 0.4535 0.2087 0.0421  -0.0200 0.0050  245 THR A CB  
600  O OG1 . THR A 245 ? 0.2373 0.4676 0.2112 0.0564  -0.0196 0.0111  245 THR A OG1 
601  C CG2 . THR A 245 ? 0.2345 0.4329 0.2003 0.0418  -0.0140 0.0073  245 THR A CG2 
602  N N   . SER A 246 ? 0.2407 0.5107 0.2491 0.0285  -0.0296 -0.0027 246 SER A N   
603  C CA  . SER A 246 ? 0.2402 0.5424 0.2604 0.0289  -0.0345 -0.0031 246 SER A CA  
604  C C   . SER A 246 ? 0.2467 0.5639 0.2623 0.0471  -0.0354 0.0028  246 SER A C   
605  O O   . SER A 246 ? 0.2454 0.5892 0.2710 0.0524  -0.0369 0.0043  246 SER A O   
606  C CB  . SER A 246 ? 0.2464 0.5656 0.2700 0.0156  -0.0431 -0.0096 246 SER A CB  
607  O OG  . SER A 246 ? 0.2766 0.5917 0.2868 0.0201  -0.0471 -0.0104 246 SER A OG  
608  N N   . SER A 247 ? 0.2529 0.5548 0.2527 0.0574  -0.0343 0.0066  247 SER A N   
609  C CA  . SER A 247 ? 0.2568 0.5674 0.2485 0.0769  -0.0344 0.0135  247 SER A CA  
610  C C   . SER A 247 ? 0.2701 0.5552 0.2544 0.0888  -0.0250 0.0197  247 SER A C   
611  O O   . SER A 247 ? 0.2889 0.5652 0.2593 0.1054  -0.0227 0.0266  247 SER A O   
612  C CB  . SER A 247 ? 0.2821 0.5891 0.2581 0.0827  -0.0379 0.0153  247 SER A CB  
613  O OG  . SER A 247 ? 0.3399 0.6161 0.3060 0.0753  -0.0332 0.0143  247 SER A OG  
614  N N   . ALA A 248 ? 0.2617 0.5337 0.2536 0.0804  -0.0196 0.0174  248 ALA A N   
615  C CA  . ALA A 248 ? 0.2616 0.5092 0.2466 0.0887  -0.0112 0.0213  248 ALA A CA  
616  C C   . ALA A 248 ? 0.2636 0.4744 0.2305 0.0911  -0.0053 0.0254  248 ALA A C   
617  O O   . ALA A 248 ? 0.2855 0.4746 0.2407 0.1019  0.0008  0.0302  248 ALA A O   
618  C CB  . ALA A 248 ? 0.2555 0.5195 0.2398 0.1078  -0.0109 0.0258  248 ALA A CB  
619  N N   . GLU A 249 ? 0.2435 0.4464 0.2068 0.0812  -0.0064 0.0237  249 GLU A N   
620  C CA  . GLU A 249 ? 0.2579 0.4298 0.2056 0.0810  -0.0002 0.0279  249 GLU A CA  
621  C C   . GLU A 249 ? 0.2571 0.4119 0.2098 0.0663  0.0044  0.0242  249 GLU A C   
622  O O   . GLU A 249 ? 0.2467 0.4133 0.2128 0.0551  0.0015  0.0180  249 GLU A O   
623  C CB  . GLU A 249 ? 0.2888 0.4648 0.2282 0.0807  -0.0035 0.0289  249 GLU A CB  
624  C CG  . GLU A 249 ? 0.3528 0.5483 0.2859 0.0952  -0.0092 0.0326  249 GLU A CG  
625  C CD  . GLU A 249 ? 0.4562 0.6641 0.3852 0.0916  -0.0151 0.0301  249 GLU A CD  
626  O OE1 . GLU A 249 ? 0.5141 0.7243 0.4288 0.1037  -0.0167 0.0356  249 GLU A OE1 
627  O OE2 . GLU A 249 ? 0.4561 0.6697 0.3942 0.0775  -0.0179 0.0225  249 GLU A OE2 
628  N N   . VAL A 250 ? 0.2695 0.3965 0.2106 0.0659  0.0116  0.0281  250 VAL A N   
629  C CA  . VAL A 250 ? 0.2795 0.3923 0.2241 0.0519  0.0159  0.0253  250 VAL A CA  
630  C C   . VAL A 250 ? 0.2949 0.3947 0.2272 0.0497  0.0195  0.0296  250 VAL A C   
631  O O   . VAL A 250 ? 0.3119 0.3906 0.2286 0.0551  0.0247  0.0362  250 VAL A O   
632  C CB  . VAL A 250 ? 0.3009 0.3934 0.2423 0.0510  0.0214  0.0256  250 VAL A CB  
633  C CG1 . VAL A 250 ? 0.3089 0.3913 0.2546 0.0356  0.0248  0.0224  250 VAL A CG1 
634  C CG2 . VAL A 250 ? 0.2968 0.4032 0.2481 0.0560  0.0188  0.0222  250 VAL A CG2 
635  N N   . GLN A 251 ? 0.2897 0.4019 0.2269 0.0434  0.0168  0.0265  251 GLN A N   
636  C CA  . GLN A 251 ? 0.3043 0.4088 0.2304 0.0418  0.0205  0.0304  251 GLN A CA  
637  C C   . GLN A 251 ? 0.3186 0.4132 0.2483 0.0294  0.0264  0.0295  251 GLN A C   
638  O O   . GLN A 251 ? 0.3276 0.4273 0.2702 0.0217  0.0252  0.0239  251 GLN A O   
639  C CB  . GLN A 251 ? 0.3193 0.4423 0.2465 0.0431  0.0148  0.0269  251 GLN A CB  
640  C CG  . GLN A 251 ? 0.3457 0.4855 0.2733 0.0526  0.0071  0.0259  251 GLN A CG  
641  C CD  . GLN A 251 ? 0.3646 0.5193 0.2883 0.0538  0.0014  0.0226  251 GLN A CD  
642  O OE1 . GLN A 251 ? 0.3469 0.4997 0.2685 0.0480  0.0029  0.0197  251 GLN A OE1 
643  N NE2 . GLN A 251 ? 0.3705 0.5415 0.2924 0.0620  -0.0056 0.0225  251 GLN A NE2 
644  N N   . LEU A 252 ? 0.3206 0.4022 0.2385 0.0272  0.0328  0.0354  252 LEU A N   
645  C CA  . LEU A 252 ? 0.3175 0.3944 0.2392 0.0145  0.0386  0.0352  252 LEU A CA  
646  C C   . LEU A 252 ? 0.2911 0.3780 0.2086 0.0138  0.0407  0.0370  252 LEU A C   
647  O O   . LEU A 252 ? 0.2989 0.3791 0.2016 0.0197  0.0434  0.0435  252 LEU A O   
648  C CB  . LEU A 252 ? 0.3408 0.3922 0.2513 0.0097  0.0457  0.0411  252 LEU A CB  
649  C CG  . LEU A 252 ? 0.3717 0.4217 0.2873 -0.0060 0.0512  0.0406  252 LEU A CG  
650  C CD1 . LEU A 252 ? 0.3744 0.4363 0.3074 -0.0125 0.0474  0.0325  252 LEU A CD1 
651  C CD2 . LEU A 252 ? 0.3956 0.4176 0.2966 -0.0128 0.0584  0.0467  252 LEU A CD2 
652  N N   . TRP A 253 ? 0.2649 0.3676 0.1939 0.0084  0.0395  0.0313  253 TRP A N   
653  C CA  . TRP A 253 ? 0.2678 0.3820 0.1932 0.0093  0.0417  0.0317  253 TRP A CA  
654  C C   . TRP A 253 ? 0.2836 0.4023 0.2141 -0.0011 0.0489  0.0333  253 TRP A C   
655  O O   . TRP A 253 ? 0.2781 0.4018 0.2216 -0.0083 0.0483  0.0292  253 TRP A O   
656  C CB  . TRP A 253 ? 0.2465 0.3757 0.1787 0.0138  0.0345  0.0233  253 TRP A CB  
657  C CG  . TRP A 253 ? 0.2367 0.3674 0.1622 0.0228  0.0276  0.0219  253 TRP A CG  
658  C CD1 . TRP A 253 ? 0.2471 0.3763 0.1763 0.0257  0.0221  0.0207  253 TRP A CD1 
659  C CD2 . TRP A 253 ? 0.2286 0.3649 0.1415 0.0304  0.0256  0.0221  253 TRP A CD2 
660  N NE1 . TRP A 253 ? 0.2469 0.3829 0.1682 0.0340  0.0165  0.0202  253 TRP A NE1 
661  C CE2 . TRP A 253 ? 0.2386 0.3781 0.1493 0.0368  0.0180  0.0207  253 TRP A CE2 
662  C CE3 . TRP A 253 ? 0.2230 0.3644 0.1267 0.0327  0.0293  0.0227  253 TRP A CE3 
663  C CZ2 . TRP A 253 ? 0.2387 0.3856 0.1375 0.0444  0.0133  0.0197  253 TRP A CZ2 
664  C CZ3 . TRP A 253 ? 0.2399 0.3859 0.1300 0.0411  0.0253  0.0219  253 TRP A CZ3 
665  C CH2 . TRP A 253 ? 0.2408 0.3893 0.1285 0.0464  0.0170  0.0202  253 TRP A CH2 
666  N N   . ASP A 254 ? 0.2951 0.4152 0.2158 -0.0018 0.0555  0.0394  254 ASP A N   
667  C CA  . ASP A 254 ? 0.2997 0.4309 0.2261 -0.0116 0.0626  0.0413  254 ASP A CA  
668  C C   . ASP A 254 ? 0.2989 0.4508 0.2303 -0.0043 0.0600  0.0352  254 ASP A C   
669  O O   . ASP A 254 ? 0.3113 0.4656 0.2313 0.0048  0.0596  0.0358  254 ASP A O   
670  C CB  . ASP A 254 ? 0.3463 0.4693 0.2576 -0.0149 0.0714  0.0514  254 ASP A CB  
671  C CG  . ASP A 254 ? 0.4120 0.5499 0.3289 -0.0267 0.0800  0.0548  254 ASP A CG  
672  O OD1 . ASP A 254 ? 0.4125 0.5745 0.3420 -0.0259 0.0794  0.0495  254 ASP A OD1 
673  O OD2 . ASP A 254 ? 0.4384 0.5640 0.3459 -0.0365 0.0876  0.0632  254 ASP A OD2 
674  N N   . VAL A 255 ? 0.2777 0.4421 0.2238 -0.0069 0.0575  0.0289  255 VAL A N   
675  C CA  . VAL A 255 ? 0.2674 0.4464 0.2158 0.0015  0.0549  0.0226  255 VAL A CA  
676  C C   . VAL A 255 ? 0.2827 0.4799 0.2289 0.0029  0.0628  0.0255  255 VAL A C   
677  O O   . VAL A 255 ? 0.2820 0.4863 0.2222 0.0134  0.0615  0.0213  255 VAL A O   
678  C CB  . VAL A 255 ? 0.2513 0.4347 0.2131 0.0010  0.0494  0.0156  255 VAL A CB  
679  C CG1 . VAL A 255 ? 0.2622 0.4303 0.2258 -0.0001 0.0425  0.0131  255 VAL A CG1 
680  C CG2 . VAL A 255 ? 0.2367 0.4335 0.2114 -0.0085 0.0539  0.0173  255 VAL A CG2 
681  N N   . GLN A 256 ? 0.2877 0.4925 0.2376 -0.0078 0.0708  0.0323  256 GLN A N   
682  C CA  . GLN A 256 ? 0.3070 0.5330 0.2549 -0.0067 0.0792  0.0359  256 GLN A CA  
683  C C   . GLN A 256 ? 0.3254 0.5433 0.2540 -0.0001 0.0827  0.0410  256 GLN A C   
684  O O   . GLN A 256 ? 0.3281 0.5601 0.2500 0.0088  0.0862  0.0403  256 GLN A O   
685  C CB  . GLN A 256 ? 0.3390 0.5801 0.2977 -0.0220 0.0870  0.0416  256 GLN A CB  
686  C CG  . GLN A 256 ? 0.3953 0.6682 0.3700 -0.0206 0.0884  0.0377  256 GLN A CG  
687  C CD  . GLN A 256 ? 0.4666 0.7659 0.4384 -0.0136 0.0965  0.0404  256 GLN A CD  
688  O OE1 . GLN A 256 ? 0.4752 0.8036 0.4586 -0.0209 0.1033  0.0437  256 GLN A OE1 
689  N NE2 . GLN A 256 ? 0.4842 0.7765 0.4403 0.0007  0.0962  0.0388  256 GLN A NE2 
690  N N   . GLN A 257 ? 0.3370 0.5321 0.2549 -0.0030 0.0818  0.0462  257 GLN A N   
691  C CA  . GLN A 257 ? 0.3507 0.5372 0.2485 0.0047  0.0840  0.0516  257 GLN A CA  
692  C C   . GLN A 257 ? 0.3436 0.5244 0.2338 0.0186  0.0743  0.0442  257 GLN A C   
693  O O   . GLN A 257 ? 0.3538 0.5327 0.2273 0.0270  0.0748  0.0465  257 GLN A O   
694  C CB  . GLN A 257 ? 0.3822 0.5452 0.2693 -0.0021 0.0870  0.0610  257 GLN A CB  
695  C CG  . GLN A 257 ? 0.4211 0.5851 0.3098 -0.0178 0.0975  0.0696  257 GLN A CG  
696  C CD  . GLN A 257 ? 0.4771 0.6120 0.3475 -0.0211 0.1011  0.0796  257 GLN A CD  
697  O OE1 . GLN A 257 ? 0.5096 0.6402 0.3624 -0.0174 0.1069  0.0878  257 GLN A OE1 
698  N NE2 . GLN A 257 ? 0.4846 0.5971 0.3565 -0.0265 0.0978  0.0792  257 GLN A NE2 
699  N N   . GLN A 258 ? 0.3289 0.5064 0.2300 0.0198  0.0654  0.0357  258 GLN A N   
700  C CA  . GLN A 258 ? 0.3391 0.5107 0.2350 0.0290  0.0554  0.0282  258 GLN A CA  
701  C C   . GLN A 258 ? 0.3451 0.5038 0.2272 0.0330  0.0529  0.0335  258 GLN A C   
702  O O   . GLN A 258 ? 0.3518 0.5120 0.2196 0.0420  0.0500  0.0324  258 GLN A O   
703  C CB  . GLN A 258 ? 0.3737 0.5558 0.2624 0.0384  0.0542  0.0213  258 GLN A CB  
704  C CG  . GLN A 258 ? 0.4212 0.6163 0.3225 0.0373  0.0570  0.0168  258 GLN A CG  
705  C CD  . GLN A 258 ? 0.4754 0.6776 0.3667 0.0487  0.0568  0.0099  258 GLN A CD  
706  O OE1 . GLN A 258 ? 0.4877 0.6818 0.3644 0.0560  0.0512  0.0049  258 GLN A OE1 
707  N NE2 . GLN A 258 ? 0.4854 0.7033 0.3837 0.0509  0.0627  0.0090  258 GLN A NE2 
708  N N   . LYS A 259 ? 0.3418 0.4877 0.2257 0.0270  0.0551  0.0402  259 LYS A N   
709  C CA  . LYS A 259 ? 0.3479 0.4801 0.2180 0.0325  0.0535  0.0465  259 LYS A CA  
710  C C   . LYS A 259 ? 0.3452 0.4644 0.2228 0.0296  0.0500  0.0469  259 LYS A C   
711  O O   . LYS A 259 ? 0.3329 0.4486 0.2225 0.0200  0.0525  0.0459  259 LYS A O   
712  C CB  . LYS A 259 ? 0.3832 0.5082 0.2369 0.0318  0.0632  0.0581  259 LYS A CB  
713  C CG  . LYS A 259 ? 0.4456 0.5537 0.2996 0.0207  0.0709  0.0664  259 LYS A CG  
714  C CD  . LYS A 259 ? 0.5035 0.6021 0.3381 0.0192  0.0809  0.0787  259 LYS A CD  
715  C CE  . LYS A 259 ? 0.5594 0.6525 0.3731 0.0339  0.0782  0.0834  259 LYS A CE  
716  N NZ  . LYS A 259 ? 0.5876 0.6885 0.3862 0.0352  0.0864  0.0903  259 LYS A NZ  
717  N N   . ARG A 260 ? 0.3555 0.4693 0.2255 0.0387  0.0440  0.0478  260 ARG A N   
718  C CA  . ARG A 260 ? 0.3734 0.4763 0.2483 0.0393  0.0409  0.0484  260 ARG A CA  
719  C C   . ARG A 260 ? 0.4011 0.4816 0.2626 0.0379  0.0490  0.0592  260 ARG A C   
720  O O   . ARG A 260 ? 0.4110 0.4843 0.2543 0.0455  0.0515  0.0670  260 ARG A O   
721  C CB  . ARG A 260 ? 0.3902 0.5005 0.2618 0.0508  0.0315  0.0460  260 ARG A CB  
722  C CG  . ARG A 260 ? 0.4330 0.5380 0.3129 0.0524  0.0280  0.0451  260 ARG A CG  
723  C CD  . ARG A 260 ? 0.4797 0.5988 0.3595 0.0630  0.0187  0.0425  260 ARG A CD  
724  N NE  . ARG A 260 ? 0.5586 0.6721 0.4193 0.0757  0.0192  0.0512  260 ARG A NE  
725  C CZ  . ARG A 260 ? 0.6152 0.7446 0.4716 0.0867  0.0112  0.0506  260 ARG A CZ  
726  N NH1 . ARG A 260 ? 0.6125 0.7640 0.4825 0.0843  0.0021  0.0413  260 ARG A NH1 
727  N NH2 . ARG A 260 ? 0.6441 0.7678 0.4817 0.0996  0.0120  0.0596  260 ARG A NH2 
728  N N   . LEU A 261 ? 0.4067 0.4747 0.2751 0.0278  0.0531  0.0596  261 LEU A N   
729  C CA  . LEU A 261 ? 0.4300 0.4709 0.2837 0.0246  0.0608  0.0689  261 LEU A CA  
730  C C   . LEU A 261 ? 0.4475 0.4721 0.2926 0.0365  0.0571  0.0713  261 LEU A C   
731  O O   . LEU A 261 ? 0.4723 0.4750 0.2970 0.0431  0.0613  0.0806  261 LEU A O   
732  C CB  . LEU A 261 ? 0.4281 0.4622 0.2917 0.0078  0.0660  0.0672  261 LEU A CB  
733  C CG  . LEU A 261 ? 0.4323 0.4866 0.3066 -0.0036 0.0701  0.0651  261 LEU A CG  
734  C CD1 . LEU A 261 ? 0.4349 0.4840 0.3183 -0.0200 0.0743  0.0638  261 LEU A CD1 
735  C CD2 . LEU A 261 ? 0.4427 0.4975 0.3021 -0.0034 0.0774  0.0738  261 LEU A CD2 
736  N N   . ARG A 262 ? 0.4322 0.4671 0.2918 0.0398  0.0498  0.0634  262 ARG A N   
737  C CA  . ARG A 262 ? 0.4409 0.4647 0.2945 0.0520  0.0467  0.0650  262 ARG A CA  
738  C C   . ARG A 262 ? 0.4225 0.4720 0.2896 0.0605  0.0368  0.0580  262 ARG A C   
739  O O   . ARG A 262 ? 0.4136 0.4829 0.2975 0.0532  0.0326  0.0499  262 ARG A O   
740  C CB  . ARG A 262 ? 0.4702 0.4729 0.3259 0.0444  0.0505  0.0635  262 ARG A CB  
741  C CG  . ARG A 262 ? 0.5225 0.4980 0.3648 0.0324  0.0601  0.0698  262 ARG A CG  
742  C CD  . ARG A 262 ? 0.5564 0.5045 0.3933 0.0284  0.0632  0.0689  262 ARG A CD  
743  N NE  . ARG A 262 ? 0.5801 0.5076 0.3990 0.0463  0.0628  0.0741  262 ARG A NE  
744  C CZ  . ARG A 262 ? 0.5963 0.4918 0.4019 0.0483  0.0664  0.0751  262 ARG A CZ  
745  N NH1 . ARG A 262 ? 0.5900 0.4703 0.3982 0.0313  0.0701  0.0708  262 ARG A NH1 
746  N NH2 . ARG A 262 ? 0.5949 0.4733 0.3832 0.0680  0.0662  0.0803  262 ARG A NH2 
747  N N   . ASN A 263 ? 0.4195 0.4685 0.2787 0.0759  0.0333  0.0613  263 ASN A N   
748  C CA  . ASN A 263 ? 0.4161 0.4914 0.2886 0.0833  0.0243  0.0553  263 ASN A CA  
749  C C   . ASN A 263 ? 0.4290 0.4922 0.2982 0.0931  0.0254  0.0576  263 ASN A C   
750  O O   . ASN A 263 ? 0.4438 0.5018 0.2987 0.1094  0.0250  0.0643  263 ASN A O   
751  C CB  . ASN A 263 ? 0.4268 0.5218 0.2928 0.0946  0.0179  0.0572  263 ASN A CB  
752  C CG  . ASN A 263 ? 0.4644 0.5915 0.3475 0.0960  0.0079  0.0492  263 ASN A CG  
753  O OD1 . ASN A 263 ? 0.4600 0.5958 0.3607 0.0854  0.0061  0.0415  263 ASN A OD1 
754  N ND2 . ASN A 263 ? 0.4758 0.6219 0.3537 0.1085  0.0012  0.0510  263 ASN A ND2 
755  N N   . MET A 264 ? 0.4210 0.4781 0.3012 0.0844  0.0274  0.0524  264 MET A N   
756  C CA  . MET A 264 ? 0.4282 0.4692 0.3031 0.0929  0.0300  0.0537  264 MET A CA  
757  C C   . MET A 264 ? 0.4233 0.4908 0.3102 0.1041  0.0236  0.0502  264 MET A C   
758  O O   . MET A 264 ? 0.4128 0.5050 0.3195 0.0957  0.0189  0.0428  264 MET A O   
759  C CB  . MET A 264 ? 0.4276 0.4486 0.3060 0.0783  0.0354  0.0497  264 MET A CB  
760  C CG  . MET A 264 ? 0.4482 0.4459 0.3156 0.0659  0.0421  0.0536  264 MET A CG  
761  S SD  . MET A 264 ? 0.4629 0.4421 0.3350 0.0467  0.0472  0.0484  264 MET A SD  
762  C CE  . MET A 264 ? 0.4281 0.4434 0.3277 0.0365  0.0409  0.0391  264 MET A CE  
763  N N   . THR A 265 ? 0.4272 0.4898 0.3011 0.1235  0.0239  0.0560  265 THR A N   
764  C CA  . THR A 265 ? 0.4191 0.5100 0.3041 0.1361  0.0186  0.0538  265 THR A CA  
765  C C   . THR A 265 ? 0.4351 0.5045 0.3115 0.1464  0.0241  0.0547  265 THR A C   
766  O O   . THR A 265 ? 0.4788 0.5094 0.3325 0.1528  0.0308  0.0604  265 THR A O   
767  C CB  . THR A 265 ? 0.4253 0.5392 0.3052 0.1529  0.0127  0.0588  265 THR A CB  
768  O OG1 . THR A 265 ? 0.4566 0.5394 0.3097 0.1675  0.0178  0.0687  265 THR A OG1 
769  C CG2 . THR A 265 ? 0.4162 0.5564 0.3063 0.1422  0.0058  0.0554  265 THR A CG2 
770  N N   . SER A 266 ? 0.3998 0.4934 0.2928 0.1478  0.0215  0.0492  266 SER A N   
771  C CA  . SER A 266 ? 0.3975 0.4775 0.2849 0.1585  0.0262  0.0484  266 SER A CA  
772  C C   . SER A 266 ? 0.3650 0.4859 0.2755 0.1591  0.0219  0.0426  266 SER A C   
773  O O   . SER A 266 ? 0.3693 0.4990 0.2775 0.1770  0.0231  0.0439  266 SER A O   
774  C CB  . SER A 266 ? 0.4238 0.4642 0.3021 0.1448  0.0331  0.0454  266 SER A CB  
775  O OG  . SER A 266 ? 0.4329 0.4853 0.3298 0.1225  0.0312  0.0385  266 SER A OG  
776  N N   . HIS A 267 ? 0.3374 0.4832 0.2690 0.1402  0.0172  0.0367  267 HIS A N   
777  C CA  . HIS A 267 ? 0.3150 0.4984 0.2684 0.1367  0.0135  0.0317  267 HIS A CA  
778  C C   . HIS A 267 ? 0.2994 0.5256 0.2627 0.1484  0.0068  0.0338  267 HIS A C   
779  O O   . HIS A 267 ? 0.2904 0.5214 0.2468 0.1546  0.0029  0.0379  267 HIS A O   
780  C CB  . HIS A 267 ? 0.3020 0.4925 0.2712 0.1127  0.0110  0.0254  267 HIS A CB  
781  C CG  . HIS A 267 ? 0.3118 0.4752 0.2782 0.1021  0.0167  0.0218  267 HIS A CG  
782  N ND1 . HIS A 267 ? 0.3266 0.4914 0.2956 0.1062  0.0202  0.0193  267 HIS A ND1 
783  C CD2 . HIS A 267 ? 0.3268 0.4646 0.2883 0.0881  0.0191  0.0202  267 HIS A CD2 
784  C CE1 . HIS A 267 ? 0.3410 0.4800 0.3058 0.0942  0.0240  0.0160  267 HIS A CE1 
785  N NE2 . HIS A 267 ? 0.3381 0.4617 0.2992 0.0828  0.0233  0.0165  267 HIS A NE2 
786  N N   . SER A 268 ? 0.2837 0.5435 0.2632 0.1508  0.0055  0.0312  268 SER A N   
787  C CA  . SER A 268 ? 0.2692 0.5772 0.2618 0.1590  -0.0014 0.0326  268 SER A CA  
788  C C   . SER A 268 ? 0.2433 0.5839 0.2575 0.1367  -0.0086 0.0270  268 SER A C   
789  O O   . SER A 268 ? 0.2395 0.6220 0.2659 0.1385  -0.0153 0.0270  268 SER A O   
790  C CB  . SER A 268 ? 0.2874 0.6179 0.2848 0.1768  0.0018  0.0340  268 SER A CB  
791  O OG  . SER A 268 ? 0.3417 0.6760 0.3514 0.1636  0.0053  0.0288  268 SER A OG  
792  N N   . ALA A 269 ? 0.2239 0.5459 0.2422 0.1159  -0.0072 0.0221  269 ALA A N   
793  C CA  . ALA A 269 ? 0.2000 0.5447 0.2350 0.0948  -0.0130 0.0168  269 ALA A CA  
794  C C   . ALA A 269 ? 0.2011 0.5132 0.2306 0.0778  -0.0121 0.0133  269 ALA A C   
795  O O   . ALA A 269 ? 0.2150 0.4923 0.2307 0.0815  -0.0068 0.0151  269 ALA A O   
796  C CB  . ALA A 269 ? 0.1817 0.5509 0.2329 0.0893  -0.0110 0.0145  269 ALA A CB  
797  N N   . ARG A 270 ? 0.1880 0.5104 0.2272 0.0594  -0.0171 0.0085  270 ARG A N   
798  C CA  . ARG A 270 ? 0.2059 0.5005 0.2396 0.0460  -0.0164 0.0053  270 ARG A CA  
799  C C   . ARG A 270 ? 0.2163 0.4814 0.2454 0.0441  -0.0089 0.0054  270 ARG A C   
800  O O   . ARG A 270 ? 0.2171 0.4850 0.2505 0.0471  -0.0048 0.0058  270 ARG A O   
801  C CB  . ARG A 270 ? 0.2170 0.5243 0.2604 0.0276  -0.0220 -0.0002 270 ARG A CB  
802  C CG  . ARG A 270 ? 0.2452 0.5638 0.3012 0.0179  -0.0201 -0.0018 270 ARG A CG  
803  C CD  . ARG A 270 ? 0.2648 0.5841 0.3250 -0.0011 -0.0247 -0.0067 270 ARG A CD  
804  N NE  . ARG A 270 ? 0.2579 0.5799 0.3269 -0.0119 -0.0217 -0.0075 270 ARG A NE  
805  C CZ  . ARG A 270 ? 0.2722 0.5983 0.3457 -0.0290 -0.0251 -0.0107 270 ARG A CZ  
806  N NH1 . ARG A 270 ? 0.2516 0.5788 0.3312 -0.0377 -0.0216 -0.0100 270 ARG A NH1 
807  N NH2 . ARG A 270 ? 0.2709 0.5982 0.3408 -0.0375 -0.0319 -0.0146 270 ARG A NH2 
808  N N   . VAL A 271 ? 0.2111 0.4495 0.2305 0.0399  -0.0071 0.0051  271 VAL A N   
809  C CA  . VAL A 271 ? 0.2165 0.4291 0.2316 0.0363  -0.0009 0.0048  271 VAL A CA  
810  C C   . VAL A 271 ? 0.2043 0.4145 0.2263 0.0208  -0.0024 0.0003  271 VAL A C   
811  O O   . VAL A 271 ? 0.2078 0.4090 0.2257 0.0154  -0.0040 -0.0011 271 VAL A O   
812  C CB  . VAL A 271 ? 0.2402 0.4274 0.2403 0.0419  0.0028  0.0082  271 VAL A CB  
813  C CG1 . VAL A 271 ? 0.2593 0.4224 0.2559 0.0347  0.0083  0.0070  271 VAL A CG1 
814  C CG2 . VAL A 271 ? 0.2447 0.4298 0.2351 0.0589  0.0048  0.0134  271 VAL A CG2 
815  N N   . GLY A 272 ? 0.1810 0.3995 0.2120 0.0150  -0.0017 -0.0015 272 GLY A N   
816  C CA  . GLY A 272 ? 0.1828 0.3987 0.2189 0.0015  -0.0032 -0.0049 272 GLY A CA  
817  C C   . GLY A 272 ? 0.1906 0.3856 0.2230 -0.0025 0.0010  -0.0056 272 GLY A C   
818  O O   . GLY A 272 ? 0.1944 0.3845 0.2285 -0.0114 -0.0003 -0.0078 272 GLY A O   
819  N N   . SER A 273 ? 0.1855 0.3678 0.2119 0.0040  0.0058  -0.0040 273 SER A N   
820  C CA  . SER A 273 ? 0.1904 0.3561 0.2137 -0.0010 0.0091  -0.0052 273 SER A CA  
821  C C   . SER A 273 ? 0.1936 0.3408 0.2066 0.0031  0.0128  -0.0035 273 SER A C   
822  O O   . SER A 273 ? 0.1856 0.3288 0.1917 0.0123  0.0143  -0.0008 273 SER A O   
823  C CB  . SER A 273 ? 0.2059 0.3745 0.2325 -0.0023 0.0113  -0.0063 273 SER A CB  
824  O OG  . SER A 273 ? 0.2259 0.3971 0.2494 0.0079  0.0141  -0.0050 273 SER A OG  
825  N N   . LEU A 274 ? 0.1963 0.3329 0.2075 -0.0038 0.0141  -0.0045 274 LEU A N   
826  C CA  . LEU A 274 ? 0.2023 0.3222 0.2043 -0.0040 0.0179  -0.0028 274 LEU A CA  
827  C C   . LEU A 274 ? 0.2074 0.3209 0.2102 -0.0128 0.0196  -0.0052 274 LEU A C   
828  O O   . LEU A 274 ? 0.1972 0.3198 0.2074 -0.0179 0.0172  -0.0072 274 LEU A O   
829  C CB  . LEU A 274 ? 0.1959 0.3168 0.1957 -0.0043 0.0170  -0.0009 274 LEU A CB  
830  C CG  . LEU A 274 ? 0.2077 0.3349 0.2042 0.0041  0.0148  0.0017  274 LEU A CG  
831  C CD1 . LEU A 274 ? 0.2103 0.3407 0.2049 0.0026  0.0133  0.0021  274 LEU A CD1 
832  C CD2 . LEU A 274 ? 0.2151 0.3291 0.2003 0.0127  0.0184  0.0058  274 LEU A CD2 
833  N N   . SER A 275 ? 0.2178 0.3149 0.2118 -0.0147 0.0235  -0.0047 275 SER A N   
834  C CA  . SER A 275 ? 0.2302 0.3232 0.2246 -0.0245 0.0247  -0.0072 275 SER A CA  
835  C C   . SER A 275 ? 0.2619 0.3361 0.2451 -0.0287 0.0290  -0.0056 275 SER A C   
836  O O   . SER A 275 ? 0.2839 0.3404 0.2556 -0.0233 0.0318  -0.0042 275 SER A O   
837  C CB  . SER A 275 ? 0.2232 0.3165 0.2186 -0.0256 0.0241  -0.0110 275 SER A CB  
838  O OG  . SER A 275 ? 0.2211 0.3121 0.2161 -0.0353 0.0243  -0.0138 275 SER A OG  
839  N N   . TRP A 276 ? 0.2621 0.3398 0.2479 -0.0384 0.0299  -0.0054 276 TRP A N   
840  C CA  . TRP A 276 ? 0.2796 0.3407 0.2553 -0.0462 0.0344  -0.0035 276 TRP A CA  
841  C C   . TRP A 276 ? 0.2947 0.3472 0.2668 -0.0571 0.0350  -0.0081 276 TRP A C   
842  O O   . TRP A 276 ? 0.2728 0.3405 0.2540 -0.0611 0.0317  -0.0119 276 TRP A O   
843  C CB  . TRP A 276 ? 0.2655 0.3399 0.2469 -0.0522 0.0355  -0.0007 276 TRP A CB  
844  C CG  . TRP A 276 ? 0.2720 0.3500 0.2521 -0.0434 0.0359  0.0038  276 TRP A CG  
845  C CD1 . TRP A 276 ? 0.2779 0.3732 0.2663 -0.0365 0.0322  0.0032  276 TRP A CD1 
846  C CD2 . TRP A 276 ? 0.2820 0.3455 0.2499 -0.0418 0.0404  0.0094  276 TRP A CD2 
847  N NE1 . TRP A 276 ? 0.2854 0.3793 0.2679 -0.0304 0.0336  0.0073  276 TRP A NE1 
848  C CE2 . TRP A 276 ? 0.2924 0.3680 0.2626 -0.0330 0.0387  0.0118  276 TRP A CE2 
849  C CE3 . TRP A 276 ? 0.3019 0.3409 0.2550 -0.0470 0.0456  0.0129  276 TRP A CE3 
850  C CZ2 . TRP A 276 ? 0.3100 0.3769 0.2689 -0.0284 0.0419  0.0177  276 TRP A CZ2 
851  C CZ3 . TRP A 276 ? 0.3254 0.3535 0.2669 -0.0425 0.0494  0.0196  276 TRP A CZ3 
852  C CH2 . TRP A 276 ? 0.3254 0.3688 0.2702 -0.0329 0.0474  0.0221  276 TRP A CH2 
853  N N   . ASN A 277 ? 0.3283 0.3554 0.2855 -0.0627 0.0392  -0.0073 277 ASN A N   
854  C CA  . ASN A 277 ? 0.3549 0.3689 0.3048 -0.0764 0.0402  -0.0118 277 ASN A CA  
855  C C   . ASN A 277 ? 0.3820 0.3788 0.3212 -0.0868 0.0454  -0.0075 277 ASN A C   
856  O O   . ASN A 277 ? 0.4066 0.3726 0.3278 -0.0827 0.0494  -0.0048 277 ASN A O   
857  C CB  . ASN A 277 ? 0.3914 0.3815 0.3273 -0.0707 0.0408  -0.0159 277 ASN A CB  
858  C CG  . ASN A 277 ? 0.4538 0.4269 0.3789 -0.0856 0.0415  -0.0217 277 ASN A CG  
859  O OD1 . ASN A 277 ? 0.4660 0.4532 0.3985 -0.1012 0.0400  -0.0236 277 ASN A OD1 
860  N ND2 . ASN A 277 ? 0.4934 0.4362 0.3998 -0.0809 0.0436  -0.0250 277 ASN A ND2 
861  N N   . SER A 278 ? 0.3709 0.3885 0.3209 -0.0987 0.0457  -0.0060 278 SER A N   
862  C CA  . SER A 278 ? 0.3889 0.3963 0.3312 -0.1102 0.0512  -0.0007 278 SER A CA  
863  C C   . SER A 278 ? 0.4120 0.4087 0.3466 -0.0964 0.0545  0.0069  278 SER A C   
864  O O   . SER A 278 ? 0.3957 0.4131 0.3412 -0.0838 0.0517  0.0081  278 SER A O   
865  C CB  . SER A 278 ? 0.4212 0.3972 0.3460 -0.1254 0.0542  -0.0035 278 SER A CB  
866  O OG  . SER A 278 ? 0.4758 0.4432 0.3937 -0.1395 0.0600  0.0020  278 SER A OG  
867  N N   . TYR A 279 ? 0.4409 0.4042 0.3552 -0.0978 0.0600  0.0116  279 TYR A N   
868  C CA  . TYR A 279 ? 0.4579 0.4095 0.3619 -0.0839 0.0629  0.0193  279 TYR A CA  
869  C C   . TYR A 279 ? 0.4499 0.3883 0.3466 -0.0638 0.0602  0.0183  279 TYR A C   
870  O O   . TYR A 279 ? 0.4633 0.3935 0.3511 -0.0502 0.0616  0.0243  279 TYR A O   
871  C CB  . TYR A 279 ? 0.4965 0.4163 0.3796 -0.0940 0.0704  0.0260  279 TYR A CB  
872  C CG  . TYR A 279 ? 0.5562 0.4368 0.4198 -0.1027 0.0727  0.0225  279 TYR A CG  
873  C CD1 . TYR A 279 ? 0.5951 0.4461 0.4420 -0.0867 0.0724  0.0214  279 TYR A CD1 
874  C CD2 . TYR A 279 ? 0.5820 0.4559 0.4430 -0.1266 0.0751  0.0199  279 TYR A CD2 
875  C CE1 . TYR A 279 ? 0.6319 0.4440 0.4582 -0.0930 0.0747  0.0172  279 TYR A CE1 
876  C CE2 . TYR A 279 ? 0.6180 0.4519 0.4580 -0.1357 0.0769  0.0157  279 TYR A CE2 
877  C CZ  . TYR A 279 ? 0.6553 0.4562 0.4767 -0.1181 0.0769  0.0142  279 TYR A CZ  
878  O OH  . TYR A 279 ? 0.7127 0.4708 0.5104 -0.1251 0.0790  0.0092  279 TYR A OH  
879  N N   . ILE A 280 ? 0.4291 0.3673 0.3291 -0.0616 0.0567  0.0110  280 ILE A N   
880  C CA  . ILE A 280 ? 0.4182 0.3508 0.3141 -0.0429 0.0546  0.0099  280 ILE A CA  
881  C C   . ILE A 280 ? 0.3922 0.3618 0.3096 -0.0354 0.0489  0.0082  280 ILE A C   
882  O O   . ILE A 280 ? 0.3864 0.3772 0.3187 -0.0434 0.0456  0.0034  280 ILE A O   
883  C CB  . ILE A 280 ? 0.4315 0.3444 0.3179 -0.0436 0.0546  0.0031  280 ILE A CB  
884  C CG1 . ILE A 280 ? 0.4637 0.3321 0.3237 -0.0498 0.0604  0.0044  280 ILE A CG1 
885  C CG2 . ILE A 280 ? 0.4365 0.3560 0.3247 -0.0239 0.0521  0.0014  280 ILE A CG2 
886  C CD1 . ILE A 280 ? 0.4925 0.3342 0.3329 -0.0336 0.0644  0.0119  280 ILE A CD1 
887  N N   . LEU A 281 ? 0.3723 0.3486 0.2898 -0.0202 0.0475  0.0120  281 LEU A N   
888  C CA  . LEU A 281 ? 0.3423 0.3496 0.2772 -0.0135 0.0420  0.0103  281 LEU A CA  
889  C C   . LEU A 281 ? 0.3356 0.3425 0.2690 -0.0002 0.0404  0.0084  281 LEU A C   
890  O O   . LEU A 281 ? 0.3540 0.3462 0.2743 0.0121  0.0424  0.0122  281 LEU A O   
891  C CB  . LEU A 281 ? 0.3386 0.3569 0.2746 -0.0074 0.0412  0.0156  281 LEU A CB  
892  C CG  . LEU A 281 ? 0.3315 0.3775 0.2815 -0.0001 0.0353  0.0138  281 LEU A CG  
893  C CD1 . LEU A 281 ? 0.3119 0.3773 0.2782 -0.0094 0.0320  0.0083  281 LEU A CD1 
894  C CD2 . LEU A 281 ? 0.3394 0.3919 0.2862 0.0050  0.0348  0.0184  281 LEU A CD2 
895  N N   . SER A 282 ? 0.3074 0.3326 0.2539 -0.0015 0.0369  0.0034  282 SER A N   
896  C CA  . SER A 282 ? 0.2928 0.3245 0.2406 0.0103  0.0356  0.0018  282 SER A CA  
897  C C   . SER A 282 ? 0.2585 0.3192 0.2208 0.0153  0.0308  0.0028  282 SER A C   
898  O O   . SER A 282 ? 0.2398 0.3162 0.2138 0.0070  0.0277  0.0014  282 SER A O   
899  C CB  . SER A 282 ? 0.2958 0.3271 0.2462 0.0047  0.0356  -0.0042 282 SER A CB  
900  O OG  . SER A 282 ? 0.3189 0.3214 0.2537 -0.0011 0.0395  -0.0062 282 SER A OG  
901  N N   . SER A 283 ? 0.2473 0.3152 0.2080 0.0290  0.0300  0.0049  283 SER A N   
902  C CA  . SER A 283 ? 0.2374 0.3338 0.2110 0.0326  0.0250  0.0055  283 SER A CA  
903  C C   . SER A 283 ? 0.2451 0.3581 0.2251 0.0402  0.0242  0.0040  283 SER A C   
904  O O   . SER A 283 ? 0.2519 0.3548 0.2223 0.0515  0.0277  0.0049  283 SER A O   
905  C CB  . SER A 283 ? 0.2432 0.3405 0.2101 0.0418  0.0239  0.0107  283 SER A CB  
906  O OG  . SER A 283 ? 0.2544 0.3364 0.2070 0.0561  0.0274  0.0143  283 SER A OG  
907  N N   . GLY A 284 ? 0.2418 0.3796 0.2368 0.0343  0.0201  0.0019  284 GLY A N   
908  C CA  . GLY A 284 ? 0.2465 0.4061 0.2503 0.0390  0.0195  0.0009  284 GLY A CA  
909  C C   . GLY A 284 ? 0.2472 0.4338 0.2602 0.0421  0.0145  0.0028  284 GLY A C   
910  O O   . GLY A 284 ? 0.2434 0.4345 0.2601 0.0344  0.0104  0.0024  284 GLY A O   
911  N N   . SER A 285 ? 0.2448 0.4509 0.2611 0.0534  0.0148  0.0043  285 SER A N   
912  C CA  . SER A 285 ? 0.2475 0.4835 0.2726 0.0571  0.0096  0.0061  285 SER A CA  
913  C C   . SER A 285 ? 0.2360 0.5055 0.2767 0.0535  0.0081  0.0049  285 SER A C   
914  O O   . SER A 285 ? 0.2224 0.4933 0.2649 0.0545  0.0126  0.0040  285 SER A O   
915  C CB  . SER A 285 ? 0.2850 0.5197 0.2997 0.0766  0.0107  0.0105  285 SER A CB  
916  O OG  . SER A 285 ? 0.3195 0.5865 0.3422 0.0817  0.0050  0.0123  285 SER A OG  
917  N N   . ARG A 286 ? 0.2352 0.5332 0.2863 0.0490  0.0019  0.0050  286 ARG A N   
918  C CA  . ARG A 286 ? 0.2301 0.5653 0.2969 0.0443  0.0001  0.0047  286 ARG A CA  
919  C C   . ARG A 286 ? 0.2241 0.5783 0.2921 0.0628  0.0044  0.0076  286 ARG A C   
920  O O   . ARG A 286 ? 0.2185 0.5985 0.2978 0.0602  0.0063  0.0075  286 ARG A O   
921  C CB  . ARG A 286 ? 0.2528 0.6133 0.3278 0.0363  -0.0081 0.0039  286 ARG A CB  
922  C CG  . ARG A 286 ? 0.2976 0.6976 0.3898 0.0255  -0.0109 0.0031  286 ARG A CG  
923  C CD  . ARG A 286 ? 0.3626 0.7793 0.4603 0.0114  -0.0196 0.0004  286 ARG A CD  
924  N NE  . ARG A 286 ? 0.4364 0.8573 0.5273 0.0234  -0.0245 0.0014  286 ARG A NE  
925  C CZ  . ARG A 286 ? 0.4690 0.8922 0.5574 0.0147  -0.0321 -0.0016 286 ARG A CZ  
926  N NH1 . ARG A 286 ? 0.4380 0.8637 0.5181 0.0276  -0.0359 0.0000  286 ARG A NH1 
927  N NH2 . ARG A 286 ? 0.4805 0.9013 0.5725 -0.0064 -0.0358 -0.0062 286 ARG A NH2 
928  N N   . SER A 287 ? 0.2342 0.5730 0.2887 0.0819  0.0068  0.0103  287 SER A N   
929  C CA  . SER A 287 ? 0.2426 0.5924 0.2936 0.1031  0.0116  0.0130  287 SER A CA  
930  C C   . SER A 287 ? 0.2528 0.5856 0.2987 0.1047  0.0194  0.0108  287 SER A C   
931  O O   . SER A 287 ? 0.2610 0.6074 0.3058 0.1209  0.0240  0.0120  287 SER A O   
932  C CB  . SER A 287 ? 0.2798 0.6055 0.3123 0.1223  0.0127  0.0166  287 SER A CB  
933  O OG  . SER A 287 ? 0.3384 0.6169 0.3551 0.1166  0.0163  0.0152  287 SER A OG  
934  N N   . GLY A 288 ? 0.2481 0.5508 0.2890 0.0901  0.0209  0.0077  288 GLY A N   
935  C CA  . GLY A 288 ? 0.2519 0.5361 0.2856 0.0905  0.0273  0.0050  288 GLY A CA  
936  C C   . GLY A 288 ? 0.2685 0.5079 0.2804 0.0986  0.0314  0.0040  288 GLY A C   
937  O O   . GLY A 288 ? 0.2798 0.4992 0.2831 0.0971  0.0360  0.0007  288 GLY A O   
938  N N   . HIS A 289 ? 0.2673 0.4900 0.2689 0.1060  0.0298  0.0069  289 HIS A N   
939  C CA  . HIS A 289 ? 0.2890 0.4671 0.2683 0.1119  0.0339  0.0067  289 HIS A CA  
940  C C   . HIS A 289 ? 0.2917 0.4452 0.2683 0.0937  0.0323  0.0050  289 HIS A C   
941  O O   . HIS A 289 ? 0.2819 0.4491 0.2700 0.0816  0.0273  0.0055  289 HIS A O   
942  C CB  . HIS A 289 ? 0.3048 0.4747 0.2707 0.1318  0.0344  0.0119  289 HIS A CB  
943  C CG  . HIS A 289 ? 0.3311 0.5269 0.2986 0.1535  0.0363  0.0141  289 HIS A CG  
944  N ND1 . HIS A 289 ? 0.3663 0.5505 0.3230 0.1662  0.0428  0.0117  289 HIS A ND1 
945  C CD2 . HIS A 289 ? 0.3239 0.5582 0.3025 0.1647  0.0323  0.0181  289 HIS A CD2 
946  C CE1 . HIS A 289 ? 0.3618 0.5783 0.3236 0.1861  0.0432  0.0149  289 HIS A CE1 
947  N NE2 . HIS A 289 ? 0.3402 0.5890 0.3158 0.1857  0.0367  0.0189  289 HIS A NE2 
948  N N   . ILE A 290 ? 0.3009 0.4180 0.2611 0.0919  0.0366  0.0028  290 ILE A N   
949  C CA  . ILE A 290 ? 0.3055 0.3993 0.2615 0.0759  0.0359  0.0016  290 ILE A CA  
950  C C   . ILE A 290 ? 0.3258 0.3851 0.2604 0.0840  0.0393  0.0049  290 ILE A C   
951  O O   . ILE A 290 ? 0.3432 0.3819 0.2614 0.0970  0.0439  0.0046  290 ILE A O   
952  C CB  . ILE A 290 ? 0.3114 0.3933 0.2665 0.0635  0.0378  -0.0041 290 ILE A CB  
953  C CG1 . ILE A 290 ? 0.2965 0.4093 0.2709 0.0541  0.0346  -0.0062 290 ILE A CG1 
954  C CG2 . ILE A 290 ? 0.3269 0.3825 0.2743 0.0494  0.0380  -0.0052 290 ILE A CG2 
955  C CD1 . ILE A 290 ? 0.3059 0.4111 0.2771 0.0481  0.0370  -0.0113 290 ILE A CD1 
956  N N   . HIS A 291 ? 0.3252 0.3759 0.2578 0.0767  0.0377  0.0082  291 HIS A N   
957  C CA  . HIS A 291 ? 0.3465 0.3621 0.2575 0.0818  0.0416  0.0122  291 HIS A CA  
958  C C   . HIS A 291 ? 0.3749 0.3689 0.2818 0.0626  0.0431  0.0105  291 HIS A C   
959  O O   . HIS A 291 ? 0.3711 0.3836 0.2934 0.0490  0.0397  0.0090  291 HIS A O   
960  C CB  . HIS A 291 ? 0.3378 0.3634 0.2473 0.0918  0.0392  0.0192  291 HIS A CB  
961  C CG  . HIS A 291 ? 0.3348 0.3812 0.2455 0.1129  0.0377  0.0220  291 HIS A CG  
962  N ND1 . HIS A 291 ? 0.3381 0.3997 0.2486 0.1234  0.0343  0.0278  291 HIS A ND1 
963  C CD2 . HIS A 291 ? 0.3382 0.3946 0.2500 0.1255  0.0393  0.0198  291 HIS A CD2 
964  C CE1 . HIS A 291 ? 0.3356 0.4185 0.2488 0.1415  0.0334  0.0291  291 HIS A CE1 
965  N NE2 . HIS A 291 ? 0.3366 0.4177 0.2510 0.1437  0.0368  0.0245  291 HIS A NE2 
966  N N   . HIS A 292 ? 0.3941 0.3489 0.2794 0.0614  0.0483  0.0108  292 HIS A N   
967  C CA  . HIS A 292 ? 0.3971 0.3332 0.2780 0.0423  0.0500  0.0103  292 HIS A CA  
968  C C   . HIS A 292 ? 0.3945 0.3160 0.2631 0.0460  0.0522  0.0184  292 HIS A C   
969  O O   . HIS A 292 ? 0.4070 0.3073 0.2571 0.0619  0.0551  0.0232  292 HIS A O   
970  C CB  . HIS A 292 ? 0.4323 0.3328 0.2953 0.0349  0.0543  0.0057  292 HIS A CB  
971  C CG  . HIS A 292 ? 0.4604 0.3730 0.3329 0.0289  0.0524  -0.0026 292 HIS A CG  
972  N ND1 . HIS A 292 ? 0.4640 0.4123 0.3603 0.0202  0.0476  -0.0051 292 HIS A ND1 
973  C CD2 . HIS A 292 ? 0.4878 0.3794 0.3466 0.0311  0.0550  -0.0085 292 HIS A CD2 
974  C CE1 . HIS A 292 ? 0.4692 0.4188 0.3662 0.0177  0.0473  -0.0117 292 HIS A CE1 
975  N NE2 . HIS A 292 ? 0.4873 0.4044 0.3624 0.0238  0.0516  -0.0143 292 HIS A NE2 
976  N N   . HIS A 293 ? 0.3800 0.3122 0.2574 0.0325  0.0511  0.0203  293 HIS A N   
977  C CA  . HIS A 293 ? 0.3986 0.3196 0.2650 0.0338  0.0535  0.0283  293 HIS A CA  
978  C C   . HIS A 293 ? 0.4199 0.3201 0.2790 0.0141  0.0580  0.0289  293 HIS A C   
979  O O   . HIS A 293 ? 0.4021 0.3209 0.2771 -0.0014 0.0561  0.0245  293 HIS A O   
980  C CB  . HIS A 293 ? 0.3773 0.3337 0.2607 0.0353  0.0486  0.0303  293 HIS A CB  
981  C CG  . HIS A 293 ? 0.3726 0.3571 0.2679 0.0495  0.0430  0.0287  293 HIS A CG  
982  N ND1 . HIS A 293 ? 0.3951 0.3803 0.2810 0.0680  0.0422  0.0342  293 HIS A ND1 
983  C CD2 . HIS A 293 ? 0.3659 0.3791 0.2811 0.0466  0.0382  0.0228  293 HIS A CD2 
984  C CE1 . HIS A 293 ? 0.3837 0.4012 0.2860 0.0746  0.0367  0.0309  293 HIS A CE1 
985  N NE2 . HIS A 293 ? 0.3717 0.4050 0.2911 0.0615  0.0344  0.0242  293 HIS A NE2 
986  N N   . ASP A 294 ? 0.4506 0.3131 0.2850 0.0146  0.0639  0.0348  294 ASP A N   
987  C CA  . ASP A 294 ? 0.4717 0.3164 0.2987 -0.0058 0.0688  0.0368  294 ASP A CA  
988  C C   . ASP A 294 ? 0.4719 0.3320 0.3016 -0.0036 0.0693  0.0447  294 ASP A C   
989  O O   . ASP A 294 ? 0.4900 0.3318 0.3016 0.0092  0.0720  0.0527  294 ASP A O   
990  C CB  . ASP A 294 ? 0.5146 0.3073 0.3111 -0.0080 0.0754  0.0396  294 ASP A CB  
991  C CG  . ASP A 294 ? 0.5836 0.3591 0.3728 -0.0327 0.0807  0.0418  294 ASP A CG  
992  O OD1 . ASP A 294 ? 0.5597 0.3646 0.3654 -0.0439 0.0802  0.0440  294 ASP A OD1 
993  O OD2 . ASP A 294 ? 0.6413 0.3739 0.4072 -0.0411 0.0855  0.0414  294 ASP A OD2 
994  N N   . VAL A 295 ? 0.4511 0.3455 0.3022 -0.0138 0.0665  0.0424  295 VAL A N   
995  C CA  . VAL A 295 ? 0.4464 0.3598 0.3011 -0.0103 0.0664  0.0483  295 VAL A CA  
996  C C   . VAL A 295 ? 0.4635 0.3555 0.3009 -0.0194 0.0740  0.0571  295 VAL A C   
997  O O   . VAL A 295 ? 0.4650 0.3678 0.3000 -0.0138 0.0749  0.0633  295 VAL A O   
998  C CB  . VAL A 295 ? 0.4320 0.3858 0.3123 -0.0167 0.0616  0.0428  295 VAL A CB  
999  C CG1 . VAL A 295 ? 0.4209 0.3936 0.3165 -0.0087 0.0546  0.0351  295 VAL A CG1 
1000 C CG2 . VAL A 295 ? 0.4282 0.3870 0.3163 -0.0377 0.0647  0.0403  295 VAL A CG2 
1001 N N   . ARG A 296 ? 0.4775 0.3382 0.3011 -0.0335 0.0796  0.0578  296 ARG A N   
1002 C CA  . ARG A 296 ? 0.4967 0.3343 0.3025 -0.0450 0.0877  0.0667  296 ARG A CA  
1003 C C   . ARG A 296 ? 0.5240 0.3213 0.2993 -0.0303 0.0920  0.0761  296 ARG A C   
1004 O O   . ARG A 296 ? 0.5332 0.3122 0.2916 -0.0366 0.0989  0.0856  296 ARG A O   
1005 C CB  . ARG A 296 ? 0.5220 0.3420 0.3247 -0.0696 0.0918  0.0632  296 ARG A CB  
1006 C CG  . ARG A 296 ? 0.5458 0.4016 0.3760 -0.0833 0.0871  0.0533  296 ARG A CG  
1007 C CD  . ARG A 296 ? 0.5944 0.4271 0.4171 -0.1046 0.0896  0.0486  296 ARG A CD  
1008 N NE  . ARG A 296 ? 0.6546 0.4503 0.4593 -0.0954 0.0886  0.0445  296 ARG A NE  
1009 C CZ  . ARG A 296 ? 0.6941 0.4530 0.4808 -0.1097 0.0917  0.0413  296 ARG A CZ  
1010 N NH1 . ARG A 296 ? 0.6933 0.4189 0.4623 -0.0978 0.0909  0.0371  296 ARG A NH1 
1011 N NH2 . ARG A 296 ? 0.6876 0.4434 0.4732 -0.1362 0.0956  0.0419  296 ARG A NH2 
1012 N N   . VAL A 297 ? 0.5302 0.3126 0.2969 -0.0109 0.0888  0.0740  297 VAL A N   
1013 C CA  . VAL A 297 ? 0.5670 0.3081 0.3025 0.0050  0.0930  0.0828  297 VAL A CA  
1014 C C   . VAL A 297 ? 0.5782 0.3359 0.3129 0.0330  0.0882  0.0871  297 VAL A C   
1015 O O   . VAL A 297 ? 0.5611 0.3578 0.3190 0.0412  0.0806  0.0807  297 VAL A O   
1016 C CB  . VAL A 297 ? 0.5955 0.2940 0.3126 0.0049  0.0954  0.0783  297 VAL A CB  
1017 C CG1 . VAL A 297 ? 0.6113 0.2930 0.3273 -0.0248 0.0996  0.0739  297 VAL A CG1 
1018 C CG2 . VAL A 297 ? 0.5871 0.3056 0.3194 0.0196  0.0884  0.0687  297 VAL A CG2 
1019 N N   . ALA A 298 ? 0.6058 0.3329 0.3124 0.0472  0.0924  0.0980  298 ALA A N   
1020 C CA  . ALA A 298 ? 0.6141 0.3543 0.3154 0.0747  0.0881  0.1035  298 ALA A CA  
1021 C C   . ALA A 298 ? 0.6157 0.3736 0.3287 0.0935  0.0812  0.0960  298 ALA A C   
1022 O O   . ALA A 298 ? 0.5974 0.3989 0.3311 0.1026  0.0737  0.0930  298 ALA A O   
1023 C CB  . ALA A 298 ? 0.6393 0.3339 0.3032 0.0870  0.0949  0.1168  298 ALA A CB  
1024 N N   . GLU A 299 ? 0.6324 0.3583 0.3324 0.0980  0.0838  0.0925  299 GLU A N   
1025 C CA  . GLU A 299 ? 0.6306 0.3754 0.3418 0.1153  0.0784  0.0855  299 GLU A CA  
1026 C C   . GLU A 299 ? 0.6060 0.3722 0.3428 0.0960  0.0756  0.0736  299 GLU A C   
1027 O O   . GLU A 299 ? 0.6227 0.3607 0.3511 0.0867  0.0792  0.0682  299 GLU A O   
1028 C CB  . GLU A 299 ? 0.7081 0.4065 0.3891 0.1338  0.0831  0.0881  299 GLU A CB  
1029 C CG  . GLU A 299 ? 0.8170 0.4963 0.4715 0.1592  0.0851  0.1006  299 GLU A CG  
1030 C CD  . GLU A 299 ? 0.9144 0.6453 0.5865 0.1784  0.0770  0.1032  299 GLU A CD  
1031 O OE1 . GLU A 299 ? 0.9107 0.6843 0.6097 0.1824  0.0704  0.0948  299 GLU A OE1 
1032 O OE2 . GLU A 299 ? 0.9616 0.6905 0.6200 0.1884  0.0773  0.1136  299 GLU A OE2 
1033 N N   . HIS A 300 ? 0.5660 0.3797 0.3319 0.0889  0.0695  0.0695  300 HIS A N   
1034 C CA  . HIS A 300 ? 0.5475 0.3852 0.3385 0.0704  0.0665  0.0593  300 HIS A CA  
1035 C C   . HIS A 300 ? 0.5438 0.3874 0.3426 0.0772  0.0640  0.0510  300 HIS A C   
1036 O O   . HIS A 300 ? 0.5339 0.3770 0.3415 0.0618  0.0642  0.0434  300 HIS A O   
1037 C CB  . HIS A 300 ? 0.5338 0.4181 0.3501 0.0662  0.0603  0.0577  300 HIS A CB  
1038 C CG  . HIS A 300 ? 0.5613 0.4745 0.3852 0.0865  0.0540  0.0586  300 HIS A CG  
1039 N ND1 . HIS A 300 ? 0.5726 0.5116 0.4140 0.0920  0.0490  0.0516  300 HIS A ND1 
1040 C CD2 . HIS A 300 ? 0.5790 0.4990 0.3939 0.1018  0.0522  0.0661  300 HIS A CD2 
1041 C CE1 . HIS A 300 ? 0.5745 0.5370 0.4185 0.1092  0.0442  0.0547  300 HIS A CE1 
1042 N NE2 . HIS A 300 ? 0.5804 0.5328 0.4087 0.1161  0.0455  0.0632  300 HIS A NE2 
1043 N N   . HIS A 301 ? 0.5425 0.3959 0.3390 0.1005  0.0616  0.0525  301 HIS A N   
1044 C CA  . HIS A 301 ? 0.5328 0.3986 0.3382 0.1089  0.0596  0.0454  301 HIS A CA  
1045 C C   . HIS A 301 ? 0.5604 0.3809 0.3424 0.1106  0.0657  0.0427  301 HIS A C   
1046 O O   . HIS A 301 ? 0.5761 0.3689 0.3346 0.1304  0.0692  0.0472  301 HIS A O   
1047 C CB  . HIS A 301 ? 0.5308 0.4262 0.3419 0.1332  0.0553  0.0485  301 HIS A CB  
1048 C CG  . HIS A 301 ? 0.5645 0.4842 0.3900 0.1409  0.0530  0.0416  301 HIS A CG  
1049 N ND1 . HIS A 301 ? 0.5811 0.5221 0.4075 0.1650  0.0510  0.0442  301 HIS A ND1 
1050 C CD2 . HIS A 301 ? 0.5713 0.4990 0.4103 0.1277  0.0527  0.0330  301 HIS A CD2 
1051 C CE1 . HIS A 301 ? 0.5785 0.5397 0.4192 0.1649  0.0502  0.0371  301 HIS A CE1 
1052 N NE2 . HIS A 301 ? 0.5774 0.5297 0.4249 0.1431  0.0512  0.0304  301 HIS A NE2 
1053 N N   . VAL A 302 ? 0.5649 0.3772 0.3521 0.0905  0.0667  0.0349  302 VAL A N   
1054 C CA  . VAL A 302 ? 0.5872 0.3539 0.3506 0.0877  0.0721  0.0307  302 VAL A CA  
1055 C C   . VAL A 302 ? 0.5856 0.3617 0.3547 0.0947  0.0710  0.0217  302 VAL A C   
1056 O O   . VAL A 302 ? 0.6133 0.3511 0.3605 0.0950  0.0752  0.0170  302 VAL A O   
1057 C CB  . VAL A 302 ? 0.5984 0.3443 0.3583 0.0589  0.0745  0.0285  302 VAL A CB  
1058 C CG1 . VAL A 302 ? 0.6098 0.3396 0.3582 0.0534  0.0777  0.0385  302 VAL A CG1 
1059 C CG2 . VAL A 302 ? 0.5771 0.3648 0.3682 0.0406  0.0692  0.0217  302 VAL A CG2 
1060 N N   . ALA A 303 ? 0.5496 0.3746 0.3462 0.0990  0.0656  0.0189  303 ALA A N   
1061 C CA  . ALA A 303 ? 0.5392 0.3774 0.3420 0.1061  0.0651  0.0114  303 ALA A CA  
1062 C C   . ALA A 303 ? 0.5039 0.3960 0.3342 0.1146  0.0599  0.0118  303 ALA A C   
1063 O O   . ALA A 303 ? 0.4907 0.4122 0.3405 0.1059  0.0553  0.0145  303 ALA A O   
1064 C CB  . ALA A 303 ? 0.5433 0.3746 0.3500 0.0839  0.0649  0.0025  303 ALA A CB  
1065 N N   . THR A 304 ? 0.4884 0.3928 0.3193 0.1310  0.0609  0.0089  304 THR A N   
1066 C CA  . THR A 304 ? 0.4562 0.4123 0.3127 0.1376  0.0568  0.0086  304 THR A CA  
1067 C C   . THR A 304 ? 0.4298 0.3921 0.2906 0.1340  0.0584  0.0007  304 THR A C   
1068 O O   . THR A 304 ? 0.4453 0.3807 0.2857 0.1459  0.0635  -0.0025 304 THR A O   
1069 C CB  . THR A 304 ? 0.4762 0.4461 0.3279 0.1652  0.0573  0.0144  304 THR A CB  
1070 O OG1 . THR A 304 ? 0.4963 0.4587 0.3417 0.1684  0.0556  0.0221  304 THR A OG1 
1071 C CG2 . THR A 304 ? 0.4537 0.4799 0.3323 0.1705  0.0533  0.0140  304 THR A CG2 
1072 N N   . LEU A 305 ? 0.3941 0.3879 0.2785 0.1177  0.0543  -0.0025 305 LEU A N   
1073 C CA  . LEU A 305 ? 0.3787 0.3829 0.2691 0.1120  0.0553  -0.0092 305 LEU A CA  
1074 C C   . LEU A 305 ? 0.3581 0.4105 0.2702 0.1199  0.0531  -0.0072 305 LEU A C   
1075 O O   . LEU A 305 ? 0.3401 0.4217 0.2723 0.1107  0.0480  -0.0044 305 LEU A O   
1076 C CB  . LEU A 305 ? 0.3699 0.3742 0.2704 0.0868  0.0521  -0.0130 305 LEU A CB  
1077 C CG  . LEU A 305 ? 0.4039 0.3668 0.2856 0.0744  0.0541  -0.0172 305 LEU A CG  
1078 C CD1 . LEU A 305 ? 0.4262 0.3580 0.2918 0.0760  0.0559  -0.0123 305 LEU A CD1 
1079 C CD2 . LEU A 305 ? 0.3956 0.3697 0.2915 0.0517  0.0501  -0.0202 305 LEU A CD2 
1080 N N   . SER A 306 ? 0.3610 0.4222 0.2682 0.1374  0.0572  -0.0085 306 SER A N   
1081 C CA  . SER A 306 ? 0.3533 0.4634 0.2808 0.1457  0.0560  -0.0060 306 SER A CA  
1082 C C   . SER A 306 ? 0.3530 0.4785 0.2859 0.1428  0.0589  -0.0108 306 SER A C   
1083 O O   . SER A 306 ? 0.3686 0.4868 0.2879 0.1593  0.0646  -0.0132 306 SER A O   
1084 C CB  . SER A 306 ? 0.3861 0.5034 0.3055 0.1729  0.0585  -0.0015 306 SER A CB  
1085 O OG  . SER A 306 ? 0.4520 0.5576 0.3666 0.1754  0.0553  0.0039  306 SER A OG  
1086 N N   . GLY A 307 ? 0.3275 0.4733 0.2785 0.1227  0.0553  -0.0118 307 GLY A N   
1087 C CA  . GLY A 307 ? 0.3099 0.4729 0.2670 0.1177  0.0578  -0.0151 307 GLY A CA  
1088 C C   . GLY A 307 ? 0.2679 0.4753 0.2508 0.1065  0.0544  -0.0118 307 GLY A C   
1089 O O   . GLY A 307 ? 0.2573 0.4791 0.2461 0.0990  0.0562  -0.0133 307 GLY A O   
1090 N N   . HIS A 308 ? 0.2411 0.4691 0.2378 0.1046  0.0496  -0.0071 308 HIS A N   
1091 C CA  . HIS A 308 ? 0.2225 0.4900 0.2419 0.0924  0.0459  -0.0043 308 HIS A CA  
1092 C C   . HIS A 308 ? 0.2247 0.5287 0.2553 0.1048  0.0448  -0.0001 308 HIS A C   
1093 O O   . HIS A 308 ? 0.2251 0.5210 0.2484 0.1185  0.0436  0.0019  308 HIS A O   
1094 C CB  . HIS A 308 ? 0.2123 0.4716 0.2388 0.0729  0.0395  -0.0040 308 HIS A CB  
1095 C CG  . HIS A 308 ? 0.2261 0.4583 0.2454 0.0594  0.0396  -0.0075 308 HIS A CG  
1096 N ND1 . HIS A 308 ? 0.2394 0.4832 0.2665 0.0464  0.0396  -0.0080 308 HIS A ND1 
1097 C CD2 . HIS A 308 ? 0.2468 0.4435 0.2525 0.0566  0.0393  -0.0101 308 HIS A CD2 
1098 C CE1 . HIS A 308 ? 0.2526 0.4692 0.2707 0.0381  0.0390  -0.0110 308 HIS A CE1 
1099 N NE2 . HIS A 308 ? 0.2620 0.4514 0.2681 0.0429  0.0387  -0.0127 308 HIS A NE2 
1100 N N   . SER A 309 ? 0.2187 0.5645 0.2671 0.0995  0.0450  0.0018  309 SER A N   
1101 C CA  . SER A 309 ? 0.2136 0.6027 0.2763 0.1086  0.0431  0.0058  309 SER A CA  
1102 C C   . SER A 309 ? 0.2041 0.6155 0.2841 0.0893  0.0351  0.0075  309 SER A C   
1103 O O   . SER A 309 ? 0.1984 0.6480 0.2915 0.0932  0.0319  0.0102  309 SER A O   
1104 C CB  . SER A 309 ? 0.2187 0.6457 0.2900 0.1170  0.0492  0.0069  309 SER A CB  
1105 O OG  . SER A 309 ? 0.2539 0.6898 0.3341 0.0967  0.0505  0.0064  309 SER A OG  
1106 N N   . GLN A 310 ? 0.2049 0.5948 0.2848 0.0688  0.0320  0.0056  310 GLN A N   
1107 C CA  . GLN A 310 ? 0.1969 0.5979 0.2883 0.0501  0.0248  0.0060  310 GLN A CA  
1108 C C   . GLN A 310 ? 0.2154 0.5746 0.2950 0.0435  0.0214  0.0038  310 GLN A C   
1109 O O   . GLN A 310 ? 0.2323 0.5590 0.2973 0.0512  0.0248  0.0023  310 GLN A O   
1110 C CB  . GLN A 310 ? 0.2013 0.6213 0.3046 0.0307  0.0255  0.0065  310 GLN A CB  
1111 C CG  . GLN A 310 ? 0.2405 0.7061 0.3570 0.0352  0.0298  0.0093  310 GLN A CG  
1112 C CD  . GLN A 310 ? 0.2911 0.7986 0.4217 0.0385  0.0249  0.0114  310 GLN A CD  
1113 O OE1 . GLN A 310 ? 0.3273 0.8345 0.4611 0.0293  0.0172  0.0106  310 GLN A OE1 
1114 N NE2 . GLN A 310 ? 0.2808 0.8273 0.4199 0.0524  0.0291  0.0139  310 GLN A NE2 
1115 N N   . GLU A 311 ? 0.2109 0.5714 0.2960 0.0292  0.0149  0.0033  311 GLU A N   
1116 C CA  . GLU A 311 ? 0.2216 0.5487 0.2969 0.0239  0.0118  0.0015  311 GLU A CA  
1117 C C   . GLU A 311 ? 0.2289 0.5220 0.2937 0.0202  0.0155  -0.0005 311 GLU A C   
1118 O O   . GLU A 311 ? 0.2329 0.5258 0.3003 0.0107  0.0175  -0.0012 311 GLU A O   
1119 C CB  . GLU A 311 ? 0.2453 0.5795 0.3276 0.0070  0.0051  0.0003  311 GLU A CB  
1120 C CG  . GLU A 311 ? 0.3080 0.6123 0.3803 0.0038  0.0020  -0.0014 311 GLU A CG  
1121 C CD  . GLU A 311 ? 0.3412 0.6533 0.4161 -0.0047 -0.0052 -0.0029 311 GLU A CD  
1122 O OE1 . GLU A 311 ? 0.3072 0.6025 0.3734 -0.0007 -0.0073 -0.0035 311 GLU A OE1 
1123 O OE2 . GLU A 311 ? 0.3656 0.7001 0.4502 -0.0161 -0.0086 -0.0036 311 GLU A OE2 
1124 N N   . VAL A 312 ? 0.2254 0.4906 0.2780 0.0266  0.0161  -0.0012 312 VAL A N   
1125 C CA  . VAL A 312 ? 0.2304 0.4659 0.2738 0.0213  0.0184  -0.0034 312 VAL A CA  
1126 C C   . VAL A 312 ? 0.2222 0.4507 0.2683 0.0077  0.0138  -0.0043 312 VAL A C   
1127 O O   . VAL A 312 ? 0.2229 0.4440 0.2658 0.0087  0.0110  -0.0039 312 VAL A O   
1128 C CB  . VAL A 312 ? 0.2588 0.4679 0.2875 0.0321  0.0213  -0.0035 312 VAL A CB  
1129 C CG1 . VAL A 312 ? 0.2811 0.4637 0.3017 0.0243  0.0232  -0.0062 312 VAL A CG1 
1130 C CG2 . VAL A 312 ? 0.2658 0.4791 0.2888 0.0486  0.0258  -0.0026 312 VAL A CG2 
1131 N N   . CYS A 313 ? 0.2163 0.4465 0.2669 -0.0037 0.0133  -0.0051 313 CYS A N   
1132 C CA  . CYS A 313 ? 0.2273 0.4493 0.2786 -0.0150 0.0093  -0.0061 313 CYS A CA  
1133 C C   . CYS A 313 ? 0.2383 0.4376 0.2826 -0.0185 0.0105  -0.0075 313 CYS A C   
1134 O O   . CYS A 313 ? 0.2384 0.4291 0.2814 -0.0244 0.0077  -0.0082 313 CYS A O   
1135 C CB  . CYS A 313 ? 0.2304 0.4681 0.2896 -0.0258 0.0074  -0.0054 313 CYS A CB  
1136 S SG  . CYS A 313 ? 0.2748 0.5246 0.3372 -0.0271 0.0126  -0.0037 313 CYS A SG  
1137 N N   . GLY A 314 ? 0.2339 0.4253 0.2732 -0.0145 0.0145  -0.0082 314 GLY A N   
1138 C CA  . GLY A 314 ? 0.2369 0.4115 0.2704 -0.0181 0.0151  -0.0099 314 GLY A CA  
1139 C C   . GLY A 314 ? 0.2350 0.3959 0.2600 -0.0117 0.0181  -0.0113 314 GLY A C   
1140 O O   . GLY A 314 ? 0.2274 0.3895 0.2489 -0.0042 0.0213  -0.0115 314 GLY A O   
1141 N N   . LEU A 315 ? 0.2354 0.3828 0.2561 -0.0143 0.0176  -0.0120 315 LEU A N   
1142 C CA  . LEU A 315 ? 0.2504 0.3812 0.2613 -0.0110 0.0206  -0.0130 315 LEU A CA  
1143 C C   . LEU A 315 ? 0.2564 0.3788 0.2657 -0.0193 0.0199  -0.0144 315 LEU A C   
1144 O O   . LEU A 315 ? 0.2547 0.3810 0.2683 -0.0224 0.0177  -0.0131 315 LEU A O   
1145 C CB  . LEU A 315 ? 0.2556 0.3832 0.2634 -0.0037 0.0211  -0.0103 315 LEU A CB  
1146 C CG  . LEU A 315 ? 0.2782 0.3849 0.2726 0.0020  0.0251  -0.0102 315 LEU A CG  
1147 C CD1 . LEU A 315 ? 0.2885 0.3908 0.2763 0.0091  0.0283  -0.0123 315 LEU A CD1 
1148 C CD2 . LEU A 315 ? 0.2822 0.3871 0.2727 0.0103  0.0251  -0.0062 315 LEU A CD2 
1149 N N   . ARG A 316 ? 0.2541 0.3673 0.2571 -0.0228 0.0215  -0.0175 316 ARG A N   
1150 C CA  . ARG A 316 ? 0.2494 0.3603 0.2525 -0.0316 0.0202  -0.0190 316 ARG A CA  
1151 C C   . ARG A 316 ? 0.2565 0.3519 0.2489 -0.0359 0.0224  -0.0227 316 ARG A C   
1152 O O   . ARG A 316 ? 0.2542 0.3463 0.2411 -0.0352 0.0231  -0.0260 316 ARG A O   
1153 C CB  . ARG A 316 ? 0.2532 0.3778 0.2633 -0.0352 0.0171  -0.0195 316 ARG A CB  
1154 C CG  . ARG A 316 ? 0.2918 0.4226 0.3064 -0.0406 0.0148  -0.0191 316 ARG A CG  
1155 C CD  . ARG A 316 ? 0.3303 0.4679 0.3511 -0.0378 0.0132  -0.0161 316 ARG A CD  
1156 N NE  . ARG A 316 ? 0.3504 0.4933 0.3740 -0.0350 0.0114  -0.0149 316 ARG A NE  
1157 C CZ  . ARG A 316 ? 0.3837 0.5281 0.4094 -0.0320 0.0109  -0.0133 316 ARG A CZ  
1158 N NH1 . ARG A 316 ? 0.3589 0.5007 0.3839 -0.0295 0.0115  -0.0125 316 ARG A NH1 
1159 N NH2 . ARG A 316 ? 0.3959 0.5451 0.4238 -0.0323 0.0095  -0.0123 316 ARG A NH2 
1160 N N   . TRP A 317 ? 0.2614 0.3469 0.2498 -0.0415 0.0237  -0.0223 317 TRP A N   
1161 C CA  . TRP A 317 ? 0.2858 0.3551 0.2634 -0.0494 0.0254  -0.0261 317 TRP A CA  
1162 C C   . TRP A 317 ? 0.2826 0.3662 0.2661 -0.0588 0.0219  -0.0292 317 TRP A C   
1163 O O   . TRP A 317 ? 0.2630 0.3659 0.2582 -0.0597 0.0191  -0.0270 317 TRP A O   
1164 C CB  . TRP A 317 ? 0.3016 0.3581 0.2740 -0.0549 0.0281  -0.0237 317 TRP A CB  
1165 C CG  . TRP A 317 ? 0.3285 0.3613 0.2874 -0.0470 0.0322  -0.0215 317 TRP A CG  
1166 C CD1 . TRP A 317 ? 0.3430 0.3758 0.3025 -0.0378 0.0334  -0.0162 317 TRP A CD1 
1167 C CD2 . TRP A 317 ? 0.3504 0.3547 0.2909 -0.0464 0.0355  -0.0247 317 TRP A CD2 
1168 N NE1 . TRP A 317 ? 0.3658 0.3728 0.3088 -0.0308 0.0373  -0.0149 317 TRP A NE1 
1169 C CE2 . TRP A 317 ? 0.3721 0.3594 0.3025 -0.0355 0.0390  -0.0202 317 TRP A CE2 
1170 C CE3 . TRP A 317 ? 0.3704 0.3601 0.2999 -0.0542 0.0357  -0.0312 317 TRP A CE3 
1171 C CZ2 . TRP A 317 ? 0.4012 0.3554 0.3103 -0.0306 0.0432  -0.0215 317 TRP A CZ2 
1172 C CZ3 . TRP A 317 ? 0.4029 0.3589 0.3109 -0.0504 0.0398  -0.0335 317 TRP A CZ3 
1173 C CH2 . TRP A 317 ? 0.4151 0.3524 0.3126 -0.0382 0.0437  -0.0285 317 TRP A CH2 
1174 N N   . ALA A 318 ? 0.2958 0.3699 0.2698 -0.0644 0.0218  -0.0347 318 ALA A N   
1175 C CA  . ALA A 318 ? 0.3057 0.3948 0.2838 -0.0735 0.0178  -0.0380 318 ALA A CA  
1176 C C   . ALA A 318 ? 0.3167 0.4120 0.2995 -0.0853 0.0173  -0.0372 318 ALA A C   
1177 O O   . ALA A 318 ? 0.3141 0.3926 0.2901 -0.0898 0.0209  -0.0362 318 ALA A O   
1178 C CB  . ALA A 318 ? 0.3099 0.3862 0.2744 -0.0773 0.0175  -0.0448 318 ALA A CB  
1179 N N   . PRO A 319 ? 0.3263 0.4469 0.3204 -0.0897 0.0134  -0.0369 319 PRO A N   
1180 C CA  . PRO A 319 ? 0.3336 0.4666 0.3341 -0.1008 0.0133  -0.0360 319 PRO A CA  
1181 C C   . PRO A 319 ? 0.3551 0.4721 0.3446 -0.1163 0.0148  -0.0405 319 PRO A C   
1182 O O   . PRO A 319 ? 0.3641 0.4812 0.3552 -0.1252 0.0175  -0.0381 319 PRO A O   
1183 C CB  . PRO A 319 ? 0.3283 0.4918 0.3401 -0.1005 0.0081  -0.0363 319 PRO A CB  
1184 C CG  . PRO A 319 ? 0.3306 0.4952 0.3440 -0.0865 0.0068  -0.0341 319 PRO A CG  
1185 C CD  . PRO A 319 ? 0.3192 0.4593 0.3202 -0.0838 0.0092  -0.0367 319 PRO A CD  
1186 N N   . ASP A 320 ? 0.3675 0.4683 0.3439 -0.1199 0.0137  -0.0469 320 ASP A N   
1187 C CA  . ASP A 320 ? 0.3825 0.4616 0.3445 -0.1357 0.0152  -0.0521 320 ASP A CA  
1188 C C   . ASP A 320 ? 0.4067 0.4457 0.3511 -0.1322 0.0214  -0.0512 320 ASP A C   
1189 O O   . ASP A 320 ? 0.4260 0.4389 0.3542 -0.1446 0.0234  -0.0553 320 ASP A O   
1190 C CB  . ASP A 320 ? 0.3924 0.4718 0.3459 -0.1425 0.0106  -0.0606 320 ASP A CB  
1191 C CG  . ASP A 320 ? 0.4651 0.5275 0.4066 -0.1291 0.0111  -0.0638 320 ASP A CG  
1192 O OD1 . ASP A 320 ? 0.4761 0.5270 0.4167 -0.1146 0.0151  -0.0593 320 ASP A OD1 
1193 O OD2 . ASP A 320 ? 0.5007 0.5634 0.4337 -0.1331 0.0076  -0.0707 320 ASP A OD2 
1194 N N   . GLY A 321 ? 0.3991 0.4328 0.3451 -0.1152 0.0240  -0.0461 321 GLY A N   
1195 C CA  . GLY A 321 ? 0.4208 0.4212 0.3512 -0.1075 0.0294  -0.0440 321 GLY A CA  
1196 C C   . GLY A 321 ? 0.4457 0.4170 0.3559 -0.1024 0.0309  -0.0501 321 GLY A C   
1197 O O   . GLY A 321 ? 0.4677 0.4087 0.3621 -0.0951 0.0356  -0.0487 321 GLY A O   
1198 N N   . ARG A 322 ? 0.4390 0.4185 0.3477 -0.1047 0.0272  -0.0569 322 ARG A N   
1199 C CA  . ARG A 322 ? 0.4543 0.4065 0.3419 -0.0995 0.0289  -0.0638 322 ARG A CA  
1200 C C   . ARG A 322 ? 0.4400 0.3939 0.3276 -0.0780 0.0312  -0.0615 322 ARG A C   
1201 O O   . ARG A 322 ? 0.4603 0.3897 0.3292 -0.0695 0.0343  -0.0660 322 ARG A O   
1202 C CB  . ARG A 322 ? 0.4793 0.4402 0.3633 -0.1110 0.0239  -0.0724 322 ARG A CB  
1203 C CG  . ARG A 322 ? 0.5278 0.4858 0.4088 -0.1343 0.0215  -0.0764 322 ARG A CG  
1204 C CD  . ARG A 322 ? 0.5756 0.5496 0.4553 -0.1457 0.0150  -0.0849 322 ARG A CD  
1205 N NE  . ARG A 322 ? 0.6430 0.6009 0.5051 -0.1364 0.0150  -0.0921 322 ARG A NE  
1206 C CZ  . ARG A 322 ? 0.6699 0.6513 0.5394 -0.1249 0.0124  -0.0919 322 ARG A CZ  
1207 N NH1 . ARG A 322 ? 0.6495 0.6679 0.5426 -0.1209 0.0094  -0.0849 322 ARG A NH1 
1208 N NH2 . ARG A 322 ? 0.6765 0.6428 0.5284 -0.1168 0.0134  -0.0984 322 ARG A NH2 
1209 N N   . HIS A 323 ? 0.4033 0.3868 0.3111 -0.0696 0.0297  -0.0552 323 HIS A N   
1210 C CA  . HIS A 323 ? 0.3942 0.3852 0.3050 -0.0518 0.0317  -0.0525 323 HIS A CA  
1211 C C   . HIS A 323 ? 0.3724 0.3828 0.3008 -0.0455 0.0314  -0.0441 323 HIS A C   
1212 O O   . HIS A 323 ? 0.3630 0.3886 0.3041 -0.0537 0.0287  -0.0412 323 HIS A O   
1213 C CB  . HIS A 323 ? 0.3904 0.4025 0.3065 -0.0502 0.0288  -0.0554 323 HIS A CB  
1214 C CG  . HIS A 323 ? 0.4192 0.4171 0.3183 -0.0559 0.0281  -0.0643 323 HIS A CG  
1215 N ND1 . HIS A 323 ? 0.4337 0.4382 0.3333 -0.0718 0.0232  -0.0688 323 HIS A ND1 
1216 C CD2 . HIS A 323 ? 0.4483 0.4281 0.3293 -0.0471 0.0314  -0.0697 323 HIS A CD2 
1217 C CE1 . HIS A 323 ? 0.4508 0.4392 0.3317 -0.0734 0.0233  -0.0771 323 HIS A CE1 
1218 N NE2 . HIS A 323 ? 0.4629 0.4344 0.3311 -0.0584 0.0285  -0.0781 323 HIS A NE2 
1219 N N   . LEU A 324 ? 0.3642 0.3761 0.2932 -0.0305 0.0340  -0.0408 324 LEU A N   
1220 C CA  . LEU A 324 ? 0.3412 0.3729 0.2858 -0.0243 0.0330  -0.0340 324 LEU A CA  
1221 C C   . LEU A 324 ? 0.3217 0.3736 0.2740 -0.0156 0.0327  -0.0334 324 LEU A C   
1222 O O   . LEU A 324 ? 0.3236 0.3685 0.2665 -0.0056 0.0360  -0.0353 324 LEU A O   
1223 C CB  . LEU A 324 ? 0.3491 0.3653 0.2862 -0.0144 0.0364  -0.0299 324 LEU A CB  
1224 C CG  . LEU A 324 ? 0.3565 0.3938 0.3072 -0.0056 0.0352  -0.0238 324 LEU A CG  
1225 C CD1 . LEU A 324 ? 0.3465 0.4005 0.3116 -0.0150 0.0314  -0.0211 324 LEU A CD1 
1226 C CD2 . LEU A 324 ? 0.3790 0.4010 0.3196 0.0060  0.0382  -0.0199 324 LEU A CD2 
1227 N N   . ALA A 325 ? 0.3043 0.3802 0.2725 -0.0188 0.0294  -0.0304 325 ALA A N   
1228 C CA  . ALA A 325 ? 0.2953 0.3904 0.2710 -0.0131 0.0294  -0.0288 325 ALA A CA  
1229 C C   . ALA A 325 ? 0.2742 0.3828 0.2603 -0.0071 0.0291  -0.0236 325 ALA A C   
1230 O O   . ALA A 325 ? 0.2659 0.3749 0.2573 -0.0102 0.0269  -0.0211 325 ALA A O   
1231 C CB  . ALA A 325 ? 0.2959 0.4052 0.2790 -0.0214 0.0260  -0.0288 325 ALA A CB  
1232 N N   . SER A 326 ? 0.2514 0.3731 0.2402 0.0014  0.0312  -0.0223 326 SER A N   
1233 C CA  . SER A 326 ? 0.2390 0.3786 0.2387 0.0057  0.0300  -0.0178 326 SER A CA  
1234 C C   . SER A 326 ? 0.2406 0.4033 0.2494 0.0051  0.0304  -0.0162 326 SER A C   
1235 O O   . SER A 326 ? 0.2487 0.4138 0.2527 0.0084  0.0337  -0.0179 326 SER A O   
1236 C CB  . SER A 326 ? 0.2459 0.3803 0.2396 0.0187  0.0326  -0.0166 326 SER A CB  
1237 O OG  . SER A 326 ? 0.2658 0.4008 0.2521 0.0293  0.0371  -0.0184 326 SER A OG  
1238 N N   . GLY A 327 ? 0.2322 0.4105 0.2527 -0.0003 0.0272  -0.0130 327 GLY A N   
1239 C CA  . GLY A 327 ? 0.2389 0.4391 0.2684 -0.0038 0.0275  -0.0106 327 GLY A CA  
1240 C C   . GLY A 327 ? 0.2453 0.4652 0.2843 -0.0004 0.0261  -0.0078 327 GLY A C   
1241 O O   . GLY A 327 ? 0.2496 0.4654 0.2898 0.0001  0.0229  -0.0074 327 GLY A O   
1242 N N   . GLY A 328 ? 0.2371 0.4805 0.2826 0.0019  0.0287  -0.0060 328 GLY A N   
1243 C CA  . GLY A 328 ? 0.2365 0.5047 0.2924 0.0048  0.0271  -0.0036 328 GLY A CA  
1244 C C   . GLY A 328 ? 0.2381 0.5330 0.3062 -0.0060 0.0264  -0.0008 328 GLY A C   
1245 O O   . GLY A 328 ? 0.2484 0.5443 0.3163 -0.0140 0.0287  0.0002  328 GLY A O   
1246 N N   . ASN A 329 ? 0.2266 0.5443 0.3046 -0.0066 0.0231  0.0007  329 ASN A N   
1247 C CA  . ASN A 329 ? 0.2159 0.5639 0.3067 -0.0178 0.0224  0.0033  329 ASN A CA  
1248 C C   . ASN A 329 ? 0.2084 0.5852 0.3047 -0.0096 0.0289  0.0054  329 ASN A C   
1249 O O   . ASN A 329 ? 0.2079 0.6154 0.3160 -0.0185 0.0296  0.0082  329 ASN A O   
1250 C CB  . ASN A 329 ? 0.2137 0.5786 0.3127 -0.0214 0.0160  0.0032  329 ASN A CB  
1251 C CG  . ASN A 329 ? 0.2313 0.6228 0.3422 -0.0384 0.0138  0.0050  329 ASN A CG  
1252 O OD1 . ASN A 329 ? 0.2536 0.6369 0.3633 -0.0528 0.0151  0.0062  329 ASN A OD1 
1253 N ND2 . ASN A 329 ? 0.2204 0.6443 0.3422 -0.0375 0.0102  0.0055  329 ASN A ND2 
1254 N N   . ASP A 330 ? 0.2109 0.5782 0.2980 0.0071  0.0339  0.0040  330 ASP A N   
1255 C CA  . ASP A 330 ? 0.2111 0.6012 0.2999 0.0172  0.0411  0.0053  330 ASP A CA  
1256 C C   . ASP A 330 ? 0.2250 0.6003 0.3054 0.0110  0.0458  0.0048  330 ASP A C   
1257 O O   . ASP A 330 ? 0.2272 0.6132 0.3038 0.0208  0.0525  0.0048  330 ASP A O   
1258 C CB  . ASP A 330 ? 0.2233 0.6084 0.3031 0.0407  0.0442  0.0035  330 ASP A CB  
1259 C CG  . ASP A 330 ? 0.2876 0.6273 0.3491 0.0466  0.0439  -0.0005 330 ASP A CG  
1260 O OD1 . ASP A 330 ? 0.2980 0.6137 0.3558 0.0331  0.0406  -0.0019 330 ASP A OD1 
1261 O OD2 . ASP A 330 ? 0.3187 0.6471 0.3689 0.0647  0.0471  -0.0021 330 ASP A OD2 
1262 N N   . ASN A 331 ? 0.2304 0.5818 0.3066 -0.0039 0.0423  0.0045  331 ASN A N   
1263 C CA  . ASN A 331 ? 0.2407 0.5775 0.3083 -0.0107 0.0452  0.0048  331 ASN A CA  
1264 C C   . ASN A 331 ? 0.2392 0.5518 0.2913 0.0014  0.0481  0.0003  331 ASN A C   
1265 O O   . ASN A 331 ? 0.2484 0.5568 0.2925 0.0002  0.0519  0.0001  331 ASN A O   
1266 C CB  . ASN A 331 ? 0.2599 0.6265 0.3345 -0.0167 0.0508  0.0094  331 ASN A CB  
1267 C CG  . ASN A 331 ? 0.3070 0.7001 0.3971 -0.0312 0.0484  0.0136  331 ASN A CG  
1268 O OD1 . ASN A 331 ? 0.3197 0.7060 0.4139 -0.0385 0.0418  0.0129  331 ASN A OD1 
1269 N ND2 . ASN A 331 ? 0.3286 0.7519 0.4262 -0.0372 0.0538  0.0181  331 ASN A ND2 
1270 N N   . LEU A 332 ? 0.2228 0.5184 0.2687 0.0123  0.0463  -0.0033 332 LEU A N   
1271 C CA  . LEU A 332 ? 0.2214 0.4912 0.2508 0.0217  0.0488  -0.0083 332 LEU A CA  
1272 C C   . LEU A 332 ? 0.2250 0.4643 0.2472 0.0149  0.0439  -0.0110 332 LEU A C   
1273 O O   . LEU A 332 ? 0.2233 0.4588 0.2515 0.0101  0.0392  -0.0098 332 LEU A O   
1274 C CB  . LEU A 332 ? 0.2171 0.4862 0.2407 0.0403  0.0519  -0.0103 332 LEU A CB  
1275 C CG  . LEU A 332 ? 0.2160 0.5160 0.2442 0.0527  0.0579  -0.0084 332 LEU A CG  
1276 C CD1 . LEU A 332 ? 0.2309 0.5234 0.2501 0.0733  0.0602  -0.0103 332 LEU A CD1 
1277 C CD2 . LEU A 332 ? 0.2145 0.5170 0.2347 0.0538  0.0637  -0.0099 332 LEU A CD2 
1278 N N   . VAL A 333 ? 0.2209 0.4396 0.2293 0.0155  0.0452  -0.0152 333 VAL A N   
1279 C CA  . VAL A 333 ? 0.2299 0.4218 0.2306 0.0108  0.0414  -0.0186 333 VAL A CA  
1280 C C   . VAL A 333 ? 0.2431 0.4146 0.2278 0.0218  0.0447  -0.0239 333 VAL A C   
1281 O O   . VAL A 333 ? 0.2444 0.4152 0.2191 0.0279  0.0490  -0.0269 333 VAL A O   
1282 C CB  . VAL A 333 ? 0.2292 0.4140 0.2268 -0.0003 0.0387  -0.0194 333 VAL A CB  
1283 C CG1 . VAL A 333 ? 0.2364 0.3979 0.2262 -0.0042 0.0353  -0.0235 333 VAL A CG1 
1284 C CG2 . VAL A 333 ? 0.2178 0.4158 0.2275 -0.0104 0.0356  -0.0140 333 VAL A CG2 
1285 N N   . ASN A 334 ? 0.2399 0.3931 0.2201 0.0246  0.0432  -0.0251 334 ASN A N   
1286 C CA  . ASN A 334 ? 0.2556 0.3820 0.2172 0.0330  0.0462  -0.0301 334 ASN A CA  
1287 C C   . ASN A 334 ? 0.2770 0.3793 0.2313 0.0212  0.0428  -0.0335 334 ASN A C   
1288 O O   . ASN A 334 ? 0.2662 0.3711 0.2304 0.0120  0.0386  -0.0308 334 ASN A O   
1289 C CB  . ASN A 334 ? 0.2602 0.3822 0.2192 0.0465  0.0482  -0.0279 334 ASN A CB  
1290 C CG  . ASN A 334 ? 0.2635 0.4099 0.2267 0.0612  0.0525  -0.0256 334 ASN A CG  
1291 O OD1 . ASN A 334 ? 0.2765 0.4226 0.2299 0.0697  0.0573  -0.0289 334 ASN A OD1 
1292 N ND2 . ASN A 334 ? 0.2339 0.4038 0.2116 0.0647  0.0508  -0.0203 334 ASN A ND2 
1293 N N   . VAL A 335 ? 0.2949 0.3752 0.2317 0.0209  0.0445  -0.0399 335 VAL A N   
1294 C CA  . VAL A 335 ? 0.3170 0.3755 0.2461 0.0088  0.0414  -0.0437 335 VAL A CA  
1295 C C   . VAL A 335 ? 0.3314 0.3580 0.2411 0.0162  0.0450  -0.0470 335 VAL A C   
1296 O O   . VAL A 335 ? 0.3324 0.3457 0.2259 0.0261  0.0491  -0.0516 335 VAL A O   
1297 C CB  . VAL A 335 ? 0.3328 0.3915 0.2567 -0.0013 0.0390  -0.0489 335 VAL A CB  
1298 C CG1 . VAL A 335 ? 0.3461 0.3861 0.2634 -0.0146 0.0356  -0.0529 335 VAL A CG1 
1299 C CG2 . VAL A 335 ? 0.3196 0.4073 0.2604 -0.0065 0.0359  -0.0442 335 VAL A CG2 
1300 N N   . TRP A 336 ? 0.3317 0.3453 0.2416 0.0128  0.0441  -0.0443 336 TRP A N   
1301 C CA  . TRP A 336 ? 0.3635 0.3441 0.2543 0.0196  0.0477  -0.0454 336 TRP A CA  
1302 C C   . TRP A 336 ? 0.4157 0.3675 0.2921 0.0044  0.0466  -0.0508 336 TRP A C   
1303 O O   . TRP A 336 ? 0.4049 0.3679 0.2925 -0.0115 0.0424  -0.0506 336 TRP A O   
1304 C CB  . TRP A 336 ? 0.3451 0.3303 0.2446 0.0245  0.0474  -0.0376 336 TRP A CB  
1305 C CG  . TRP A 336 ? 0.3254 0.3423 0.2408 0.0367  0.0473  -0.0324 336 TRP A CG  
1306 C CD1 . TRP A 336 ? 0.3142 0.3631 0.2515 0.0306  0.0434  -0.0287 336 TRP A CD1 
1307 C CD2 . TRP A 336 ? 0.3248 0.3450 0.2348 0.0566  0.0512  -0.0304 336 TRP A CD2 
1308 N NE1 . TRP A 336 ? 0.3058 0.3783 0.2523 0.0430  0.0443  -0.0248 336 TRP A NE1 
1309 C CE2 . TRP A 336 ? 0.3123 0.3707 0.2437 0.0597  0.0490  -0.0255 336 TRP A CE2 
1310 C CE3 . TRP A 336 ? 0.3506 0.3448 0.2389 0.0727  0.0564  -0.0323 336 TRP A CE3 
1311 C CZ2 . TRP A 336 ? 0.3139 0.3906 0.2482 0.0773  0.0514  -0.0223 336 TRP A CZ2 
1312 C CZ3 . TRP A 336 ? 0.3576 0.3688 0.2478 0.0931  0.0592  -0.0288 336 TRP A CZ3 
1313 C CH2 . TRP A 336 ? 0.3340 0.3889 0.2484 0.0948  0.0566  -0.0239 336 TRP A CH2 
1314 N N   . PRO A 337 ? 0.4730 0.3868 0.3241 0.0091  0.0506  -0.0550 337 PRO A N   
1315 C CA  . PRO A 337 ? 0.5147 0.3983 0.3510 -0.0081 0.0498  -0.0597 337 PRO A CA  
1316 C C   . PRO A 337 ? 0.5471 0.4257 0.3893 -0.0152 0.0496  -0.0526 337 PRO A C   
1317 O O   . PRO A 337 ? 0.5363 0.4291 0.3896 -0.0044 0.0503  -0.0450 337 PRO A O   
1318 C CB  . PRO A 337 ? 0.5469 0.3877 0.3518 0.0019  0.0550  -0.0655 337 PRO A CB  
1319 C CG  . PRO A 337 ? 0.5475 0.3928 0.3525 0.0263  0.0592  -0.0595 337 PRO A CG  
1320 C CD  . PRO A 337 ? 0.4912 0.3864 0.3249 0.0304  0.0563  -0.0552 337 PRO A CD  
1321 N N   . SER A 338 ? 0.5802 0.4419 0.4157 -0.0344 0.0484  -0.0552 338 SER A N   
1322 C CA  . SER A 338 ? 0.6061 0.4626 0.4454 -0.0429 0.0492  -0.0485 338 SER A CA  
1323 C C   . SER A 338 ? 0.6588 0.4717 0.4728 -0.0347 0.0550  -0.0455 338 SER A C   
1324 O O   . SER A 338 ? 0.6669 0.4752 0.4824 -0.0371 0.0566  -0.0382 338 SER A O   
1325 C CB  . SER A 338 ? 0.6218 0.4820 0.4655 -0.0678 0.0461  -0.0516 338 SER A CB  
1326 O OG  . SER A 338 ? 0.6751 0.4999 0.4945 -0.0785 0.0473  -0.0598 338 SER A OG  
1327 N N   . ALA A 339 ? 0.6962 0.4758 0.4852 -0.0243 0.0585  -0.0510 339 ALA A N   
1328 C CA  . ALA A 339 ? 0.7439 0.4766 0.5042 -0.0135 0.0645  -0.0486 339 ALA A CA  
1329 C C   . ALA A 339 ? 0.7733 0.4920 0.5170 0.0107  0.0678  -0.0524 339 ALA A C   
1330 O O   . ALA A 339 ? 0.7687 0.5024 0.5160 0.0123  0.0661  -0.0597 339 ALA A O   
1331 C CB  . ALA A 339 ? 0.7669 0.4565 0.5036 -0.0349 0.0661  -0.0535 339 ALA A CB  
1332 N N   . PRO A 340 ? 0.8010 0.4918 0.5256 0.0311  0.0729  -0.0473 340 PRO A N   
1333 C CA  . PRO A 340 ? 0.8196 0.4987 0.5277 0.0566  0.0768  -0.0508 340 PRO A CA  
1334 C C   . PRO A 340 ? 0.8655 0.4908 0.5372 0.0535  0.0803  -0.0611 340 PRO A C   
1335 O O   . PRO A 340 ? 0.8910 0.4797 0.5458 0.0326  0.0805  -0.0640 340 PRO A O   
1336 C CB  . PRO A 340 ? 0.8290 0.5029 0.5319 0.0802  0.0802  -0.0405 340 PRO A CB  
1337 C CG  . PRO A 340 ? 0.8411 0.4939 0.5394 0.0650  0.0804  -0.0338 340 PRO A CG  
1338 C CD  . PRO A 340 ? 0.8091 0.4777 0.5244 0.0334  0.0758  -0.0377 340 PRO A CD  
1339 N N   . GLY A 344 ? 0.8005 0.4650 0.4574 0.1535  0.0931  -0.0628 344 GLY A N   
1340 C CA  . GLY A 344 ? 0.7876 0.4780 0.4675 0.1518  0.0901  -0.0511 344 GLY A CA  
1341 C C   . GLY A 344 ? 0.7515 0.4975 0.4713 0.1323  0.0834  -0.0488 344 GLY A C   
1342 O O   . GLY A 344 ? 0.7515 0.5038 0.4782 0.1113  0.0802  -0.0555 344 GLY A O   
1343 N N   . TRP A 345 ? 0.7188 0.5052 0.4637 0.1399  0.0810  -0.0395 345 TRP A N   
1344 C CA  . TRP A 345 ? 0.6839 0.5203 0.4647 0.1230  0.0748  -0.0368 345 TRP A CA  
1345 C C   . TRP A 345 ? 0.6575 0.5395 0.4582 0.1291  0.0743  -0.0390 345 TRP A C   
1346 O O   . TRP A 345 ? 0.6415 0.5641 0.4628 0.1396  0.0731  -0.0330 345 TRP A O   
1347 C CB  . TRP A 345 ? 0.6658 0.5221 0.4628 0.1246  0.0719  -0.0267 345 TRP A CB  
1348 C CG  . TRP A 345 ? 0.6792 0.5056 0.4677 0.1081  0.0709  -0.0240 345 TRP A CG  
1349 C CD1 . TRP A 345 ? 0.7088 0.5050 0.4793 0.1167  0.0735  -0.0175 345 TRP A CD1 
1350 C CD2 . TRP A 345 ? 0.6714 0.4982 0.4695 0.0803  0.0673  -0.0267 345 TRP A CD2 
1351 N NE1 . TRP A 345 ? 0.7171 0.4949 0.4856 0.0946  0.0723  -0.0160 345 TRP A NE1 
1352 C CE2 . TRP A 345 ? 0.6957 0.4939 0.4821 0.0724  0.0684  -0.0217 345 TRP A CE2 
1353 C CE3 . TRP A 345 ? 0.6610 0.5104 0.4758 0.0624  0.0635  -0.0325 345 TRP A CE3 
1354 C CZ2 . TRP A 345 ? 0.6972 0.4927 0.4902 0.0469  0.0660  -0.0226 345 TRP A CZ2 
1355 C CZ3 . TRP A 345 ? 0.6690 0.5149 0.4896 0.0387  0.0606  -0.0333 345 TRP A CZ3 
1356 C CH2 . TRP A 345 ? 0.6814 0.5018 0.4917 0.0309  0.0620  -0.0287 345 TRP A CH2 
1357 N N   . VAL A 346 ? 0.6484 0.5244 0.4425 0.1212  0.0750  -0.0475 346 VAL A N   
1358 C CA  . VAL A 346 ? 0.6187 0.5344 0.4285 0.1251  0.0753  -0.0494 346 VAL A CA  
1359 C C   . VAL A 346 ? 0.5853 0.5174 0.4109 0.0998  0.0700  -0.0525 346 VAL A C   
1360 O O   . VAL A 346 ? 0.6019 0.5058 0.4162 0.0831  0.0679  -0.0575 346 VAL A O   
1361 C CB  . VAL A 346 ? 0.6488 0.5428 0.4325 0.1435  0.0818  -0.0566 346 VAL A CB  
1362 C CG1 . VAL A 346 ? 0.6407 0.5661 0.4341 0.1416  0.0826  -0.0610 346 VAL A CG1 
1363 C CG2 . VAL A 346 ? 0.6600 0.5529 0.4343 0.1732  0.0870  -0.0519 346 VAL A CG2 
1364 N N   . PRO A 347 ? 0.5330 0.5107 0.3845 0.0962  0.0677  -0.0491 347 PRO A N   
1365 C CA  . PRO A 347 ? 0.5014 0.4932 0.3657 0.0749  0.0629  -0.0512 347 PRO A CA  
1366 C C   . PRO A 347 ? 0.4891 0.4621 0.3350 0.0697  0.0640  -0.0605 347 PRO A C   
1367 O O   . PRO A 347 ? 0.4885 0.4552 0.3192 0.0843  0.0691  -0.0648 347 PRO A O   
1368 C CB  . PRO A 347 ? 0.4880 0.5273 0.3773 0.0768  0.0621  -0.0457 347 PRO A CB  
1369 C CG  . PRO A 347 ? 0.4934 0.5474 0.3892 0.0936  0.0643  -0.0397 347 PRO A CG  
1370 C CD  . PRO A 347 ? 0.5012 0.5196 0.3706 0.1109  0.0693  -0.0429 347 PRO A CD  
1371 N N   . LEU A 348 ? 0.4747 0.4412 0.3221 0.0494  0.0590  -0.0637 348 LEU A N   
1372 C CA  . LEU A 348 ? 0.4751 0.4316 0.3092 0.0405  0.0578  -0.0723 348 LEU A CA  
1373 C C   . LEU A 348 ? 0.4499 0.4441 0.2982 0.0417  0.0577  -0.0705 348 LEU A C   
1374 O O   . LEU A 348 ? 0.4559 0.4469 0.2906 0.0431  0.0591  -0.0769 348 LEU A O   
1375 C CB  . LEU A 348 ? 0.4737 0.4213 0.3105 0.0180  0.0516  -0.0745 348 LEU A CB  
1376 C CG  . LEU A 348 ? 0.5081 0.4173 0.3288 0.0120  0.0520  -0.0768 348 LEU A CG  
1377 C CD1 . LEU A 348 ? 0.5024 0.4142 0.3317 -0.0108 0.0460  -0.0774 348 LEU A CD1 
1378 C CD2 . LEU A 348 ? 0.5515 0.4196 0.3390 0.0179  0.0560  -0.0865 348 LEU A CD2 
1379 N N   . GLN A 349 ? 0.4162 0.4440 0.2903 0.0393  0.0556  -0.0619 349 GLN A N   
1380 C CA  . GLN A 349 ? 0.3916 0.4536 0.2794 0.0393  0.0560  -0.0584 349 GLN A CA  
1381 C C   . GLN A 349 ? 0.3707 0.4610 0.2792 0.0458  0.0572  -0.0496 349 GLN A C   
1382 O O   . GLN A 349 ? 0.3639 0.4529 0.2821 0.0433  0.0545  -0.0455 349 GLN A O   
1383 C CB  . GLN A 349 ? 0.3849 0.4582 0.2824 0.0219  0.0498  -0.0575 349 GLN A CB  
1384 C CG  . GLN A 349 ? 0.4252 0.4780 0.3059 0.0121  0.0467  -0.0659 349 GLN A CG  
1385 C CD  . GLN A 349 ? 0.4417 0.4925 0.3048 0.0183  0.0499  -0.0721 349 GLN A CD  
1386 O OE1 . GLN A 349 ? 0.4313 0.4984 0.2953 0.0305  0.0554  -0.0696 349 GLN A OE1 
1387 N NE2 . GLN A 349 ? 0.4486 0.4811 0.2952 0.0095  0.0466  -0.0805 349 GLN A NE2 
1388 N N   . THR A 350 ? 0.3523 0.4699 0.2674 0.0529  0.0611  -0.0467 350 THR A N   
1389 C CA  . THR A 350 ? 0.3191 0.4692 0.2554 0.0553  0.0617  -0.0386 350 THR A CA  
1390 C C   . THR A 350 ? 0.3030 0.4788 0.2483 0.0476  0.0623  -0.0353 350 THR A C   
1391 O O   . THR A 350 ? 0.3039 0.4899 0.2418 0.0550  0.0678  -0.0367 350 THR A O   
1392 C CB  . THR A 350 ? 0.3244 0.4841 0.2594 0.0745  0.0673  -0.0372 350 THR A CB  
1393 O OG1 . THR A 350 ? 0.3423 0.4738 0.2669 0.0810  0.0663  -0.0391 350 THR A OG1 
1394 C CG2 . THR A 350 ? 0.3124 0.5108 0.2709 0.0743  0.0670  -0.0292 350 THR A CG2 
1395 N N   . PHE A 351 ? 0.2856 0.4696 0.2446 0.0330  0.0571  -0.0308 351 PHE A N   
1396 C CA  . PHE A 351 ? 0.2671 0.4709 0.2331 0.0243  0.0573  -0.0264 351 PHE A CA  
1397 C C   . PHE A 351 ? 0.2445 0.4786 0.2283 0.0240  0.0593  -0.0191 351 PHE A C   
1398 O O   . PHE A 351 ? 0.2314 0.4695 0.2278 0.0194  0.0553  -0.0159 351 PHE A O   
1399 C CB  . PHE A 351 ? 0.2607 0.4540 0.2292 0.0100  0.0505  -0.0255 351 PHE A CB  
1400 C CG  . PHE A 351 ? 0.2762 0.4445 0.2296 0.0078  0.0476  -0.0327 351 PHE A CG  
1401 C CD1 . PHE A 351 ? 0.2889 0.4488 0.2247 0.0132  0.0507  -0.0387 351 PHE A CD1 
1402 C CD2 . PHE A 351 ? 0.2898 0.4445 0.2461 -0.0004 0.0416  -0.0337 351 PHE A CD2 
1403 C CE1 . PHE A 351 ? 0.3123 0.4502 0.2339 0.0086  0.0471  -0.0460 351 PHE A CE1 
1404 C CE2 . PHE A 351 ? 0.3049 0.4407 0.2488 -0.0048 0.0387  -0.0401 351 PHE A CE2 
1405 C CZ  . PHE A 351 ? 0.3119 0.4393 0.2387 -0.0012 0.0410  -0.0465 351 PHE A CZ  
1406 N N   . THR A 352 ? 0.2297 0.4867 0.2143 0.0280  0.0654  -0.0166 352 THR A N   
1407 C CA  . THR A 352 ? 0.2295 0.5204 0.2313 0.0261  0.0681  -0.0096 352 THR A CA  
1408 C C   . THR A 352 ? 0.2251 0.5295 0.2339 0.0101  0.0679  -0.0030 352 THR A C   
1409 O O   . THR A 352 ? 0.2155 0.5478 0.2378 0.0049  0.0704  0.0029  352 THR A O   
1410 C CB  . THR A 352 ? 0.2477 0.5594 0.2460 0.0417  0.0765  -0.0104 352 THR A CB  
1411 O OG1 . THR A 352 ? 0.2754 0.5834 0.2595 0.0423  0.0809  -0.0123 352 THR A OG1 
1412 C CG2 . THR A 352 ? 0.2645 0.5610 0.2532 0.0598  0.0777  -0.0162 352 THR A CG2 
1413 N N   . GLN A 353 ? 0.2287 0.5139 0.2271 0.0027  0.0653  -0.0037 353 GLN A N   
1414 C CA  . GLN A 353 ? 0.2243 0.5160 0.2231 -0.0097 0.0659  0.0028  353 GLN A CA  
1415 C C   . GLN A 353 ? 0.2191 0.5139 0.2311 -0.0238 0.0615  0.0088  353 GLN A C   
1416 O O   . GLN A 353 ? 0.2107 0.5167 0.2251 -0.0339 0.0641  0.0156  353 GLN A O   
1417 C CB  . GLN A 353 ? 0.2385 0.5083 0.2209 -0.0113 0.0633  0.0001  353 GLN A CB  
1418 C CG  . GLN A 353 ? 0.2663 0.5329 0.2326 0.0004  0.0679  -0.0062 353 GLN A CG  
1419 C CD  . GLN A 353 ? 0.3257 0.5698 0.2832 0.0087  0.0648  -0.0157 353 GLN A CD  
1420 O OE1 . GLN A 353 ? 0.3263 0.5632 0.2915 0.0100  0.0617  -0.0173 353 GLN A OE1 
1421 N NE2 . GLN A 353 ? 0.3651 0.5960 0.3043 0.0138  0.0656  -0.0223 353 GLN A NE2 
1422 N N   . HIS A 354 ? 0.2239 0.5076 0.2426 -0.0249 0.0555  0.0064  354 HIS A N   
1423 C CA  . HIS A 354 ? 0.2265 0.5122 0.2558 -0.0374 0.0514  0.0110  354 HIS A CA  
1424 C C   . HIS A 354 ? 0.2217 0.5393 0.2651 -0.0401 0.0551  0.0147  354 HIS A C   
1425 O O   . HIS A 354 ? 0.2146 0.5485 0.2631 -0.0289 0.0576  0.0122  354 HIS A O   
1426 C CB  . HIS A 354 ? 0.2276 0.4955 0.2596 -0.0368 0.0445  0.0072  354 HIS A CB  
1427 C CG  . HIS A 354 ? 0.2583 0.5002 0.2800 -0.0380 0.0401  0.0050  354 HIS A CG  
1428 N ND1 . HIS A 354 ? 0.2896 0.5211 0.3080 -0.0474 0.0375  0.0092  354 HIS A ND1 
1429 C CD2 . HIS A 354 ? 0.2683 0.4943 0.2831 -0.0312 0.0379  -0.0007 354 HIS A CD2 
1430 C CE1 . HIS A 354 ? 0.2957 0.5093 0.3066 -0.0444 0.0336  0.0059  354 HIS A CE1 
1431 N NE2 . HIS A 354 ? 0.2878 0.4986 0.2969 -0.0362 0.0337  -0.0001 354 HIS A NE2 
1432 N N   . GLN A 355 ? 0.2260 0.5527 0.2745 -0.0547 0.0556  0.0209  355 GLN A N   
1433 C CA  . GLN A 355 ? 0.2264 0.5866 0.2892 -0.0614 0.0588  0.0250  355 GLN A CA  
1434 C C   . GLN A 355 ? 0.2261 0.5838 0.2982 -0.0725 0.0519  0.0250  355 GLN A C   
1435 O O   . GLN A 355 ? 0.2317 0.5969 0.3085 -0.0890 0.0517  0.0297  355 GLN A O   
1436 C CB  . GLN A 355 ? 0.2510 0.6231 0.3112 -0.0730 0.0650  0.0323  355 GLN A CB  
1437 C CG  . GLN A 355 ? 0.3273 0.6970 0.3742 -0.0629 0.0713  0.0323  355 GLN A CG  
1438 C CD  . GLN A 355 ? 0.4075 0.8032 0.4580 -0.0466 0.0773  0.0290  355 GLN A CD  
1439 O OE1 . GLN A 355 ? 0.4082 0.8397 0.4691 -0.0481 0.0836  0.0330  355 GLN A OE1 
1440 N NE2 . GLN A 355 ? 0.4302 0.8082 0.4710 -0.0307 0.0760  0.0217  355 GLN A NE2 
1441 N N   . GLY A 356 ? 0.2241 0.5667 0.2960 -0.0645 0.0462  0.0196  356 GLY A N   
1442 C CA  . GLY A 356 ? 0.2161 0.5539 0.2942 -0.0724 0.0393  0.0184  356 GLY A CA  
1443 C C   . GLY A 356 ? 0.2204 0.5391 0.2947 -0.0605 0.0346  0.0128  356 GLY A C   
1444 O O   . GLY A 356 ? 0.2327 0.5367 0.2983 -0.0492 0.0363  0.0100  356 GLY A O   
1445 N N   . ALA A 357 ? 0.2039 0.5219 0.2836 -0.0638 0.0288  0.0109  357 ALA A N   
1446 C CA  . ALA A 357 ? 0.2092 0.5104 0.2851 -0.0532 0.0249  0.0065  357 ALA A CA  
1447 C C   . ALA A 357 ? 0.2197 0.4892 0.2833 -0.0506 0.0242  0.0046  357 ALA A C   
1448 O O   . ALA A 357 ? 0.2301 0.4863 0.2882 -0.0593 0.0238  0.0066  357 ALA A O   
1449 C CB  . ALA A 357 ? 0.2066 0.5092 0.2875 -0.0598 0.0185  0.0053  357 ALA A CB  
1450 N N   . VAL A 358 ? 0.2076 0.4665 0.2663 -0.0386 0.0246  0.0012  358 VAL A N   
1451 C CA  . VAL A 358 ? 0.2149 0.4486 0.2635 -0.0372 0.0236  -0.0009 358 VAL A CA  
1452 C C   . VAL A 358 ? 0.2269 0.4464 0.2744 -0.0354 0.0192  -0.0033 358 VAL A C   
1453 O O   . VAL A 358 ? 0.2370 0.4524 0.2823 -0.0267 0.0198  -0.0055 358 VAL A O   
1454 C CB  . VAL A 358 ? 0.2170 0.4456 0.2577 -0.0283 0.0278  -0.0032 358 VAL A CB  
1455 C CG1 . VAL A 358 ? 0.2293 0.4362 0.2611 -0.0299 0.0257  -0.0054 358 VAL A CG1 
1456 C CG2 . VAL A 358 ? 0.2065 0.4511 0.2472 -0.0289 0.0330  -0.0007 358 VAL A CG2 
1457 N N   . LYS A 359 ? 0.2222 0.4327 0.2693 -0.0432 0.0154  -0.0027 359 LYS A N   
1458 C CA  . LYS A 359 ? 0.2324 0.4306 0.2776 -0.0415 0.0117  -0.0048 359 LYS A CA  
1459 C C   . LYS A 359 ? 0.2534 0.4345 0.2915 -0.0403 0.0114  -0.0060 359 LYS A C   
1460 O O   . LYS A 359 ? 0.2599 0.4333 0.2960 -0.0362 0.0107  -0.0080 359 LYS A O   
1461 C CB  . LYS A 359 ? 0.2391 0.4369 0.2862 -0.0494 0.0076  -0.0043 359 LYS A CB  
1462 C CG  . LYS A 359 ? 0.2452 0.4321 0.2894 -0.0465 0.0043  -0.0067 359 LYS A CG  
1463 C CD  . LYS A 359 ? 0.2612 0.4424 0.3033 -0.0540 0.0003  -0.0074 359 LYS A CD  
1464 C CE  . LYS A 359 ? 0.2862 0.4579 0.3241 -0.0494 -0.0023 -0.0100 359 LYS A CE  
1465 N NZ  . LYS A 359 ? 0.2973 0.4637 0.3315 -0.0557 -0.0065 -0.0120 359 LYS A NZ  
1466 N N   . ALA A 360 ? 0.2580 0.4349 0.2923 -0.0440 0.0120  -0.0044 360 ALA A N   
1467 C CA  . ALA A 360 ? 0.2662 0.4319 0.2946 -0.0427 0.0110  -0.0052 360 ALA A CA  
1468 C C   . ALA A 360 ? 0.2669 0.4329 0.2925 -0.0384 0.0133  -0.0078 360 ALA A C   
1469 O O   . ALA A 360 ? 0.2768 0.4485 0.3005 -0.0375 0.0162  -0.0075 360 ALA A O   
1470 C CB  . ALA A 360 ? 0.2733 0.4343 0.2968 -0.0468 0.0105  -0.0019 360 ALA A CB  
1471 N N   . VAL A 361 ? 0.2521 0.4117 0.2764 -0.0363 0.0122  -0.0104 361 VAL A N   
1472 C CA  . VAL A 361 ? 0.2501 0.4060 0.2697 -0.0344 0.0140  -0.0137 361 VAL A CA  
1473 C C   . VAL A 361 ? 0.2264 0.3778 0.2450 -0.0365 0.0116  -0.0152 361 VAL A C   
1474 O O   . VAL A 361 ? 0.2061 0.3554 0.2276 -0.0363 0.0108  -0.0149 361 VAL A O   
1475 C CB  . VAL A 361 ? 0.2774 0.4307 0.2966 -0.0298 0.0165  -0.0151 361 VAL A CB  
1476 C CG1 . VAL A 361 ? 0.2957 0.4388 0.3066 -0.0287 0.0185  -0.0190 361 VAL A CG1 
1477 C CG2 . VAL A 361 ? 0.2920 0.4557 0.3144 -0.0262 0.0188  -0.0133 361 VAL A CG2 
1478 N N   . ALA A 362 ? 0.2104 0.3630 0.2251 -0.0385 0.0105  -0.0166 362 ALA A N   
1479 C CA  . ALA A 362 ? 0.2077 0.3620 0.2232 -0.0411 0.0081  -0.0181 362 ALA A CA  
1480 C C   . ALA A 362 ? 0.2169 0.3726 0.2267 -0.0444 0.0074  -0.0217 362 ALA A C   
1481 O O   . ALA A 362 ? 0.2187 0.3767 0.2237 -0.0435 0.0073  -0.0217 362 ALA A O   
1482 C CB  . ALA A 362 ? 0.1930 0.3524 0.2112 -0.0393 0.0052  -0.0148 362 ALA A CB  
1483 N N   . TRP A 363 ? 0.2179 0.3724 0.2272 -0.0491 0.0071  -0.0249 363 TRP A N   
1484 C CA  . TRP A 363 ? 0.2299 0.3853 0.2330 -0.0547 0.0057  -0.0296 363 TRP A CA  
1485 C C   . TRP A 363 ? 0.2313 0.4030 0.2383 -0.0566 0.0012  -0.0290 363 TRP A C   
1486 O O   . TRP A 363 ? 0.2334 0.4140 0.2482 -0.0553 0.0000  -0.0262 363 TRP A O   
1487 C CB  . TRP A 363 ? 0.2351 0.3797 0.2346 -0.0614 0.0075  -0.0334 363 TRP A CB  
1488 C CG  . TRP A 363 ? 0.2591 0.3854 0.2514 -0.0575 0.0119  -0.0343 363 TRP A CG  
1489 C CD1 . TRP A 363 ? 0.2752 0.3954 0.2705 -0.0526 0.0146  -0.0309 363 TRP A CD1 
1490 C CD2 . TRP A 363 ? 0.2740 0.3872 0.2540 -0.0562 0.0141  -0.0387 363 TRP A CD2 
1491 N NE1 . TRP A 363 ? 0.2910 0.3966 0.2775 -0.0474 0.0182  -0.0324 363 TRP A NE1 
1492 C CE2 . TRP A 363 ? 0.2892 0.3892 0.2658 -0.0491 0.0184  -0.0374 363 TRP A CE2 
1493 C CE3 . TRP A 363 ? 0.2791 0.3910 0.2495 -0.0592 0.0128  -0.0439 363 TRP A CE3 
1494 C CZ2 . TRP A 363 ? 0.3014 0.3861 0.2650 -0.0440 0.0218  -0.0410 363 TRP A CZ2 
1495 C CZ3 . TRP A 363 ? 0.3002 0.3955 0.2571 -0.0551 0.0163  -0.0482 363 TRP A CZ3 
1496 C CH2 . TRP A 363 ? 0.3102 0.3925 0.2641 -0.0467 0.0210  -0.0464 363 TRP A CH2 
1497 N N   . CYS A 364 ? 0.2310 0.4081 0.2318 -0.0590 -0.0013 -0.0320 364 CYS A N   
1498 C CA  . CYS A 364 ? 0.2360 0.4319 0.2397 -0.0604 -0.0063 -0.0318 364 CYS A CA  
1499 C C   . CYS A 364 ? 0.2385 0.4426 0.2475 -0.0698 -0.0075 -0.0352 364 CYS A C   
1500 O O   . CYS A 364 ? 0.2416 0.4360 0.2445 -0.0788 -0.0065 -0.0406 364 CYS A O   
1501 C CB  . CYS A 364 ? 0.2513 0.4517 0.2455 -0.0609 -0.0091 -0.0346 364 CYS A CB  
1502 S SG  . CYS A 364 ? 0.2940 0.5219 0.2913 -0.0611 -0.0163 -0.0341 364 CYS A SG  
1503 N N   . PRO A 365 ? 0.2395 0.4604 0.2586 -0.0678 -0.0091 -0.0318 365 PRO A N   
1504 C CA  . PRO A 365 ? 0.2440 0.4771 0.2696 -0.0777 -0.0095 -0.0341 365 PRO A CA  
1505 C C   . PRO A 365 ? 0.2618 0.5106 0.2855 -0.0883 -0.0141 -0.0395 365 PRO A C   
1506 O O   . PRO A 365 ? 0.2658 0.5164 0.2906 -0.1014 -0.0136 -0.0432 365 PRO A O   
1507 C CB  . PRO A 365 ? 0.2360 0.4880 0.2723 -0.0696 -0.0102 -0.0289 365 PRO A CB  
1508 C CG  . PRO A 365 ? 0.2440 0.4827 0.2774 -0.0572 -0.0088 -0.0245 365 PRO A CG  
1509 C CD  . PRO A 365 ? 0.2299 0.4583 0.2538 -0.0563 -0.0100 -0.0258 365 PRO A CD  
1510 N N   . TRP A 366 ? 0.2718 0.5308 0.2911 -0.0837 -0.0187 -0.0401 366 TRP A N   
1511 C CA  . TRP A 366 ? 0.2803 0.5573 0.2972 -0.0936 -0.0243 -0.0457 366 TRP A CA  
1512 C C   . TRP A 366 ? 0.3003 0.5584 0.3011 -0.0991 -0.0248 -0.0524 366 TRP A C   
1513 O O   . TRP A 366 ? 0.3029 0.5744 0.2987 -0.1066 -0.0303 -0.0578 366 TRP A O   
1514 C CB  . TRP A 366 ? 0.2699 0.5778 0.2925 -0.0844 -0.0302 -0.0419 366 TRP A CB  
1515 C CG  . TRP A 366 ? 0.2885 0.5879 0.3031 -0.0700 -0.0306 -0.0372 366 TRP A CG  
1516 C CD1 . TRP A 366 ? 0.3050 0.6026 0.3076 -0.0685 -0.0336 -0.0392 366 TRP A CD1 
1517 C CD2 . TRP A 366 ? 0.2988 0.5895 0.3152 -0.0560 -0.0277 -0.0296 366 TRP A CD2 
1518 N NE1 . TRP A 366 ? 0.3154 0.6039 0.3127 -0.0548 -0.0321 -0.0323 366 TRP A NE1 
1519 C CE2 . TRP A 366 ? 0.3144 0.5973 0.3199 -0.0477 -0.0286 -0.0266 366 TRP A CE2 
1520 C CE3 . TRP A 366 ? 0.3117 0.5996 0.3366 -0.0503 -0.0243 -0.0253 366 TRP A CE3 
1521 C CZ2 . TRP A 366 ? 0.3281 0.5985 0.3308 -0.0357 -0.0262 -0.0193 366 TRP A CZ2 
1522 C CZ3 . TRP A 366 ? 0.3301 0.6043 0.3514 -0.0379 -0.0222 -0.0192 366 TRP A CZ3 
1523 C CH2 . TRP A 366 ? 0.3340 0.5993 0.3445 -0.0315 -0.0233 -0.0162 366 TRP A CH2 
1524 N N   . GLN A 367 ? 0.3089 0.5380 0.3012 -0.0947 -0.0194 -0.0523 367 GLN A N   
1525 C CA  . GLN A 367 ? 0.3324 0.5417 0.3082 -0.0974 -0.0184 -0.0586 367 GLN A CA  
1526 C C   . GLN A 367 ? 0.3530 0.5329 0.3239 -0.0968 -0.0115 -0.0592 367 GLN A C   
1527 O O   . GLN A 367 ? 0.3489 0.5206 0.3222 -0.0860 -0.0075 -0.0538 367 GLN A O   
1528 C CB  . GLN A 367 ? 0.3494 0.5604 0.3186 -0.0858 -0.0190 -0.0558 367 GLN A CB  
1529 C CG  . GLN A 367 ? 0.3982 0.6338 0.3660 -0.0853 -0.0260 -0.0561 367 GLN A CG  
1530 C CD  . GLN A 367 ? 0.4751 0.7114 0.4401 -0.0716 -0.0249 -0.0489 367 GLN A CD  
1531 O OE1 . GLN A 367 ? 0.5046 0.7400 0.4782 -0.0634 -0.0224 -0.0412 367 GLN A OE1 
1532 N NE2 . GLN A 367 ? 0.4901 0.7255 0.4414 -0.0695 -0.0263 -0.0512 367 GLN A NE2 
1533 N N   . SER A 368 ? 0.3678 0.5320 0.3309 -0.1087 -0.0104 -0.0655 368 SER A N   
1534 C CA  . SER A 368 ? 0.3918 0.5264 0.3477 -0.1088 -0.0041 -0.0662 368 SER A CA  
1535 C C   . SER A 368 ? 0.3879 0.5041 0.3353 -0.0953 0.0007  -0.0650 368 SER A C   
1536 O O   . SER A 368 ? 0.3941 0.4991 0.3447 -0.0883 0.0054  -0.0605 368 SER A O   
1537 C CB  . SER A 368 ? 0.4454 0.5612 0.3873 -0.1242 -0.0043 -0.0746 368 SER A CB  
1538 O OG  . SER A 368 ? 0.5207 0.6340 0.4484 -0.1271 -0.0078 -0.0825 368 SER A OG  
1539 N N   . ASN A 369 ? 0.3669 0.4825 0.3035 -0.0914 -0.0004 -0.0689 369 ASN A N   
1540 C CA  . ASN A 369 ? 0.3561 0.4577 0.2841 -0.0791 0.0047  -0.0683 369 ASN A CA  
1541 C C   . ASN A 369 ? 0.3169 0.4365 0.2544 -0.0682 0.0051  -0.0609 369 ASN A C   
1542 O O   . ASN A 369 ? 0.3114 0.4248 0.2430 -0.0590 0.0095  -0.0600 369 ASN A O   
1543 C CB  . ASN A 369 ? 0.3855 0.4723 0.2927 -0.0807 0.0048  -0.0774 369 ASN A CB  
1544 C CG  . ASN A 369 ? 0.4452 0.5077 0.3387 -0.0925 0.0048  -0.0855 369 ASN A CG  
1545 O OD1 . ASN A 369 ? 0.4578 0.5030 0.3517 -0.0937 0.0084  -0.0838 369 ASN A OD1 
1546 N ND2 . ASN A 369 ? 0.4844 0.5441 0.3640 -0.1022 0.0005  -0.0944 369 ASN A ND2 
1547 N N   . VAL A 370 ? 0.2857 0.4265 0.2367 -0.0689 0.0012  -0.0553 370 VAL A N   
1548 C CA  . VAL A 370 ? 0.2638 0.4167 0.2208 -0.0600 0.0017  -0.0480 370 VAL A CA  
1549 C C   . VAL A 370 ? 0.2587 0.4103 0.2278 -0.0552 0.0046  -0.0415 370 VAL A C   
1550 O O   . VAL A 370 ? 0.2556 0.4101 0.2339 -0.0583 0.0033  -0.0397 370 VAL A O   
1551 C CB  . VAL A 370 ? 0.2554 0.4283 0.2149 -0.0608 -0.0042 -0.0458 370 VAL A CB  
1552 C CG1 . VAL A 370 ? 0.2485 0.4284 0.2125 -0.0522 -0.0032 -0.0371 370 VAL A CG1 
1553 C CG2 . VAL A 370 ? 0.2578 0.4330 0.2031 -0.0643 -0.0072 -0.0524 370 VAL A CG2 
1554 N N   . LEU A 371 ? 0.2471 0.3958 0.2156 -0.0480 0.0088  -0.0381 371 LEU A N   
1555 C CA  . LEU A 371 ? 0.2355 0.3835 0.2140 -0.0440 0.0114  -0.0327 371 LEU A CA  
1556 C C   . LEU A 371 ? 0.2295 0.3870 0.2121 -0.0405 0.0117  -0.0262 371 LEU A C   
1557 O O   . LEU A 371 ? 0.2364 0.3971 0.2122 -0.0383 0.0134  -0.0256 371 LEU A O   
1558 C CB  . LEU A 371 ? 0.2330 0.3697 0.2070 -0.0393 0.0166  -0.0348 371 LEU A CB  
1559 C CG  . LEU A 371 ? 0.2356 0.3743 0.2193 -0.0347 0.0189  -0.0298 371 LEU A CG  
1560 C CD1 . LEU A 371 ? 0.2338 0.3684 0.2241 -0.0378 0.0170  -0.0290 371 LEU A CD1 
1561 C CD2 . LEU A 371 ? 0.2374 0.3708 0.2161 -0.0271 0.0240  -0.0311 371 LEU A CD2 
1562 N N   . ALA A 372 ? 0.2110 0.3712 0.2030 -0.0401 0.0105  -0.0214 372 ALA A N   
1563 C CA  . ALA A 372 ? 0.2049 0.3692 0.1990 -0.0385 0.0112  -0.0152 372 ALA A CA  
1564 C C   . ALA A 372 ? 0.1920 0.3552 0.1930 -0.0375 0.0141  -0.0132 372 ALA A C   
1565 O O   . ALA A 372 ? 0.1913 0.3509 0.1975 -0.0374 0.0135  -0.0145 372 ALA A O   
1566 C CB  . ALA A 372 ? 0.2030 0.3689 0.1994 -0.0385 0.0071  -0.0116 372 ALA A CB  
1567 N N   . THR A 373 ? 0.1776 0.3459 0.1784 -0.0371 0.0173  -0.0100 373 THR A N   
1568 C CA  . THR A 373 ? 0.1925 0.3653 0.2009 -0.0372 0.0194  -0.0079 373 THR A CA  
1569 C C   . THR A 373 ? 0.2118 0.3884 0.2215 -0.0419 0.0197  -0.0019 373 THR A C   
1570 O O   . THR A 373 ? 0.2083 0.3845 0.2112 -0.0433 0.0203  0.0010  373 THR A O   
1571 C CB  . THR A 373 ? 0.1889 0.3677 0.1966 -0.0324 0.0239  -0.0101 373 THR A CB  
1572 O OG1 . THR A 373 ? 0.2027 0.3873 0.2037 -0.0318 0.0270  -0.0091 373 THR A OG1 
1573 C CG2 . THR A 373 ? 0.1911 0.3601 0.1943 -0.0281 0.0241  -0.0159 373 THR A CG2 
1574 N N   . GLY A 374 ? 0.2172 0.3965 0.2342 -0.0449 0.0193  0.0000  374 GLY A N   
1575 C CA  . GLY A 374 ? 0.2252 0.4056 0.2425 -0.0520 0.0196  0.0052  374 GLY A CA  
1576 C C   . GLY A 374 ? 0.2283 0.4230 0.2546 -0.0557 0.0215  0.0062  374 GLY A C   
1577 O O   . GLY A 374 ? 0.2178 0.4167 0.2506 -0.0528 0.0201  0.0032  374 GLY A O   
1578 N N   . GLY A 375 ? 0.2319 0.4360 0.2584 -0.0621 0.0248  0.0107  375 GLY A N   
1579 C CA  . GLY A 375 ? 0.2342 0.4582 0.2708 -0.0671 0.0268  0.0122  375 GLY A CA  
1580 C C   . GLY A 375 ? 0.2521 0.4716 0.2907 -0.0793 0.0237  0.0146  375 GLY A C   
1581 O O   . GLY A 375 ? 0.2714 0.4697 0.3008 -0.0841 0.0215  0.0165  375 GLY A O   
1582 N N   . GLY A 376 ? 0.2408 0.4805 0.2903 -0.0840 0.0235  0.0143  376 GLY A N   
1583 C CA  . GLY A 376 ? 0.2469 0.4854 0.2987 -0.0974 0.0201  0.0152  376 GLY A CA  
1584 C C   . GLY A 376 ? 0.2598 0.4977 0.3078 -0.1121 0.0231  0.0212  376 GLY A C   
1585 O O   . GLY A 376 ? 0.2799 0.5129 0.3206 -0.1110 0.0275  0.0252  376 GLY A O   
1586 N N   . THR A 377 ? 0.2549 0.4980 0.3066 -0.1270 0.0209  0.0218  377 THR A N   
1587 C CA  . THR A 377 ? 0.2645 0.5026 0.3108 -0.1450 0.0233  0.0276  377 THR A CA  
1588 C C   . THR A 377 ? 0.2681 0.5303 0.3188 -0.1482 0.0311  0.0338  377 THR A C   
1589 O O   . THR A 377 ? 0.2859 0.5342 0.3259 -0.1578 0.0348  0.0400  377 THR A O   
1590 C CB  . THR A 377 ? 0.2654 0.5100 0.3170 -0.1614 0.0188  0.0256  377 THR A CB  
1591 O OG1 . THR A 377 ? 0.2855 0.5054 0.3302 -0.1568 0.0121  0.0196  377 THR A OG1 
1592 C CG2 . THR A 377 ? 0.2769 0.5086 0.3196 -0.1830 0.0209  0.0312  377 THR A CG2 
1593 N N   . SER A 378 ? 0.2443 0.5420 0.3093 -0.1395 0.0340  0.0324  378 SER A N   
1594 C CA  . SER A 378 ? 0.2345 0.5584 0.3037 -0.1404 0.0422  0.0378  378 SER A CA  
1595 C C   . SER A 378 ? 0.2291 0.5404 0.2871 -0.1255 0.0463  0.0385  378 SER A C   
1596 O O   . SER A 378 ? 0.2245 0.5545 0.2828 -0.1241 0.0534  0.0425  378 SER A O   
1597 C CB  . SER A 378 ? 0.2265 0.5949 0.3142 -0.1351 0.0441  0.0360  378 SER A CB  
1598 O OG  . SER A 378 ? 0.2405 0.6067 0.3297 -0.1151 0.0414  0.0298  378 SER A OG  
1599 N N   . ASP A 379 ? 0.2283 0.5109 0.2768 -0.1146 0.0418  0.0343  379 ASP A N   
1600 C CA  . ASP A 379 ? 0.2368 0.5087 0.2749 -0.1017 0.0443  0.0337  379 ASP A CA  
1601 C C   . ASP A 379 ? 0.2595 0.4980 0.2815 -0.1047 0.0419  0.0366  379 ASP A C   
1602 O O   . ASP A 379 ? 0.2628 0.4969 0.2744 -0.1053 0.0460  0.0416  379 ASP A O   
1603 C CB  . ASP A 379 ? 0.2438 0.5158 0.2851 -0.0853 0.0417  0.0261  379 ASP A CB  
1604 C CG  . ASP A 379 ? 0.2847 0.5449 0.3144 -0.0742 0.0433  0.0243  379 ASP A CG  
1605 O OD1 . ASP A 379 ? 0.2733 0.5483 0.3005 -0.0703 0.0494  0.0259  379 ASP A OD1 
1606 O OD2 . ASP A 379 ? 0.3185 0.5562 0.3412 -0.0700 0.0386  0.0214  379 ASP A OD2 
1607 N N   . ARG A 380 ? 0.2782 0.4943 0.2973 -0.1045 0.0354  0.0334  380 ARG A N   
1608 C CA  . ARG A 380 ? 0.3127 0.4968 0.3167 -0.1051 0.0324  0.0357  380 ARG A CA  
1609 C C   . ARG A 380 ? 0.3163 0.4908 0.3105 -0.0923 0.0321  0.0351  380 ARG A C   
1610 O O   . ARG A 380 ? 0.3364 0.4884 0.3171 -0.0914 0.0303  0.0386  380 ARG A O   
1611 C CB  . ARG A 380 ? 0.3528 0.5249 0.3469 -0.1199 0.0352  0.0438  380 ARG A CB  
1612 C CG  . ARG A 380 ? 0.4025 0.5868 0.4057 -0.1368 0.0358  0.0449  380 ARG A CG  
1613 C CD  . ARG A 380 ? 0.4712 0.6443 0.4633 -0.1534 0.0402  0.0539  380 ARG A CD  
1614 N NE  . ARG A 380 ? 0.5346 0.7090 0.5170 -0.1490 0.0462  0.0606  380 ARG A NE  
1615 C CZ  . ARG A 380 ? 0.5619 0.7667 0.5516 -0.1513 0.0531  0.0640  380 ARG A CZ  
1616 N NH1 . ARG A 380 ? 0.5412 0.7799 0.5493 -0.1577 0.0550  0.0619  380 ARG A NH1 
1617 N NH2 . ARG A 380 ? 0.5679 0.7714 0.5461 -0.1461 0.0583  0.0696  380 ARG A NH2 
1618 N N   . HIS A 381 ? 0.2867 0.4775 0.2861 -0.0825 0.0337  0.0307  381 HIS A N   
1619 C CA  . HIS A 381 ? 0.2816 0.4657 0.2716 -0.0725 0.0329  0.0293  381 HIS A CA  
1620 C C   . HIS A 381 ? 0.2613 0.4405 0.2544 -0.0633 0.0281  0.0219  381 HIS A C   
1621 O O   . HIS A 381 ? 0.2435 0.4305 0.2466 -0.0613 0.0274  0.0171  381 HIS A O   
1622 C CB  . HIS A 381 ? 0.2896 0.4911 0.2773 -0.0689 0.0388  0.0298  381 HIS A CB  
1623 C CG  . HIS A 381 ? 0.3195 0.5226 0.2984 -0.0762 0.0439  0.0384  381 HIS A CG  
1624 N ND1 . HIS A 381 ? 0.3400 0.5492 0.3239 -0.0889 0.0471  0.0441  381 HIS A ND1 
1625 C CD2 . HIS A 381 ? 0.3425 0.5428 0.3075 -0.0731 0.0464  0.0423  381 HIS A CD2 
1626 C CE1 . HIS A 381 ? 0.3524 0.5609 0.3252 -0.0936 0.0521  0.0518  381 HIS A CE1 
1627 N NE2 . HIS A 381 ? 0.3588 0.5617 0.3194 -0.0835 0.0518  0.0512  381 HIS A NE2 
1628 N N   . ILE A 382 ? 0.2553 0.4232 0.2391 -0.0579 0.0250  0.0216  382 ILE A N   
1629 C CA  . ILE A 382 ? 0.2466 0.4130 0.2317 -0.0505 0.0212  0.0152  382 ILE A CA  
1630 C C   . ILE A 382 ? 0.2356 0.4113 0.2151 -0.0461 0.0236  0.0125  382 ILE A C   
1631 O O   . ILE A 382 ? 0.2290 0.4060 0.1987 -0.0463 0.0257  0.0167  382 ILE A O   
1632 C CB  . ILE A 382 ? 0.2627 0.4159 0.2412 -0.0473 0.0163  0.0168  382 ILE A CB  
1633 C CG1 . ILE A 382 ? 0.2726 0.4145 0.2550 -0.0501 0.0140  0.0176  382 ILE A CG1 
1634 C CG2 . ILE A 382 ? 0.2684 0.4256 0.2475 -0.0412 0.0127  0.0109  382 ILE A CG2 
1635 C CD1 . ILE A 382 ? 0.2939 0.4200 0.2665 -0.0464 0.0108  0.0213  382 ILE A CD1 
1636 N N   . ARG A 383 ? 0.2273 0.4076 0.2111 -0.0424 0.0237  0.0056  383 ARG A N   
1637 C CA  . ARG A 383 ? 0.2308 0.4156 0.2069 -0.0381 0.0256  0.0011  383 ARG A CA  
1638 C C   . ARG A 383 ? 0.2365 0.4153 0.2111 -0.0359 0.0211  -0.0056 383 ARG A C   
1639 O O   . ARG A 383 ? 0.2431 0.4177 0.2255 -0.0364 0.0191  -0.0082 383 ARG A O   
1640 C CB  . ARG A 383 ? 0.2263 0.4210 0.2052 -0.0354 0.0315  -0.0009 383 ARG A CB  
1641 C CG  . ARG A 383 ? 0.2056 0.4117 0.1836 -0.0383 0.0369  0.0058  383 ARG A CG  
1642 C CD  . ARG A 383 ? 0.2267 0.4478 0.2100 -0.0345 0.0429  0.0045  383 ARG A CD  
1643 N NE  . ARG A 383 ? 0.2581 0.4942 0.2406 -0.0383 0.0488  0.0112  383 ARG A NE  
1644 C CZ  . ARG A 383 ? 0.2823 0.5243 0.2535 -0.0350 0.0533  0.0120  383 ARG A CZ  
1645 N NH1 . ARG A 383 ? 0.2447 0.5019 0.2159 -0.0396 0.0594  0.0192  383 ARG A NH1 
1646 N NH2 . ARG A 383 ? 0.2904 0.5236 0.2492 -0.0280 0.0519  0.0054  383 ARG A NH2 
1647 N N   . ILE A 384 ? 0.2329 0.4121 0.1971 -0.0346 0.0192  -0.0082 384 ILE A N   
1648 C CA  . ILE A 384 ? 0.2313 0.4073 0.1935 -0.0350 0.0147  -0.0150 384 ILE A CA  
1649 C C   . ILE A 384 ? 0.2376 0.4115 0.1904 -0.0333 0.0175  -0.0221 384 ILE A C   
1650 O O   . ILE A 384 ? 0.2415 0.4195 0.1846 -0.0308 0.0203  -0.0215 384 ILE A O   
1651 C CB  . ILE A 384 ? 0.2336 0.4138 0.1902 -0.0351 0.0092  -0.0132 384 ILE A CB  
1652 C CG1 . ILE A 384 ? 0.2363 0.4152 0.1977 -0.0341 0.0075  -0.0052 384 ILE A CG1 
1653 C CG2 . ILE A 384 ? 0.2301 0.4120 0.1867 -0.0378 0.0042  -0.0204 384 ILE A CG2 
1654 C CD1 . ILE A 384 ? 0.2472 0.4223 0.2197 -0.0352 0.0060  -0.0058 384 ILE A CD1 
1655 N N   . TRP A 385 ? 0.2400 0.4056 0.1936 -0.0342 0.0171  -0.0287 385 TRP A N   
1656 C CA  . TRP A 385 ? 0.2564 0.4138 0.1982 -0.0317 0.0202  -0.0362 385 TRP A CA  
1657 C C   . TRP A 385 ? 0.2782 0.4267 0.2130 -0.0373 0.0157  -0.0441 385 TRP A C   
1658 O O   . TRP A 385 ? 0.2728 0.4218 0.2159 -0.0428 0.0115  -0.0437 385 TRP A O   
1659 C CB  . TRP A 385 ? 0.2557 0.4060 0.2019 -0.0270 0.0250  -0.0369 385 TRP A CB  
1660 C CG  . TRP A 385 ? 0.2568 0.4183 0.2146 -0.0239 0.0284  -0.0293 385 TRP A CG  
1661 C CD1 . TRP A 385 ? 0.2669 0.4312 0.2381 -0.0264 0.0266  -0.0246 385 TRP A CD1 
1662 C CD2 . TRP A 385 ? 0.2563 0.4284 0.2129 -0.0184 0.0343  -0.0265 385 TRP A CD2 
1663 N NE1 . TRP A 385 ? 0.2656 0.4413 0.2440 -0.0242 0.0304  -0.0193 385 TRP A NE1 
1664 C CE2 . TRP A 385 ? 0.2605 0.4430 0.2312 -0.0196 0.0353  -0.0199 385 TRP A CE2 
1665 C CE3 . TRP A 385 ? 0.2674 0.4425 0.2119 -0.0126 0.0391  -0.0293 385 TRP A CE3 
1666 C CZ2 . TRP A 385 ? 0.2627 0.4610 0.2375 -0.0168 0.0407  -0.0155 385 TRP A CZ2 
1667 C CZ3 . TRP A 385 ? 0.2773 0.4685 0.2257 -0.0082 0.0452  -0.0244 385 TRP A CZ3 
1668 C CH2 . TRP A 385 ? 0.2673 0.4713 0.2316 -0.0111 0.0459  -0.0174 385 TRP A CH2 
1669 N N   . ASN A 386 ? 0.2953 0.4348 0.2142 -0.0363 0.0171  -0.0517 386 ASN A N   
1670 C CA  . ASN A 386 ? 0.3280 0.4536 0.2375 -0.0431 0.0140  -0.0607 386 ASN A CA  
1671 C C   . ASN A 386 ? 0.3501 0.4559 0.2528 -0.0371 0.0202  -0.0642 386 ASN A C   
1672 O O   . ASN A 386 ? 0.3591 0.4614 0.2511 -0.0284 0.0253  -0.0662 386 ASN A O   
1673 C CB  . ASN A 386 ? 0.3591 0.4851 0.2518 -0.0462 0.0109  -0.0678 386 ASN A CB  
1674 C CG  . ASN A 386 ? 0.4410 0.5516 0.3242 -0.0565 0.0072  -0.0776 386 ASN A CG  
1675 O OD1 . ASN A 386 ? 0.4616 0.5487 0.3351 -0.0559 0.0110  -0.0832 386 ASN A OD1 
1676 N ND2 . ASN A 386 ? 0.4597 0.5834 0.3457 -0.0663 -0.0002 -0.0795 386 ASN A ND2 
1677 N N   . VAL A 387 ? 0.3547 0.4485 0.2628 -0.0402 0.0203  -0.0644 387 VAL A N   
1678 C CA  . VAL A 387 ? 0.3793 0.4536 0.2806 -0.0324 0.0261  -0.0661 387 VAL A CA  
1679 C C   . VAL A 387 ? 0.4168 0.4644 0.2942 -0.0323 0.0279  -0.0764 387 VAL A C   
1680 O O   . VAL A 387 ? 0.4319 0.4621 0.2992 -0.0218 0.0336  -0.0780 387 VAL A O   
1681 C CB  . VAL A 387 ? 0.3874 0.4567 0.3005 -0.0348 0.0259  -0.0618 387 VAL A CB  
1682 C CG1 . VAL A 387 ? 0.3725 0.4654 0.3064 -0.0348 0.0239  -0.0529 387 VAL A CG1 
1683 C CG2 . VAL A 387 ? 0.4007 0.4565 0.3092 -0.0480 0.0221  -0.0665 387 VAL A CG2 
1684 N N   . CYS A 388 ? 0.4298 0.4738 0.2968 -0.0430 0.0231  -0.0834 388 CYS A N   
1685 C CA  . CYS A 388 ? 0.4643 0.4802 0.3058 -0.0450 0.0241  -0.0945 388 CYS A CA  
1686 C C   . CYS A 388 ? 0.4625 0.4812 0.2900 -0.0333 0.0278  -0.0978 388 CYS A C   
1687 O O   . CYS A 388 ? 0.4826 0.4803 0.2935 -0.0220 0.0338  -0.1021 388 CYS A O   
1688 C CB  . CYS A 388 ? 0.5012 0.5151 0.3379 -0.0633 0.0166  -0.1013 388 CYS A CB  
1689 S SG  . CYS A 388 ? 0.6505 0.6245 0.4534 -0.0706 0.0168  -0.1164 388 CYS A SG  
1690 N N   . SER A 389 ? 0.4378 0.4825 0.2711 -0.0343 0.0248  -0.0950 389 SER A N   
1691 C CA  . SER A 389 ? 0.4388 0.4896 0.2591 -0.0236 0.0288  -0.0970 389 SER A CA  
1692 C C   . SER A 389 ? 0.4276 0.4939 0.2594 -0.0093 0.0362  -0.0879 389 SER A C   
1693 O O   . SER A 389 ? 0.4377 0.5072 0.2580 0.0016  0.0418  -0.0894 389 SER A O   
1694 C CB  . SER A 389 ? 0.4362 0.5087 0.2567 -0.0301 0.0229  -0.0964 389 SER A CB  
1695 O OG  . SER A 389 ? 0.4432 0.5401 0.2872 -0.0323 0.0205  -0.0850 389 SER A OG  
1696 N N   . GLY A 390 ? 0.4068 0.4851 0.2609 -0.0101 0.0360  -0.0787 390 GLY A N   
1697 C CA  . GLY A 390 ? 0.3936 0.4909 0.2618 -0.0003 0.0416  -0.0696 390 GLY A CA  
1698 C C   . GLY A 390 ? 0.3756 0.4992 0.2528 -0.0026 0.0408  -0.0621 390 GLY A C   
1699 O O   . GLY A 390 ? 0.3696 0.5108 0.2583 0.0026  0.0453  -0.0543 390 GLY A O   
1700 N N   . ALA A 391 ? 0.3650 0.4917 0.2363 -0.0106 0.0350  -0.0641 391 ALA A N   
1701 C CA  . ALA A 391 ? 0.3590 0.5062 0.2339 -0.0118 0.0343  -0.0568 391 ALA A CA  
1702 C C   . ALA A 391 ? 0.3449 0.5049 0.2404 -0.0159 0.0324  -0.0463 391 ALA A C   
1703 O O   . ALA A 391 ? 0.3473 0.5024 0.2530 -0.0217 0.0276  -0.0462 391 ALA A O   
1704 C CB  . ALA A 391 ? 0.3630 0.5101 0.2251 -0.0181 0.0276  -0.0618 391 ALA A CB  
1705 N N   . CYS A 392 ? 0.3356 0.5110 0.2361 -0.0136 0.0364  -0.0377 392 CYS A N   
1706 C CA  . CYS A 392 ? 0.3339 0.5179 0.2497 -0.0185 0.0342  -0.0280 392 CYS A CA  
1707 C C   . CYS A 392 ? 0.3243 0.5117 0.2325 -0.0220 0.0290  -0.0256 392 CYS A C   
1708 O O   . CYS A 392 ? 0.3259 0.5200 0.2226 -0.0196 0.0315  -0.0231 392 CYS A O   
1709 C CB  . CYS A 392 ? 0.3499 0.5472 0.2734 -0.0165 0.0410  -0.0197 392 CYS A CB  
1710 S SG  . CYS A 392 ? 0.4322 0.6342 0.3690 -0.0243 0.0383  -0.0083 392 CYS A SG  
1711 N N   . LEU A 393 ? 0.3165 0.5004 0.2296 -0.0266 0.0218  -0.0266 393 LEU A N   
1712 C CA  . LEU A 393 ? 0.3155 0.5049 0.2222 -0.0282 0.0157  -0.0245 393 LEU A CA  
1713 C C   . LEU A 393 ? 0.3113 0.5058 0.2209 -0.0273 0.0165  -0.0127 393 LEU A C   
1714 O O   . LEU A 393 ? 0.3197 0.5190 0.2185 -0.0254 0.0142  -0.0088 393 LEU A O   
1715 C CB  . LEU A 393 ? 0.3133 0.5011 0.2272 -0.0329 0.0083  -0.0289 393 LEU A CB  
1716 C CG  . LEU A 393 ? 0.3273 0.5056 0.2383 -0.0366 0.0075  -0.0400 393 LEU A CG  
1717 C CD1 . LEU A 393 ? 0.3295 0.5094 0.2496 -0.0431 0.0011  -0.0427 393 LEU A CD1 
1718 C CD2 . LEU A 393 ? 0.3359 0.5118 0.2279 -0.0362 0.0073  -0.0480 393 LEU A CD2 
1719 N N   . SER A 394 ? 0.2918 0.4837 0.2139 -0.0288 0.0196  -0.0070 394 SER A N   
1720 C CA  . SER A 394 ? 0.2933 0.4847 0.2167 -0.0297 0.0206  0.0037  394 SER A CA  
1721 C C   . SER A 394 ? 0.2951 0.4856 0.2301 -0.0331 0.0259  0.0076  394 SER A C   
1722 O O   . SER A 394 ? 0.2942 0.4834 0.2401 -0.0338 0.0259  0.0029  394 SER A O   
1723 C CB  . SER A 394 ? 0.3074 0.4946 0.2342 -0.0293 0.0136  0.0058  394 SER A CB  
1724 O OG  . SER A 394 ? 0.3347 0.5155 0.2590 -0.0294 0.0147  0.0160  394 SER A OG  
1725 N N   . ALA A 395 ? 0.3037 0.4951 0.2358 -0.0358 0.0301  0.0164  395 ALA A N   
1726 C CA  . ALA A 395 ? 0.3167 0.5100 0.2598 -0.0414 0.0344  0.0208  395 ALA A CA  
1727 C C   . ALA A 395 ? 0.3355 0.5179 0.2732 -0.0461 0.0337  0.0305  395 ALA A C   
1728 O O   . ALA A 395 ? 0.3441 0.5257 0.2688 -0.0462 0.0362  0.0371  395 ALA A O   
1729 C CB  . ALA A 395 ? 0.3164 0.5244 0.2590 -0.0417 0.0425  0.0218  395 ALA A CB  
1730 N N   . VAL A 396 ? 0.3375 0.5089 0.2824 -0.0489 0.0301  0.0314  396 VAL A N   
1731 C CA  . VAL A 396 ? 0.3554 0.5102 0.2922 -0.0521 0.0289  0.0397  396 VAL A CA  
1732 C C   . VAL A 396 ? 0.3582 0.5078 0.3027 -0.0620 0.0312  0.0429  396 VAL A C   
1733 O O   . VAL A 396 ? 0.3540 0.5066 0.3113 -0.0633 0.0293  0.0373  396 VAL A O   
1734 C CB  . VAL A 396 ? 0.3814 0.5253 0.3153 -0.0446 0.0216  0.0377  396 VAL A CB  
1735 C CG1 . VAL A 396 ? 0.4062 0.5284 0.3309 -0.0457 0.0204  0.0453  396 VAL A CG1 
1736 C CG2 . VAL A 396 ? 0.3907 0.5417 0.3150 -0.0365 0.0187  0.0361  396 VAL A CG2 
1737 N N   . ASP A 397 ? 0.3689 0.5092 0.3041 -0.0698 0.0350  0.0519  397 ASP A N   
1738 C CA  . ASP A 397 ? 0.3800 0.5136 0.3200 -0.0823 0.0368  0.0551  397 ASP A CA  
1739 C C   . ASP A 397 ? 0.3892 0.4968 0.3240 -0.0814 0.0313  0.0550  397 ASP A C   
1740 O O   . ASP A 397 ? 0.4079 0.4942 0.3262 -0.0775 0.0299  0.0607  397 ASP A O   
1741 C CB  . ASP A 397 ? 0.4099 0.5403 0.3390 -0.0929 0.0434  0.0655  397 ASP A CB  
1742 C CG  . ASP A 397 ? 0.4695 0.6030 0.4066 -0.1096 0.0466  0.0682  397 ASP A CG  
1743 O OD1 . ASP A 397 ? 0.4629 0.5939 0.4104 -0.1127 0.0426  0.0627  397 ASP A OD1 
1744 O OD2 . ASP A 397 ? 0.5109 0.6512 0.4438 -0.1202 0.0533  0.0758  397 ASP A OD2 
1745 N N   . ALA A 398 ? 0.3768 0.4859 0.3240 -0.0835 0.0282  0.0487  398 ALA A N   
1746 C CA  . ALA A 398 ? 0.3898 0.4745 0.3315 -0.0826 0.0235  0.0477  398 ALA A CA  
1747 C C   . ALA A 398 ? 0.4025 0.4698 0.3384 -0.0976 0.0251  0.0520  398 ALA A C   
1748 O O   . ALA A 398 ? 0.4161 0.4588 0.3439 -0.0975 0.0216  0.0510  398 ALA A O   
1749 C CB  . ALA A 398 ? 0.3799 0.4736 0.3354 -0.0768 0.0192  0.0386  398 ALA A CB  
1750 N N   . HIS A 399 ? 0.3954 0.4763 0.3352 -0.1109 0.0304  0.0562  399 HIS A N   
1751 C CA  . HIS A 399 ? 0.4066 0.4748 0.3416 -0.1291 0.0324  0.0606  399 HIS A CA  
1752 C C   . HIS A 399 ? 0.3960 0.4631 0.3405 -0.1364 0.0281  0.0537  399 HIS A C   
1753 O O   . HIS A 399 ? 0.4097 0.4572 0.3459 -0.1509 0.0277  0.0556  399 HIS A O   
1754 C CB  . HIS A 399 ? 0.4454 0.4752 0.3551 -0.1309 0.0332  0.0689  399 HIS A CB  
1755 C CG  . HIS A 399 ? 0.4857 0.5182 0.3848 -0.1249 0.0377  0.0767  399 HIS A CG  
1756 N ND1 . HIS A 399 ? 0.5114 0.5585 0.4105 -0.1371 0.0448  0.0838  399 HIS A ND1 
1757 C CD2 . HIS A 399 ? 0.5088 0.5354 0.3980 -0.1078 0.0357  0.0780  399 HIS A CD2 
1758 C CE1 . HIS A 399 ? 0.5229 0.5692 0.4101 -0.1268 0.0471  0.0893  399 HIS A CE1 
1759 N NE2 . HIS A 399 ? 0.5269 0.5614 0.4079 -0.1092 0.0413  0.0859  399 HIS A NE2 
1760 N N   . SER A 400 ? 0.3697 0.4575 0.3301 -0.1277 0.0250  0.0457  400 SER A N   
1761 C CA  . SER A 400 ? 0.3588 0.4484 0.3280 -0.1319 0.0205  0.0388  400 SER A CA  
1762 C C   . SER A 400 ? 0.3348 0.4527 0.3216 -0.1208 0.0191  0.0322  400 SER A C   
1763 O O   . SER A 400 ? 0.3375 0.4635 0.3259 -0.1084 0.0204  0.0318  400 SER A O   
1764 C CB  . SER A 400 ? 0.3904 0.4452 0.3448 -0.1257 0.0156  0.0364  400 SER A CB  
1765 O OG  . SER A 400 ? 0.4056 0.4613 0.3665 -0.1280 0.0110  0.0290  400 SER A OG  
1766 N N   . GLN A 401 ? 0.3128 0.4421 0.3105 -0.1247 0.0158  0.0267  401 GLN A N   
1767 C CA  . GLN A 401 ? 0.2959 0.4461 0.3072 -0.1134 0.0143  0.0209  401 GLN A CA  
1768 C C   . GLN A 401 ? 0.3024 0.4366 0.3076 -0.0985 0.0117  0.0178  401 GLN A C   
1769 O O   . GLN A 401 ? 0.3199 0.4283 0.3126 -0.0968 0.0093  0.0182  401 GLN A O   
1770 C CB  . GLN A 401 ? 0.2981 0.4605 0.3191 -0.1194 0.0105  0.0162  401 GLN A CB  
1771 C CG  . GLN A 401 ? 0.3329 0.4689 0.3434 -0.1249 0.0055  0.0133  401 GLN A CG  
1772 C CD  . GLN A 401 ? 0.3981 0.5480 0.4175 -0.1290 0.0010  0.0078  401 GLN A CD  
1773 O OE1 . GLN A 401 ? 0.4105 0.5439 0.4234 -0.1248 -0.0033 0.0030  401 GLN A OE1 
1774 N NE2 . GLN A 401 ? 0.4006 0.5823 0.4341 -0.1364 0.0018  0.0082  401 GLN A NE2 
1775 N N   . VAL A 402 ? 0.2819 0.4314 0.2947 -0.0879 0.0127  0.0151  402 VAL A N   
1776 C CA  . VAL A 402 ? 0.2860 0.4262 0.2953 -0.0760 0.0106  0.0123  402 VAL A CA  
1777 C C   . VAL A 402 ? 0.2866 0.4355 0.3050 -0.0711 0.0084  0.0068  402 VAL A C   
1778 O O   . VAL A 402 ? 0.2921 0.4574 0.3184 -0.0669 0.0102  0.0050  402 VAL A O   
1779 C CB  . VAL A 402 ? 0.2856 0.4333 0.2936 -0.0692 0.0136  0.0134  402 VAL A CB  
1780 C CG1 . VAL A 402 ? 0.2965 0.4354 0.3004 -0.0596 0.0108  0.0108  402 VAL A CG1 
1781 C CG2 . VAL A 402 ? 0.2821 0.4259 0.2813 -0.0744 0.0168  0.0198  402 VAL A CG2 
1782 N N   . CYS A 403 ? 0.2804 0.4169 0.2957 -0.0712 0.0046  0.0042  403 CYS A N   
1783 C CA  . CYS A 403 ? 0.2729 0.4165 0.2948 -0.0669 0.0025  -0.0002 403 CYS A CA  
1784 C C   . CYS A 403 ? 0.2616 0.4050 0.2842 -0.0567 0.0028  -0.0024 403 CYS A C   
1785 O O   . CYS A 403 ? 0.2601 0.4119 0.2883 -0.0527 0.0027  -0.0048 403 CYS A O   
1786 C CB  . CYS A 403 ? 0.2880 0.4185 0.3045 -0.0709 -0.0014 -0.0026 403 CYS A CB  
1787 S SG  . CYS A 403 ? 0.3494 0.4538 0.3522 -0.0638 -0.0031 -0.0031 403 CYS A SG  
1788 N N   . SER A 404 ? 0.2519 0.3854 0.2680 -0.0527 0.0029  -0.0012 404 SER A N   
1789 C CA  . SER A 404 ? 0.2442 0.3789 0.2612 -0.0452 0.0026  -0.0033 404 SER A CA  
1790 C C   . SER A 404 ? 0.2195 0.3518 0.2315 -0.0420 0.0029  -0.0014 404 SER A C   
1791 O O   . SER A 404 ? 0.2120 0.3347 0.2164 -0.0430 0.0024  0.0018  404 SER A O   
1792 C CB  . SER A 404 ? 0.2898 0.4159 0.3040 -0.0421 0.0002  -0.0054 404 SER A CB  
1793 O OG  . SER A 404 ? 0.3604 0.4918 0.3779 -0.0366 0.0005  -0.0075 404 SER A OG  
1794 N N   . ILE A 405 ? 0.2040 0.3442 0.2188 -0.0386 0.0035  -0.0034 405 ILE A N   
1795 C CA  . ILE A 405 ? 0.1923 0.3345 0.2031 -0.0354 0.0027  -0.0026 405 ILE A CA  
1796 C C   . ILE A 405 ? 0.1888 0.3370 0.2034 -0.0321 0.0015  -0.0056 405 ILE A C   
1797 O O   . ILE A 405 ? 0.1827 0.3340 0.2020 -0.0337 0.0028  -0.0083 405 ILE A O   
1798 C CB  . ILE A 405 ? 0.1895 0.3384 0.1990 -0.0373 0.0046  -0.0027 405 ILE A CB  
1799 C CG1 . ILE A 405 ? 0.1925 0.3390 0.1985 -0.0409 0.0066  0.0012  405 ILE A CG1 
1800 C CG2 . ILE A 405 ? 0.1939 0.3479 0.1993 -0.0344 0.0026  -0.0030 405 ILE A CG2 
1801 C CD1 . ILE A 405 ? 0.2021 0.3571 0.2080 -0.0420 0.0097  0.0002  405 ILE A CD1 
1802 N N   . LEU A 406 ? 0.1878 0.3385 0.1996 -0.0275 -0.0006 -0.0045 406 LEU A N   
1803 C CA  . LEU A 406 ? 0.1924 0.3544 0.2088 -0.0254 -0.0016 -0.0067 406 LEU A CA  
1804 C C   . LEU A 406 ? 0.2003 0.3723 0.2140 -0.0232 -0.0039 -0.0058 406 LEU A C   
1805 O O   . LEU A 406 ? 0.2151 0.3819 0.2215 -0.0197 -0.0050 -0.0023 406 LEU A O   
1806 C CB  . LEU A 406 ? 0.2006 0.3609 0.2169 -0.0191 -0.0023 -0.0061 406 LEU A CB  
1807 C CG  . LEU A 406 ? 0.2230 0.3744 0.2402 -0.0202 -0.0009 -0.0073 406 LEU A CG  
1808 C CD1 . LEU A 406 ? 0.2349 0.3825 0.2484 -0.0125 -0.0017 -0.0070 406 LEU A CD1 
1809 C CD2 . LEU A 406 ? 0.2151 0.3732 0.2390 -0.0248 0.0011  -0.0099 406 LEU A CD2 
1810 N N   . TRP A 407 ? 0.1869 0.3731 0.2055 -0.0259 -0.0048 -0.0088 407 TRP A N   
1811 C CA  . TRP A 407 ? 0.1952 0.3958 0.2123 -0.0244 -0.0080 -0.0088 407 TRP A CA  
1812 C C   . TRP A 407 ? 0.2057 0.4222 0.2284 -0.0192 -0.0098 -0.0083 407 TRP A C   
1813 O O   . TRP A 407 ? 0.1865 0.4072 0.2160 -0.0222 -0.0079 -0.0103 407 TRP A O   
1814 C CB  . TRP A 407 ? 0.1853 0.3931 0.2037 -0.0335 -0.0083 -0.0137 407 TRP A CB  
1815 C CG  . TRP A 407 ? 0.1875 0.3831 0.1998 -0.0374 -0.0061 -0.0151 407 TRP A CG  
1816 C CD1 . TRP A 407 ? 0.2029 0.3859 0.2157 -0.0402 -0.0023 -0.0164 407 TRP A CD1 
1817 C CD2 . TRP A 407 ? 0.1877 0.3854 0.1921 -0.0381 -0.0074 -0.0159 407 TRP A CD2 
1818 N NE1 . TRP A 407 ? 0.2063 0.3840 0.2126 -0.0417 -0.0007 -0.0177 407 TRP A NE1 
1819 C CE2 . TRP A 407 ? 0.1994 0.3851 0.2000 -0.0408 -0.0035 -0.0175 407 TRP A CE2 
1820 C CE3 . TRP A 407 ? 0.1901 0.4000 0.1897 -0.0355 -0.0114 -0.0150 407 TRP A CE3 
1821 C CZ2 . TRP A 407 ? 0.2069 0.3917 0.1986 -0.0412 -0.0030 -0.0185 407 TRP A CZ2 
1822 C CZ3 . TRP A 407 ? 0.2043 0.4124 0.1944 -0.0367 -0.0114 -0.0162 407 TRP A CZ3 
1823 C CH2 . TRP A 407 ? 0.2151 0.4104 0.2011 -0.0395 -0.0069 -0.0179 407 TRP A CH2 
1824 N N   . SER A 408 ? 0.2290 0.4563 0.2487 -0.0109 -0.0131 -0.0055 408 SER A N   
1825 C CA  . SER A 408 ? 0.2504 0.4993 0.2765 -0.0045 -0.0148 -0.0051 408 SER A CA  
1826 C C   . SER A 408 ? 0.2796 0.5531 0.3119 -0.0126 -0.0178 -0.0085 408 SER A C   
1827 O O   . SER A 408 ? 0.2878 0.5667 0.3148 -0.0122 -0.0212 -0.0083 408 SER A O   
1828 C CB  . SER A 408 ? 0.2595 0.5079 0.2775 0.0110  -0.0171 0.0001  408 SER A CB  
1829 O OG  . SER A 408 ? 0.2633 0.5399 0.2878 0.0189  -0.0195 0.0007  408 SER A OG  
1830 N N   . PRO A 409 ? 0.2950 0.5844 0.3377 -0.0205 -0.0167 -0.0117 409 PRO A N   
1831 C CA  . PRO A 409 ? 0.3043 0.6185 0.3526 -0.0306 -0.0200 -0.0155 409 PRO A CA  
1832 C C   . PRO A 409 ? 0.3138 0.6597 0.3658 -0.0214 -0.0251 -0.0133 409 PRO A C   
1833 O O   . PRO A 409 ? 0.3275 0.6934 0.3809 -0.0281 -0.0297 -0.0161 409 PRO A O   
1834 C CB  . PRO A 409 ? 0.3076 0.6280 0.3650 -0.0420 -0.0165 -0.0182 409 PRO A CB  
1835 C CG  . PRO A 409 ? 0.3180 0.6161 0.3737 -0.0367 -0.0114 -0.0159 409 PRO A CG  
1836 C CD  . PRO A 409 ? 0.2957 0.5821 0.3442 -0.0213 -0.0124 -0.0117 409 PRO A CD  
1837 N N   . HIS A 410 ? 0.3050 0.6544 0.3567 -0.0050 -0.0247 -0.0083 410 HIS A N   
1838 C CA  . HIS A 410 ? 0.2935 0.6739 0.3480 0.0075  -0.0292 -0.0054 410 HIS A CA  
1839 C C   . HIS A 410 ? 0.3024 0.6754 0.3438 0.0187  -0.0334 -0.0016 410 HIS A C   
1840 O O   . HIS A 410 ? 0.2930 0.6929 0.3356 0.0199  -0.0390 -0.0017 410 HIS A O   
1841 C CB  . HIS A 410 ? 0.2865 0.6753 0.3451 0.0220  -0.0262 -0.0021 410 HIS A CB  
1842 C CG  . HIS A 410 ? 0.2921 0.6891 0.3623 0.0109  -0.0216 -0.0050 410 HIS A CG  
1843 N ND1 . HIS A 410 ? 0.2981 0.7269 0.3814 -0.0038 -0.0227 -0.0083 410 HIS A ND1 
1844 C CD2 . HIS A 410 ? 0.3092 0.6833 0.3778 0.0099  -0.0160 -0.0052 410 HIS A CD2 
1845 C CE1 . HIS A 410 ? 0.3053 0.7294 0.3942 -0.0119 -0.0171 -0.0094 410 HIS A CE1 
1846 N NE2 . HIS A 410 ? 0.3166 0.7089 0.3969 -0.0032 -0.0131 -0.0076 410 HIS A NE2 
1847 N N   . TYR A 411 ? 0.3148 0.6524 0.3430 0.0261  -0.0308 0.0021  411 TYR A N   
1848 C CA  . TYR A 411 ? 0.3232 0.6501 0.3367 0.0371  -0.0337 0.0072  411 TYR A CA  
1849 C C   . TYR A 411 ? 0.3341 0.6490 0.3397 0.0266  -0.0348 0.0057  411 TYR A C   
1850 O O   . TYR A 411 ? 0.3557 0.6662 0.3487 0.0351  -0.0374 0.0104  411 TYR A O   
1851 C CB  . TYR A 411 ? 0.3359 0.6305 0.3367 0.0503  -0.0304 0.0127  411 TYR A CB  
1852 C CG  . TYR A 411 ? 0.3409 0.6474 0.3427 0.0680  -0.0304 0.0156  411 TYR A CG  
1853 C CD1 . TYR A 411 ? 0.3561 0.6736 0.3492 0.0867  -0.0342 0.0212  411 TYR A CD1 
1854 C CD2 . TYR A 411 ? 0.3451 0.6545 0.3561 0.0673  -0.0267 0.0127  411 TYR A CD2 
1855 C CE1 . TYR A 411 ? 0.3606 0.6898 0.3534 0.1056  -0.0338 0.0238  411 TYR A CE1 
1856 C CE2 . TYR A 411 ? 0.3491 0.6717 0.3605 0.0849  -0.0262 0.0149  411 TYR A CE2 
1857 C CZ  . TYR A 411 ? 0.3660 0.6980 0.3682 0.1046  -0.0296 0.0203  411 TYR A CZ  
1858 O OH  . TYR A 411 ? 0.3912 0.7364 0.3926 0.1246  -0.0286 0.0225  411 TYR A OH  
1859 N N   . LYS A 412 ? 0.3189 0.6273 0.3297 0.0099  -0.0325 -0.0002 412 LYS A N   
1860 C CA  . LYS A 412 ? 0.3204 0.6157 0.3222 0.0014  -0.0325 -0.0021 412 LYS A CA  
1861 C C   . LYS A 412 ? 0.3170 0.5817 0.3062 0.0076  -0.0289 0.0038  412 LYS A C   
1862 O O   . LYS A 412 ? 0.3272 0.5865 0.3039 0.0126  -0.0303 0.0080  412 LYS A O   
1863 C CB  . LYS A 412 ? 0.3385 0.6576 0.3365 0.0003  -0.0387 -0.0039 412 LYS A CB  
1864 N N   . GLU A 413 ? 0.3008 0.5467 0.2928 0.0074  -0.0244 0.0045  413 GLU A N   
1865 C CA  . GLU A 413 ? 0.3011 0.5182 0.2832 0.0103  -0.0208 0.0093  413 GLU A CA  
1866 C C   . GLU A 413 ? 0.2891 0.4922 0.2775 0.0002  -0.0163 0.0057  413 GLU A C   
1867 O O   . GLU A 413 ? 0.2801 0.4925 0.2792 -0.0060 -0.0157 0.0006  413 GLU A O   
1868 C CB  . GLU A 413 ? 0.3294 0.5371 0.3054 0.0245  -0.0211 0.0148  413 GLU A CB  
1869 C CG  . GLU A 413 ? 0.3700 0.5875 0.3361 0.0383  -0.0253 0.0202  413 GLU A CG  
1870 C CD  . GLU A 413 ? 0.4149 0.6253 0.3744 0.0552  -0.0257 0.0248  413 GLU A CD  
1871 O OE1 . GLU A 413 ? 0.4433 0.6462 0.4080 0.0558  -0.0231 0.0224  413 GLU A OE1 
1872 O OE2 . GLU A 413 ? 0.4133 0.6256 0.3611 0.0690  -0.0285 0.0307  413 GLU A OE2 
1873 N N   . LEU A 414 ? 0.2903 0.4716 0.2714 -0.0018 -0.0132 0.0089  414 LEU A N   
1874 C CA  . LEU A 414 ? 0.2898 0.4587 0.2759 -0.0095 -0.0093 0.0066  414 LEU A CA  
1875 C C   . LEU A 414 ? 0.2775 0.4264 0.2572 -0.0051 -0.0082 0.0106  414 LEU A C   
1876 O O   . LEU A 414 ? 0.2887 0.4269 0.2567 0.0016  -0.0090 0.0160  414 LEU A O   
1877 C CB  . LEU A 414 ? 0.3132 0.4767 0.2958 -0.0170 -0.0065 0.0068  414 LEU A CB  
1878 C CG  . LEU A 414 ? 0.3502 0.5264 0.3362 -0.0224 -0.0065 0.0015  414 LEU A CG  
1879 C CD1 . LEU A 414 ? 0.3655 0.5506 0.3429 -0.0195 -0.0092 0.0029  414 LEU A CD1 
1880 C CD2 . LEU A 414 ? 0.3676 0.5369 0.3543 -0.0287 -0.0020 0.0001  414 LEU A CD2 
1881 N N   . ILE A 415 ? 0.2548 0.3964 0.2401 -0.0093 -0.0063 0.0080  415 ILE A N   
1882 C CA  . ILE A 415 ? 0.2494 0.3698 0.2275 -0.0081 -0.0054 0.0103  415 ILE A CA  
1883 C C   . ILE A 415 ? 0.2401 0.3554 0.2231 -0.0187 -0.0029 0.0083  415 ILE A C   
1884 O O   . ILE A 415 ? 0.2339 0.3605 0.2273 -0.0228 -0.0020 0.0042  415 ILE A O   
1885 C CB  . ILE A 415 ? 0.2525 0.3703 0.2299 0.0010  -0.0067 0.0089  415 ILE A CB  
1886 C CG1 . ILE A 415 ? 0.2757 0.3661 0.2410 0.0022  -0.0061 0.0106  415 ILE A CG1 
1887 C CG2 . ILE A 415 ? 0.2417 0.3747 0.2322 -0.0018 -0.0061 0.0037  415 ILE A CG2 
1888 C CD1 . ILE A 415 ? 0.2943 0.3790 0.2542 0.0145  -0.0070 0.0094  415 ILE A CD1 
1889 N N   . SER A 416 ? 0.2437 0.3429 0.2189 -0.0235 -0.0016 0.0118  416 SER A N   
1890 C CA  . SER A 416 ? 0.2388 0.3375 0.2194 -0.0339 0.0004  0.0105  416 SER A CA  
1891 C C   . SER A 416 ? 0.2488 0.3281 0.2226 -0.0373 -0.0002 0.0108  416 SER A C   
1892 O O   . SER A 416 ? 0.2701 0.3303 0.2306 -0.0331 -0.0011 0.0138  416 SER A O   
1893 C CB  . SER A 416 ? 0.2420 0.3446 0.2207 -0.0402 0.0032  0.0142  416 SER A CB  
1894 O OG  . SER A 416 ? 0.2690 0.3557 0.2335 -0.0389 0.0034  0.0203  416 SER A OG  
1895 N N   . GLY A 417 ? 0.2335 0.3168 0.2147 -0.0446 0.0000  0.0075  417 GLY A N   
1896 C CA  . GLY A 417 ? 0.2456 0.3122 0.2204 -0.0504 -0.0014 0.0065  417 GLY A CA  
1897 C C   . GLY A 417 ? 0.2584 0.3264 0.2344 -0.0639 0.0003  0.0089  417 GLY A C   
1898 O O   . GLY A 417 ? 0.2480 0.3364 0.2349 -0.0675 0.0024  0.0094  417 GLY A O   
1899 N N   . HIS A 418 ? 0.2795 0.3253 0.2434 -0.0717 -0.0004 0.0106  418 HIS A N   
1900 C CA  . HIS A 418 ? 0.2904 0.3379 0.2546 -0.0868 0.0016  0.0140  418 HIS A CA  
1901 C C   . HIS A 418 ? 0.3070 0.3414 0.2661 -0.0996 -0.0009 0.0112  418 HIS A C   
1902 O O   . HIS A 418 ? 0.3069 0.3262 0.2592 -0.0958 -0.0042 0.0063  418 HIS A O   
1903 C CB  . HIS A 418 ? 0.3146 0.3478 0.2660 -0.0878 0.0046  0.0216  418 HIS A CB  
1904 C CG  . HIS A 418 ? 0.3487 0.3964 0.3040 -0.0766 0.0062  0.0237  418 HIS A CG  
1905 N ND1 . HIS A 418 ? 0.3691 0.4422 0.3359 -0.0793 0.0093  0.0247  418 HIS A ND1 
1906 C CD2 . HIS A 418 ? 0.3722 0.4144 0.3217 -0.0626 0.0047  0.0239  418 HIS A CD2 
1907 C CE1 . HIS A 418 ? 0.3790 0.4578 0.3447 -0.0683 0.0094  0.0252  418 HIS A CE1 
1908 N NE2 . HIS A 418 ? 0.3850 0.4477 0.3415 -0.0585 0.0064  0.0250  418 HIS A NE2 
1909 N N   . GLY A 419 ? 0.3095 0.3538 0.2731 -0.1153 0.0009  0.0138  419 GLY A N   
1910 C CA  . GLY A 419 ? 0.3350 0.3710 0.2949 -0.1312 -0.0017 0.0111  419 GLY A CA  
1911 C C   . GLY A 419 ? 0.3783 0.3888 0.3222 -0.1455 0.0005  0.0169  419 GLY A C   
1912 O O   . GLY A 419 ? 0.3968 0.3783 0.3232 -0.1389 0.0021  0.0213  419 GLY A O   
1913 N N   . PHE A 420 ? 0.3864 0.4093 0.3361 -0.1656 0.0010  0.0178  420 PHE A N   
1914 C CA  . PHE A 420 ? 0.4151 0.4164 0.3506 -0.1840 0.0037  0.0238  420 PHE A CA  
1915 C C   . PHE A 420 ? 0.4315 0.4243 0.3587 -0.1778 0.0097  0.0333  420 PHE A C   
1916 O O   . PHE A 420 ? 0.4186 0.4414 0.3602 -0.1685 0.0126  0.0353  420 PHE A O   
1917 C CB  . PHE A 420 ? 0.4019 0.4355 0.3532 -0.2054 0.0043  0.0240  420 PHE A CB  
1918 C CG  . PHE A 420 ? 0.4259 0.4353 0.3619 -0.2295 0.0062  0.0287  420 PHE A CG  
1919 C CD1 . PHE A 420 ? 0.4551 0.4305 0.3740 -0.2422 0.0014  0.0235  420 PHE A CD1 
1920 C CD2 . PHE A 420 ? 0.4310 0.4473 0.3664 -0.2391 0.0132  0.0385  420 PHE A CD2 
1921 C CE1 . PHE A 420 ? 0.4774 0.4246 0.3789 -0.2656 0.0034  0.0280  420 PHE A CE1 
1922 C CE2 . PHE A 420 ? 0.4563 0.4469 0.3754 -0.2623 0.0156  0.0438  420 PHE A CE2 
1923 C CZ  . PHE A 420 ? 0.4739 0.4291 0.3760 -0.2761 0.0107  0.0385  420 PHE A CZ  
1924 N N   . ALA A 421 ? 0.4590 0.4093 0.3610 -0.1804 0.0112  0.0386  421 ALA A N   
1925 C CA  . ALA A 421 ? 0.4901 0.3982 0.3707 -0.1904 0.0080  0.0356  421 ALA A CA  
1926 C C   . ALA A 421 ? 0.5160 0.3890 0.3783 -0.1699 0.0048  0.0321  421 ALA A C   
1927 O O   . ALA A 421 ? 0.5354 0.3769 0.3817 -0.1743 0.0012  0.0266  421 ALA A O   
1928 C CB  . ALA A 421 ? 0.5076 0.3874 0.3692 -0.2094 0.0125  0.0444  421 ALA A CB  
1929 N N   . GLN A 422 ? 0.5131 0.3918 0.3766 -0.1479 0.0061  0.0351  422 GLN A N   
1930 C CA  . GLN A 422 ? 0.5329 0.3811 0.3786 -0.1275 0.0038  0.0331  422 GLN A CA  
1931 C C   . GLN A 422 ? 0.5091 0.3714 0.3658 -0.1143 -0.0007 0.0234  422 GLN A C   
1932 O O   . GLN A 422 ? 0.5289 0.3646 0.3694 -0.0996 -0.0025 0.0208  422 GLN A O   
1933 C CB  . GLN A 422 ? 0.5720 0.4183 0.4111 -0.1102 0.0066  0.0411  422 GLN A CB  
1934 C CG  . GLN A 422 ? 0.6671 0.4920 0.4891 -0.1203 0.0114  0.0521  422 GLN A CG  
1935 C CD  . GLN A 422 ? 0.8087 0.5782 0.5992 -0.1275 0.0116  0.0543  422 GLN A CD  
1936 O OE1 . GLN A 422 ? 0.8558 0.5949 0.6296 -0.1139 0.0086  0.0500  422 GLN A OE1 
1937 N NE2 . GLN A 422 ? 0.8404 0.5946 0.6208 -0.1492 0.0155  0.0613  422 GLN A NE2 
1938 N N   . ASN A 423 ? 0.4645 0.3682 0.3471 -0.1176 -0.0019 0.0187  423 ASN A N   
1939 C CA  . ASN A 423 ? 0.4459 0.3658 0.3396 -0.1062 -0.0054 0.0104  423 ASN A CA  
1940 C C   . ASN A 423 ? 0.4392 0.3549 0.3285 -0.0831 -0.0053 0.0108  423 ASN A C   
1941 O O   . ASN A 423 ? 0.4470 0.3523 0.3301 -0.0720 -0.0077 0.0052  423 ASN A O   
1942 C CB  . ASN A 423 ? 0.4602 0.3598 0.3436 -0.1140 -0.0095 0.0027  423 ASN A CB  
1943 C CG  . ASN A 423 ? 0.4803 0.3884 0.3693 -0.1381 -0.0106 0.0016  423 ASN A CG  
1944 O OD1 . ASN A 423 ? 0.4657 0.4122 0.3769 -0.1447 -0.0099 0.0024  423 ASN A OD1 
1945 N ND2 . ASN A 423 ? 0.5047 0.3773 0.3731 -0.1516 -0.0124 -0.0004 423 ASN A ND2 
1946 N N   . GLN A 424 ? 0.4156 0.3414 0.3078 -0.0760 -0.0026 0.0174  424 GLN A N   
1947 C CA  . GLN A 424 ? 0.4133 0.3376 0.3009 -0.0556 -0.0027 0.0188  424 GLN A CA  
1948 C C   . GLN A 424 ? 0.3839 0.3468 0.2930 -0.0474 -0.0026 0.0175  424 GLN A C   
1949 O O   . GLN A 424 ? 0.3660 0.3548 0.2921 -0.0562 -0.0016 0.0164  424 GLN A O   
1950 C CB  . GLN A 424 ? 0.4451 0.3442 0.3130 -0.0520 -0.0005 0.0276  424 GLN A CB  
1951 C CG  . GLN A 424 ? 0.4689 0.3904 0.3452 -0.0528 0.0021  0.0342  424 GLN A CG  
1952 C CD  . GLN A 424 ? 0.5027 0.4318 0.3844 -0.0724 0.0053  0.0377  424 GLN A CD  
1953 O OE1 . GLN A 424 ? 0.4912 0.4334 0.3854 -0.0859 0.0049  0.0332  424 GLN A OE1 
1954 N NE2 . GLN A 424 ? 0.5104 0.4343 0.3826 -0.0736 0.0086  0.0464  424 GLN A NE2 
1955 N N   . LEU A 425 ? 0.3704 0.3365 0.2774 -0.0300 -0.0035 0.0175  425 LEU A N   
1956 C CA  . LEU A 425 ? 0.3419 0.3402 0.2653 -0.0233 -0.0034 0.0170  425 LEU A CA  
1957 C C   . LEU A 425 ? 0.3411 0.3379 0.2562 -0.0170 -0.0025 0.0241  425 LEU A C   
1958 O O   . LEU A 425 ? 0.3558 0.3273 0.2520 -0.0092 -0.0027 0.0284  425 LEU A O   
1959 C CB  . LEU A 425 ? 0.3342 0.3436 0.2629 -0.0100 -0.0050 0.0125  425 LEU A CB  
1960 C CG  . LEU A 425 ? 0.3435 0.3499 0.2749 -0.0117 -0.0060 0.0059  425 LEU A CG  
1961 C CD1 . LEU A 425 ? 0.3261 0.3526 0.2667 0.0002  -0.0063 0.0026  425 LEU A CD1 
1962 C CD2 . LEU A 425 ? 0.3442 0.3611 0.2873 -0.0269 -0.0058 0.0031  425 LEU A CD2 
1963 N N   . VAL A 426 ? 0.3173 0.3391 0.2441 -0.0196 -0.0016 0.0252  426 VAL A N   
1964 C CA  . VAL A 426 ? 0.3189 0.3426 0.2377 -0.0130 -0.0014 0.0314  426 VAL A CA  
1965 C C   . VAL A 426 ? 0.3159 0.3675 0.2460 -0.0036 -0.0036 0.0284  426 VAL A C   
1966 O O   . VAL A 426 ? 0.2953 0.3682 0.2414 -0.0090 -0.0034 0.0232  426 VAL A O   
1967 C CB  . VAL A 426 ? 0.3228 0.3487 0.2404 -0.0248 0.0019  0.0361  426 VAL A CB  
1968 C CG1 . VAL A 426 ? 0.3249 0.3541 0.2326 -0.0169 0.0019  0.0423  426 VAL A CG1 
1969 C CG2 . VAL A 426 ? 0.3375 0.3371 0.2438 -0.0368 0.0043  0.0396  426 VAL A CG2 
1970 N N   . ILE A 427 ? 0.3276 0.3792 0.2487 0.0102  -0.0058 0.0319  427 ILE A N   
1971 C CA  . ILE A 427 ? 0.3219 0.4031 0.2532 0.0175  -0.0084 0.0296  427 ILE A CA  
1972 C C   . ILE A 427 ? 0.3227 0.4111 0.2482 0.0166  -0.0086 0.0342  427 ILE A C   
1973 O O   . ILE A 427 ? 0.3382 0.4076 0.2465 0.0209  -0.0079 0.0416  427 ILE A O   
1974 C CB  . ILE A 427 ? 0.3282 0.4126 0.2557 0.0343  -0.0112 0.0299  427 ILE A CB  
1975 C CG1 . ILE A 427 ? 0.3362 0.4143 0.2688 0.0348  -0.0103 0.0247  427 ILE A CG1 
1976 C CG2 . ILE A 427 ? 0.3204 0.4396 0.2586 0.0399  -0.0145 0.0282  427 ILE A CG2 
1977 C CD1 . ILE A 427 ? 0.3521 0.4333 0.2805 0.0523  -0.0119 0.0247  427 ILE A CD1 
1978 N N   . TRP A 428 ? 0.3044 0.4174 0.2421 0.0104  -0.0091 0.0299  428 TRP A N   
1979 C CA  . TRP A 428 ? 0.3124 0.4347 0.2445 0.0091  -0.0093 0.0327  428 TRP A CA  
1980 C C   . TRP A 428 ? 0.3172 0.4672 0.2554 0.0151  -0.0140 0.0291  428 TRP A C   
1981 O O   . TRP A 428 ? 0.3044 0.4702 0.2567 0.0124  -0.0153 0.0224  428 TRP A O   
1982 C CB  . TRP A 428 ? 0.3008 0.4276 0.2399 -0.0043 -0.0055 0.0294  428 TRP A CB  
1983 C CG  . TRP A 428 ? 0.3088 0.4188 0.2489 -0.0133 -0.0013 0.0304  428 TRP A CG  
1984 C CD1 . TRP A 428 ? 0.3137 0.4225 0.2650 -0.0182 -0.0006 0.0255  428 TRP A CD1 
1985 C CD2 . TRP A 428 ? 0.3238 0.4205 0.2546 -0.0204 0.0028  0.0365  428 TRP A CD2 
1986 N NE1 . TRP A 428 ? 0.3223 0.4186 0.2720 -0.0274 0.0028  0.0278  428 TRP A NE1 
1987 C CE2 . TRP A 428 ? 0.3339 0.4234 0.2719 -0.0299 0.0053  0.0345  428 TRP A CE2 
1988 C CE3 . TRP A 428 ? 0.3477 0.4394 0.2645 -0.0201 0.0048  0.0437  428 TRP A CE3 
1989 C CZ2 . TRP A 428 ? 0.3539 0.4336 0.2871 -0.0403 0.0096  0.0392  428 TRP A CZ2 
1990 C CZ3 . TRP A 428 ? 0.3678 0.4470 0.2786 -0.0302 0.0099  0.0492  428 TRP A CZ3 
1991 C CH2 . TRP A 428 ? 0.3667 0.4412 0.2866 -0.0408 0.0121  0.0467  428 TRP A CH2 
1992 N N   . LYS A 429 ? 0.3347 0.4916 0.2623 0.0217  -0.0165 0.0334  429 LYS A N   
1993 C CA  . LYS A 429 ? 0.3440 0.5301 0.2767 0.0256  -0.0219 0.0297  429 LYS A CA  
1994 C C   . LYS A 429 ? 0.3541 0.5522 0.2925 0.0134  -0.0211 0.0232  429 LYS A C   
1995 O O   . LYS A 429 ? 0.3664 0.5535 0.2971 0.0082  -0.0175 0.0253  429 LYS A O   
1996 C CB  . LYS A 429 ? 0.3763 0.5660 0.2934 0.0386  -0.0255 0.0371  429 LYS A CB  
1997 C CG  . LYS A 429 ? 0.4386 0.6634 0.3619 0.0429  -0.0323 0.0330  429 LYS A CG  
1998 C CD  . LYS A 429 ? 0.4932 0.7361 0.4306 0.0487  -0.0351 0.0297  429 LYS A CD  
1999 C CE  . LYS A 429 ? 0.5309 0.8131 0.4771 0.0495  -0.0418 0.0251  429 LYS A CE  
2000 N NZ  . LYS A 429 ? 0.5583 0.8531 0.5180 0.0316  -0.0416 0.0151  429 LYS A NZ  
2001 N N   . TYR A 430 ? 0.3485 0.5679 0.2994 0.0084  -0.0240 0.0152  430 TYR A N   
2002 C CA  . TYR A 430 ? 0.3530 0.5800 0.3062 -0.0026 -0.0235 0.0080  430 TYR A CA  
2003 C C   . TYR A 430 ? 0.3582 0.6092 0.3077 -0.0010 -0.0299 0.0052  430 TYR A C   
2004 O O   . TYR A 430 ? 0.3531 0.6231 0.3084 0.0046  -0.0349 0.0053  430 TYR A O   
2005 C CB  . TYR A 430 ? 0.3450 0.5732 0.3124 -0.0117 -0.0217 0.0007  430 TYR A CB  
2006 C CG  . TYR A 430 ? 0.3551 0.5810 0.3214 -0.0218 -0.0194 -0.0061 430 TYR A CG  
2007 C CD1 . TYR A 430 ? 0.3732 0.5827 0.3350 -0.0242 -0.0137 -0.0048 430 TYR A CD1 
2008 C CD2 . TYR A 430 ? 0.3582 0.5983 0.3265 -0.0286 -0.0229 -0.0139 430 TYR A CD2 
2009 C CE1 . TYR A 430 ? 0.3854 0.5923 0.3444 -0.0306 -0.0111 -0.0110 430 TYR A CE1 
2010 C CE2 . TYR A 430 ? 0.3737 0.6067 0.3374 -0.0366 -0.0205 -0.0207 430 TYR A CE2 
2011 C CZ  . TYR A 430 ? 0.3935 0.6097 0.3520 -0.0361 -0.0144 -0.0191 430 TYR A CZ  
2012 O OH  . TYR A 430 ? 0.4144 0.6232 0.3666 -0.0411 -0.0116 -0.0257 430 TYR A OH  
2013 N N   . PRO A 431 ? 0.3603 0.6133 0.2999 -0.0053 -0.0302 0.0025  431 PRO A N   
2014 C CA  . PRO A 431 ? 0.3678 0.6041 0.3007 -0.0113 -0.0241 0.0015  431 PRO A CA  
2015 C C   . PRO A 431 ? 0.3815 0.6042 0.3002 -0.0058 -0.0203 0.0107  431 PRO A C   
2016 O O   . PRO A 431 ? 0.3782 0.5915 0.2924 -0.0106 -0.0148 0.0102  431 PRO A O   
2017 C CB  . PRO A 431 ? 0.3768 0.6255 0.3050 -0.0181 -0.0272 -0.0076 431 PRO A CB  
2018 C CG  . PRO A 431 ? 0.3771 0.6480 0.3007 -0.0120 -0.0352 -0.0062 431 PRO A CG  
2019 C CD  . PRO A 431 ? 0.3489 0.6261 0.2839 -0.0051 -0.0374 -0.0014 431 PRO A CD  
2020 N N   . THR A 432 ? 0.3918 0.6131 0.3025 0.0045  -0.0228 0.0195  432 THR A N   
2021 C CA  . THR A 432 ? 0.4091 0.6148 0.3035 0.0089  -0.0189 0.0294  432 THR A CA  
2022 C C   . THR A 432 ? 0.4148 0.5976 0.3110 0.0039  -0.0115 0.0340  432 THR A C   
2023 O O   . THR A 432 ? 0.4224 0.5932 0.3062 0.0029  -0.0068 0.0412  432 THR A O   
2024 C CB  . THR A 432 ? 0.4283 0.6342 0.3114 0.0225  -0.0234 0.0382  432 THR A CB  
2025 O OG1 . THR A 432 ? 0.4444 0.6409 0.3353 0.0274  -0.0236 0.0404  432 THR A OG1 
2026 C CG2 . THR A 432 ? 0.4193 0.6528 0.3001 0.0282  -0.0315 0.0346  432 THR A CG2 
2027 N N   . MET A 433 ? 0.4080 0.5855 0.3185 0.0004  -0.0107 0.0304  433 MET A N   
2028 C CA  . MET A 433 ? 0.4142 0.5724 0.3282 -0.0052 -0.0051 0.0335  433 MET A CA  
2029 C C   . MET A 433 ? 0.4323 0.5690 0.3322 -0.0002 -0.0036 0.0442  433 MET A C   
2030 O O   . MET A 433 ? 0.4450 0.5656 0.3422 -0.0074 0.0017  0.0484  433 MET A O   
2031 C CB  . MET A 433 ? 0.4181 0.5770 0.3352 -0.0150 0.0009  0.0309  433 MET A CB  
2032 C CG  . MET A 433 ? 0.4355 0.6067 0.3660 -0.0198 0.0005  0.0204  433 MET A CG  
2033 S SD  . MET A 433 ? 0.4738 0.6427 0.4211 -0.0210 -0.0015 0.0155  433 MET A SD  
2034 C CE  . MET A 433 ? 0.4277 0.5791 0.3769 -0.0262 0.0039  0.0209  433 MET A CE  
2035 N N   . ALA A 434 ? 0.4332 0.5695 0.3233 0.0120  -0.0082 0.0488  434 ALA A N   
2036 C CA  . ALA A 434 ? 0.4494 0.5602 0.3224 0.0188  -0.0069 0.0592  434 ALA A CA  
2037 C C   . ALA A 434 ? 0.4610 0.5551 0.3396 0.0197  -0.0067 0.0579  434 ALA A C   
2038 O O   . ALA A 434 ? 0.4501 0.5582 0.3429 0.0224  -0.0100 0.0508  434 ALA A O   
2039 C CB  . ALA A 434 ? 0.4483 0.5660 0.3079 0.0346  -0.0123 0.0644  434 ALA A CB  
2040 N N   . LYS A 435 ? 0.4804 0.5440 0.3466 0.0166  -0.0028 0.0646  435 LYS A N   
2041 C CA  . LYS A 435 ? 0.5016 0.5449 0.3688 0.0175  -0.0027 0.0631  435 LYS A CA  
2042 C C   . LYS A 435 ? 0.5124 0.5523 0.3709 0.0367  -0.0073 0.0652  435 LYS A C   
2043 O O   . LYS A 435 ? 0.5295 0.5598 0.3697 0.0480  -0.0084 0.0734  435 LYS A O   
2044 C CB  . LYS A 435 ? 0.5417 0.5508 0.3945 0.0077  0.0024  0.0697  435 LYS A CB  
2045 C CG  . LYS A 435 ? 0.6062 0.5930 0.4594 0.0054  0.0024  0.0663  435 LYS A CG  
2046 C CD  . LYS A 435 ? 0.6797 0.6376 0.5228 -0.0105 0.0072  0.0705  435 LYS A CD  
2047 C CE  . LYS A 435 ? 0.7170 0.6951 0.5764 -0.0284 0.0108  0.0677  435 LYS A CE  
2048 N NZ  . LYS A 435 ? 0.7550 0.7106 0.6088 -0.0454 0.0145  0.0702  435 LYS A NZ  
2049 N N   . VAL A 436 ? 0.5025 0.5523 0.3737 0.0416  -0.0098 0.0584  436 VAL A N   
2050 C CA  . VAL A 436 ? 0.5078 0.5599 0.3735 0.0609  -0.0137 0.0596  436 VAL A CA  
2051 C C   . VAL A 436 ? 0.5138 0.5297 0.3660 0.0662  -0.0117 0.0614  436 VAL A C   
2052 O O   . VAL A 436 ? 0.5389 0.5357 0.3717 0.0828  -0.0127 0.0677  436 VAL A O   
2053 C CB  . VAL A 436 ? 0.5080 0.5980 0.3964 0.0630  -0.0172 0.0509  436 VAL A CB  
2054 C CG1 . VAL A 436 ? 0.5181 0.6138 0.4039 0.0825  -0.0202 0.0515  436 VAL A CG1 
2055 C CG2 . VAL A 436 ? 0.5065 0.6287 0.4033 0.0594  -0.0201 0.0491  436 VAL A CG2 
2056 N N   . ALA A 437 ? 0.4863 0.4922 0.3472 0.0531  -0.0093 0.0555  437 ALA A N   
2057 C CA  . ALA A 437 ? 0.4920 0.4646 0.3406 0.0563  -0.0079 0.0549  437 ALA A CA  
2058 C C   . ALA A 437 ? 0.4825 0.4428 0.3378 0.0361  -0.0051 0.0502  437 ALA A C   
2059 O O   . ALA A 437 ? 0.4660 0.4506 0.3406 0.0229  -0.0045 0.0457  437 ALA A O   
2060 C CB  . ALA A 437 ? 0.4840 0.4719 0.3403 0.0717  -0.0105 0.0494  437 ALA A CB  
2061 N N   . GLU A 438 ? 0.4917 0.4142 0.3300 0.0344  -0.0037 0.0509  438 GLU A N   
2062 C CA  . GLU A 438 ? 0.4965 0.4083 0.3401 0.0162  -0.0021 0.0458  438 GLU A CA  
2063 C C   . GLU A 438 ? 0.4974 0.3926 0.3350 0.0243  -0.0035 0.0397  438 GLU A C   
2064 O O   . GLU A 438 ? 0.5251 0.3908 0.3407 0.0385  -0.0037 0.0425  438 GLU A O   
2065 C CB  . GLU A 438 ? 0.5493 0.4300 0.3763 0.0011  0.0010  0.0521  438 GLU A CB  
2066 C CG  . GLU A 438 ? 0.6171 0.5198 0.4536 -0.0100 0.0034  0.0567  438 GLU A CG  
2067 C CD  . GLU A 438 ? 0.7403 0.6209 0.5665 -0.0295 0.0073  0.0619  438 GLU A CD  
2068 O OE1 . GLU A 438 ? 0.7924 0.6406 0.5941 -0.0275 0.0093  0.0706  438 GLU A OE1 
2069 O OE2 . GLU A 438 ? 0.7406 0.6369 0.5827 -0.0466 0.0086  0.0578  438 GLU A OE2 
2070 N N   . LEU A 439 ? 0.4708 0.3843 0.3262 0.0172  -0.0043 0.0315  439 LEU A N   
2071 C CA  . LEU A 439 ? 0.4700 0.3701 0.3201 0.0239  -0.0053 0.0250  439 LEU A CA  
2072 C C   . LEU A 439 ? 0.4737 0.3484 0.3166 0.0062  -0.0050 0.0214  439 LEU A C   
2073 O O   . LEU A 439 ? 0.4606 0.3546 0.3207 -0.0090 -0.0052 0.0174  439 LEU A O   
2074 C CB  . LEU A 439 ? 0.4537 0.3913 0.3261 0.0296  -0.0064 0.0188  439 LEU A CB  
2075 C CG  . LEU A 439 ? 0.4620 0.4294 0.3436 0.0444  -0.0072 0.0216  439 LEU A CG  
2076 C CD1 . LEU A 439 ? 0.4437 0.4474 0.3477 0.0449  -0.0077 0.0157  439 LEU A CD1 
2077 C CD2 . LEU A 439 ? 0.4868 0.4368 0.3487 0.0660  -0.0077 0.0254  439 LEU A CD2 
2078 N N   . LYS A 440 ? 0.4950 0.3254 0.3107 0.0080  -0.0046 0.0234  440 LYS A N   
2079 C CA  . LYS A 440 ? 0.5104 0.3096 0.3135 -0.0098 -0.0047 0.0201  440 LYS A CA  
2080 C C   . LYS A 440 ? 0.5220 0.3028 0.3144 -0.0023 -0.0066 0.0113  440 LYS A C   
2081 O O   . LYS A 440 ? 0.5340 0.3091 0.3172 0.0199  -0.0066 0.0103  440 LYS A O   
2082 C CB  . LYS A 440 ? 0.5447 0.3018 0.3213 -0.0155 -0.0026 0.0281  440 LYS A CB  
2083 C CG  . LYS A 440 ? 0.5821 0.3587 0.3688 -0.0254 -0.0002 0.0367  440 LYS A CG  
2084 C CD  . LYS A 440 ? 0.6561 0.3913 0.4142 -0.0269 0.0026  0.0468  440 LYS A CD  
2085 C CE  . LYS A 440 ? 0.6990 0.4471 0.4649 -0.0466 0.0058  0.0537  440 LYS A CE  
2086 N NZ  . LYS A 440 ? 0.7558 0.4894 0.5041 -0.0372 0.0085  0.0654  440 LYS A NZ  
2087 N N   . GLY A 441 ? 0.5136 0.2891 0.3080 -0.0202 -0.0083 0.0047  441 GLY A N   
2088 C CA  . GLY A 441 ? 0.5304 0.2890 0.3139 -0.0155 -0.0104 -0.0046 441 GLY A CA  
2089 C C   . GLY A 441 ? 0.5212 0.2936 0.3171 -0.0357 -0.0131 -0.0120 441 GLY A C   
2090 O O   . GLY A 441 ? 0.5455 0.2886 0.3237 -0.0427 -0.0154 -0.0187 441 GLY A O   
2091 N N   . HIS A 442 ? 0.4938 0.3099 0.3185 -0.0445 -0.0132 -0.0110 442 HIS A N   
2092 C CA  . HIS A 442 ? 0.4829 0.3171 0.3209 -0.0622 -0.0161 -0.0169 442 HIS A CA  
2093 C C   . HIS A 442 ? 0.4941 0.3046 0.3205 -0.0857 -0.0171 -0.0163 442 HIS A C   
2094 O O   . HIS A 442 ? 0.4951 0.2949 0.3166 -0.0921 -0.0144 -0.0085 442 HIS A O   
2095 C CB  . HIS A 442 ? 0.4603 0.3438 0.3294 -0.0648 -0.0153 -0.0148 442 HIS A CB  
2096 C CG  . HIS A 442 ? 0.4706 0.3792 0.3524 -0.0483 -0.0151 -0.0177 442 HIS A CG  
2097 N ND1 . HIS A 442 ? 0.4975 0.4079 0.3777 -0.0453 -0.0175 -0.0252 442 HIS A ND1 
2098 C CD2 . HIS A 442 ? 0.4642 0.3972 0.3596 -0.0360 -0.0127 -0.0139 442 HIS A CD2 
2099 C CE1 . HIS A 442 ? 0.4854 0.4208 0.3785 -0.0316 -0.0158 -0.0250 442 HIS A CE1 
2100 N NE2 . HIS A 442 ? 0.4747 0.4241 0.3773 -0.0263 -0.0132 -0.0185 442 HIS A NE2 
2101 N N   . THR A 443 ? 0.4990 0.3024 0.3207 -0.0991 -0.0211 -0.0243 443 THR A N   
2102 C CA  . THR A 443 ? 0.5168 0.3009 0.3286 -0.1247 -0.0227 -0.0246 443 THR A CA  
2103 C C   . THR A 443 ? 0.4826 0.3107 0.3215 -0.1441 -0.0241 -0.0243 443 THR A C   
2104 O O   . THR A 443 ? 0.4848 0.3061 0.3201 -0.1671 -0.0252 -0.0238 443 THR A O   
2105 C CB  . THR A 443 ? 0.5650 0.3076 0.3495 -0.1295 -0.0265 -0.0337 443 THR A CB  
2106 O OG1 . THR A 443 ? 0.5757 0.3421 0.3706 -0.1245 -0.0305 -0.0425 443 THR A OG1 
2107 C CG2 . THR A 443 ? 0.5968 0.2915 0.3511 -0.1103 -0.0243 -0.0331 443 THR A CG2 
2108 N N   . SER A 444 ? 0.4481 0.3207 0.3131 -0.1346 -0.0238 -0.0240 444 SER A N   
2109 C CA  . SER A 444 ? 0.4214 0.3384 0.3124 -0.1469 -0.0245 -0.0229 444 SER A CA  
2110 C C   . SER A 444 ? 0.3933 0.3434 0.3051 -0.1315 -0.0206 -0.0176 444 SER A C   
2111 O O   . SER A 444 ? 0.3881 0.3301 0.2956 -0.1129 -0.0187 -0.0163 444 SER A O   
2112 C CB  . SER A 444 ? 0.4337 0.3675 0.3307 -0.1532 -0.0303 -0.0317 444 SER A CB  
2113 O OG  . SER A 444 ? 0.4737 0.3809 0.3531 -0.1726 -0.0343 -0.0367 444 SER A OG  
2114 N N   . ARG A 445 ? 0.3689 0.3566 0.3024 -0.1390 -0.0195 -0.0147 445 ARG A N   
2115 C CA  . ARG A 445 ? 0.3532 0.3683 0.3035 -0.1269 -0.0156 -0.0100 445 ARG A CA  
2116 C C   . ARG A 445 ? 0.3464 0.3685 0.3010 -0.1076 -0.0160 -0.0130 445 ARG A C   
2117 O O   . ARG A 445 ? 0.3421 0.3668 0.2965 -0.1044 -0.0194 -0.0190 445 ARG A O   
2118 C CB  . ARG A 445 ? 0.3513 0.4060 0.3229 -0.1361 -0.0145 -0.0079 445 ARG A CB  
2119 C CG  . ARG A 445 ? 0.3827 0.4633 0.3668 -0.1359 -0.0186 -0.0136 445 ARG A CG  
2120 C CD  . ARG A 445 ? 0.4104 0.5307 0.4144 -0.1425 -0.0171 -0.0108 445 ARG A CD  
2121 N NE  . ARG A 445 ? 0.4393 0.5845 0.4537 -0.1408 -0.0215 -0.0157 445 ARG A NE  
2122 C CZ  . ARG A 445 ? 0.4547 0.6376 0.4866 -0.1410 -0.0211 -0.0143 445 ARG A CZ  
2123 N NH1 . ARG A 445 ? 0.4400 0.6433 0.4787 -0.1376 -0.0256 -0.0183 445 ARG A NH1 
2124 N NH2 . ARG A 445 ? 0.4552 0.6564 0.4968 -0.1433 -0.0159 -0.0086 445 ARG A NH2 
2125 N N   . VAL A 446 ? 0.3329 0.3575 0.2900 -0.0954 -0.0124 -0.0086 446 VAL A N   
2126 C CA  . VAL A 446 ? 0.3289 0.3642 0.2921 -0.0793 -0.0121 -0.0106 446 VAL A CA  
2127 C C   . VAL A 446 ? 0.3171 0.3858 0.2995 -0.0802 -0.0117 -0.0113 446 VAL A C   
2128 O O   . VAL A 446 ? 0.3071 0.3929 0.2991 -0.0873 -0.0098 -0.0081 446 VAL A O   
2129 C CB  . VAL A 446 ? 0.3328 0.3634 0.2930 -0.0681 -0.0091 -0.0059 446 VAL A CB  
2130 C CG1 . VAL A 446 ? 0.3173 0.3632 0.2858 -0.0545 -0.0085 -0.0078 446 VAL A CG1 
2131 C CG2 . VAL A 446 ? 0.3563 0.3528 0.2954 -0.0647 -0.0094 -0.0044 446 VAL A CG2 
2132 N N   . LEU A 447 ? 0.3141 0.3911 0.3003 -0.0726 -0.0133 -0.0153 447 LEU A N   
2133 C CA  . LEU A 447 ? 0.3126 0.4164 0.3134 -0.0711 -0.0130 -0.0158 447 LEU A CA  
2134 C C   . LEU A 447 ? 0.3095 0.4219 0.3164 -0.0596 -0.0097 -0.0140 447 LEU A C   
2135 O O   . LEU A 447 ? 0.3116 0.4408 0.3283 -0.0590 -0.0075 -0.0120 447 LEU A O   
2136 C CB  . LEU A 447 ? 0.3159 0.4220 0.3146 -0.0710 -0.0170 -0.0208 447 LEU A CB  
2137 C CG  . LEU A 447 ? 0.3361 0.4369 0.3295 -0.0846 -0.0211 -0.0237 447 LEU A CG  
2138 C CD1 . LEU A 447 ? 0.3554 0.4528 0.3418 -0.0827 -0.0256 -0.0297 447 LEU A CD1 
2139 C CD2 . LEU A 447 ? 0.3284 0.4552 0.3354 -0.0941 -0.0212 -0.0214 447 LEU A CD2 
2140 N N   . SER A 448 ? 0.3062 0.4076 0.3067 -0.0507 -0.0093 -0.0150 448 SER A N   
2141 C CA  . SER A 448 ? 0.3091 0.4196 0.3153 -0.0424 -0.0065 -0.0137 448 SER A CA  
2142 C C   . SER A 448 ? 0.2902 0.3908 0.2898 -0.0350 -0.0058 -0.0131 448 SER A C   
2143 O O   . SER A 448 ? 0.2984 0.3837 0.2876 -0.0322 -0.0073 -0.0147 448 SER A O   
2144 C CB  . SER A 448 ? 0.3563 0.4768 0.3669 -0.0382 -0.0064 -0.0157 448 SER A CB  
2145 O OG  . SER A 448 ? 0.4261 0.5597 0.4439 -0.0420 -0.0067 -0.0153 448 SER A OG  
2146 N N   . LEU A 449 ? 0.2641 0.3741 0.2691 -0.0312 -0.0037 -0.0113 449 LEU A N   
2147 C CA  . LEU A 449 ? 0.2554 0.3644 0.2572 -0.0233 -0.0032 -0.0106 449 LEU A CA  
2148 C C   . LEU A 449 ? 0.2339 0.3574 0.2434 -0.0204 -0.0014 -0.0116 449 LEU A C   
2149 O O   . LEU A 449 ? 0.2370 0.3692 0.2533 -0.0244 0.0000  -0.0115 449 LEU A O   
2150 C CB  . LEU A 449 ? 0.2571 0.3676 0.2584 -0.0232 -0.0027 -0.0073 449 LEU A CB  
2151 C CG  . LEU A 449 ? 0.2863 0.3819 0.2788 -0.0267 -0.0035 -0.0045 449 LEU A CG  
2152 C CD1 . LEU A 449 ? 0.2894 0.3883 0.2799 -0.0238 -0.0030 -0.0009 449 LEU A CD1 
2153 C CD2 . LEU A 449 ? 0.3041 0.3789 0.2837 -0.0229 -0.0051 -0.0053 449 LEU A CD2 
2154 N N   . THR A 450 ? 0.2106 0.3367 0.2181 -0.0132 -0.0009 -0.0121 450 THR A N   
2155 C CA  . THR A 450 ? 0.1931 0.3345 0.2078 -0.0121 0.0013  -0.0123 450 THR A CA  
2156 C C   . THR A 450 ? 0.1831 0.3335 0.1977 -0.0047 0.0016  -0.0114 450 THR A C   
2157 O O   . THR A 450 ? 0.1797 0.3217 0.1864 0.0031  0.0005  -0.0113 450 THR A O   
2158 C CB  . THR A 450 ? 0.2055 0.3475 0.2204 -0.0123 0.0027  -0.0137 450 THR A CB  
2159 O OG1 . THR A 450 ? 0.2220 0.3769 0.2432 -0.0141 0.0056  -0.0129 450 THR A OG1 
2160 C CG2 . THR A 450 ? 0.2094 0.3442 0.2159 -0.0053 0.0021  -0.0155 450 THR A CG2 
2161 N N   . MET A 451 ? 0.1757 0.3430 0.1983 -0.0071 0.0028  -0.0108 451 MET A N   
2162 C CA  . MET A 451 ? 0.1788 0.3618 0.2039 -0.0009 0.0026  -0.0098 451 MET A CA  
2163 C C   . MET A 451 ? 0.1881 0.3865 0.2177 0.0018  0.0055  -0.0101 451 MET A C   
2164 O O   . MET A 451 ? 0.1898 0.3911 0.2234 -0.0053 0.0079  -0.0106 451 MET A O   
2165 C CB  . MET A 451 ? 0.1771 0.3720 0.2078 -0.0068 0.0013  -0.0093 451 MET A CB  
2166 C CG  . MET A 451 ? 0.2175 0.4325 0.2513 -0.0002 -0.0001 -0.0081 451 MET A CG  
2167 S SD  . MET A 451 ? 0.3042 0.5297 0.3404 -0.0061 -0.0033 -0.0080 451 MET A SD  
2168 C CE  . MET A 451 ? 0.2870 0.4904 0.3113 0.0003  -0.0054 -0.0053 451 MET A CE  
2169 N N   . SER A 452 ? 0.1961 0.4052 0.2245 0.0129  0.0056  -0.0094 452 SER A N   
2170 C CA  . SER A 452 ? 0.1990 0.4290 0.2330 0.0162  0.0091  -0.0091 452 SER A CA  
2171 C C   . SER A 452 ? 0.2120 0.4663 0.2585 0.0053  0.0100  -0.0084 452 SER A C   
2172 O O   . SER A 452 ? 0.2165 0.4739 0.2659 -0.0003 0.0071  -0.0085 452 SER A O   
2173 C CB  . SER A 452 ? 0.2020 0.4404 0.2316 0.0327  0.0089  -0.0084 452 SER A CB  
2174 O OG  . SER A 452 ? 0.2194 0.4732 0.2533 0.0358  0.0060  -0.0066 452 SER A OG  
2175 N N   . PRO A 453 ? 0.2210 0.4924 0.2737 0.0013  0.0142  -0.0077 453 PRO A N   
2176 C CA  . PRO A 453 ? 0.2187 0.5113 0.2820 -0.0121 0.0152  -0.0072 453 PRO A CA  
2177 C C   . PRO A 453 ? 0.2113 0.5309 0.2824 -0.0096 0.0120  -0.0070 453 PRO A C   
2178 O O   . PRO A 453 ? 0.2201 0.5483 0.2964 -0.0218 0.0100  -0.0081 453 PRO A O   
2179 C CB  . PRO A 453 ? 0.2207 0.5266 0.2876 -0.0153 0.0212  -0.0055 453 PRO A CB  
2180 C CG  . PRO A 453 ? 0.2281 0.5262 0.2871 -0.0004 0.0229  -0.0054 453 PRO A CG  
2181 C CD  . PRO A 453 ? 0.2159 0.4874 0.2648 0.0079  0.0184  -0.0073 453 PRO A CD  
2182 N N   . ASP A 454 ? 0.1963 0.5279 0.2663 0.0068  0.0111  -0.0058 454 ASP A N   
2183 C CA  . ASP A 454 ? 0.1836 0.5436 0.2605 0.0118  0.0075  -0.0049 454 ASP A CA  
2184 C C   . ASP A 454 ? 0.1752 0.5193 0.2451 0.0145  0.0018  -0.0052 454 ASP A C   
2185 O O   . ASP A 454 ? 0.1587 0.5252 0.2332 0.0167  -0.0021 -0.0045 454 ASP A O   
2186 C CB  . ASP A 454 ? 0.2036 0.5866 0.2819 0.0302  0.0093  -0.0029 454 ASP A CB  
2187 C CG  . ASP A 454 ? 0.2917 0.6474 0.3546 0.0492  0.0090  -0.0027 454 ASP A CG  
2188 O OD1 . ASP A 454 ? 0.3120 0.6314 0.3641 0.0461  0.0077  -0.0040 454 ASP A OD1 
2189 O OD2 . ASP A 454 ? 0.3260 0.6968 0.3869 0.0673  0.0103  -0.0014 454 ASP A OD2 
2190 N N   . GLY A 455 ? 0.1827 0.4910 0.2417 0.0135  0.0014  -0.0059 455 GLY A N   
2191 C CA  . GLY A 455 ? 0.1866 0.4785 0.2381 0.0147  -0.0028 -0.0055 455 GLY A CA  
2192 C C   . GLY A 455 ? 0.1964 0.4775 0.2369 0.0324  -0.0047 -0.0028 455 GLY A C   
2193 O O   . GLY A 455 ? 0.2165 0.4807 0.2485 0.0336  -0.0075 -0.0014 455 GLY A O   
2194 N N   . ALA A 456 ? 0.1878 0.4758 0.2261 0.0468  -0.0028 -0.0018 456 ALA A N   
2195 C CA  . ALA A 456 ? 0.1986 0.4730 0.2233 0.0658  -0.0043 0.0008  456 ALA A CA  
2196 C C   . ALA A 456 ? 0.2146 0.4462 0.2228 0.0679  -0.0036 0.0003  456 ALA A C   
2197 O O   . ALA A 456 ? 0.2341 0.4445 0.2282 0.0773  -0.0055 0.0028  456 ALA A O   
2198 C CB  . ALA A 456 ? 0.1894 0.4866 0.2161 0.0823  -0.0020 0.0015  456 ALA A CB  
2199 N N   . THR A 457 ? 0.2105 0.4299 0.2194 0.0595  -0.0008 -0.0028 457 THR A N   
2200 C CA  . THR A 457 ? 0.2297 0.4130 0.2240 0.0604  -0.0005 -0.0043 457 THR A CA  
2201 C C   . THR A 457 ? 0.2295 0.3979 0.2261 0.0435  -0.0008 -0.0058 457 THR A C   
2202 O O   . THR A 457 ? 0.2313 0.4138 0.2395 0.0326  0.0005  -0.0071 457 THR A O   
2203 C CB  . THR A 457 ? 0.2564 0.4387 0.2463 0.0693  0.0028  -0.0070 457 THR A CB  
2204 O OG1 . THR A 457 ? 0.2730 0.4741 0.2620 0.0869  0.0039  -0.0054 457 THR A OG1 
2205 C CG2 . THR A 457 ? 0.2757 0.4207 0.2480 0.0712  0.0025  -0.0097 457 THR A CG2 
2206 N N   . VAL A 458 ? 0.2282 0.3675 0.2126 0.0417  -0.0023 -0.0055 458 VAL A N   
2207 C CA  . VAL A 458 ? 0.2222 0.3488 0.2081 0.0273  -0.0027 -0.0067 458 VAL A CA  
2208 C C   . VAL A 458 ? 0.2307 0.3339 0.2056 0.0275  -0.0026 -0.0097 458 VAL A C   
2209 O O   . VAL A 458 ? 0.2497 0.3306 0.2093 0.0349  -0.0035 -0.0095 458 VAL A O   
2210 C CB  . VAL A 458 ? 0.2354 0.3517 0.2174 0.0223  -0.0044 -0.0035 458 VAL A CB  
2211 C CG1 . VAL A 458 ? 0.2471 0.3507 0.2295 0.0089  -0.0044 -0.0046 458 VAL A CG1 
2212 C CG2 . VAL A 458 ? 0.2268 0.3666 0.2185 0.0210  -0.0052 -0.0016 458 VAL A CG2 
2213 N N   . ALA A 459 ? 0.2164 0.3222 0.1967 0.0193  -0.0018 -0.0125 459 ALA A N   
2214 C CA  . ALA A 459 ? 0.2340 0.3201 0.2043 0.0172  -0.0028 -0.0160 459 ALA A CA  
2215 C C   . ALA A 459 ? 0.2439 0.3201 0.2149 0.0041  -0.0047 -0.0154 459 ALA A C   
2216 O O   . ALA A 459 ? 0.2384 0.3289 0.2213 -0.0037 -0.0041 -0.0142 459 ALA A O   
2217 C CB  . ALA A 459 ? 0.2423 0.3403 0.2178 0.0166  -0.0011 -0.0187 459 ALA A CB  
2218 N N   . SER A 460 ? 0.2571 0.3089 0.2148 0.0016  -0.0066 -0.0164 460 SER A N   
2219 C CA  . SER A 460 ? 0.2631 0.3080 0.2216 -0.0121 -0.0081 -0.0160 460 SER A CA  
2220 C C   . SER A 460 ? 0.2672 0.3017 0.2191 -0.0176 -0.0104 -0.0210 460 SER A C   
2221 O O   . SER A 460 ? 0.2927 0.3055 0.2288 -0.0132 -0.0116 -0.0242 460 SER A O   
2222 C CB  . SER A 460 ? 0.2870 0.3115 0.2342 -0.0144 -0.0086 -0.0124 460 SER A CB  
2223 O OG  . SER A 460 ? 0.3225 0.3208 0.2508 -0.0057 -0.0092 -0.0139 460 SER A OG  
2224 N N   . ALA A 461 ? 0.2560 0.3051 0.2185 -0.0264 -0.0113 -0.0221 461 ALA A N   
2225 C CA  . ALA A 461 ? 0.2690 0.3130 0.2265 -0.0333 -0.0145 -0.0268 461 ALA A CA  
2226 C C   . ALA A 461 ? 0.2737 0.3106 0.2301 -0.0475 -0.0165 -0.0259 461 ALA A C   
2227 O O   . ALA A 461 ? 0.2676 0.3180 0.2350 -0.0526 -0.0149 -0.0217 461 ALA A O   
2228 C CB  . ALA A 461 ? 0.2584 0.3259 0.2285 -0.0334 -0.0144 -0.0275 461 ALA A CB  
2229 N N   . ALA A 462 ? 0.2914 0.3071 0.2336 -0.0545 -0.0197 -0.0299 462 ALA A N   
2230 C CA  . ALA A 462 ? 0.3042 0.3126 0.2443 -0.0707 -0.0214 -0.0288 462 ALA A CA  
2231 C C   . ALA A 462 ? 0.3188 0.3265 0.2548 -0.0828 -0.0264 -0.0349 462 ALA A C   
2232 O O   . ALA A 462 ? 0.3323 0.3355 0.2608 -0.0773 -0.0289 -0.0406 462 ALA A O   
2233 C CB  . ALA A 462 ? 0.3192 0.2953 0.2419 -0.0707 -0.0201 -0.0262 462 ALA A CB  
2234 N N   . ALA A 463 ? 0.3223 0.3375 0.2637 -0.0996 -0.0279 -0.0336 463 ALA A N   
2235 C CA  . ALA A 463 ? 0.3426 0.3621 0.2822 -0.1144 -0.0334 -0.0391 463 ALA A CA  
2236 C C   . ALA A 463 ? 0.3774 0.3582 0.2916 -0.1202 -0.0369 -0.0456 463 ALA A C   
2237 O O   . ALA A 463 ? 0.3915 0.3732 0.3012 -0.1331 -0.0424 -0.0517 463 ALA A O   
2238 C CB  . ALA A 463 ? 0.3311 0.3703 0.2833 -0.1315 -0.0332 -0.0351 463 ALA A CB  
2239 N N   . ASP A 464 ? 0.3907 0.3375 0.2872 -0.1103 -0.0340 -0.0447 464 ASP A N   
2240 C CA  . ASP A 464 ? 0.4144 0.3193 0.2831 -0.1111 -0.0365 -0.0513 464 ASP A CA  
2241 C C   . ASP A 464 ? 0.4151 0.3184 0.2762 -0.0949 -0.0379 -0.0581 464 ASP A C   
2242 O O   . ASP A 464 ? 0.4397 0.3074 0.2760 -0.0889 -0.0387 -0.0635 464 ASP A O   
2243 C CB  . ASP A 464 ? 0.4582 0.3272 0.3096 -0.1045 -0.0324 -0.0465 464 ASP A CB  
2244 C CG  . ASP A 464 ? 0.5139 0.3917 0.3716 -0.0818 -0.0276 -0.0414 464 ASP A CG  
2245 O OD1 . ASP A 464 ? 0.5058 0.4105 0.3770 -0.0705 -0.0273 -0.0428 464 ASP A OD1 
2246 O OD2 . ASP A 464 ? 0.5610 0.4180 0.4085 -0.0756 -0.0244 -0.0359 464 ASP A OD2 
2247 N N   . GLU A 465 ? 0.3848 0.3246 0.2652 -0.0867 -0.0376 -0.0572 465 GLU A N   
2248 C CA  . GLU A 465 ? 0.3788 0.3239 0.2548 -0.0728 -0.0382 -0.0622 465 GLU A CA  
2249 C C   . GLU A 465 ? 0.3802 0.3084 0.2453 -0.0527 -0.0335 -0.0613 465 GLU A C   
2250 O O   . GLU A 465 ? 0.3841 0.3002 0.2342 -0.0425 -0.0339 -0.0673 465 GLU A O   
2251 C CB  . GLU A 465 ? 0.4074 0.3403 0.2675 -0.0820 -0.0446 -0.0720 465 GLU A CB  
2252 C CG  . GLU A 465 ? 0.4573 0.4173 0.3321 -0.1007 -0.0497 -0.0725 465 GLU A CG  
2253 C CD  . GLU A 465 ? 0.5593 0.5116 0.4192 -0.1114 -0.0573 -0.0826 465 GLU A CD  
2254 O OE1 . GLU A 465 ? 0.5732 0.5538 0.4418 -0.1088 -0.0606 -0.0847 465 GLU A OE1 
2255 O OE2 . GLU A 465 ? 0.6593 0.5756 0.4971 -0.1219 -0.0600 -0.0885 465 GLU A OE2 
2256 N N   . THR A 466 ? 0.3705 0.3021 0.2440 -0.0461 -0.0288 -0.0538 466 THR A N   
2257 C CA  . THR A 466 ? 0.3757 0.3011 0.2435 -0.0261 -0.0243 -0.0518 466 THR A CA  
2258 C C   . THR A 466 ? 0.3693 0.3269 0.2602 -0.0199 -0.0204 -0.0444 466 THR A C   
2259 O O   . THR A 466 ? 0.3519 0.3255 0.2582 -0.0302 -0.0204 -0.0398 466 THR A O   
2260 C CB  . THR A 466 ? 0.3988 0.2870 0.2461 -0.0216 -0.0231 -0.0505 466 THR A CB  
2261 O OG1 . THR A 466 ? 0.4002 0.2923 0.2572 -0.0295 -0.0217 -0.0429 466 THR A OG1 
2262 C CG2 . THR A 466 ? 0.4116 0.2598 0.2317 -0.0290 -0.0267 -0.0581 466 THR A CG2 
2263 N N   . LEU A 467 ? 0.3754 0.3422 0.2677 -0.0034 -0.0168 -0.0435 467 LEU A N   
2264 C CA  . LEU A 467 ? 0.3778 0.3697 0.2876 0.0029  -0.0131 -0.0371 467 LEU A CA  
2265 C C   . LEU A 467 ? 0.3806 0.3579 0.2792 0.0168  -0.0109 -0.0350 467 LEU A C   
2266 O O   . LEU A 467 ? 0.3920 0.3619 0.2789 0.0306  -0.0094 -0.0382 467 LEU A O   
2267 C CB  . LEU A 467 ? 0.3885 0.4078 0.3104 0.0092  -0.0106 -0.0371 467 LEU A CB  
2268 C CG  . LEU A 467 ? 0.4234 0.4670 0.3646 -0.0008 -0.0107 -0.0340 467 LEU A CG  
2269 C CD1 . LEU A 467 ? 0.4408 0.4831 0.3800 -0.0110 -0.0146 -0.0378 467 LEU A CD1 
2270 C CD2 . LEU A 467 ? 0.4281 0.4957 0.3808 0.0059  -0.0068 -0.0315 467 LEU A CD2 
2271 N N   . ARG A 468 ? 0.3710 0.3446 0.2720 0.0146  -0.0105 -0.0296 468 ARG A N   
2272 C CA  . ARG A 468 ? 0.3803 0.3418 0.2705 0.0294  -0.0087 -0.0264 468 ARG A CA  
2273 C C   . ARG A 468 ? 0.3594 0.3550 0.2680 0.0373  -0.0062 -0.0220 468 ARG A C   
2274 O O   . ARG A 468 ? 0.3518 0.3678 0.2773 0.0275  -0.0062 -0.0189 468 ARG A O   
2275 C CB  . ARG A 468 ? 0.4147 0.3490 0.2927 0.0229  -0.0099 -0.0226 468 ARG A CB  
2276 C CG  . ARG A 468 ? 0.4931 0.3861 0.3463 0.0180  -0.0120 -0.0274 468 ARG A CG  
2277 C CD  . ARG A 468 ? 0.5506 0.4161 0.3917 0.0077  -0.0126 -0.0229 468 ARG A CD  
2278 N NE  . ARG A 468 ? 0.6262 0.4481 0.4406 0.0022  -0.0145 -0.0279 468 ARG A NE  
2279 C CZ  . ARG A 468 ? 0.6893 0.4704 0.4770 0.0109  -0.0136 -0.0262 468 ARG A CZ  
2280 N NH1 . ARG A 468 ? 0.7190 0.4575 0.4808 0.0037  -0.0154 -0.0317 468 ARG A NH1 
2281 N NH2 . ARG A 468 ? 0.6808 0.4625 0.4658 0.0273  -0.0110 -0.0191 468 ARG A NH2 
2282 N N   . LEU A 469 ? 0.3509 0.3536 0.2558 0.0548  -0.0041 -0.0219 469 LEU A N   
2283 C CA  . LEU A 469 ? 0.3285 0.3666 0.2508 0.0614  -0.0019 -0.0182 469 LEU A CA  
2284 C C   . LEU A 469 ? 0.3303 0.3653 0.2466 0.0731  -0.0022 -0.0133 469 LEU A C   
2285 O O   . LEU A 469 ? 0.3448 0.3675 0.2462 0.0900  -0.0013 -0.0137 469 LEU A O   
2286 C CB  . LEU A 469 ? 0.3201 0.3765 0.2452 0.0723  0.0011  -0.0210 469 LEU A CB  
2287 C CG  . LEU A 469 ? 0.3261 0.4031 0.2658 0.0614  0.0023  -0.0229 469 LEU A CG  
2288 C CD1 . LEU A 469 ? 0.3431 0.4006 0.2773 0.0480  -0.0004 -0.0265 469 LEU A CD1 
2289 C CD2 . LEU A 469 ? 0.3247 0.4163 0.2633 0.0727  0.0060  -0.0250 469 LEU A CD2 
2290 N N   . TRP A 470 ? 0.3186 0.3639 0.2444 0.0656  -0.0034 -0.0087 470 TRP A N   
2291 C CA  . TRP A 470 ? 0.3204 0.3627 0.2393 0.0759  -0.0043 -0.0034 470 TRP A CA  
2292 C C   . TRP A 470 ? 0.3221 0.4044 0.2572 0.0838  -0.0039 -0.0010 470 TRP A C   
2293 O O   . TRP A 470 ? 0.3076 0.4140 0.2603 0.0717  -0.0042 -0.0007 470 TRP A O   
2294 C CB  . TRP A 470 ? 0.3194 0.3504 0.2380 0.0620  -0.0059 0.0003  470 TRP A CB  
2295 C CG  . TRP A 470 ? 0.3365 0.3376 0.2454 0.0481  -0.0064 -0.0018 470 TRP A CG  
2296 C CD1 . TRP A 470 ? 0.3391 0.3469 0.2590 0.0323  -0.0066 -0.0054 470 TRP A CD1 
2297 C CD2 . TRP A 470 ? 0.3597 0.3207 0.2457 0.0478  -0.0069 -0.0002 470 TRP A CD2 
2298 N NE1 . TRP A 470 ? 0.3576 0.3365 0.2650 0.0216  -0.0076 -0.0064 470 TRP A NE1 
2299 C CE2 . TRP A 470 ? 0.3743 0.3226 0.2604 0.0293  -0.0076 -0.0033 470 TRP A CE2 
2300 C CE3 . TRP A 470 ? 0.3803 0.3140 0.2444 0.0613  -0.0068 0.0040  470 TRP A CE3 
2301 C CZ2 . TRP A 470 ? 0.3987 0.3091 0.2649 0.0213  -0.0083 -0.0028 470 TRP A CZ2 
2302 C CZ3 . TRP A 470 ? 0.4141 0.3049 0.2559 0.0546  -0.0070 0.0048  470 TRP A CZ3 
2303 C CH2 . TRP A 470 ? 0.4185 0.2985 0.2620 0.0333  -0.0077 0.0013  470 TRP A CH2 
2304 N N   . ARG A 471 ? 0.3340 0.4238 0.2628 0.1038  -0.0033 0.0006  471 ARG A N   
2305 C CA  . ARG A 471 ? 0.3364 0.4680 0.2808 0.1109  -0.0035 0.0031  471 ARG A CA  
2306 C C   . ARG A 471 ? 0.3582 0.4876 0.2984 0.1125  -0.0067 0.0088  471 ARG A C   
2307 O O   . ARG A 471 ? 0.3757 0.5054 0.3056 0.1308  -0.0078 0.0128  471 ARG A O   
2308 C CB  . ARG A 471 ? 0.3555 0.4993 0.2949 0.1332  -0.0014 0.0028  471 ARG A CB  
2309 C CG  . ARG A 471 ? 0.3839 0.5767 0.3406 0.1412  -0.0017 0.0054  471 ARG A CG  
2310 C CD  . ARG A 471 ? 0.4353 0.6476 0.3924 0.1588  0.0021  0.0037  471 ARG A CD  
2311 N NE  . ARG A 471 ? 0.4701 0.7055 0.4444 0.1448  0.0053  0.0001  471 ARG A NE  
2312 C CZ  . ARG A 471 ? 0.4811 0.7622 0.4776 0.1375  0.0060  0.0010  471 ARG A CZ  
2313 N NH1 . ARG A 471 ? 0.4802 0.7931 0.4857 0.1436  0.0032  0.0046  471 ARG A NH1 
2314 N NH2 . ARG A 471 ? 0.4672 0.7623 0.4758 0.1238  0.0095  -0.0015 471 ARG A NH2 
2315 N N   . CYS A 472 ? 0.3595 0.4843 0.3052 0.0945  -0.0081 0.0094  472 CYS A N   
2316 C CA  . CYS A 472 ? 0.3735 0.4937 0.3136 0.0938  -0.0106 0.0147  472 CYS A CA  
2317 C C   . CYS A 472 ? 0.3728 0.5332 0.3292 0.0916  -0.0131 0.0159  472 CYS A C   
2318 O O   . CYS A 472 ? 0.3799 0.5399 0.3307 0.0929  -0.0155 0.0202  472 CYS A O   
2319 C CB  . CYS A 472 ? 0.3811 0.4742 0.3160 0.0767  -0.0102 0.0148  472 CYS A CB  
2320 S SG  . CYS A 472 ? 0.3650 0.4755 0.3208 0.0548  -0.0091 0.0094  472 CYS A SG  
2321 N N   . PHE A 473 ? 0.3637 0.5572 0.3390 0.0863  -0.0124 0.0119  473 PHE A N   
2322 C CA  . PHE A 473 ? 0.3615 0.5935 0.3518 0.0823  -0.0150 0.0120  473 PHE A CA  
2323 C C   . PHE A 473 ? 0.3850 0.6523 0.3851 0.0945  -0.0147 0.0116  473 PHE A C   
2324 O O   . PHE A 473 ? 0.3826 0.6806 0.4000 0.0842  -0.0142 0.0086  473 PHE A O   
2325 C CB  . PHE A 473 ? 0.3362 0.5763 0.3399 0.0606  -0.0144 0.0079  473 PHE A CB  
2326 C CG  . PHE A 473 ? 0.3368 0.5487 0.3333 0.0491  -0.0141 0.0081  473 PHE A CG  
2327 C CD1 . PHE A 473 ? 0.3438 0.5488 0.3314 0.0501  -0.0165 0.0118  473 PHE A CD1 
2328 C CD2 . PHE A 473 ? 0.3384 0.5343 0.3375 0.0373  -0.0112 0.0049  473 PHE A CD2 
2329 C CE1 . PHE A 473 ? 0.3571 0.5401 0.3390 0.0391  -0.0154 0.0123  473 PHE A CE1 
2330 C CE2 . PHE A 473 ? 0.3540 0.5295 0.3481 0.0272  -0.0106 0.0052  473 PHE A CE2 
2331 C CZ  . PHE A 473 ? 0.3518 0.5218 0.3379 0.0278  -0.0124 0.0089  473 PHE A CZ  
2332 N N   . GLU A 474 ? 0.4058 0.6680 0.3937 0.1166  -0.0147 0.0149  474 GLU A N   
2333 C CA  . GLU A 474 ? 0.4167 0.7142 0.4117 0.1335  -0.0142 0.0157  474 GLU A CA  
2334 C C   . GLU A 474 ? 0.4503 0.7294 0.4249 0.1606  -0.0142 0.0200  474 GLU A C   
2335 O O   . GLU A 474 ? 0.4848 0.7184 0.4384 0.1642  -0.0140 0.0219  474 GLU A O   
2336 C CB  . GLU A 474 ? 0.4398 0.7528 0.4471 0.1285  -0.0095 0.0113  474 GLU A CB  
2337 C CG  . GLU A 474 ? 0.4876 0.8464 0.5187 0.1133  -0.0098 0.0093  474 GLU A CG  
2338 C CD  . GLU A 474 ? 0.5604 0.9702 0.6041 0.1256  -0.0107 0.0112  474 GLU A CD  
2339 O OE1 . GLU A 474 ? 0.5699 0.9841 0.6041 0.1479  -0.0129 0.0151  474 GLU A OE1 
2340 O OE2 . GLU A 474 ? 0.5773 1.0231 0.6398 0.1128  -0.0091 0.0091  474 GLU A OE2 
# 
