data_9MS1
# 
_entry.id   9MS1 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9MS1         pdb_00009ms1 10.2210/pdb9ms1/pdb 
WWPDB D_1000291661 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-04-16 ? 
2 'Structure model' 1 1 2025-04-23 ? 
# 
_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_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Database references' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' citation        
2 2 'Structure model' citation_author 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 2 'Structure model' '_citation.journal_volume'          
2 2 'Structure model' '_citation.page_first'              
3 2 'Structure model' '_citation.page_last'               
4 2 'Structure model' '_citation.pdbx_database_id_PubMed' 
5 2 'Structure model' '_citation.title'                   
6 2 'Structure model' '_citation_author.name'             
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9MS1 
_pdbx_database_status.recvd_initial_deposition_date   2025-01-09 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_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           N 
# 
_pdbx_database_related.db_name        PDB 
_pdbx_database_related.details        Isoform 
_pdbx_database_related.db_id          9MS2 
_pdbx_database_related.content_type   unspecified 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              taosheng.chen@stjude.org 
_pdbx_contact_author.name_first         Taosheng 
_pdbx_contact_author.name_last          Chen 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-6420-3809 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Jingheng, W.'      1 0000-0001-5747-6673 
'Nithianantham, S.' 2 0000-0001-6238-647X 
'Miller, D.J.'      3 0000-0003-1202-511X 
'Chen, T.'          4 0000-0001-6420-3809 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Nat Commun' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2041-1723 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            16 
_citation.language                  ? 
_citation.page_first                3423 
_citation.page_last                 3423 
_citation.title                     'Decoding the selective chemical modulation of CYP3A4.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1038/s41467-025-58749-8 
_citation.pdbx_database_id_PubMed   40210880 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Wang, J.'          1  ? 
primary 'Nithianantham, S.' 2  ? 
primary 'Chai, S.C.'        3  ? 
primary 'Jung, Y.H.'        4  ? 
primary 'Yang, L.'          5  ? 
primary 'Ong, H.W.'         6  ? 
primary 'Li, Y.'            7  ? 
primary 'Zhang, Y.'         8  ? 
primary 'Miller, D.J.'      9  ? 
primary 'Chen, T.'          10 ? 
# 
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 'Cytochrome P450 3A4'                                                                                         
55594.637 1 1.14.14.1,1.14.14.56,1.14.14.73,1.14.14.55 ? ? 
;First residues (M) - Initiating methionine Second residue (A) - Expression Tag Last 4 residues (HHHH) - Expression Tag Missing residues (DGTVGA)
;
2 non-polymer syn 'PROTOPORPHYRIN IX CONTAINING FE'                                                                             
616.487   1 ?                                          ? ? ? 
3 non-polymer syn "N'-(2-chlorophenyl)-N-[(3-hydroxyphenyl)methyl]-N-[(2P)-2-(1H-imidazol-1-yl)-5-(trifluoromethyl)phenyl]urea" 
486.874   1 ?                                          ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        
;1,4-cineole 2-exo-monooxygenase,8-cineole 2-exo-monooxygenase,Albendazole monooxygenase (sulfoxide-forming),Albendazole sulfoxidase,CYPIIIA3,CYPIIIA4,Cholesterol 25-hydroxylase,Cytochrome P450 3A3,Cytochrome P450 HLp,Cytochrome P450 NF-25,Cytochrome P450-PCN1,Nifedipine oxidase,Quinine 3-monooxygenase
;
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;MALYGTHSHGLFKKLGIPGPTPLPFLGNILSYHKGFCMFDMECHKKYGKVWGFYDGQQPVLAITDPDMIKTVLVKECYSV
FTNRRPFGPVGFMKSAISIAEDEEWKRLRSLLSPTFTSGKLKEMVPIIAQYGDVLVRNLRREAETGKPVTLKDVFGAYSM
DVITSTSFGVNIDSLNNPQDPFVENTKKLLRFDFLDPFFLSITVFPFLIPILEVLNICVFPREVTNFLRKSVKRMKESRL
EDTQKHRVDFLQLMIDSQNSKETESHKALSDLELVAQSIIFIFAGYETTSSVLSFIMYELATHPDVQQKLQEEIDAVLPN
KAPPTYDTVLQMEYLDMVVNETLRLFPIAMRLERVCKKDVEINGMFIPKGVVVMIPSYALHRDPKYWTEPEKFLPERFSK
KNKDNIDPYIYTPFGSGPRNCIGMRFALMNMKLALIRVLQNFSFKPCKETQIPLKLSLGGLLQPEKPVVLKVESRDGTVS
GAHHHH
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MALYGTHSHGLFKKLGIPGPTPLPFLGNILSYHKGFCMFDMECHKKYGKVWGFYDGQQPVLAITDPDMIKTVLVKECYSV
FTNRRPFGPVGFMKSAISIAEDEEWKRLRSLLSPTFTSGKLKEMVPIIAQYGDVLVRNLRREAETGKPVTLKDVFGAYSM
DVITSTSFGVNIDSLNNPQDPFVENTKKLLRFDFLDPFFLSITVFPFLIPILEVLNICVFPREVTNFLRKSVKRMKESRL
EDTQKHRVDFLQLMIDSQNSKETESHKALSDLELVAQSIIFIFAGYETTSSVLSFIMYELATHPDVQQKLQEEIDAVLPN
KAPPTYDTVLQMEYLDMVVNETLRLFPIAMRLERVCKKDVEINGMFIPKGVVVMIPSYALHRDPKYWTEPEKFLPERFSK
KNKDNIDPYIYTPFGSGPRNCIGMRFALMNMKLALIRVLQNFSFKPCKETQIPLKLSLGGLLQPEKPVVLKVESRDGTVS
GAHHHH
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'PROTOPORPHYRIN IX CONTAINING FE'                                                                             HEM   
3 "N'-(2-chlorophenyl)-N-[(3-hydroxyphenyl)methyl]-N-[(2P)-2-(1H-imidazol-1-yl)-5-(trifluoromethyl)phenyl]urea" A1BNX 
# 
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   LEU n 
1 4   TYR n 
1 5   GLY n 
1 6   THR n 
1 7   HIS n 
1 8   SER n 
1 9   HIS n 
1 10  GLY n 
1 11  LEU n 
1 12  PHE n 
1 13  LYS n 
1 14  LYS n 
1 15  LEU n 
1 16  GLY n 
1 17  ILE n 
1 18  PRO n 
1 19  GLY n 
1 20  PRO n 
1 21  THR n 
1 22  PRO n 
1 23  LEU n 
1 24  PRO n 
1 25  PHE n 
1 26  LEU n 
1 27  GLY n 
1 28  ASN n 
1 29  ILE n 
1 30  LEU n 
1 31  SER n 
1 32  TYR n 
1 33  HIS n 
1 34  LYS n 
1 35  GLY n 
1 36  PHE n 
1 37  CYS n 
1 38  MET n 
1 39  PHE n 
1 40  ASP n 
1 41  MET n 
1 42  GLU n 
1 43  CYS n 
1 44  HIS n 
1 45  LYS n 
1 46  LYS n 
1 47  TYR n 
1 48  GLY n 
1 49  LYS n 
1 50  VAL n 
1 51  TRP n 
1 52  GLY n 
1 53  PHE n 
1 54  TYR n 
1 55  ASP n 
1 56  GLY n 
1 57  GLN n 
1 58  GLN n 
1 59  PRO n 
1 60  VAL n 
1 61  LEU n 
1 62  ALA n 
1 63  ILE n 
1 64  THR n 
1 65  ASP n 
1 66  PRO n 
1 67  ASP n 
1 68  MET n 
1 69  ILE n 
1 70  LYS n 
1 71  THR n 
1 72  VAL n 
1 73  LEU n 
1 74  VAL n 
1 75  LYS n 
1 76  GLU n 
1 77  CYS n 
1 78  TYR n 
1 79  SER n 
1 80  VAL n 
1 81  PHE n 
1 82  THR n 
1 83  ASN n 
1 84  ARG n 
1 85  ARG n 
1 86  PRO n 
1 87  PHE n 
1 88  GLY n 
1 89  PRO n 
1 90  VAL n 
1 91  GLY n 
1 92  PHE n 
1 93  MET n 
1 94  LYS n 
1 95  SER n 
1 96  ALA n 
1 97  ILE n 
1 98  SER n 
1 99  ILE n 
1 100 ALA n 
1 101 GLU n 
1 102 ASP n 
1 103 GLU n 
1 104 GLU n 
1 105 TRP n 
1 106 LYS n 
1 107 ARG n 
1 108 LEU n 
1 109 ARG n 
1 110 SER n 
1 111 LEU n 
1 112 LEU n 
1 113 SER n 
1 114 PRO n 
1 115 THR n 
1 116 PHE n 
1 117 THR n 
1 118 SER n 
1 119 GLY n 
1 120 LYS n 
1 121 LEU n 
1 122 LYS n 
1 123 GLU n 
1 124 MET n 
1 125 VAL n 
1 126 PRO n 
1 127 ILE n 
1 128 ILE n 
1 129 ALA n 
1 130 GLN n 
1 131 TYR n 
1 132 GLY n 
1 133 ASP n 
1 134 VAL n 
1 135 LEU n 
1 136 VAL n 
1 137 ARG n 
1 138 ASN n 
1 139 LEU n 
1 140 ARG n 
1 141 ARG n 
1 142 GLU n 
1 143 ALA n 
1 144 GLU n 
1 145 THR n 
1 146 GLY n 
1 147 LYS n 
1 148 PRO n 
1 149 VAL n 
1 150 THR n 
1 151 LEU n 
1 152 LYS n 
1 153 ASP n 
1 154 VAL n 
1 155 PHE n 
1 156 GLY n 
1 157 ALA n 
1 158 TYR n 
1 159 SER n 
1 160 MET n 
1 161 ASP n 
1 162 VAL n 
1 163 ILE n 
1 164 THR n 
1 165 SER n 
1 166 THR n 
1 167 SER n 
1 168 PHE n 
1 169 GLY n 
1 170 VAL n 
1 171 ASN n 
1 172 ILE n 
1 173 ASP n 
1 174 SER n 
1 175 LEU n 
1 176 ASN n 
1 177 ASN n 
1 178 PRO n 
1 179 GLN n 
1 180 ASP n 
1 181 PRO n 
1 182 PHE n 
1 183 VAL n 
1 184 GLU n 
1 185 ASN n 
1 186 THR n 
1 187 LYS n 
1 188 LYS n 
1 189 LEU n 
1 190 LEU n 
1 191 ARG n 
1 192 PHE n 
1 193 ASP n 
1 194 PHE n 
1 195 LEU n 
1 196 ASP n 
1 197 PRO n 
1 198 PHE n 
1 199 PHE n 
1 200 LEU n 
1 201 SER n 
1 202 ILE n 
1 203 THR n 
1 204 VAL n 
1 205 PHE n 
1 206 PRO n 
1 207 PHE n 
1 208 LEU n 
1 209 ILE n 
1 210 PRO n 
1 211 ILE n 
1 212 LEU n 
1 213 GLU n 
1 214 VAL n 
1 215 LEU n 
1 216 ASN n 
1 217 ILE n 
1 218 CYS n 
1 219 VAL n 
1 220 PHE n 
1 221 PRO n 
1 222 ARG n 
1 223 GLU n 
1 224 VAL n 
1 225 THR n 
1 226 ASN n 
1 227 PHE n 
1 228 LEU n 
1 229 ARG n 
1 230 LYS n 
1 231 SER n 
1 232 VAL n 
1 233 LYS n 
1 234 ARG n 
1 235 MET n 
1 236 LYS n 
1 237 GLU n 
1 238 SER n 
1 239 ARG n 
1 240 LEU n 
1 241 GLU n 
1 242 ASP n 
1 243 THR n 
1 244 GLN n 
1 245 LYS n 
1 246 HIS n 
1 247 ARG n 
1 248 VAL n 
1 249 ASP n 
1 250 PHE n 
1 251 LEU n 
1 252 GLN n 
1 253 LEU n 
1 254 MET n 
1 255 ILE n 
1 256 ASP n 
1 257 SER n 
1 258 GLN n 
1 259 ASN n 
1 260 SER n 
1 261 LYS n 
1 262 GLU n 
1 263 THR n 
1 264 GLU n 
1 265 SER n 
1 266 HIS n 
1 267 LYS n 
1 268 ALA n 
1 269 LEU n 
1 270 SER n 
1 271 ASP n 
1 272 LEU n 
1 273 GLU n 
1 274 LEU n 
1 275 VAL n 
1 276 ALA n 
1 277 GLN n 
1 278 SER n 
1 279 ILE n 
1 280 ILE n 
1 281 PHE n 
1 282 ILE n 
1 283 PHE n 
1 284 ALA n 
1 285 GLY n 
1 286 TYR n 
1 287 GLU n 
1 288 THR n 
1 289 THR n 
1 290 SER n 
1 291 SER n 
1 292 VAL n 
1 293 LEU n 
1 294 SER n 
1 295 PHE n 
1 296 ILE n 
1 297 MET n 
1 298 TYR n 
1 299 GLU n 
1 300 LEU n 
1 301 ALA n 
1 302 THR n 
1 303 HIS n 
1 304 PRO n 
1 305 ASP n 
1 306 VAL n 
1 307 GLN n 
1 308 GLN n 
1 309 LYS n 
1 310 LEU n 
1 311 GLN n 
1 312 GLU n 
1 313 GLU n 
1 314 ILE n 
1 315 ASP n 
1 316 ALA n 
1 317 VAL n 
1 318 LEU n 
1 319 PRO n 
1 320 ASN n 
1 321 LYS n 
1 322 ALA n 
1 323 PRO n 
1 324 PRO n 
1 325 THR n 
1 326 TYR n 
1 327 ASP n 
1 328 THR n 
1 329 VAL n 
1 330 LEU n 
1 331 GLN n 
1 332 MET n 
1 333 GLU n 
1 334 TYR n 
1 335 LEU n 
1 336 ASP n 
1 337 MET n 
1 338 VAL n 
1 339 VAL n 
1 340 ASN n 
1 341 GLU n 
1 342 THR n 
1 343 LEU n 
1 344 ARG n 
1 345 LEU n 
1 346 PHE n 
1 347 PRO n 
1 348 ILE n 
1 349 ALA n 
1 350 MET n 
1 351 ARG n 
1 352 LEU n 
1 353 GLU n 
1 354 ARG n 
1 355 VAL n 
1 356 CYS n 
1 357 LYS n 
1 358 LYS n 
1 359 ASP n 
1 360 VAL n 
1 361 GLU n 
1 362 ILE n 
1 363 ASN n 
1 364 GLY n 
1 365 MET n 
1 366 PHE n 
1 367 ILE n 
1 368 PRO n 
1 369 LYS n 
1 370 GLY n 
1 371 VAL n 
1 372 VAL n 
1 373 VAL n 
1 374 MET n 
1 375 ILE n 
1 376 PRO n 
1 377 SER n 
1 378 TYR n 
1 379 ALA n 
1 380 LEU n 
1 381 HIS n 
1 382 ARG n 
1 383 ASP n 
1 384 PRO n 
1 385 LYS n 
1 386 TYR n 
1 387 TRP n 
1 388 THR n 
1 389 GLU n 
1 390 PRO n 
1 391 GLU n 
1 392 LYS n 
1 393 PHE n 
1 394 LEU n 
1 395 PRO n 
1 396 GLU n 
1 397 ARG n 
1 398 PHE n 
1 399 SER n 
1 400 LYS n 
1 401 LYS n 
1 402 ASN n 
1 403 LYS n 
1 404 ASP n 
1 405 ASN n 
1 406 ILE n 
1 407 ASP n 
1 408 PRO n 
1 409 TYR n 
1 410 ILE n 
1 411 TYR n 
1 412 THR n 
1 413 PRO n 
1 414 PHE n 
1 415 GLY n 
1 416 SER n 
1 417 GLY n 
1 418 PRO n 
1 419 ARG n 
1 420 ASN n 
1 421 CYS n 
1 422 ILE n 
1 423 GLY n 
1 424 MET n 
1 425 ARG n 
1 426 PHE n 
1 427 ALA n 
1 428 LEU n 
1 429 MET n 
1 430 ASN n 
1 431 MET n 
1 432 LYS n 
1 433 LEU n 
1 434 ALA n 
1 435 LEU n 
1 436 ILE n 
1 437 ARG n 
1 438 VAL n 
1 439 LEU n 
1 440 GLN n 
1 441 ASN n 
1 442 PHE n 
1 443 SER n 
1 444 PHE n 
1 445 LYS n 
1 446 PRO n 
1 447 CYS n 
1 448 LYS n 
1 449 GLU n 
1 450 THR n 
1 451 GLN n 
1 452 ILE n 
1 453 PRO n 
1 454 LEU n 
1 455 LYS n 
1 456 LEU n 
1 457 SER n 
1 458 LEU n 
1 459 GLY n 
1 460 GLY n 
1 461 LEU n 
1 462 LEU n 
1 463 GLN n 
1 464 PRO n 
1 465 GLU n 
1 466 LYS n 
1 467 PRO n 
1 468 VAL n 
1 469 VAL n 
1 470 LEU n 
1 471 LYS n 
1 472 VAL n 
1 473 GLU n 
1 474 SER n 
1 475 ARG n 
1 476 ASP n 
1 477 GLY n 
1 478 THR n 
1 479 VAL n 
1 480 SER n 
1 481 GLY n 
1 482 ALA n 
1 483 HIS n 
1 484 HIS n 
1 485 HIS n 
1 486 HIS n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   486 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'CYP3A4, CYP3A3' 
_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      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               DH5alpha 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          PLASMID 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       pCWori 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
A1BNX non-polymer         . 
"N'-(2-chlorophenyl)-N-[(3-hydroxyphenyl)methyl]-N-[(2P)-2-(1H-imidazol-1-yl)-5-(trifluoromethyl)phenyl]urea" ?    
'C24 H18 Cl F3 N4 O2' 486.874 
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  
HEM   non-polymer         . 'PROTOPORPHYRIN IX CONTAINING FE' HEME 'C34 H32 Fe N4 O4'    616.487 
HIS   'L-peptide linking' y HISTIDINE ?    'C6 H10 N3 O2 1'      156.162 
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   22  ?   ?   ?   A . n 
A 1 2   ALA 2   23  ?   ?   ?   A . n 
A 1 3   LEU 3   24  ?   ?   ?   A . n 
A 1 4   TYR 4   25  ?   ?   ?   A . n 
A 1 5   GLY 5   26  ?   ?   ?   A . n 
A 1 6   THR 6   27  ?   ?   ?   A . n 
A 1 7   HIS 7   28  28  HIS HIS A . n 
A 1 8   SER 8   29  29  SER SER A . n 
A 1 9   HIS 9   30  30  HIS HIS A . n 
A 1 10  GLY 10  31  31  GLY GLY A . n 
A 1 11  LEU 11  32  32  LEU LEU A . n 
A 1 12  PHE 12  33  33  PHE PHE A . n 
A 1 13  LYS 13  34  34  LYS LYS A . n 
A 1 14  LYS 14  35  35  LYS LYS A . n 
A 1 15  LEU 15  36  36  LEU LEU A . n 
A 1 16  GLY 16  37  37  GLY GLY A . n 
A 1 17  ILE 17  38  38  ILE ILE A . n 
A 1 18  PRO 18  39  39  PRO PRO A . n 
A 1 19  GLY 19  40  40  GLY GLY A . n 
A 1 20  PRO 20  41  41  PRO PRO A . n 
A 1 21  THR 21  42  42  THR THR A . n 
A 1 22  PRO 22  43  43  PRO PRO A . n 
A 1 23  LEU 23  44  44  LEU LEU A . n 
A 1 24  PRO 24  45  45  PRO PRO A . n 
A 1 25  PHE 25  46  46  PHE PHE A . n 
A 1 26  LEU 26  47  47  LEU LEU A . n 
A 1 27  GLY 27  48  48  GLY GLY A . n 
A 1 28  ASN 28  49  49  ASN ASN A . n 
A 1 29  ILE 29  50  50  ILE ILE A . n 
A 1 30  LEU 30  51  51  LEU LEU A . n 
A 1 31  SER 31  52  52  SER SER A . n 
A 1 32  TYR 32  53  53  TYR TYR A . n 
A 1 33  HIS 33  54  54  HIS HIS A . n 
A 1 34  LYS 34  55  55  LYS LYS A . n 
A 1 35  GLY 35  56  56  GLY GLY A . n 
A 1 36  PHE 36  57  57  PHE PHE A . n 
A 1 37  CYS 37  58  58  CYS CYS A . n 
A 1 38  MET 38  59  59  MET MET A . n 
A 1 39  PHE 39  60  60  PHE PHE A . n 
A 1 40  ASP 40  61  61  ASP ASP A . n 
A 1 41  MET 41  62  62  MET MET A . n 
A 1 42  GLU 42  63  63  GLU GLU A . n 
A 1 43  CYS 43  64  64  CYS CYS A . n 
A 1 44  HIS 44  65  65  HIS HIS A . n 
A 1 45  LYS 45  66  66  LYS LYS A . n 
A 1 46  LYS 46  67  67  LYS LYS A . n 
A 1 47  TYR 47  68  68  TYR TYR A . n 
A 1 48  GLY 48  69  69  GLY GLY A . n 
A 1 49  LYS 49  70  70  LYS LYS A . n 
A 1 50  VAL 50  71  71  VAL VAL A . n 
A 1 51  TRP 51  72  72  TRP TRP A . n 
A 1 52  GLY 52  73  73  GLY GLY A . n 
A 1 53  PHE 53  74  74  PHE PHE A . n 
A 1 54  TYR 54  75  75  TYR TYR A . n 
A 1 55  ASP 55  76  76  ASP ASP A . n 
A 1 56  GLY 56  77  77  GLY GLY A . n 
A 1 57  GLN 57  78  78  GLN GLN A . n 
A 1 58  GLN 58  79  79  GLN GLN A . n 
A 1 59  PRO 59  80  80  PRO PRO A . n 
A 1 60  VAL 60  81  81  VAL VAL A . n 
A 1 61  LEU 61  82  82  LEU LEU A . n 
A 1 62  ALA 62  83  83  ALA ALA A . n 
A 1 63  ILE 63  84  84  ILE ILE A . n 
A 1 64  THR 64  85  85  THR THR A . n 
A 1 65  ASP 65  86  86  ASP ASP A . n 
A 1 66  PRO 66  87  87  PRO PRO A . n 
A 1 67  ASP 67  88  88  ASP ASP A . n 
A 1 68  MET 68  89  89  MET MET A . n 
A 1 69  ILE 69  90  90  ILE ILE A . n 
A 1 70  LYS 70  91  91  LYS LYS A . n 
A 1 71  THR 71  92  92  THR THR A . n 
A 1 72  VAL 72  93  93  VAL VAL A . n 
A 1 73  LEU 73  94  94  LEU LEU A . n 
A 1 74  VAL 74  95  95  VAL VAL A . n 
A 1 75  LYS 75  96  96  LYS LYS A . n 
A 1 76  GLU 76  97  97  GLU GLU A . n 
A 1 77  CYS 77  98  98  CYS CYS A . n 
A 1 78  TYR 78  99  99  TYR TYR A . n 
A 1 79  SER 79  100 100 SER SER A . n 
A 1 80  VAL 80  101 101 VAL VAL A . n 
A 1 81  PHE 81  102 102 PHE PHE A . n 
A 1 82  THR 82  103 103 THR THR A . n 
A 1 83  ASN 83  104 104 ASN ASN A . n 
A 1 84  ARG 84  105 105 ARG ARG A . n 
A 1 85  ARG 85  106 106 ARG ARG A . n 
A 1 86  PRO 86  107 107 PRO PRO A . n 
A 1 87  PHE 87  108 108 PHE PHE A . n 
A 1 88  GLY 88  109 109 GLY GLY A . n 
A 1 89  PRO 89  110 110 PRO PRO A . n 
A 1 90  VAL 90  111 111 VAL VAL A . n 
A 1 91  GLY 91  112 112 GLY GLY A . n 
A 1 92  PHE 92  113 113 PHE PHE A . n 
A 1 93  MET 93  114 114 MET MET A . n 
A 1 94  LYS 94  115 115 LYS LYS A . n 
A 1 95  SER 95  116 116 SER SER A . n 
A 1 96  ALA 96  117 117 ALA ALA A . n 
A 1 97  ILE 97  118 118 ILE ILE A . n 
A 1 98  SER 98  119 119 SER SER A . n 
A 1 99  ILE 99  120 120 ILE ILE A . n 
A 1 100 ALA 100 121 121 ALA ALA A . n 
A 1 101 GLU 101 122 122 GLU GLU A . n 
A 1 102 ASP 102 123 123 ASP ASP A . n 
A 1 103 GLU 103 124 124 GLU GLU A . n 
A 1 104 GLU 104 125 125 GLU GLU A . n 
A 1 105 TRP 105 126 126 TRP TRP A . n 
A 1 106 LYS 106 127 127 LYS LYS A . n 
A 1 107 ARG 107 128 128 ARG ARG A . n 
A 1 108 LEU 108 129 129 LEU LEU A . n 
A 1 109 ARG 109 130 130 ARG ARG A . n 
A 1 110 SER 110 131 131 SER SER A . n 
A 1 111 LEU 111 132 132 LEU LEU A . n 
A 1 112 LEU 112 133 133 LEU LEU A . n 
A 1 113 SER 113 134 134 SER SER A . n 
A 1 114 PRO 114 135 135 PRO PRO A . n 
A 1 115 THR 115 136 136 THR THR A . n 
A 1 116 PHE 116 137 137 PHE PHE A . n 
A 1 117 THR 117 138 138 THR THR A . n 
A 1 118 SER 118 139 139 SER SER A . n 
A 1 119 GLY 119 140 140 GLY GLY A . n 
A 1 120 LYS 120 141 141 LYS LYS A . n 
A 1 121 LEU 121 142 142 LEU LEU A . n 
A 1 122 LYS 122 143 143 LYS LYS A . n 
A 1 123 GLU 123 144 144 GLU GLU A . n 
A 1 124 MET 124 145 145 MET MET A . n 
A 1 125 VAL 125 146 146 VAL VAL A . n 
A 1 126 PRO 126 147 147 PRO PRO A . n 
A 1 127 ILE 127 148 148 ILE ILE A . n 
A 1 128 ILE 128 149 149 ILE ILE A . n 
A 1 129 ALA 129 150 150 ALA ALA A . n 
A 1 130 GLN 130 151 151 GLN GLN A . n 
A 1 131 TYR 131 152 152 TYR TYR A . n 
A 1 132 GLY 132 153 153 GLY GLY A . n 
A 1 133 ASP 133 154 154 ASP ASP A . n 
A 1 134 VAL 134 155 155 VAL VAL A . n 
A 1 135 LEU 135 156 156 LEU LEU A . n 
A 1 136 VAL 136 157 157 VAL VAL A . n 
A 1 137 ARG 137 158 158 ARG ARG A . n 
A 1 138 ASN 138 159 159 ASN ASN A . n 
A 1 139 LEU 139 160 160 LEU LEU A . n 
A 1 140 ARG 140 161 161 ARG ARG A . n 
A 1 141 ARG 141 162 162 ARG ARG A . n 
A 1 142 GLU 142 163 163 GLU GLU A . n 
A 1 143 ALA 143 164 164 ALA ALA A . n 
A 1 144 GLU 144 165 165 GLU GLU A . n 
A 1 145 THR 145 166 166 THR THR A . n 
A 1 146 GLY 146 167 167 GLY GLY A . n 
A 1 147 LYS 147 168 168 LYS LYS A . n 
A 1 148 PRO 148 169 169 PRO PRO A . n 
A 1 149 VAL 149 170 170 VAL VAL A . n 
A 1 150 THR 150 171 171 THR THR A . n 
A 1 151 LEU 151 172 172 LEU LEU A . n 
A 1 152 LYS 152 173 173 LYS LYS A . n 
A 1 153 ASP 153 174 174 ASP ASP A . n 
A 1 154 VAL 154 175 175 VAL VAL A . n 
A 1 155 PHE 155 176 176 PHE PHE A . n 
A 1 156 GLY 156 177 177 GLY GLY A . n 
A 1 157 ALA 157 178 178 ALA ALA A . n 
A 1 158 TYR 158 179 179 TYR TYR A . n 
A 1 159 SER 159 180 180 SER SER A . n 
A 1 160 MET 160 181 181 MET MET A . n 
A 1 161 ASP 161 182 182 ASP ASP A . n 
A 1 162 VAL 162 183 183 VAL VAL A . n 
A 1 163 ILE 163 184 184 ILE ILE A . n 
A 1 164 THR 164 185 185 THR THR A . n 
A 1 165 SER 165 186 186 SER SER A . n 
A 1 166 THR 166 187 187 THR THR A . n 
A 1 167 SER 167 188 188 SER SER A . n 
A 1 168 PHE 168 189 189 PHE PHE A . n 
A 1 169 GLY 169 190 190 GLY GLY A . n 
A 1 170 VAL 170 191 191 VAL VAL A . n 
A 1 171 ASN 171 192 192 ASN ASN A . n 
A 1 172 ILE 172 193 193 ILE ILE A . n 
A 1 173 ASP 173 194 194 ASP ASP A . n 
A 1 174 SER 174 195 195 SER SER A . n 
A 1 175 LEU 175 196 196 LEU LEU A . n 
A 1 176 ASN 176 197 197 ASN ASN A . n 
A 1 177 ASN 177 198 198 ASN ASN A . n 
A 1 178 PRO 178 199 199 PRO PRO A . n 
A 1 179 GLN 179 200 200 GLN GLN A . n 
A 1 180 ASP 180 201 201 ASP ASP A . n 
A 1 181 PRO 181 202 202 PRO PRO A . n 
A 1 182 PHE 182 203 203 PHE PHE A . n 
A 1 183 VAL 183 204 204 VAL VAL A . n 
A 1 184 GLU 184 205 205 GLU GLU A . n 
A 1 185 ASN 185 206 206 ASN ASN A . n 
A 1 186 THR 186 207 207 THR THR A . n 
A 1 187 LYS 187 208 208 LYS LYS A . n 
A 1 188 LYS 188 209 209 LYS LYS A . n 
A 1 189 LEU 189 210 210 LEU LEU A . n 
A 1 190 LEU 190 211 ?   ?   ?   A . n 
A 1 191 ARG 191 212 ?   ?   ?   A . n 
A 1 192 PHE 192 213 ?   ?   ?   A . n 
A 1 193 ASP 193 214 ?   ?   ?   A . n 
A 1 194 PHE 194 215 ?   ?   ?   A . n 
A 1 195 LEU 195 216 216 LEU LEU A . n 
A 1 196 ASP 196 217 217 ASP ASP A . n 
A 1 197 PRO 197 218 218 PRO PRO A . n 
A 1 198 PHE 198 219 219 PHE PHE A . n 
A 1 199 PHE 199 220 220 PHE PHE A . n 
A 1 200 LEU 200 221 221 LEU LEU A . n 
A 1 201 SER 201 222 222 SER SER A . n 
A 1 202 ILE 202 223 223 ILE ILE A . n 
A 1 203 THR 203 224 224 THR THR A . n 
A 1 204 VAL 204 225 225 VAL VAL A . n 
A 1 205 PHE 205 226 226 PHE PHE A . n 
A 1 206 PRO 206 227 227 PRO PRO A . n 
A 1 207 PHE 207 228 228 PHE PHE A . n 
A 1 208 LEU 208 229 229 LEU LEU A . n 
A 1 209 ILE 209 230 230 ILE ILE A . n 
A 1 210 PRO 210 231 231 PRO PRO A . n 
A 1 211 ILE 211 232 232 ILE ILE A . n 
A 1 212 LEU 212 233 233 LEU LEU A . n 
A 1 213 GLU 213 234 234 GLU GLU A . n 
A 1 214 VAL 214 235 235 VAL VAL A . n 
A 1 215 LEU 215 236 236 LEU LEU A . n 
A 1 216 ASN 216 237 237 ASN ASN A . n 
A 1 217 ILE 217 238 238 ILE ILE A . n 
A 1 218 CYS 218 239 239 CYS CYS A . n 
A 1 219 VAL 219 240 240 VAL VAL A . n 
A 1 220 PHE 220 241 241 PHE PHE A . n 
A 1 221 PRO 221 242 242 PRO PRO A . n 
A 1 222 ARG 222 243 243 ARG ARG A . n 
A 1 223 GLU 223 244 244 GLU GLU A . n 
A 1 224 VAL 224 245 245 VAL VAL A . n 
A 1 225 THR 225 246 246 THR THR A . n 
A 1 226 ASN 226 247 247 ASN ASN A . n 
A 1 227 PHE 227 248 248 PHE PHE A . n 
A 1 228 LEU 228 249 249 LEU LEU A . n 
A 1 229 ARG 229 250 250 ARG ARG A . n 
A 1 230 LYS 230 251 251 LYS LYS A . n 
A 1 231 SER 231 252 252 SER SER A . n 
A 1 232 VAL 232 253 253 VAL VAL A . n 
A 1 233 LYS 233 254 254 LYS LYS A . n 
A 1 234 ARG 234 255 255 ARG ARG A . n 
A 1 235 MET 235 256 256 MET MET A . n 
A 1 236 LYS 236 257 257 LYS LYS A . n 
A 1 237 GLU 237 258 258 GLU GLU A . n 
A 1 238 SER 238 259 259 SER SER A . n 
A 1 239 ARG 239 260 260 ARG ARG A . n 
A 1 240 LEU 240 261 261 LEU LEU A . n 
A 1 241 GLU 241 262 ?   ?   ?   A . n 
A 1 242 ASP 242 263 ?   ?   ?   A . n 
A 1 243 THR 243 264 ?   ?   ?   A . n 
A 1 244 GLN 244 265 ?   ?   ?   A . n 
A 1 245 LYS 245 266 266 LYS LYS A . n 
A 1 246 HIS 246 267 267 HIS HIS A . n 
A 1 247 ARG 247 268 268 ARG ARG A . n 
A 1 248 VAL 248 269 269 VAL VAL A . n 
A 1 249 ASP 249 270 270 ASP ASP A . n 
A 1 250 PHE 250 271 271 PHE PHE A . n 
A 1 251 LEU 251 272 272 LEU LEU A . n 
A 1 252 GLN 252 273 273 GLN GLN A . n 
A 1 253 LEU 253 274 274 LEU LEU A . n 
A 1 254 MET 254 275 275 MET MET A . n 
A 1 255 ILE 255 276 276 ILE ILE A . n 
A 1 256 ASP 256 277 277 ASP ASP A . n 
A 1 257 SER 257 278 278 SER SER A . n 
A 1 258 GLN 258 279 279 GLN GLN A . n 
A 1 259 ASN 259 280 280 ASN ASN A . n 
A 1 260 SER 260 281 ?   ?   ?   A . n 
A 1 261 LYS 261 282 ?   ?   ?   A . n 
A 1 262 GLU 262 283 ?   ?   ?   A . n 
A 1 263 THR 263 284 ?   ?   ?   A . n 
A 1 264 GLU 264 285 ?   ?   ?   A . n 
A 1 265 SER 265 286 ?   ?   ?   A . n 
A 1 266 HIS 266 287 287 HIS HIS A . n 
A 1 267 LYS 267 288 288 LYS LYS A . n 
A 1 268 ALA 268 289 289 ALA ALA A . n 
A 1 269 LEU 269 290 290 LEU LEU A . n 
A 1 270 SER 270 291 291 SER SER A . n 
A 1 271 ASP 271 292 292 ASP ASP A . n 
A 1 272 LEU 272 293 293 LEU LEU A . n 
A 1 273 GLU 273 294 294 GLU GLU A . n 
A 1 274 LEU 274 295 295 LEU LEU A . n 
A 1 275 VAL 275 296 296 VAL VAL A . n 
A 1 276 ALA 276 297 297 ALA ALA A . n 
A 1 277 GLN 277 298 298 GLN GLN A . n 
A 1 278 SER 278 299 299 SER SER A . n 
A 1 279 ILE 279 300 300 ILE ILE A . n 
A 1 280 ILE 280 301 301 ILE ILE A . n 
A 1 281 PHE 281 302 302 PHE PHE A . n 
A 1 282 ILE 282 303 303 ILE ILE A . n 
A 1 283 PHE 283 304 304 PHE PHE A . n 
A 1 284 ALA 284 305 305 ALA ALA A . n 
A 1 285 GLY 285 306 306 GLY GLY A . n 
A 1 286 TYR 286 307 307 TYR TYR A . n 
A 1 287 GLU 287 308 308 GLU GLU A . n 
A 1 288 THR 288 309 309 THR THR A . n 
A 1 289 THR 289 310 310 THR THR A . n 
A 1 290 SER 290 311 311 SER SER A . n 
A 1 291 SER 291 312 312 SER SER A . n 
A 1 292 VAL 292 313 313 VAL VAL A . n 
A 1 293 LEU 293 314 314 LEU LEU A . n 
A 1 294 SER 294 315 315 SER SER A . n 
A 1 295 PHE 295 316 316 PHE PHE A . n 
A 1 296 ILE 296 317 317 ILE ILE A . n 
A 1 297 MET 297 318 318 MET MET A . n 
A 1 298 TYR 298 319 319 TYR TYR A . n 
A 1 299 GLU 299 320 320 GLU GLU A . n 
A 1 300 LEU 300 321 321 LEU LEU A . n 
A 1 301 ALA 301 322 322 ALA ALA A . n 
A 1 302 THR 302 323 323 THR THR A . n 
A 1 303 HIS 303 324 324 HIS HIS A . n 
A 1 304 PRO 304 325 325 PRO PRO A . n 
A 1 305 ASP 305 326 326 ASP ASP A . n 
A 1 306 VAL 306 327 327 VAL VAL A . n 
A 1 307 GLN 307 328 328 GLN GLN A . n 
A 1 308 GLN 308 329 329 GLN GLN A . n 
A 1 309 LYS 309 330 330 LYS LYS A . n 
A 1 310 LEU 310 331 331 LEU LEU A . n 
A 1 311 GLN 311 332 332 GLN GLN A . n 
A 1 312 GLU 312 333 333 GLU GLU A . n 
A 1 313 GLU 313 334 334 GLU GLU A . n 
A 1 314 ILE 314 335 335 ILE ILE A . n 
A 1 315 ASP 315 336 336 ASP ASP A . n 
A 1 316 ALA 316 337 337 ALA ALA A . n 
A 1 317 VAL 317 338 338 VAL VAL A . n 
A 1 318 LEU 318 339 339 LEU LEU A . n 
A 1 319 PRO 319 340 340 PRO PRO A . n 
A 1 320 ASN 320 341 341 ASN ASN A . n 
A 1 321 LYS 321 342 342 LYS LYS A . n 
A 1 322 ALA 322 343 343 ALA ALA A . n 
A 1 323 PRO 323 344 344 PRO PRO A . n 
A 1 324 PRO 324 345 345 PRO PRO A . n 
A 1 325 THR 325 346 346 THR THR A . n 
A 1 326 TYR 326 347 347 TYR TYR A . n 
A 1 327 ASP 327 348 348 ASP ASP A . n 
A 1 328 THR 328 349 349 THR THR A . n 
A 1 329 VAL 329 350 350 VAL VAL A . n 
A 1 330 LEU 330 351 351 LEU LEU A . n 
A 1 331 GLN 331 352 352 GLN GLN A . n 
A 1 332 MET 332 353 353 MET MET A . n 
A 1 333 GLU 333 354 354 GLU GLU A . n 
A 1 334 TYR 334 355 355 TYR TYR A . n 
A 1 335 LEU 335 356 356 LEU LEU A . n 
A 1 336 ASP 336 357 357 ASP ASP A . n 
A 1 337 MET 337 358 358 MET MET A . n 
A 1 338 VAL 338 359 359 VAL VAL A . n 
A 1 339 VAL 339 360 360 VAL VAL A . n 
A 1 340 ASN 340 361 361 ASN ASN A . n 
A 1 341 GLU 341 362 362 GLU GLU A . n 
A 1 342 THR 342 363 363 THR THR A . n 
A 1 343 LEU 343 364 364 LEU LEU A . n 
A 1 344 ARG 344 365 365 ARG ARG A . n 
A 1 345 LEU 345 366 366 LEU LEU A . n 
A 1 346 PHE 346 367 367 PHE PHE A . n 
A 1 347 PRO 347 368 368 PRO PRO A . n 
A 1 348 ILE 348 369 369 ILE ILE A . n 
A 1 349 ALA 349 370 370 ALA ALA A . n 
A 1 350 MET 350 371 371 MET MET A . n 
A 1 351 ARG 351 372 372 ARG ARG A . n 
A 1 352 LEU 352 373 373 LEU LEU A . n 
A 1 353 GLU 353 374 374 GLU GLU A . n 
A 1 354 ARG 354 375 375 ARG ARG A . n 
A 1 355 VAL 355 376 376 VAL VAL A . n 
A 1 356 CYS 356 377 377 CYS CYS A . n 
A 1 357 LYS 357 378 378 LYS LYS A . n 
A 1 358 LYS 358 379 379 LYS LYS A . n 
A 1 359 ASP 359 380 380 ASP ASP A . n 
A 1 360 VAL 360 381 381 VAL VAL A . n 
A 1 361 GLU 361 382 382 GLU GLU A . n 
A 1 362 ILE 362 383 383 ILE ILE A . n 
A 1 363 ASN 363 384 384 ASN ASN A . n 
A 1 364 GLY 364 385 385 GLY GLY A . n 
A 1 365 MET 365 386 386 MET MET A . n 
A 1 366 PHE 366 387 387 PHE PHE A . n 
A 1 367 ILE 367 388 388 ILE ILE A . n 
A 1 368 PRO 368 389 389 PRO PRO A . n 
A 1 369 LYS 369 390 390 LYS LYS A . n 
A 1 370 GLY 370 391 391 GLY GLY A . n 
A 1 371 VAL 371 392 392 VAL VAL A . n 
A 1 372 VAL 372 393 393 VAL VAL A . n 
A 1 373 VAL 373 394 394 VAL VAL A . n 
A 1 374 MET 374 395 395 MET MET A . n 
A 1 375 ILE 375 396 396 ILE ILE A . n 
A 1 376 PRO 376 397 397 PRO PRO A . n 
A 1 377 SER 377 398 398 SER SER A . n 
A 1 378 TYR 378 399 399 TYR TYR A . n 
A 1 379 ALA 379 400 400 ALA ALA A . n 
A 1 380 LEU 380 401 401 LEU LEU A . n 
A 1 381 HIS 381 402 402 HIS HIS A . n 
A 1 382 ARG 382 403 403 ARG ARG A . n 
A 1 383 ASP 383 404 404 ASP ASP A . n 
A 1 384 PRO 384 405 405 PRO PRO A . n 
A 1 385 LYS 385 406 406 LYS LYS A . n 
A 1 386 TYR 386 407 407 TYR TYR A . n 
A 1 387 TRP 387 408 408 TRP TRP A . n 
A 1 388 THR 388 409 409 THR THR A . n 
A 1 389 GLU 389 410 410 GLU GLU A . n 
A 1 390 PRO 390 411 411 PRO PRO A . n 
A 1 391 GLU 391 412 412 GLU GLU A . n 
A 1 392 LYS 392 413 413 LYS LYS A . n 
A 1 393 PHE 393 414 414 PHE PHE A . n 
A 1 394 LEU 394 415 415 LEU LEU A . n 
A 1 395 PRO 395 416 416 PRO PRO A . n 
A 1 396 GLU 396 417 417 GLU GLU A . n 
A 1 397 ARG 397 418 418 ARG ARG A . n 
A 1 398 PHE 398 419 419 PHE PHE A . n 
A 1 399 SER 399 420 420 SER SER A . n 
A 1 400 LYS 400 421 421 LYS LYS A . n 
A 1 401 LYS 401 422 422 LYS LYS A . n 
A 1 402 ASN 402 423 423 ASN ASN A . n 
A 1 403 LYS 403 424 424 LYS LYS A . n 
A 1 404 ASP 404 425 425 ASP ASP A . n 
A 1 405 ASN 405 426 426 ASN ASN A . n 
A 1 406 ILE 406 427 427 ILE ILE A . n 
A 1 407 ASP 407 428 428 ASP ASP A . n 
A 1 408 PRO 408 429 429 PRO PRO A . n 
A 1 409 TYR 409 430 430 TYR TYR A . n 
A 1 410 ILE 410 431 431 ILE ILE A . n 
A 1 411 TYR 411 432 432 TYR TYR A . n 
A 1 412 THR 412 433 433 THR THR A . n 
A 1 413 PRO 413 434 434 PRO PRO A . n 
A 1 414 PHE 414 435 435 PHE PHE A . n 
A 1 415 GLY 415 436 436 GLY GLY A . n 
A 1 416 SER 416 437 437 SER SER A . n 
A 1 417 GLY 417 438 438 GLY GLY A . n 
A 1 418 PRO 418 439 439 PRO PRO A . n 
A 1 419 ARG 419 440 440 ARG ARG A . n 
A 1 420 ASN 420 441 441 ASN ASN A . n 
A 1 421 CYS 421 442 442 CYS CYS A . n 
A 1 422 ILE 422 443 443 ILE ILE A . n 
A 1 423 GLY 423 444 444 GLY GLY A . n 
A 1 424 MET 424 445 445 MET MET A . n 
A 1 425 ARG 425 446 446 ARG ARG A . n 
A 1 426 PHE 426 447 447 PHE PHE A . n 
A 1 427 ALA 427 448 448 ALA ALA A . n 
A 1 428 LEU 428 449 449 LEU LEU A . n 
A 1 429 MET 429 450 450 MET MET A . n 
A 1 430 ASN 430 451 451 ASN ASN A . n 
A 1 431 MET 431 452 452 MET MET A . n 
A 1 432 LYS 432 453 453 LYS LYS A . n 
A 1 433 LEU 433 454 454 LEU LEU A . n 
A 1 434 ALA 434 455 455 ALA ALA A . n 
A 1 435 LEU 435 456 456 LEU LEU A . n 
A 1 436 ILE 436 457 457 ILE ILE A . n 
A 1 437 ARG 437 458 458 ARG ARG A . n 
A 1 438 VAL 438 459 459 VAL VAL A . n 
A 1 439 LEU 439 460 460 LEU LEU A . n 
A 1 440 GLN 440 461 461 GLN GLN A . n 
A 1 441 ASN 441 462 462 ASN ASN A . n 
A 1 442 PHE 442 463 463 PHE PHE A . n 
A 1 443 SER 443 464 464 SER SER A . n 
A 1 444 PHE 444 465 465 PHE PHE A . n 
A 1 445 LYS 445 466 466 LYS LYS A . n 
A 1 446 PRO 446 467 467 PRO PRO A . n 
A 1 447 CYS 447 468 468 CYS CYS A . n 
A 1 448 LYS 448 469 469 LYS LYS A . n 
A 1 449 GLU 449 470 ?   ?   ?   A . n 
A 1 450 THR 450 471 471 THR THR A . n 
A 1 451 GLN 451 472 472 GLN GLN A . n 
A 1 452 ILE 452 473 473 ILE ILE A . n 
A 1 453 PRO 453 474 474 PRO PRO A . n 
A 1 454 LEU 454 475 475 LEU LEU A . n 
A 1 455 LYS 455 476 476 LYS LYS A . n 
A 1 456 LEU 456 477 477 LEU LEU A . n 
A 1 457 SER 457 478 478 SER SER A . n 
A 1 458 LEU 458 479 479 LEU LEU A . n 
A 1 459 GLY 459 480 480 GLY GLY A . n 
A 1 460 GLY 460 481 481 GLY GLY A . n 
A 1 461 LEU 461 482 482 LEU LEU A . n 
A 1 462 LEU 462 483 483 LEU LEU A . n 
A 1 463 GLN 463 484 484 GLN GLN A . n 
A 1 464 PRO 464 485 485 PRO PRO A . n 
A 1 465 GLU 465 486 486 GLU GLU A . n 
A 1 466 LYS 466 487 487 LYS LYS A . n 
A 1 467 PRO 467 488 488 PRO PRO A . n 
A 1 468 VAL 468 489 489 VAL VAL A . n 
A 1 469 VAL 469 490 490 VAL VAL A . n 
A 1 470 LEU 470 491 491 LEU LEU A . n 
A 1 471 LYS 471 492 492 LYS LYS A . n 
A 1 472 VAL 472 493 493 VAL VAL A . n 
A 1 473 GLU 473 494 494 GLU GLU A . n 
A 1 474 SER 474 495 495 SER SER A . n 
A 1 475 ARG 475 496 496 ARG ARG A . n 
A 1 476 ASP 476 497 ?   ?   ?   A . n 
A 1 477 GLY 477 498 ?   ?   ?   A . n 
A 1 478 THR 478 499 ?   ?   ?   A . n 
A 1 479 VAL 479 500 ?   ?   ?   A . n 
A 1 480 SER 480 501 ?   ?   ?   A . n 
A 1 481 GLY 481 502 ?   ?   ?   A . n 
A 1 482 ALA 482 503 ?   ?   ?   A . n 
A 1 483 HIS 483 504 ?   ?   ?   A . n 
A 1 484 HIS 484 505 ?   ?   ?   A . n 
A 1 485 HIS 485 506 ?   ?   ?   A . n 
A 1 486 HIS 486 507 ?   ?   ?   A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1BNX 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1BNX 
_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 
B 2 HEM   1 601 501 HEM   HEM A . 
C 3 A1BNX 1 602 502 A1BNX S11 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 34  ? CG  ? A LYS 13  CG  
2   1 Y 1 A LYS 34  ? CD  ? A LYS 13  CD  
3   1 Y 1 A LYS 34  ? CE  ? A LYS 13  CE  
4   1 Y 1 A LYS 34  ? NZ  ? A LYS 13  NZ  
5   1 Y 1 A LYS 35  ? CG  ? A LYS 14  CG  
6   1 Y 1 A LYS 35  ? CD  ? A LYS 14  CD  
7   1 Y 1 A LYS 35  ? CE  ? A LYS 14  CE  
8   1 Y 1 A LYS 35  ? NZ  ? A LYS 14  NZ  
9   1 Y 1 A LEU 36  ? CG  ? A LEU 15  CG  
10  1 Y 1 A LEU 36  ? CD1 ? A LEU 15  CD1 
11  1 Y 1 A LEU 36  ? CD2 ? A LEU 15  CD2 
12  1 Y 1 A LYS 55  ? CG  ? A LYS 34  CG  
13  1 Y 1 A LYS 55  ? CD  ? A LYS 34  CD  
14  1 Y 1 A LYS 55  ? CE  ? A LYS 34  CE  
15  1 Y 1 A LYS 55  ? NZ  ? A LYS 34  NZ  
16  1 Y 1 A MET 59  ? CG  ? A MET 38  CG  
17  1 Y 1 A MET 59  ? SD  ? A MET 38  SD  
18  1 Y 1 A MET 59  ? CE  ? A MET 38  CE  
19  1 Y 1 A LYS 66  ? CG  ? A LYS 45  CG  
20  1 Y 1 A LYS 66  ? CD  ? A LYS 45  CD  
21  1 Y 1 A LYS 66  ? CE  ? A LYS 45  CE  
22  1 Y 1 A LYS 66  ? NZ  ? A LYS 45  NZ  
23  1 Y 1 A LYS 67  ? CG  ? A LYS 46  CG  
24  1 Y 1 A LYS 67  ? CD  ? A LYS 46  CD  
25  1 Y 1 A LYS 67  ? CE  ? A LYS 46  CE  
26  1 Y 1 A LYS 67  ? NZ  ? A LYS 46  NZ  
27  1 Y 1 A LYS 70  ? CG  ? A LYS 49  CG  
28  1 Y 1 A LYS 70  ? CD  ? A LYS 49  CD  
29  1 Y 1 A LYS 70  ? CE  ? A LYS 49  CE  
30  1 Y 1 A LYS 70  ? NZ  ? A LYS 49  NZ  
31  1 Y 1 A ASP 88  ? CG  ? A ASP 67  CG  
32  1 Y 1 A ASP 88  ? OD1 ? A ASP 67  OD1 
33  1 Y 1 A ASP 88  ? OD2 ? A ASP 67  OD2 
34  1 Y 1 A LYS 91  ? CG  ? A LYS 70  CG  
35  1 Y 1 A LYS 91  ? CD  ? A LYS 70  CD  
36  1 Y 1 A LYS 91  ? CE  ? A LYS 70  CE  
37  1 Y 1 A LYS 91  ? NZ  ? A LYS 70  NZ  
38  1 Y 1 A LYS 96  ? CG  ? A LYS 75  CG  
39  1 Y 1 A LYS 96  ? CD  ? A LYS 75  CD  
40  1 Y 1 A LYS 96  ? CE  ? A LYS 75  CE  
41  1 Y 1 A LYS 96  ? NZ  ? A LYS 75  NZ  
42  1 Y 1 A VAL 101 ? CG1 ? A VAL 80  CG1 
43  1 Y 1 A VAL 101 ? CG2 ? A VAL 80  CG2 
44  1 Y 1 A LYS 115 ? CG  ? A LYS 94  CG  
45  1 Y 1 A LYS 115 ? CD  ? A LYS 94  CD  
46  1 Y 1 A LYS 115 ? CE  ? A LYS 94  CE  
47  1 Y 1 A LYS 115 ? NZ  ? A LYS 94  NZ  
48  1 Y 1 A LYS 127 ? CG  ? A LYS 106 CG  
49  1 Y 1 A LYS 127 ? CD  ? A LYS 106 CD  
50  1 Y 1 A LYS 127 ? CE  ? A LYS 106 CE  
51  1 Y 1 A LYS 127 ? NZ  ? A LYS 106 NZ  
52  1 Y 1 A LEU 132 ? CG  ? A LEU 111 CG  
53  1 Y 1 A LEU 132 ? CD1 ? A LEU 111 CD1 
54  1 Y 1 A LEU 132 ? CD2 ? A LEU 111 CD2 
55  1 Y 1 A PHE 137 ? CG  ? A PHE 116 CG  
56  1 Y 1 A PHE 137 ? CD1 ? A PHE 116 CD1 
57  1 Y 1 A PHE 137 ? CD2 ? A PHE 116 CD2 
58  1 Y 1 A PHE 137 ? CE1 ? A PHE 116 CE1 
59  1 Y 1 A PHE 137 ? CE2 ? A PHE 116 CE2 
60  1 Y 1 A PHE 137 ? CZ  ? A PHE 116 CZ  
61  1 Y 1 A LYS 141 ? CG  ? A LYS 120 CG  
62  1 Y 1 A LYS 141 ? CD  ? A LYS 120 CD  
63  1 Y 1 A LYS 141 ? CE  ? A LYS 120 CE  
64  1 Y 1 A LYS 141 ? NZ  ? A LYS 120 NZ  
65  1 Y 1 A LEU 142 ? CG  ? A LEU 121 CG  
66  1 Y 1 A LEU 142 ? CD1 ? A LEU 121 CD1 
67  1 Y 1 A LEU 142 ? CD2 ? A LEU 121 CD2 
68  1 Y 1 A LYS 143 ? CG  ? A LYS 122 CG  
69  1 Y 1 A LYS 143 ? CD  ? A LYS 122 CD  
70  1 Y 1 A LYS 143 ? CE  ? A LYS 122 CE  
71  1 Y 1 A LYS 143 ? NZ  ? A LYS 122 NZ  
72  1 Y 1 A GLU 144 ? CG  ? A GLU 123 CG  
73  1 Y 1 A GLU 144 ? CD  ? A GLU 123 CD  
74  1 Y 1 A GLU 144 ? OE1 ? A GLU 123 OE1 
75  1 Y 1 A GLU 144 ? OE2 ? A GLU 123 OE2 
76  1 Y 1 A MET 145 ? CG  ? A MET 124 CG  
77  1 Y 1 A MET 145 ? SD  ? A MET 124 SD  
78  1 Y 1 A MET 145 ? CE  ? A MET 124 CE  
79  1 Y 1 A VAL 146 ? CG1 ? A VAL 125 CG1 
80  1 Y 1 A VAL 146 ? CG2 ? A VAL 125 CG2 
81  1 Y 1 A ILE 148 ? CG1 ? A ILE 127 CG1 
82  1 Y 1 A ILE 148 ? CG2 ? A ILE 127 CG2 
83  1 Y 1 A ILE 148 ? CD1 ? A ILE 127 CD1 
84  1 Y 1 A ILE 149 ? CG1 ? A ILE 128 CG1 
85  1 Y 1 A ILE 149 ? CG2 ? A ILE 128 CG2 
86  1 Y 1 A ILE 149 ? CD1 ? A ILE 128 CD1 
87  1 Y 1 A GLN 151 ? CG  ? A GLN 130 CG  
88  1 Y 1 A GLN 151 ? CD  ? A GLN 130 CD  
89  1 Y 1 A GLN 151 ? OE1 ? A GLN 130 OE1 
90  1 Y 1 A GLN 151 ? NE2 ? A GLN 130 NE2 
91  1 Y 1 A TYR 152 ? CG  ? A TYR 131 CG  
92  1 Y 1 A TYR 152 ? CD1 ? A TYR 131 CD1 
93  1 Y 1 A TYR 152 ? CD2 ? A TYR 131 CD2 
94  1 Y 1 A TYR 152 ? CE1 ? A TYR 131 CE1 
95  1 Y 1 A TYR 152 ? CE2 ? A TYR 131 CE2 
96  1 Y 1 A TYR 152 ? CZ  ? A TYR 131 CZ  
97  1 Y 1 A TYR 152 ? OH  ? A TYR 131 OH  
98  1 Y 1 A ASP 154 ? CG  ? A ASP 133 CG  
99  1 Y 1 A ASP 154 ? OD1 ? A ASP 133 OD1 
100 1 Y 1 A ASP 154 ? OD2 ? A ASP 133 OD2 
101 1 Y 1 A VAL 155 ? CG1 ? A VAL 134 CG1 
102 1 Y 1 A VAL 155 ? CG2 ? A VAL 134 CG2 
103 1 Y 1 A LEU 156 ? CG  ? A LEU 135 CG  
104 1 Y 1 A LEU 156 ? CD1 ? A LEU 135 CD1 
105 1 Y 1 A LEU 156 ? CD2 ? A LEU 135 CD2 
106 1 Y 1 A VAL 157 ? CG1 ? A VAL 136 CG1 
107 1 Y 1 A VAL 157 ? CG2 ? A VAL 136 CG2 
108 1 Y 1 A ARG 158 ? CG  ? A ARG 137 CG  
109 1 Y 1 A ARG 158 ? CD  ? A ARG 137 CD  
110 1 Y 1 A ARG 158 ? NE  ? A ARG 137 NE  
111 1 Y 1 A ARG 158 ? CZ  ? A ARG 137 CZ  
112 1 Y 1 A ARG 158 ? NH1 ? A ARG 137 NH1 
113 1 Y 1 A ARG 158 ? NH2 ? A ARG 137 NH2 
114 1 Y 1 A ASN 159 ? CG  ? A ASN 138 CG  
115 1 Y 1 A ASN 159 ? OD1 ? A ASN 138 OD1 
116 1 Y 1 A ASN 159 ? ND2 ? A ASN 138 ND2 
117 1 Y 1 A LEU 160 ? CG  ? A LEU 139 CG  
118 1 Y 1 A LEU 160 ? CD1 ? A LEU 139 CD1 
119 1 Y 1 A LEU 160 ? CD2 ? A LEU 139 CD2 
120 1 Y 1 A ARG 161 ? CG  ? A ARG 140 CG  
121 1 Y 1 A ARG 161 ? CD  ? A ARG 140 CD  
122 1 Y 1 A ARG 161 ? NE  ? A ARG 140 NE  
123 1 Y 1 A ARG 161 ? CZ  ? A ARG 140 CZ  
124 1 Y 1 A ARG 161 ? NH1 ? A ARG 140 NH1 
125 1 Y 1 A ARG 161 ? NH2 ? A ARG 140 NH2 
126 1 Y 1 A ARG 162 ? CG  ? A ARG 141 CG  
127 1 Y 1 A ARG 162 ? CD  ? A ARG 141 CD  
128 1 Y 1 A ARG 162 ? NE  ? A ARG 141 NE  
129 1 Y 1 A ARG 162 ? CZ  ? A ARG 141 CZ  
130 1 Y 1 A ARG 162 ? NH1 ? A ARG 141 NH1 
131 1 Y 1 A ARG 162 ? NH2 ? A ARG 141 NH2 
132 1 Y 1 A GLU 163 ? CG  ? A GLU 142 CG  
133 1 Y 1 A GLU 163 ? CD  ? A GLU 142 CD  
134 1 Y 1 A GLU 163 ? OE1 ? A GLU 142 OE1 
135 1 Y 1 A GLU 163 ? OE2 ? A GLU 142 OE2 
136 1 Y 1 A GLU 165 ? CG  ? A GLU 144 CG  
137 1 Y 1 A GLU 165 ? CD  ? A GLU 144 CD  
138 1 Y 1 A GLU 165 ? OE1 ? A GLU 144 OE1 
139 1 Y 1 A GLU 165 ? OE2 ? A GLU 144 OE2 
140 1 Y 1 A LYS 168 ? CG  ? A LYS 147 CG  
141 1 Y 1 A LYS 168 ? CD  ? A LYS 147 CD  
142 1 Y 1 A LYS 168 ? CE  ? A LYS 147 CE  
143 1 Y 1 A LYS 168 ? NZ  ? A LYS 147 NZ  
144 1 Y 1 A VAL 170 ? CG1 ? A VAL 149 CG1 
145 1 Y 1 A VAL 170 ? CG2 ? A VAL 149 CG2 
146 1 Y 1 A THR 171 ? OG1 ? A THR 150 OG1 
147 1 Y 1 A THR 171 ? CG2 ? A THR 150 CG2 
148 1 Y 1 A LYS 173 ? CG  ? A LYS 152 CG  
149 1 Y 1 A LYS 173 ? CD  ? A LYS 152 CD  
150 1 Y 1 A LYS 173 ? CE  ? A LYS 152 CE  
151 1 Y 1 A LYS 173 ? NZ  ? A LYS 152 NZ  
152 1 Y 1 A VAL 175 ? CG1 ? A VAL 154 CG1 
153 1 Y 1 A VAL 175 ? CG2 ? A VAL 154 CG2 
154 1 Y 1 A PHE 176 ? CG  ? A PHE 155 CG  
155 1 Y 1 A PHE 176 ? CD1 ? A PHE 155 CD1 
156 1 Y 1 A PHE 176 ? CD2 ? A PHE 155 CD2 
157 1 Y 1 A PHE 176 ? CE1 ? A PHE 155 CE1 
158 1 Y 1 A PHE 176 ? CE2 ? A PHE 155 CE2 
159 1 Y 1 A PHE 176 ? CZ  ? A PHE 155 CZ  
160 1 Y 1 A SER 180 ? OG  ? A SER 159 OG  
161 1 Y 1 A MET 181 ? CG  ? A MET 160 CG  
162 1 Y 1 A MET 181 ? SD  ? A MET 160 SD  
163 1 Y 1 A MET 181 ? CE  ? A MET 160 CE  
164 1 Y 1 A ILE 184 ? CG1 ? A ILE 163 CG1 
165 1 Y 1 A ILE 184 ? CG2 ? A ILE 163 CG2 
166 1 Y 1 A ILE 184 ? CD1 ? A ILE 163 CD1 
167 1 Y 1 A SER 186 ? OG  ? A SER 165 OG  
168 1 Y 1 A SER 188 ? OG  ? A SER 167 OG  
169 1 Y 1 A VAL 191 ? CG1 ? A VAL 170 CG1 
170 1 Y 1 A VAL 191 ? CG2 ? A VAL 170 CG2 
171 1 Y 1 A ASN 192 ? CG  ? A ASN 171 CG  
172 1 Y 1 A ASN 192 ? OD1 ? A ASN 171 OD1 
173 1 Y 1 A ASN 192 ? ND2 ? A ASN 171 ND2 
174 1 Y 1 A ILE 193 ? CG1 ? A ILE 172 CG1 
175 1 Y 1 A ILE 193 ? CG2 ? A ILE 172 CG2 
176 1 Y 1 A ILE 193 ? CD1 ? A ILE 172 CD1 
177 1 Y 1 A SER 195 ? OG  ? A SER 174 OG  
178 1 Y 1 A LEU 196 ? CG  ? A LEU 175 CG  
179 1 Y 1 A LEU 196 ? CD1 ? A LEU 175 CD1 
180 1 Y 1 A LEU 196 ? CD2 ? A LEU 175 CD2 
181 1 Y 1 A ASN 197 ? CG  ? A ASN 176 CG  
182 1 Y 1 A ASN 197 ? OD1 ? A ASN 176 OD1 
183 1 Y 1 A ASN 197 ? ND2 ? A ASN 176 ND2 
184 1 Y 1 A ASN 198 ? CG  ? A ASN 177 CG  
185 1 Y 1 A ASN 198 ? OD1 ? A ASN 177 OD1 
186 1 Y 1 A ASN 198 ? ND2 ? A ASN 177 ND2 
187 1 Y 1 A GLN 200 ? CG  ? A GLN 179 CG  
188 1 Y 1 A GLN 200 ? CD  ? A GLN 179 CD  
189 1 Y 1 A GLN 200 ? OE1 ? A GLN 179 OE1 
190 1 Y 1 A GLN 200 ? NE2 ? A GLN 179 NE2 
191 1 Y 1 A ASP 201 ? CG  ? A ASP 180 CG  
192 1 Y 1 A ASP 201 ? OD1 ? A ASP 180 OD1 
193 1 Y 1 A ASP 201 ? OD2 ? A ASP 180 OD2 
194 1 Y 1 A PHE 203 ? CG  ? A PHE 182 CG  
195 1 Y 1 A PHE 203 ? CD1 ? A PHE 182 CD1 
196 1 Y 1 A PHE 203 ? CD2 ? A PHE 182 CD2 
197 1 Y 1 A PHE 203 ? CE1 ? A PHE 182 CE1 
198 1 Y 1 A PHE 203 ? CE2 ? A PHE 182 CE2 
199 1 Y 1 A PHE 203 ? CZ  ? A PHE 182 CZ  
200 1 Y 1 A GLU 205 ? CG  ? A GLU 184 CG  
201 1 Y 1 A GLU 205 ? CD  ? A GLU 184 CD  
202 1 Y 1 A GLU 205 ? OE1 ? A GLU 184 OE1 
203 1 Y 1 A GLU 205 ? OE2 ? A GLU 184 OE2 
204 1 Y 1 A THR 207 ? OG1 ? A THR 186 OG1 
205 1 Y 1 A THR 207 ? CG2 ? A THR 186 CG2 
206 1 Y 1 A LYS 208 ? CG  ? A LYS 187 CG  
207 1 Y 1 A LYS 208 ? CD  ? A LYS 187 CD  
208 1 Y 1 A LYS 208 ? CE  ? A LYS 187 CE  
209 1 Y 1 A LYS 208 ? NZ  ? A LYS 187 NZ  
210 1 Y 1 A LYS 209 ? CG  ? A LYS 188 CG  
211 1 Y 1 A LYS 209 ? CD  ? A LYS 188 CD  
212 1 Y 1 A LYS 209 ? CE  ? A LYS 188 CE  
213 1 Y 1 A LYS 209 ? NZ  ? A LYS 188 NZ  
214 1 Y 1 A LEU 216 ? CG  ? A LEU 195 CG  
215 1 Y 1 A LEU 216 ? CD1 ? A LEU 195 CD1 
216 1 Y 1 A LEU 216 ? CD2 ? A LEU 195 CD2 
217 1 Y 1 A ASP 217 ? CG  ? A ASP 196 CG  
218 1 Y 1 A ASP 217 ? OD1 ? A ASP 196 OD1 
219 1 Y 1 A ASP 217 ? OD2 ? A ASP 196 OD2 
220 1 Y 1 A PHE 219 ? CG  ? A PHE 198 CG  
221 1 Y 1 A PHE 219 ? CD1 ? A PHE 198 CD1 
222 1 Y 1 A PHE 219 ? CD2 ? A PHE 198 CD2 
223 1 Y 1 A PHE 219 ? CE1 ? A PHE 198 CE1 
224 1 Y 1 A PHE 219 ? CE2 ? A PHE 198 CE2 
225 1 Y 1 A PHE 219 ? CZ  ? A PHE 198 CZ  
226 1 Y 1 A PHE 220 ? CG  ? A PHE 199 CG  
227 1 Y 1 A PHE 220 ? CD1 ? A PHE 199 CD1 
228 1 Y 1 A PHE 220 ? CD2 ? A PHE 199 CD2 
229 1 Y 1 A PHE 220 ? CE1 ? A PHE 199 CE1 
230 1 Y 1 A PHE 220 ? CE2 ? A PHE 199 CE2 
231 1 Y 1 A PHE 220 ? CZ  ? A PHE 199 CZ  
232 1 Y 1 A LEU 221 ? CG  ? A LEU 200 CG  
233 1 Y 1 A LEU 221 ? CD1 ? A LEU 200 CD1 
234 1 Y 1 A LEU 221 ? CD2 ? A LEU 200 CD2 
235 1 Y 1 A ILE 223 ? CG1 ? A ILE 202 CG1 
236 1 Y 1 A ILE 223 ? CG2 ? A ILE 202 CG2 
237 1 Y 1 A ILE 223 ? CD1 ? A ILE 202 CD1 
238 1 Y 1 A PHE 226 ? CG  ? A PHE 205 CG  
239 1 Y 1 A PHE 226 ? CD1 ? A PHE 205 CD1 
240 1 Y 1 A PHE 226 ? CD2 ? A PHE 205 CD2 
241 1 Y 1 A PHE 226 ? CE1 ? A PHE 205 CE1 
242 1 Y 1 A PHE 226 ? CE2 ? A PHE 205 CE2 
243 1 Y 1 A PHE 226 ? CZ  ? A PHE 205 CZ  
244 1 Y 1 A LEU 229 ? CG  ? A LEU 208 CG  
245 1 Y 1 A LEU 229 ? CD1 ? A LEU 208 CD1 
246 1 Y 1 A LEU 229 ? CD2 ? A LEU 208 CD2 
247 1 Y 1 A ILE 232 ? CG1 ? A ILE 211 CG1 
248 1 Y 1 A ILE 232 ? CG2 ? A ILE 211 CG2 
249 1 Y 1 A ILE 232 ? CD1 ? A ILE 211 CD1 
250 1 Y 1 A VAL 235 ? CG1 ? A VAL 214 CG1 
251 1 Y 1 A VAL 235 ? CG2 ? A VAL 214 CG2 
252 1 Y 1 A LEU 236 ? CG  ? A LEU 215 CG  
253 1 Y 1 A LEU 236 ? CD1 ? A LEU 215 CD1 
254 1 Y 1 A LEU 236 ? CD2 ? A LEU 215 CD2 
255 1 Y 1 A ASN 237 ? CG  ? A ASN 216 CG  
256 1 Y 1 A ASN 237 ? OD1 ? A ASN 216 OD1 
257 1 Y 1 A ASN 237 ? ND2 ? A ASN 216 ND2 
258 1 Y 1 A ARG 243 ? CG  ? A ARG 222 CG  
259 1 Y 1 A ARG 243 ? CD  ? A ARG 222 CD  
260 1 Y 1 A ARG 243 ? NE  ? A ARG 222 NE  
261 1 Y 1 A ARG 243 ? CZ  ? A ARG 222 CZ  
262 1 Y 1 A ARG 243 ? NH1 ? A ARG 222 NH1 
263 1 Y 1 A ARG 243 ? NH2 ? A ARG 222 NH2 
264 1 Y 1 A GLU 244 ? CG  ? A GLU 223 CG  
265 1 Y 1 A GLU 244 ? CD  ? A GLU 223 CD  
266 1 Y 1 A GLU 244 ? OE1 ? A GLU 223 OE1 
267 1 Y 1 A GLU 244 ? OE2 ? A GLU 223 OE2 
268 1 Y 1 A VAL 245 ? CG1 ? A VAL 224 CG1 
269 1 Y 1 A VAL 245 ? CG2 ? A VAL 224 CG2 
270 1 Y 1 A PHE 248 ? CG  ? A PHE 227 CG  
271 1 Y 1 A PHE 248 ? CD1 ? A PHE 227 CD1 
272 1 Y 1 A PHE 248 ? CD2 ? A PHE 227 CD2 
273 1 Y 1 A PHE 248 ? CE1 ? A PHE 227 CE1 
274 1 Y 1 A PHE 248 ? CE2 ? A PHE 227 CE2 
275 1 Y 1 A PHE 248 ? CZ  ? A PHE 227 CZ  
276 1 Y 1 A LEU 249 ? CG  ? A LEU 228 CG  
277 1 Y 1 A LEU 249 ? CD1 ? A LEU 228 CD1 
278 1 Y 1 A LEU 249 ? CD2 ? A LEU 228 CD2 
279 1 Y 1 A ARG 250 ? CG  ? A ARG 229 CG  
280 1 Y 1 A ARG 250 ? CD  ? A ARG 229 CD  
281 1 Y 1 A ARG 250 ? NE  ? A ARG 229 NE  
282 1 Y 1 A ARG 250 ? CZ  ? A ARG 229 CZ  
283 1 Y 1 A ARG 250 ? NH1 ? A ARG 229 NH1 
284 1 Y 1 A ARG 250 ? NH2 ? A ARG 229 NH2 
285 1 Y 1 A LYS 251 ? CG  ? A LYS 230 CG  
286 1 Y 1 A LYS 251 ? CD  ? A LYS 230 CD  
287 1 Y 1 A LYS 251 ? CE  ? A LYS 230 CE  
288 1 Y 1 A LYS 251 ? NZ  ? A LYS 230 NZ  
289 1 Y 1 A VAL 253 ? CG1 ? A VAL 232 CG1 
290 1 Y 1 A VAL 253 ? CG2 ? A VAL 232 CG2 
291 1 Y 1 A LYS 254 ? CG  ? A LYS 233 CG  
292 1 Y 1 A LYS 254 ? CD  ? A LYS 233 CD  
293 1 Y 1 A LYS 254 ? CE  ? A LYS 233 CE  
294 1 Y 1 A LYS 254 ? NZ  ? A LYS 233 NZ  
295 1 Y 1 A ARG 255 ? CG  ? A ARG 234 CG  
296 1 Y 1 A ARG 255 ? CD  ? A ARG 234 CD  
297 1 Y 1 A ARG 255 ? NE  ? A ARG 234 NE  
298 1 Y 1 A ARG 255 ? CZ  ? A ARG 234 CZ  
299 1 Y 1 A ARG 255 ? NH1 ? A ARG 234 NH1 
300 1 Y 1 A ARG 255 ? NH2 ? A ARG 234 NH2 
301 1 Y 1 A MET 256 ? CG  ? A MET 235 CG  
302 1 Y 1 A MET 256 ? SD  ? A MET 235 SD  
303 1 Y 1 A MET 256 ? CE  ? A MET 235 CE  
304 1 Y 1 A LYS 257 ? CG  ? A LYS 236 CG  
305 1 Y 1 A LYS 257 ? CD  ? A LYS 236 CD  
306 1 Y 1 A LYS 257 ? CE  ? A LYS 236 CE  
307 1 Y 1 A LYS 257 ? NZ  ? A LYS 236 NZ  
308 1 Y 1 A GLU 258 ? CG  ? A GLU 237 CG  
309 1 Y 1 A GLU 258 ? CD  ? A GLU 237 CD  
310 1 Y 1 A GLU 258 ? OE1 ? A GLU 237 OE1 
311 1 Y 1 A GLU 258 ? OE2 ? A GLU 237 OE2 
312 1 Y 1 A SER 259 ? OG  ? A SER 238 OG  
313 1 Y 1 A ARG 260 ? CG  ? A ARG 239 CG  
314 1 Y 1 A ARG 260 ? CD  ? A ARG 239 CD  
315 1 Y 1 A ARG 260 ? NE  ? A ARG 239 NE  
316 1 Y 1 A ARG 260 ? CZ  ? A ARG 239 CZ  
317 1 Y 1 A ARG 260 ? NH1 ? A ARG 239 NH1 
318 1 Y 1 A ARG 260 ? NH2 ? A ARG 239 NH2 
319 1 Y 1 A LEU 261 ? CG  ? A LEU 240 CG  
320 1 Y 1 A LEU 261 ? CD1 ? A LEU 240 CD1 
321 1 Y 1 A LEU 261 ? CD2 ? A LEU 240 CD2 
322 1 Y 1 A LYS 266 ? CG  ? A LYS 245 CG  
323 1 Y 1 A LYS 266 ? CD  ? A LYS 245 CD  
324 1 Y 1 A LYS 266 ? CE  ? A LYS 245 CE  
325 1 Y 1 A LYS 266 ? NZ  ? A LYS 245 NZ  
326 1 Y 1 A HIS 267 ? CG  ? A HIS 246 CG  
327 1 Y 1 A HIS 267 ? ND1 ? A HIS 246 ND1 
328 1 Y 1 A HIS 267 ? CD2 ? A HIS 246 CD2 
329 1 Y 1 A HIS 267 ? CE1 ? A HIS 246 CE1 
330 1 Y 1 A HIS 267 ? NE2 ? A HIS 246 NE2 
331 1 Y 1 A ARG 268 ? CG  ? A ARG 247 CG  
332 1 Y 1 A ARG 268 ? CD  ? A ARG 247 CD  
333 1 Y 1 A ARG 268 ? NE  ? A ARG 247 NE  
334 1 Y 1 A ARG 268 ? CZ  ? A ARG 247 CZ  
335 1 Y 1 A ARG 268 ? NH1 ? A ARG 247 NH1 
336 1 Y 1 A ARG 268 ? NH2 ? A ARG 247 NH2 
337 1 Y 1 A VAL 269 ? CG1 ? A VAL 248 CG1 
338 1 Y 1 A VAL 269 ? CG2 ? A VAL 248 CG2 
339 1 Y 1 A LEU 272 ? CG  ? A LEU 251 CG  
340 1 Y 1 A LEU 272 ? CD1 ? A LEU 251 CD1 
341 1 Y 1 A LEU 272 ? CD2 ? A LEU 251 CD2 
342 1 Y 1 A GLN 273 ? CG  ? A GLN 252 CG  
343 1 Y 1 A GLN 273 ? CD  ? A GLN 252 CD  
344 1 Y 1 A GLN 273 ? OE1 ? A GLN 252 OE1 
345 1 Y 1 A GLN 273 ? NE2 ? A GLN 252 NE2 
346 1 Y 1 A LEU 274 ? CG  ? A LEU 253 CG  
347 1 Y 1 A LEU 274 ? CD1 ? A LEU 253 CD1 
348 1 Y 1 A LEU 274 ? CD2 ? A LEU 253 CD2 
349 1 Y 1 A ASP 277 ? CG  ? A ASP 256 CG  
350 1 Y 1 A ASP 277 ? OD1 ? A ASP 256 OD1 
351 1 Y 1 A ASP 277 ? OD2 ? A ASP 256 OD2 
352 1 Y 1 A SER 278 ? OG  ? A SER 257 OG  
353 1 Y 1 A LYS 288 ? CG  ? A LYS 267 CG  
354 1 Y 1 A LYS 288 ? CD  ? A LYS 267 CD  
355 1 Y 1 A LYS 288 ? CE  ? A LYS 267 CE  
356 1 Y 1 A LYS 288 ? NZ  ? A LYS 267 NZ  
357 1 Y 1 A LEU 290 ? CG  ? A LEU 269 CG  
358 1 Y 1 A LEU 290 ? CD1 ? A LEU 269 CD1 
359 1 Y 1 A LEU 290 ? CD2 ? A LEU 269 CD2 
360 1 Y 1 A GLU 294 ? CG  ? A GLU 273 CG  
361 1 Y 1 A GLU 294 ? CD  ? A GLU 273 CD  
362 1 Y 1 A GLU 294 ? OE1 ? A GLU 273 OE1 
363 1 Y 1 A GLU 294 ? OE2 ? A GLU 273 OE2 
364 1 Y 1 A LEU 295 ? CG  ? A LEU 274 CG  
365 1 Y 1 A LEU 295 ? CD1 ? A LEU 274 CD1 
366 1 Y 1 A LEU 295 ? CD2 ? A LEU 274 CD2 
367 1 Y 1 A ILE 303 ? CG1 ? A ILE 282 CG1 
368 1 Y 1 A ILE 303 ? CG2 ? A ILE 282 CG2 
369 1 Y 1 A ILE 303 ? CD1 ? A ILE 282 CD1 
370 1 Y 1 A HIS 324 ? CG  ? A HIS 303 CG  
371 1 Y 1 A HIS 324 ? ND1 ? A HIS 303 ND1 
372 1 Y 1 A HIS 324 ? CD2 ? A HIS 303 CD2 
373 1 Y 1 A HIS 324 ? CE1 ? A HIS 303 CE1 
374 1 Y 1 A HIS 324 ? NE2 ? A HIS 303 NE2 
375 1 Y 1 A GLN 329 ? CG  ? A GLN 308 CG  
376 1 Y 1 A GLN 329 ? CD  ? A GLN 308 CD  
377 1 Y 1 A GLN 329 ? OE1 ? A GLN 308 OE1 
378 1 Y 1 A GLN 329 ? NE2 ? A GLN 308 NE2 
379 1 Y 1 A GLU 334 ? CG  ? A GLU 313 CG  
380 1 Y 1 A GLU 334 ? CD  ? A GLU 313 CD  
381 1 Y 1 A GLU 334 ? OE1 ? A GLU 313 OE1 
382 1 Y 1 A GLU 334 ? OE2 ? A GLU 313 OE2 
383 1 Y 1 A ILE 335 ? CG1 ? A ILE 314 CG1 
384 1 Y 1 A ILE 335 ? CG2 ? A ILE 314 CG2 
385 1 Y 1 A ILE 335 ? CD1 ? A ILE 314 CD1 
386 1 Y 1 A ASP 336 ? CG  ? A ASP 315 CG  
387 1 Y 1 A ASP 336 ? OD1 ? A ASP 315 OD1 
388 1 Y 1 A ASP 336 ? OD2 ? A ASP 315 OD2 
389 1 Y 1 A VAL 338 ? CG1 ? A VAL 317 CG1 
390 1 Y 1 A VAL 338 ? CG2 ? A VAL 317 CG2 
391 1 Y 1 A LEU 339 ? CG  ? A LEU 318 CG  
392 1 Y 1 A LEU 339 ? CD1 ? A LEU 318 CD1 
393 1 Y 1 A LEU 339 ? CD2 ? A LEU 318 CD2 
394 1 Y 1 A ASN 341 ? CG  ? A ASN 320 CG  
395 1 Y 1 A ASN 341 ? OD1 ? A ASN 320 OD1 
396 1 Y 1 A ASN 341 ? ND2 ? A ASN 320 ND2 
397 1 Y 1 A LYS 342 ? CG  ? A LYS 321 CG  
398 1 Y 1 A LYS 342 ? CD  ? A LYS 321 CD  
399 1 Y 1 A LYS 342 ? CE  ? A LYS 321 CE  
400 1 Y 1 A LYS 342 ? NZ  ? A LYS 321 NZ  
401 1 Y 1 A ASP 348 ? CG  ? A ASP 327 CG  
402 1 Y 1 A ASP 348 ? OD1 ? A ASP 327 OD1 
403 1 Y 1 A ASP 348 ? OD2 ? A ASP 327 OD2 
404 1 Y 1 A LEU 351 ? CG  ? A LEU 330 CG  
405 1 Y 1 A LEU 351 ? CD1 ? A LEU 330 CD1 
406 1 Y 1 A LEU 351 ? CD2 ? A LEU 330 CD2 
407 1 Y 1 A GLN 352 ? CG  ? A GLN 331 CG  
408 1 Y 1 A GLN 352 ? CD  ? A GLN 331 CD  
409 1 Y 1 A GLN 352 ? OE1 ? A GLN 331 OE1 
410 1 Y 1 A GLN 352 ? NE2 ? A GLN 331 NE2 
411 1 Y 1 A MET 353 ? CG  ? A MET 332 CG  
412 1 Y 1 A MET 353 ? SD  ? A MET 332 SD  
413 1 Y 1 A MET 353 ? CE  ? A MET 332 CE  
414 1 Y 1 A VAL 359 ? CG1 ? A VAL 338 CG1 
415 1 Y 1 A VAL 359 ? CG2 ? A VAL 338 CG2 
416 1 Y 1 A LEU 366 ? CG  ? A LEU 345 CG  
417 1 Y 1 A LEU 366 ? CD1 ? A LEU 345 CD1 
418 1 Y 1 A LEU 366 ? CD2 ? A LEU 345 CD2 
419 1 Y 1 A LYS 379 ? CG  ? A LYS 358 CG  
420 1 Y 1 A LYS 379 ? CD  ? A LYS 358 CD  
421 1 Y 1 A LYS 379 ? CE  ? A LYS 358 CE  
422 1 Y 1 A LYS 379 ? NZ  ? A LYS 358 NZ  
423 1 Y 1 A VAL 381 ? CG1 ? A VAL 360 CG1 
424 1 Y 1 A VAL 381 ? CG2 ? A VAL 360 CG2 
425 1 Y 1 A GLU 382 ? CG  ? A GLU 361 CG  
426 1 Y 1 A GLU 382 ? CD  ? A GLU 361 CD  
427 1 Y 1 A GLU 382 ? OE1 ? A GLU 361 OE1 
428 1 Y 1 A GLU 382 ? OE2 ? A GLU 361 OE2 
429 1 Y 1 A ILE 383 ? CG1 ? A ILE 362 CG1 
430 1 Y 1 A ILE 383 ? CG2 ? A ILE 362 CG2 
431 1 Y 1 A ILE 383 ? CD1 ? A ILE 362 CD1 
432 1 Y 1 A LYS 390 ? CG  ? A LYS 369 CG  
433 1 Y 1 A LYS 390 ? CD  ? A LYS 369 CD  
434 1 Y 1 A LYS 390 ? CE  ? A LYS 369 CE  
435 1 Y 1 A LYS 390 ? NZ  ? A LYS 369 NZ  
436 1 Y 1 A LEU 401 ? CG  ? A LEU 380 CG  
437 1 Y 1 A LEU 401 ? CD1 ? A LEU 380 CD1 
438 1 Y 1 A LEU 401 ? CD2 ? A LEU 380 CD2 
439 1 Y 1 A LYS 406 ? CG  ? A LYS 385 CG  
440 1 Y 1 A LYS 406 ? CD  ? A LYS 385 CD  
441 1 Y 1 A LYS 406 ? CE  ? A LYS 385 CE  
442 1 Y 1 A LYS 406 ? NZ  ? A LYS 385 NZ  
443 1 Y 1 A TYR 407 ? CG  ? A TYR 386 CG  
444 1 Y 1 A TYR 407 ? CD1 ? A TYR 386 CD1 
445 1 Y 1 A TYR 407 ? CD2 ? A TYR 386 CD2 
446 1 Y 1 A TYR 407 ? CE1 ? A TYR 386 CE1 
447 1 Y 1 A TYR 407 ? CE2 ? A TYR 386 CE2 
448 1 Y 1 A TYR 407 ? CZ  ? A TYR 386 CZ  
449 1 Y 1 A TYR 407 ? OH  ? A TYR 386 OH  
450 1 Y 1 A THR 409 ? OG1 ? A THR 388 OG1 
451 1 Y 1 A THR 409 ? CG2 ? A THR 388 CG2 
452 1 Y 1 A GLU 410 ? CG  ? A GLU 389 CG  
453 1 Y 1 A GLU 410 ? CD  ? A GLU 389 CD  
454 1 Y 1 A GLU 410 ? OE1 ? A GLU 389 OE1 
455 1 Y 1 A GLU 410 ? OE2 ? A GLU 389 OE2 
456 1 Y 1 A LEU 415 ? CG  ? A LEU 394 CG  
457 1 Y 1 A LEU 415 ? CD1 ? A LEU 394 CD1 
458 1 Y 1 A LEU 415 ? CD2 ? A LEU 394 CD2 
459 1 Y 1 A ARG 418 ? CG  ? A ARG 397 CG  
460 1 Y 1 A ARG 418 ? CD  ? A ARG 397 CD  
461 1 Y 1 A ARG 418 ? NE  ? A ARG 397 NE  
462 1 Y 1 A ARG 418 ? CZ  ? A ARG 397 CZ  
463 1 Y 1 A ARG 418 ? NH1 ? A ARG 397 NH1 
464 1 Y 1 A ARG 418 ? NH2 ? A ARG 397 NH2 
465 1 Y 1 A LYS 421 ? CG  ? A LYS 400 CG  
466 1 Y 1 A LYS 421 ? CD  ? A LYS 400 CD  
467 1 Y 1 A LYS 421 ? CE  ? A LYS 400 CE  
468 1 Y 1 A LYS 421 ? NZ  ? A LYS 400 NZ  
469 1 Y 1 A LYS 422 ? CG  ? A LYS 401 CG  
470 1 Y 1 A LYS 422 ? CD  ? A LYS 401 CD  
471 1 Y 1 A LYS 422 ? CE  ? A LYS 401 CE  
472 1 Y 1 A LYS 422 ? NZ  ? A LYS 401 NZ  
473 1 Y 1 A LYS 424 ? CG  ? A LYS 403 CG  
474 1 Y 1 A LYS 424 ? CD  ? A LYS 403 CD  
475 1 Y 1 A LYS 424 ? CE  ? A LYS 403 CE  
476 1 Y 1 A LYS 424 ? NZ  ? A LYS 403 NZ  
477 1 Y 1 A ASP 425 ? CG  ? A ASP 404 CG  
478 1 Y 1 A ASP 425 ? OD1 ? A ASP 404 OD1 
479 1 Y 1 A ASP 425 ? OD2 ? A ASP 404 OD2 
480 1 Y 1 A ARG 446 ? CG  ? A ARG 425 CG  
481 1 Y 1 A ARG 446 ? CD  ? A ARG 425 CD  
482 1 Y 1 A ARG 446 ? NE  ? A ARG 425 NE  
483 1 Y 1 A ARG 446 ? CZ  ? A ARG 425 CZ  
484 1 Y 1 A ARG 446 ? NH1 ? A ARG 425 NH1 
485 1 Y 1 A ARG 446 ? NH2 ? A ARG 425 NH2 
486 1 Y 1 A MET 450 ? CG  ? A MET 429 CG  
487 1 Y 1 A MET 450 ? SD  ? A MET 429 SD  
488 1 Y 1 A MET 450 ? CE  ? A MET 429 CE  
489 1 Y 1 A LYS 453 ? CG  ? A LYS 432 CG  
490 1 Y 1 A LYS 453 ? CD  ? A LYS 432 CD  
491 1 Y 1 A LYS 453 ? CE  ? A LYS 432 CE  
492 1 Y 1 A LYS 453 ? NZ  ? A LYS 432 NZ  
493 1 Y 1 A LEU 454 ? CG  ? A LEU 433 CG  
494 1 Y 1 A LEU 454 ? CD1 ? A LEU 433 CD1 
495 1 Y 1 A LEU 454 ? CD2 ? A LEU 433 CD2 
496 1 Y 1 A LEU 456 ? CG  ? A LEU 435 CG  
497 1 Y 1 A LEU 456 ? CD1 ? A LEU 435 CD1 
498 1 Y 1 A LEU 456 ? CD2 ? A LEU 435 CD2 
499 1 Y 1 A ILE 457 ? CG1 ? A ILE 436 CG1 
500 1 Y 1 A ILE 457 ? CG2 ? A ILE 436 CG2 
501 1 Y 1 A ILE 457 ? CD1 ? A ILE 436 CD1 
502 1 Y 1 A ARG 458 ? CG  ? A ARG 437 CG  
503 1 Y 1 A ARG 458 ? CD  ? A ARG 437 CD  
504 1 Y 1 A ARG 458 ? NE  ? A ARG 437 NE  
505 1 Y 1 A ARG 458 ? CZ  ? A ARG 437 CZ  
506 1 Y 1 A ARG 458 ? NH1 ? A ARG 437 NH1 
507 1 Y 1 A ARG 458 ? NH2 ? A ARG 437 NH2 
508 1 Y 1 A VAL 459 ? CG1 ? A VAL 438 CG1 
509 1 Y 1 A VAL 459 ? CG2 ? A VAL 438 CG2 
510 1 Y 1 A LEU 460 ? CG  ? A LEU 439 CG  
511 1 Y 1 A LEU 460 ? CD1 ? A LEU 439 CD1 
512 1 Y 1 A LEU 460 ? CD2 ? A LEU 439 CD2 
513 1 Y 1 A SER 464 ? OG  ? A SER 443 OG  
514 1 Y 1 A LYS 466 ? CG  ? A LYS 445 CG  
515 1 Y 1 A LYS 466 ? CD  ? A LYS 445 CD  
516 1 Y 1 A LYS 466 ? CE  ? A LYS 445 CE  
517 1 Y 1 A LYS 466 ? NZ  ? A LYS 445 NZ  
518 1 Y 1 A LYS 469 ? CG  ? A LYS 448 CG  
519 1 Y 1 A LYS 469 ? CD  ? A LYS 448 CD  
520 1 Y 1 A LYS 469 ? CE  ? A LYS 448 CE  
521 1 Y 1 A LYS 469 ? NZ  ? A LYS 448 NZ  
522 1 Y 1 A GLN 472 ? CG  ? A GLN 451 CG  
523 1 Y 1 A GLN 472 ? CD  ? A GLN 451 CD  
524 1 Y 1 A GLN 472 ? OE1 ? A GLN 451 OE1 
525 1 Y 1 A GLN 472 ? NE2 ? A GLN 451 NE2 
526 1 Y 1 A ILE 473 ? CG1 ? A ILE 452 CG1 
527 1 Y 1 A ILE 473 ? CG2 ? A ILE 452 CG2 
528 1 Y 1 A ILE 473 ? CD1 ? A ILE 452 CD1 
529 1 Y 1 A LEU 475 ? CG  ? A LEU 454 CG  
530 1 Y 1 A LEU 475 ? CD1 ? A LEU 454 CD1 
531 1 Y 1 A LEU 475 ? CD2 ? A LEU 454 CD2 
532 1 Y 1 A LYS 476 ? CG  ? A LYS 455 CG  
533 1 Y 1 A LYS 476 ? CD  ? A LYS 455 CD  
534 1 Y 1 A LYS 476 ? CE  ? A LYS 455 CE  
535 1 Y 1 A LYS 476 ? NZ  ? A LYS 455 NZ  
536 1 Y 1 A GLU 486 ? CG  ? A GLU 465 CG  
537 1 Y 1 A GLU 486 ? CD  ? A GLU 465 CD  
538 1 Y 1 A GLU 486 ? OE1 ? A GLU 465 OE1 
539 1 Y 1 A GLU 486 ? OE2 ? A GLU 465 OE2 
540 1 Y 1 A LYS 487 ? CG  ? A LYS 466 CG  
541 1 Y 1 A LYS 487 ? CD  ? A LYS 466 CD  
542 1 Y 1 A LYS 487 ? CE  ? A LYS 466 CE  
543 1 Y 1 A LYS 487 ? NZ  ? A LYS 466 NZ  
544 1 Y 1 A VAL 490 ? CG1 ? A VAL 469 CG1 
545 1 Y 1 A VAL 490 ? CG2 ? A VAL 469 CG2 
546 1 Y 1 A LEU 491 ? CG  ? A LEU 470 CG  
547 1 Y 1 A LEU 491 ? CD1 ? A LEU 470 CD1 
548 1 Y 1 A LEU 491 ? CD2 ? A LEU 470 CD2 
549 1 Y 1 A LYS 492 ? CG  ? A LYS 471 CG  
550 1 Y 1 A LYS 492 ? CD  ? A LYS 471 CD  
551 1 Y 1 A LYS 492 ? CE  ? A LYS 471 CE  
552 1 Y 1 A LYS 492 ? NZ  ? A LYS 471 NZ  
553 1 Y 1 A ARG 496 ? CG  ? A ARG 475 CG  
554 1 Y 1 A ARG 496 ? CD  ? A ARG 475 CD  
555 1 Y 1 A ARG 496 ? NE  ? A ARG 475 NE  
556 1 Y 1 A ARG 496 ? CZ  ? A ARG 475 CZ  
557 1 Y 1 A ARG 496 ? NH1 ? A ARG 475 NH1 
558 1 Y 1 A ARG 496 ? NH2 ? A ARG 475 NH2 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX  ? ? ? '(1.20.1_4487)' 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .               2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .               3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHENIX  ? ? ? .               4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9MS1 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     75.772 
_cell.length_a_esd                 ? 
_cell.length_b                     100.654 
_cell.length_b_esd                 ? 
_cell.length_c                     121.133 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9MS1 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                23 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'I 2 2 2' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9MS1 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.08 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          40.79 
_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, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              7.0 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.1 M HEPES, pH 7.0, 10-12% PEG 3350' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER X 9M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2024-09-18 
_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                    'SI(111)' 
_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   0.92012 
_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                        'NSLS-II BEAMLINE 17-ID-1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.92012 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   17-ID-1 
_diffrn_source.pdbx_synchrotron_site       NSLS-II 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9MS1 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              3.40 
_reflns.d_resolution_low                               30.27 
_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                                     6641 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.8 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                5.7 
_reflns.pdbx_netI_over_av_sigmaI                       6.4 
_reflns.pdbx_netI_over_sigmaI                          6.4 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               1.08 
_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                                0.192 
_reflns.pdbx_Rpim_I_all                                0.078 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.997 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.160 
_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                                    3.40 
_reflns_shell.d_res_low                                     3.67 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.5 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             1348 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               5.6 
_reflns_shell.pdbx_chi_squared                              1.06 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               1.760 
_reflns_shell.pdbx_Rpim_I_all                               0.716 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.655 
_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                                  1.598 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9MS1 
_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                            3.40 
_refine.ls_d_res_low                             30.27 
_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                     6575 
_refine.ls_number_reflns_R_free                  334 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    98.90 
_refine.ls_percent_reflns_R_free                 5.08 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2849 
_refine.ls_R_factor_R_free                       0.2970 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2841 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.34 
_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       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.10 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 35.56 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.44 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        3086 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         77 
_refine_hist.number_atoms_solvent             0 
_refine_hist.number_atoms_total               3163 
_refine_hist.d_res_high                       3.40 
_refine_hist.d_res_low                        30.27 
# 
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' ? 0.004  ? 3249 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.668  ? 4485 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 11.887 ? 1021 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.049  ? 510  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.012  ? 595  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 3.40 3.52  . . 40 611 100.00 . . . . 0.3728 . . . . . . . . . . . 0.4812 
'X-RAY DIFFRACTION' 3.52 3.66  . . 32 615 100.00 . . . . 0.3514 . . . . . . . . . . . 0.3630 
'X-RAY DIFFRACTION' 3.66 3.83  . . 33 618 100.00 . . . . 0.3270 . . . . . . . . . . . 0.3273 
'X-RAY DIFFRACTION' 3.83 4.03  . . 31 626 100.00 . . . . 0.3351 . . . . . . . . . . . 0.3406 
'X-RAY DIFFRACTION' 4.03 4.28  . . 33 617 100.00 . . . . 0.3068 . . . . . . . . . . . 0.3446 
'X-RAY DIFFRACTION' 4.28 4.61  . . 36 630 99.00  . . . . 0.3229 . . . . . . . . . . . 0.3301 
'X-RAY DIFFRACTION' 5.07 5.80  . . 34 619 97.00  . . . . 0.3183 . . . . . . . . . . . 0.3355 
'X-RAY DIFFRACTION' 5.80 7.29  . . 31 624 97.00  . . . . 0.2932 . . . . . . . . . . . 0.3201 
'X-RAY DIFFRACTION' 7.30 30.27 . . 35 660 97.00  . . . . 0.1971 . . . . . . . . . . . 0.2357 
# 
_struct.entry_id                     9MS1 
_struct.title                        'Crystal structure of human CYP3A4 in complex with SJYHJ-111' 
_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        9MS1 
_struct_keywords.text            
'Cytochrome P450 3A4, CYP3A4, CYP3A4-selective inhibitor, drug metabolizing enzyme, OXIDOREDUCTASE, OXIDOREDUCTASE-INHIBITOR complex' 
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE/INHIBITOR 
# 
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 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    CP3A4_HUMAN 
_struct_ref.pdbx_db_accession          P08684 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;LYGTHSHGLFKKLGIPGPTPLPFLGNILSYHKGFCMFDMECHKKYGKVWGFYDGQQPVLAITDPDMIKTVLVKECYSVFT
NRRPFGPVGFMKSAISIAEDEEWKRLRSLLSPTFTSGKLKEMVPIIAQYGDVLVRNLRREAETGKPVTLKDVFGAYSMDV
ITSTSFGVNIDSLNNPQDPFVENTKKLLRFDFLDPFFLSITVFPFLIPILEVLNICVFPREVTNFLRKSVKRMKESRLED
TQKHRVDFLQLMIDSQNSKETESHKALSDLELVAQSIIFIFAGYETTSSVLSFIMYELATHPDVQQKLQEEIDAVLPNKA
PPTYDTVLQMEYLDMVVNETLRLFPIAMRLERVCKKDVEINGMFIPKGVVVMIPSYALHRDPKYWTEPEKFLPERFSKKN
KDNIDPYIYTPFGSGPRNCIGMRFALMNMKLALIRVLQNFSFKPCKETQIPLKLSLGGLLQPEKPVVLKVESRDGTVSGA

;
_struct_ref.pdbx_align_begin           24 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9MS1 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 3 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 482 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             P08684 
_struct_ref_seq.db_align_beg                  24 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  503 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       24 
_struct_ref_seq.pdbx_auth_seq_align_end       503 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 9MS1 MET A 1   ? UNP P08684 ? ? 'initiating methionine' 22  1 
1 9MS1 ALA A 2   ? UNP P08684 ? ? 'expression tag'        23  2 
1 9MS1 HIS A 483 ? UNP P08684 ? ? 'expression tag'        504 3 
1 9MS1 HIS A 484 ? UNP P08684 ? ? 'expression tag'        505 4 
1 9MS1 HIS A 485 ? UNP P08684 ? ? 'expression tag'        506 5 
1 9MS1 HIS A 486 ? UNP P08684 ? ? 'expression tag'        507 6 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_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_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 GLY A 10  ? LEU A 15  ? GLY A 31  LEU A 36  1 ? 6  
HELX_P HELX_P2  AA2 ASN A 28  ? HIS A 33  ? ASN A 49  HIS A 54  5 ? 6  
HELX_P HELX_P3  AA3 LYS A 34  ? TYR A 47  ? LYS A 55  TYR A 68  1 ? 14 
HELX_P HELX_P4  AA4 ASP A 65  ? VAL A 74  ? ASP A 86  VAL A 95  1 ? 10 
HELX_P HELX_P5  AA5 GLY A 91  ? ALA A 96  ? GLY A 112 ALA A 117 5 ? 6  
HELX_P HELX_P6  AA6 ASP A 102 ? SER A 113 ? ASP A 123 SER A 134 1 ? 12 
HELX_P HELX_P7  AA7 PRO A 114 ? PHE A 116 ? PRO A 135 PHE A 137 5 ? 3  
HELX_P HELX_P8  AA8 THR A 117 ? GLU A 123 ? THR A 138 GLU A 144 1 ? 7  
HELX_P HELX_P9  AA9 MET A 124 ? VAL A 125 ? MET A 145 VAL A 146 5 ? 2  
HELX_P HELX_P10 AB1 PRO A 126 ? ILE A 128 ? PRO A 147 ILE A 149 5 ? 3  
HELX_P HELX_P11 AB2 ALA A 129 ? GLU A 144 ? ALA A 150 GLU A 165 1 ? 16 
HELX_P HELX_P12 AB3 LEU A 151 ? PHE A 168 ? LEU A 172 PHE A 189 1 ? 18 
HELX_P HELX_P13 AB4 ASP A 180 ? LEU A 189 ? ASP A 201 LEU A 210 1 ? 10 
HELX_P HELX_P14 AB5 ASP A 196 ? PHE A 205 ? ASP A 217 PHE A 226 1 ? 10 
HELX_P HELX_P15 AB6 PHE A 207 ? LEU A 215 ? PHE A 228 LEU A 236 1 ? 9  
HELX_P HELX_P16 AB7 PRO A 221 ? LEU A 240 ? PRO A 242 LEU A 261 1 ? 20 
HELX_P HELX_P17 AB8 ASP A 249 ? ASN A 259 ? ASP A 270 ASN A 280 1 ? 11 
HELX_P HELX_P18 AB9 SER A 270 ? GLY A 285 ? SER A 291 GLY A 306 1 ? 16 
HELX_P HELX_P19 AC1 TYR A 286 ? HIS A 303 ? TYR A 307 HIS A 324 1 ? 18 
HELX_P HELX_P20 AC2 HIS A 303 ? LEU A 318 ? HIS A 324 LEU A 339 1 ? 16 
HELX_P HELX_P21 AC3 THR A 325 ? LEU A 330 ? THR A 346 LEU A 351 1 ? 6  
HELX_P HELX_P22 AC4 MET A 332 ? PHE A 346 ? MET A 353 PHE A 367 1 ? 15 
HELX_P HELX_P23 AC5 PRO A 376 ? ARG A 382 ? PRO A 397 ARG A 403 1 ? 7  
HELX_P HELX_P24 AC6 LEU A 394 ? SER A 399 ? LEU A 415 SER A 420 5 ? 6  
HELX_P HELX_P25 AC7 GLY A 423 ? GLN A 440 ? GLY A 444 GLN A 461 1 ? 18 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1 metalc ? ? A CYS 421 SG ? ? ? 1_555 B HEM   . FE  ? ? A CYS 442 A HEM   601 1_555 ? ? ? ? ? ? ? 2.254 ? ? 
metalc2 metalc ? ? B HEM .   FE ? ? ? 1_555 C A1BNX . N33 ? ? A HEM 601 A A1BNX 602 1_555 ? ? ? ? ? ? ? 2.356 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  SG ? A CYS 421 ? A CYS 442 ? 1_555 FE ? B HEM . ? A HEM 601 ? 1_555 NA  ? B HEM   . ? A HEM   601 ? 1_555 100.5 ? 
2  SG ? A CYS 421 ? A CYS 442 ? 1_555 FE ? B HEM . ? A HEM 601 ? 1_555 NB  ? B HEM   . ? A HEM   601 ? 1_555 83.3  ? 
3  NA ? B HEM .   ? A HEM 601 ? 1_555 FE ? B HEM . ? A HEM 601 ? 1_555 NB  ? B HEM   . ? A HEM   601 ? 1_555 88.3  ? 
4  SG ? A CYS 421 ? A CYS 442 ? 1_555 FE ? B HEM . ? A HEM 601 ? 1_555 NC  ? B HEM   . ? A HEM   601 ? 1_555 83.2  ? 
5  NA ? B HEM .   ? A HEM 601 ? 1_555 FE ? B HEM . ? A HEM 601 ? 1_555 NC  ? B HEM   . ? A HEM   601 ? 1_555 176.1 ? 
6  NB ? B HEM .   ? A HEM 601 ? 1_555 FE ? B HEM . ? A HEM 601 ? 1_555 NC  ? B HEM   . ? A HEM   601 ? 1_555 93.3  ? 
7  SG ? A CYS 421 ? A CYS 442 ? 1_555 FE ? B HEM . ? A HEM 601 ? 1_555 ND  ? B HEM   . ? A HEM   601 ? 1_555 100.3 ? 
8  NA ? B HEM .   ? A HEM 601 ? 1_555 FE ? B HEM . ? A HEM 601 ? 1_555 ND  ? B HEM   . ? A HEM   601 ? 1_555 90.2  ? 
9  NB ? B HEM .   ? A HEM 601 ? 1_555 FE ? B HEM . ? A HEM 601 ? 1_555 ND  ? B HEM   . ? A HEM   601 ? 1_555 176.3 ? 
10 NC ? B HEM .   ? A HEM 601 ? 1_555 FE ? B HEM . ? A HEM 601 ? 1_555 ND  ? B HEM   . ? A HEM   601 ? 1_555 88.0  ? 
11 SG ? A CYS 421 ? A CYS 442 ? 1_555 FE ? B HEM . ? A HEM 601 ? 1_555 N33 ? C A1BNX . ? A A1BNX 602 ? 1_555 171.5 ? 
12 NA ? B HEM .   ? A HEM 601 ? 1_555 FE ? B HEM . ? A HEM 601 ? 1_555 N33 ? C A1BNX . ? A A1BNX 602 ? 1_555 86.9  ? 
13 NB ? B HEM .   ? A HEM 601 ? 1_555 FE ? B HEM . ? A HEM 601 ? 1_555 N33 ? C A1BNX . ? A A1BNX 602 ? 1_555 101.2 ? 
14 NC ? B HEM .   ? A HEM 601 ? 1_555 FE ? B HEM . ? A HEM 601 ? 1_555 N33 ? C A1BNX . ? A A1BNX 602 ? 1_555 89.3  ? 
15 ND ? B HEM .   ? A HEM 601 ? 1_555 FE ? B HEM . ? A HEM 601 ? 1_555 N33 ? C A1BNX . ? A A1BNX 602 ? 1_555 75.3  ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 3 ? 
AA3 ? 2 ? 
# 
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 ? parallel      
AA1 3 4 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA3 1 2 ? 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 VAL A 50  ? ASP A 55  ? VAL A 71  ASP A 76  
AA1 2 GLN A 58  ? ILE A 63  ? GLN A 79  ILE A 84  
AA1 3 VAL A 371 ? ILE A 375 ? VAL A 392 ILE A 396 
AA1 4 LEU A 352 ? CYS A 356 ? LEU A 373 CYS A 377 
AA2 1 VAL A 149 ? THR A 150 ? VAL A 170 THR A 171 
AA2 2 VAL A 469 ? GLU A 473 ? VAL A 490 GLU A 494 
AA2 3 SER A 443 ? LYS A 445 ? SER A 464 LYS A 466 
AA3 1 VAL A 360 ? GLU A 361 ? VAL A 381 GLU A 382 
AA3 2 PHE A 366 ? ILE A 367 ? PHE A 387 ILE A 388 
# 
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 TRP A 51  ? N TRP A 72  O ALA A 62  ? O ALA A 83  
AA1 2 3 N LEU A 61  ? N LEU A 82  O MET A 374 ? O MET A 395 
AA1 3 4 O VAL A 373 ? O VAL A 394 N ARG A 354 ? N ARG A 375 
AA2 1 2 N VAL A 149 ? N VAL A 170 O LEU A 470 ? O LEU A 491 
AA2 2 3 O LYS A 471 ? O LYS A 492 N LYS A 445 ? N LYS A 466 
AA3 1 2 N VAL A 360 ? N VAL A 381 O ILE A 367 ? O ILE A 388 
# 
_pdbx_entry_details.entry_id                   9MS1 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 PHE A 46  ? ? 66.90   -12.78  
2  1 GLU A 97  ? ? -98.18  48.79   
3  1 PRO A 110 ? ? -75.65  38.16   
4  1 ASP A 123 ? ? 59.81   -118.21 
5  1 PHE A 189 ? ? -134.65 -158.43 
6  1 PRO A 199 ? ? -87.70  50.00   
7  1 LYS A 288 ? ? -100.51 -165.60 
8  1 TYR A 307 ? ? -110.80 -90.18  
9  1 MET A 353 ? ? -66.48  99.25   
10 1 MET A 371 ? ? 73.94   -15.86  
# 
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 22  ? A MET 1   
2  1 Y 1 A ALA 23  ? A ALA 2   
3  1 Y 1 A LEU 24  ? A LEU 3   
4  1 Y 1 A TYR 25  ? A TYR 4   
5  1 Y 1 A GLY 26  ? A GLY 5   
6  1 Y 1 A THR 27  ? A THR 6   
7  1 Y 1 A LEU 211 ? A LEU 190 
8  1 Y 1 A ARG 212 ? A ARG 191 
9  1 Y 1 A PHE 213 ? A PHE 192 
10 1 Y 1 A ASP 214 ? A ASP 193 
11 1 Y 1 A PHE 215 ? A PHE 194 
12 1 Y 1 A GLU 262 ? A GLU 241 
13 1 Y 1 A ASP 263 ? A ASP 242 
14 1 Y 1 A THR 264 ? A THR 243 
15 1 Y 1 A GLN 265 ? A GLN 244 
16 1 Y 1 A SER 281 ? A SER 260 
17 1 Y 1 A LYS 282 ? A LYS 261 
18 1 Y 1 A GLU 283 ? A GLU 262 
19 1 Y 1 A THR 284 ? A THR 263 
20 1 Y 1 A GLU 285 ? A GLU 264 
21 1 Y 1 A SER 286 ? A SER 265 
22 1 Y 1 A GLU 470 ? A GLU 449 
23 1 Y 1 A ASP 497 ? A ASP 476 
24 1 Y 1 A GLY 498 ? A GLY 477 
25 1 Y 1 A THR 499 ? A THR 478 
26 1 Y 1 A VAL 500 ? A VAL 479 
27 1 Y 1 A SER 501 ? A SER 480 
28 1 Y 1 A GLY 502 ? A GLY 481 
29 1 Y 1 A ALA 503 ? A ALA 482 
30 1 Y 1 A HIS 504 ? A HIS 483 
31 1 Y 1 A HIS 505 ? A HIS 484 
32 1 Y 1 A HIS 506 ? A HIS 485 
33 1 Y 1 A HIS 507 ? A HIS 486 
# 
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 
A1BNX C12  C  N N 1   
A1BNX C13  C  Y N 2   
A1BNX C14  C  Y N 3   
A1BNX C15  C  Y N 4   
A1BNX C16  C  Y N 5   
A1BNX C21  C  Y N 6   
A1BNX C20  C  Y N 7   
A1BNX C17  C  Y N 8   
A1BNX C23  C  N N 9   
A1BNX C02  C  N N 10  
A1BNX C04  C  Y N 11  
A1BNX C05  C  Y N 12  
A1BNX C06  C  Y N 13  
A1BNX C07  C  Y N 14  
A1BNX C08  C  Y N 15  
A1BNX C09  C  Y N 16  
A1BNX C19  C  Y N 17  
A1BNX C22  C  Y N 18  
A1BNX C27  C  Y N 19  
A1BNX C28  C  Y N 20  
A1BNX C29  C  Y N 21  
A1BNX C31  C  Y N 22  
A1BNX C32  C  Y N 23  
A1BNX C34  C  Y N 24  
A1BNX F24  F  N N 25  
A1BNX F25  F  N N 26  
A1BNX F26  F  N N 27  
A1BNX N03  N  N N 28  
A1BNX N11  N  N N 29  
A1BNX N30  N  Y N 30  
A1BNX N33  N  Y N 31  
A1BNX O01  O  N N 32  
A1BNX O18  O  N N 33  
A1BNX CL10 CL N N 34  
A1BNX H1   H  N N 35  
A1BNX H2   H  N N 36  
A1BNX H3   H  N N 37  
A1BNX H4   H  N N 38  
A1BNX H5   H  N N 39  
A1BNX H6   H  N N 40  
A1BNX H7   H  N N 41  
A1BNX H8   H  N N 42  
A1BNX H9   H  N N 43  
A1BNX H10  H  N N 44  
A1BNX H11  H  N N 45  
A1BNX H12  H  N N 46  
A1BNX H13  H  N N 47  
A1BNX H14  H  N N 48  
A1BNX H15  H  N N 49  
A1BNX H16  H  N N 50  
A1BNX H17  H  N N 51  
A1BNX H18  H  N N 52  
ALA   N    N  N N 53  
ALA   CA   C  N S 54  
ALA   C    C  N N 55  
ALA   O    O  N N 56  
ALA   CB   C  N N 57  
ALA   OXT  O  N N 58  
ALA   H    H  N N 59  
ALA   H2   H  N N 60  
ALA   HA   H  N N 61  
ALA   HB1  H  N N 62  
ALA   HB2  H  N N 63  
ALA   HB3  H  N N 64  
ALA   HXT  H  N N 65  
ARG   N    N  N N 66  
ARG   CA   C  N S 67  
ARG   C    C  N N 68  
ARG   O    O  N N 69  
ARG   CB   C  N N 70  
ARG   CG   C  N N 71  
ARG   CD   C  N N 72  
ARG   NE   N  N N 73  
ARG   CZ   C  N N 74  
ARG   NH1  N  N N 75  
ARG   NH2  N  N N 76  
ARG   OXT  O  N N 77  
ARG   H    H  N N 78  
ARG   H2   H  N N 79  
ARG   HA   H  N N 80  
ARG   HB2  H  N N 81  
ARG   HB3  H  N N 82  
ARG   HG2  H  N N 83  
ARG   HG3  H  N N 84  
ARG   HD2  H  N N 85  
ARG   HD3  H  N N 86  
ARG   HE   H  N N 87  
ARG   HH11 H  N N 88  
ARG   HH12 H  N N 89  
ARG   HH21 H  N N 90  
ARG   HH22 H  N N 91  
ARG   HXT  H  N N 92  
ASN   N    N  N N 93  
ASN   CA   C  N S 94  
ASN   C    C  N N 95  
ASN   O    O  N N 96  
ASN   CB   C  N N 97  
ASN   CG   C  N N 98  
ASN   OD1  O  N N 99  
ASN   ND2  N  N N 100 
ASN   OXT  O  N N 101 
ASN   H    H  N N 102 
ASN   H2   H  N N 103 
ASN   HA   H  N N 104 
ASN   HB2  H  N N 105 
ASN   HB3  H  N N 106 
ASN   HD21 H  N N 107 
ASN   HD22 H  N N 108 
ASN   HXT  H  N N 109 
ASP   N    N  N N 110 
ASP   CA   C  N S 111 
ASP   C    C  N N 112 
ASP   O    O  N N 113 
ASP   CB   C  N N 114 
ASP   CG   C  N N 115 
ASP   OD1  O  N N 116 
ASP   OD2  O  N N 117 
ASP   OXT  O  N N 118 
ASP   H    H  N N 119 
ASP   H2   H  N N 120 
ASP   HA   H  N N 121 
ASP   HB2  H  N N 122 
ASP   HB3  H  N N 123 
ASP   HD2  H  N N 124 
ASP   HXT  H  N N 125 
CYS   N    N  N N 126 
CYS   CA   C  N R 127 
CYS   C    C  N N 128 
CYS   O    O  N N 129 
CYS   CB   C  N N 130 
CYS   SG   S  N N 131 
CYS   OXT  O  N N 132 
CYS   H    H  N N 133 
CYS   H2   H  N N 134 
CYS   HA   H  N N 135 
CYS   HB2  H  N N 136 
CYS   HB3  H  N N 137 
CYS   HG   H  N N 138 
CYS   HXT  H  N N 139 
GLN   N    N  N N 140 
GLN   CA   C  N S 141 
GLN   C    C  N N 142 
GLN   O    O  N N 143 
GLN   CB   C  N N 144 
GLN   CG   C  N N 145 
GLN   CD   C  N N 146 
GLN   OE1  O  N N 147 
GLN   NE2  N  N N 148 
GLN   OXT  O  N N 149 
GLN   H    H  N N 150 
GLN   H2   H  N N 151 
GLN   HA   H  N N 152 
GLN   HB2  H  N N 153 
GLN   HB3  H  N N 154 
GLN   HG2  H  N N 155 
GLN   HG3  H  N N 156 
GLN   HE21 H  N N 157 
GLN   HE22 H  N N 158 
GLN   HXT  H  N N 159 
GLU   N    N  N N 160 
GLU   CA   C  N S 161 
GLU   C    C  N N 162 
GLU   O    O  N N 163 
GLU   CB   C  N N 164 
GLU   CG   C  N N 165 
GLU   CD   C  N N 166 
GLU   OE1  O  N N 167 
GLU   OE2  O  N N 168 
GLU   OXT  O  N N 169 
GLU   H    H  N N 170 
GLU   H2   H  N N 171 
GLU   HA   H  N N 172 
GLU   HB2  H  N N 173 
GLU   HB3  H  N N 174 
GLU   HG2  H  N N 175 
GLU   HG3  H  N N 176 
GLU   HE2  H  N N 177 
GLU   HXT  H  N N 178 
GLY   N    N  N N 179 
GLY   CA   C  N N 180 
GLY   C    C  N N 181 
GLY   O    O  N N 182 
GLY   OXT  O  N N 183 
GLY   H    H  N N 184 
GLY   H2   H  N N 185 
GLY   HA2  H  N N 186 
GLY   HA3  H  N N 187 
GLY   HXT  H  N N 188 
HEM   CHA  C  N N 189 
HEM   CHB  C  N N 190 
HEM   CHC  C  N N 191 
HEM   CHD  C  N N 192 
HEM   C1A  C  Y N 193 
HEM   C2A  C  Y N 194 
HEM   C3A  C  Y N 195 
HEM   C4A  C  Y N 196 
HEM   CMA  C  N N 197 
HEM   CAA  C  N N 198 
HEM   CBA  C  N N 199 
HEM   CGA  C  N N 200 
HEM   O1A  O  N N 201 
HEM   O2A  O  N N 202 
HEM   C1B  C  N N 203 
HEM   C2B  C  N N 204 
HEM   C3B  C  N N 205 
HEM   C4B  C  N N 206 
HEM   CMB  C  N N 207 
HEM   CAB  C  N N 208 
HEM   CBB  C  N N 209 
HEM   C1C  C  Y N 210 
HEM   C2C  C  Y N 211 
HEM   C3C  C  Y N 212 
HEM   C4C  C  Y N 213 
HEM   CMC  C  N N 214 
HEM   CAC  C  N N 215 
HEM   CBC  C  N N 216 
HEM   C1D  C  N N 217 
HEM   C2D  C  N N 218 
HEM   C3D  C  N N 219 
HEM   C4D  C  N N 220 
HEM   CMD  C  N N 221 
HEM   CAD  C  N N 222 
HEM   CBD  C  N N 223 
HEM   CGD  C  N N 224 
HEM   O1D  O  N N 225 
HEM   O2D  O  N N 226 
HEM   NA   N  Y N 227 
HEM   NB   N  N N 228 
HEM   NC   N  Y N 229 
HEM   ND   N  N N 230 
HEM   FE   FE N N 231 
HEM   HHB  H  N N 232 
HEM   HHC  H  N N 233 
HEM   HHD  H  N N 234 
HEM   HMA  H  N N 235 
HEM   HMAA H  N N 236 
HEM   HMAB H  N N 237 
HEM   HAA  H  N N 238 
HEM   HAAA H  N N 239 
HEM   HBA  H  N N 240 
HEM   HBAA H  N N 241 
HEM   HMB  H  N N 242 
HEM   HMBA H  N N 243 
HEM   HMBB H  N N 244 
HEM   HAB  H  N N 245 
HEM   HBB  H  N N 246 
HEM   HBBA H  N N 247 
HEM   HMC  H  N N 248 
HEM   HMCA H  N N 249 
HEM   HMCB H  N N 250 
HEM   HAC  H  N N 251 
HEM   HBC  H  N N 252 
HEM   HBCA H  N N 253 
HEM   HMD  H  N N 254 
HEM   HMDA H  N N 255 
HEM   HMDB H  N N 256 
HEM   HAD  H  N N 257 
HEM   HADA H  N N 258 
HEM   HBD  H  N N 259 
HEM   HBDA H  N N 260 
HEM   H2A  H  N N 261 
HEM   H2D  H  N N 262 
HEM   HHA  H  N N 263 
HIS   N    N  N N 264 
HIS   CA   C  N S 265 
HIS   C    C  N N 266 
HIS   O    O  N N 267 
HIS   CB   C  N N 268 
HIS   CG   C  Y N 269 
HIS   ND1  N  Y N 270 
HIS   CD2  C  Y N 271 
HIS   CE1  C  Y N 272 
HIS   NE2  N  Y N 273 
HIS   OXT  O  N N 274 
HIS   H    H  N N 275 
HIS   H2   H  N N 276 
HIS   HA   H  N N 277 
HIS   HB2  H  N N 278 
HIS   HB3  H  N N 279 
HIS   HD1  H  N N 280 
HIS   HD2  H  N N 281 
HIS   HE1  H  N N 282 
HIS   HE2  H  N N 283 
HIS   HXT  H  N N 284 
ILE   N    N  N N 285 
ILE   CA   C  N S 286 
ILE   C    C  N N 287 
ILE   O    O  N N 288 
ILE   CB   C  N S 289 
ILE   CG1  C  N N 290 
ILE   CG2  C  N N 291 
ILE   CD1  C  N N 292 
ILE   OXT  O  N N 293 
ILE   H    H  N N 294 
ILE   H2   H  N N 295 
ILE   HA   H  N N 296 
ILE   HB   H  N N 297 
ILE   HG12 H  N N 298 
ILE   HG13 H  N N 299 
ILE   HG21 H  N N 300 
ILE   HG22 H  N N 301 
ILE   HG23 H  N N 302 
ILE   HD11 H  N N 303 
ILE   HD12 H  N N 304 
ILE   HD13 H  N N 305 
ILE   HXT  H  N N 306 
LEU   N    N  N N 307 
LEU   CA   C  N S 308 
LEU   C    C  N N 309 
LEU   O    O  N N 310 
LEU   CB   C  N N 311 
LEU   CG   C  N N 312 
LEU   CD1  C  N N 313 
LEU   CD2  C  N N 314 
LEU   OXT  O  N N 315 
LEU   H    H  N N 316 
LEU   H2   H  N N 317 
LEU   HA   H  N N 318 
LEU   HB2  H  N N 319 
LEU   HB3  H  N N 320 
LEU   HG   H  N N 321 
LEU   HD11 H  N N 322 
LEU   HD12 H  N N 323 
LEU   HD13 H  N N 324 
LEU   HD21 H  N N 325 
LEU   HD22 H  N N 326 
LEU   HD23 H  N N 327 
LEU   HXT  H  N N 328 
LYS   N    N  N N 329 
LYS   CA   C  N S 330 
LYS   C    C  N N 331 
LYS   O    O  N N 332 
LYS   CB   C  N N 333 
LYS   CG   C  N N 334 
LYS   CD   C  N N 335 
LYS   CE   C  N N 336 
LYS   NZ   N  N N 337 
LYS   OXT  O  N N 338 
LYS   H    H  N N 339 
LYS   H2   H  N N 340 
LYS   HA   H  N N 341 
LYS   HB2  H  N N 342 
LYS   HB3  H  N N 343 
LYS   HG2  H  N N 344 
LYS   HG3  H  N N 345 
LYS   HD2  H  N N 346 
LYS   HD3  H  N N 347 
LYS   HE2  H  N N 348 
LYS   HE3  H  N N 349 
LYS   HZ1  H  N N 350 
LYS   HZ2  H  N N 351 
LYS   HZ3  H  N N 352 
LYS   HXT  H  N N 353 
MET   N    N  N N 354 
MET   CA   C  N S 355 
MET   C    C  N N 356 
MET   O    O  N N 357 
MET   CB   C  N N 358 
MET   CG   C  N N 359 
MET   SD   S  N N 360 
MET   CE   C  N N 361 
MET   OXT  O  N N 362 
MET   H    H  N N 363 
MET   H2   H  N N 364 
MET   HA   H  N N 365 
MET   HB2  H  N N 366 
MET   HB3  H  N N 367 
MET   HG2  H  N N 368 
MET   HG3  H  N N 369 
MET   HE1  H  N N 370 
MET   HE2  H  N N 371 
MET   HE3  H  N N 372 
MET   HXT  H  N N 373 
PHE   N    N  N N 374 
PHE   CA   C  N S 375 
PHE   C    C  N N 376 
PHE   O    O  N N 377 
PHE   CB   C  N N 378 
PHE   CG   C  Y N 379 
PHE   CD1  C  Y N 380 
PHE   CD2  C  Y N 381 
PHE   CE1  C  Y N 382 
PHE   CE2  C  Y N 383 
PHE   CZ   C  Y N 384 
PHE   OXT  O  N N 385 
PHE   H    H  N N 386 
PHE   H2   H  N N 387 
PHE   HA   H  N N 388 
PHE   HB2  H  N N 389 
PHE   HB3  H  N N 390 
PHE   HD1  H  N N 391 
PHE   HD2  H  N N 392 
PHE   HE1  H  N N 393 
PHE   HE2  H  N N 394 
PHE   HZ   H  N N 395 
PHE   HXT  H  N N 396 
PRO   N    N  N N 397 
PRO   CA   C  N S 398 
PRO   C    C  N N 399 
PRO   O    O  N N 400 
PRO   CB   C  N N 401 
PRO   CG   C  N N 402 
PRO   CD   C  N N 403 
PRO   OXT  O  N N 404 
PRO   H    H  N N 405 
PRO   HA   H  N N 406 
PRO   HB2  H  N N 407 
PRO   HB3  H  N N 408 
PRO   HG2  H  N N 409 
PRO   HG3  H  N N 410 
PRO   HD2  H  N N 411 
PRO   HD3  H  N N 412 
PRO   HXT  H  N N 413 
SER   N    N  N N 414 
SER   CA   C  N S 415 
SER   C    C  N N 416 
SER   O    O  N N 417 
SER   CB   C  N N 418 
SER   OG   O  N N 419 
SER   OXT  O  N N 420 
SER   H    H  N N 421 
SER   H2   H  N N 422 
SER   HA   H  N N 423 
SER   HB2  H  N N 424 
SER   HB3  H  N N 425 
SER   HG   H  N N 426 
SER   HXT  H  N N 427 
THR   N    N  N N 428 
THR   CA   C  N S 429 
THR   C    C  N N 430 
THR   O    O  N N 431 
THR   CB   C  N R 432 
THR   OG1  O  N N 433 
THR   CG2  C  N N 434 
THR   OXT  O  N N 435 
THR   H    H  N N 436 
THR   H2   H  N N 437 
THR   HA   H  N N 438 
THR   HB   H  N N 439 
THR   HG1  H  N N 440 
THR   HG21 H  N N 441 
THR   HG22 H  N N 442 
THR   HG23 H  N N 443 
THR   HXT  H  N N 444 
TRP   N    N  N N 445 
TRP   CA   C  N S 446 
TRP   C    C  N N 447 
TRP   O    O  N N 448 
TRP   CB   C  N N 449 
TRP   CG   C  Y N 450 
TRP   CD1  C  Y N 451 
TRP   CD2  C  Y N 452 
TRP   NE1  N  Y N 453 
TRP   CE2  C  Y N 454 
TRP   CE3  C  Y N 455 
TRP   CZ2  C  Y N 456 
TRP   CZ3  C  Y N 457 
TRP   CH2  C  Y N 458 
TRP   OXT  O  N N 459 
TRP   H    H  N N 460 
TRP   H2   H  N N 461 
TRP   HA   H  N N 462 
TRP   HB2  H  N N 463 
TRP   HB3  H  N N 464 
TRP   HD1  H  N N 465 
TRP   HE1  H  N N 466 
TRP   HE3  H  N N 467 
TRP   HZ2  H  N N 468 
TRP   HZ3  H  N N 469 
TRP   HH2  H  N N 470 
TRP   HXT  H  N N 471 
TYR   N    N  N N 472 
TYR   CA   C  N S 473 
TYR   C    C  N N 474 
TYR   O    O  N N 475 
TYR   CB   C  N N 476 
TYR   CG   C  Y N 477 
TYR   CD1  C  Y N 478 
TYR   CD2  C  Y N 479 
TYR   CE1  C  Y N 480 
TYR   CE2  C  Y N 481 
TYR   CZ   C  Y N 482 
TYR   OH   O  N N 483 
TYR   OXT  O  N N 484 
TYR   H    H  N N 485 
TYR   H2   H  N N 486 
TYR   HA   H  N N 487 
TYR   HB2  H  N N 488 
TYR   HB3  H  N N 489 
TYR   HD1  H  N N 490 
TYR   HD2  H  N N 491 
TYR   HE1  H  N N 492 
TYR   HE2  H  N N 493 
TYR   HH   H  N N 494 
TYR   HXT  H  N N 495 
VAL   N    N  N N 496 
VAL   CA   C  N S 497 
VAL   C    C  N N 498 
VAL   O    O  N N 499 
VAL   CB   C  N N 500 
VAL   CG1  C  N N 501 
VAL   CG2  C  N N 502 
VAL   OXT  O  N N 503 
VAL   H    H  N N 504 
VAL   H2   H  N N 505 
VAL   HA   H  N N 506 
VAL   HB   H  N N 507 
VAL   HG11 H  N N 508 
VAL   HG12 H  N N 509 
VAL   HG13 H  N N 510 
VAL   HG21 H  N N 511 
VAL   HG22 H  N N 512 
VAL   HG23 H  N N 513 
VAL   HXT  H  N N 514 
# 
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 
A1BNX O18  C17  sing N N 1   
A1BNX C17  C16  doub Y N 2   
A1BNX C17  C19  sing Y N 3   
A1BNX N33  C34  doub Y N 4   
A1BNX N33  C32  sing Y N 5   
A1BNX C16  C15  sing Y N 6   
A1BNX C19  C13  doub Y N 7   
A1BNX C34  N30  sing Y N 8   
A1BNX C15  C14  doub Y N 9   
A1BNX C32  C31  doub Y N 10  
A1BNX C13  C14  sing Y N 11  
A1BNX C13  C12  sing N N 12  
A1BNX C12  N11  sing N N 13  
A1BNX N30  C31  sing Y N 14  
A1BNX N30  C29  sing N N 15  
A1BNX C29  C28  doub Y N 16  
A1BNX C29  C20  sing Y N 17  
A1BNX C28  C27  sing Y N 18  
A1BNX N11  C20  sing N N 19  
A1BNX N11  C02  sing N N 20  
A1BNX C20  C21  doub Y N 21  
A1BNX C27  C22  doub Y N 22  
A1BNX C21  C22  sing Y N 23  
A1BNX C22  C23  sing N N 24  
A1BNX O01  C02  doub N N 25  
A1BNX C02  N03  sing N N 26  
A1BNX F24  C23  sing N N 27  
A1BNX C23  F25  sing N N 28  
A1BNX C23  F26  sing N N 29  
A1BNX N03  C04  sing N N 30  
A1BNX CL10 C09  sing N N 31  
A1BNX C04  C09  doub Y N 32  
A1BNX C04  C05  sing Y N 33  
A1BNX C09  C08  sing Y N 34  
A1BNX C05  C06  doub Y N 35  
A1BNX C08  C07  doub Y N 36  
A1BNX C06  C07  sing Y N 37  
A1BNX C12  H1   sing N N 38  
A1BNX C12  H2   sing N N 39  
A1BNX C14  H3   sing N N 40  
A1BNX C15  H4   sing N N 41  
A1BNX C16  H5   sing N N 42  
A1BNX C21  H6   sing N N 43  
A1BNX C05  H7   sing N N 44  
A1BNX C06  H8   sing N N 45  
A1BNX C07  H9   sing N N 46  
A1BNX C08  H10  sing N N 47  
A1BNX C19  H11  sing N N 48  
A1BNX C27  H12  sing N N 49  
A1BNX C28  H13  sing N N 50  
A1BNX C31  H14  sing N N 51  
A1BNX C32  H15  sing N N 52  
A1BNX C34  H16  sing N N 53  
A1BNX N03  H17  sing N N 54  
A1BNX O18  H18  sing N N 55  
ALA   N    CA   sing N N 56  
ALA   N    H    sing N N 57  
ALA   N    H2   sing N N 58  
ALA   CA   C    sing N N 59  
ALA   CA   CB   sing N N 60  
ALA   CA   HA   sing N N 61  
ALA   C    O    doub N N 62  
ALA   C    OXT  sing N N 63  
ALA   CB   HB1  sing N N 64  
ALA   CB   HB2  sing N N 65  
ALA   CB   HB3  sing N N 66  
ALA   OXT  HXT  sing N N 67  
ARG   N    CA   sing N N 68  
ARG   N    H    sing N N 69  
ARG   N    H2   sing N N 70  
ARG   CA   C    sing N N 71  
ARG   CA   CB   sing N N 72  
ARG   CA   HA   sing N N 73  
ARG   C    O    doub N N 74  
ARG   C    OXT  sing N N 75  
ARG   CB   CG   sing N N 76  
ARG   CB   HB2  sing N N 77  
ARG   CB   HB3  sing N N 78  
ARG   CG   CD   sing N N 79  
ARG   CG   HG2  sing N N 80  
ARG   CG   HG3  sing N N 81  
ARG   CD   NE   sing N N 82  
ARG   CD   HD2  sing N N 83  
ARG   CD   HD3  sing N N 84  
ARG   NE   CZ   sing N N 85  
ARG   NE   HE   sing N N 86  
ARG   CZ   NH1  sing N N 87  
ARG   CZ   NH2  doub N N 88  
ARG   NH1  HH11 sing N N 89  
ARG   NH1  HH12 sing N N 90  
ARG   NH2  HH21 sing N N 91  
ARG   NH2  HH22 sing N N 92  
ARG   OXT  HXT  sing N N 93  
ASN   N    CA   sing N N 94  
ASN   N    H    sing N N 95  
ASN   N    H2   sing N N 96  
ASN   CA   C    sing N N 97  
ASN   CA   CB   sing N N 98  
ASN   CA   HA   sing N N 99  
ASN   C    O    doub N N 100 
ASN   C    OXT  sing N N 101 
ASN   CB   CG   sing N N 102 
ASN   CB   HB2  sing N N 103 
ASN   CB   HB3  sing N N 104 
ASN   CG   OD1  doub N N 105 
ASN   CG   ND2  sing N N 106 
ASN   ND2  HD21 sing N N 107 
ASN   ND2  HD22 sing N N 108 
ASN   OXT  HXT  sing N N 109 
ASP   N    CA   sing N N 110 
ASP   N    H    sing N N 111 
ASP   N    H2   sing N N 112 
ASP   CA   C    sing N N 113 
ASP   CA   CB   sing N N 114 
ASP   CA   HA   sing N N 115 
ASP   C    O    doub N N 116 
ASP   C    OXT  sing N N 117 
ASP   CB   CG   sing N N 118 
ASP   CB   HB2  sing N N 119 
ASP   CB   HB3  sing N N 120 
ASP   CG   OD1  doub N N 121 
ASP   CG   OD2  sing N N 122 
ASP   OD2  HD2  sing N N 123 
ASP   OXT  HXT  sing N N 124 
CYS   N    CA   sing N N 125 
CYS   N    H    sing N N 126 
CYS   N    H2   sing N N 127 
CYS   CA   C    sing N N 128 
CYS   CA   CB   sing N N 129 
CYS   CA   HA   sing N N 130 
CYS   C    O    doub N N 131 
CYS   C    OXT  sing N N 132 
CYS   CB   SG   sing N N 133 
CYS   CB   HB2  sing N N 134 
CYS   CB   HB3  sing N N 135 
CYS   SG   HG   sing N N 136 
CYS   OXT  HXT  sing N N 137 
GLN   N    CA   sing N N 138 
GLN   N    H    sing N N 139 
GLN   N    H2   sing N N 140 
GLN   CA   C    sing N N 141 
GLN   CA   CB   sing N N 142 
GLN   CA   HA   sing N N 143 
GLN   C    O    doub N N 144 
GLN   C    OXT  sing N N 145 
GLN   CB   CG   sing N N 146 
GLN   CB   HB2  sing N N 147 
GLN   CB   HB3  sing N N 148 
GLN   CG   CD   sing N N 149 
GLN   CG   HG2  sing N N 150 
GLN   CG   HG3  sing N N 151 
GLN   CD   OE1  doub N N 152 
GLN   CD   NE2  sing N N 153 
GLN   NE2  HE21 sing N N 154 
GLN   NE2  HE22 sing N N 155 
GLN   OXT  HXT  sing N N 156 
GLU   N    CA   sing N N 157 
GLU   N    H    sing N N 158 
GLU   N    H2   sing N N 159 
GLU   CA   C    sing N N 160 
GLU   CA   CB   sing N N 161 
GLU   CA   HA   sing N N 162 
GLU   C    O    doub N N 163 
GLU   C    OXT  sing N N 164 
GLU   CB   CG   sing N N 165 
GLU   CB   HB2  sing N N 166 
GLU   CB   HB3  sing N N 167 
GLU   CG   CD   sing N N 168 
GLU   CG   HG2  sing N N 169 
GLU   CG   HG3  sing N N 170 
GLU   CD   OE1  doub N N 171 
GLU   CD   OE2  sing N N 172 
GLU   OE2  HE2  sing N N 173 
GLU   OXT  HXT  sing N N 174 
GLY   N    CA   sing N N 175 
GLY   N    H    sing N N 176 
GLY   N    H2   sing N N 177 
GLY   CA   C    sing N N 178 
GLY   CA   HA2  sing N N 179 
GLY   CA   HA3  sing N N 180 
GLY   C    O    doub N N 181 
GLY   C    OXT  sing N N 182 
GLY   OXT  HXT  sing N N 183 
HEM   CHA  C1A  sing N N 184 
HEM   CHA  C4D  doub N N 185 
HEM   CHA  HHA  sing N N 186 
HEM   CHB  C4A  sing N N 187 
HEM   CHB  C1B  doub N N 188 
HEM   CHB  HHB  sing N N 189 
HEM   CHC  C4B  sing N N 190 
HEM   CHC  C1C  doub N N 191 
HEM   CHC  HHC  sing N N 192 
HEM   CHD  C4C  doub N N 193 
HEM   CHD  C1D  sing N N 194 
HEM   CHD  HHD  sing N N 195 
HEM   C1A  C2A  doub Y N 196 
HEM   C1A  NA   sing Y N 197 
HEM   C2A  C3A  sing Y N 198 
HEM   C2A  CAA  sing N N 199 
HEM   C3A  C4A  doub Y N 200 
HEM   C3A  CMA  sing N N 201 
HEM   C4A  NA   sing Y N 202 
HEM   CMA  HMA  sing N N 203 
HEM   CMA  HMAA sing N N 204 
HEM   CMA  HMAB sing N N 205 
HEM   CAA  CBA  sing N N 206 
HEM   CAA  HAA  sing N N 207 
HEM   CAA  HAAA sing N N 208 
HEM   CBA  CGA  sing N N 209 
HEM   CBA  HBA  sing N N 210 
HEM   CBA  HBAA sing N N 211 
HEM   CGA  O1A  doub N N 212 
HEM   CGA  O2A  sing N N 213 
HEM   C1B  C2B  sing N N 214 
HEM   C1B  NB   sing N N 215 
HEM   C2B  C3B  doub N N 216 
HEM   C2B  CMB  sing N N 217 
HEM   C3B  C4B  sing N N 218 
HEM   C3B  CAB  sing N N 219 
HEM   C4B  NB   doub N N 220 
HEM   CMB  HMB  sing N N 221 
HEM   CMB  HMBA sing N N 222 
HEM   CMB  HMBB sing N N 223 
HEM   CAB  CBB  doub N N 224 
HEM   CAB  HAB  sing N N 225 
HEM   CBB  HBB  sing N N 226 
HEM   CBB  HBBA sing N N 227 
HEM   C1C  C2C  sing Y N 228 
HEM   C1C  NC   sing Y N 229 
HEM   C2C  C3C  doub Y N 230 
HEM   C2C  CMC  sing N N 231 
HEM   C3C  C4C  sing Y N 232 
HEM   C3C  CAC  sing N N 233 
HEM   C4C  NC   sing Y N 234 
HEM   CMC  HMC  sing N N 235 
HEM   CMC  HMCA sing N N 236 
HEM   CMC  HMCB sing N N 237 
HEM   CAC  CBC  doub N N 238 
HEM   CAC  HAC  sing N N 239 
HEM   CBC  HBC  sing N N 240 
HEM   CBC  HBCA sing N N 241 
HEM   C1D  C2D  sing N N 242 
HEM   C1D  ND   doub N N 243 
HEM   C2D  C3D  doub N N 244 
HEM   C2D  CMD  sing N N 245 
HEM   C3D  C4D  sing N N 246 
HEM   C3D  CAD  sing N N 247 
HEM   C4D  ND   sing N N 248 
HEM   CMD  HMD  sing N N 249 
HEM   CMD  HMDA sing N N 250 
HEM   CMD  HMDB sing N N 251 
HEM   CAD  CBD  sing N N 252 
HEM   CAD  HAD  sing N N 253 
HEM   CAD  HADA sing N N 254 
HEM   CBD  CGD  sing N N 255 
HEM   CBD  HBD  sing N N 256 
HEM   CBD  HBDA sing N N 257 
HEM   CGD  O1D  doub N N 258 
HEM   CGD  O2D  sing N N 259 
HEM   O2A  H2A  sing N N 260 
HEM   O2D  H2D  sing N N 261 
HEM   FE   NA   sing N N 262 
HEM   FE   NB   sing N N 263 
HEM   FE   NC   sing N N 264 
HEM   FE   ND   sing N N 265 
HIS   N    CA   sing N N 266 
HIS   N    H    sing N N 267 
HIS   N    H2   sing N N 268 
HIS   CA   C    sing N N 269 
HIS   CA   CB   sing N N 270 
HIS   CA   HA   sing N N 271 
HIS   C    O    doub N N 272 
HIS   C    OXT  sing N N 273 
HIS   CB   CG   sing N N 274 
HIS   CB   HB2  sing N N 275 
HIS   CB   HB3  sing N N 276 
HIS   CG   ND1  sing Y N 277 
HIS   CG   CD2  doub Y N 278 
HIS   ND1  CE1  doub Y N 279 
HIS   ND1  HD1  sing N N 280 
HIS   CD2  NE2  sing Y N 281 
HIS   CD2  HD2  sing N N 282 
HIS   CE1  NE2  sing Y N 283 
HIS   CE1  HE1  sing N N 284 
HIS   NE2  HE2  sing N N 285 
HIS   OXT  HXT  sing N N 286 
ILE   N    CA   sing N N 287 
ILE   N    H    sing N N 288 
ILE   N    H2   sing N N 289 
ILE   CA   C    sing N N 290 
ILE   CA   CB   sing N N 291 
ILE   CA   HA   sing N N 292 
ILE   C    O    doub N N 293 
ILE   C    OXT  sing N N 294 
ILE   CB   CG1  sing N N 295 
ILE   CB   CG2  sing N N 296 
ILE   CB   HB   sing N N 297 
ILE   CG1  CD1  sing N N 298 
ILE   CG1  HG12 sing N N 299 
ILE   CG1  HG13 sing N N 300 
ILE   CG2  HG21 sing N N 301 
ILE   CG2  HG22 sing N N 302 
ILE   CG2  HG23 sing N N 303 
ILE   CD1  HD11 sing N N 304 
ILE   CD1  HD12 sing N N 305 
ILE   CD1  HD13 sing N N 306 
ILE   OXT  HXT  sing N N 307 
LEU   N    CA   sing N N 308 
LEU   N    H    sing N N 309 
LEU   N    H2   sing N N 310 
LEU   CA   C    sing N N 311 
LEU   CA   CB   sing N N 312 
LEU   CA   HA   sing N N 313 
LEU   C    O    doub N N 314 
LEU   C    OXT  sing N N 315 
LEU   CB   CG   sing N N 316 
LEU   CB   HB2  sing N N 317 
LEU   CB   HB3  sing N N 318 
LEU   CG   CD1  sing N N 319 
LEU   CG   CD2  sing N N 320 
LEU   CG   HG   sing N N 321 
LEU   CD1  HD11 sing N N 322 
LEU   CD1  HD12 sing N N 323 
LEU   CD1  HD13 sing N N 324 
LEU   CD2  HD21 sing N N 325 
LEU   CD2  HD22 sing N N 326 
LEU   CD2  HD23 sing N N 327 
LEU   OXT  HXT  sing N N 328 
LYS   N    CA   sing N N 329 
LYS   N    H    sing N N 330 
LYS   N    H2   sing N N 331 
LYS   CA   C    sing N N 332 
LYS   CA   CB   sing N N 333 
LYS   CA   HA   sing N N 334 
LYS   C    O    doub N N 335 
LYS   C    OXT  sing N N 336 
LYS   CB   CG   sing N N 337 
LYS   CB   HB2  sing N N 338 
LYS   CB   HB3  sing N N 339 
LYS   CG   CD   sing N N 340 
LYS   CG   HG2  sing N N 341 
LYS   CG   HG3  sing N N 342 
LYS   CD   CE   sing N N 343 
LYS   CD   HD2  sing N N 344 
LYS   CD   HD3  sing N N 345 
LYS   CE   NZ   sing N N 346 
LYS   CE   HE2  sing N N 347 
LYS   CE   HE3  sing N N 348 
LYS   NZ   HZ1  sing N N 349 
LYS   NZ   HZ2  sing N N 350 
LYS   NZ   HZ3  sing N N 351 
LYS   OXT  HXT  sing N N 352 
MET   N    CA   sing N N 353 
MET   N    H    sing N N 354 
MET   N    H2   sing N N 355 
MET   CA   C    sing N N 356 
MET   CA   CB   sing N N 357 
MET   CA   HA   sing N N 358 
MET   C    O    doub N N 359 
MET   C    OXT  sing N N 360 
MET   CB   CG   sing N N 361 
MET   CB   HB2  sing N N 362 
MET   CB   HB3  sing N N 363 
MET   CG   SD   sing N N 364 
MET   CG   HG2  sing N N 365 
MET   CG   HG3  sing N N 366 
MET   SD   CE   sing N N 367 
MET   CE   HE1  sing N N 368 
MET   CE   HE2  sing N N 369 
MET   CE   HE3  sing N N 370 
MET   OXT  HXT  sing N N 371 
PHE   N    CA   sing N N 372 
PHE   N    H    sing N N 373 
PHE   N    H2   sing N N 374 
PHE   CA   C    sing N N 375 
PHE   CA   CB   sing N N 376 
PHE   CA   HA   sing N N 377 
PHE   C    O    doub N N 378 
PHE   C    OXT  sing N N 379 
PHE   CB   CG   sing N N 380 
PHE   CB   HB2  sing N N 381 
PHE   CB   HB3  sing N N 382 
PHE   CG   CD1  doub Y N 383 
PHE   CG   CD2  sing Y N 384 
PHE   CD1  CE1  sing Y N 385 
PHE   CD1  HD1  sing N N 386 
PHE   CD2  CE2  doub Y N 387 
PHE   CD2  HD2  sing N N 388 
PHE   CE1  CZ   doub Y N 389 
PHE   CE1  HE1  sing N N 390 
PHE   CE2  CZ   sing Y N 391 
PHE   CE2  HE2  sing N N 392 
PHE   CZ   HZ   sing N N 393 
PHE   OXT  HXT  sing N N 394 
PRO   N    CA   sing N N 395 
PRO   N    CD   sing N N 396 
PRO   N    H    sing N N 397 
PRO   CA   C    sing N N 398 
PRO   CA   CB   sing N N 399 
PRO   CA   HA   sing N N 400 
PRO   C    O    doub N N 401 
PRO   C    OXT  sing N N 402 
PRO   CB   CG   sing N N 403 
PRO   CB   HB2  sing N N 404 
PRO   CB   HB3  sing N N 405 
PRO   CG   CD   sing N N 406 
PRO   CG   HG2  sing N N 407 
PRO   CG   HG3  sing N N 408 
PRO   CD   HD2  sing N N 409 
PRO   CD   HD3  sing N N 410 
PRO   OXT  HXT  sing N N 411 
SER   N    CA   sing N N 412 
SER   N    H    sing N N 413 
SER   N    H2   sing N N 414 
SER   CA   C    sing N N 415 
SER   CA   CB   sing N N 416 
SER   CA   HA   sing N N 417 
SER   C    O    doub N N 418 
SER   C    OXT  sing N N 419 
SER   CB   OG   sing N N 420 
SER   CB   HB2  sing N N 421 
SER   CB   HB3  sing N N 422 
SER   OG   HG   sing N N 423 
SER   OXT  HXT  sing N N 424 
THR   N    CA   sing N N 425 
THR   N    H    sing N N 426 
THR   N    H2   sing N N 427 
THR   CA   C    sing N N 428 
THR   CA   CB   sing N N 429 
THR   CA   HA   sing N N 430 
THR   C    O    doub N N 431 
THR   C    OXT  sing N N 432 
THR   CB   OG1  sing N N 433 
THR   CB   CG2  sing N N 434 
THR   CB   HB   sing N N 435 
THR   OG1  HG1  sing N N 436 
THR   CG2  HG21 sing N N 437 
THR   CG2  HG22 sing N N 438 
THR   CG2  HG23 sing N N 439 
THR   OXT  HXT  sing N N 440 
TRP   N    CA   sing N N 441 
TRP   N    H    sing N N 442 
TRP   N    H2   sing N N 443 
TRP   CA   C    sing N N 444 
TRP   CA   CB   sing N N 445 
TRP   CA   HA   sing N N 446 
TRP   C    O    doub N N 447 
TRP   C    OXT  sing N N 448 
TRP   CB   CG   sing N N 449 
TRP   CB   HB2  sing N N 450 
TRP   CB   HB3  sing N N 451 
TRP   CG   CD1  doub Y N 452 
TRP   CG   CD2  sing Y N 453 
TRP   CD1  NE1  sing Y N 454 
TRP   CD1  HD1  sing N N 455 
TRP   CD2  CE2  doub Y N 456 
TRP   CD2  CE3  sing Y N 457 
TRP   NE1  CE2  sing Y N 458 
TRP   NE1  HE1  sing N N 459 
TRP   CE2  CZ2  sing Y N 460 
TRP   CE3  CZ3  doub Y N 461 
TRP   CE3  HE3  sing N N 462 
TRP   CZ2  CH2  doub Y N 463 
TRP   CZ2  HZ2  sing N N 464 
TRP   CZ3  CH2  sing Y N 465 
TRP   CZ3  HZ3  sing N N 466 
TRP   CH2  HH2  sing N N 467 
TRP   OXT  HXT  sing N N 468 
TYR   N    CA   sing N N 469 
TYR   N    H    sing N N 470 
TYR   N    H2   sing N N 471 
TYR   CA   C    sing N N 472 
TYR   CA   CB   sing N N 473 
TYR   CA   HA   sing N N 474 
TYR   C    O    doub N N 475 
TYR   C    OXT  sing N N 476 
TYR   CB   CG   sing N N 477 
TYR   CB   HB2  sing N N 478 
TYR   CB   HB3  sing N N 479 
TYR   CG   CD1  doub Y N 480 
TYR   CG   CD2  sing Y N 481 
TYR   CD1  CE1  sing Y N 482 
TYR   CD1  HD1  sing N N 483 
TYR   CD2  CE2  doub Y N 484 
TYR   CD2  HD2  sing N N 485 
TYR   CE1  CZ   doub Y N 486 
TYR   CE1  HE1  sing N N 487 
TYR   CE2  CZ   sing Y N 488 
TYR   CE2  HE2  sing N N 489 
TYR   CZ   OH   sing N N 490 
TYR   OH   HH   sing N N 491 
TYR   OXT  HXT  sing N N 492 
VAL   N    CA   sing N N 493 
VAL   N    H    sing N N 494 
VAL   N    H2   sing N N 495 
VAL   CA   C    sing N N 496 
VAL   CA   CB   sing N N 497 
VAL   CA   HA   sing N N 498 
VAL   C    O    doub N N 499 
VAL   C    OXT  sing N N 500 
VAL   CB   CG1  sing N N 501 
VAL   CB   CG2  sing N N 502 
VAL   CB   HB   sing N N 503 
VAL   CG1  HG11 sing N N 504 
VAL   CG1  HG12 sing N N 505 
VAL   CG1  HG13 sing N N 506 
VAL   CG2  HG21 sing N N 507 
VAL   CG2  HG22 sing N N 508 
VAL   CG2  HG23 sing N N 509 
VAL   OXT  HXT  sing N N 510 
# 
_pdbx_audit_support.funding_organization   
'National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           R35GM118041 
_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   9BV9 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9MS1 
_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]   0.013197 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.009935 
_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]   0.008255 
_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  
CL 
F  
FE 
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    . HIS   A 1 7   ? 9.230  -9.253  15.867  1.00 105.12 ? 28  HIS   A N    1 
ATOM   2    C  CA   . HIS   A 1 7   ? 10.370 -9.884  15.209  1.00 107.06 ? 28  HIS   A CA   1 
ATOM   3    C  C    . HIS   A 1 7   ? 11.611 -8.999  15.286  1.00 105.55 ? 28  HIS   A C    1 
ATOM   4    O  O    . HIS   A 1 7   ? 12.701 -9.470  15.614  1.00 100.83 ? 28  HIS   A O    1 
ATOM   5    C  CB   . HIS   A 1 7   ? 10.036 -10.205 13.751  1.00 111.03 ? 28  HIS   A CB   1 
ATOM   6    C  CG   . HIS   A 1 7   ? 9.406  -9.067  13.010  1.00 106.79 ? 28  HIS   A CG   1 
ATOM   7    N  ND1  . HIS   A 1 7   ? 8.046  -8.841  13.011  1.00 108.78 ? 28  HIS   A ND1  1 
ATOM   8    C  CD2  . HIS   A 1 7   ? 9.948  -8.092  12.242  1.00 103.96 ? 28  HIS   A CD2  1 
ATOM   9    C  CE1  . HIS   A 1 7   ? 7.778  -7.775  12.277  1.00 111.09 ? 28  HIS   A CE1  1 
ATOM   10   N  NE2  . HIS   A 1 7   ? 8.915  -7.302  11.799  1.00 110.14 ? 28  HIS   A NE2  1 
ATOM   11   N  N    . SER   A 1 8   ? 11.438 -7.712  14.978  1.00 103.57 ? 29  SER   A N    1 
ATOM   12   C  CA   . SER   A 1 8   ? 12.536 -6.761  15.079  1.00 99.04  ? 29  SER   A CA   1 
ATOM   13   C  C    . SER   A 1 8   ? 12.762 -6.285  16.506  1.00 87.44  ? 29  SER   A C    1 
ATOM   14   O  O    . SER   A 1 8   ? 13.832 -5.745  16.803  1.00 86.55  ? 29  SER   A O    1 
ATOM   15   C  CB   . SER   A 1 8   ? 12.278 -5.555  14.171  1.00 103.22 ? 29  SER   A CB   1 
ATOM   16   O  OG   . SER   A 1 8   ? 12.193 -5.941  12.810  1.00 97.70  ? 29  SER   A OG   1 
ATOM   17   N  N    . HIS   A 1 9   ? 11.785 -6.487  17.392  1.00 87.69  ? 30  HIS   A N    1 
ATOM   18   C  CA   . HIS   A 1 9   ? 11.888 -5.997  18.761  1.00 91.31  ? 30  HIS   A CA   1 
ATOM   19   C  C    . HIS   A 1 9   ? 12.870 -6.803  19.599  1.00 88.32  ? 30  HIS   A C    1 
ATOM   20   O  O    . HIS   A 1 9   ? 13.304 -6.325  20.653  1.00 86.99  ? 30  HIS   A O    1 
ATOM   21   C  CB   . HIS   A 1 9   ? 10.505 -6.003  19.409  1.00 91.72  ? 30  HIS   A CB   1 
ATOM   22   C  CG   . HIS   A 1 9   ? 9.408  -5.606  18.473  1.00 97.11  ? 30  HIS   A CG   1 
ATOM   23   N  ND1  . HIS   A 1 9   ? 9.450  -4.448  17.727  1.00 96.73  ? 30  HIS   A ND1  1 
ATOM   24   C  CD2  . HIS   A 1 9   ? 8.245  -6.220  18.150  1.00 102.29 ? 30  HIS   A CD2  1 
ATOM   25   C  CE1  . HIS   A 1 9   ? 8.358  -4.362  16.989  1.00 99.17  ? 30  HIS   A CE1  1 
ATOM   26   N  NE2  . HIS   A 1 9   ? 7.610  -5.424  17.227  1.00 107.11 ? 30  HIS   A NE2  1 
ATOM   27   N  N    . GLY   A 1 10  ? 13.227 -8.008  19.163  1.00 87.57  ? 31  GLY   A N    1 
ATOM   28   C  CA   . GLY   A 1 10  ? 14.235 -8.793  19.842  1.00 88.26  ? 31  GLY   A CA   1 
ATOM   29   C  C    . GLY   A 1 10  ? 15.661 -8.463  19.475  1.00 84.67  ? 31  GLY   A C    1 
ATOM   30   O  O    . GLY   A 1 10  ? 16.589 -9.058  20.030  1.00 85.15  ? 31  GLY   A O    1 
ATOM   31   N  N    . LEU   A 1 11  ? 15.866 -7.525  18.548  1.00 86.36  ? 32  LEU   A N    1 
ATOM   32   C  CA   . LEU   A 1 11  ? 17.217 -7.168  18.128  1.00 86.86  ? 32  LEU   A CA   1 
ATOM   33   C  C    . LEU   A 1 11  ? 17.988 -6.515  19.268  1.00 86.27  ? 32  LEU   A C    1 
ATOM   34   O  O    . LEU   A 1 11  ? 19.050 -7.000  19.676  1.00 88.46  ? 32  LEU   A O    1 
ATOM   35   C  CB   . LEU   A 1 11  ? 17.163 -6.241  16.913  1.00 77.35  ? 32  LEU   A CB   1 
ATOM   36   C  CG   . LEU   A 1 11  ? 18.522 -5.839  16.340  1.00 73.55  ? 32  LEU   A CG   1 
ATOM   37   C  CD1  . LEU   A 1 11  ? 19.176 -7.017  15.633  1.00 82.32  ? 32  LEU   A CD1  1 
ATOM   38   C  CD2  . LEU   A 1 11  ? 18.388 -4.648  15.406  1.00 82.59  ? 32  LEU   A CD2  1 
ATOM   39   N  N    . PHE   A 1 12  ? 17.467 -5.404  19.796  1.00 86.28  ? 33  PHE   A N    1 
ATOM   40   C  CA   . PHE   A 1 12  ? 18.118 -4.744  20.922  1.00 86.93  ? 33  PHE   A CA   1 
ATOM   41   C  C    . PHE   A 1 12  ? 18.067 -5.585  22.190  1.00 90.73  ? 33  PHE   A C    1 
ATOM   42   O  O    . PHE   A 1 12  ? 18.843 -5.333  23.118  1.00 88.76  ? 33  PHE   A O    1 
ATOM   43   C  CB   . PHE   A 1 12  ? 17.487 -3.375  21.170  1.00 86.00  ? 33  PHE   A CB   1 
ATOM   44   C  CG   . PHE   A 1 12  ? 17.762 -2.381  20.081  1.00 85.43  ? 33  PHE   A CG   1 
ATOM   45   C  CD1  . PHE   A 1 12  ? 19.063 -2.045  19.749  1.00 83.06  ? 33  PHE   A CD1  1 
ATOM   46   C  CD2  . PHE   A 1 12  ? 16.723 -1.778  19.393  1.00 83.43  ? 33  PHE   A CD2  1 
ATOM   47   C  CE1  . PHE   A 1 12  ? 19.324 -1.132  18.747  1.00 81.93  ? 33  PHE   A CE1  1 
ATOM   48   C  CE2  . PHE   A 1 12  ? 16.977 -0.862  18.390  1.00 83.16  ? 33  PHE   A CE2  1 
ATOM   49   C  CZ   . PHE   A 1 12  ? 18.280 -0.540  18.066  1.00 84.72  ? 33  PHE   A CZ   1 
ATOM   50   N  N    . LYS   A 1 13  ? 17.170 -6.571  22.253  1.00 92.88  ? 34  LYS   A N    1 
ATOM   51   C  CA   . LYS   A 1 13  ? 17.206 -7.535  23.345  1.00 88.76  ? 34  LYS   A CA   1 
ATOM   52   C  C    . LYS   A 1 13  ? 18.292 -8.582  23.132  1.00 87.13  ? 34  LYS   A C    1 
ATOM   53   O  O    . LYS   A 1 13  ? 18.889 -9.056  24.105  1.00 91.29  ? 34  LYS   A O    1 
ATOM   54   C  CB   . LYS   A 1 13  ? 15.843 -8.213  23.498  1.00 83.70  ? 34  LYS   A CB   1 
ATOM   55   N  N    . LYS   A 1 14  ? 18.563 -8.948  21.877  1.00 87.64  ? 35  LYS   A N    1 
ATOM   56   C  CA   . LYS   A 1 14  ? 19.635 -9.898  21.599  1.00 90.87  ? 35  LYS   A CA   1 
ATOM   57   C  C    . LYS   A 1 14  ? 21.002 -9.274  21.848  1.00 97.24  ? 35  LYS   A C    1 
ATOM   58   O  O    . LYS   A 1 14  ? 21.906 -9.934  22.373  1.00 102.42 ? 35  LYS   A O    1 
ATOM   59   C  CB   . LYS   A 1 14  ? 19.531 -10.403 20.160  1.00 85.58  ? 35  LYS   A CB   1 
ATOM   60   N  N    . LEU   A 1 15  ? 21.172 -8.004  21.482  1.00 96.79  ? 36  LEU   A N    1 
ATOM   61   C  CA   . LEU   A 1 15  ? 22.426 -7.298  21.708  1.00 95.93  ? 36  LEU   A CA   1 
ATOM   62   C  C    . LEU   A 1 15  ? 22.605 -6.854  23.154  1.00 96.11  ? 36  LEU   A C    1 
ATOM   63   O  O    . LEU   A 1 15  ? 23.625 -6.231  23.471  1.00 99.35  ? 36  LEU   A O    1 
ATOM   64   C  CB   . LEU   A 1 15  ? 22.520 -6.083  20.779  1.00 92.10  ? 36  LEU   A CB   1 
ATOM   65   N  N    . GLY   A 1 16  ? 21.650 -7.154  24.031  1.00 94.43  ? 37  GLY   A N    1 
ATOM   66   C  CA   . GLY   A 1 16  ? 21.762 -6.792  25.430  1.00 96.93  ? 37  GLY   A CA   1 
ATOM   67   C  C    . GLY   A 1 16  ? 21.776 -5.296  25.660  1.00 91.28  ? 37  GLY   A C    1 
ATOM   68   O  O    . GLY   A 1 16  ? 22.617 -4.782  26.403  1.00 92.20  ? 37  GLY   A O    1 
ATOM   69   N  N    . ILE   A 1 17  ? 20.850 -4.590  25.028  1.00 92.33  ? 38  ILE   A N    1 
ATOM   70   C  CA   . ILE   A 1 17  ? 20.760 -3.135  25.103  1.00 95.26  ? 38  ILE   A CA   1 
ATOM   71   C  C    . ILE   A 1 17  ? 19.448 -2.782  25.795  1.00 92.03  ? 38  ILE   A C    1 
ATOM   72   O  O    . ILE   A 1 17  ? 18.379 -3.201  25.330  1.00 90.51  ? 38  ILE   A O    1 
ATOM   73   C  CB   . ILE   A 1 17  ? 20.844 -2.491  23.710  1.00 92.80  ? 38  ILE   A CB   1 
ATOM   74   C  CG1  . ILE   A 1 17  ? 22.137 -2.915  23.009  1.00 91.12  ? 38  ILE   A CG1  1 
ATOM   75   C  CG2  . ILE   A 1 17  ? 20.762 -0.977  23.815  1.00 85.14  ? 38  ILE   A CG2  1 
ATOM   76   C  CD1  . ILE   A 1 17  ? 22.226 -2.477  21.562  1.00 92.49  ? 38  ILE   A CD1  1 
ATOM   77   N  N    . PRO   A 1 18  ? 19.474 -2.034  26.895  1.00 87.88  ? 39  PRO   A N    1 
ATOM   78   C  CA   . PRO   A 1 18  ? 18.225 -1.675  27.572  1.00 88.50  ? 39  PRO   A CA   1 
ATOM   79   C  C    . PRO   A 1 18  ? 17.425 -0.668  26.762  1.00 82.26  ? 39  PRO   A C    1 
ATOM   80   O  O    . PRO   A 1 18  ? 17.941 0.027   25.884  1.00 80.28  ? 39  PRO   A O    1 
ATOM   81   C  CB   . PRO   A 1 18  ? 18.699 -1.071  28.897  1.00 85.53  ? 39  PRO   A CB   1 
ATOM   82   C  CG   . PRO   A 1 18  ? 20.056 -0.532  28.587  1.00 85.25  ? 39  PRO   A CG   1 
ATOM   83   C  CD   . PRO   A 1 18  ? 20.655 -1.480  27.580  1.00 83.72  ? 39  PRO   A CD   1 
ATOM   84   N  N    . GLY   A 1 19  ? 16.136 -0.600  27.073  1.00 83.87  ? 40  GLY   A N    1 
ATOM   85   C  CA   . GLY   A 1 19  ? 15.236 0.298   26.394  1.00 80.92  ? 40  GLY   A CA   1 
ATOM   86   C  C    . GLY   A 1 19  ? 13.792 -0.008  26.727  1.00 86.83  ? 40  GLY   A C    1 
ATOM   87   O  O    . GLY   A 1 19  ? 13.463 -1.088  27.230  1.00 93.28  ? 40  GLY   A O    1 
ATOM   88   N  N    . PRO   A 1 20  ? 12.900 0.943   26.462  1.00 83.34  ? 41  PRO   A N    1 
ATOM   89   C  CA   . PRO   A 1 20  ? 11.477 0.706   26.729  1.00 87.31  ? 41  PRO   A CA   1 
ATOM   90   C  C    . PRO   A 1 20  ? 10.941 -0.403  25.837  1.00 89.52  ? 41  PRO   A C    1 
ATOM   91   O  O    . PRO   A 1 20  ? 11.203 -0.437  24.632  1.00 91.07  ? 41  PRO   A O    1 
ATOM   92   C  CB   . PRO   A 1 20  ? 10.827 2.058   26.418  1.00 88.54  ? 41  PRO   A CB   1 
ATOM   93   C  CG   . PRO   A 1 20  ? 11.772 2.720   25.470  1.00 90.37  ? 41  PRO   A CG   1 
ATOM   94   C  CD   . PRO   A 1 20  ? 13.144 2.277   25.889  1.00 84.23  ? 41  PRO   A CD   1 
ATOM   95   N  N    . THR   A 1 21  ? 10.201 -1.322  26.445  1.00 91.05  ? 42  THR   A N    1 
ATOM   96   C  CA   . THR   A 1 21  ? 9.643  -2.457  25.724  1.00 91.84  ? 42  THR   A CA   1 
ATOM   97   C  C    . THR   A 1 21  ? 8.665  -1.972  24.658  1.00 94.18  ? 42  THR   A C    1 
ATOM   98   O  O    . THR   A 1 21  ? 7.659  -1.328  24.996  1.00 89.14  ? 42  THR   A O    1 
ATOM   99   C  CB   . THR   A 1 21  ? 8.948  -3.412  26.691  1.00 96.33  ? 42  THR   A CB   1 
ATOM   100  O  OG1  . THR   A 1 21  ? 8.114  -2.667  27.588  1.00 100.08 ? 42  THR   A OG1  1 
ATOM   101  C  CG2  . THR   A 1 21  ? 9.976  -4.199  27.493  1.00 99.04  ? 42  THR   A CG2  1 
ATOM   102  N  N    . PRO   A 1 22  ? 8.914  -2.247  23.382  1.00 97.56  ? 43  PRO   A N    1 
ATOM   103  C  CA   . PRO   A 1 22  ? 8.057  -1.709  22.323  1.00 92.84  ? 43  PRO   A CA   1 
ATOM   104  C  C    . PRO   A 1 22  ? 6.814  -2.557  22.096  1.00 90.25  ? 43  PRO   A C    1 
ATOM   105  O  O    . PRO   A 1 22  ? 6.776  -3.756  22.380  1.00 89.08  ? 43  PRO   A O    1 
ATOM   106  C  CB   . PRO   A 1 22  ? 8.970  -1.745  21.094  1.00 91.88  ? 43  PRO   A CB   1 
ATOM   107  C  CG   . PRO   A 1 22  ? 9.836  -2.936  21.342  1.00 95.76  ? 43  PRO   A CG   1 
ATOM   108  C  CD   . PRO   A 1 22  ? 10.070 -2.980  22.836  1.00 96.02  ? 43  PRO   A CD   1 
ATOM   109  N  N    . LEU   A 1 23  ? 5.766  -1.890  21.558  1.00 85.84  ? 44  LEU   A N    1 
ATOM   110  C  CA   . LEU   A 1 23  ? 4.540  -2.560  21.156  1.00 84.04  ? 44  LEU   A CA   1 
ATOM   111  C  C    . LEU   A 1 23  ? 4.631  -2.992  19.695  1.00 92.19  ? 44  LEU   A C    1 
ATOM   112  O  O    . LEU   A 1 23  ? 5.334  -2.361  18.898  1.00 97.84  ? 44  LEU   A O    1 
ATOM   113  C  CB   . LEU   A 1 23  ? 3.338  -1.638  21.348  1.00 80.18  ? 44  LEU   A CB   1 
ATOM   114  C  CG   . LEU   A 1 23  ? 3.051  -1.195  22.785  1.00 80.49  ? 44  LEU   A CG   1 
ATOM   115  C  CD1  . LEU   A 1 23  ? 1.798  -0.340  22.843  1.00 73.47  ? 44  LEU   A CD1  1 
ATOM   116  C  CD2  . LEU   A 1 23  ? 2.927  -2.395  23.714  1.00 85.40  ? 44  LEU   A CD2  1 
ATOM   117  N  N    . PRO   A 1 24  ? 3.946  -4.072  19.320  1.00 93.01  ? 45  PRO   A N    1 
ATOM   118  C  CA   . PRO   A 1 24  ? 4.039  -4.556  17.937  1.00 92.82  ? 45  PRO   A CA   1 
ATOM   119  C  C    . PRO   A 1 24  ? 3.526  -3.530  16.938  1.00 92.94  ? 45  PRO   A C    1 
ATOM   120  O  O    . PRO   A 1 24  ? 2.603  -2.762  17.219  1.00 91.43  ? 45  PRO   A O    1 
ATOM   121  C  CB   . PRO   A 1 24  ? 3.155  -5.809  17.939  1.00 94.59  ? 45  PRO   A CB   1 
ATOM   122  C  CG   . PRO   A 1 24  ? 3.117  -6.243  19.370  1.00 93.50  ? 45  PRO   A CG   1 
ATOM   123  C  CD   . PRO   A 1 24  ? 3.157  -4.978  20.172  1.00 91.97  ? 45  PRO   A CD   1 
ATOM   124  N  N    . PHE   A 1 25  ? 4.172  -3.504  15.769  1.00 94.21  ? 46  PHE   A N    1 
ATOM   125  C  CA   . PHE   A 1 25  ? 3.781  -2.670  14.634  1.00 93.64  ? 46  PHE   A CA   1 
ATOM   126  C  C    . PHE   A 1 25  ? 3.957  -1.180  14.907  1.00 93.78  ? 46  PHE   A C    1 
ATOM   127  O  O    . PHE   A 1 25  ? 3.905  -0.370  13.976  1.00 98.49  ? 46  PHE   A O    1 
ATOM   128  C  CB   . PHE   A 1 25  ? 2.332  -2.956  14.224  1.00 93.98  ? 46  PHE   A CB   1 
ATOM   129  C  CG   . PHE   A 1 25  ? 2.102  -4.363  13.750  1.00 101.98 ? 46  PHE   A CG   1 
ATOM   130  C  CD1  . PHE   A 1 25  ? 2.258  -4.691  12.413  1.00 107.36 ? 46  PHE   A CD1  1 
ATOM   131  C  CD2  . PHE   A 1 25  ? 1.728  -5.358  14.639  1.00 105.51 ? 46  PHE   A CD2  1 
ATOM   132  C  CE1  . PHE   A 1 25  ? 2.048  -5.985  11.972  1.00 112.56 ? 46  PHE   A CE1  1 
ATOM   133  C  CE2  . PHE   A 1 25  ? 1.516  -6.655  14.204  1.00 107.49 ? 46  PHE   A CE2  1 
ATOM   134  C  CZ   . PHE   A 1 25  ? 1.676  -6.968  12.868  1.00 111.26 ? 46  PHE   A CZ   1 
ATOM   135  N  N    . LEU   A 1 26  ? 4.174  -0.802  16.163  1.00 92.13  ? 47  LEU   A N    1 
ATOM   136  C  CA   . LEU   A 1 26  ? 4.290  0.599   16.539  1.00 91.00  ? 47  LEU   A CA   1 
ATOM   137  C  C    . LEU   A 1 26  ? 5.614  0.958   17.194  1.00 88.83  ? 47  LEU   A C    1 
ATOM   138  O  O    . LEU   A 1 26  ? 6.090  2.079   17.007  1.00 92.82  ? 47  LEU   A O    1 
ATOM   139  C  CB   . LEU   A 1 26  ? 3.147  0.992   17.487  1.00 92.04  ? 47  LEU   A CB   1 
ATOM   140  C  CG   . LEU   A 1 26  ? 1.989  1.778   16.869  1.00 95.22  ? 47  LEU   A CG   1 
ATOM   141  C  CD1  . LEU   A 1 26  ? 1.448  1.083   15.630  1.00 94.80  ? 47  LEU   A CD1  1 
ATOM   142  C  CD2  . LEU   A 1 26  ? 0.885  1.990   17.894  1.00 91.24  ? 47  LEU   A CD2  1 
ATOM   143  N  N    . GLY   A 1 27  ? 6.219  0.048   17.949  1.00 87.05  ? 48  GLY   A N    1 
ATOM   144  C  CA   . GLY   A 1 27  ? 7.463  0.352   18.625  1.00 87.43  ? 48  GLY   A CA   1 
ATOM   145  C  C    . GLY   A 1 27  ? 7.269  1.236   19.840  1.00 89.92  ? 48  GLY   A C    1 
ATOM   146  O  O    . GLY   A 1 27  ? 6.585  0.849   20.792  1.00 88.79  ? 48  GLY   A O    1 
ATOM   147  N  N    . ASN   A 1 28  ? 7.864  2.431   19.818  1.00 89.57  ? 49  ASN   A N    1 
ATOM   148  C  CA   . ASN   A 1 28  ? 7.769  3.371   20.929  1.00 86.77  ? 49  ASN   A CA   1 
ATOM   149  C  C    . ASN   A 1 28  ? 7.254  4.729   20.465  1.00 80.97  ? 49  ASN   A C    1 
ATOM   150  O  O    . ASN   A 1 28  ? 7.630  5.764   21.023  1.00 81.67  ? 49  ASN   A O    1 
ATOM   151  C  CB   . ASN   A 1 28  ? 9.119  3.528   21.631  1.00 86.79  ? 49  ASN   A CB   1 
ATOM   152  C  CG   . ASN   A 1 28  ? 9.645  2.219   22.187  1.00 87.19  ? 49  ASN   A CG   1 
ATOM   153  O  OD1  . ASN   A 1 28  ? 10.385 1.498   21.517  1.00 88.85  ? 49  ASN   A OD1  1 
ATOM   154  N  ND2  . ASN   A 1 28  ? 9.266  1.908   23.420  1.00 87.95  ? 49  ASN   A ND2  1 
ATOM   155  N  N    . ILE   A 1 29  ? 6.392  4.746   19.446  1.00 81.31  ? 50  ILE   A N    1 
ATOM   156  C  CA   . ILE   A 1 29  ? 5.881  6.022   18.953  1.00 86.54  ? 50  ILE   A CA   1 
ATOM   157  C  C    . ILE   A 1 29  ? 4.908  6.638   19.950  1.00 84.50  ? 50  ILE   A C    1 
ATOM   158  O  O    . ILE   A 1 29  ? 4.748  7.864   19.993  1.00 83.23  ? 50  ILE   A O    1 
ATOM   159  C  CB   . ILE   A 1 29  ? 5.232  5.850   17.567  1.00 81.98  ? 50  ILE   A CB   1 
ATOM   160  C  CG1  . ILE   A 1 29  ? 4.003  4.947   17.659  1.00 87.37  ? 50  ILE   A CG1  1 
ATOM   161  C  CG2  . ILE   A 1 29  ? 6.237  5.293   16.572  1.00 79.79  ? 50  ILE   A CG2  1 
ATOM   162  C  CD1  . ILE   A 1 29  ? 2.922  5.295   16.665  1.00 89.16  ? 50  ILE   A CD1  1 
ATOM   163  N  N    . LEU   A 1 30  ? 4.243  5.814   20.764  1.00 86.06  ? 51  LEU   A N    1 
ATOM   164  C  CA   . LEU   A 1 30  ? 3.359  6.349   21.793  1.00 85.31  ? 51  LEU   A CA   1 
ATOM   165  C  C    . LEU   A 1 30  ? 4.122  7.152   22.834  1.00 87.95  ? 51  LEU   A C    1 
ATOM   166  O  O    . LEU   A 1 30  ? 3.532  8.018   23.489  1.00 93.17  ? 51  LEU   A O    1 
ATOM   167  C  CB   . LEU   A 1 30  ? 2.586  5.217   22.473  1.00 87.32  ? 51  LEU   A CB   1 
ATOM   168  C  CG   . LEU   A 1 30  ? 1.561  4.473   21.615  1.00 87.39  ? 51  LEU   A CG   1 
ATOM   169  C  CD1  . LEU   A 1 30  ? 0.793  3.458   22.450  1.00 85.88  ? 51  LEU   A CD1  1 
ATOM   170  C  CD2  . LEU   A 1 30  ? 0.612  5.457   20.949  1.00 86.70  ? 51  LEU   A CD2  1 
ATOM   171  N  N    . SER   A 1 31  ? 5.418  6.885   22.998  1.00 84.19  ? 52  SER   A N    1 
ATOM   172  C  CA   . SER   A 1 31  ? 6.244  7.662   23.911  1.00 85.48  ? 52  SER   A CA   1 
ATOM   173  C  C    . SER   A 1 31  ? 6.574  9.046   23.368  1.00 86.15  ? 52  SER   A C    1 
ATOM   174  O  O    . SER   A 1 31  ? 7.121  9.869   24.110  1.00 87.54  ? 52  SER   A O    1 
ATOM   175  C  CB   . SER   A 1 31  ? 7.534  6.903   24.217  1.00 81.51  ? 52  SER   A CB   1 
ATOM   176  O  OG   . SER   A 1 31  ? 7.259  5.607   24.719  1.00 83.92  ? 52  SER   A OG   1 
ATOM   177  N  N    . TYR   A 1 32  ? 6.257  9.322   22.105  1.00 84.65  ? 53  TYR   A N    1 
ATOM   178  C  CA   . TYR   A 1 32  ? 6.475  10.637  21.518  1.00 87.13  ? 53  TYR   A CA   1 
ATOM   179  C  C    . TYR   A 1 32  ? 5.400  11.645  21.903  1.00 90.27  ? 53  TYR   A C    1 
ATOM   180  O  O    . TYR   A 1 32  ? 5.382  12.747  21.345  1.00 94.20  ? 53  TYR   A O    1 
ATOM   181  C  CB   . TYR   A 1 32  ? 6.554  10.526  19.993  1.00 83.53  ? 53  TYR   A CB   1 
ATOM   182  C  CG   . TYR   A 1 32  ? 7.846  9.927   19.490  1.00 85.27  ? 53  TYR   A CG   1 
ATOM   183  C  CD1  . TYR   A 1 32  ? 9.011  10.013  20.239  1.00 85.52  ? 53  TYR   A CD1  1 
ATOM   184  C  CD2  . TYR   A 1 32  ? 7.900  9.276   18.265  1.00 88.60  ? 53  TYR   A CD2  1 
ATOM   185  C  CE1  . TYR   A 1 32  ? 10.195 9.468   19.783  1.00 86.26  ? 53  TYR   A CE1  1 
ATOM   186  C  CE2  . TYR   A 1 32  ? 9.079  8.727   17.800  1.00 89.62  ? 53  TYR   A CE2  1 
ATOM   187  C  CZ   . TYR   A 1 32  ? 10.224 8.826   18.563  1.00 89.89  ? 53  TYR   A CZ   1 
ATOM   188  O  OH   . TYR   A 1 32  ? 11.401 8.281   18.103  1.00 92.07  ? 53  TYR   A OH   1 
ATOM   189  N  N    . HIS   A 1 33  ? 4.507  11.298  22.834  1.00 89.45  ? 54  HIS   A N    1 
ATOM   190  C  CA   . HIS   A 1 33  ? 3.462  12.232  23.240  1.00 92.92  ? 54  HIS   A CA   1 
ATOM   191  C  C    . HIS   A 1 33  ? 4.040  13.450  23.950  1.00 94.66  ? 54  HIS   A C    1 
ATOM   192  O  O    . HIS   A 1 33  ? 3.467  14.542  23.867  1.00 96.72  ? 54  HIS   A O    1 
ATOM   193  C  CB   . HIS   A 1 33  ? 2.450  11.529  24.142  1.00 96.87  ? 54  HIS   A CB   1 
ATOM   194  C  CG   . HIS   A 1 33  ? 2.994  11.166  25.488  1.00 93.22  ? 54  HIS   A CG   1 
ATOM   195  N  ND1  . HIS   A 1 33  ? 3.711  10.011  25.714  1.00 91.62  ? 54  HIS   A ND1  1 
ATOM   196  C  CD2  . HIS   A 1 33  ? 2.930  11.808  26.678  1.00 97.99  ? 54  HIS   A CD2  1 
ATOM   197  C  CE1  . HIS   A 1 33  ? 4.064  9.956   26.986  1.00 95.09  ? 54  HIS   A CE1  1 
ATOM   198  N  NE2  . HIS   A 1 33  ? 3.602  11.034  27.593  1.00 101.53 ? 54  HIS   A NE2  1 
ATOM   199  N  N    . LYS   A 1 34  ? 5.158  13.285  24.651  1.00 95.82  ? 55  LYS   A N    1 
ATOM   200  C  CA   . LYS   A 1 34  ? 5.830  14.390  25.320  1.00 94.34  ? 55  LYS   A CA   1 
ATOM   201  C  C    . LYS   A 1 34  ? 6.838  15.095  24.423  1.00 92.82  ? 55  LYS   A C    1 
ATOM   202  O  O    . LYS   A 1 34  ? 7.511  16.025  24.880  1.00 96.07  ? 55  LYS   A O    1 
ATOM   203  C  CB   . LYS   A 1 34  ? 6.528  13.892  26.590  1.00 90.94  ? 55  LYS   A CB   1 
ATOM   204  N  N    . GLY   A 1 35  ? 6.957  14.681  23.169  1.00 85.55  ? 56  GLY   A N    1 
ATOM   205  C  CA   . GLY   A 1 35  ? 7.894  15.284  22.248  1.00 85.16  ? 56  GLY   A CA   1 
ATOM   206  C  C    . GLY   A 1 35  ? 9.190  14.496  22.152  1.00 83.45  ? 56  GLY   A C    1 
ATOM   207  O  O    . GLY   A 1 35  ? 9.539  13.694  23.022  1.00 81.37  ? 56  GLY   A O    1 
ATOM   208  N  N    . PHE   A 1 36  ? 9.910  14.729  21.052  1.00 84.94  ? 57  PHE   A N    1 
ATOM   209  C  CA   . PHE   A 1 36  ? 11.218 14.106  20.879  1.00 84.65  ? 57  PHE   A CA   1 
ATOM   210  C  C    . PHE   A 1 36  ? 12.150 14.463  22.027  1.00 79.62  ? 57  PHE   A C    1 
ATOM   211  O  O    . PHE   A 1 36  ? 12.906 13.615  22.514  1.00 73.97  ? 57  PHE   A O    1 
ATOM   212  C  CB   . PHE   A 1 36  ? 11.833 14.540  19.549  1.00 87.68  ? 57  PHE   A CB   1 
ATOM   213  C  CG   . PHE   A 1 36  ? 11.160 13.950  18.348  1.00 88.62  ? 57  PHE   A CG   1 
ATOM   214  C  CD1  . PHE   A 1 36  ? 10.777 12.620  18.337  1.00 88.02  ? 57  PHE   A CD1  1 
ATOM   215  C  CD2  . PHE   A 1 36  ? 10.908 14.726  17.229  1.00 99.97  ? 57  PHE   A CD2  1 
ATOM   216  C  CE1  . PHE   A 1 36  ? 10.159 12.073  17.230  1.00 91.29  ? 57  PHE   A CE1  1 
ATOM   217  C  CE2  . PHE   A 1 36  ? 10.289 14.186  16.119  1.00 101.04 ? 57  PHE   A CE2  1 
ATOM   218  C  CZ   . PHE   A 1 36  ? 9.914  12.857  16.119  1.00 95.72  ? 57  PHE   A CZ   1 
ATOM   219  N  N    . CYS   A 1 37  ? 12.094 15.715  22.481  1.00 79.83  ? 58  CYS   A N    1 
ATOM   220  C  CA   . CYS   A 1 37  ? 13.056 16.197  23.464  1.00 80.43  ? 58  CYS   A CA   1 
ATOM   221  C  C    . CYS   A 1 37  ? 12.818 15.568  24.830  1.00 78.45  ? 58  CYS   A C    1 
ATOM   222  O  O    . CYS   A 1 37  ? 13.754 15.064  25.463  1.00 75.73  ? 58  CYS   A O    1 
ATOM   223  C  CB   . CYS   A 1 37  ? 12.983 17.720  23.539  1.00 79.56  ? 58  CYS   A CB   1 
ATOM   224  S  SG   . CYS   A 1 37  ? 13.241 18.515  21.938  1.00 75.81  ? 58  CYS   A SG   1 
ATOM   225  N  N    . MET   A 1 38  ? 11.571 15.586  25.303  1.00 76.89  ? 59  MET   A N    1 
ATOM   226  C  CA   . MET   A 1 38  ? 11.279 15.010  26.611  1.00 77.94  ? 59  MET   A CA   1 
ATOM   227  C  C    . MET   A 1 38  ? 11.540 13.509  26.624  1.00 75.83  ? 59  MET   A C    1 
ATOM   228  O  O    . MET   A 1 38  ? 12.040 12.968  27.617  1.00 75.60  ? 59  MET   A O    1 
ATOM   229  C  CB   . MET   A 1 38  ? 9.835  15.312  27.008  1.00 76.08  ? 59  MET   A CB   1 
ATOM   230  N  N    . PHE   A 1 39  ? 11.222 12.821  25.525  1.00 78.31  ? 60  PHE   A N    1 
ATOM   231  C  CA   . PHE   A 1 39  ? 11.422 11.375  25.474  1.00 80.67  ? 60  PHE   A CA   1 
ATOM   232  C  C    . PHE   A 1 39  ? 12.902 11.014  25.514  1.00 79.43  ? 60  PHE   A C    1 
ATOM   233  O  O    . PHE   A 1 39  ? 13.291 10.033  26.161  1.00 68.85  ? 60  PHE   A O    1 
ATOM   234  C  CB   . PHE   A 1 39  ? 10.764 10.799  24.220  1.00 81.80  ? 60  PHE   A CB   1 
ATOM   235  C  CG   . PHE   A 1 39  ? 11.140 9.370   23.941  1.00 81.51  ? 60  PHE   A CG   1 
ATOM   236  C  CD1  . PHE   A 1 39  ? 10.648 8.343   24.729  1.00 80.92  ? 60  PHE   A CD1  1 
ATOM   237  C  CD2  . PHE   A 1 39  ? 11.981 9.053   22.887  1.00 81.64  ? 60  PHE   A CD2  1 
ATOM   238  C  CE1  . PHE   A 1 39  ? 10.989 7.027   24.473  1.00 77.36  ? 60  PHE   A CE1  1 
ATOM   239  C  CE2  . PHE   A 1 39  ? 12.326 7.738   22.626  1.00 81.02  ? 60  PHE   A CE2  1 
ATOM   240  C  CZ   . PHE   A 1 39  ? 11.829 6.724   23.421  1.00 74.94  ? 60  PHE   A CZ   1 
ATOM   241  N  N    . ASP   A 1 40  ? 13.741 11.792  24.827  1.00 84.45  ? 61  ASP   A N    1 
ATOM   242  C  CA   . ASP   A 1 40  ? 15.170 11.497  24.795  1.00 78.57  ? 61  ASP   A CA   1 
ATOM   243  C  C    . ASP   A 1 40  ? 15.815 11.717  26.157  1.00 77.69  ? 61  ASP   A C    1 
ATOM   244  O  O    . ASP   A 1 40  ? 16.719 10.970  26.548  1.00 73.88  ? 61  ASP   A O    1 
ATOM   245  C  CB   . ASP   A 1 40  ? 15.860 12.354  23.736  1.00 81.63  ? 61  ASP   A CB   1 
ATOM   246  C  CG   . ASP   A 1 40  ? 15.566 11.885  22.326  1.00 79.89  ? 61  ASP   A CG   1 
ATOM   247  O  OD1  . ASP   A 1 40  ? 14.946 10.810  22.172  1.00 75.83  ? 61  ASP   A OD1  1 
ATOM   248  O  OD2  . ASP   A 1 40  ? 15.958 12.593  21.373  1.00 72.45  ? 61  ASP   A OD2  1 
ATOM   249  N  N    . MET   A 1 41  ? 15.370 12.740  26.890  1.00 82.46  ? 62  MET   A N    1 
ATOM   250  C  CA   . MET   A 1 41  ? 15.971 13.027  28.187  1.00 76.61  ? 62  MET   A CA   1 
ATOM   251  C  C    . MET   A 1 41  ? 15.589 11.976  29.220  1.00 71.94  ? 62  MET   A C    1 
ATOM   252  O  O    . MET   A 1 41  ? 16.415 11.595  30.058  1.00 74.62  ? 62  MET   A O    1 
ATOM   253  C  CB   . MET   A 1 41  ? 15.564 14.420  28.662  1.00 72.20  ? 62  MET   A CB   1 
ATOM   254  C  CG   . MET   A 1 41  ? 16.187 15.542  27.855  1.00 77.29  ? 62  MET   A CG   1 
ATOM   255  S  SD   . MET   A 1 41  ? 16.318 17.075  28.790  1.00 86.90  ? 62  MET   A SD   1 
ATOM   256  C  CE   . MET   A 1 41  ? 14.591 17.424  29.117  1.00 88.05  ? 62  MET   A CE   1 
ATOM   257  N  N    . GLU   A 1 42  ? 14.346 11.496  29.179  1.00 71.98  ? 63  GLU   A N    1 
ATOM   258  C  CA   . GLU   A 1 42  ? 13.916 10.481  30.135  1.00 77.25  ? 63  GLU   A CA   1 
ATOM   259  C  C    . GLU   A 1 42  ? 14.695 9.185   29.948  1.00 78.44  ? 63  GLU   A C    1 
ATOM   260  O  O    . GLU   A 1 42  ? 15.182 8.594   30.918  1.00 79.98  ? 63  GLU   A O    1 
ATOM   261  C  CB   . GLU   A 1 42  ? 12.415 10.229  29.998  1.00 77.31  ? 63  GLU   A CB   1 
ATOM   262  C  CG   . GLU   A 1 42  ? 11.545 11.430  30.326  1.00 79.55  ? 63  GLU   A CG   1 
ATOM   263  C  CD   . GLU   A 1 42  ? 10.074 11.074  30.417  1.00 82.41  ? 63  GLU   A CD   1 
ATOM   264  O  OE1  . GLU   A 1 42  ? 9.714  10.252  31.285  1.00 82.99  ? 63  GLU   A OE1  1 
ATOM   265  O  OE2  . GLU   A 1 42  ? 9.278  11.607  29.614  1.00 86.78  ? 63  GLU   A OE2  1 
ATOM   266  N  N    . CYS   A 1 43  ? 14.823 8.726   28.700  1.00 75.49  ? 64  CYS   A N    1 
ATOM   267  C  CA   . CYS   A 1 43  ? 15.511 7.464   28.452  1.00 74.00  ? 64  CYS   A CA   1 
ATOM   268  C  C    . CYS   A 1 43  ? 17.000 7.561   28.755  1.00 73.27  ? 64  CYS   A C    1 
ATOM   269  O  O    . CYS   A 1 43  ? 17.631 6.543   29.063  1.00 72.40  ? 64  CYS   A O    1 
ATOM   270  C  CB   . CYS   A 1 43  ? 15.289 7.012   27.008  1.00 76.97  ? 64  CYS   A CB   1 
ATOM   271  S  SG   . CYS   A 1 43  ? 13.607 6.449   26.661  1.00 93.15  ? 64  CYS   A SG   1 
ATOM   272  N  N    . HIS   A 1 44  ? 17.578 8.762   28.674  1.00 73.43  ? 65  HIS   A N    1 
ATOM   273  C  CA   . HIS   A 1 44  ? 18.991 8.914   29.003  1.00 74.48  ? 65  HIS   A CA   1 
ATOM   274  C  C    . HIS   A 1 44  ? 19.241 8.752   30.497  1.00 82.79  ? 65  HIS   A C    1 
ATOM   275  O  O    . HIS   A 1 44  ? 20.294 8.240   30.898  1.00 84.08  ? 65  HIS   A O    1 
ATOM   276  C  CB   . HIS   A 1 44  ? 19.503 10.270  28.526  1.00 74.45  ? 65  HIS   A CB   1 
ATOM   277  C  CG   . HIS   A 1 44  ? 20.957 10.492  28.805  1.00 72.38  ? 65  HIS   A CG   1 
ATOM   278  N  ND1  . HIS   A 1 44  ? 21.890 9.479   28.733  1.00 68.24  ? 65  HIS   A ND1  1 
ATOM   279  C  CD2  . HIS   A 1 44  ? 21.640 11.607  29.156  1.00 73.00  ? 65  HIS   A CD2  1 
ATOM   280  C  CE1  . HIS   A 1 44  ? 23.084 9.961   29.028  1.00 71.70  ? 65  HIS   A CE1  1 
ATOM   281  N  NE2  . HIS   A 1 44  ? 22.960 11.250  29.288  1.00 75.46  ? 65  HIS   A NE2  1 
ATOM   282  N  N    . LYS   A 1 45  ? 18.290 9.172   31.333  1.00 82.80  ? 66  LYS   A N    1 
ATOM   283  C  CA   . LYS   A 1 45  ? 18.462 9.025   32.774  1.00 75.58  ? 66  LYS   A CA   1 
ATOM   284  C  C    . LYS   A 1 45  ? 18.289 7.575   33.205  1.00 75.23  ? 66  LYS   A C    1 
ATOM   285  O  O    . LYS   A 1 45  ? 19.082 7.061   34.002  1.00 84.73  ? 66  LYS   A O    1 
ATOM   286  C  CB   . LYS   A 1 45  ? 17.476 9.928   33.516  1.00 78.41  ? 66  LYS   A CB   1 
ATOM   287  N  N    . LYS   A 1 46  ? 17.267 6.898   32.682  1.00 75.74  ? 67  LYS   A N    1 
ATOM   288  C  CA   . LYS   A 1 46  ? 16.958 5.543   33.128  1.00 77.99  ? 67  LYS   A CA   1 
ATOM   289  C  C    . LYS   A 1 46  ? 17.823 4.506   32.420  1.00 78.70  ? 67  LYS   A C    1 
ATOM   290  O  O    . LYS   A 1 46  ? 18.573 3.763   33.063  1.00 76.18  ? 67  LYS   A O    1 
ATOM   291  C  CB   . LYS   A 1 46  ? 15.473 5.244   32.903  1.00 75.81  ? 67  LYS   A CB   1 
ATOM   292  N  N    . TYR   A 1 47  ? 17.734 4.444   31.094  1.00 82.34  ? 68  TYR   A N    1 
ATOM   293  C  CA   . TYR   A 1 47  ? 18.342 3.358   30.334  1.00 80.06  ? 68  TYR   A CA   1 
ATOM   294  C  C    . TYR   A 1 47  ? 19.831 3.561   30.060  1.00 76.07  ? 68  TYR   A C    1 
ATOM   295  O  O    . TYR   A 1 47  ? 20.391 2.839   29.228  1.00 69.42  ? 68  TYR   A O    1 
ATOM   296  C  CB   . TYR   A 1 47  ? 17.582 3.158   29.022  1.00 74.53  ? 68  TYR   A CB   1 
ATOM   297  C  CG   . TYR   A 1 47  ? 16.136 2.770   29.227  1.00 75.12  ? 68  TYR   A CG   1 
ATOM   298  C  CD1  . TYR   A 1 47  ? 15.795 1.489   29.637  1.00 76.11  ? 68  TYR   A CD1  1 
ATOM   299  C  CD2  . TYR   A 1 47  ? 15.113 3.686   29.018  1.00 82.00  ? 68  TYR   A CD2  1 
ATOM   300  C  CE1  . TYR   A 1 47  ? 14.474 1.126   29.830  1.00 81.22  ? 68  TYR   A CE1  1 
ATOM   301  C  CE2  . TYR   A 1 47  ? 13.789 3.334   29.208  1.00 89.08  ? 68  TYR   A CE2  1 
ATOM   302  C  CZ   . TYR   A 1 47  ? 13.475 2.052   29.613  1.00 87.25  ? 68  TYR   A CZ   1 
ATOM   303  O  OH   . TYR   A 1 47  ? 12.160 1.693   29.804  1.00 88.94  ? 68  TYR   A OH   1 
ATOM   304  N  N    . GLY   A 1 48  ? 20.480 4.511   30.730  1.00 79.24  ? 69  GLY   A N    1 
ATOM   305  C  CA   . GLY   A 1 48  ? 21.929 4.596   30.707  1.00 77.53  ? 69  GLY   A CA   1 
ATOM   306  C  C    . GLY   A 1 48  ? 22.533 5.474   29.630  1.00 76.17  ? 69  GLY   A C    1 
ATOM   307  O  O    . GLY   A 1 48  ? 21.920 6.451   29.188  1.00 78.89  ? 69  GLY   A O    1 
ATOM   308  N  N    . LYS   A 1 49  ? 23.754 5.135   29.210  1.00 78.63  ? 70  LYS   A N    1 
ATOM   309  C  CA   . LYS   A 1 49  ? 24.464 5.892   28.186  1.00 79.26  ? 70  LYS   A CA   1 
ATOM   310  C  C    . LYS   A 1 49  ? 24.106 5.455   26.773  1.00 77.86  ? 70  LYS   A C    1 
ATOM   311  O  O    . LYS   A 1 49  ? 24.174 6.270   25.845  1.00 71.64  ? 70  LYS   A O    1 
ATOM   312  C  CB   . LYS   A 1 49  ? 25.977 5.764   28.388  1.00 76.36  ? 70  LYS   A CB   1 
ATOM   313  N  N    . VAL   A 1 50  ? 23.736 4.190   26.585  1.00 80.11  ? 71  VAL   A N    1 
ATOM   314  C  CA   . VAL   A 1 50  ? 23.331 3.664   25.287  1.00 77.76  ? 71  VAL   A CA   1 
ATOM   315  C  C    . VAL   A 1 50  ? 22.041 2.878   25.471  1.00 78.53  ? 71  VAL   A C    1 
ATOM   316  O  O    . VAL   A 1 50  ? 21.971 1.983   26.320  1.00 81.47  ? 71  VAL   A O    1 
ATOM   317  C  CB   . VAL   A 1 50  ? 24.422 2.773   24.660  1.00 82.29  ? 71  VAL   A CB   1 
ATOM   318  C  CG1  . VAL   A 1 50  ? 23.890 2.075   23.419  1.00 78.09  ? 71  VAL   A CG1  1 
ATOM   319  C  CG2  . VAL   A 1 50  ? 25.656 3.600   24.317  1.00 89.08  ? 71  VAL   A CG2  1 
ATOM   320  N  N    . TRP   A 1 51  ? 21.021 3.217   24.682  1.00 81.49  ? 72  TRP   A N    1 
ATOM   321  C  CA   . TRP   A 1 51  ? 19.750 2.508   24.714  1.00 77.26  ? 72  TRP   A CA   1 
ATOM   322  C  C    . TRP   A 1 51  ? 19.189 2.423   23.300  1.00 75.19  ? 72  TRP   A C    1 
ATOM   323  O  O    . TRP   A 1 51  ? 19.715 3.025   22.360  1.00 73.38  ? 72  TRP   A O    1 
ATOM   324  C  CB   . TRP   A 1 51  ? 18.751 3.180   25.668  1.00 73.27  ? 72  TRP   A CB   1 
ATOM   325  C  CG   . TRP   A 1 51  ? 18.209 4.498   25.199  1.00 75.66  ? 72  TRP   A CG   1 
ATOM   326  C  CD1  . TRP   A 1 51  ? 17.042 4.709   24.524  1.00 80.96  ? 72  TRP   A CD1  1 
ATOM   327  C  CD2  . TRP   A 1 51  ? 18.801 5.790   25.389  1.00 67.69  ? 72  TRP   A CD2  1 
ATOM   328  N  NE1  . TRP   A 1 51  ? 16.874 6.049   24.274  1.00 78.41  ? 72  TRP   A NE1  1 
ATOM   329  C  CE2  . TRP   A 1 51  ? 17.940 6.734   24.795  1.00 71.94  ? 72  TRP   A CE2  1 
ATOM   330  C  CE3  . TRP   A 1 51  ? 19.976 6.239   25.998  1.00 65.58  ? 72  TRP   A CE3  1 
ATOM   331  C  CZ2  . TRP   A 1 51  ? 18.217 8.099   24.792  1.00 73.22  ? 72  TRP   A CZ2  1 
ATOM   332  C  CZ3  . TRP   A 1 51  ? 20.249 7.594   25.993  1.00 67.97  ? 72  TRP   A CZ3  1 
ATOM   333  C  CH2  . TRP   A 1 51  ? 19.373 8.508   25.396  1.00 67.74  ? 72  TRP   A CH2  1 
ATOM   334  N  N    . GLY   A 1 52  ? 18.116 1.658   23.156  1.00 75.63  ? 73  GLY   A N    1 
ATOM   335  C  CA   . GLY   A 1 52  ? 17.520 1.431   21.853  1.00 74.13  ? 73  GLY   A CA   1 
ATOM   336  C  C    . GLY   A 1 52  ? 16.011 1.363   21.942  1.00 72.98  ? 73  GLY   A C    1 
ATOM   337  O  O    . GLY   A 1 52  ? 15.444 0.895   22.931  1.00 76.29  ? 73  GLY   A O    1 
ATOM   338  N  N    . PHE   A 1 53  ? 15.363 1.841   20.886  1.00 77.73  ? 74  PHE   A N    1 
ATOM   339  C  CA   . PHE   A 1 53  ? 13.910 1.813   20.777  1.00 80.33  ? 74  PHE   A CA   1 
ATOM   340  C  C    . PHE   A 1 53  ? 13.555 1.605   19.308  1.00 77.61  ? 74  PHE   A C    1 
ATOM   341  O  O    . PHE   A 1 53  ? 14.430 1.370   18.469  1.00 78.39  ? 74  PHE   A O    1 
ATOM   342  C  CB   . PHE   A 1 53  ? 13.295 3.089   21.367  1.00 83.97  ? 74  PHE   A CB   1 
ATOM   343  C  CG   . PHE   A 1 53  ? 13.840 4.359   20.777  1.00 81.10  ? 74  PHE   A CG   1 
ATOM   344  C  CD1  . PHE   A 1 53  ? 15.000 4.930   21.275  1.00 76.16  ? 74  PHE   A CD1  1 
ATOM   345  C  CD2  . PHE   A 1 53  ? 13.185 4.988   19.731  1.00 79.94  ? 74  PHE   A CD2  1 
ATOM   346  C  CE1  . PHE   A 1 53  ? 15.502 6.097   20.735  1.00 78.51  ? 74  PHE   A CE1  1 
ATOM   347  C  CE2  . PHE   A 1 53  ? 13.680 6.157   19.188  1.00 78.42  ? 74  PHE   A CE2  1 
ATOM   348  C  CZ   . PHE   A 1 53  ? 14.840 6.713   19.692  1.00 81.45  ? 74  PHE   A CZ   1 
ATOM   349  N  N    . TYR   A 1 54  ? 12.265 1.688   18.991  1.00 73.73  ? 75  TYR   A N    1 
ATOM   350  C  CA   . TYR   A 1 54  ? 11.802 1.392   17.642  1.00 83.58  ? 75  TYR   A CA   1 
ATOM   351  C  C    . TYR   A 1 54  ? 10.804 2.442   17.182  1.00 92.22  ? 75  TYR   A C    1 
ATOM   352  O  O    . TYR   A 1 54  ? 9.820  2.714   17.876  1.00 90.15  ? 75  TYR   A O    1 
ATOM   353  C  CB   . TYR   A 1 54  ? 11.164 0.000   17.571  1.00 83.73  ? 75  TYR   A CB   1 
ATOM   354  C  CG   . TYR   A 1 54  ? 12.104 -1.117  17.951  1.00 82.67  ? 75  TYR   A CG   1 
ATOM   355  C  CD1  . TYR   A 1 54  ? 12.212 -1.540  19.268  1.00 82.42  ? 75  TYR   A CD1  1 
ATOM   356  C  CD2  . TYR   A 1 54  ? 12.889 -1.746  16.995  1.00 85.69  ? 75  TYR   A CD2  1 
ATOM   357  C  CE1  . TYR   A 1 54  ? 13.071 -2.559  19.623  1.00 80.13  ? 75  TYR   A CE1  1 
ATOM   358  C  CE2  . TYR   A 1 54  ? 13.752 -2.765  17.340  1.00 83.51  ? 75  TYR   A CE2  1 
ATOM   359  C  CZ   . TYR   A 1 54  ? 13.838 -3.168  18.657  1.00 79.64  ? 75  TYR   A CZ   1 
ATOM   360  O  OH   . TYR   A 1 54  ? 14.695 -4.183  19.012  1.00 82.61  ? 75  TYR   A OH   1 
ATOM   361  N  N    . ASP   A 1 55  ? 11.068 3.030   16.014  1.00 92.00  ? 76  ASP   A N    1 
ATOM   362  C  CA   . ASP   A 1 55  ? 10.086 3.860   15.319  1.00 87.38  ? 76  ASP   A CA   1 
ATOM   363  C  C    . ASP   A 1 55  ? 9.346  2.957   14.338  1.00 88.52  ? 76  ASP   A C    1 
ATOM   364  O  O    . ASP   A 1 55  ? 9.640  2.899   13.142  1.00 96.37  ? 76  ASP   A O    1 
ATOM   365  C  CB   . ASP   A 1 55  ? 10.760 5.036   14.622  1.00 90.82  ? 76  ASP   A CB   1 
ATOM   366  C  CG   . ASP   A 1 55  ? 11.241 6.095   15.596  1.00 88.26  ? 76  ASP   A CG   1 
ATOM   367  O  OD1  . ASP   A 1 55  ? 10.690 6.168   16.714  1.00 91.64  ? 76  ASP   A OD1  1 
ATOM   368  O  OD2  . ASP   A 1 55  ? 12.163 6.859   15.241  1.00 85.68  ? 76  ASP   A OD2  1 
ATOM   369  N  N    . GLY   A 1 56  ? 8.369  2.228   14.871  1.00 87.29  ? 77  GLY   A N    1 
ATOM   370  C  CA   . GLY   A 1 56  ? 7.684  1.208   14.103  1.00 95.24  ? 77  GLY   A CA   1 
ATOM   371  C  C    . GLY   A 1 56  ? 8.505  -0.061  14.022  1.00 93.67  ? 77  GLY   A C    1 
ATOM   372  O  O    . GLY   A 1 56  ? 8.777  -0.697  15.044  1.00 93.55  ? 77  GLY   A O    1 
ATOM   373  N  N    . GLN   A 1 57  ? 8.909  -0.441  12.813  1.00 97.92  ? 78  GLN   A N    1 
ATOM   374  C  CA   . GLN   A 1 57  ? 9.814  -1.567  12.632  1.00 102.57 ? 78  GLN   A CA   1 
ATOM   375  C  C    . GLN   A 1 57  ? 11.273 -1.141  12.532  1.00 96.49  ? 78  GLN   A C    1 
ATOM   376  O  O    . GLN   A 1 57  ? 12.154 -2.007  12.523  1.00 96.68  ? 78  GLN   A O    1 
ATOM   377  C  CB   . GLN   A 1 57  ? 9.430  -2.367  11.379  1.00 108.56 ? 78  GLN   A CB   1 
ATOM   378  C  CG   . GLN   A 1 57  ? 8.565  -3.592  11.655  1.00 100.49 ? 78  GLN   A CG   1 
ATOM   379  C  CD   . GLN   A 1 57  ? 7.175  -3.235  12.142  1.00 100.78 ? 78  GLN   A CD   1 
ATOM   380  O  OE1  . GLN   A 1 57  ? 6.763  -3.644  13.227  1.00 100.94 ? 78  GLN   A OE1  1 
ATOM   381  N  NE2  . GLN   A 1 57  ? 6.440  -2.477  11.334  1.00 99.71  ? 78  GLN   A NE2  1 
ATOM   382  N  N    . GLN   A 1 58  ? 11.545 0.157   12.462  1.00 94.60  ? 79  GLN   A N    1 
ATOM   383  C  CA   . GLN   A 1 58  ? 12.910 0.637   12.292  1.00 93.68  ? 79  GLN   A CA   1 
ATOM   384  C  C    . GLN   A 1 58  ? 13.636 0.633   13.632  1.00 88.27  ? 79  GLN   A C    1 
ATOM   385  O  O    . GLN   A 1 58  ? 13.214 1.340   14.554  1.00 83.85  ? 79  GLN   A O    1 
ATOM   386  C  CB   . GLN   A 1 58  ? 12.913 2.041   11.700  1.00 91.22  ? 79  GLN   A CB   1 
ATOM   387  C  CG   . GLN   A 1 58  ? 14.296 2.655   11.572  1.00 83.96  ? 79  GLN   A CG   1 
ATOM   388  C  CD   . GLN   A 1 58  ? 15.175 1.906   10.590  1.00 88.78  ? 79  GLN   A CD   1 
ATOM   389  O  OE1  . GLN   A 1 58  ? 16.257 1.436   10.940  1.00 85.19  ? 79  GLN   A OE1  1 
ATOM   390  N  NE2  . GLN   A 1 58  ? 14.715 1.798   9.348   1.00 92.54  ? 79  GLN   A NE2  1 
ATOM   391  N  N    . PRO   A 1 59  ? 14.711 -0.136  13.784  1.00 89.13  ? 80  PRO   A N    1 
ATOM   392  C  CA   . PRO   A 1 59  ? 15.466 -0.106  15.040  1.00 81.16  ? 80  PRO   A CA   1 
ATOM   393  C  C    . PRO   A 1 59  ? 16.323 1.145   15.132  1.00 79.86  ? 80  PRO   A C    1 
ATOM   394  O  O    . PRO   A 1 59  ? 16.998 1.536   14.177  1.00 82.88  ? 80  PRO   A O    1 
ATOM   395  C  CB   . PRO   A 1 59  ? 16.331 -1.369  14.959  1.00 79.60  ? 80  PRO   A CB   1 
ATOM   396  C  CG   . PRO   A 1 59  ? 16.549 -1.559  13.497  1.00 87.70  ? 80  PRO   A CG   1 
ATOM   397  C  CD   . PRO   A 1 59  ? 15.285 -1.087  12.816  1.00 92.60  ? 80  PRO   A CD   1 
ATOM   398  N  N    . VAL   A 1 60  ? 16.286 1.778   16.301  1.00 77.26  ? 81  VAL   A N    1 
ATOM   399  C  CA   . VAL   A 1 60  ? 17.013 3.016   16.550  1.00 76.20  ? 81  VAL   A CA   1 
ATOM   400  C  C    . VAL   A 1 60  ? 17.887 2.822   17.779  1.00 74.70  ? 81  VAL   A C    1 
ATOM   401  O  O    . VAL   A 1 60  ? 17.400 2.381   18.826  1.00 79.46  ? 81  VAL   A O    1 
ATOM   402  C  CB   . VAL   A 1 60  ? 16.060 4.209   16.748  1.00 79.50  ? 81  VAL   A CB   1 
ATOM   403  C  CG1  . VAL   A 1 60  ? 16.848 5.465   17.075  1.00 73.87  ? 81  VAL   A CG1  1 
ATOM   404  C  CG2  . VAL   A 1 60  ? 15.198 4.414   15.509  1.00 82.63  ? 81  VAL   A CG2  1 
ATOM   405  N  N    . LEU   A 1 61  ? 19.170 3.152   17.653  1.00 70.53  ? 82  LEU   A N    1 
ATOM   406  C  CA   . LEU   A 1 61  ? 20.128 3.038   18.745  1.00 69.33  ? 82  LEU   A CA   1 
ATOM   407  C  C    . LEU   A 1 61  ? 20.608 4.424   19.151  1.00 68.95  ? 82  LEU   A C    1 
ATOM   408  O  O    . LEU   A 1 61  ? 21.111 5.182   18.314  1.00 65.34  ? 82  LEU   A O    1 
ATOM   409  C  CB   . LEU   A 1 61  ? 21.322 2.171   18.344  1.00 72.30  ? 82  LEU   A CB   1 
ATOM   410  C  CG   . LEU   A 1 61  ? 22.378 1.990   19.435  1.00 77.60  ? 82  LEU   A CG   1 
ATOM   411  C  CD1  . LEU   A 1 61  ? 21.892 1.011   20.492  1.00 86.89  ? 82  LEU   A CD1  1 
ATOM   412  C  CD2  . LEU   A 1 61  ? 23.699 1.539   18.841  1.00 79.60  ? 82  LEU   A CD2  1 
ATOM   413  N  N    . ALA   A 1 62  ? 20.459 4.748   20.431  1.00 73.84  ? 83  ALA   A N    1 
ATOM   414  C  CA   . ALA   A 1 62  ? 20.916 6.019   20.976  1.00 71.39  ? 83  ALA   A CA   1 
ATOM   415  C  C    . ALA   A 1 62  ? 22.284 5.832   21.617  1.00 71.15  ? 83  ALA   A C    1 
ATOM   416  O  O    . ALA   A 1 62  ? 22.501 4.869   22.359  1.00 71.83  ? 83  ALA   A O    1 
ATOM   417  C  CB   . ALA   A 1 62  ? 19.919 6.566   21.998  1.00 61.87  ? 83  ALA   A CB   1 
ATOM   418  N  N    . ILE   A 1 63  ? 23.208 6.743   21.317  1.00 71.00  ? 84  ILE   A N    1 
ATOM   419  C  CA   . ILE   A 1 63  ? 24.546 6.724   21.894  1.00 76.15  ? 84  ILE   A CA   1 
ATOM   420  C  C    . ILE   A 1 63  ? 24.848 8.105   22.456  1.00 74.51  ? 84  ILE   A C    1 
ATOM   421  O  O    . ILE   A 1 63  ? 24.438 9.123   21.887  1.00 61.29  ? 84  ILE   A O    1 
ATOM   422  C  CB   . ILE   A 1 63  ? 25.625 6.300   20.870  1.00 76.39  ? 84  ILE   A CB   1 
ATOM   423  C  CG1  . ILE   A 1 63  ? 25.684 7.276   19.692  1.00 72.43  ? 84  ILE   A CG1  1 
ATOM   424  C  CG2  . ILE   A 1 63  ? 25.376 4.878   20.381  1.00 76.02  ? 84  ILE   A CG2  1 
ATOM   425  C  CD1  . ILE   A 1 63  ? 26.784 6.965   18.695  1.00 69.90  ? 84  ILE   A CD1  1 
ATOM   426  N  N    . THR   A 1 64  ? 25.550 8.134   23.589  1.00 79.50  ? 85  THR   A N    1 
ATOM   427  C  CA   . THR   A 1 64  ? 25.967 9.375   24.221  1.00 74.69  ? 85  THR   A CA   1 
ATOM   428  C  C    . THR   A 1 64  ? 27.469 9.466   24.430  1.00 77.61  ? 85  THR   A C    1 
ATOM   429  O  O    . THR   A 1 64  ? 27.968 10.557  24.732  1.00 77.78  ? 85  THR   A O    1 
ATOM   430  C  CB   . THR   A 1 64  ? 25.268 9.554   25.579  1.00 71.42  ? 85  THR   A CB   1 
ATOM   431  O  OG1  . THR   A 1 64  ? 25.644 8.484   26.456  1.00 78.76  ? 85  THR   A OG1  1 
ATOM   432  C  CG2  . THR   A 1 64  ? 23.755 9.559   25.409  1.00 65.12  ? 85  THR   A CG2  1 
ATOM   433  N  N    . ASP   A 1 65  ? 28.198 8.368   24.279  1.00 79.96  ? 86  ASP   A N    1 
ATOM   434  C  CA   . ASP   A 1 65  ? 29.640 8.366   24.468  1.00 82.92  ? 86  ASP   A CA   1 
ATOM   435  C  C    . ASP   A 1 65  ? 30.311 9.234   23.409  1.00 81.68  ? 86  ASP   A C    1 
ATOM   436  O  O    . ASP   A 1 65  ? 30.112 8.996   22.207  1.00 82.61  ? 86  ASP   A O    1 
ATOM   437  C  CB   . ASP   A 1 65  ? 30.171 6.937   24.401  1.00 85.76  ? 86  ASP   A CB   1 
ATOM   438  C  CG   . ASP   A 1 65  ? 31.652 6.852   24.700  1.00 87.92  ? 86  ASP   A CG   1 
ATOM   439  O  OD1  . ASP   A 1 65  ? 32.028 6.957   25.887  1.00 86.27  ? 86  ASP   A OD1  1 
ATOM   440  O  OD2  . ASP   A 1 65  ? 32.438 6.679   23.746  1.00 86.97  ? 86  ASP   A OD2  1 
ATOM   441  N  N    . PRO   A 1 66  ? 31.095 10.244  23.799  1.00 78.95  ? 87  PRO   A N    1 
ATOM   442  C  CA   . PRO   A 1 66  ? 31.726 11.114  22.792  1.00 80.37  ? 87  PRO   A CA   1 
ATOM   443  C  C    . PRO   A 1 66  ? 32.620 10.369  21.818  1.00 80.69  ? 87  PRO   A C    1 
ATOM   444  O  O    . PRO   A 1 66  ? 32.712 10.768  20.650  1.00 75.01  ? 87  PRO   A O    1 
ATOM   445  C  CB   . PRO   A 1 66  ? 32.525 12.109  23.645  1.00 76.18  ? 87  PRO   A CB   1 
ATOM   446  C  CG   . PRO   A 1 66  ? 31.835 12.114  24.966  1.00 78.17  ? 87  PRO   A CG   1 
ATOM   447  C  CD   . PRO   A 1 66  ? 31.352 10.708  25.172  1.00 82.72  ? 87  PRO   A CD   1 
ATOM   448  N  N    . ASP   A 1 67  ? 33.282 9.298   22.259  1.00 82.34  ? 88  ASP   A N    1 
ATOM   449  C  CA   . ASP   A 1 67  ? 34.121 8.531   21.344  1.00 87.09  ? 88  ASP   A CA   1 
ATOM   450  C  C    . ASP   A 1 67  ? 33.278 7.815   20.295  1.00 84.90  ? 88  ASP   A C    1 
ATOM   451  O  O    . ASP   A 1 67  ? 33.666 7.746   19.123  1.00 82.70  ? 88  ASP   A O    1 
ATOM   452  C  CB   . ASP   A 1 67  ? 34.980 7.535   22.123  1.00 86.37  ? 88  ASP   A CB   1 
ATOM   453  N  N    . MET   A 1 68  ? 32.132 7.290   20.725  1.00 82.80  ? 89  MET   A N    1 
ATOM   454  C  CA   . MET   A 1 68  ? 31.230 6.603   19.773  1.00 82.15  ? 89  MET   A CA   1 
ATOM   455  C  C    . MET   A 1 68  ? 30.705 7.669   18.817  1.00 80.30  ? 89  MET   A C    1 
ATOM   456  O  O    . MET   A 1 68  ? 30.622 7.406   17.604  1.00 76.16  ? 89  MET   A O    1 
ATOM   457  C  CB   . MET   A 1 68  ? 30.056 5.950   20.504  1.00 80.72  ? 89  MET   A CB   1 
ATOM   458  C  CG   . MET   A 1 68  ? 30.468 4.863   21.470  1.00 87.54  ? 89  MET   A CG   1 
ATOM   459  S  SD   . MET   A 1 68  ? 29.410 3.410   21.331  1.00 105.88 ? 89  MET   A SD   1 
ATOM   460  C  CE   . MET   A 1 68  ? 29.312 3.264   19.543  1.00 88.29  ? 89  MET   A CE   1 
ATOM   461  N  N    . ILE   A 1 69  ? 30.401 8.841   19.363  1.00 79.10  ? 90  ILE   A N    1 
ATOM   462  C  CA   . ILE   A 1 69  ? 29.844 9.935   18.520  1.00 78.36  ? 90  ILE   A CA   1 
ATOM   463  C  C    . ILE   A 1 69  ? 30.877 10.292  17.440  1.00 76.51  ? 90  ILE   A C    1 
ATOM   464  O  O    . ILE   A 1 69  ? 30.495 10.344  16.256  1.00 73.49  ? 90  ILE   A O    1 
ATOM   465  C  CB   . ILE   A 1 69  ? 29.457 11.127  19.410  1.00 71.95  ? 90  ILE   A CB   1 
ATOM   466  C  CG1  . ILE   A 1 69  ? 28.210 10.810  20.232  1.00 66.56  ? 90  ILE   A CG1  1 
ATOM   467  C  CG2  . ILE   A 1 69  ? 29.279 12.397  18.579  1.00 72.98  ? 90  ILE   A CG2  1 
ATOM   468  C  CD1  . ILE   A 1 69  ? 27.991 11.731  21.416  1.00 62.18  ? 90  ILE   A CD1  1 
ATOM   469  N  N    . LYS   A 1 70  ? 32.138 10.479  17.827  1.00 77.98  ? 91  LYS   A N    1 
ATOM   470  C  CA   . LYS   A 1 70  ? 33.190 10.869  16.857  1.00 78.29  ? 91  LYS   A CA   1 
ATOM   471  C  C    . LYS   A 1 70  ? 33.328 9.775   15.808  1.00 77.19  ? 91  LYS   A C    1 
ATOM   472  O  O    . LYS   A 1 70  ? 33.496 10.094  14.620  1.00 74.39  ? 91  LYS   A O    1 
ATOM   473  C  CB   . LYS   A 1 70  ? 34.545 10.984  17.552  1.00 82.59  ? 91  LYS   A CB   1 
ATOM   474  N  N    . THR   A 1 71  ? 33.275 8.527   16.257  1.00 80.40  ? 92  THR   A N    1 
ATOM   475  C  CA   . THR   A 1 71  ? 33.415 7.398   15.329  1.00 81.32  ? 92  THR   A CA   1 
ATOM   476  C  C    . THR   A 1 71  ? 32.292 7.456   14.329  1.00 81.22  ? 92  THR   A C    1 
ATOM   477  O  O    . THR   A 1 71  ? 32.570 7.322   13.122  1.00 77.19  ? 92  THR   A O    1 
ATOM   478  C  CB   . THR   A 1 71  ? 33.366 6.114   16.150  1.00 81.07  ? 92  THR   A CB   1 
ATOM   479  O  OG1  . THR   A 1 71  ? 34.301 6.302   17.206  1.00 83.78  ? 92  THR   A OG1  1 
ATOM   480  C  CG2  . THR   A 1 71  ? 33.740 4.889   15.336  1.00 83.91  ? 92  THR   A CG2  1 
ATOM   481  N  N    . VAL   A 1 72  ? 31.067 7.679   14.801  1.00 78.85  ? 93  VAL   A N    1 
ATOM   482  C  CA   . VAL   A 1 72  ? 29.886 7.640   13.893  1.00 73.61  ? 93  VAL   A CA   1 
ATOM   483  C  C    . VAL   A 1 72  ? 29.917 8.845   12.951  1.00 70.68  ? 93  VAL   A C    1 
ATOM   484  O  O    . VAL   A 1 72  ? 29.647 8.652   11.755  1.00 73.67  ? 93  VAL   A O    1 
ATOM   485  C  CB   . VAL   A 1 72  ? 28.599 7.612   14.734  1.00 74.23  ? 93  VAL   A CB   1 
ATOM   486  C  CG1  . VAL   A 1 72  ? 27.362 7.899   13.895  1.00 69.75  ? 93  VAL   A CG1  1 
ATOM   487  C  CG2  . VAL   A 1 72  ? 28.443 6.294   15.480  1.00 68.45  ? 93  VAL   A CG2  1 
ATOM   488  N  N    . LEU   A 1 73  ? 30.262 10.028  13.456  1.00 70.39  ? 94  LEU   A N    1 
ATOM   489  C  CA   . LEU   A 1 73  ? 30.196 11.223  12.623  1.00 72.39  ? 94  LEU   A CA   1 
ATOM   490  C  C    . LEU   A 1 73  ? 31.488 11.514  11.872  1.00 79.25  ? 94  LEU   A C    1 
ATOM   491  O  O    . LEU   A 1 73  ? 31.435 12.040  10.753  1.00 79.92  ? 94  LEU   A O    1 
ATOM   492  C  CB   . LEU   A 1 73  ? 29.832 12.443  13.473  1.00 63.72  ? 94  LEU   A CB   1 
ATOM   493  C  CG   . LEU   A 1 73  ? 28.466 12.425  14.157  1.00 64.86  ? 94  LEU   A CG   1 
ATOM   494  C  CD1  . LEU   A 1 73  ? 28.184 13.771  14.801  1.00 74.47  ? 94  LEU   A CD1  1 
ATOM   495  C  CD2  . LEU   A 1 73  ? 27.370 12.061  13.173  1.00 59.76  ? 94  LEU   A CD2  1 
ATOM   496  N  N    . VAL   A 1 74  ? 32.645 11.193  12.450  1.00 78.18  ? 95  VAL   A N    1 
ATOM   497  C  CA   . VAL   A 1 74  ? 33.917 11.611  11.869  1.00 75.80  ? 95  VAL   A CA   1 
ATOM   498  C  C    . VAL   A 1 74  ? 34.751 10.409  11.441  1.00 80.22  ? 95  VAL   A C    1 
ATOM   499  O  O    . VAL   A 1 74  ? 35.051 10.245  10.253  1.00 85.45  ? 95  VAL   A O    1 
ATOM   500  C  CB   . VAL   A 1 74  ? 34.706 12.494  12.852  1.00 78.98  ? 95  VAL   A CB   1 
ATOM   501  C  CG1  . VAL   A 1 74  ? 35.928 13.089  12.168  1.00 83.26  ? 95  VAL   A CG1  1 
ATOM   502  C  CG2  . VAL   A 1 74  ? 33.812 13.588  13.415  1.00 83.77  ? 95  VAL   A CG2  1 
ATOM   503  N  N    . LYS   A 1 75  ? 35.139 9.570   12.404  1.00 83.12  ? 96  LYS   A N    1 
ATOM   504  C  CA   . LYS   A 1 75  ? 36.074 8.478   12.150  1.00 82.12  ? 96  LYS   A CA   1 
ATOM   505  C  C    . LYS   A 1 75  ? 35.562 7.523   11.078  1.00 82.75  ? 96  LYS   A C    1 
ATOM   506  O  O    . LYS   A 1 75  ? 36.118 7.464   9.977   1.00 81.33  ? 96  LYS   A O    1 
ATOM   507  C  CB   . LYS   A 1 75  ? 36.363 7.711   13.443  1.00 77.40  ? 96  LYS   A CB   1 
ATOM   508  N  N    . GLU   A 1 76  ? 34.509 6.776   11.386  1.00 83.09  ? 97  GLU   A N    1 
ATOM   509  C  CA   . GLU   A 1 76  ? 33.948 5.798   10.452  1.00 86.06  ? 97  GLU   A CA   1 
ATOM   510  C  C    . GLU   A 1 76  ? 32.741 6.363   9.711   1.00 80.68  ? 97  GLU   A C    1 
ATOM   511  O  O    . GLU   A 1 76  ? 31.689 5.731   9.622   1.00 78.09  ? 97  GLU   A O    1 
ATOM   512  C  CB   . GLU   A 1 76  ? 33.585 4.517   11.194  1.00 82.23  ? 97  GLU   A CB   1 
ATOM   513  C  CG   . GLU   A 1 76  ? 34.746 3.893   11.950  1.00 81.26  ? 97  GLU   A CG   1 
ATOM   514  C  CD   . GLU   A 1 76  ? 35.893 3.497   11.040  1.00 84.74  ? 97  GLU   A CD   1 
ATOM   515  O  OE1  . GLU   A 1 76  ? 35.631 3.118   9.878   1.00 86.80  ? 97  GLU   A OE1  1 
ATOM   516  O  OE2  . GLU   A 1 76  ? 37.057 3.571   11.487  1.00 83.72  ? 97  GLU   A OE2  1 
ATOM   517  N  N    . CYS   A 1 77  ? 32.885 7.569   9.162   1.00 76.76  ? 98  CYS   A N    1 
ATOM   518  C  CA   . CYS   A 1 77  ? 31.771 8.208   8.469   1.00 77.28  ? 98  CYS   A CA   1 
ATOM   519  C  C    . CYS   A 1 77  ? 31.583 7.635   7.069   1.00 78.92  ? 98  CYS   A C    1 
ATOM   520  O  O    . CYS   A 1 77  ? 30.506 7.132   6.731   1.00 77.63  ? 98  CYS   A O    1 
ATOM   521  C  CB   . CYS   A 1 77  ? 31.988 9.721   8.399   1.00 83.50  ? 98  CYS   A CB   1 
ATOM   522  S  SG   . CYS   A 1 77  ? 30.739 10.589  7.420   1.00 84.34  ? 98  CYS   A SG   1 
ATOM   523  N  N    . TYR   A 1 78  ? 32.623 7.712   6.235   1.00 82.21  ? 99  TYR   A N    1 
ATOM   524  C  CA   . TYR   A 1 78  ? 32.507 7.252   4.856   1.00 81.61  ? 99  TYR   A CA   1 
ATOM   525  C  C    . TYR   A 1 78  ? 32.257 5.753   4.761   1.00 81.65  ? 99  TYR   A C    1 
ATOM   526  O  O    . TYR   A 1 78  ? 31.748 5.284   3.737   1.00 85.54  ? 99  TYR   A O    1 
ATOM   527  C  CB   . TYR   A 1 78  ? 33.772 7.607   4.071   1.00 87.19  ? 99  TYR   A CB   1 
ATOM   528  C  CG   . TYR   A 1 78  ? 34.026 9.091   3.905   1.00 83.18  ? 99  TYR   A CG   1 
ATOM   529  C  CD1  . TYR   A 1 78  ? 33.345 9.829   2.945   1.00 79.41  ? 99  TYR   A CD1  1 
ATOM   530  C  CD2  . TYR   A 1 78  ? 34.965 9.748   4.691   1.00 82.37  ? 99  TYR   A CD2  1 
ATOM   531  C  CE1  . TYR   A 1 78  ? 33.579 11.184  2.782   1.00 78.05  ? 99  TYR   A CE1  1 
ATOM   532  C  CE2  . TYR   A 1 78  ? 35.207 11.104  4.534   1.00 87.43  ? 99  TYR   A CE2  1 
ATOM   533  C  CZ   . TYR   A 1 78  ? 34.510 11.817  3.578   1.00 84.02  ? 99  TYR   A CZ   1 
ATOM   534  O  OH   . TYR   A 1 78  ? 34.743 13.166  3.414   1.00 80.13  ? 99  TYR   A OH   1 
ATOM   535  N  N    . SER   A 1 79  ? 32.593 4.991   5.800   1.00 79.87  ? 100 SER   A N    1 
ATOM   536  C  CA   . SER   A 1 79  ? 32.591 3.536   5.722   1.00 78.60  ? 100 SER   A CA   1 
ATOM   537  C  C    . SER   A 1 79  ? 31.308 2.909   6.257   1.00 80.46  ? 100 SER   A C    1 
ATOM   538  O  O    . SER   A 1 79  ? 30.756 2.003   5.626   1.00 74.04  ? 100 SER   A O    1 
ATOM   539  C  CB   . SER   A 1 79  ? 33.802 2.975   6.477   1.00 85.36  ? 100 SER   A CB   1 
ATOM   540  O  OG   . SER   A 1 79  ? 33.841 3.466   7.808   1.00 84.44  ? 100 SER   A OG   1 
ATOM   541  N  N    . VAL   A 1 80  ? 30.815 3.367   7.408   1.00 80.14  ? 101 VAL   A N    1 
ATOM   542  C  CA   . VAL   A 1 80  ? 29.718 2.708   8.099   1.00 71.48  ? 101 VAL   A CA   1 
ATOM   543  C  C    . VAL   A 1 80  ? 28.549 3.650   8.348   1.00 67.65  ? 101 VAL   A C    1 
ATOM   544  O  O    . VAL   A 1 80  ? 27.386 3.258   8.193   1.00 69.07  ? 101 VAL   A O    1 
ATOM   545  C  CB   . VAL   A 1 80  ? 30.198 2.087   9.426   1.00 68.72  ? 101 VAL   A CB   1 
ATOM   546  N  N    . PHE   A 1 81  ? 28.825 4.888   8.744   1.00 69.58  ? 102 PHE   A N    1 
ATOM   547  C  CA   . PHE   A 1 81  ? 27.787 5.841   9.137   1.00 70.01  ? 102 PHE   A CA   1 
ATOM   548  C  C    . PHE   A 1 81  ? 27.894 7.076   8.247   1.00 68.44  ? 102 PHE   A C    1 
ATOM   549  O  O    . PHE   A 1 81  ? 28.561 8.051   8.600   1.00 71.57  ? 102 PHE   A O    1 
ATOM   550  C  CB   . PHE   A 1 81  ? 27.926 6.201   10.607  1.00 72.83  ? 102 PHE   A CB   1 
ATOM   551  C  CG   . PHE   A 1 81  ? 28.162 5.016   11.499  1.00 66.26  ? 102 PHE   A CG   1 
ATOM   552  C  CD1  . PHE   A 1 81  ? 27.100 4.252   11.946  1.00 64.36  ? 102 PHE   A CD1  1 
ATOM   553  C  CD2  . PHE   A 1 81  ? 29.445 4.669   11.890  1.00 63.88  ? 102 PHE   A CD2  1 
ATOM   554  C  CE1  . PHE   A 1 81  ? 27.311 3.163   12.764  1.00 67.29  ? 102 PHE   A CE1  1 
ATOM   555  C  CE2  . PHE   A 1 81  ? 29.662 3.579   12.709  1.00 64.93  ? 102 PHE   A CE2  1 
ATOM   556  C  CZ   . PHE   A 1 81  ? 28.593 2.825   13.147  1.00 70.04  ? 102 PHE   A CZ   1 
ATOM   557  N  N    . THR   A 1 82  ? 27.208 7.044   7.111   1.00 66.32  ? 103 THR   A N    1 
ATOM   558  C  CA   . THR   A 1 82  ? 27.350 8.073   6.089   1.00 69.94  ? 103 THR   A CA   1 
ATOM   559  C  C    . THR   A 1 82  ? 26.075 8.854   5.824   1.00 70.07  ? 103 THR   A C    1 
ATOM   560  O  O    . THR   A 1 82  ? 26.129 10.079  5.678   1.00 69.07  ? 103 THR   A O    1 
ATOM   561  C  CB   . THR   A 1 82  ? 27.835 7.442   4.773   1.00 72.69  ? 103 THR   A CB   1 
ATOM   562  O  OG1  . THR   A 1 82  ? 29.059 6.733   5.003   1.00 79.94  ? 103 THR   A OG1  1 
ATOM   563  C  CG2  . THR   A 1 82  ? 28.072 8.509   3.715   1.00 71.55  ? 103 THR   A CG2  1 
ATOM   564  N  N    . ASN   A 1 83  ? 24.926 8.188   5.763   1.00 74.50  ? 104 ASN   A N    1 
ATOM   565  C  CA   . ASN   A 1 83  ? 23.691 8.811   5.314   1.00 74.46  ? 104 ASN   A CA   1 
ATOM   566  C  C    . ASN   A 1 83  ? 22.666 8.866   6.440   1.00 69.87  ? 104 ASN   A C    1 
ATOM   567  O  O    . ASN   A 1 83  ? 22.787 8.184   7.461   1.00 66.46  ? 104 ASN   A O    1 
ATOM   568  C  CB   . ASN   A 1 83  ? 23.109 8.057   4.115   1.00 73.22  ? 104 ASN   A CB   1 
ATOM   569  C  CG   . ASN   A 1 83  ? 24.137 7.813   3.033   1.00 75.82  ? 104 ASN   A CG   1 
ATOM   570  O  OD1  . ASN   A 1 83  ? 24.988 8.662   2.769   1.00 76.12  ? 104 ASN   A OD1  1 
ATOM   571  N  ND2  . ASN   A 1 83  ? 24.073 6.642   2.408   1.00 74.86  ? 104 ASN   A ND2  1 
ATOM   572  N  N    . ARG   A 1 84  ? 21.643 9.687   6.228   1.00 67.87  ? 105 ARG   A N    1 
ATOM   573  C  CA   . ARG   A 1 84  ? 20.582 9.882   7.201   1.00 61.60  ? 105 ARG   A CA   1 
ATOM   574  C  C    . ARG   A 1 84  ? 19.398 8.964   6.898   1.00 68.94  ? 105 ARG   A C    1 
ATOM   575  O  O    . ARG   A 1 84  ? 19.319 8.324   5.847   1.00 74.32  ? 105 ARG   A O    1 
ATOM   576  C  CB   . ARG   A 1 84  ? 20.133 11.345  7.213   1.00 65.21  ? 105 ARG   A CB   1 
ATOM   577  C  CG   . ARG   A 1 84  ? 21.268 12.350  7.392   1.00 68.08  ? 105 ARG   A CG   1 
ATOM   578  C  CD   . ARG   A 1 84  ? 20.748 13.785  7.486   1.00 65.61  ? 105 ARG   A CD   1 
ATOM   579  N  NE   . ARG   A 1 84  ? 21.808 14.741  7.794   1.00 65.38  ? 105 ARG   A NE   1 
ATOM   580  C  CZ   . ARG   A 1 84  ? 22.383 15.541  6.905   1.00 64.25  ? 105 ARG   A CZ   1 
ATOM   581  N  NH1  . ARG   A 1 84  ? 22.018 15.536  5.634   1.00 77.22  ? 105 ARG   A NH1  1 
ATOM   582  N  NH2  . ARG   A 1 84  ? 23.345 16.369  7.303   1.00 56.91  ? 105 ARG   A NH2  1 
ATOM   583  N  N    . ARG   A 1 85  ? 18.447 8.920   7.828   1.00 73.23  ? 106 ARG   A N    1 
ATOM   584  C  CA   . ARG   A 1 85  ? 17.269 8.034   7.663   1.00 77.11  ? 106 ARG   A CA   1 
ATOM   585  C  C    . ARG   A 1 85  ? 16.334 8.618   6.601   1.00 77.18  ? 106 ARG   A C    1 
ATOM   586  O  O    . ARG   A 1 85  ? 16.151 9.844   6.585   1.00 79.87  ? 106 ARG   A O    1 
ATOM   587  C  CB   . ARG   A 1 85  ? 16.544 7.907   9.004   1.00 80.41  ? 106 ARG   A CB   1 
ATOM   588  C  CG   . ARG   A 1 85  ? 15.221 7.157   8.983   1.00 83.43  ? 106 ARG   A CG   1 
ATOM   589  C  CD   . ARG   A 1 85  ? 14.268 7.696   10.036  1.00 86.21  ? 106 ARG   A CD   1 
ATOM   590  N  NE   . ARG   A 1 85  ? 14.878 7.740   11.369  1.00 75.18  ? 106 ARG   A NE   1 
ATOM   591  C  CZ   . ARG   A 1 85  ? 14.285 7.298   12.469  1.00 78.02  ? 106 ARG   A CZ   1 
ATOM   592  N  NH1  . ARG   A 1 85  ? 13.173 6.594   12.379  1.00 82.65  ? 106 ARG   A NH1  1 
ATOM   593  N  NH2  . ARG   A 1 85  ? 14.801 7.565   13.654  1.00 82.46  ? 106 ARG   A NH2  1 
ATOM   594  N  N    . PRO   A 1 86  ? 15.742 7.795   5.715   1.00 81.66  ? 107 PRO   A N    1 
ATOM   595  C  CA   . PRO   A 1 86  ? 14.897 8.313   4.653   1.00 85.99  ? 107 PRO   A CA   1 
ATOM   596  C  C    . PRO   A 1 86  ? 13.848 9.261   5.186   1.00 89.57  ? 107 PRO   A C    1 
ATOM   597  O  O    . PRO   A 1 86  ? 13.171 8.932   6.173   1.00 87.50  ? 107 PRO   A O    1 
ATOM   598  C  CB   . PRO   A 1 86  ? 14.286 7.033   4.089   1.00 89.20  ? 107 PRO   A CB   1 
ATOM   599  C  CG   . PRO   A 1 86  ? 15.358 5.997   4.308   1.00 87.94  ? 107 PRO   A CG   1 
ATOM   600  C  CD   . PRO   A 1 86  ? 15.902 6.352   5.679   1.00 90.37  ? 107 PRO   A CD   1 
ATOM   601  N  N    . PHE   A 1 87  ? 13.705 10.393  4.540   1.00 96.21  ? 108 PHE   A N    1 
ATOM   602  C  CA   . PHE   A 1 87  ? 12.688 11.389  4.963   1.00 96.60  ? 108 PHE   A CA   1 
ATOM   603  C  C    . PHE   A 1 87  ? 11.333 10.798  4.690   1.00 97.33  ? 108 PHE   A C    1 
ATOM   604  O  O    . PHE   A 1 87  ? 10.566 10.538  5.634   1.00 96.82  ? 108 PHE   A O    1 
ATOM   605  C  CB   . PHE   A 1 87  ? 12.834 12.702  4.190   1.00 97.70  ? 108 PHE   A CB   1 
ATOM   606  C  CG   . PHE   A 1 87  ? 13.347 13.875  5.012   1.00 103.16 ? 108 PHE   A CG   1 
ATOM   607  C  CD1  . PHE   A 1 87  ? 12.638 14.336  6.115   1.00 107.74 ? 108 PHE   A CD1  1 
ATOM   608  C  CD2  . PHE   A 1 87  ? 14.538 14.511  4.682   1.00 105.69 ? 108 PHE   A CD2  1 
ATOM   609  C  CE1  . PHE   A 1 87  ? 13.110 15.403  6.865   1.00 110.60 ? 108 PHE   A CE1  1 
ATOM   610  C  CE2  . PHE   A 1 87  ? 15.005 15.576  5.436   1.00 113.07 ? 108 PHE   A CE2  1 
ATOM   611  C  CZ   . PHE   A 1 87  ? 14.291 16.020  6.525   1.00 110.64 ? 108 PHE   A CZ   1 
ATOM   612  N  N    . GLY   A 1 88  ? 11.044 10.612  3.408   1.00 98.00  ? 109 GLY   A N    1 
ATOM   613  C  CA   . GLY   A 1 88  ? 9.735  10.054  3.035   1.00 101.65 ? 109 GLY   A CA   1 
ATOM   614  C  C    . GLY   A 1 88  ? 9.434  10.205  1.562   1.00 104.67 ? 109 GLY   A C    1 
ATOM   615  O  O    . GLY   A 1 88  ? 10.283 9.814   0.740   1.00 111.25 ? 109 GLY   A O    1 
ATOM   616  N  N    . PRO   A 1 89  ? 8.280  10.782  1.183   1.00 101.47 ? 110 PRO   A N    1 
ATOM   617  C  CA   . PRO   A 1 89  ? 7.847  10.859  -0.219  1.00 108.63 ? 110 PRO   A CA   1 
ATOM   618  C  C    . PRO   A 1 89  ? 8.578  11.906  -1.051  1.00 110.55 ? 110 PRO   A C    1 
ATOM   619  O  O    . PRO   A 1 89  ? 7.962  12.549  -1.905  1.00 112.53 ? 110 PRO   A O    1 
ATOM   620  C  CB   . PRO   A 1 89  ? 6.359  11.204  -0.095  1.00 107.23 ? 110 PRO   A CB   1 
ATOM   621  C  CG   . PRO   A 1 89  ? 6.283  12.007  1.157   1.00 111.59 ? 110 PRO   A CG   1 
ATOM   622  C  CD   . PRO   A 1 89  ? 7.323  11.436  2.094   1.00 105.60 ? 110 PRO   A CD   1 
ATOM   623  N  N    . VAL   A 1 90  ? 9.882  12.081  -0.837  1.00 106.44 ? 111 VAL   A N    1 
ATOM   624  C  CA   . VAL   A 1 90  ? 10.637 13.058  -1.613  1.00 99.45  ? 111 VAL   A CA   1 
ATOM   625  C  C    . VAL   A 1 90  ? 10.760 12.578  -3.053  1.00 97.92  ? 111 VAL   A C    1 
ATOM   626  O  O    . VAL   A 1 90  ? 10.972 11.387  -3.316  1.00 100.05 ? 111 VAL   A O    1 
ATOM   627  C  CB   . VAL   A 1 90  ? 12.016 13.306  -0.976  1.00 98.46  ? 111 VAL   A CB   1 
ATOM   628  C  CG1  . VAL   A 1 90  ? 11.851 13.969  0.376   1.00 106.04 ? 111 VAL   A CG1  1 
ATOM   629  C  CG2  . VAL   A 1 90  ? 12.787 11.999  -0.835  1.00 99.85  ? 111 VAL   A CG2  1 
ATOM   630  N  N    . GLY   A 1 91  ? 10.604 13.505  -3.996  1.00 93.19  ? 112 GLY   A N    1 
ATOM   631  C  CA   . GLY   A 1 91  ? 10.660 13.171  -5.406  1.00 89.98  ? 112 GLY   A CA   1 
ATOM   632  C  C    . GLY   A 1 91  ? 11.976 13.551  -6.053  1.00 84.55  ? 112 GLY   A C    1 
ATOM   633  O  O    . GLY   A 1 91  ? 13.006 12.921  -5.794  1.00 83.07  ? 112 GLY   A O    1 
ATOM   634  N  N    . PHE   A 1 92  ? 11.954 14.584  -6.899  1.00 83.23  ? 113 PHE   A N    1 
ATOM   635  C  CA   . PHE   A 1 92  ? 13.182 15.065  -7.520  1.00 79.88  ? 113 PHE   A CA   1 
ATOM   636  C  C    . PHE   A 1 92  ? 14.147 15.653  -6.500  1.00 76.13  ? 113 PHE   A C    1 
ATOM   637  O  O    . PHE   A 1 92  ? 15.334 15.807  -6.805  1.00 71.57  ? 113 PHE   A O    1 
ATOM   638  C  CB   . PHE   A 1 92  ? 12.861 16.109  -8.591  1.00 85.31  ? 113 PHE   A CB   1 
ATOM   639  C  CG   . PHE   A 1 92  ? 12.506 17.460  -8.036  1.00 84.44  ? 113 PHE   A CG   1 
ATOM   640  C  CD1  . PHE   A 1 92  ? 11.264 17.685  -7.465  1.00 82.04  ? 113 PHE   A CD1  1 
ATOM   641  C  CD2  . PHE   A 1 92  ? 13.412 18.508  -8.095  1.00 83.09  ? 113 PHE   A CD2  1 
ATOM   642  C  CE1  . PHE   A 1 92  ? 10.935 18.928  -6.956  1.00 87.91  ? 113 PHE   A CE1  1 
ATOM   643  C  CE2  . PHE   A 1 92  ? 13.088 19.753  -7.589  1.00 83.20  ? 113 PHE   A CE2  1 
ATOM   644  C  CZ   . PHE   A 1 92  ? 11.848 19.964  -7.019  1.00 83.64  ? 113 PHE   A CZ   1 
ATOM   645  N  N    . MET   A 1 93  ? 13.664 15.983  -5.301  1.00 77.91  ? 114 MET   A N    1 
ATOM   646  C  CA   . MET   A 1 93  ? 14.516 16.493  -4.234  1.00 72.74  ? 114 MET   A CA   1 
ATOM   647  C  C    . MET   A 1 93  ? 15.445 15.435  -3.658  1.00 68.60  ? 114 MET   A C    1 
ATOM   648  O  O    . MET   A 1 93  ? 16.268 15.768  -2.801  1.00 66.84  ? 114 MET   A O    1 
ATOM   649  C  CB   . MET   A 1 93  ? 13.655 17.090  -3.120  1.00 73.33  ? 114 MET   A CB   1 
ATOM   650  C  CG   . MET   A 1 93  ? 12.900 18.342  -3.533  1.00 79.49  ? 114 MET   A CG   1 
ATOM   651  S  SD   . MET   A 1 93  ? 13.995 19.727  -3.913  1.00 81.24  ? 114 MET   A SD   1 
ATOM   652  C  CE   . MET   A 1 93  ? 14.539 20.195  -2.272  1.00 85.75  ? 114 MET   A CE   1 
ATOM   653  N  N    . LYS   A 1 94  ? 15.341 14.179  -4.099  1.00 71.06  ? 115 LYS   A N    1 
ATOM   654  C  CA   . LYS   A 1 94  ? 16.271 13.154  -3.641  1.00 69.16  ? 115 LYS   A CA   1 
ATOM   655  C  C    . LYS   A 1 94  ? 17.714 13.503  -3.977  1.00 69.96  ? 115 LYS   A C    1 
ATOM   656  O  O    . LYS   A 1 94  ? 18.633 12.989  -3.331  1.00 68.83  ? 115 LYS   A O    1 
ATOM   657  C  CB   . LYS   A 1 94  ? 15.905 11.800  -4.250  1.00 74.12  ? 115 LYS   A CB   1 
ATOM   658  N  N    . SER   A 1 95  ? 17.933 14.365  -4.969  1.00 76.84  ? 116 SER   A N    1 
ATOM   659  C  CA   . SER   A 1 95  ? 19.269 14.836  -5.308  1.00 80.28  ? 116 SER   A CA   1 
ATOM   660  C  C    . SER   A 1 95  ? 19.742 15.969  -4.407  1.00 72.27  ? 116 SER   A C    1 
ATOM   661  O  O    . SER   A 1 95  ? 20.840 16.492  -4.625  1.00 71.91  ? 116 SER   A O    1 
ATOM   662  C  CB   . SER   A 1 95  ? 19.313 15.288  -6.771  1.00 79.80  ? 116 SER   A CB   1 
ATOM   663  O  OG   . SER   A 1 95  ? 19.107 14.195  -7.650  1.00 69.08  ? 116 SER   A OG   1 
ATOM   664  N  N    . ALA   A 1 96  ? 18.948 16.366  -3.416  1.00 68.77  ? 117 ALA   A N    1 
ATOM   665  C  CA   . ALA   A 1 96  ? 19.390 17.391  -2.481  1.00 73.70  ? 117 ALA   A CA   1 
ATOM   666  C  C    . ALA   A 1 96  ? 20.593 16.896  -1.690  1.00 73.73  ? 117 ALA   A C    1 
ATOM   667  O  O    . ALA   A 1 96  ? 20.692 15.714  -1.350  1.00 76.09  ? 117 ALA   A O    1 
ATOM   668  C  CB   . ALA   A 1 96  ? 18.258 17.777  -1.532  1.00 74.43  ? 117 ALA   A CB   1 
ATOM   669  N  N    . ILE   A 1 97  ? 21.516 17.815  -1.401  1.00 70.64  ? 118 ILE   A N    1 
ATOM   670  C  CA   . ILE   A 1 97  ? 22.740 17.445  -0.697  1.00 67.03  ? 118 ILE   A CA   1 
ATOM   671  C  C    . ILE   A 1 97  ? 22.413 16.869  0.675   1.00 76.91  ? 118 ILE   A C    1 
ATOM   672  O  O    . ILE   A 1 97  ? 23.074 15.936  1.148   1.00 81.37  ? 118 ILE   A O    1 
ATOM   673  C  CB   . ILE   A 1 97  ? 23.682 18.661  -0.603  1.00 69.35  ? 118 ILE   A CB   1 
ATOM   674  C  CG1  . ILE   A 1 97  ? 24.907 18.339  0.256   1.00 73.23  ? 118 ILE   A CG1  1 
ATOM   675  C  CG2  . ILE   A 1 97  ? 22.934 19.880  -0.086  1.00 72.43  ? 118 ILE   A CG2  1 
ATOM   676  C  CD1  . ILE   A 1 97  ? 25.834 17.319  -0.363  1.00 74.44  ? 118 ILE   A CD1  1 
ATOM   677  N  N    . SER   A 1 98  ? 21.378 17.399  1.330   1.00 78.93  ? 119 SER   A N    1 
ATOM   678  C  CA   . SER   A 1 98  ? 20.972 16.861  2.623   1.00 72.41  ? 119 SER   A CA   1 
ATOM   679  C  C    . SER   A 1 98  ? 20.237 15.535  2.488   1.00 69.19  ? 119 SER   A C    1 
ATOM   680  O  O    . SER   A 1 98  ? 20.084 14.822  3.486   1.00 65.71  ? 119 SER   A O    1 
ATOM   681  C  CB   . SER   A 1 98  ? 20.099 17.875  3.363   1.00 71.72  ? 119 SER   A CB   1 
ATOM   682  O  OG   . SER   A 1 98  ? 19.009 18.289  2.559   1.00 77.95  ? 119 SER   A OG   1 
ATOM   683  N  N    . ILE   A 1 99  ? 19.792 15.188  1.283   1.00 71.47  ? 120 ILE   A N    1 
ATOM   684  C  CA   . ILE   A 1 99  ? 19.068 13.947  1.054   1.00 66.63  ? 120 ILE   A CA   1 
ATOM   685  C  C    . ILE   A 1 99  ? 19.881 12.934  0.255   1.00 60.00  ? 120 ILE   A C    1 
ATOM   686  O  O    . ILE   A 1 99  ? 19.561 11.736  0.300   1.00 61.85  ? 120 ILE   A O    1 
ATOM   687  C  CB   . ILE   A 1 99  ? 17.716 14.219  0.360   1.00 60.82  ? 120 ILE   A CB   1 
ATOM   688  C  CG1  . ILE   A 1 99  ? 17.048 15.448  0.978   1.00 70.10  ? 120 ILE   A CG1  1 
ATOM   689  C  CG2  . ILE   A 1 99  ? 16.788 13.025  0.487   1.00 57.35  ? 120 ILE   A CG2  1 
ATOM   690  C  CD1  . ILE   A 1 99  ? 15.696 15.779  0.383   1.00 76.44  ? 120 ILE   A CD1  1 
ATOM   691  N  N    . ALA   A 1 100 ? 20.924 13.362  -0.453  1.00 61.15  ? 121 ALA   A N    1 
ATOM   692  C  CA   . ALA   A 1 100 ? 21.716 12.440  -1.251  1.00 72.57  ? 121 ALA   A CA   1 
ATOM   693  C  C    . ALA   A 1 100 ? 22.449 11.443  -0.357  1.00 71.86  ? 121 ALA   A C    1 
ATOM   694  O  O    . ALA   A 1 100 ? 22.686 11.684  0.829   1.00 71.05  ? 121 ALA   A O    1 
ATOM   695  C  CB   . ALA   A 1 100 ? 22.718 13.200  -2.118  1.00 81.63  ? 121 ALA   A CB   1 
ATOM   696  N  N    . GLU   A 1 101 ? 22.815 10.310  -0.950  1.00 78.98  ? 122 GLU   A N    1 
ATOM   697  C  CA   . GLU   A 1 101 ? 23.416 9.207   -0.217  1.00 73.56  ? 122 GLU   A CA   1 
ATOM   698  C  C    . GLU   A 1 101 ? 24.678 8.727   -0.918  1.00 76.04  ? 122 GLU   A C    1 
ATOM   699  O  O    . GLU   A 1 101 ? 24.722 8.636   -2.149  1.00 80.12  ? 122 GLU   A O    1 
ATOM   700  C  CB   . GLU   A 1 101 ? 22.430 8.038   -0.071  1.00 71.22  ? 122 GLU   A CB   1 
ATOM   701  C  CG   . GLU   A 1 101 ? 21.187 8.364   0.745   1.00 77.14  ? 122 GLU   A CG   1 
ATOM   702  C  CD   . GLU   A 1 101 ? 20.252 7.176   0.886   1.00 78.82  ? 122 GLU   A CD   1 
ATOM   703  O  OE1  . GLU   A 1 101 ? 20.420 6.192   0.134   1.00 68.92  ? 122 GLU   A OE1  1 
ATOM   704  O  OE2  . GLU   A 1 101 ? 19.353 7.223   1.753   1.00 87.51  ? 122 GLU   A OE2  1 
ATOM   705  N  N    . ASP   A 1 102 ? 25.705 8.436   -0.117  1.00 81.76  ? 123 ASP   A N    1 
ATOM   706  C  CA   . ASP   A 1 102 ? 26.930 7.756   -0.554  1.00 82.81  ? 123 ASP   A CA   1 
ATOM   707  C  C    . ASP   A 1 102 ? 27.609 8.582   -1.641  1.00 80.90  ? 123 ASP   A C    1 
ATOM   708  O  O    . ASP   A 1 102 ? 28.001 9.729   -1.362  1.00 83.17  ? 123 ASP   A O    1 
ATOM   709  C  CB   . ASP   A 1 102 ? 26.571 6.317   -0.933  1.00 82.31  ? 123 ASP   A CB   1 
ATOM   710  C  CG   . ASP   A 1 102 ? 26.193 5.475   0.274   1.00 78.15  ? 123 ASP   A CG   1 
ATOM   711  O  OD1  . ASP   A 1 102 ? 26.824 5.644   1.340   1.00 78.49  ? 123 ASP   A OD1  1 
ATOM   712  O  OD2  . ASP   A 1 102 ? 25.264 4.648   0.159   1.00 73.46  ? 123 ASP   A OD2  1 
ATOM   713  N  N    . GLU   A 1 103 ? 27.772 8.069   -2.863  1.00 86.33  ? 124 GLU   A N    1 
ATOM   714  C  CA   . GLU   A 1 103 ? 28.642 8.721   -3.836  1.00 92.09  ? 124 GLU   A CA   1 
ATOM   715  C  C    . GLU   A 1 103 ? 28.065 10.042  -4.329  1.00 84.55  ? 124 GLU   A C    1 
ATOM   716  O  O    . GLU   A 1 103 ? 28.824 10.980  -4.602  1.00 82.27  ? 124 GLU   A O    1 
ATOM   717  C  CB   . GLU   A 1 103 ? 28.906 7.779   -5.013  1.00 95.04  ? 124 GLU   A CB   1 
ATOM   718  C  CG   . GLU   A 1 103 ? 29.150 6.333   -4.600  1.00 93.89  ? 124 GLU   A CG   1 
ATOM   719  C  CD   . GLU   A 1 103 ? 30.192 6.202   -3.503  1.00 97.60  ? 124 GLU   A CD   1 
ATOM   720  O  OE1  . GLU   A 1 103 ? 31.304 6.748   -3.666  1.00 101.45 ? 124 GLU   A OE1  1 
ATOM   721  O  OE2  . GLU   A 1 103 ? 29.894 5.559   -2.473  1.00 93.58  ? 124 GLU   A OE2  1 
ATOM   722  N  N    . GLU   A 1 104 ? 26.739 10.142  -4.450  1.00 82.38  ? 125 GLU   A N    1 
ATOM   723  C  CA   . GLU   A 1 104 ? 26.144 11.398  -4.892  1.00 83.51  ? 125 GLU   A CA   1 
ATOM   724  C  C    . GLU   A 1 104 ? 26.338 12.501  -3.860  1.00 85.52  ? 125 GLU   A C    1 
ATOM   725  O  O    . GLU   A 1 104 ? 26.519 13.667  -4.227  1.00 84.63  ? 125 GLU   A O    1 
ATOM   726  C  CB   . GLU   A 1 104 ? 24.656 11.206  -5.190  1.00 82.72  ? 125 GLU   A CB   1 
ATOM   727  C  CG   . GLU   A 1 104 ? 24.050 12.318  -6.039  1.00 81.87  ? 125 GLU   A CG   1 
ATOM   728  C  CD   . GLU   A 1 104 ? 22.555 12.154  -6.238  1.00 90.08  ? 125 GLU   A CD   1 
ATOM   729  O  OE1  . GLU   A 1 104 ? 21.942 11.375  -5.479  1.00 103.29 ? 125 GLU   A OE1  1 
ATOM   730  O  OE2  . GLU   A 1 104 ? 21.994 12.802  -7.151  1.00 72.62  ? 125 GLU   A OE2  1 
ATOM   731  N  N    . TRP   A 1 105 ? 26.315 12.156  -2.570  1.00 83.82  ? 126 TRP   A N    1 
ATOM   732  C  CA   . TRP   A 1 105 ? 26.550 13.160  -1.538  1.00 77.26  ? 126 TRP   A CA   1 
ATOM   733  C  C    . TRP   A 1 105 ? 27.981 13.680  -1.589  1.00 78.44  ? 126 TRP   A C    1 
ATOM   734  O  O    . TRP   A 1 105 ? 28.212 14.888  -1.467  1.00 81.85  ? 126 TRP   A O    1 
ATOM   735  C  CB   . TRP   A 1 105 ? 26.242 12.583  -0.157  1.00 75.62  ? 126 TRP   A CB   1 
ATOM   736  C  CG   . TRP   A 1 105 ? 26.784 13.421  0.958   1.00 75.67  ? 126 TRP   A CG   1 
ATOM   737  C  CD1  . TRP   A 1 105 ? 26.185 14.501  1.536   1.00 74.79  ? 126 TRP   A CD1  1 
ATOM   738  C  CD2  . TRP   A 1 105 ? 28.040 13.252  1.629   1.00 76.17  ? 126 TRP   A CD2  1 
ATOM   739  N  NE1  . TRP   A 1 105 ? 26.988 15.016  2.524   1.00 74.21  ? 126 TRP   A NE1  1 
ATOM   740  C  CE2  . TRP   A 1 105 ? 28.133 14.268  2.601   1.00 74.96  ? 126 TRP   A CE2  1 
ATOM   741  C  CE3  . TRP   A 1 105 ? 29.093 12.342  1.501   1.00 76.73  ? 126 TRP   A CE3  1 
ATOM   742  C  CZ2  . TRP   A 1 105 ? 29.237 14.397  3.442   1.00 78.01  ? 126 TRP   A CZ2  1 
ATOM   743  C  CZ3  . TRP   A 1 105 ? 30.188 12.472  2.337   1.00 79.66  ? 126 TRP   A CZ3  1 
ATOM   744  C  CH2  . TRP   A 1 105 ? 30.251 13.492  3.294   1.00 79.58  ? 126 TRP   A CH2  1 
ATOM   745  N  N    . LYS   A 1 106 ? 28.955 12.783  -1.760  1.00 76.19  ? 127 LYS   A N    1 
ATOM   746  C  CA   . LYS   A 1 106 ? 30.343 13.217  -1.857  1.00 77.47  ? 127 LYS   A CA   1 
ATOM   747  C  C    . LYS   A 1 106 ? 30.575 14.064  -3.101  1.00 85.72  ? 127 LYS   A C    1 
ATOM   748  O  O    . LYS   A 1 106 ? 31.379 15.003  -3.071  1.00 88.82  ? 127 LYS   A O    1 
ATOM   749  C  CB   . LYS   A 1 106 ? 31.275 12.005  -1.851  1.00 75.45  ? 127 LYS   A CB   1 
ATOM   750  N  N    . ARG   A 1 107 ? 29.879 13.754  -4.198  1.00 85.76  ? 128 ARG   A N    1 
ATOM   751  C  CA   . ARG   A 1 107 ? 30.007 14.563  -5.406  1.00 86.28  ? 128 ARG   A CA   1 
ATOM   752  C  C    . ARG   A 1 107 ? 29.357 15.928  -5.225  1.00 88.24  ? 128 ARG   A C    1 
ATOM   753  O  O    . ARG   A 1 107 ? 29.886 16.942  -5.697  1.00 91.98  ? 128 ARG   A O    1 
ATOM   754  C  CB   . ARG   A 1 107 ? 29.388 13.831  -6.597  1.00 88.57  ? 128 ARG   A CB   1 
ATOM   755  C  CG   . ARG   A 1 107 ? 29.606 14.527  -7.934  1.00 95.68  ? 128 ARG   A CG   1 
ATOM   756  C  CD   . ARG   A 1 107 ? 28.895 13.807  -9.070  1.00 95.48  ? 128 ARG   A CD   1 
ATOM   757  N  NE   . ARG   A 1 107 ? 27.449 13.989  -9.017  1.00 93.35  ? 128 ARG   A NE   1 
ATOM   758  C  CZ   . ARG   A 1 107 ? 26.798 14.980  -9.610  1.00 96.66  ? 128 ARG   A CZ   1 
ATOM   759  N  NH1  . ARG   A 1 107 ? 27.435 15.904  -10.309 1.00 103.75 ? 128 ARG   A NH1  1 
ATOM   760  N  NH2  . ARG   A 1 107 ? 25.474 15.047  -9.498  1.00 95.37  ? 128 ARG   A NH2  1 
ATOM   761  N  N    . LEU   A 1 108 ? 28.213 15.974  -4.540  1.00 85.77  ? 129 LEU   A N    1 
ATOM   762  C  CA   . LEU   A 1 108 ? 27.491 17.233  -4.388  1.00 83.94  ? 129 LEU   A CA   1 
ATOM   763  C  C    . LEU   A 1 108 ? 28.174 18.153  -3.385  1.00 85.48  ? 129 LEU   A C    1 
ATOM   764  O  O    . LEU   A 1 108 ? 28.230 19.371  -3.593  1.00 87.50  ? 129 LEU   A O    1 
ATOM   765  C  CB   . LEU   A 1 108 ? 26.049 16.958  -3.969  1.00 81.23  ? 129 LEU   A CB   1 
ATOM   766  C  CG   . LEU   A 1 108 ? 25.126 16.408  -5.056  1.00 81.96  ? 129 LEU   A CG   1 
ATOM   767  C  CD1  . LEU   A 1 108 ? 23.930 15.721  -4.430  1.00 79.52  ? 129 LEU   A CD1  1 
ATOM   768  C  CD2  . LEU   A 1 108 ? 24.675 17.522  -5.987  1.00 84.78  ? 129 LEU   A CD2  1 
ATOM   769  N  N    . ARG   A 1 109 ? 28.697 17.597  -2.290  1.00 82.20  ? 130 ARG   A N    1 
ATOM   770  C  CA   . ARG   A 1 109 ? 29.312 18.445  -1.274  1.00 84.36  ? 130 ARG   A CA   1 
ATOM   771  C  C    . ARG   A 1 109 ? 30.616 19.052  -1.775  1.00 89.65  ? 130 ARG   A C    1 
ATOM   772  O  O    . ARG   A 1 109 ? 30.896 20.229  -1.519  1.00 90.62  ? 130 ARG   A O    1 
ATOM   773  C  CB   . ARG   A 1 109 ? 29.547 17.654  0.012   1.00 81.39  ? 130 ARG   A CB   1 
ATOM   774  C  CG   . ARG   A 1 109 ? 29.938 18.534  1.188   1.00 80.61  ? 130 ARG   A CG   1 
ATOM   775  C  CD   . ARG   A 1 109 ? 29.957 17.760  2.488   1.00 81.79  ? 130 ARG   A CD   1 
ATOM   776  N  NE   . ARG   A 1 109 ? 30.208 18.627  3.634   1.00 83.05  ? 130 ARG   A NE   1 
ATOM   777  C  CZ   . ARG   A 1 109 ? 29.263 19.132  4.416   1.00 78.28  ? 130 ARG   A CZ   1 
ATOM   778  N  NH1  . ARG   A 1 109 ? 27.982 18.873  4.209   1.00 74.09  ? 130 ARG   A NH1  1 
ATOM   779  N  NH2  . ARG   A 1 109 ? 29.613 19.912  5.436   1.00 75.45  ? 130 ARG   A NH2  1 
ATOM   780  N  N    . SER   A 1 110 ? 31.427 18.269  -2.489  1.00 89.48  ? 131 SER   A N    1 
ATOM   781  C  CA   . SER   A 1 110 ? 32.641 18.824  -3.079  1.00 92.64  ? 131 SER   A CA   1 
ATOM   782  C  C    . SER   A 1 110 ? 32.307 19.905  -4.098  1.00 92.79  ? 131 SER   A C    1 
ATOM   783  O  O    . SER   A 1 110 ? 33.019 20.911  -4.204  1.00 94.23  ? 131 SER   A O    1 
ATOM   784  C  CB   . SER   A 1 110 ? 33.470 17.713  -3.723  1.00 95.66  ? 131 SER   A CB   1 
ATOM   785  O  OG   . SER   A 1 110 ? 33.967 16.818  -2.743  1.00 97.35  ? 131 SER   A OG   1 
ATOM   786  N  N    . LEU   A 1 111 ? 31.221 19.722  -4.850  1.00 90.60  ? 132 LEU   A N    1 
ATOM   787  C  CA   . LEU   A 1 111 ? 30.789 20.727  -5.811  1.00 94.33  ? 132 LEU   A CA   1 
ATOM   788  C  C    . LEU   A 1 111 ? 30.148 21.939  -5.148  1.00 95.17  ? 132 LEU   A C    1 
ATOM   789  O  O    . LEU   A 1 111 ? 29.944 22.955  -5.821  1.00 96.40  ? 132 LEU   A O    1 
ATOM   790  C  CB   . LEU   A 1 111 ? 29.813 20.107  -6.813  1.00 91.25  ? 132 LEU   A CB   1 
ATOM   791  N  N    . LEU   A 1 112 ? 29.833 21.862  -3.855  1.00 94.53  ? 133 LEU   A N    1 
ATOM   792  C  CA   . LEU   A 1 112 ? 29.192 22.958  -3.144  1.00 94.77  ? 133 LEU   A CA   1 
ATOM   793  C  C    . LEU   A 1 112 ? 30.008 23.501  -1.981  1.00 96.24  ? 133 LEU   A C    1 
ATOM   794  O  O    . LEU   A 1 112 ? 29.653 24.556  -1.444  1.00 98.55  ? 133 LEU   A O    1 
ATOM   795  C  CB   . LEU   A 1 112 ? 27.816 22.521  -2.618  1.00 93.27  ? 133 LEU   A CB   1 
ATOM   796  C  CG   . LEU   A 1 112 ? 26.709 22.392  -3.662  1.00 94.34  ? 133 LEU   A CG   1 
ATOM   797  C  CD1  . LEU   A 1 112 ? 25.553 21.569  -3.120  1.00 88.25  ? 133 LEU   A CD1  1 
ATOM   798  C  CD2  . LEU   A 1 112 ? 26.233 23.772  -4.080  1.00 99.31  ? 133 LEU   A CD2  1 
ATOM   799  N  N    . SER   A 1 113 ? 31.079 22.818  -1.576  1.00 96.70  ? 134 SER   A N    1 
ATOM   800  C  CA   . SER   A 1 113 ? 31.875 23.291  -0.444  1.00 101.98 ? 134 SER   A CA   1 
ATOM   801  C  C    . SER   A 1 113 ? 32.541 24.637  -0.703  1.00 102.21 ? 134 SER   A C    1 
ATOM   802  O  O    . SER   A 1 113 ? 32.483 25.505  0.186   1.00 99.15  ? 134 SER   A O    1 
ATOM   803  C  CB   . SER   A 1 113 ? 32.905 22.223  -0.057  1.00 101.52 ? 134 SER   A CB   1 
ATOM   804  O  OG   . SER   A 1 113 ? 32.268 21.011  0.309   1.00 99.15  ? 134 SER   A OG   1 
ATOM   805  N  N    . PRO   A 1 114 ? 33.181 24.889  -1.852  1.00 96.95  ? 135 PRO   A N    1 
ATOM   806  C  CA   . PRO   A 1 114 ? 33.775 26.218  -2.069  1.00 97.71  ? 135 PRO   A CA   1 
ATOM   807  C  C    . PRO   A 1 114 ? 32.761 27.347  -2.067  1.00 103.75 ? 135 PRO   A C    1 
ATOM   808  O  O    . PRO   A 1 114 ? 33.153 28.511  -1.913  1.00 107.12 ? 135 PRO   A O    1 
ATOM   809  C  CB   . PRO   A 1 114 ? 34.456 26.082  -3.438  1.00 106.67 ? 135 PRO   A CB   1 
ATOM   810  C  CG   . PRO   A 1 114 ? 34.702 24.630  -3.592  1.00 104.18 ? 135 PRO   A CG   1 
ATOM   811  C  CD   . PRO   A 1 114 ? 33.522 23.970  -2.954  1.00 102.48 ? 135 PRO   A CD   1 
ATOM   812  N  N    . THR   A 1 115 ? 31.472 27.045  -2.231  1.00 100.99 ? 136 THR   A N    1 
ATOM   813  C  CA   . THR   A 1 115 ? 30.463 28.097  -2.207  1.00 102.18 ? 136 THR   A CA   1 
ATOM   814  C  C    . THR   A 1 115 ? 30.321 28.703  -0.818  1.00 101.99 ? 136 THR   A C    1 
ATOM   815  O  O    . THR   A 1 115 ? 30.020 29.895  -0.690  1.00 103.83 ? 136 THR   A O    1 
ATOM   816  C  CB   . THR   A 1 115 ? 29.119 27.549  -2.684  1.00 103.71 ? 136 THR   A CB   1 
ATOM   817  O  OG1  . THR   A 1 115 ? 29.332 26.652  -3.781  1.00 110.13 ? 136 THR   A OG1  1 
ATOM   818  C  CG2  . THR   A 1 115 ? 28.224 28.683  -3.143  1.00 108.31 ? 136 THR   A CG2  1 
ATOM   819  N  N    . PHE   A 1 116 ? 30.537 27.907  0.230   1.00 102.16 ? 137 PHE   A N    1 
ATOM   820  C  CA   . PHE   A 1 116 ? 30.450 28.374  1.607   1.00 105.51 ? 137 PHE   A CA   1 
ATOM   821  C  C    . PHE   A 1 116 ? 31.822 28.670  2.205   1.00 107.09 ? 137 PHE   A C    1 
ATOM   822  O  O    . PHE   A 1 116 ? 32.008 28.557  3.422   1.00 107.68 ? 137 PHE   A O    1 
ATOM   823  C  CB   . PHE   A 1 116 ? 29.706 27.350  2.465   1.00 101.88 ? 137 PHE   A CB   1 
ATOM   824  N  N    . THR   A 1 117 ? 32.788 29.047  1.371   1.00 104.88 ? 138 THR   A N    1 
ATOM   825  C  CA   . THR   A 1 117 ? 34.126 29.353  1.857   1.00 106.75 ? 138 THR   A CA   1 
ATOM   826  C  C    . THR   A 1 117 ? 34.132 30.680  2.609   1.00 110.80 ? 138 THR   A C    1 
ATOM   827  O  O    . THR   A 1 117 ? 33.388 31.609  2.281   1.00 112.04 ? 138 THR   A O    1 
ATOM   828  C  CB   . THR   A 1 117 ? 35.120 29.402  0.692   1.00 107.04 ? 138 THR   A CB   1 
ATOM   829  O  OG1  . THR   A 1 117 ? 35.131 28.138  0.019   1.00 115.59 ? 138 THR   A OG1  1 
ATOM   830  C  CG2  . THR   A 1 117 ? 36.530 29.704  1.182   1.00 108.21 ? 138 THR   A CG2  1 
ATOM   831  N  N    . SER   A 1 118 ? 34.978 30.752  3.642   1.00 111.20 ? 139 SER   A N    1 
ATOM   832  C  CA   . SER   A 1 118 ? 35.163 31.995  4.383   1.00 111.32 ? 139 SER   A CA   1 
ATOM   833  C  C    . SER   A 1 118 ? 35.498 33.163  3.464   1.00 110.03 ? 139 SER   A C    1 
ATOM   834  O  O    . SER   A 1 118 ? 35.110 34.304  3.741   1.00 108.66 ? 139 SER   A O    1 
ATOM   835  C  CB   . SER   A 1 118 ? 36.264 31.816  5.429   1.00 109.59 ? 139 SER   A CB   1 
ATOM   836  O  OG   . SER   A 1 118 ? 37.486 31.434  4.819   1.00 103.70 ? 139 SER   A OG   1 
ATOM   837  N  N    . GLY   A 1 119 ? 36.216 32.903  2.369   1.00 104.97 ? 140 GLY   A N    1 
ATOM   838  C  CA   . GLY   A 1 119 ? 36.511 33.961  1.420   1.00 105.09 ? 140 GLY   A CA   1 
ATOM   839  C  C    . GLY   A 1 119 ? 35.301 34.402  0.622   1.00 106.03 ? 140 GLY   A C    1 
ATOM   840  O  O    . GLY   A 1 119 ? 35.187 35.577  0.261   1.00 110.09 ? 140 GLY   A O    1 
ATOM   841  N  N    . LYS   A 1 120 ? 34.382 33.477  0.338   1.00 103.56 ? 141 LYS   A N    1 
ATOM   842  C  CA   . LYS   A 1 120 ? 33.183 33.824  -0.416  1.00 104.39 ? 141 LYS   A CA   1 
ATOM   843  C  C    . LYS   A 1 120 ? 32.146 34.527  0.451   1.00 106.18 ? 141 LYS   A C    1 
ATOM   844  O  O    . LYS   A 1 120 ? 31.359 35.331  -0.061  1.00 106.91 ? 141 LYS   A O    1 
ATOM   845  C  CB   . LYS   A 1 120 ? 32.574 32.570  -1.045  1.00 109.09 ? 141 LYS   A CB   1 
ATOM   846  N  N    . LEU   A 1 121 ? 32.129 34.241  1.755   1.00 108.88 ? 142 LEU   A N    1 
ATOM   847  C  CA   . LEU   A 1 121 ? 31.174 34.896  2.641   1.00 110.17 ? 142 LEU   A CA   1 
ATOM   848  C  C    . LEU   A 1 121 ? 31.556 36.347  2.907   1.00 114.75 ? 142 LEU   A C    1 
ATOM   849  O  O    . LEU   A 1 121 ? 30.674 37.199  3.063   1.00 112.55 ? 142 LEU   A O    1 
ATOM   850  C  CB   . LEU   A 1 121 ? 31.066 34.124  3.957   1.00 107.04 ? 142 LEU   A CB   1 
ATOM   851  N  N    . LYS   A 1 122 ? 32.857 36.647  2.958   1.00 115.91 ? 143 LYS   A N    1 
ATOM   852  C  CA   . LYS   A 1 122 ? 33.295 38.015  3.215   1.00 115.04 ? 143 LYS   A CA   1 
ATOM   853  C  C    . LYS   A 1 122 ? 32.936 38.949  2.065   1.00 115.04 ? 143 LYS   A C    1 
ATOM   854  O  O    . LYS   A 1 122 ? 32.659 40.132  2.294   1.00 120.02 ? 143 LYS   A O    1 
ATOM   855  C  CB   . LYS   A 1 122 ? 34.802 38.046  3.472   1.00 110.12 ? 143 LYS   A CB   1 
ATOM   856  N  N    . GLU   A 1 123 ? 32.935 38.443  0.830   1.00 114.18 ? 144 GLU   A N    1 
ATOM   857  C  CA   . GLU   A 1 123 ? 32.578 39.259  -0.324  1.00 118.90 ? 144 GLU   A CA   1 
ATOM   858  C  C    . GLU   A 1 123 ? 31.080 39.514  -0.428  1.00 125.31 ? 144 GLU   A C    1 
ATOM   859  O  O    . GLU   A 1 123 ? 30.667 40.343  -1.246  1.00 125.77 ? 144 GLU   A O    1 
ATOM   860  C  CB   . GLU   A 1 123 ? 33.078 38.598  -1.610  1.00 112.13 ? 144 GLU   A CB   1 
ATOM   861  N  N    . MET   A 1 124 ? 30.265 38.827  0.370   1.00 124.97 ? 145 MET   A N    1 
ATOM   862  C  CA   . MET   A 1 124 ? 28.822 39.020  0.372   1.00 124.94 ? 145 MET   A CA   1 
ATOM   863  C  C    . MET   A 1 124 ? 28.322 39.741  1.616   1.00 126.94 ? 145 MET   A C    1 
ATOM   864  O  O    . MET   A 1 124 ? 27.107 39.886  1.784   1.00 127.88 ? 145 MET   A O    1 
ATOM   865  C  CB   . MET   A 1 124 ? 28.109 37.669  0.237   1.00 124.38 ? 145 MET   A CB   1 
ATOM   866  N  N    . VAL   A 1 125 ? 29.220 40.196  2.485   1.00 123.94 ? 146 VAL   A N    1 
ATOM   867  C  CA   . VAL   A 1 125 ? 28.840 40.872  3.725   1.00 125.58 ? 146 VAL   A CA   1 
ATOM   868  C  C    . VAL   A 1 125 ? 28.180 42.219  3.435   1.00 129.51 ? 146 VAL   A C    1 
ATOM   869  O  O    . VAL   A 1 125 ? 27.122 42.506  4.016   1.00 131.57 ? 146 VAL   A O    1 
ATOM   870  C  CB   . VAL   A 1 125 ? 30.049 41.033  4.663   1.00 120.21 ? 146 VAL   A CB   1 
ATOM   871  N  N    . PRO   A 1 126 ? 28.740 43.083  2.575   1.00 126.66 ? 147 PRO   A N    1 
ATOM   872  C  CA   . PRO   A 1 126 ? 28.054 44.359  2.306   1.00 127.47 ? 147 PRO   A CA   1 
ATOM   873  C  C    . PRO   A 1 126 ? 26.704 44.191  1.628   1.00 127.98 ? 147 PRO   A C    1 
ATOM   874  O  O    . PRO   A 1 126 ? 25.812 45.023  1.835   1.00 128.20 ? 147 PRO   A O    1 
ATOM   875  C  CB   . PRO   A 1 126 ? 29.047 45.111  1.407   1.00 128.77 ? 147 PRO   A CB   1 
ATOM   876  C  CG   . PRO   A 1 126 ? 30.365 44.488  1.691   1.00 122.70 ? 147 PRO   A CG   1 
ATOM   877  C  CD   . PRO   A 1 126 ? 30.059 43.044  1.914   1.00 122.57 ? 147 PRO   A CD   1 
ATOM   878  N  N    . ILE   A 1 127 ? 26.524 43.141  0.826   1.00 127.16 ? 148 ILE   A N    1 
ATOM   879  C  CA   . ILE   A 1 127 ? 25.239 42.931  0.170   1.00 127.63 ? 148 ILE   A CA   1 
ATOM   880  C  C    . ILE   A 1 127 ? 24.198 42.411  1.156   1.00 127.93 ? 148 ILE   A C    1 
ATOM   881  O  O    . ILE   A 1 127 ? 23.006 42.711  1.019   1.00 124.73 ? 148 ILE   A O    1 
ATOM   882  C  CB   . ILE   A 1 127 ? 25.401 41.979  -1.027  1.00 129.72 ? 148 ILE   A CB   1 
ATOM   883  N  N    . ILE   A 1 128 ? 24.621 41.641  2.162   1.00 132.27 ? 149 ILE   A N    1 
ATOM   884  C  CA   . ILE   A 1 128 ? 23.691 41.108  3.152   1.00 134.17 ? 149 ILE   A CA   1 
ATOM   885  C  C    . ILE   A 1 128 ? 23.181 42.168  4.113   1.00 131.00 ? 149 ILE   A C    1 
ATOM   886  O  O    . ILE   A 1 128 ? 22.295 41.880  4.925   1.00 129.39 ? 149 ILE   A O    1 
ATOM   887  C  CB   . ILE   A 1 128 ? 24.345 39.964  3.953   1.00 127.28 ? 149 ILE   A CB   1 
ATOM   888  N  N    . ALA   A 1 129 ? 23.716 43.388  4.042   1.00 131.74 ? 150 ALA   A N    1 
ATOM   889  C  CA   . ALA   A 1 129 ? 23.304 44.467  4.927   1.00 134.41 ? 150 ALA   A CA   1 
ATOM   890  C  C    . ALA   A 1 129 ? 22.272 45.400  4.307   1.00 135.51 ? 150 ALA   A C    1 
ATOM   891  O  O    . ALA   A 1 129 ? 21.635 46.164  5.041   1.00 135.68 ? 150 ALA   A O    1 
ATOM   892  C  CB   . ALA   A 1 129 ? 24.523 45.289  5.364   1.00 134.82 ? 150 ALA   A CB   1 
ATOM   893  N  N    . GLN   A 1 130 ? 22.095 45.362  2.984   1.00 136.58 ? 151 GLN   A N    1 
ATOM   894  C  CA   . GLN   A 1 130 ? 21.092 46.210  2.348   1.00 135.81 ? 151 GLN   A CA   1 
ATOM   895  C  C    . GLN   A 1 130 ? 19.690 45.835  2.811   1.00 136.92 ? 151 GLN   A C    1 
ATOM   896  O  O    . GLN   A 1 130 ? 18.907 46.697  3.226   1.00 136.56 ? 151 GLN   A O    1 
ATOM   897  C  CB   . GLN   A 1 130 ? 21.206 46.109  0.826   1.00 133.27 ? 151 GLN   A CB   1 
ATOM   898  N  N    . TYR   A 1 131 ? 19.355 44.543  2.749   1.00 135.11 ? 152 TYR   A N    1 
ATOM   899  C  CA   . TYR   A 1 131 ? 18.077 44.083  3.278   1.00 135.64 ? 152 TYR   A CA   1 
ATOM   900  C  C    . TYR   A 1 131 ? 18.027 44.160  4.798   1.00 135.05 ? 152 TYR   A C    1 
ATOM   901  O  O    . TYR   A 1 131 ? 16.931 44.209  5.368   1.00 132.92 ? 152 TYR   A O    1 
ATOM   902  C  CB   . TYR   A 1 131 ? 17.799 42.652  2.817   1.00 125.80 ? 152 TYR   A CB   1 
ATOM   903  N  N    . GLY   A 1 132 ? 19.184 44.169  5.463   1.00 135.54 ? 153 GLY   A N    1 
ATOM   904  C  CA   . GLY   A 1 132 ? 19.194 44.319  6.908   1.00 134.02 ? 153 GLY   A CA   1 
ATOM   905  C  C    . GLY   A 1 132 ? 18.805 45.716  7.349   1.00 136.46 ? 153 GLY   A C    1 
ATOM   906  O  O    . GLY   A 1 132 ? 18.090 45.889  8.340   1.00 135.05 ? 153 GLY   A O    1 
ATOM   907  N  N    . ASP   A 1 133 ? 19.274 46.735  6.622   1.00 136.96 ? 154 ASP   A N    1 
ATOM   908  C  CA   . ASP   A 1 133 ? 18.837 48.099  6.897   1.00 138.37 ? 154 ASP   A CA   1 
ATOM   909  C  C    . ASP   A 1 133 ? 17.351 48.271  6.616   1.00 139.63 ? 154 ASP   A C    1 
ATOM   910  O  O    . ASP   A 1 133 ? 16.696 49.116  7.237   1.00 138.71 ? 154 ASP   A O    1 
ATOM   911  C  CB   . ASP   A 1 133 ? 19.655 49.091  6.070   1.00 134.20 ? 154 ASP   A CB   1 
ATOM   912  N  N    . VAL   A 1 134 ? 16.803 47.482  5.688   1.00 136.89 ? 155 VAL   A N    1 
ATOM   913  C  CA   . VAL   A 1 134 ? 15.365 47.505  5.455   1.00 136.00 ? 155 VAL   A CA   1 
ATOM   914  C  C    . VAL   A 1 134 ? 14.624 46.880  6.628   1.00 136.24 ? 155 VAL   A C    1 
ATOM   915  O  O    . VAL   A 1 134 ? 13.494 47.275  6.940   1.00 136.97 ? 155 VAL   A O    1 
ATOM   916  C  CB   . VAL   A 1 134 ? 15.026 46.794  4.132   1.00 136.23 ? 155 VAL   A CB   1 
ATOM   917  N  N    . LEU   A 1 135 ? 15.238 45.899  7.296   1.00 134.08 ? 156 LEU   A N    1 
ATOM   918  C  CA   . LEU   A 1 135 ? 14.606 45.289  8.461   1.00 134.88 ? 156 LEU   A CA   1 
ATOM   919  C  C    . LEU   A 1 135 ? 14.551 46.262  9.631   1.00 136.80 ? 156 LEU   A C    1 
ATOM   920  O  O    . LEU   A 1 135 ? 13.581 46.267  10.398  1.00 136.31 ? 156 LEU   A O    1 
ATOM   921  C  CB   . LEU   A 1 135 ? 15.351 44.014  8.855   1.00 134.53 ? 156 LEU   A CB   1 
ATOM   922  N  N    . VAL   A 1 136 ? 15.585 47.093  9.787   1.00 138.02 ? 157 VAL   A N    1 
ATOM   923  C  CA   . VAL   A 1 136 ? 15.563 48.107  10.836  1.00 141.03 ? 157 VAL   A CA   1 
ATOM   924  C  C    . VAL   A 1 136 ? 14.553 49.197  10.505  1.00 140.81 ? 157 VAL   A C    1 
ATOM   925  O  O    . VAL   A 1 136 ? 13.928 49.769  11.407  1.00 135.71 ? 157 VAL   A O    1 
ATOM   926  C  CB   . VAL   A 1 136 ? 16.972 48.689  11.050  1.00 141.35 ? 157 VAL   A CB   1 
ATOM   927  N  N    . ARG   A 1 137 ? 14.379 49.508  9.217   1.00 141.86 ? 158 ARG   A N    1 
ATOM   928  C  CA   . ARG   A 1 137 ? 13.351 50.465  8.821   1.00 139.34 ? 158 ARG   A CA   1 
ATOM   929  C  C    . ARG   A 1 137 ? 11.962 49.941  9.159   1.00 141.64 ? 158 ARG   A C    1 
ATOM   930  O  O    . ARG   A 1 137 ? 11.103 50.694  9.633   1.00 142.36 ? 158 ARG   A O    1 
ATOM   931  C  CB   . ARG   A 1 137 ? 13.464 50.771  7.327   1.00 132.38 ? 158 ARG   A CB   1 
ATOM   932  N  N    . ASN   A 1 138 ? 11.724 48.648  8.926   1.00 142.18 ? 159 ASN   A N    1 
ATOM   933  C  CA   . ASN   A 1 138 ? 10.473 48.023  9.336   1.00 137.29 ? 159 ASN   A CA   1 
ATOM   934  C  C    . ASN   A 1 138 ? 10.399 47.801  10.840  1.00 133.75 ? 159 ASN   A C    1 
ATOM   935  O  O    . ASN   A 1 138 ? 9.313  47.514  11.353  1.00 130.21 ? 159 ASN   A O    1 
ATOM   936  C  CB   . ASN   A 1 138 ? 10.286 46.691  8.606   1.00 133.14 ? 159 ASN   A CB   1 
ATOM   937  N  N    . LEU   A 1 139 ? 11.520 47.924  11.551  1.00 135.56 ? 160 LEU   A N    1 
ATOM   938  C  CA   . LEU   A 1 139 ? 11.532 47.789  13.001  1.00 142.05 ? 160 LEU   A CA   1 
ATOM   939  C  C    . LEU   A 1 139 ? 11.285 49.107  13.721  1.00 144.80 ? 160 LEU   A C    1 
ATOM   940  O  O    . LEU   A 1 139 ? 10.835 49.091  14.873  1.00 143.18 ? 160 LEU   A O    1 
ATOM   941  C  CB   . LEU   A 1 139 ? 12.868 47.201  13.467  1.00 140.84 ? 160 LEU   A CB   1 
ATOM   942  N  N    . ARG   A 1 140 ? 11.568 50.241  13.075  1.00 145.00 ? 161 ARG   A N    1 
ATOM   943  C  CA   . ARG   A 1 140 ? 11.306 51.533  13.702  1.00 142.08 ? 161 ARG   A CA   1 
ATOM   944  C  C    . ARG   A 1 140 ? 9.813  51.837  13.735  1.00 140.53 ? 161 ARG   A C    1 
ATOM   945  O  O    . ARG   A 1 140 ? 9.318  52.441  14.694  1.00 142.47 ? 161 ARG   A O    1 
ATOM   946  C  CB   . ARG   A 1 140 ? 12.064 52.638  12.967  1.00 138.88 ? 161 ARG   A CB   1 
ATOM   947  N  N    . ARG   A 1 141 ? 9.081  51.428  12.695  1.00 140.16 ? 162 ARG   A N    1 
ATOM   948  C  CA   . ARG   A 1 141 ? 7.635  51.624  12.688  1.00 141.35 ? 162 ARG   A CA   1 
ATOM   949  C  C    . ARG   A 1 141 ? 6.960  50.777  13.760  1.00 143.73 ? 162 ARG   A C    1 
ATOM   950  O  O    . ARG   A 1 141 ? 5.967  51.203  14.362  1.00 145.35 ? 162 ARG   A O    1 
ATOM   951  C  CB   . ARG   A 1 141 ? 7.067  51.297  11.306  1.00 137.01 ? 162 ARG   A CB   1 
ATOM   952  N  N    . GLU   A 1 142 ? 7.483  49.574  14.011  1.00 145.33 ? 163 GLU   A N    1 
ATOM   953  C  CA   . GLU   A 1 142 ? 6.956  48.752  15.095  1.00 146.70 ? 163 GLU   A CA   1 
ATOM   954  C  C    . GLU   A 1 142 ? 7.326  49.323  16.457  1.00 144.18 ? 163 GLU   A C    1 
ATOM   955  O  O    . GLU   A 1 142 ? 6.616  49.086  17.441  1.00 142.60 ? 163 GLU   A O    1 
ATOM   956  C  CB   . GLU   A 1 142 ? 7.463  47.316  14.963  1.00 147.65 ? 163 GLU   A CB   1 
ATOM   957  N  N    . ALA   A 1 143 ? 8.430  50.071  16.536  1.00 144.61 ? 164 ALA   A N    1 
ATOM   958  C  CA   . ALA   A 1 143 ? 8.788  50.732  17.786  1.00 143.78 ? 164 ALA   A CA   1 
ATOM   959  C  C    . ALA   A 1 143 ? 7.900  51.938  18.054  1.00 144.55 ? 164 ALA   A C    1 
ATOM   960  O  O    . ALA   A 1 143 ? 7.715  52.325  19.214  1.00 144.05 ? 164 ALA   A O    1 
ATOM   961  C  CB   . ALA   A 1 143 ? 10.257 51.151  17.761  1.00 138.97 ? 164 ALA   A CB   1 
ATOM   962  N  N    . GLU   A 1 144 ? 7.345  52.544  17.001  1.00 146.44 ? 165 GLU   A N    1 
ATOM   963  C  CA   . GLU   A 1 144 ? 6.410  53.648  17.179  1.00 145.08 ? 165 GLU   A CA   1 
ATOM   964  C  C    . GLU   A 1 144 ? 5.133  53.206  17.880  1.00 144.81 ? 165 GLU   A C    1 
ATOM   965  O  O    . GLU   A 1 144 ? 4.425  54.046  18.446  1.00 141.93 ? 165 GLU   A O    1 
ATOM   966  C  CB   . GLU   A 1 144 ? 6.075  54.276  15.825  1.00 141.75 ? 165 GLU   A CB   1 
ATOM   967  N  N    . THR   A 1 145 ? 4.827  51.912  17.856  1.00 145.83 ? 166 THR   A N    1 
ATOM   968  C  CA   . THR   A 1 145 ? 3.669  51.360  18.543  1.00 144.26 ? 166 THR   A CA   1 
ATOM   969  C  C    . THR   A 1 145 ? 4.115  50.752  19.867  1.00 141.23 ? 166 THR   A C    1 
ATOM   970  O  O    . THR   A 1 145 ? 5.092  49.997  19.911  1.00 140.37 ? 166 THR   A O    1 
ATOM   971  C  CB   . THR   A 1 145 ? 2.974  50.300  17.684  1.00 143.84 ? 166 THR   A CB   1 
ATOM   972  O  OG1  . THR   A 1 145 ? 3.731  49.083  17.714  1.00 144.64 ? 166 THR   A OG1  1 
ATOM   973  C  CG2  . THR   A 1 145 ? 2.859  50.776  16.241  1.00 139.34 ? 166 THR   A CG2  1 
ATOM   974  N  N    . GLY   A 1 146 ? 3.405  51.088  20.943  1.00 138.06 ? 167 GLY   A N    1 
ATOM   975  C  CA   . GLY   A 1 146 ? 3.664  50.472  22.231  1.00 135.95 ? 167 GLY   A CA   1 
ATOM   976  C  C    . GLY   A 1 146 ? 3.201  49.037  22.353  1.00 139.27 ? 167 GLY   A C    1 
ATOM   977  O  O    . GLY   A 1 146 ? 3.387  48.426  23.408  1.00 135.91 ? 167 GLY   A O    1 
ATOM   978  N  N    . LYS   A 1 147 ? 2.610  48.487  21.307  1.00 143.46 ? 168 LYS   A N    1 
ATOM   979  C  CA   . LYS   A 1 147 ? 2.084  47.131  21.321  1.00 141.61 ? 168 LYS   A CA   1 
ATOM   980  C  C    . LYS   A 1 147 ? 3.192  46.137  20.972  1.00 142.64 ? 168 LYS   A C    1 
ATOM   981  O  O    . LYS   A 1 147 ? 4.088  46.460  20.185  1.00 141.20 ? 168 LYS   A O    1 
ATOM   982  C  CB   . LYS   A 1 147 ? 0.932  47.001  20.331  1.00 136.38 ? 168 LYS   A CB   1 
ATOM   983  N  N    . PRO   A 1 148 ? 3.161  44.930  21.541  1.00 145.29 ? 169 PRO   A N    1 
ATOM   984  C  CA   . PRO   A 1 148 ? 4.204  43.945  21.233  1.00 139.78 ? 169 PRO   A CA   1 
ATOM   985  C  C    . PRO   A 1 148 ? 4.156  43.509  19.774  1.00 139.70 ? 169 PRO   A C    1 
ATOM   986  O  O    . PRO   A 1 148 ? 3.168  43.711  19.066  1.00 142.28 ? 169 PRO   A O    1 
ATOM   987  C  CB   . PRO   A 1 148 ? 3.885  42.780  22.178  1.00 136.76 ? 169 PRO   A CB   1 
ATOM   988  C  CG   . PRO   A 1 148 ? 2.439  42.932  22.504  1.00 139.24 ? 169 PRO   A CG   1 
ATOM   989  C  CD   . PRO   A 1 148 ? 2.203  44.421  22.539  1.00 144.20 ? 169 PRO   A CD   1 
ATOM   990  N  N    . VAL   A 1 149 ? 5.253  42.896  19.327  1.00 138.03 ? 170 VAL   A N    1 
ATOM   991  C  CA   . VAL   A 1 149 ? 5.405  42.448  17.947  1.00 133.62 ? 170 VAL   A CA   1 
ATOM   992  C  C    . VAL   A 1 149 ? 5.926  41.018  17.936  1.00 128.80 ? 170 VAL   A C    1 
ATOM   993  O  O    . VAL   A 1 149 ? 6.842  40.674  18.691  1.00 126.74 ? 170 VAL   A O    1 
ATOM   994  C  CB   . VAL   A 1 149 ? 6.352  43.370  17.149  1.00 131.51 ? 170 VAL   A CB   1 
ATOM   995  N  N    . THR   A 1 150 ? 5.347  40.187  17.070  1.00 130.39 ? 171 THR   A N    1 
ATOM   996  C  CA   . THR   A 1 150 ? 5.809  38.813  16.919  1.00 131.71 ? 171 THR   A CA   1 
ATOM   997  C  C    . THR   A 1 150 ? 7.125  38.797  16.150  1.00 129.09 ? 171 THR   A C    1 
ATOM   998  O  O    . THR   A 1 150 ? 7.204  39.311  15.029  1.00 127.00 ? 171 THR   A O    1 
ATOM   999  C  CB   . THR   A 1 150 ? 4.758  37.969  16.201  1.00 133.62 ? 171 THR   A CB   1 
ATOM   1000 N  N    . LEU   A 1 151 ? 8.158  38.205  16.751  1.00 126.23 ? 172 LEU   A N    1 
ATOM   1001 C  CA   . LEU   A 1 151 ? 9.493  38.241  16.166  1.00 125.41 ? 172 LEU   A CA   1 
ATOM   1002 C  C    . LEU   A 1 151 ? 9.655  37.288  14.990  1.00 128.50 ? 172 LEU   A C    1 
ATOM   1003 O  O    . LEU   A 1 151 ? 10.524 37.519  14.142  1.00 128.36 ? 172 LEU   A O    1 
ATOM   1004 C  CB   . LEU   A 1 151 ? 10.539 37.915  17.233  1.00 125.21 ? 172 LEU   A CB   1 
ATOM   1005 C  CG   . LEU   A 1 151 ? 10.450 38.725  18.526  1.00 123.46 ? 172 LEU   A CG   1 
ATOM   1006 C  CD1  . LEU   A 1 151 ? 11.549 38.316  19.489  1.00 118.27 ? 172 LEU   A CD1  1 
ATOM   1007 C  CD2  . LEU   A 1 151 ? 10.515 40.215  18.234  1.00 129.64 ? 172 LEU   A CD2  1 
ATOM   1008 N  N    . LYS   A 1 152 ? 8.846  36.228  14.918  1.00 130.46 ? 173 LYS   A N    1 
ATOM   1009 C  CA   . LYS   A 1 152 ? 9.012  35.245  13.851  1.00 128.69 ? 173 LYS   A CA   1 
ATOM   1010 C  C    . LYS   A 1 152 ? 8.695  35.833  12.482  1.00 126.87 ? 173 LYS   A C    1 
ATOM   1011 O  O    . LYS   A 1 152 ? 9.325  35.456  11.488  1.00 123.94 ? 173 LYS   A O    1 
ATOM   1012 C  CB   . LYS   A 1 152 ? 8.132  34.025  14.120  1.00 134.24 ? 173 LYS   A CB   1 
ATOM   1013 N  N    . ASP   A 1 153 ? 7.731  36.753  12.408  1.00 130.21 ? 174 ASP   A N    1 
ATOM   1014 C  CA   . ASP   A 1 153 ? 7.370  37.344  11.124  1.00 127.88 ? 174 ASP   A CA   1 
ATOM   1015 C  C    . ASP   A 1 153 ? 8.394  38.378  10.673  1.00 124.91 ? 174 ASP   A C    1 
ATOM   1016 O  O    . ASP   A 1 153 ? 8.700  38.471  9.479   1.00 122.45 ? 174 ASP   A O    1 
ATOM   1017 C  CB   . ASP   A 1 153 ? 5.980  37.974  11.207  1.00 129.43 ? 174 ASP   A CB   1 
ATOM   1018 C  CG   . ASP   A 1 153 ? 4.893  36.952  11.467  1.00 135.12 ? 174 ASP   A CG   1 
ATOM   1019 O  OD1  . ASP   A 1 153 ? 4.847  36.404  12.589  1.00 138.30 ? 174 ASP   A OD1  1 
ATOM   1020 O  OD2  . ASP   A 1 153 ? 4.085  36.695  10.549  1.00 134.61 ? 174 ASP   A OD2  1 
ATOM   1021 N  N    . VAL   A 1 154 ? 8.931  39.164  11.608  1.00 125.40 ? 175 VAL   A N    1 
ATOM   1022 C  CA   . VAL   A 1 154 ? 9.931  40.164  11.249  1.00 124.55 ? 175 VAL   A CA   1 
ATOM   1023 C  C    . VAL   A 1 154 ? 11.250 39.494  10.889  1.00 126.47 ? 175 VAL   A C    1 
ATOM   1024 O  O    . VAL   A 1 154 ? 11.923 39.893  9.931   1.00 126.25 ? 175 VAL   A O    1 
ATOM   1025 C  CB   . VAL   A 1 154 ? 10.105 41.181  12.391  1.00 122.97 ? 175 VAL   A CB   1 
ATOM   1026 N  N    . PHE   A 1 155 ? 11.644 38.470  11.650  1.00 126.98 ? 176 PHE   A N    1 
ATOM   1027 C  CA   . PHE   A 1 155 ? 12.863 37.736  11.325  1.00 122.79 ? 176 PHE   A CA   1 
ATOM   1028 C  C    . PHE   A 1 155 ? 12.707 36.965  10.021  1.00 120.64 ? 176 PHE   A C    1 
ATOM   1029 O  O    . PHE   A 1 155 ? 13.631 36.929  9.201   1.00 117.18 ? 176 PHE   A O    1 
ATOM   1030 C  CB   . PHE   A 1 155 ? 13.230 36.792  12.469  1.00 115.90 ? 176 PHE   A CB   1 
ATOM   1031 N  N    . GLY   A 1 156 ? 11.544 36.343  9.813   1.00 122.83 ? 177 GLY   A N    1 
ATOM   1032 C  CA   . GLY   A 1 156 ? 11.296 35.654  8.559   1.00 123.76 ? 177 GLY   A CA   1 
ATOM   1033 C  C    . GLY   A 1 156 ? 11.282 36.587  7.366   1.00 125.82 ? 177 GLY   A C    1 
ATOM   1034 O  O    . GLY   A 1 156 ? 11.710 36.209  6.272   1.00 126.32 ? 177 GLY   A O    1 
ATOM   1035 N  N    . ALA   A 1 157 ? 10.790 37.814  7.556   1.00 125.37 ? 178 ALA   A N    1 
ATOM   1036 C  CA   . ALA   A 1 157 ? 10.848 38.805  6.487   1.00 128.68 ? 178 ALA   A CA   1 
ATOM   1037 C  C    . ALA   A 1 157 ? 12.290 39.117  6.112   1.00 124.58 ? 178 ALA   A C    1 
ATOM   1038 O  O    . ALA   A 1 157 ? 12.623 39.225  4.926   1.00 124.24 ? 178 ALA   A O    1 
ATOM   1039 C  CB   . ALA   A 1 157 ? 10.117 40.078  6.911   1.00 128.16 ? 178 ALA   A CB   1 
ATOM   1040 N  N    . TYR   A 1 158 ? 13.160 39.260  7.111   1.00 121.58 ? 179 TYR   A N    1 
ATOM   1041 C  CA   . TYR   A 1 158 ? 14.576 39.462  6.832   1.00 121.16 ? 179 TYR   A CA   1 
ATOM   1042 C  C    . TYR   A 1 158 ? 15.219 38.188  6.301   1.00 121.00 ? 179 TYR   A C    1 
ATOM   1043 O  O    . TYR   A 1 158 ? 16.020 38.237  5.360   1.00 116.20 ? 179 TYR   A O    1 
ATOM   1044 C  CB   . TYR   A 1 158 ? 15.294 39.941  8.093   1.00 122.27 ? 179 TYR   A CB   1 
ATOM   1045 C  CG   . TYR   A 1 158 ? 16.802 39.897  7.994   1.00 123.97 ? 179 TYR   A CG   1 
ATOM   1046 C  CD1  . TYR   A 1 158 ? 17.503 40.893  7.328   1.00 124.07 ? 179 TYR   A CD1  1 
ATOM   1047 C  CD2  . TYR   A 1 158 ? 17.526 38.861  8.573   1.00 121.00 ? 179 TYR   A CD2  1 
ATOM   1048 C  CE1  . TYR   A 1 158 ? 18.882 40.857  7.237   1.00 121.75 ? 179 TYR   A CE1  1 
ATOM   1049 C  CE2  . TYR   A 1 158 ? 18.905 38.817  8.487   1.00 115.97 ? 179 TYR   A CE2  1 
ATOM   1050 C  CZ   . TYR   A 1 158 ? 19.578 39.819  7.819   1.00 117.33 ? 179 TYR   A CZ   1 
ATOM   1051 O  OH   . TYR   A 1 158 ? 20.952 39.782  7.731   1.00 112.00 ? 179 TYR   A OH   1 
ATOM   1052 N  N    . SER   A 1 159 ? 14.878 37.038  6.890   1.00 123.64 ? 180 SER   A N    1 
ATOM   1053 C  CA   . SER   A 1 159 ? 15.484 35.778  6.469   1.00 122.46 ? 180 SER   A CA   1 
ATOM   1054 C  C    . SER   A 1 159 ? 15.155 35.451  5.019   1.00 122.38 ? 180 SER   A C    1 
ATOM   1055 O  O    . SER   A 1 159 ? 15.980 34.856  4.317   1.00 123.14 ? 180 SER   A O    1 
ATOM   1056 C  CB   . SER   A 1 159 ? 15.030 34.642  7.386   1.00 117.63 ? 180 SER   A CB   1 
ATOM   1057 N  N    . MET   A 1 160 ? 13.963 35.827  4.552   1.00 123.87 ? 181 MET   A N    1 
ATOM   1058 C  CA   . MET   A 1 160 ? 13.619 35.597  3.152   1.00 124.24 ? 181 MET   A CA   1 
ATOM   1059 C  C    . MET   A 1 160 ? 14.378 36.548  2.237   1.00 122.24 ? 181 MET   A C    1 
ATOM   1060 O  O    . MET   A 1 160 ? 14.845 36.145  1.165   1.00 117.69 ? 181 MET   A O    1 
ATOM   1061 C  CB   . MET   A 1 160 ? 12.112 35.746  2.947   1.00 123.83 ? 181 MET   A CB   1 
ATOM   1062 N  N    . ASP   A 1 161 ? 14.512 37.813  2.644   1.00 127.38 ? 182 ASP   A N    1 
ATOM   1063 C  CA   . ASP   A 1 161 ? 15.203 38.791  1.810   1.00 126.96 ? 182 ASP   A CA   1 
ATOM   1064 C  C    . ASP   A 1 161 ? 16.669 38.424  1.625   1.00 122.40 ? 182 ASP   A C    1 
ATOM   1065 O  O    . ASP   A 1 161 ? 17.200 38.506  0.512   1.00 117.51 ? 182 ASP   A O    1 
ATOM   1066 C  CB   . ASP   A 1 161 ? 15.075 40.187  2.418   1.00 129.92 ? 182 ASP   A CB   1 
ATOM   1067 C  CG   . ASP   A 1 161 ? 13.644 40.682  2.440   1.00 131.03 ? 182 ASP   A CG   1 
ATOM   1068 O  OD1  . ASP   A 1 161 ? 12.852 40.249  1.577   1.00 130.05 ? 182 ASP   A OD1  1 
ATOM   1069 O  OD2  . ASP   A 1 161 ? 13.313 41.507  3.316   1.00 134.09 ? 182 ASP   A OD2  1 
ATOM   1070 N  N    . VAL   A 1 162 ? 17.341 38.016  2.703   1.00 123.22 ? 183 VAL   A N    1 
ATOM   1071 C  CA   . VAL   A 1 162 ? 18.747 37.642  2.587   1.00 123.67 ? 183 VAL   A CA   1 
ATOM   1072 C  C    . VAL   A 1 162 ? 18.891 36.350  1.790   1.00 119.83 ? 183 VAL   A C    1 
ATOM   1073 O  O    . VAL   A 1 162 ? 19.812 36.208  0.979   1.00 115.89 ? 183 VAL   A O    1 
ATOM   1074 C  CB   . VAL   A 1 162 ? 19.398 37.537  3.981   1.00 121.39 ? 183 VAL   A CB   1 
ATOM   1075 C  CG1  . VAL   A 1 162 ? 18.662 36.538  4.858   1.00 116.34 ? 183 VAL   A CG1  1 
ATOM   1076 C  CG2  . VAL   A 1 162 ? 20.867 37.158  3.858   1.00 117.56 ? 183 VAL   A CG2  1 
ATOM   1077 N  N    . ILE   A 1 163 ? 17.974 35.400  1.987   1.00 119.97 ? 184 ILE   A N    1 
ATOM   1078 C  CA   . ILE   A 1 163 ? 18.054 34.132  1.268   1.00 118.74 ? 184 ILE   A CA   1 
ATOM   1079 C  C    . ILE   A 1 163 ? 17.847 34.355  -0.223  1.00 119.23 ? 184 ILE   A C    1 
ATOM   1080 O  O    . ILE   A 1 163 ? 18.595 33.831  -1.056  1.00 123.22 ? 184 ILE   A O    1 
ATOM   1081 C  CB   . ILE   A 1 163 ? 17.036 33.125  1.833   1.00 118.66 ? 184 ILE   A CB   1 
ATOM   1082 N  N    . THR   A 1 164 ? 16.832 35.143  -0.583  1.00 120.11 ? 185 THR   A N    1 
ATOM   1083 C  CA   . THR   A 1 164 ? 16.593 35.434  -1.992  1.00 120.10 ? 185 THR   A CA   1 
ATOM   1084 C  C    . THR   A 1 164 ? 17.727 36.260  -2.585  1.00 122.48 ? 185 THR   A C    1 
ATOM   1085 O  O    . THR   A 1 164 ? 18.156 36.013  -3.718  1.00 120.31 ? 185 THR   A O    1 
ATOM   1086 C  CB   . THR   A 1 164 ? 15.257 36.158  -2.164  1.00 122.19 ? 185 THR   A CB   1 
ATOM   1087 O  OG1  . THR   A 1 164 ? 15.221 37.313  -1.317  1.00 125.25 ? 185 THR   A OG1  1 
ATOM   1088 C  CG2  . THR   A 1 164 ? 14.098 35.235  -1.813  1.00 121.20 ? 185 THR   A CG2  1 
ATOM   1089 N  N    . SER   A 1 165 ? 18.234 37.241  -1.835  1.00 128.48 ? 186 SER   A N    1 
ATOM   1090 C  CA   . SER   A 1 165 ? 19.310 38.083  -2.340  1.00 126.98 ? 186 SER   A CA   1 
ATOM   1091 C  C    . SER   A 1 165 ? 20.661 37.379  -2.348  1.00 125.69 ? 186 SER   A C    1 
ATOM   1092 O  O    . SER   A 1 165 ? 21.599 37.895  -2.964  1.00 128.92 ? 186 SER   A O    1 
ATOM   1093 C  CB   . SER   A 1 165 ? 19.405 39.371  -1.517  1.00 124.56 ? 186 SER   A CB   1 
ATOM   1094 N  N    . THR   A 1 166 ? 20.788 36.229  -1.688  1.00 122.11 ? 187 THR   A N    1 
ATOM   1095 C  CA   . THR   A 1 166 ? 22.025 35.455  -1.706  1.00 122.46 ? 187 THR   A CA   1 
ATOM   1096 C  C    . THR   A 1 166 ? 21.938 34.212  -2.575  1.00 124.74 ? 187 THR   A C    1 
ATOM   1097 O  O    . THR   A 1 166 ? 22.925 33.850  -3.220  1.00 125.68 ? 187 THR   A O    1 
ATOM   1098 C  CB   . THR   A 1 166 ? 22.426 35.048  -0.283  1.00 118.93 ? 187 THR   A CB   1 
ATOM   1099 O  OG1  . THR   A 1 166 ? 22.081 36.098  0.630   1.00 117.83 ? 187 THR   A OG1  1 
ATOM   1100 C  CG2  . THR   A 1 166 ? 23.925 34.805  -0.207  1.00 114.32 ? 187 THR   A CG2  1 
ATOM   1101 N  N    . SER   A 1 167 ? 20.782 33.543  -2.608  1.00 125.44 ? 188 SER   A N    1 
ATOM   1102 C  CA   . SER   A 1 167 ? 20.594 32.438  -3.543  1.00 125.43 ? 188 SER   A CA   1 
ATOM   1103 C  C    . SER   A 1 167 ? 20.398 32.936  -4.969  1.00 128.12 ? 188 SER   A C    1 
ATOM   1104 O  O    . SER   A 1 167 ? 20.827 32.272  -5.918  1.00 127.67 ? 188 SER   A O    1 
ATOM   1105 C  CB   . SER   A 1 167 ? 19.400 31.580  -3.119  1.00 122.80 ? 188 SER   A CB   1 
ATOM   1106 N  N    . PHE   A 1 168 ? 19.763 34.091  -5.136  1.00 131.85 ? 189 PHE   A N    1 
ATOM   1107 C  CA   . PHE   A 1 168 ? 19.606 34.716  -6.445  1.00 130.55 ? 189 PHE   A CA   1 
ATOM   1108 C  C    . PHE   A 1 168 ? 19.940 36.198  -6.282  1.00 131.13 ? 189 PHE   A C    1 
ATOM   1109 O  O    . PHE   A 1 168 ? 20.628 36.614  -5.341  1.00 132.13 ? 189 PHE   A O    1 
ATOM   1110 C  CB   . PHE   A 1 168 ? 18.196 34.474  -6.999  1.00 126.55 ? 189 PHE   A CB   1 
ATOM   1111 C  CG   . PHE   A 1 168 ? 17.690 33.081  -6.770  1.00 120.44 ? 189 PHE   A CG   1 
ATOM   1112 C  CD1  . PHE   A 1 168 ? 18.105 32.037  -7.578  1.00 120.65 ? 189 PHE   A CD1  1 
ATOM   1113 C  CD2  . PHE   A 1 168 ? 16.804 32.815  -5.740  1.00 121.01 ? 189 PHE   A CD2  1 
ATOM   1114 C  CE1  . PHE   A 1 168 ? 17.644 30.752  -7.365  1.00 123.50 ? 189 PHE   A CE1  1 
ATOM   1115 C  CE2  . PHE   A 1 168 ? 16.339 31.534  -5.522  1.00 128.32 ? 189 PHE   A CE2  1 
ATOM   1116 C  CZ   . PHE   A 1 168 ? 16.759 30.501  -6.335  1.00 130.36 ? 189 PHE   A CZ   1 
ATOM   1117 N  N    . GLY   A 1 169 ? 19.450 37.023  -7.205  1.00 131.14 ? 190 GLY   A N    1 
ATOM   1118 C  CA   . GLY   A 1 169 ? 19.655 38.456  -7.141  1.00 131.91 ? 190 GLY   A CA   1 
ATOM   1119 C  C    . GLY   A 1 169 ? 18.443 39.274  -6.758  1.00 131.27 ? 190 GLY   A C    1 
ATOM   1120 O  O    . GLY   A 1 169 ? 18.459 40.498  -6.951  1.00 134.92 ? 190 GLY   A O    1 
ATOM   1121 N  N    . VAL   A 1 170 ? 17.395 38.658  -6.216  1.00 130.37 ? 191 VAL   A N    1 
ATOM   1122 C  CA   . VAL   A 1 170 ? 16.152 39.360  -5.917  1.00 130.92 ? 191 VAL   A CA   1 
ATOM   1123 C  C    . VAL   A 1 170 ? 16.270 40.111  -4.598  1.00 130.95 ? 191 VAL   A C    1 
ATOM   1124 O  O    . VAL   A 1 170 ? 15.991 39.558  -3.528  1.00 130.39 ? 191 VAL   A O    1 
ATOM   1125 C  CB   . VAL   A 1 170 ? 14.961 38.385  -5.883  1.00 128.29 ? 191 VAL   A CB   1 
ATOM   1126 N  N    . ASN   A 1 171 ? 16.684 41.374  -4.664  1.00 131.70 ? 192 ASN   A N    1 
ATOM   1127 C  CA   . ASN   A 1 171 ? 16.657 42.250  -3.498  1.00 132.90 ? 192 ASN   A CA   1 
ATOM   1128 C  C    . ASN   A 1 171 ? 15.215 42.686  -3.274  1.00 133.73 ? 192 ASN   A C    1 
ATOM   1129 O  O    . ASN   A 1 171 ? 14.665 43.464  -4.060  1.00 135.28 ? 192 ASN   A O    1 
ATOM   1130 C  CB   . ASN   A 1 171 ? 17.576 43.451  -3.703  1.00 128.29 ? 192 ASN   A CB   1 
ATOM   1131 N  N    . ILE   A 1 172 ? 14.593 42.178  -2.212  1.00 133.01 ? 193 ILE   A N    1 
ATOM   1132 C  CA   . ILE   A 1 172 ? 13.172 42.379  -1.977  1.00 131.39 ? 193 ILE   A CA   1 
ATOM   1133 C  C    . ILE   A 1 172 ? 12.954 42.816  -0.534  1.00 136.35 ? 193 ILE   A C    1 
ATOM   1134 O  O    . ILE   A 1 172 ? 13.865 42.803  0.294   1.00 135.83 ? 193 ILE   A O    1 
ATOM   1135 C  CB   . ILE   A 1 172 ? 12.347 41.112  -2.284  1.00 131.12 ? 193 ILE   A CB   1 
ATOM   1136 N  N    . ASP   A 1 173 ? 11.719 43.221  -0.255  1.00 139.27 ? 194 ASP   A N    1 
ATOM   1137 C  CA   . ASP   A 1 173 ? 11.231 43.521  1.088   1.00 142.42 ? 194 ASP   A CA   1 
ATOM   1138 C  C    . ASP   A 1 173 ? 10.036 42.593  1.289   1.00 143.55 ? 194 ASP   A C    1 
ATOM   1139 O  O    . ASP   A 1 173 ? 8.899  42.959  0.984   1.00 146.04 ? 194 ASP   A O    1 
ATOM   1140 C  CB   . ASP   A 1 173 ? 10.854 45.001  1.233   1.00 145.30 ? 194 ASP   A CB   1 
ATOM   1141 C  CG   . ASP   A 1 173 ? 10.720 45.435  2.681   1.00 146.37 ? 194 ASP   A CG   1 
ATOM   1142 O  OD1  . ASP   A 1 173 ? 10.375 44.590  3.533   1.00 145.25 ? 194 ASP   A OD1  1 
ATOM   1143 O  OD2  . ASP   A 1 173 ? 10.957 46.629  2.967   1.00 146.27 ? 194 ASP   A OD2  1 
ATOM   1144 N  N    . SER   A 1 174 ? 10.309 41.387  1.799   1.00 143.37 ? 195 SER   A N    1 
ATOM   1145 C  CA   . SER   A 1 174 ? 9.324  40.308  1.768   1.00 143.94 ? 195 SER   A CA   1 
ATOM   1146 C  C    . SER   A 1 174 ? 8.028  40.704  2.466   1.00 147.33 ? 195 SER   A C    1 
ATOM   1147 O  O    . SER   A 1 174 ? 6.933  40.491  1.932   1.00 147.64 ? 195 SER   A O    1 
ATOM   1148 C  CB   . SER   A 1 174 ? 9.912  39.050  2.408   1.00 138.33 ? 195 SER   A CB   1 
ATOM   1149 N  N    . LEU   A 1 175 ? 8.130  41.279  3.665   1.00 148.20 ? 196 LEU   A N    1 
ATOM   1150 C  CA   . LEU   A 1 175 ? 6.924  41.651  4.398   1.00 148.03 ? 196 LEU   A CA   1 
ATOM   1151 C  C    . LEU   A 1 175 ? 6.228  42.841  3.752   1.00 146.72 ? 196 LEU   A C    1 
ATOM   1152 O  O    . LEU   A 1 175 ? 4.994  42.916  3.746   1.00 143.73 ? 196 LEU   A O    1 
ATOM   1153 C  CB   . LEU   A 1 175 ? 7.264  41.957  5.857   1.00 150.50 ? 196 LEU   A CB   1 
ATOM   1154 N  N    . ASN   A 1 176 ? 7.000  43.782  3.206   1.00 146.23 ? 197 ASN   A N    1 
ATOM   1155 C  CA   . ASN   A 1 176 ? 6.433  44.966  2.577   1.00 147.85 ? 197 ASN   A CA   1 
ATOM   1156 C  C    . ASN   A 1 176 ? 6.077  44.755  1.110   1.00 150.34 ? 197 ASN   A C    1 
ATOM   1157 O  O    . ASN   A 1 176 ? 5.342  45.571  0.542   1.00 150.66 ? 197 ASN   A O    1 
ATOM   1158 C  CB   . ASN   A 1 176 ? 7.402  46.146  2.699   1.00 145.89 ? 197 ASN   A CB   1 
ATOM   1159 N  N    . ASN   A 1 177 ? 6.578  43.691  0.484   1.00 149.87 ? 198 ASN   A N    1 
ATOM   1160 C  CA   . ASN   A 1 177 ? 6.232  43.342  -0.894  1.00 145.83 ? 198 ASN   A CA   1 
ATOM   1161 C  C    . ASN   A 1 177 ? 5.732  41.904  -0.924  1.00 146.89 ? 198 ASN   A C    1 
ATOM   1162 O  O    . ASN   A 1 177 ? 6.437  40.994  -1.380  1.00 148.27 ? 198 ASN   A O    1 
ATOM   1163 C  CB   . ASN   A 1 177 ? 7.428  43.531  -1.829  1.00 141.52 ? 198 ASN   A CB   1 
ATOM   1164 N  N    . PRO   A 1 178 ? 4.498  41.660  -0.438  1.00 146.88 ? 199 PRO   A N    1 
ATOM   1165 C  CA   . PRO   A 1 178 ? 3.954  40.300  -0.364  1.00 151.22 ? 199 PRO   A CA   1 
ATOM   1166 C  C    . PRO   A 1 178 ? 3.243  39.868  -1.645  1.00 156.70 ? 199 PRO   A C    1 
ATOM   1167 O  O    . PRO   A 1 178 ? 2.107  39.380  -1.619  1.00 159.98 ? 199 PRO   A O    1 
ATOM   1168 C  CB   . PRO   A 1 178 ? 2.982  40.395  0.817   1.00 147.79 ? 199 PRO   A CB   1 
ATOM   1169 C  CG   . PRO   A 1 178 ? 2.448  41.788  0.710   1.00 145.14 ? 199 PRO   A CG   1 
ATOM   1170 C  CD   . PRO   A 1 178 ? 3.567  42.645  0.143   1.00 144.99 ? 199 PRO   A CD   1 
ATOM   1171 N  N    . GLN   A 1 179 ? 3.910  40.048  -2.785  1.00 157.09 ? 200 GLN   A N    1 
ATOM   1172 C  CA   . GLN   A 1 179 ? 3.326  39.677  -4.072  1.00 152.40 ? 200 GLN   A CA   1 
ATOM   1173 C  C    . GLN   A 1 179 ? 4.298  39.017  -5.037  1.00 153.34 ? 200 GLN   A C    1 
ATOM   1174 O  O    . GLN   A 1 179 ? 3.840  38.404  -6.007  1.00 154.11 ? 200 GLN   A O    1 
ATOM   1175 C  CB   . GLN   A 1 179 ? 2.711  40.905  -4.754  1.00 147.57 ? 200 GLN   A CB   1 
ATOM   1176 N  N    . ASP   A 1 180 ? 5.608  39.111  -4.824  1.00 153.22 ? 201 ASP   A N    1 
ATOM   1177 C  CA   . ASP   A 1 180 ? 6.553  38.468  -5.724  1.00 153.33 ? 201 ASP   A CA   1 
ATOM   1178 C  C    . ASP   A 1 180 ? 6.453  36.950  -5.592  1.00 155.97 ? 201 ASP   A C    1 
ATOM   1179 O  O    . ASP   A 1 180 ? 6.268  36.434  -4.485  1.00 157.83 ? 201 ASP   A O    1 
ATOM   1180 C  CB   . ASP   A 1 180 ? 7.979  38.927  -5.422  1.00 151.94 ? 201 ASP   A CB   1 
ATOM   1181 N  N    . PRO   A 1 181 ? 6.563  36.210  -6.699  1.00 158.15 ? 202 PRO   A N    1 
ATOM   1182 C  CA   . PRO   A 1 181 ? 6.459  34.743  -6.610  1.00 158.90 ? 202 PRO   A CA   1 
ATOM   1183 C  C    . PRO   A 1 181 ? 7.525  34.110  -5.734  1.00 158.65 ? 202 PRO   A C    1 
ATOM   1184 O  O    . PRO   A 1 181 ? 7.281  33.045  -5.153  1.00 159.98 ? 202 PRO   A O    1 
ATOM   1185 C  CB   . PRO   A 1 181 ? 6.591  34.295  -8.073  1.00 162.15 ? 202 PRO   A CB   1 
ATOM   1186 C  CG   . PRO   A 1 181 ? 6.189  35.490  -8.876  1.00 165.77 ? 202 PRO   A CG   1 
ATOM   1187 C  CD   . PRO   A 1 181 ? 6.664  36.676  -8.092  1.00 162.01 ? 202 PRO   A CD   1 
ATOM   1188 N  N    . PHE   A 1 182 ? 8.702  34.731  -5.618  1.00 158.99 ? 203 PHE   A N    1 
ATOM   1189 C  CA   . PHE   A 1 182 ? 9.740  34.184  -4.750  1.00 158.44 ? 203 PHE   A CA   1 
ATOM   1190 C  C    . PHE   A 1 182 ? 9.341  34.281  -3.282  1.00 152.82 ? 203 PHE   A C    1 
ATOM   1191 O  O    . PHE   A 1 182 ? 9.536  33.330  -2.516  1.00 151.14 ? 203 PHE   A O    1 
ATOM   1192 C  CB   . PHE   A 1 182 ? 11.064 34.906  -4.997  1.00 157.68 ? 203 PHE   A CB   1 
ATOM   1193 N  N    . VAL   A 1 183 ? 8.782  35.422  -2.872  1.00 150.39 ? 204 VAL   A N    1 
ATOM   1194 C  CA   . VAL   A 1 183 ? 8.326  35.569  -1.494  1.00 149.78 ? 204 VAL   A CA   1 
ATOM   1195 C  C    . VAL   A 1 183 ? 7.077  34.731  -1.248  1.00 149.45 ? 204 VAL   A C    1 
ATOM   1196 O  O    . VAL   A 1 183 ? 6.892  34.186  -0.152  1.00 147.34 ? 204 VAL   A O    1 
ATOM   1197 C  CB   . VAL   A 1 183 ? 8.084  37.057  -1.172  1.00 147.89 ? 204 VAL   A CB   1 
ATOM   1198 C  CG1  . VAL   A 1 183 ? 7.580  37.227  0.254   1.00 141.74 ? 204 VAL   A CG1  1 
ATOM   1199 C  CG2  . VAL   A 1 183 ? 9.357  37.862  -1.388  1.00 146.08 ? 204 VAL   A CG2  1 
ATOM   1200 N  N    . GLU   A 1 184 ? 6.214  34.593  -2.258  1.00 149.32 ? 205 GLU   A N    1 
ATOM   1201 C  CA   . GLU   A 1 184 ? 4.944  33.896  -2.065  1.00 150.42 ? 205 GLU   A CA   1 
ATOM   1202 C  C    . GLU   A 1 184 ? 5.149  32.402  -1.837  1.00 148.90 ? 205 GLU   A C    1 
ATOM   1203 O  O    . GLU   A 1 184 ? 4.499  31.809  -0.967  1.00 146.15 ? 205 GLU   A O    1 
ATOM   1204 C  CB   . GLU   A 1 184 ? 4.030  34.133  -3.267  1.00 151.23 ? 205 GLU   A CB   1 
ATOM   1205 N  N    . ASN   A 1 185 ? 6.038  31.775  -2.610  1.00 149.97 ? 206 ASN   A N    1 
ATOM   1206 C  CA   . ASN   A 1 185 ? 6.255  30.338  -2.466  1.00 145.01 ? 206 ASN   A CA   1 
ATOM   1207 C  C    . ASN   A 1 185 ? 6.894  30.004  -1.123  1.00 141.64 ? 206 ASN   A C    1 
ATOM   1208 O  O    . ASN   A 1 185 ? 6.493  29.039  -0.462  1.00 138.86 ? 206 ASN   A O    1 
ATOM   1209 C  CB   . ASN   A 1 185 ? 7.123  29.816  -3.614  1.00 142.19 ? 206 ASN   A CB   1 
ATOM   1210 C  CG   . ASN   A 1 185 ? 6.463  29.980  -4.971  1.00 141.56 ? 206 ASN   A CG   1 
ATOM   1211 O  OD1  . ASN   A 1 185 ? 7.109  30.374  -5.943  1.00 140.82 ? 206 ASN   A OD1  1 
ATOM   1212 N  ND2  . ASN   A 1 185 ? 5.173  29.675  -5.045  1.00 141.58 ? 206 ASN   A ND2  1 
ATOM   1213 N  N    . THR   A 1 186 ? 7.886  30.791  -0.702  1.00 140.13 ? 207 THR   A N    1 
ATOM   1214 C  CA   . THR   A 1 186 ? 8.588  30.494  0.543   1.00 140.25 ? 207 THR   A CA   1 
ATOM   1215 C  C    . THR   A 1 186 ? 7.720  30.795  1.759   1.00 141.82 ? 207 THR   A C    1 
ATOM   1216 O  O    . THR   A 1 186 ? 7.712  30.026  2.728   1.00 140.68 ? 207 THR   A O    1 
ATOM   1217 C  CB   . THR   A 1 186 ? 9.895  31.283  0.613   1.00 139.11 ? 207 THR   A CB   1 
ATOM   1218 N  N    . LYS   A 1 187 ? 6.986  31.911  1.732   1.00 142.35 ? 208 LYS   A N    1 
ATOM   1219 C  CA   . LYS   A 1 187 ? 6.140  32.270  2.864   1.00 140.85 ? 208 LYS   A CA   1 
ATOM   1220 C  C    . LYS   A 1 187 ? 4.975  31.306  3.048   1.00 141.42 ? 208 LYS   A C    1 
ATOM   1221 O  O    . LYS   A 1 187 ? 4.440  31.207  4.158   1.00 139.18 ? 208 LYS   A O    1 
ATOM   1222 C  CB   . LYS   A 1 187 ? 5.612  33.697  2.698   1.00 142.30 ? 208 LYS   A CB   1 
ATOM   1223 N  N    . LYS   A 1 188 ? 4.569  30.599  1.991   1.00 142.20 ? 209 LYS   A N    1 
ATOM   1224 C  CA   . LYS   A 1 188 ? 3.499  29.616  2.130   1.00 141.24 ? 209 LYS   A CA   1 
ATOM   1225 C  C    . LYS   A 1 188 ? 3.984  28.375  2.870   1.00 138.10 ? 209 LYS   A C    1 
ATOM   1226 O  O    . LYS   A 1 188 ? 3.249  27.803  3.683   1.00 135.38 ? 209 LYS   A O    1 
ATOM   1227 C  CB   . LYS   A 1 188 ? 2.947  29.244  0.754   1.00 141.08 ? 209 LYS   A CB   1 
ATOM   1228 N  N    . LEU   A 1 189 ? 5.212  27.945  2.600   1.00 135.77 ? 210 LEU   A N    1 
ATOM   1229 C  CA   . LEU   A 1 189 ? 5.806  26.820  3.310   1.00 126.70 ? 210 LEU   A CA   1 
ATOM   1230 C  C    . LEU   A 1 189 ? 7.159  27.208  3.895   1.00 122.52 ? 210 LEU   A C    1 
ATOM   1231 O  O    . LEU   A 1 189 ? 7.453  26.916  5.053   1.00 117.47 ? 210 LEU   A O    1 
ATOM   1232 C  CB   . LEU   A 1 189 ? 5.962  25.613  2.385   1.00 121.91 ? 210 LEU   A CB   1 
ATOM   1233 C  CG   . LEU   A 1 189 ? 6.615  24.395  3.041   1.00 117.73 ? 210 LEU   A CG   1 
ATOM   1234 C  CD1  . LEU   A 1 189 ? 5.586  23.581  3.812   1.00 115.81 ? 210 LEU   A CD1  1 
ATOM   1235 C  CD2  . LEU   A 1 189 ? 7.326  23.539  2.010   1.00 116.92 ? 210 LEU   A CD2  1 
ATOM   1236 N  N    . LEU   A 1 195 ? 4.745  14.665  15.822  1.00 123.38 ? 216 LEU   A N    1 
ATOM   1237 C  CA   . LEU   A 1 195 ? 4.820  15.861  14.991  1.00 124.92 ? 216 LEU   A CA   1 
ATOM   1238 C  C    . LEU   A 1 195 ? 3.513  16.091  14.242  1.00 127.16 ? 216 LEU   A C    1 
ATOM   1239 O  O    . LEU   A 1 195 ? 2.428  15.936  14.804  1.00 123.39 ? 216 LEU   A O    1 
ATOM   1240 C  CB   . LEU   A 1 195 ? 5.979  15.751  13.999  1.00 127.01 ? 216 LEU   A CB   1 
ATOM   1241 N  N    . ASP   A 1 196 ? 3.626  16.472  12.972  1.00 132.29 ? 217 ASP   A N    1 
ATOM   1242 C  CA   . ASP   A 1 196 ? 2.461  16.593  12.116  1.00 126.98 ? 217 ASP   A CA   1 
ATOM   1243 C  C    . ASP   A 1 196 ? 1.875  15.209  11.842  1.00 123.86 ? 217 ASP   A C    1 
ATOM   1244 O  O    . ASP   A 1 196 ? 2.579  14.200  11.927  1.00 121.64 ? 217 ASP   A O    1 
ATOM   1245 C  CB   . ASP   A 1 196 ? 2.833  17.284  10.806  1.00 119.60 ? 217 ASP   A CB   1 
ATOM   1246 N  N    . PRO   A 1 197 ? 0.580  15.135  11.523  1.00 124.62 ? 218 PRO   A N    1 
ATOM   1247 C  CA   . PRO   A 1 197 ? -0.032 13.817  11.275  1.00 126.51 ? 218 PRO   A CA   1 
ATOM   1248 C  C    . PRO   A 1 197 ? 0.613  13.043  10.136  1.00 121.34 ? 218 PRO   A C    1 
ATOM   1249 O  O    . PRO   A 1 197 ? 0.537  11.808  10.121  1.00 115.13 ? 218 PRO   A O    1 
ATOM   1250 C  CB   . PRO   A 1 197 ? -1.494 14.167  10.961  1.00 126.08 ? 218 PRO   A CB   1 
ATOM   1251 C  CG   . PRO   A 1 197 ? -1.722 15.477  11.639  1.00 124.63 ? 218 PRO   A CG   1 
ATOM   1252 C  CD   . PRO   A 1 197 ? -0.420 16.217  11.529  1.00 122.00 ? 218 PRO   A CD   1 
ATOM   1253 N  N    . PHE   A 1 198 ? 1.253  13.726  9.185   1.00 124.52 ? 219 PHE   A N    1 
ATOM   1254 C  CA   . PHE   A 1 198 ? 1.838  13.039  8.039   1.00 122.40 ? 219 PHE   A CA   1 
ATOM   1255 C  C    . PHE   A 1 198 ? 3.177  12.399  8.390   1.00 123.65 ? 219 PHE   A C    1 
ATOM   1256 O  O    . PHE   A 1 198 ? 3.390  11.209  8.131   1.00 121.95 ? 219 PHE   A O    1 
ATOM   1257 C  CB   . PHE   A 1 198 ? 2.000  14.013  6.870   1.00 126.11 ? 219 PHE   A CB   1 
ATOM   1258 N  N    . PHE   A 1 199 ? 4.092  13.175  8.978   1.00 123.61 ? 220 PHE   A N    1 
ATOM   1259 C  CA   . PHE   A 1 199 ? 5.427  12.659  9.272   1.00 120.81 ? 220 PHE   A CA   1 
ATOM   1260 C  C    . PHE   A 1 199 ? 5.385  11.522  10.284  1.00 116.07 ? 220 PHE   A C    1 
ATOM   1261 O  O    . PHE   A 1 199 ? 6.202  10.597  10.211  1.00 111.48 ? 220 PHE   A O    1 
ATOM   1262 C  CB   . PHE   A 1 199 ? 6.325  13.788  9.778   1.00 124.50 ? 220 PHE   A CB   1 
ATOM   1263 N  N    . LEU   A 1 200 ? 4.447  11.570  11.232  1.00 117.60 ? 221 LEU   A N    1 
ATOM   1264 C  CA   . LEU   A 1 200 ? 4.343  10.497  12.214  1.00 116.21 ? 221 LEU   A CA   1 
ATOM   1265 C  C    . LEU   A 1 200 ? 3.862  9.199   11.580  1.00 113.44 ? 221 LEU   A C    1 
ATOM   1266 O  O    . LEU   A 1 200 ? 4.219  8.113   12.051  1.00 113.85 ? 221 LEU   A O    1 
ATOM   1267 C  CB   . LEU   A 1 200 ? 3.408  10.913  13.350  1.00 119.30 ? 221 LEU   A CB   1 
ATOM   1268 N  N    . SER   A 1 201 ? 3.062  9.285   10.514  1.00 112.69 ? 222 SER   A N    1 
ATOM   1269 C  CA   . SER   A 1 201 ? 2.561  8.076   9.870   1.00 110.42 ? 222 SER   A CA   1 
ATOM   1270 C  C    . SER   A 1 201 ? 3.641  7.385   9.047   1.00 110.17 ? 222 SER   A C    1 
ATOM   1271 O  O    . SER   A 1 201 ? 3.596  6.161   8.873   1.00 108.80 ? 222 SER   A O    1 
ATOM   1272 C  CB   . SER   A 1 201 ? 1.357  8.407   8.990   1.00 109.14 ? 222 SER   A CB   1 
ATOM   1273 O  OG   . SER   A 1 201 ? 0.283  8.914   9.763   1.00 111.09 ? 222 SER   A OG   1 
ATOM   1274 N  N    . ILE   A 1 202 ? 4.613  8.144   8.536   1.00 109.73 ? 223 ILE   A N    1 
ATOM   1275 C  CA   . ILE   A 1 202 ? 5.667  7.546   7.723   1.00 109.71 ? 223 ILE   A CA   1 
ATOM   1276 C  C    . ILE   A 1 202 ? 6.607  6.710   8.580   1.00 107.58 ? 223 ILE   A C    1 
ATOM   1277 O  O    . ILE   A 1 202 ? 7.235  5.766   8.085   1.00 110.96 ? 223 ILE   A O    1 
ATOM   1278 C  CB   . ILE   A 1 202 ? 6.431  8.637   6.952   1.00 108.49 ? 223 ILE   A CB   1 
ATOM   1279 N  N    . THR   A 1 203 ? 6.726  7.036   9.869   1.00 108.45 ? 224 THR   A N    1 
ATOM   1280 C  CA   . THR   A 1 203 ? 7.597  6.264   10.750  1.00 108.48 ? 224 THR   A CA   1 
ATOM   1281 C  C    . THR   A 1 203 ? 7.051  4.860   10.977  1.00 103.78 ? 224 THR   A C    1 
ATOM   1282 O  O    . THR   A 1 203 ? 7.806  3.881   10.946  1.00 102.22 ? 224 THR   A O    1 
ATOM   1283 C  CB   . THR   A 1 203 ? 7.769  6.990   12.083  1.00 104.51 ? 224 THR   A CB   1 
ATOM   1284 O  OG1  . THR   A 1 203 ? 6.486  7.165   12.697  1.00 103.02 ? 224 THR   A OG1  1 
ATOM   1285 C  CG2  . THR   A 1 203 ? 8.412  8.353   11.868  1.00 107.87 ? 224 THR   A CG2  1 
ATOM   1286 N  N    . VAL   A 1 204 ? 5.743  4.743   11.211  1.00 102.90 ? 225 VAL   A N    1 
ATOM   1287 C  CA   . VAL   A 1 204 ? 5.139  3.429   11.400  1.00 102.43 ? 225 VAL   A CA   1 
ATOM   1288 C  C    . VAL   A 1 204 ? 5.072  2.672   10.083  1.00 103.60 ? 225 VAL   A C    1 
ATOM   1289 O  O    . VAL   A 1 204 ? 5.186  1.440   10.058  1.00 103.34 ? 225 VAL   A O    1 
ATOM   1290 C  CB   . VAL   A 1 204 ? 3.745  3.577   12.038  1.00 103.58 ? 225 VAL   A CB   1 
ATOM   1291 C  CG1  . VAL   A 1 204 ? 3.076  2.218   12.199  1.00 101.20 ? 225 VAL   A CG1  1 
ATOM   1292 C  CG2  . VAL   A 1 204 ? 3.858  4.281   13.373  1.00 101.86 ? 225 VAL   A CG2  1 
ATOM   1293 N  N    . PHE   A 1 205 ? 4.904  3.385   8.969   1.00 102.48 ? 226 PHE   A N    1 
ATOM   1294 C  CA   . PHE   A 1 205 ? 4.742  2.778   7.650   1.00 103.09 ? 226 PHE   A CA   1 
ATOM   1295 C  C    . PHE   A 1 205 ? 5.855  3.247   6.719   1.00 103.55 ? 226 PHE   A C    1 
ATOM   1296 O  O    . PHE   A 1 205 ? 5.621  4.067   5.820   1.00 104.48 ? 226 PHE   A O    1 
ATOM   1297 C  CB   . PHE   A 1 205 ? 3.373  3.111   7.062   1.00 102.67 ? 226 PHE   A CB   1 
ATOM   1298 N  N    . PRO   A 1 206 ? 7.082  2.743   6.898   1.00 105.39 ? 227 PRO   A N    1 
ATOM   1299 C  CA   . PRO   A 1 206 ? 8.127  3.022   5.903   1.00 103.34 ? 227 PRO   A CA   1 
ATOM   1300 C  C    . PRO   A 1 206 ? 7.862  2.341   4.576   1.00 100.80 ? 227 PRO   A C    1 
ATOM   1301 O  O    . PRO   A 1 206 ? 8.416  2.766   3.555   1.00 100.39 ? 227 PRO   A O    1 
ATOM   1302 C  CB   . PRO   A 1 206 ? 9.400  2.485   6.567   1.00 101.34 ? 227 PRO   A CB   1 
ATOM   1303 C  CG   . PRO   A 1 206 ? 8.913  1.399   7.457   1.00 105.87 ? 227 PRO   A CG   1 
ATOM   1304 C  CD   . PRO   A 1 206 ? 7.569  1.854   7.968   1.00 106.57 ? 227 PRO   A CD   1 
ATOM   1305 N  N    . PHE   A 1 207 ? 7.031  1.296   4.562   1.00 99.15  ? 228 PHE   A N    1 
ATOM   1306 C  CA   . PHE   A 1 207 ? 6.617  0.676   3.312   1.00 100.80 ? 228 PHE   A CA   1 
ATOM   1307 C  C    . PHE   A 1 207 ? 5.753  1.603   2.472   1.00 102.39 ? 228 PHE   A C    1 
ATOM   1308 O  O    . PHE   A 1 207 ? 5.627  1.387   1.262   1.00 107.37 ? 228 PHE   A O    1 
ATOM   1309 C  CB   . PHE   A 1 207 ? 5.867  -0.628  3.596   1.00 102.11 ? 228 PHE   A CB   1 
ATOM   1310 C  CG   . PHE   A 1 207 ? 4.762  -0.489  4.608   1.00 104.96 ? 228 PHE   A CG   1 
ATOM   1311 C  CD1  . PHE   A 1 207 ? 3.478  -0.150  4.213   1.00 104.48 ? 228 PHE   A CD1  1 
ATOM   1312 C  CD2  . PHE   A 1 207 ? 5.005  -0.708  5.956   1.00 102.25 ? 228 PHE   A CD2  1 
ATOM   1313 C  CE1  . PHE   A 1 207 ? 2.460  -0.026  5.141   1.00 102.52 ? 228 PHE   A CE1  1 
ATOM   1314 C  CE2  . PHE   A 1 207 ? 3.992  -0.585  6.888   1.00 95.25  ? 228 PHE   A CE2  1 
ATOM   1315 C  CZ   . PHE   A 1 207 ? 2.718  -0.245  6.480   1.00 97.69  ? 228 PHE   A CZ   1 
ATOM   1316 N  N    . LEU   A 1 208 ? 5.157  2.627   3.083   1.00 97.59  ? 229 LEU   A N    1 
ATOM   1317 C  CA   . LEU   A 1 208 ? 4.363  3.590   2.333   1.00 99.43  ? 229 LEU   A CA   1 
ATOM   1318 C  C    . LEU   A 1 208 ? 5.223  4.608   1.595   1.00 99.55  ? 229 LEU   A C    1 
ATOM   1319 O  O    . LEU   A 1 208 ? 4.715  5.292   0.700   1.00 99.03  ? 229 LEU   A O    1 
ATOM   1320 C  CB   . LEU   A 1 208 ? 3.393  4.313   3.270   1.00 97.68  ? 229 LEU   A CB   1 
ATOM   1321 N  N    . ILE   A 1 209 ? 6.508  4.719   1.945   1.00 98.60  ? 230 ILE   A N    1 
ATOM   1322 C  CA   . ILE   A 1 209 ? 7.378  5.692   1.281   1.00 99.21  ? 230 ILE   A CA   1 
ATOM   1323 C  C    . ILE   A 1 209 ? 7.493  5.432   -0.218  1.00 103.47 ? 230 ILE   A C    1 
ATOM   1324 O  O    . ILE   A 1 209 ? 7.256  6.365   -1.003  1.00 106.67 ? 230 ILE   A O    1 
ATOM   1325 C  CB   . ILE   A 1 209 ? 8.746  5.745   1.981   1.00 101.61 ? 230 ILE   A CB   1 
ATOM   1326 C  CG1  . ILE   A 1 209 ? 8.616  6.379   3.367   1.00 102.96 ? 230 ILE   A CG1  1 
ATOM   1327 C  CG2  . ILE   A 1 209 ? 9.758  6.495   1.125   1.00 105.77 ? 230 ILE   A CG2  1 
ATOM   1328 C  CD1  . ILE   A 1 209 ? 9.923  6.460   4.126   1.00 99.37  ? 230 ILE   A CD1  1 
ATOM   1329 N  N    . PRO   A 1 210 ? 7.843  4.226   -0.687  1.00 100.41 ? 231 PRO   A N    1 
ATOM   1330 C  CA   . PRO   A 1 210 ? 7.912  4.019   -2.142  1.00 102.13 ? 231 PRO   A CA   1 
ATOM   1331 C  C    . PRO   A 1 210 ? 6.557  4.073   -2.823  1.00 100.93 ? 231 PRO   A C    1 
ATOM   1332 O  O    . PRO   A 1 210 ? 6.499  4.377   -4.021  1.00 104.78 ? 231 PRO   A O    1 
ATOM   1333 C  CB   . PRO   A 1 210 ? 8.547  2.629   -2.269  1.00 105.14 ? 231 PRO   A CB   1 
ATOM   1334 C  CG   . PRO   A 1 210 ? 8.159  1.938   -1.019  1.00 99.05  ? 231 PRO   A CG   1 
ATOM   1335 C  CD   . PRO   A 1 210 ? 8.193  2.994   0.045   1.00 98.21  ? 231 PRO   A CD   1 
ATOM   1336 N  N    . ILE   A 1 211 ? 5.469  3.793   -2.103  1.00 100.90 ? 232 ILE   A N    1 
ATOM   1337 C  CA   . ILE   A 1 211 ? 4.144  3.888   -2.705  1.00 101.79 ? 232 ILE   A CA   1 
ATOM   1338 C  C    . ILE   A 1 211 ? 3.752  5.343   -2.916  1.00 107.55 ? 232 ILE   A C    1 
ATOM   1339 O  O    . ILE   A 1 211 ? 3.057  5.672   -3.886  1.00 112.77 ? 232 ILE   A O    1 
ATOM   1340 C  CB   . ILE   A 1 211 ? 3.109  3.147   -1.839  1.00 100.25 ? 232 ILE   A CB   1 
ATOM   1341 N  N    . LEU   A 1 212 ? 4.181  6.238   -2.023  1.00 101.67 ? 233 LEU   A N    1 
ATOM   1342 C  CA   . LEU   A 1 212 ? 3.876  7.654   -2.192  1.00 99.90  ? 233 LEU   A CA   1 
ATOM   1343 C  C    . LEU   A 1 212 ? 4.597  8.232   -3.404  1.00 105.92 ? 233 LEU   A C    1 
ATOM   1344 O  O    . LEU   A 1 212 ? 4.024  9.037   -4.148  1.00 108.97 ? 233 LEU   A O    1 
ATOM   1345 C  CB   . LEU   A 1 212 ? 4.246  8.426   -0.926  1.00 104.02 ? 233 LEU   A CB   1 
ATOM   1346 C  CG   . LEU   A 1 212 ? 3.373  8.189   0.308   1.00 102.64 ? 233 LEU   A CG   1 
ATOM   1347 C  CD1  . LEU   A 1 212 ? 4.027  8.780   1.548   1.00 105.23 ? 233 LEU   A CD1  1 
ATOM   1348 C  CD2  . LEU   A 1 212 ? 1.984  8.775   0.104   1.00 101.88 ? 233 LEU   A CD2  1 
ATOM   1349 N  N    . GLU   A 1 213 ? 5.854  7.833   -3.619  1.00 107.22 ? 234 GLU   A N    1 
ATOM   1350 C  CA   . GLU   A 1 213 ? 6.586  8.295   -4.794  1.00 107.32 ? 234 GLU   A CA   1 
ATOM   1351 C  C    . GLU   A 1 213 ? 5.985  7.750   -6.081  1.00 106.63 ? 234 GLU   A C    1 
ATOM   1352 O  O    . GLU   A 1 213 ? 6.036  8.420   -7.119  1.00 114.17 ? 234 GLU   A O    1 
ATOM   1353 C  CB   . GLU   A 1 213 ? 8.059  7.903   -4.683  1.00 108.01 ? 234 GLU   A CB   1 
ATOM   1354 C  CG   . GLU   A 1 213 ? 8.913  8.919   -3.942  1.00 109.30 ? 234 GLU   A CG   1 
ATOM   1355 C  CD   . GLU   A 1 213 ? 10.221 8.333   -3.447  1.00 113.42 ? 234 GLU   A CD   1 
ATOM   1356 O  OE1  . GLU   A 1 213 ? 10.186 7.513   -2.505  1.00 110.92 ? 234 GLU   A OE1  1 
ATOM   1357 O  OE2  . GLU   A 1 213 ? 11.284 8.685   -4.002  1.00 112.09 ? 234 GLU   A OE2  1 
ATOM   1358 N  N    . VAL   A 1 214 ? 5.415  6.543   -6.038  1.00 103.35 ? 235 VAL   A N    1 
ATOM   1359 C  CA   . VAL   A 1 214 ? 4.713  6.022   -7.205  1.00 105.64 ? 235 VAL   A CA   1 
ATOM   1360 C  C    . VAL   A 1 214 ? 3.467  6.849   -7.489  1.00 111.16 ? 235 VAL   A C    1 
ATOM   1361 O  O    . VAL   A 1 214 ? 3.059  6.995   -8.648  1.00 115.77 ? 235 VAL   A O    1 
ATOM   1362 C  CB   . VAL   A 1 214 ? 4.371  4.534   -7.007  1.00 106.25 ? 235 VAL   A CB   1 
ATOM   1363 N  N    . LEU   A 1 215 ? 2.844  7.405   -6.450  1.00 107.13 ? 236 LEU   A N    1 
ATOM   1364 C  CA   . LEU   A 1 215 ? 1.712  8.306   -6.621  1.00 106.34 ? 236 LEU   A CA   1 
ATOM   1365 C  C    . LEU   A 1 215 ? 2.138  9.733   -6.941  1.00 110.31 ? 236 LEU   A C    1 
ATOM   1366 O  O    . LEU   A 1 215 ? 1.274  10.611  -7.039  1.00 116.53 ? 236 LEU   A O    1 
ATOM   1367 C  CB   . LEU   A 1 215 ? 0.837  8.298   -5.364  1.00 102.55 ? 236 LEU   A CB   1 
ATOM   1368 N  N    . ASN   A 1 216 ? 3.441  9.981   -7.092  1.00 109.38 ? 237 ASN   A N    1 
ATOM   1369 C  CA   . ASN   A 1 216 ? 3.995  11.283  -7.462  1.00 111.05 ? 237 ASN   A CA   1 
ATOM   1370 C  C    . ASN   A 1 216 ? 3.572  12.395  -6.508  1.00 112.05 ? 237 ASN   A C    1 
ATOM   1371 O  O    . ASN   A 1 216 ? 3.559  13.571  -6.886  1.00 110.05 ? 237 ASN   A O    1 
ATOM   1372 C  CB   . ASN   A 1 216 ? 3.620  11.656  -8.902  1.00 111.58 ? 237 ASN   A CB   1 
ATOM   1373 N  N    . ILE   A 1 217 ? 3.229  12.051  -5.272  1.00 112.52 ? 238 ILE   A N    1 
ATOM   1374 C  CA   . ILE   A 1 217 ? 2.800  13.021  -4.273  1.00 111.44 ? 238 ILE   A CA   1 
ATOM   1375 C  C    . ILE   A 1 217 ? 3.972  13.223  -3.317  1.00 115.22 ? 238 ILE   A C    1 
ATOM   1376 O  O    . ILE   A 1 217 ? 4.262  12.374  -2.469  1.00 111.56 ? 238 ILE   A O    1 
ATOM   1377 C  CB   . ILE   A 1 217 ? 1.522  12.568  -3.557  1.00 108.99 ? 238 ILE   A CB   1 
ATOM   1378 C  CG1  . ILE   A 1 217 ? 1.219  13.464  -2.355  1.00 110.41 ? 238 ILE   A CG1  1 
ATOM   1379 C  CG2  . ILE   A 1 217 ? 1.595  11.092  -3.161  1.00 103.85 ? 238 ILE   A CG2  1 
ATOM   1380 C  CD1  . ILE   A 1 217 ? -0.154 13.230  -1.772  1.00 108.29 ? 238 ILE   A CD1  1 
ATOM   1381 N  N    . CYS   A 1 218 ? 4.667  14.347  -3.466  1.00 119.02 ? 239 CYS   A N    1 
ATOM   1382 C  CA   . CYS   A 1 218 ? 5.839  14.645  -2.658  1.00 116.81 ? 239 CYS   A CA   1 
ATOM   1383 C  C    . CYS   A 1 218 ? 5.484  15.610  -1.532  1.00 121.12 ? 239 CYS   A C    1 
ATOM   1384 O  O    . CYS   A 1 218 ? 4.558  16.417  -1.648  1.00 123.89 ? 239 CYS   A O    1 
ATOM   1385 C  CB   . CYS   A 1 218 ? 6.969  15.225  -3.516  1.00 114.74 ? 239 CYS   A CB   1 
ATOM   1386 S  SG   . CYS   A 1 218 ? 6.588  16.772  -4.374  1.00 114.57 ? 239 CYS   A SG   1 
ATOM   1387 N  N    . VAL   A 1 219 ? 6.242  15.516  -0.435  1.00 123.58 ? 240 VAL   A N    1 
ATOM   1388 C  CA   . VAL   A 1 219 ? 5.940  16.284  0.769   1.00 126.33 ? 240 VAL   A CA   1 
ATOM   1389 C  C    . VAL   A 1 219 ? 6.095  17.785  0.548   1.00 125.96 ? 240 VAL   A C    1 
ATOM   1390 O  O    . VAL   A 1 219 ? 5.572  18.581  1.337   1.00 124.05 ? 240 VAL   A O    1 
ATOM   1391 C  CB   . VAL   A 1 219 ? 6.831  15.798  1.931   1.00 123.53 ? 240 VAL   A CB   1 
ATOM   1392 C  CG1  . VAL   A 1 219 ? 8.266  16.271  1.742   1.00 122.92 ? 240 VAL   A CG1  1 
ATOM   1393 C  CG2  . VAL   A 1 219 ? 6.271  16.249  3.275   1.00 121.64 ? 240 VAL   A CG2  1 
ATOM   1394 N  N    . PHE   A 1 220 ? 6.792  18.198  -0.512  1.00 127.52 ? 241 PHE   A N    1 
ATOM   1395 C  CA   . PHE   A 1 220 ? 6.958  19.612  -0.816  1.00 130.39 ? 241 PHE   A CA   1 
ATOM   1396 C  C    . PHE   A 1 220 ? 5.914  20.035  -1.837  1.00 129.15 ? 241 PHE   A C    1 
ATOM   1397 O  O    . PHE   A 1 220 ? 5.817  19.400  -2.898  1.00 127.40 ? 241 PHE   A O    1 
ATOM   1398 C  CB   . PHE   A 1 220 ? 8.360  19.887  -1.348  1.00 125.98 ? 241 PHE   A CB   1 
ATOM   1399 C  CG   . PHE   A 1 220 ? 9.450  19.224  -0.554  1.00 121.26 ? 241 PHE   A CG   1 
ATOM   1400 C  CD1  . PHE   A 1 220 ? 9.769  19.673  0.717   1.00 121.65 ? 241 PHE   A CD1  1 
ATOM   1401 C  CD2  . PHE   A 1 220 ? 10.156 18.153  -1.078  1.00 117.41 ? 241 PHE   A CD2  1 
ATOM   1402 C  CE1  . PHE   A 1 220 ? 10.770 19.064  1.453   1.00 117.44 ? 241 PHE   A CE1  1 
ATOM   1403 C  CE2  . PHE   A 1 220 ? 11.160 17.540  -0.348  1.00 112.54 ? 241 PHE   A CE2  1 
ATOM   1404 C  CZ   . PHE   A 1 220 ? 11.467 17.996  0.919   1.00 110.24 ? 241 PHE   A CZ   1 
ATOM   1405 N  N    . PRO   A 1 221 ? 5.100  21.071  -1.555  1.00 124.32 ? 242 PRO   A N    1 
ATOM   1406 C  CA   . PRO   A 1 221 ? 4.107  21.540  -2.533  1.00 123.44 ? 242 PRO   A CA   1 
ATOM   1407 C  C    . PRO   A 1 221 ? 4.651  21.662  -3.948  1.00 126.66 ? 242 PRO   A C    1 
ATOM   1408 O  O    . PRO   A 1 221 ? 5.575  22.439  -4.204  1.00 130.53 ? 242 PRO   A O    1 
ATOM   1409 C  CB   . PRO   A 1 221 ? 3.699  22.913  -1.980  1.00 131.50 ? 242 PRO   A CB   1 
ATOM   1410 C  CG   . PRO   A 1 221 ? 4.062  22.883  -0.505  1.00 128.76 ? 242 PRO   A CG   1 
ATOM   1411 C  CD   . PRO   A 1 221 ? 4.855  21.633  -0.218  1.00 124.06 ? 242 PRO   A CD   1 
ATOM   1412 N  N    . ARG   A 1 222 ? 4.079  20.887  -4.874  1.00 128.87 ? 243 ARG   A N    1 
ATOM   1413 C  CA   . ARG   A 1 222 ? 4.568  20.868  -6.247  1.00 128.67 ? 243 ARG   A CA   1 
ATOM   1414 C  C    . ARG   A 1 222 ? 4.365  22.198  -6.959  1.00 127.75 ? 243 ARG   A C    1 
ATOM   1415 O  O    . ARG   A 1 222 ? 5.063  22.472  -7.941  1.00 128.75 ? 243 ARG   A O    1 
ATOM   1416 C  CB   . ARG   A 1 222 ? 3.885  19.748  -7.034  1.00 124.36 ? 243 ARG   A CB   1 
ATOM   1417 N  N    . GLU   A 1 223 ? 3.429  23.029  -6.491  1.00 128.56 ? 244 GLU   A N    1 
ATOM   1418 C  CA   . GLU   A 1 223 ? 3.218  24.329  -7.117  1.00 130.41 ? 244 GLU   A CA   1 
ATOM   1419 C  C    . GLU   A 1 223 ? 4.420  25.246  -6.930  1.00 133.85 ? 244 GLU   A C    1 
ATOM   1420 O  O    . GLU   A 1 223 ? 4.719  26.062  -7.809  1.00 133.28 ? 244 GLU   A O    1 
ATOM   1421 C  CB   . GLU   A 1 223 ? 1.957  24.985  -6.555  1.00 123.18 ? 244 GLU   A CB   1 
ATOM   1422 N  N    . VAL   A 1 224 ? 5.120  25.127  -5.800  1.00 134.73 ? 245 VAL   A N    1 
ATOM   1423 C  CA   . VAL   A 1 224 ? 6.297  25.957  -5.570  1.00 132.16 ? 245 VAL   A CA   1 
ATOM   1424 C  C    . VAL   A 1 224 ? 7.520  25.382  -6.276  1.00 133.49 ? 245 VAL   A C    1 
ATOM   1425 O  O    . VAL   A 1 224 ? 8.438  26.128  -6.638  1.00 133.83 ? 245 VAL   A O    1 
ATOM   1426 C  CB   . VAL   A 1 224 ? 6.548  26.121  -4.062  1.00 128.87 ? 245 VAL   A CB   1 
ATOM   1427 N  N    . THR   A 1 225 ? 7.557  24.062  -6.483  1.00 132.55 ? 246 THR   A N    1 
ATOM   1428 C  CA   . THR   A 1 225 ? 8.699  23.447  -7.153  1.00 131.10 ? 246 THR   A CA   1 
ATOM   1429 C  C    . THR   A 1 225 ? 8.772  23.866  -8.616  1.00 135.88 ? 246 THR   A C    1 
ATOM   1430 O  O    . THR   A 1 225 ? 9.852  24.199  -9.121  1.00 134.65 ? 246 THR   A O    1 
ATOM   1431 C  CB   . THR   A 1 225 ? 8.624  21.924  -7.037  1.00 124.99 ? 246 THR   A CB   1 
ATOM   1432 O  OG1  . THR   A 1 225 ? 7.475  21.442  -7.748  1.00 129.02 ? 246 THR   A OG1  1 
ATOM   1433 C  CG2  . THR   A 1 225 ? 8.520  21.505  -5.579  1.00 121.64 ? 246 THR   A CG2  1 
ATOM   1434 N  N    . ASN   A 1 226 ? 7.634  23.854  -9.314  1.00 135.96 ? 247 ASN   A N    1 
ATOM   1435 C  CA   . ASN   A 1 226 ? 7.618  24.298  -10.703 1.00 136.49 ? 247 ASN   A CA   1 
ATOM   1436 C  C    . ASN   A 1 226 ? 7.855  25.798  -10.809 1.00 138.83 ? 247 ASN   A C    1 
ATOM   1437 O  O    . ASN   A 1 226 ? 8.412  26.267  -11.809 1.00 138.70 ? 247 ASN   A O    1 
ATOM   1438 C  CB   . ASN   A 1 226 ? 6.292  23.916  -11.359 1.00 134.92 ? 247 ASN   A CB   1 
ATOM   1439 C  CG   . ASN   A 1 226 ? 5.891  22.481  -11.070 1.00 140.26 ? 247 ASN   A CG   1 
ATOM   1440 O  OD1  . ASN   A 1 226 ? 4.739  22.200  -10.740 1.00 143.03 ? 247 ASN   A OD1  1 
ATOM   1441 N  ND2  . ASN   A 1 226 ? 6.847  21.565  -11.184 1.00 140.11 ? 247 ASN   A ND2  1 
ATOM   1442 N  N    . PHE   A 1 227 ? 7.441  26.562  -9.795  1.00 135.74 ? 248 PHE   A N    1 
ATOM   1443 C  CA   . PHE   A 1 227 ? 7.720  27.994  -9.787  1.00 133.77 ? 248 PHE   A CA   1 
ATOM   1444 C  C    . PHE   A 1 227 ? 9.212  28.261  -9.634  1.00 136.52 ? 248 PHE   A C    1 
ATOM   1445 O  O    . PHE   A 1 227 ? 9.750  29.187  -10.251 1.00 139.29 ? 248 PHE   A O    1 
ATOM   1446 C  CB   . PHE   A 1 227 ? 6.932  28.675  -8.669  1.00 127.48 ? 248 PHE   A CB   1 
ATOM   1447 N  N    . LEU   A 1 228 ? 9.895  27.458  -8.815  1.00 134.15 ? 249 LEU   A N    1 
ATOM   1448 C  CA   . LEU   A 1 228 ? 11.342 27.593  -8.689  1.00 136.94 ? 249 LEU   A CA   1 
ATOM   1449 C  C    . LEU   A 1 228 ? 12.064 27.035  -9.908  1.00 140.69 ? 249 LEU   A C    1 
ATOM   1450 O  O    . LEU   A 1 228 ? 13.179 27.470  -10.220 1.00 139.69 ? 249 LEU   A O    1 
ATOM   1451 C  CB   . LEU   A 1 228 ? 11.826 26.895  -7.418  1.00 129.20 ? 249 LEU   A CB   1 
ATOM   1452 N  N    . ARG   A 1 229 ? 11.451 26.076  -10.606 1.00 140.81 ? 250 ARG   A N    1 
ATOM   1453 C  CA   . ARG   A 1 229 ? 12.062 25.534  -11.815 1.00 140.68 ? 250 ARG   A CA   1 
ATOM   1454 C  C    . ARG   A 1 229 ? 12.079 26.573  -12.929 1.00 142.71 ? 250 ARG   A C    1 
ATOM   1455 O  O    . ARG   A 1 229 ? 13.100 26.761  -13.602 1.00 143.80 ? 250 ARG   A O    1 
ATOM   1456 C  CB   . ARG   A 1 229 ? 11.319 24.274  -12.260 1.00 137.22 ? 250 ARG   A CB   1 
ATOM   1457 N  N    . LYS   A 1 230 ? 10.954 27.261  -13.138 1.00 139.91 ? 251 LYS   A N    1 
ATOM   1458 C  CA   . LYS   A 1 230 ? 10.912 28.318  -14.142 1.00 141.32 ? 251 LYS   A CA   1 
ATOM   1459 C  C    . LYS   A 1 230 ? 11.743 29.522  -13.721 1.00 142.24 ? 251 LYS   A C    1 
ATOM   1460 O  O    . LYS   A 1 230 ? 12.349 30.183  -14.573 1.00 141.20 ? 251 LYS   A O    1 
ATOM   1461 C  CB   . LYS   A 1 230 ? 9.465  28.734  -14.407 1.00 140.07 ? 251 LYS   A CB   1 
ATOM   1462 N  N    . SER   A 1 231 ? 11.785 29.822  -12.420 1.00 144.14 ? 252 SER   A N    1 
ATOM   1463 C  CA   . SER   A 1 231 ? 12.610 30.927  -11.942 1.00 144.64 ? 252 SER   A CA   1 
ATOM   1464 C  C    . SER   A 1 231 ? 14.090 30.649  -12.171 1.00 144.36 ? 252 SER   A C    1 
ATOM   1465 O  O    . SER   A 1 231 ? 14.850 31.557  -12.525 1.00 141.96 ? 252 SER   A O    1 
ATOM   1466 C  CB   . SER   A 1 231 ? 12.338 31.184  -10.460 1.00 138.45 ? 252 SER   A CB   1 
ATOM   1467 O  OG   . SER   A 1 231 ? 13.271 32.105  -9.923  1.00 135.41 ? 252 SER   A OG   1 
ATOM   1468 N  N    . VAL   A 1 232 ? 14.517 29.400  -11.970 1.00 143.33 ? 253 VAL   A N    1 
ATOM   1469 C  CA   . VAL   A 1 232 ? 15.911 29.050  -12.216 1.00 143.63 ? 253 VAL   A CA   1 
ATOM   1470 C  C    . VAL   A 1 232 ? 16.212 29.059  -13.708 1.00 145.91 ? 253 VAL   A C    1 
ATOM   1471 O  O    . VAL   A 1 232 ? 17.344 29.344  -14.118 1.00 147.23 ? 253 VAL   A O    1 
ATOM   1472 C  CB   . VAL   A 1 232 ? 16.240 27.684  -11.585 1.00 137.55 ? 253 VAL   A CB   1 
ATOM   1473 N  N    . LYS   A 1 233 ? 15.217 28.749  -14.541 1.00 144.46 ? 254 LYS   A N    1 
ATOM   1474 C  CA   . LYS   A 1 233 ? 15.427 28.779  -15.985 1.00 146.85 ? 254 LYS   A CA   1 
ATOM   1475 C  C    . LYS   A 1 233 ? 15.598 30.208  -16.485 1.00 148.49 ? 254 LYS   A C    1 
ATOM   1476 O  O    . LYS   A 1 233 ? 16.492 30.488  -17.293 1.00 146.89 ? 254 LYS   A O    1 
ATOM   1477 C  CB   . LYS   A 1 233 ? 14.262 28.092  -16.697 1.00 144.89 ? 254 LYS   A CB   1 
ATOM   1478 N  N    . ARG   A 1 234 ? 14.751 31.128  -16.014 1.00 149.28 ? 255 ARG   A N    1 
ATOM   1479 C  CA   . ARG   A 1 234 ? 14.886 32.526  -16.409 1.00 149.55 ? 255 ARG   A CA   1 
ATOM   1480 C  C    . ARG   A 1 234 ? 16.140 33.156  -15.818 1.00 147.54 ? 255 ARG   A C    1 
ATOM   1481 O  O    . ARG   A 1 234 ? 16.767 34.005  -16.462 1.00 146.46 ? 255 ARG   A O    1 
ATOM   1482 C  CB   . ARG   A 1 234 ? 13.646 33.315  -15.988 1.00 145.75 ? 255 ARG   A CB   1 
ATOM   1483 N  N    . MET   A 1 235 ? 16.517 32.759  -14.600 1.00 146.47 ? 256 MET   A N    1 
ATOM   1484 C  CA   . MET   A 1 235 ? 17.754 33.262  -14.013 1.00 146.06 ? 256 MET   A CA   1 
ATOM   1485 C  C    . MET   A 1 235 ? 18.969 32.756  -14.780 1.00 144.05 ? 256 MET   A C    1 
ATOM   1486 O  O    . MET   A 1 235 ? 19.953 33.486  -14.947 1.00 144.84 ? 256 MET   A O    1 
ATOM   1487 C  CB   . MET   A 1 235 ? 17.838 32.863  -12.541 1.00 143.82 ? 256 MET   A CB   1 
ATOM   1488 N  N    . LYS   A 1 236 ? 18.919 31.507  -15.253 1.00 142.96 ? 257 LYS   A N    1 
ATOM   1489 C  CA   . LYS   A 1 236 ? 19.997 30.995  -16.092 1.00 143.12 ? 257 LYS   A CA   1 
ATOM   1490 C  C    . LYS   A 1 236 ? 20.083 31.756  -17.406 1.00 142.98 ? 257 LYS   A C    1 
ATOM   1491 O  O    . LYS   A 1 236 ? 21.181 31.951  -17.941 1.00 141.86 ? 257 LYS   A O    1 
ATOM   1492 C  CB   . LYS   A 1 236 ? 19.799 29.501  -16.352 1.00 142.52 ? 257 LYS   A CB   1 
ATOM   1493 N  N    . GLU   A 1 237 ? 18.940 32.192  -17.941 1.00 144.19 ? 258 GLU   A N    1 
ATOM   1494 C  CA   . GLU   A 1 237 ? 18.957 33.037  -19.129 1.00 145.35 ? 258 GLU   A CA   1 
ATOM   1495 C  C    . GLU   A 1 237 ? 19.433 34.446  -18.801 1.00 142.74 ? 258 GLU   A C    1 
ATOM   1496 O  O    . GLU   A 1 237 ? 20.022 35.115  -19.658 1.00 141.59 ? 258 GLU   A O    1 
ATOM   1497 C  CB   . GLU   A 1 237 ? 17.569 33.079  -19.767 1.00 147.76 ? 258 GLU   A CB   1 
ATOM   1498 N  N    . SER   A 1 238 ? 19.188 34.912  -17.573 1.00 140.37 ? 259 SER   A N    1 
ATOM   1499 C  CA   . SER   A 1 238 ? 19.693 36.218  -17.165 1.00 140.40 ? 259 SER   A CA   1 
ATOM   1500 C  C    . SER   A 1 238 ? 21.209 36.212  -17.029 1.00 142.94 ? 259 SER   A C    1 
ATOM   1501 O  O    . SER   A 1 238 ? 21.853 37.247  -17.241 1.00 146.17 ? 259 SER   A O    1 
ATOM   1502 C  CB   . SER   A 1 238 ? 19.041 36.649  -15.851 1.00 137.61 ? 259 SER   A CB   1 
ATOM   1503 N  N    . ARG   A 1 239 ? 21.795 35.066  -16.677 1.00 140.71 ? 260 ARG   A N    1 
ATOM   1504 C  CA   . ARG   A 1 239 ? 23.250 34.960  -16.627 1.00 139.95 ? 260 ARG   A CA   1 
ATOM   1505 C  C    . ARG   A 1 239 ? 23.852 35.100  -18.020 1.00 141.23 ? 260 ARG   A C    1 
ATOM   1506 O  O    . ARG   A 1 239 ? 24.739 35.933  -18.243 1.00 142.64 ? 260 ARG   A O    1 
ATOM   1507 C  CB   . ARG   A 1 239 ? 23.657 33.631  -15.991 1.00 137.84 ? 260 ARG   A CB   1 
ATOM   1508 N  N    . LEU   A 1 240 ? 23.376 34.295  -18.968 1.00 142.09 ? 261 LEU   A N    1 
ATOM   1509 C  CA   . LEU   A 1 240 ? 23.801 34.363  -20.367 1.00 142.54 ? 261 LEU   A CA   1 
ATOM   1510 C  C    . LEU   A 1 240 ? 25.318 34.279  -20.524 1.00 145.95 ? 261 LEU   A C    1 
ATOM   1511 O  O    . LEU   A 1 240 ? 25.967 35.256  -20.900 1.00 149.40 ? 261 LEU   A O    1 
ATOM   1512 C  CB   . LEU   A 1 240 ? 23.280 35.647  -21.018 1.00 141.57 ? 261 LEU   A CB   1 
ATOM   1513 N  N    . LYS   A 1 245 ? 27.204 40.312  -14.724 1.00 127.95 ? 266 LYS   A N    1 
ATOM   1514 C  CA   . LYS   A 1 245 ? 28.516 40.075  -14.135 1.00 130.64 ? 266 LYS   A CA   1 
ATOM   1515 C  C    . LYS   A 1 245 ? 28.390 39.611  -12.688 1.00 135.55 ? 266 LYS   A C    1 
ATOM   1516 O  O    . LYS   A 1 245 ? 29.260 39.884  -11.861 1.00 135.69 ? 266 LYS   A O    1 
ATOM   1517 C  CB   . LYS   A 1 245 ? 29.374 41.339  -14.210 1.00 123.17 ? 266 LYS   A CB   1 
ATOM   1518 N  N    . HIS   A 1 246 ? 27.301 38.905  -12.391 1.00 137.99 ? 267 HIS   A N    1 
ATOM   1519 C  CA   . HIS   A 1 246 ? 27.017 38.441  -11.035 1.00 137.81 ? 267 HIS   A CA   1 
ATOM   1520 C  C    . HIS   A 1 246 ? 28.028 37.370  -10.646 1.00 141.16 ? 267 HIS   A C    1 
ATOM   1521 O  O    . HIS   A 1 246 ? 27.926 36.215  -11.067 1.00 141.44 ? 267 HIS   A O    1 
ATOM   1522 C  CB   . HIS   A 1 246 ? 25.591 37.909  -10.944 1.00 132.97 ? 267 HIS   A CB   1 
ATOM   1523 N  N    . ARG   A 1 247 ? 29.015 37.753  -9.837  1.00 140.66 ? 268 ARG   A N    1 
ATOM   1524 C  CA   . ARG   A 1 247 ? 30.013 36.828  -9.316  1.00 138.50 ? 268 ARG   A CA   1 
ATOM   1525 C  C    . ARG   A 1 247 ? 29.867 36.605  -7.816  1.00 142.46 ? 268 ARG   A C    1 
ATOM   1526 O  O    . ARG   A 1 247 ? 30.723 35.953  -7.208  1.00 145.10 ? 268 ARG   A O    1 
ATOM   1527 C  CB   . ARG   A 1 247 ? 31.422 37.330  -9.639  1.00 138.08 ? 268 ARG   A CB   1 
ATOM   1528 N  N    . VAL   A 1 248 ? 28.807 37.135  -7.206  1.00 141.39 ? 269 VAL   A N    1 
ATOM   1529 C  CA   . VAL   A 1 248 ? 28.546 36.943  -5.784  1.00 141.89 ? 269 VAL   A CA   1 
ATOM   1530 C  C    . VAL   A 1 248 ? 27.121 36.435  -5.611  1.00 142.49 ? 269 VAL   A C    1 
ATOM   1531 O  O    . VAL   A 1 248 ? 26.225 37.187  -5.209  1.00 142.23 ? 269 VAL   A O    1 
ATOM   1532 C  CB   . VAL   A 1 248 ? 28.772 38.244  -4.992  1.00 145.00 ? 269 VAL   A CB   1 
ATOM   1533 N  N    . ASP   A 1 249 ? 26.904 35.156  -5.911  1.00 142.05 ? 270 ASP   A N    1 
ATOM   1534 C  CA   . ASP   A 1 249 ? 25.569 34.574  -5.883  1.00 134.76 ? 270 ASP   A CA   1 
ATOM   1535 C  C    . ASP   A 1 249 ? 25.694 33.069  -5.698  1.00 130.45 ? 270 ASP   A C    1 
ATOM   1536 O  O    . ASP   A 1 249 ? 26.598 32.446  -6.262  1.00 128.58 ? 270 ASP   A O    1 
ATOM   1537 C  CB   . ASP   A 1 249 ? 24.805 34.896  -7.175  1.00 133.90 ? 270 ASP   A CB   1 
ATOM   1538 C  CG   . ASP   A 1 249 ? 23.332 34.553  -7.085  1.00 129.97 ? 270 ASP   A CG   1 
ATOM   1539 O  OD1  . ASP   A 1 249 ? 22.832 34.384  -5.956  1.00 128.03 ? 270 ASP   A OD1  1 
ATOM   1540 O  OD2  . ASP   A 1 249 ? 22.677 34.452  -8.144  1.00 129.98 ? 270 ASP   A OD2  1 
ATOM   1541 N  N    . PHE   A 1 250 ? 24.777 32.483  -4.926  1.00 128.89 ? 271 PHE   A N    1 
ATOM   1542 C  CA   . PHE   A 1 250 ? 24.806 31.012  -4.702  1.00 126.53 ? 271 PHE   A CA   1 
ATOM   1543 C  C    . PHE   A 1 250 ? 24.679 30.302  -6.042  1.00 126.43 ? 271 PHE   A C    1 
ATOM   1544 O  O    . PHE   A 1 250 ? 25.551 29.477  -6.381  1.00 121.32 ? 271 PHE   A O    1 
ATOM   1545 C  CB   . PHE   A 1 250 ? 23.670 30.618  -3.758  1.00 123.47 ? 271 PHE   A CB   1 
ATOM   1546 C  CG   . PHE   A 1 250 ? 24.008 30.707  -2.276  1.00 123.17 ? 271 PHE   A CG   1 
ATOM   1547 C  CD1  . PHE   A 1 250 ? 25.301 30.990  -1.854  1.00 118.05 ? 271 PHE   A CD1  1 
ATOM   1548 C  CD2  . PHE   A 1 250 ? 23.031 30.506  -1.309  1.00 122.61 ? 271 PHE   A CD2  1 
ATOM   1549 C  CE1  . PHE   A 1 250 ? 25.604 31.069  -0.505  1.00 115.72 ? 271 PHE   A CE1  1 
ATOM   1550 C  CE2  . PHE   A 1 250 ? 23.340 30.587  0.039   1.00 115.30 ? 271 PHE   A CE2  1 
ATOM   1551 C  CZ   . PHE   A 1 250 ? 24.624 30.868  0.438   1.00 112.35 ? 271 PHE   A CZ   1 
ATOM   1552 N  N    . LEU   A 1 251 ? 23.625 30.624  -6.798  1.00 130.87 ? 272 LEU   A N    1 
ATOM   1553 C  CA   . LEU   A 1 251 ? 23.378 29.961  -8.105  1.00 124.03 ? 272 LEU   A CA   1 
ATOM   1554 C  C    . LEU   A 1 251 ? 24.561 30.229  -9.038  1.00 122.04 ? 272 LEU   A C    1 
ATOM   1555 O  O    . LEU   A 1 251 ? 25.058 29.283  -9.670  1.00 120.56 ? 272 LEU   A O    1 
ATOM   1556 C  CB   . LEU   A 1 251 ? 22.080 30.497  -8.702  1.00 115.52 ? 272 LEU   A CB   1 
ATOM   1557 N  N    . GLN   A 1 252 ? 24.972 31.487  -9.120  1.00 125.56 ? 273 GLN   A N    1 
ATOM   1558 C  CA   . GLN   A 1 252 ? 26.123 31.831  -9.980  1.00 128.97 ? 273 GLN   A CA   1 
ATOM   1559 C  C    . GLN   A 1 252 ? 27.224 30.818  -9.698  1.00 124.06 ? 273 GLN   A C    1 
ATOM   1560 O  O    . GLN   A 1 252 ? 27.658 30.108  -10.627 1.00 124.53 ? 273 GLN   A O    1 
ATOM   1561 C  CB   . GLN   A 1 252 ? 26.623 33.228  -9.624  1.00 130.82 ? 273 GLN   A CB   1 
ATOM   1562 N  N    . LEU   A 1 253 ? 27.642 30.760  -8.442  1.00 123.96 ? 274 LEU   A N    1 
ATOM   1563 C  CA   . LEU   A 1 253 ? 28.734 29.863  -8.082  1.00 127.00 ? 274 LEU   A CA   1 
ATOM   1564 C  C    . LEU   A 1 253 ? 28.433 28.416  -8.447  1.00 125.67 ? 274 LEU   A C    1 
ATOM   1565 O  O    . LEU   A 1 253 ? 29.363 27.607  -8.536  1.00 125.78 ? 274 LEU   A O    1 
ATOM   1566 C  CB   . LEU   A 1 253 ? 29.035 29.974  -6.587  1.00 123.84 ? 274 LEU   A CB   1 
ATOM   1567 N  N    . MET   A 1 254 ? 27.162 28.072  -8.656  1.00 124.95 ? 275 MET   A N    1 
ATOM   1568 C  CA   . MET   A 1 254 ? 26.789 26.725  -9.070  1.00 124.26 ? 275 MET   A CA   1 
ATOM   1569 C  C    . MET   A 1 254 ? 26.756 26.562  -10.582 1.00 120.79 ? 275 MET   A C    1 
ATOM   1570 O  O    . MET   A 1 254 ? 26.996 25.457  -11.083 1.00 119.67 ? 275 MET   A O    1 
ATOM   1571 C  CB   . MET   A 1 254 ? 25.422 26.350  -8.489  1.00 126.38 ? 275 MET   A CB   1 
ATOM   1572 C  CG   . MET   A 1 254 ? 25.484 25.736  -7.098  1.00 124.52 ? 275 MET   A CG   1 
ATOM   1573 S  SD   . MET   A 1 254 ? 23.865 25.277  -6.442  1.00 111.62 ? 275 MET   A SD   1 
ATOM   1574 C  CE   . MET   A 1 254 ? 23.210 26.879  -5.982  1.00 112.69 ? 275 MET   A CE   1 
ATOM   1575 N  N    . ILE   A 1 255 ? 26.461 27.632  -11.320 1.00 123.50 ? 276 ILE   A N    1 
ATOM   1576 C  CA   . ILE   A 1 255 ? 26.437 27.544  -12.775 1.00 122.73 ? 276 ILE   A CA   1 
ATOM   1577 C  C    . ILE   A 1 255 ? 27.848 27.620  -13.343 1.00 123.57 ? 276 ILE   A C    1 
ATOM   1578 O  O    . ILE   A 1 255 ? 28.181 26.916  -14.303 1.00 123.01 ? 276 ILE   A O    1 
ATOM   1579 C  CB   . ILE   A 1 255 ? 25.527 28.642  -13.355 1.00 117.80 ? 276 ILE   A CB   1 
ATOM   1580 C  CG1  . ILE   A 1 255 ? 24.071 28.392  -12.959 1.00 110.57 ? 276 ILE   A CG1  1 
ATOM   1581 C  CG2  . ILE   A 1 255 ? 25.658 28.706  -14.869 1.00 125.79 ? 276 ILE   A CG2  1 
ATOM   1582 C  CD1  . ILE   A 1 255 ? 23.482 27.138  -13.567 1.00 113.55 ? 276 ILE   A CD1  1 
ATOM   1583 N  N    . ASP   A 1 256 ? 28.700 28.464  -12.757 1.00 124.97 ? 277 ASP   A N    1 
ATOM   1584 C  CA   . ASP   A 1 256 ? 30.070 28.595  -13.243 1.00 128.21 ? 277 ASP   A CA   1 
ATOM   1585 C  C    . ASP   A 1 256 ? 30.850 27.301  -13.041 1.00 128.96 ? 277 ASP   A C    1 
ATOM   1586 O  O    . ASP   A 1 256 ? 31.553 26.839  -13.948 1.00 128.63 ? 277 ASP   A O    1 
ATOM   1587 C  CB   . ASP   A 1 256 ? 30.766 29.762  -12.542 1.00 133.74 ? 277 ASP   A CB   1 
ATOM   1588 N  N    . SER   A 1 257 ? 30.738 26.699  -11.854 1.00 130.44 ? 278 SER   A N    1 
ATOM   1589 C  CA   . SER   A 1 257 ? 31.385 25.416  -11.607 1.00 132.36 ? 278 SER   A CA   1 
ATOM   1590 C  C    . SER   A 1 257 ? 30.775 24.297  -12.441 1.00 128.74 ? 278 SER   A C    1 
ATOM   1591 O  O    . SER   A 1 257 ? 31.425 23.265  -12.645 1.00 119.89 ? 278 SER   A O    1 
ATOM   1592 C  CB   . SER   A 1 257 ? 31.307 25.064  -10.121 1.00 127.39 ? 278 SER   A CB   1 
ATOM   1593 N  N    . GLN   A 1 258 ? 29.545 24.480  -12.926 1.00 130.83 ? 279 GLN   A N    1 
ATOM   1594 C  CA   . GLN   A 1 258 ? 28.921 23.478  -13.782 1.00 127.06 ? 279 GLN   A CA   1 
ATOM   1595 C  C    . GLN   A 1 258 ? 29.627 23.390  -15.129 1.00 125.23 ? 279 GLN   A C    1 
ATOM   1596 O  O    . GLN   A 1 258 ? 29.981 22.296  -15.587 1.00 124.53 ? 279 GLN   A O    1 
ATOM   1597 C  CB   . GLN   A 1 258 ? 27.439 23.806  -13.967 1.00 122.17 ? 279 GLN   A CB   1 
ATOM   1598 C  CG   . GLN   A 1 258 ? 26.733 22.950  -15.000 1.00 121.78 ? 279 GLN   A CG   1 
ATOM   1599 C  CD   . GLN   A 1 258 ? 25.261 23.287  -15.116 1.00 122.32 ? 279 GLN   A CD   1 
ATOM   1600 O  OE1  . GLN   A 1 258 ? 24.844 24.409  -14.823 1.00 116.65 ? 279 GLN   A OE1  1 
ATOM   1601 N  NE2  . GLN   A 1 258 ? 24.463 22.313  -15.538 1.00 123.32 ? 279 GLN   A NE2  1 
ATOM   1602 N  N    . ASN   A 1 259 ? 29.842 24.530  -15.777 1.00 125.12 ? 280 ASN   A N    1 
ATOM   1603 C  CA   . ASN   A 1 259 ? 30.515 24.562  -17.070 1.00 126.33 ? 280 ASN   A CA   1 
ATOM   1604 C  C    . ASN   A 1 259 ? 32.028 24.666  -16.898 1.00 121.49 ? 280 ASN   A C    1 
ATOM   1605 O  O    . ASN   A 1 259 ? 32.728 23.653  -16.843 1.00 116.36 ? 280 ASN   A O    1 
ATOM   1606 C  CB   . ASN   A 1 259 ? 29.997 25.730  -17.914 1.00 120.26 ? 280 ASN   A CB   1 
ATOM   1607 C  CG   . ASN   A 1 259 ? 28.506 25.641  -18.178 1.00 120.29 ? 280 ASN   A CG   1 
ATOM   1608 O  OD1  . ASN   A 1 259 ? 27.752 26.562  -17.863 1.00 121.30 ? 280 ASN   A OD1  1 
ATOM   1609 N  ND2  . ASN   A 1 259 ? 28.073 24.528  -18.759 1.00 117.06 ? 280 ASN   A ND2  1 
ATOM   1610 N  N    . HIS   A 1 266 ? 35.364 14.498  -10.361 1.00 111.08 ? 287 HIS   A N    1 
ATOM   1611 C  CA   . HIS   A 1 266 ? 33.959 14.129  -10.243 1.00 113.72 ? 287 HIS   A CA   1 
ATOM   1612 C  C    . HIS   A 1 266 ? 33.245 14.290  -11.578 1.00 117.77 ? 287 HIS   A C    1 
ATOM   1613 O  O    . HIS   A 1 266 ? 33.881 14.418  -12.626 1.00 118.70 ? 287 HIS   A O    1 
ATOM   1614 C  CB   . HIS   A 1 266 ? 33.264 14.974  -9.171  1.00 112.58 ? 287 HIS   A CB   1 
ATOM   1615 C  CG   . HIS   A 1 266 ? 33.820 14.786  -7.793  1.00 118.72 ? 287 HIS   A CG   1 
ATOM   1616 N  ND1  . HIS   A 1 266 ? 33.548 13.674  -7.026  1.00 117.32 ? 287 HIS   A ND1  1 
ATOM   1617 C  CD2  . HIS   A 1 266 ? 34.627 15.572  -7.042  1.00 118.99 ? 287 HIS   A CD2  1 
ATOM   1618 C  CE1  . HIS   A 1 266 ? 34.167 13.780  -5.864  1.00 111.65 ? 287 HIS   A CE1  1 
ATOM   1619 N  NE2  . HIS   A 1 266 ? 34.829 14.923  -5.848  1.00 116.46 ? 287 HIS   A NE2  1 
ATOM   1620 N  N    . LYS   A 1 267 ? 31.920 14.278  -11.532 1.00 114.20 ? 288 LYS   A N    1 
ATOM   1621 C  CA   . LYS   A 1 267 ? 31.097 14.460  -12.712 1.00 111.05 ? 288 LYS   A CA   1 
ATOM   1622 C  C    . LYS   A 1 267 ? 30.590 15.908  -12.750 1.00 116.50 ? 288 LYS   A C    1 
ATOM   1623 O  O    . LYS   A 1 267 ? 31.110 16.775  -12.040 1.00 121.51 ? 288 LYS   A O    1 
ATOM   1624 C  CB   . LYS   A 1 267 ? 29.977 13.410  -12.699 1.00 108.85 ? 288 LYS   A CB   1 
ATOM   1625 N  N    . ALA   A 1 268 ? 29.593 16.187  -13.587 1.00 117.20 ? 289 ALA   A N    1 
ATOM   1626 C  CA   . ALA   A 1 268 ? 29.043 17.531  -13.725 1.00 117.95 ? 289 ALA   A CA   1 
ATOM   1627 C  C    . ALA   A 1 268 ? 27.756 17.680  -12.919 1.00 117.78 ? 289 ALA   A C    1 
ATOM   1628 O  O    . ALA   A 1 268 ? 27.043 16.705  -12.670 1.00 118.87 ? 289 ALA   A O    1 
ATOM   1629 C  CB   . ALA   A 1 268 ? 28.766 17.865  -15.194 1.00 118.90 ? 289 ALA   A CB   1 
ATOM   1630 N  N    . LEU   A 1 269 ? 27.457 18.917  -12.522 1.00 115.20 ? 290 LEU   A N    1 
ATOM   1631 C  CA   . LEU   A 1 269 ? 26.236 19.215  -11.781 1.00 117.18 ? 290 LEU   A CA   1 
ATOM   1632 C  C    . LEU   A 1 269 ? 25.086 19.460  -12.751 1.00 119.03 ? 290 LEU   A C    1 
ATOM   1633 O  O    . LEU   A 1 269 ? 25.219 20.242  -13.698 1.00 124.56 ? 290 LEU   A O    1 
ATOM   1634 C  CB   . LEU   A 1 269 ? 26.432 20.431  -10.873 1.00 117.45 ? 290 LEU   A CB   1 
ATOM   1635 N  N    . SER   A 1 270 ? 23.957 18.795  -12.509 1.00 113.69 ? 291 SER   A N    1 
ATOM   1636 C  CA   . SER   A 1 270 ? 22.817 18.872  -13.409 1.00 113.24 ? 291 SER   A CA   1 
ATOM   1637 C  C    . SER   A 1 270 ? 22.047 20.178  -13.209 1.00 111.49 ? 291 SER   A C    1 
ATOM   1638 O  O    . SER   A 1 270 ? 22.275 20.934  -12.261 1.00 105.58 ? 291 SER   A O    1 
ATOM   1639 C  CB   . SER   A 1 270 ? 21.890 17.674  -13.202 1.00 110.58 ? 291 SER   A CB   1 
ATOM   1640 O  OG   . SER   A 1 270 ? 20.672 17.840  -13.908 1.00 113.45 ? 291 SER   A OG   1 
ATOM   1641 N  N    . ASP   A 1 271 ? 21.119 20.440  -14.134 1.00 114.53 ? 292 ASP   A N    1 
ATOM   1642 C  CA   . ASP   A 1 271 ? 20.273 21.626  -14.036 1.00 115.64 ? 292 ASP   A CA   1 
ATOM   1643 C  C    . ASP   A 1 271 ? 19.189 21.447  -12.980 1.00 108.89 ? 292 ASP   A C    1 
ATOM   1644 O  O    . ASP   A 1 271 ? 19.046 22.284  -12.082 1.00 102.32 ? 292 ASP   A O    1 
ATOM   1645 C  CB   . ASP   A 1 271 ? 19.648 21.945  -15.394 1.00 115.87 ? 292 ASP   A CB   1 
ATOM   1646 C  CG   . ASP   A 1 271 ? 20.399 23.029  -16.142 1.00 115.12 ? 292 ASP   A CG   1 
ATOM   1647 O  OD1  . ASP   A 1 271 ? 21.450 23.484  -15.641 1.00 112.21 ? 292 ASP   A OD1  1 
ATOM   1648 O  OD2  . ASP   A 1 271 ? 19.933 23.432  -17.228 1.00 120.50 ? 292 ASP   A OD2  1 
ATOM   1649 N  N    . LEU   A 1 272 ? 18.409 20.367  -13.080 1.00 108.26 ? 293 LEU   A N    1 
ATOM   1650 C  CA   . LEU   A 1 272 ? 17.408 20.095  -12.054 1.00 108.08 ? 293 LEU   A CA   1 
ATOM   1651 C  C    . LEU   A 1 272 ? 18.062 19.823  -10.707 1.00 106.06 ? 293 LEU   A C    1 
ATOM   1652 O  O    . LEU   A 1 272 ? 17.464 20.096  -9.659  1.00 103.55 ? 293 LEU   A O    1 
ATOM   1653 C  CB   . LEU   A 1 272 ? 16.527 18.915  -12.465 1.00 108.18 ? 293 LEU   A CB   1 
ATOM   1654 C  CG   . LEU   A 1 272 ? 15.317 18.661  -11.562 1.00 99.44  ? 293 LEU   A CG   1 
ATOM   1655 C  CD1  . LEU   A 1 272 ? 14.363 19.847  -11.600 1.00 97.38  ? 293 LEU   A CD1  1 
ATOM   1656 C  CD2  . LEU   A 1 272 ? 14.601 17.375  -11.949 1.00 98.65  ? 293 LEU   A CD2  1 
ATOM   1657 N  N    . GLU   A 1 273 ? 19.286 19.286  -10.713 1.00 106.64 ? 294 GLU   A N    1 
ATOM   1658 C  CA   . GLU   A 1 273 ? 20.041 19.166  -9.471  1.00 103.55 ? 294 GLU   A CA   1 
ATOM   1659 C  C    . GLU   A 1 273 ? 20.309 20.538  -8.866  1.00 98.70  ? 294 GLU   A C    1 
ATOM   1660 O  O    . GLU   A 1 273 ? 20.174 20.726  -7.652  1.00 91.53  ? 294 GLU   A O    1 
ATOM   1661 C  CB   . GLU   A 1 273 ? 21.352 18.420  -9.721  1.00 102.98 ? 294 GLU   A CB   1 
ATOM   1662 N  N    . LEU   A 1 274 ? 20.675 21.514  -9.702  1.00 105.50 ? 295 LEU   A N    1 
ATOM   1663 C  CA   . LEU   A 1 274 ? 20.873 22.873  -9.210  1.00 108.39 ? 295 LEU   A CA   1 
ATOM   1664 C  C    . LEU   A 1 274 ? 19.574 23.472  -8.684  1.00 103.73 ? 295 LEU   A C    1 
ATOM   1665 O  O    . LEU   A 1 274 ? 19.599 24.286  -7.754  1.00 100.63 ? 295 LEU   A O    1 
ATOM   1666 C  CB   . LEU   A 1 274 ? 21.456 23.754  -10.317 1.00 109.13 ? 295 LEU   A CB   1 
ATOM   1667 N  N    . VAL   A 1 275 ? 18.435 23.084  -9.263  1.00 99.72  ? 296 VAL   A N    1 
ATOM   1668 C  CA   . VAL   A 1 275 ? 17.151 23.571  -8.769  1.00 98.20  ? 296 VAL   A CA   1 
ATOM   1669 C  C    . VAL   A 1 275 ? 16.875 23.024  -7.373  1.00 92.13  ? 296 VAL   A C    1 
ATOM   1670 O  O    . VAL   A 1 275 ? 16.336 23.728  -6.512  1.00 88.10  ? 296 VAL   A O    1 
ATOM   1671 C  CB   . VAL   A 1 275 ? 16.028 23.206  -9.757  1.00 103.05 ? 296 VAL   A CB   1 
ATOM   1672 C  CG1  . VAL   A 1 275 ? 14.671 23.634  -9.213  1.00 104.10 ? 296 VAL   A CG1  1 
ATOM   1673 C  CG2  . VAL   A 1 275 ? 16.285 23.847  -11.111 1.00 103.72 ? 296 VAL   A CG2  1 
ATOM   1674 N  N    . ALA   A 1 276 ? 17.255 21.770  -7.121  1.00 91.08  ? 297 ALA   A N    1 
ATOM   1675 C  CA   . ALA   A 1 276 ? 16.967 21.157  -5.828  1.00 89.36  ? 297 ALA   A CA   1 
ATOM   1676 C  C    . ALA   A 1 276 ? 17.831 21.749  -4.720  1.00 90.28  ? 297 ALA   A C    1 
ATOM   1677 O  O    . ALA   A 1 276 ? 17.329 22.043  -3.628  1.00 85.81  ? 297 ALA   A O    1 
ATOM   1678 C  CB   . ALA   A 1 276 ? 17.164 19.644  -5.910  1.00 87.90  ? 297 ALA   A CB   1 
ATOM   1679 N  N    . GLN   A 1 277 ? 19.130 21.928  -4.976  1.00 91.49  ? 298 GLN   A N    1 
ATOM   1680 C  CA   . GLN   A 1 277 ? 20.018 22.451  -3.942  1.00 85.65  ? 298 GLN   A CA   1 
ATOM   1681 C  C    . GLN   A 1 277 ? 19.649 23.875  -3.554  1.00 89.12  ? 298 GLN   A C    1 
ATOM   1682 O  O    . GLN   A 1 277 ? 19.813 24.266  -2.392  1.00 88.42  ? 298 GLN   A O    1 
ATOM   1683 C  CB   . GLN   A 1 277 ? 21.474 22.400  -4.409  1.00 87.42  ? 298 GLN   A CB   1 
ATOM   1684 C  CG   . GLN   A 1 277 ? 21.880 21.103  -5.081  1.00 86.72  ? 298 GLN   A CG   1 
ATOM   1685 C  CD   . GLN   A 1 277 ? 21.506 19.878  -4.275  1.00 84.64  ? 298 GLN   A CD   1 
ATOM   1686 O  OE1  . GLN   A 1 277 ? 21.715 19.828  -3.064  1.00 85.73  ? 298 GLN   A OE1  1 
ATOM   1687 N  NE2  . GLN   A 1 277 ? 20.945 18.879  -4.947  1.00 86.88  ? 298 GLN   A NE2  1 
ATOM   1688 N  N    . SER   A 1 278 ? 19.160 24.667  -4.510  1.00 93.96  ? 299 SER   A N    1 
ATOM   1689 C  CA   . SER   A 1 278 ? 18.763 26.035  -4.198  1.00 96.26  ? 299 SER   A CA   1 
ATOM   1690 C  C    . SER   A 1 278 ? 17.579 26.056  -3.243  1.00 90.48  ? 299 SER   A C    1 
ATOM   1691 O  O    . SER   A 1 278 ? 17.506 26.911  -2.352  1.00 93.98  ? 299 SER   A O    1 
ATOM   1692 C  CB   . SER   A 1 278 ? 18.436 26.788  -5.486  1.00 99.14  ? 299 SER   A CB   1 
ATOM   1693 O  OG   . SER   A 1 278 ? 19.546 26.781  -6.366  1.00 96.25  ? 299 SER   A OG   1 
ATOM   1694 N  N    . ILE   A 1 279 ? 16.644 25.118  -3.408  1.00 80.81  ? 300 ILE   A N    1 
ATOM   1695 C  CA   . ILE   A 1 279 ? 15.528 25.012  -2.476  1.00 81.66  ? 300 ILE   A CA   1 
ATOM   1696 C  C    . ILE   A 1 279 ? 16.030 24.630  -1.092  1.00 84.41  ? 300 ILE   A C    1 
ATOM   1697 O  O    . ILE   A 1 279 ? 15.475 25.067  -0.076  1.00 83.11  ? 300 ILE   A O    1 
ATOM   1698 C  CB   . ILE   A 1 279 ? 14.491 24.007  -3.010  1.00 81.86  ? 300 ILE   A CB   1 
ATOM   1699 C  CG1  . ILE   A 1 279 ? 14.074 24.388  -4.431  1.00 85.32  ? 300 ILE   A CG1  1 
ATOM   1700 C  CG2  . ILE   A 1 279 ? 13.277 23.960  -2.102  1.00 80.38  ? 300 ILE   A CG2  1 
ATOM   1701 C  CD1  . ILE   A 1 279 ? 13.243 23.336  -5.132  1.00 90.61  ? 300 ILE   A CD1  1 
ATOM   1702 N  N    . ILE   A 1 280 ? 17.089 23.820  -1.025  1.00 84.05  ? 301 ILE   A N    1 
ATOM   1703 C  CA   . ILE   A 1 280 ? 17.707 23.511  0.260   1.00 82.99  ? 301 ILE   A CA   1 
ATOM   1704 C  C    . ILE   A 1 280 ? 18.270 24.776  0.887   1.00 87.17  ? 301 ILE   A C    1 
ATOM   1705 O  O    . ILE   A 1 280 ? 17.974 25.105  2.041   1.00 90.77  ? 301 ILE   A O    1 
ATOM   1706 C  CB   . ILE   A 1 280 ? 18.798 22.440  0.090   1.00 81.27  ? 301 ILE   A CB   1 
ATOM   1707 C  CG1  . ILE   A 1 280 ? 18.194 21.162  -0.479  1.00 83.69  ? 301 ILE   A CG1  1 
ATOM   1708 C  CG2  . ILE   A 1 280 ? 19.479 22.167  1.418   1.00 84.02  ? 301 ILE   A CG2  1 
ATOM   1709 C  CD1  . ILE   A 1 280 ? 17.099 20.592  0.375   1.00 81.73  ? 301 ILE   A CD1  1 
ATOM   1710 N  N    . PHE   A 1 281 ? 19.089 25.508  0.128   1.00 88.57  ? 302 PHE   A N    1 
ATOM   1711 C  CA   . PHE   A 1 281 ? 19.646 26.759  0.629   1.00 92.25  ? 302 PHE   A CA   1 
ATOM   1712 C  C    . PHE   A 1 281 ? 18.553 27.757  0.979   1.00 90.80  ? 302 PHE   A C    1 
ATOM   1713 O  O    . PHE   A 1 281 ? 18.729 28.577  1.887   1.00 91.93  ? 302 PHE   A O    1 
ATOM   1714 C  CB   . PHE   A 1 281 ? 20.596 27.363  -0.405  1.00 93.05  ? 302 PHE   A CB   1 
ATOM   1715 C  CG   . PHE   A 1 281 ? 21.752 26.475  -0.763  1.00 95.75  ? 302 PHE   A CG   1 
ATOM   1716 C  CD1  . PHE   A 1 281 ? 22.235 25.541  0.140   1.00 95.43  ? 302 PHE   A CD1  1 
ATOM   1717 C  CD2  . PHE   A 1 281 ? 22.357 26.575  -2.005  1.00 92.46  ? 302 PHE   A CD2  1 
ATOM   1718 C  CE1  . PHE   A 1 281 ? 23.299 24.725  -0.191  1.00 94.80  ? 302 PHE   A CE1  1 
ATOM   1719 C  CE2  . PHE   A 1 281 ? 23.421 25.763  -2.341  1.00 89.26  ? 302 PHE   A CE2  1 
ATOM   1720 C  CZ   . PHE   A 1 281 ? 23.893 24.837  -1.433  1.00 95.22  ? 302 PHE   A CZ   1 
ATOM   1721 N  N    . ILE   A 1 282 ? 17.420 27.699  0.278   1.00 87.22  ? 303 ILE   A N    1 
ATOM   1722 C  CA   . ILE   A 1 282 ? 16.328 28.631  0.543   1.00 89.40  ? 303 ILE   A CA   1 
ATOM   1723 C  C    . ILE   A 1 282 ? 15.731 28.372  1.921   1.00 95.80  ? 303 ILE   A C    1 
ATOM   1724 O  O    . ILE   A 1 282 ? 15.725 29.251  2.790   1.00 100.50 ? 303 ILE   A O    1 
ATOM   1725 C  CB   . ILE   A 1 282 ? 15.258 28.534  -0.557  1.00 85.38  ? 303 ILE   A CB   1 
ATOM   1726 N  N    . PHE   A 1 283 ? 15.221 27.159  2.141   1.00 95.18  ? 304 PHE   A N    1 
ATOM   1727 C  CA   . PHE   A 1 283 ? 14.539 26.879  3.399   1.00 99.75  ? 304 PHE   A CA   1 
ATOM   1728 C  C    . PHE   A 1 283 ? 15.507 26.832  4.571   1.00 99.00  ? 304 PHE   A C    1 
ATOM   1729 O  O    . PHE   A 1 283 ? 15.148 27.234  5.685   1.00 102.07 ? 304 PHE   A O    1 
ATOM   1730 C  CB   . PHE   A 1 283 ? 13.766 25.566  3.311   1.00 103.68 ? 304 PHE   A CB   1 
ATOM   1731 C  CG   . PHE   A 1 283 ? 13.182 25.128  4.624   1.00 109.93 ? 304 PHE   A CG   1 
ATOM   1732 C  CD1  . PHE   A 1 283 ? 12.174 25.860  5.227   1.00 112.03 ? 304 PHE   A CD1  1 
ATOM   1733 C  CD2  . PHE   A 1 283 ? 13.647 23.991  5.259   1.00 107.53 ? 304 PHE   A CD2  1 
ATOM   1734 C  CE1  . PHE   A 1 283 ? 11.638 25.461  6.439   1.00 114.72 ? 304 PHE   A CE1  1 
ATOM   1735 C  CE2  . PHE   A 1 283 ? 13.117 23.585  6.469   1.00 109.19 ? 304 PHE   A CE2  1 
ATOM   1736 C  CZ   . PHE   A 1 283 ? 12.111 24.321  7.060   1.00 112.91 ? 304 PHE   A CZ   1 
ATOM   1737 N  N    . ALA   A 1 284 ? 16.730 26.349  4.349   1.00 93.85  ? 305 ALA   A N    1 
ATOM   1738 C  CA   . ALA   A 1 284 ? 17.686 26.248  5.444   1.00 94.29  ? 305 ALA   A CA   1 
ATOM   1739 C  C    . ALA   A 1 284 ? 18.075 27.612  5.997   1.00 93.02  ? 305 ALA   A C    1 
ATOM   1740 O  O    . ALA   A 1 284 ? 18.600 27.688  7.112   1.00 92.16  ? 305 ALA   A O    1 
ATOM   1741 C  CB   . ALA   A 1 284 ? 18.930 25.487  4.990   1.00 93.08  ? 305 ALA   A CB   1 
ATOM   1742 N  N    . GLY   A 1 285 ? 17.827 28.688  5.250   1.00 96.25  ? 306 GLY   A N    1 
ATOM   1743 C  CA   . GLY   A 1 285 ? 18.074 30.034  5.727   1.00 98.16  ? 306 GLY   A CA   1 
ATOM   1744 C  C    . GLY   A 1 285 ? 16.838 30.845  6.036   1.00 104.58 ? 306 GLY   A C    1 
ATOM   1745 O  O    . GLY   A 1 285 ? 16.952 32.062  6.240   1.00 104.47 ? 306 GLY   A O    1 
ATOM   1746 N  N    . TYR   A 1 286 ? 15.654 30.226  6.082   1.00 106.80 ? 307 TYR   A N    1 
ATOM   1747 C  CA   . TYR   A 1 286 ? 14.417 30.952  6.326   1.00 109.79 ? 307 TYR   A CA   1 
ATOM   1748 C  C    . TYR   A 1 286 ? 13.904 30.566  7.687   1.00 103.41 ? 307 TYR   A C    1 
ATOM   1749 O  O    . TYR   A 1 286 ? 14.256 31.217  8.696   1.00 99.79  ? 307 TYR   A O    1 
ATOM   1750 C  CB   . TYR   A 1 286 ? 13.414 30.682  5.191   1.00 111.94 ? 307 TYR   A CB   1 
ATOM   1751 C  CG   . TYR   A 1 286 ? 12.083 31.385  5.360   1.00 120.93 ? 307 TYR   A CG   1 
ATOM   1752 C  CD1  . TYR   A 1 286 ? 11.938 32.727  5.032   1.00 122.39 ? 307 TYR   A CD1  1 
ATOM   1753 C  CD2  . TYR   A 1 286 ? 10.968 30.705  5.837   1.00 120.35 ? 307 TYR   A CD2  1 
ATOM   1754 C  CE1  . TYR   A 1 286 ? 10.723 33.372  5.183   1.00 126.07 ? 307 TYR   A CE1  1 
ATOM   1755 C  CE2  . TYR   A 1 286 ? 9.751  31.342  5.992   1.00 120.53 ? 307 TYR   A CE2  1 
ATOM   1756 C  CZ   . TYR   A 1 286 ? 9.634  32.675  5.663   1.00 128.13 ? 307 TYR   A CZ   1 
ATOM   1757 O  OH   . TYR   A 1 286 ? 8.423  33.312  5.814   1.00 137.67 ? 307 TYR   A OH   1 
ATOM   1758 N  N    . GLU   A 1 287 ? 13.068 29.525  7.814   1.00 99.93  ? 308 GLU   A N    1 
ATOM   1759 C  CA   . GLU   A 1 287 ? 12.527 29.144  9.113   1.00 99.38  ? 308 GLU   A CA   1 
ATOM   1760 C  C    . GLU   A 1 287 ? 13.639 28.761  10.080  1.00 96.48  ? 308 GLU   A C    1 
ATOM   1761 O  O    . GLU   A 1 287 ? 13.556 29.048  11.280  1.00 98.21  ? 308 GLU   A O    1 
ATOM   1762 C  CB   . GLU   A 1 287 ? 11.533 27.992  8.948   1.00 101.21 ? 308 GLU   A CB   1 
ATOM   1763 C  CG   . GLU   A 1 287 ? 11.176 27.255  10.236  1.00 104.45 ? 308 GLU   A CG   1 
ATOM   1764 C  CD   . GLU   A 1 287 ? 9.868  27.724  10.851  1.00 104.29 ? 308 GLU   A CD   1 
ATOM   1765 O  OE1  . GLU   A 1 287 ? 9.411  28.836  10.514  1.00 103.30 ? 308 GLU   A OE1  1 
ATOM   1766 O  OE2  . GLU   A 1 287 ? 9.295  26.973  11.670  1.00 106.69 ? 308 GLU   A OE2  1 
ATOM   1767 N  N    . THR   A 1 288 ? 14.694 28.124  9.572   1.00 97.53  ? 309 THR   A N    1 
ATOM   1768 C  CA   . THR   A 1 288 ? 15.819 27.750  10.423  1.00 96.53  ? 309 THR   A CA   1 
ATOM   1769 C  C    . THR   A 1 288 ? 16.491 28.984  11.015  1.00 96.66  ? 309 THR   A C    1 
ATOM   1770 O  O    . THR   A 1 288 ? 16.756 29.043  12.221  1.00 96.70  ? 309 THR   A O    1 
ATOM   1771 C  CB   . THR   A 1 288 ? 16.818 26.917  9.620   1.00 94.76  ? 309 THR   A CB   1 
ATOM   1772 O  OG1  . THR   A 1 288 ? 16.257 25.627  9.346   1.00 93.95  ? 309 THR   A OG1  1 
ATOM   1773 C  CG2  . THR   A 1 288 ? 18.120 26.753  10.381  1.00 87.32  ? 309 THR   A CG2  1 
ATOM   1774 N  N    . THR   A 1 289 ? 16.765 29.987  10.178  1.00 96.27  ? 310 THR   A N    1 
ATOM   1775 C  CA   . THR   A 1 289 ? 17.379 31.215  10.676  1.00 94.67  ? 310 THR   A CA   1 
ATOM   1776 C  C    . THR   A 1 289 ? 16.408 32.007  11.542  1.00 99.03  ? 310 THR   A C    1 
ATOM   1777 O  O    . THR   A 1 289 ? 16.785 32.508  12.608  1.00 98.61  ? 310 THR   A O    1 
ATOM   1778 C  CB   . THR   A 1 289 ? 17.869 32.069  9.508   1.00 96.57  ? 310 THR   A CB   1 
ATOM   1779 O  OG1  . THR   A 1 289 ? 18.887 31.362  8.789   1.00 95.41  ? 310 THR   A OG1  1 
ATOM   1780 C  CG2  . THR   A 1 289 ? 18.433 33.388  10.012  1.00 100.75 ? 310 THR   A CG2  1 
ATOM   1781 N  N    . SER   A 1 290 ? 15.152 32.128  11.103  1.00 99.17  ? 311 SER   A N    1 
ATOM   1782 C  CA   . SER   A 1 290 ? 14.176 32.897  11.866  1.00 95.79  ? 311 SER   A CA   1 
ATOM   1783 C  C    . SER   A 1 290 ? 13.887 32.257  13.215  1.00 95.59  ? 311 SER   A C    1 
ATOM   1784 O  O    . SER   A 1 290 ? 13.625 32.967  14.193  1.00 99.41  ? 311 SER   A O    1 
ATOM   1785 C  CB   . SER   A 1 290 ? 12.881 33.048  11.068  1.00 99.94  ? 311 SER   A CB   1 
ATOM   1786 O  OG   . SER   A 1 290 ? 12.139 31.840  11.073  1.00 100.66 ? 311 SER   A OG   1 
ATOM   1787 N  N    . SER   A 1 291 ? 13.925 30.924  13.291  1.00 95.69  ? 312 SER   A N    1 
ATOM   1788 C  CA   . SER   A 1 291 ? 13.687 30.251  14.564  1.00 99.67  ? 312 SER   A CA   1 
ATOM   1789 C  C    . SER   A 1 291 ? 14.775 30.594  15.573  1.00 104.21 ? 312 SER   A C    1 
ATOM   1790 O  O    . SER   A 1 291 ? 14.483 30.957  16.718  1.00 109.43 ? 312 SER   A O    1 
ATOM   1791 C  CB   . SER   A 1 291 ? 13.606 28.737  14.359  1.00 101.22 ? 312 SER   A CB   1 
ATOM   1792 O  OG   . SER   A 1 291 ? 12.541 28.389  13.491  1.00 106.65 ? 312 SER   A OG   1 
ATOM   1793 N  N    . VAL   A 1 292 ? 16.040 30.493  15.159  1.00 101.44 ? 313 VAL   A N    1 
ATOM   1794 C  CA   . VAL   A 1 292 ? 17.143 30.765  16.075  1.00 103.33 ? 313 VAL   A CA   1 
ATOM   1795 C  C    . VAL   A 1 292 ? 17.170 32.239  16.462  1.00 104.28 ? 313 VAL   A C    1 
ATOM   1796 O  O    . VAL   A 1 292 ? 17.440 32.586  17.618  1.00 103.88 ? 313 VAL   A O    1 
ATOM   1797 C  CB   . VAL   A 1 292 ? 18.476 30.317  15.452  1.00 95.31  ? 313 VAL   A CB   1 
ATOM   1798 C  CG1  . VAL   A 1 292 ? 19.620 30.548  16.426  1.00 98.36  ? 313 VAL   A CG1  1 
ATOM   1799 C  CG2  . VAL   A 1 292 ? 18.400 28.857  15.053  1.00 95.87  ? 313 VAL   A CG2  1 
ATOM   1800 N  N    . LEU   A 1 293 ? 16.887 33.128  15.507  1.00 99.88  ? 314 LEU   A N    1 
ATOM   1801 C  CA   . LEU   A 1 293 ? 16.851 34.553  15.818  1.00 96.75  ? 314 LEU   A CA   1 
ATOM   1802 C  C    . LEU   A 1 293 ? 15.780 34.875  16.851  1.00 99.56  ? 314 LEU   A C    1 
ATOM   1803 O  O    . LEU   A 1 293 ? 15.967 35.773  17.678  1.00 98.97  ? 314 LEU   A O    1 
ATOM   1804 C  CB   . LEU   A 1 293 ? 16.625 35.363  14.543  1.00 97.25  ? 314 LEU   A CB   1 
ATOM   1805 C  CG   . LEU   A 1 293 ? 17.828 35.433  13.604  1.00 97.72  ? 314 LEU   A CG   1 
ATOM   1806 C  CD1  . LEU   A 1 293 ? 17.503 36.261  12.373  1.00 99.99  ? 314 LEU   A CD1  1 
ATOM   1807 C  CD2  . LEU   A 1 293 ? 19.028 36.006  14.340  1.00 101.00 ? 314 LEU   A CD2  1 
ATOM   1808 N  N    . SER   A 1 294 ? 14.660 34.150  16.827  1.00 99.41  ? 315 SER   A N    1 
ATOM   1809 C  CA   . SER   A 1 294 ? 13.612 34.384  17.816  1.00 101.11 ? 315 SER   A CA   1 
ATOM   1810 C  C    . SER   A 1 294 ? 14.006 33.832  19.182  1.00 101.00 ? 315 SER   A C    1 
ATOM   1811 O  O    . SER   A 1 294 ? 13.712 34.449  20.212  1.00 106.32 ? 315 SER   A O    1 
ATOM   1812 C  CB   . SER   A 1 294 ? 12.296 33.768  17.342  1.00 102.00 ? 315 SER   A CB   1 
ATOM   1813 O  OG   . SER   A 1 294 ? 11.861 34.363  16.130  1.00 102.57 ? 315 SER   A OG   1 
ATOM   1814 N  N    . PHE   A 1 295 ? 14.670 32.672  19.212  1.00 98.21  ? 316 PHE   A N    1 
ATOM   1815 C  CA   . PHE   A 1 295 ? 15.122 32.113  20.483  1.00 98.40  ? 316 PHE   A CA   1 
ATOM   1816 C  C    . PHE   A 1 295 ? 16.151 33.011  21.157  1.00 96.70  ? 316 PHE   A C    1 
ATOM   1817 O  O    . PHE   A 1 295 ? 16.195 33.091  22.390  1.00 93.89  ? 316 PHE   A O    1 
ATOM   1818 C  CB   . PHE   A 1 295 ? 15.710 30.716  20.274  1.00 102.04 ? 316 PHE   A CB   1 
ATOM   1819 C  CG   . PHE   A 1 295 ? 14.680 29.628  20.162  1.00 100.66 ? 316 PHE   A CG   1 
ATOM   1820 C  CD1  . PHE   A 1 295 ? 13.889 29.289  21.248  1.00 97.87  ? 316 PHE   A CD1  1 
ATOM   1821 C  CD2  . PHE   A 1 295 ? 14.522 28.926  18.980  1.00 99.51  ? 316 PHE   A CD2  1 
ATOM   1822 C  CE1  . PHE   A 1 295 ? 12.945 28.282  21.149  1.00 97.13  ? 316 PHE   A CE1  1 
ATOM   1823 C  CE2  . PHE   A 1 295 ? 13.582 27.920  18.874  1.00 104.21 ? 316 PHE   A CE2  1 
ATOM   1824 C  CZ   . PHE   A 1 295 ? 12.793 27.596  19.961  1.00 102.23 ? 316 PHE   A CZ   1 
ATOM   1825 N  N    . ILE   A 1 296 ? 16.986 33.688  20.369  1.00 97.04  ? 317 ILE   A N    1 
ATOM   1826 C  CA   . ILE   A 1 296 ? 18.011 34.554  20.940  1.00 97.01  ? 317 ILE   A CA   1 
ATOM   1827 C  C    . ILE   A 1 296 ? 17.372 35.751  21.632  1.00 100.29 ? 317 ILE   A C    1 
ATOM   1828 O  O    . ILE   A 1 296 ? 17.711 36.083  22.773  1.00 100.69 ? 317 ILE   A O    1 
ATOM   1829 C  CB   . ILE   A 1 296 ? 19.004 34.996  19.851  1.00 97.22  ? 317 ILE   A CB   1 
ATOM   1830 C  CG1  . ILE   A 1 296 ? 19.822 33.802  19.359  1.00 96.64  ? 317 ILE   A CG1  1 
ATOM   1831 C  CG2  . ILE   A 1 296 ? 19.918 36.094  20.371  1.00 96.10  ? 317 ILE   A CG2  1 
ATOM   1832 C  CD1  . ILE   A 1 296 ? 20.758 34.134  18.220  1.00 91.48  ? 317 ILE   A CD1  1 
ATOM   1833 N  N    . MET   A 1 297 ? 16.425 36.407  20.955  1.00 103.39 ? 318 MET   A N    1 
ATOM   1834 C  CA   . MET   A 1 297 ? 15.866 37.649  21.480  1.00 104.66 ? 318 MET   A CA   1 
ATOM   1835 C  C    . MET   A 1 297 ? 15.003 37.414  22.713  1.00 102.56 ? 318 MET   A C    1 
ATOM   1836 O  O    . MET   A 1 297 ? 14.917 38.292  23.579  1.00 103.27 ? 318 MET   A O    1 
ATOM   1837 C  CB   . MET   A 1 297 ? 15.061 38.363  20.396  1.00 107.91 ? 318 MET   A CB   1 
ATOM   1838 C  CG   . MET   A 1 297 ? 15.851 38.653  19.132  1.00 107.32 ? 318 MET   A CG   1 
ATOM   1839 S  SD   . MET   A 1 297 ? 17.473 39.368  19.465  1.00 103.28 ? 318 MET   A SD   1 
ATOM   1840 C  CE   . MET   A 1 297 ? 17.024 40.876  20.322  1.00 119.95 ? 318 MET   A CE   1 
ATOM   1841 N  N    . TYR   A 1 298 ? 14.351 36.253  22.809  1.00 101.18 ? 319 TYR   A N    1 
ATOM   1842 C  CA   . TYR   A 1 298 ? 13.599 35.936  24.019  1.00 100.64 ? 319 TYR   A CA   1 
ATOM   1843 C  C    . TYR   A 1 298 ? 14.524 35.861  25.226  1.00 101.34 ? 319 TYR   A C    1 
ATOM   1844 O  O    . TYR   A 1 298 ? 14.250 36.456  26.274  1.00 103.76 ? 319 TYR   A O    1 
ATOM   1845 C  CB   . TYR   A 1 298 ? 12.839 34.622  23.846  1.00 99.21  ? 319 TYR   A CB   1 
ATOM   1846 C  CG   . TYR   A 1 298 ? 12.356 34.037  25.154  1.00 101.10 ? 319 TYR   A CG   1 
ATOM   1847 C  CD1  . TYR   A 1 298 ? 11.181 34.484  25.744  1.00 105.11 ? 319 TYR   A CD1  1 
ATOM   1848 C  CD2  . TYR   A 1 298 ? 13.077 33.041  25.803  1.00 101.08 ? 319 TYR   A CD2  1 
ATOM   1849 C  CE1  . TYR   A 1 298 ? 10.737 33.954  26.940  1.00 110.09 ? 319 TYR   A CE1  1 
ATOM   1850 C  CE2  . TYR   A 1 298 ? 12.643 32.508  27.000  1.00 105.57 ? 319 TYR   A CE2  1 
ATOM   1851 C  CZ   . TYR   A 1 298 ? 11.472 32.968  27.564  1.00 112.82 ? 319 TYR   A CZ   1 
ATOM   1852 O  OH   . TYR   A 1 298 ? 11.035 32.438  28.756  1.00 120.04 ? 319 TYR   A OH   1 
ATOM   1853 N  N    . GLU   A 1 299 ? 15.628 35.122  25.095  1.00 99.24  ? 320 GLU   A N    1 
ATOM   1854 C  CA   . GLU   A 1 299 ? 16.584 35.029  26.191  1.00 101.26 ? 320 GLU   A CA   1 
ATOM   1855 C  C    . GLU   A 1 299 ? 17.248 36.370  26.469  1.00 104.36 ? 320 GLU   A C    1 
ATOM   1856 O  O    . GLU   A 1 299 ? 17.659 36.631  27.604  1.00 106.19 ? 320 GLU   A O    1 
ATOM   1857 C  CB   . GLU   A 1 299 ? 17.633 33.963  25.882  1.00 97.90  ? 320 GLU   A CB   1 
ATOM   1858 C  CG   . GLU   A 1 299 ? 17.072 32.554  25.741  1.00 93.19  ? 320 GLU   A CG   1 
ATOM   1859 C  CD   . GLU   A 1 299 ? 16.673 31.934  27.070  1.00 100.35 ? 320 GLU   A CD   1 
ATOM   1860 O  OE1  . GLU   A 1 299 ? 15.809 32.500  27.773  1.00 105.89 ? 320 GLU   A OE1  1 
ATOM   1861 O  OE2  . GLU   A 1 299 ? 17.232 30.873  27.416  1.00 104.44 ? 320 GLU   A OE2  1 
ATOM   1862 N  N    . LEU   A 1 300 ? 17.360 37.230  25.455  1.00 102.11 ? 321 LEU   A N    1 
ATOM   1863 C  CA   . LEU   A 1 300 ? 17.874 38.574  25.691  1.00 105.00 ? 321 LEU   A CA   1 
ATOM   1864 C  C    . LEU   A 1 300 ? 16.840 39.453  26.382  1.00 111.10 ? 321 LEU   A C    1 
ATOM   1865 O  O    . LEU   A 1 300 ? 17.206 40.374  27.122  1.00 111.99 ? 321 LEU   A O    1 
ATOM   1866 C  CB   . LEU   A 1 300 ? 18.321 39.210  24.375  1.00 107.07 ? 321 LEU   A CB   1 
ATOM   1867 C  CG   . LEU   A 1 300 ? 19.560 38.614  23.704  1.00 102.49 ? 321 LEU   A CG   1 
ATOM   1868 C  CD1  . LEU   A 1 300 ? 19.952 39.436  22.487  1.00 93.59  ? 321 LEU   A CD1  1 
ATOM   1869 C  CD2  . LEU   A 1 300 ? 20.715 38.524  24.689  1.00 107.17 ? 321 LEU   A CD2  1 
ATOM   1870 N  N    . ALA   A 1 301 ? 15.551 39.189  26.156  1.00 110.82 ? 322 ALA   A N    1 
ATOM   1871 C  CA   . ALA   A 1 301 ? 14.508 39.956  26.828  1.00 109.68 ? 322 ALA   A CA   1 
ATOM   1872 C  C    . ALA   A 1 301 ? 14.331 39.506  28.273  1.00 110.97 ? 322 ALA   A C    1 
ATOM   1873 O  O    . ALA   A 1 301 ? 14.101 40.336  29.160  1.00 117.08 ? 322 ALA   A O    1 
ATOM   1874 C  CB   . ALA   A 1 301 ? 13.190 39.835  26.062  1.00 110.64 ? 322 ALA   A CB   1 
ATOM   1875 N  N    . THR   A 1 302 ? 14.439 38.202  28.529  1.00 105.10 ? 323 THR   A N    1 
ATOM   1876 C  CA   . THR   A 1 302 ? 14.336 37.678  29.884  1.00 107.39 ? 323 THR   A CA   1 
ATOM   1877 C  C    . THR   A 1 302 ? 15.637 37.799  30.666  1.00 111.13 ? 323 THR   A C    1 
ATOM   1878 O  O    . THR   A 1 302 ? 15.642 37.523  31.871  1.00 113.81 ? 323 THR   A O    1 
ATOM   1879 C  CB   . THR   A 1 302 ? 13.898 36.213  29.853  1.00 106.91 ? 323 THR   A CB   1 
ATOM   1880 O  OG1  . THR   A 1 302 ? 14.894 35.427  29.186  1.00 104.83 ? 323 THR   A OG1  1 
ATOM   1881 C  CG2  . THR   A 1 302 ? 12.573 36.074  29.122  1.00 102.37 ? 323 THR   A CG2  1 
ATOM   1882 N  N    . HIS   A 1 303 ? 16.730 38.193  30.017  1.00 110.37 ? 324 HIS   A N    1 
ATOM   1883 C  CA   . HIS   A 1 303 ? 18.013 38.419  30.684  1.00 113.12 ? 324 HIS   A CA   1 
ATOM   1884 C  C    . HIS   A 1 303 ? 18.616 39.704  30.135  1.00 112.18 ? 324 HIS   A C    1 
ATOM   1885 O  O    . HIS   A 1 303 ? 19.543 39.677  29.316  1.00 110.44 ? 324 HIS   A O    1 
ATOM   1886 C  CB   . HIS   A 1 303 ? 18.958 37.231  30.485  1.00 108.99 ? 324 HIS   A CB   1 
ATOM   1887 N  N    . PRO   A 1 304 ? 18.114 40.862  30.576  1.00 113.82 ? 325 PRO   A N    1 
ATOM   1888 C  CA   . PRO   A 1 304 ? 18.567 42.132  29.985  1.00 113.75 ? 325 PRO   A CA   1 
ATOM   1889 C  C    . PRO   A 1 304 ? 19.996 42.507  30.340  1.00 111.53 ? 325 PRO   A C    1 
ATOM   1890 O  O    . PRO   A 1 304 ? 20.568 43.379  29.673  1.00 108.71 ? 325 PRO   A O    1 
ATOM   1891 C  CB   . PRO   A 1 304 ? 17.568 43.154  30.541  1.00 112.76 ? 325 PRO   A CB   1 
ATOM   1892 C  CG   . PRO   A 1 304 ? 17.114 42.558  31.830  1.00 111.39 ? 325 PRO   A CG   1 
ATOM   1893 C  CD   . PRO   A 1 304 ? 17.095 41.068  31.621  1.00 109.54 ? 325 PRO   A CD   1 
ATOM   1894 N  N    . ASP   A 1 305 ? 20.590 41.893  31.368  1.00 113.05 ? 326 ASP   A N    1 
ATOM   1895 C  CA   . ASP   A 1 305 ? 21.995 42.155  31.662  1.00 113.99 ? 326 ASP   A CA   1 
ATOM   1896 C  C    . ASP   A 1 305 ? 22.891 41.652  30.536  1.00 110.17 ? 326 ASP   A C    1 
ATOM   1897 O  O    . ASP   A 1 305 ? 23.881 42.304  30.182  1.00 104.82 ? 326 ASP   A O    1 
ATOM   1898 C  CB   . ASP   A 1 305 ? 22.385 41.516  32.997  1.00 108.73 ? 326 ASP   A CB   1 
ATOM   1899 C  CG   . ASP   A 1 305 ? 21.944 40.068  33.104  1.00 109.33 ? 326 ASP   A CG   1 
ATOM   1900 O  OD1  . ASP   A 1 305 ? 20.889 39.722  32.533  1.00 112.27 ? 326 ASP   A OD1  1 
ATOM   1901 O  OD2  . ASP   A 1 305 ? 22.652 39.276  33.762  1.00 107.01 ? 326 ASP   A OD2  1 
ATOM   1902 N  N    . VAL   A 1 306 ? 22.555 40.496  29.959  1.00 108.67 ? 327 VAL   A N    1 
ATOM   1903 C  CA   . VAL   A 1 306 ? 23.266 40.023  28.777  1.00 108.94 ? 327 VAL   A CA   1 
ATOM   1904 C  C    . VAL   A 1 306 ? 22.968 40.926  27.587  1.00 109.25 ? 327 VAL   A C    1 
ATOM   1905 O  O    . VAL   A 1 306 ? 23.854 41.223  26.777  1.00 108.17 ? 327 VAL   A O    1 
ATOM   1906 C  CB   . VAL   A 1 306 ? 22.898 38.557  28.484  1.00 109.23 ? 327 VAL   A CB   1 
ATOM   1907 C  CG1  . VAL   A 1 306 ? 23.699 38.031  27.302  1.00 110.49 ? 327 VAL   A CG1  1 
ATOM   1908 C  CG2  . VAL   A 1 306 ? 23.120 37.696  29.718  1.00 106.36 ? 327 VAL   A CG2  1 
ATOM   1909 N  N    . GLN   A 1 307 ? 21.718 41.382  27.467  1.00 108.00 ? 328 GLN   A N    1 
ATOM   1910 C  CA   . GLN   A 1 307 ? 21.363 42.307  26.396  1.00 104.54 ? 328 GLN   A CA   1 
ATOM   1911 C  C    . GLN   A 1 307 ? 22.102 43.631  26.545  1.00 110.18 ? 328 GLN   A C    1 
ATOM   1912 O  O    . GLN   A 1 307 ? 22.605 44.184  25.560  1.00 112.17 ? 328 GLN   A O    1 
ATOM   1913 C  CB   . GLN   A 1 307 ? 19.851 42.534  26.383  1.00 102.47 ? 328 GLN   A CB   1 
ATOM   1914 C  CG   . GLN   A 1 307 ? 19.369 43.490  25.305  1.00 109.18 ? 328 GLN   A CG   1 
ATOM   1915 C  CD   . GLN   A 1 307 ? 17.858 43.624  25.280  1.00 117.28 ? 328 GLN   A CD   1 
ATOM   1916 O  OE1  . GLN   A 1 307 ? 17.300 44.342  24.449  1.00 121.68 ? 328 GLN   A OE1  1 
ATOM   1917 N  NE2  . GLN   A 1 307 ? 17.186 42.929  26.192  1.00 112.40 ? 328 GLN   A NE2  1 
ATOM   1918 N  N    . GLN   A 1 308 ? 22.183 44.152  27.771  1.00 113.60 ? 329 GLN   A N    1 
ATOM   1919 C  CA   . GLN   A 1 308 ? 22.900 45.402  27.999  1.00 112.42 ? 329 GLN   A CA   1 
ATOM   1920 C  C    . GLN   A 1 308 ? 24.386 45.241  27.704  1.00 110.43 ? 329 GLN   A C    1 
ATOM   1921 O  O    . GLN   A 1 308 ? 24.976 46.048  26.977  1.00 108.08 ? 329 GLN   A O    1 
ATOM   1922 C  CB   . GLN   A 1 308 ? 22.683 45.880  29.436  1.00 114.87 ? 329 GLN   A CB   1 
ATOM   1923 N  N    . LYS   A 1 309 ? 25.006 44.195  28.258  1.00 109.35 ? 330 LYS   A N    1 
ATOM   1924 C  CA   . LYS   A 1 309 ? 26.434 43.983  28.040  1.00 109.66 ? 330 LYS   A CA   1 
ATOM   1925 C  C    . LYS   A 1 309 ? 26.736 43.724  26.568  1.00 108.82 ? 330 LYS   A C    1 
ATOM   1926 O  O    . LYS   A 1 309 ? 27.756 44.189  26.046  1.00 109.27 ? 330 LYS   A O    1 
ATOM   1927 C  CB   . LYS   A 1 309 ? 26.936 42.825  28.902  1.00 106.27 ? 330 LYS   A CB   1 
ATOM   1928 C  CG   . LYS   A 1 309 ? 28.448 42.657  28.869  1.00 107.44 ? 330 LYS   A CG   1 
ATOM   1929 C  CD   . LYS   A 1 309 ? 28.884 41.316  29.438  1.00 108.98 ? 330 LYS   A CD   1 
ATOM   1930 C  CE   . LYS   A 1 309 ? 28.485 41.167  30.895  1.00 115.20 ? 330 LYS   A CE   1 
ATOM   1931 N  NZ   . LYS   A 1 309 ? 28.975 39.881  31.467  1.00 109.83 ? 330 LYS   A NZ   1 
ATOM   1932 N  N    . LEU   A 1 310 ? 25.863 42.983  25.881  1.00 107.31 ? 331 LEU   A N    1 
ATOM   1933 C  CA   . LEU   A 1 310 ? 26.062 42.756  24.453  1.00 109.38 ? 331 LEU   A CA   1 
ATOM   1934 C  C    . LEU   A 1 310 ? 25.863 44.043  23.661  1.00 108.40 ? 331 LEU   A C    1 
ATOM   1935 O  O    . LEU   A 1 310 ? 26.586 44.298  22.691  1.00 106.60 ? 331 LEU   A O    1 
ATOM   1936 C  CB   . LEU   A 1 310 ? 25.121 41.660  23.954  1.00 109.42 ? 331 LEU   A CB   1 
ATOM   1937 C  CG   . LEU   A 1 310 ? 25.220 41.275  22.476  1.00 107.32 ? 331 LEU   A CG   1 
ATOM   1938 C  CD1  . LEU   A 1 310 ? 26.654 40.941  22.099  1.00 103.48 ? 331 LEU   A CD1  1 
ATOM   1939 C  CD2  . LEU   A 1 310 ? 24.299 40.103  22.169  1.00 102.48 ? 331 LEU   A CD2  1 
ATOM   1940 N  N    . GLN   A 1 311 ? 24.886 44.864  24.056  1.00 109.05 ? 332 GLN   A N    1 
ATOM   1941 C  CA   . GLN   A 1 311 ? 24.741 46.182  23.445  1.00 109.29 ? 332 GLN   A CA   1 
ATOM   1942 C  C    . GLN   A 1 311 ? 25.943 47.063  23.757  1.00 109.65 ? 332 GLN   A C    1 
ATOM   1943 O  O    . GLN   A 1 311 ? 26.376 47.856  22.912  1.00 112.26 ? 332 GLN   A O    1 
ATOM   1944 C  CB   . GLN   A 1 311 ? 23.451 46.848  23.921  1.00 111.24 ? 332 GLN   A CB   1 
ATOM   1945 C  CG   . GLN   A 1 311 ? 22.194 46.330  23.244  1.00 113.59 ? 332 GLN   A CG   1 
ATOM   1946 C  CD   . GLN   A 1 311 ? 20.931 46.948  23.811  1.00 120.93 ? 332 GLN   A CD   1 
ATOM   1947 O  OE1  . GLN   A 1 311 ? 20.889 47.346  24.976  1.00 124.83 ? 332 GLN   A OE1  1 
ATOM   1948 N  NE2  . GLN   A 1 311 ? 19.893 47.034  22.987  1.00 117.67 ? 332 GLN   A NE2  1 
ATOM   1949 N  N    . GLU   A 1 312 ? 26.491 46.941  24.968  1.00 108.97 ? 333 GLU   A N    1 
ATOM   1950 C  CA   . GLU   A 1 312 ? 27.710 47.668  25.303  1.00 112.37 ? 333 GLU   A CA   1 
ATOM   1951 C  C    . GLU   A 1 312 ? 28.907 47.110  24.543  1.00 113.00 ? 333 GLU   A C    1 
ATOM   1952 O  O    . GLU   A 1 312 ? 29.781 47.868  24.106  1.00 116.74 ? 333 GLU   A O    1 
ATOM   1953 C  CB   . GLU   A 1 312 ? 27.950 47.618  26.813  1.00 110.04 ? 333 GLU   A CB   1 
ATOM   1954 C  CG   . GLU   A 1 312 ? 26.944 48.422  27.632  1.00 110.31 ? 333 GLU   A CG   1 
ATOM   1955 C  CD   . GLU   A 1 312 ? 26.975 48.073  29.110  1.00 109.52 ? 333 GLU   A CD   1 
ATOM   1956 O  OE1  . GLU   A 1 312 ? 27.789 47.212  29.503  1.00 105.36 ? 333 GLU   A OE1  1 
ATOM   1957 O  OE2  . GLU   A 1 312 ? 26.180 48.658  29.879  1.00 106.58 ? 333 GLU   A OE2  1 
ATOM   1958 N  N    . GLU   A 1 313 ? 28.962 45.786  24.368  1.00 109.27 ? 334 GLU   A N    1 
ATOM   1959 C  CA   . GLU   A 1 313 ? 30.051 45.190  23.602  1.00 107.96 ? 334 GLU   A CA   1 
ATOM   1960 C  C    . GLU   A 1 313 ? 29.901 45.458  22.110  1.00 102.87 ? 334 GLU   A C    1 
ATOM   1961 O  O    . GLU   A 1 313 ? 30.904 45.522  21.391  1.00 99.16  ? 334 GLU   A O    1 
ATOM   1962 C  CB   . GLU   A 1 313 ? 30.122 43.686  23.867  1.00 105.92 ? 334 GLU   A CB   1 
ATOM   1963 N  N    . ILE   A 1 314 ? 28.666 45.612  21.629  1.00 102.02 ? 335 ILE   A N    1 
ATOM   1964 C  CA   . ILE   A 1 314 ? 28.453 45.914  20.217  1.00 105.68 ? 335 ILE   A CA   1 
ATOM   1965 C  C    . ILE   A 1 314 ? 28.981 47.303  19.885  1.00 111.58 ? 335 ILE   A C    1 
ATOM   1966 O  O    . ILE   A 1 314 ? 29.622 47.507  18.847  1.00 114.42 ? 335 ILE   A O    1 
ATOM   1967 C  CB   . ILE   A 1 314 ? 26.963 45.775  19.857  1.00 107.06 ? 335 ILE   A CB   1 
ATOM   1968 N  N    . ASP   A 1 315 ? 28.724 48.278  20.759  1.00 111.73 ? 336 ASP   A N    1 
ATOM   1969 C  CA   . ASP   A 1 315 ? 29.242 49.622  20.546  1.00 109.65 ? 336 ASP   A CA   1 
ATOM   1970 C  C    . ASP   A 1 315 ? 30.741 49.710  20.803  1.00 107.76 ? 336 ASP   A C    1 
ATOM   1971 O  O    . ASP   A 1 315 ? 31.381 50.660  20.341  1.00 109.79 ? 336 ASP   A O    1 
ATOM   1972 C  CB   . ASP   A 1 315 ? 28.498 50.620  21.435  1.00 106.93 ? 336 ASP   A CB   1 
ATOM   1973 N  N    . ALA   A 1 316 ? 31.316 48.739  21.517  1.00 105.66 ? 337 ALA   A N    1 
ATOM   1974 C  CA   . ALA   A 1 316 ? 32.741 48.786  21.830  1.00 107.31 ? 337 ALA   A CA   1 
ATOM   1975 C  C    . ALA   A 1 316 ? 33.587 48.521  20.589  1.00 107.80 ? 337 ALA   A C    1 
ATOM   1976 O  O    . ALA   A 1 316 ? 34.431 49.342  20.210  1.00 101.25 ? 337 ALA   A O    1 
ATOM   1977 C  CB   . ALA   A 1 316 ? 33.067 47.778  22.934  1.00 106.06 ? 337 ALA   A CB   1 
ATOM   1978 N  N    . VAL   A 1 317 ? 33.376 47.372  19.943  1.00 111.70 ? 338 VAL   A N    1 
ATOM   1979 C  CA   . VAL   A 1 317 ? 34.154 47.036  18.754  1.00 114.13 ? 338 VAL   A CA   1 
ATOM   1980 C  C    . VAL   A 1 317 ? 33.793 47.953  17.592  1.00 112.83 ? 338 VAL   A C    1 
ATOM   1981 O  O    . VAL   A 1 317 ? 34.636 48.241  16.733  1.00 102.37 ? 338 VAL   A O    1 
ATOM   1982 C  CB   . VAL   A 1 317 ? 33.950 45.555  18.385  1.00 106.32 ? 338 VAL   A CB   1 
ATOM   1983 N  N    . LEU   A 1 318 ? 32.551 48.423  17.542  1.00 114.32 ? 339 LEU   A N    1 
ATOM   1984 C  CA   . LEU   A 1 318 ? 32.102 49.340  16.504  1.00 113.69 ? 339 LEU   A CA   1 
ATOM   1985 C  C    . LEU   A 1 318 ? 31.132 50.344  17.114  1.00 115.03 ? 339 LEU   A C    1 
ATOM   1986 O  O    . LEU   A 1 318 ? 30.041 49.957  17.552  1.00 115.45 ? 339 LEU   A O    1 
ATOM   1987 C  CB   . LEU   A 1 318 ? 31.441 48.575  15.356  1.00 117.35 ? 339 LEU   A CB   1 
ATOM   1988 N  N    . PRO   A 1 319 ? 31.485 51.629  17.158  1.00 116.99 ? 340 PRO   A N    1 
ATOM   1989 C  CA   . PRO   A 1 319 ? 30.635 52.617  17.838  1.00 119.08 ? 340 PRO   A CA   1 
ATOM   1990 C  C    . PRO   A 1 319 ? 29.251 52.708  17.214  1.00 118.48 ? 340 PRO   A C    1 
ATOM   1991 O  O    . PRO   A 1 319 ? 28.943 52.086  16.195  1.00 117.14 ? 340 PRO   A O    1 
ATOM   1992 C  CB   . PRO   A 1 319 ? 31.411 53.929  17.668  1.00 116.86 ? 340 PRO   A CB   1 
ATOM   1993 C  CG   . PRO   A 1 319 ? 32.826 53.506  17.431  1.00 110.95 ? 340 PRO   A CG   1 
ATOM   1994 C  CD   . PRO   A 1 319 ? 32.733 52.227  16.656  1.00 113.90 ? 340 PRO   A CD   1 
ATOM   1995 N  N    . ASN   A 1 320 ? 28.397 53.501  17.859  1.00 117.56 ? 341 ASN   A N    1 
ATOM   1996 C  CA   . ASN   A 1 320 ? 27.053 53.726  17.344  1.00 121.10 ? 341 ASN   A CA   1 
ATOM   1997 C  C    . ASN   A 1 320 ? 27.124 54.262  15.920  1.00 124.77 ? 341 ASN   A C    1 
ATOM   1998 O  O    . ASN   A 1 320 ? 27.868 55.206  15.635  1.00 123.70 ? 341 ASN   A O    1 
ATOM   1999 C  CB   . ASN   A 1 320 ? 26.295 54.700  18.246  1.00 119.78 ? 341 ASN   A CB   1 
ATOM   2000 N  N    . LYS   A 1 321 ? 26.355 53.634  15.025  1.00 127.43 ? 342 LYS   A N    1 
ATOM   2001 C  CA   . LYS   A 1 321 ? 26.363 53.940  13.591  1.00 126.28 ? 342 LYS   A CA   1 
ATOM   2002 C  C    . LYS   A 1 321 ? 27.716 53.599  12.961  1.00 128.03 ? 342 LYS   A C    1 
ATOM   2003 O  O    . LYS   A 1 321 ? 28.302 54.397  12.228  1.00 126.50 ? 342 LYS   A O    1 
ATOM   2004 C  CB   . LYS   A 1 321 ? 25.980 55.399  13.320  1.00 125.61 ? 342 LYS   A CB   1 
ATOM   2005 N  N    . ALA   A 1 322 ? 28.211 52.400  13.261  1.00 127.07 ? 343 ALA   A N    1 
ATOM   2006 C  CA   . ALA   A 1 322 ? 29.378 51.836  12.592  1.00 125.67 ? 343 ALA   A CA   1 
ATOM   2007 C  C    . ALA   A 1 322 ? 28.961 50.532  11.927  1.00 129.66 ? 343 ALA   A C    1 
ATOM   2008 O  O    . ALA   A 1 322 ? 28.511 49.606  12.624  1.00 129.18 ? 343 ALA   A O    1 
ATOM   2009 C  CB   . ALA   A 1 322 ? 30.531 51.599  13.568  1.00 117.65 ? 343 ALA   A CB   1 
ATOM   2010 N  N    . PRO   A 1 323 ? 29.084 50.407  10.604  1.00 129.67 ? 344 PRO   A N    1 
ATOM   2011 C  CA   . PRO   A 1 323 ? 28.552 49.224  9.934   1.00 132.59 ? 344 PRO   A CA   1 
ATOM   2012 C  C    . PRO   A 1 323 ? 29.373 47.993  10.270  1.00 135.27 ? 344 PRO   A C    1 
ATOM   2013 O  O    . PRO   A 1 323 ? 30.597 48.080  10.472  1.00 134.64 ? 344 PRO   A O    1 
ATOM   2014 C  CB   . PRO   A 1 323 ? 28.664 49.584  8.442   1.00 130.29 ? 344 PRO   A CB   1 
ATOM   2015 C  CG   . PRO   A 1 323 ? 29.785 50.562  8.384   1.00 130.28 ? 344 PRO   A CG   1 
ATOM   2016 C  CD   . PRO   A 1 323 ? 29.705 51.353  9.661   1.00 126.25 ? 344 PRO   A CD   1 
ATOM   2017 N  N    . PRO   A 1 324 ? 28.742 46.825  10.352  1.00 133.85 ? 345 PRO   A N    1 
ATOM   2018 C  CA   . PRO   A 1 324 ? 29.491 45.597  10.637  1.00 132.54 ? 345 PRO   A CA   1 
ATOM   2019 C  C    . PRO   A 1 324 ? 30.354 45.177  9.456   1.00 129.35 ? 345 PRO   A C    1 
ATOM   2020 O  O    . PRO   A 1 324 ? 30.155 45.601  8.315   1.00 130.17 ? 345 PRO   A O    1 
ATOM   2021 C  CB   . PRO   A 1 324 ? 28.393 44.562  10.915  1.00 130.98 ? 345 PRO   A CB   1 
ATOM   2022 C  CG   . PRO   A 1 324 ? 27.151 45.366  11.182  1.00 133.86 ? 345 PRO   A CG   1 
ATOM   2023 C  CD   . PRO   A 1 324 ? 27.289 46.596  10.347  1.00 133.44 ? 345 PRO   A CD   1 
ATOM   2024 N  N    . THR   A 1 325 ? 31.330 44.323  9.753   1.00 126.87 ? 346 THR   A N    1 
ATOM   2025 C  CA   . THR   A 1 325 ? 32.240 43.805  8.742   1.00 126.22 ? 346 THR   A CA   1 
ATOM   2026 C  C    . THR   A 1 325 ? 32.614 42.377  9.115   1.00 123.85 ? 346 THR   A C    1 
ATOM   2027 O  O    . THR   A 1 325 ? 32.498 41.969  10.274  1.00 122.93 ? 346 THR   A O    1 
ATOM   2028 C  CB   . THR   A 1 325 ? 33.495 44.682  8.610   1.00 127.67 ? 346 THR   A CB   1 
ATOM   2029 O  OG1  . THR   A 1 325 ? 33.115 46.063  8.627   1.00 130.77 ? 346 THR   A OG1  1 
ATOM   2030 C  CG2  . THR   A 1 325 ? 34.229 44.395  7.304   1.00 131.03 ? 346 THR   A CG2  1 
ATOM   2031 N  N    . TYR   A 1 326 ? 33.056 41.616  8.109   1.00 125.74 ? 347 TYR   A N    1 
ATOM   2032 C  CA   . TYR   A 1 326 ? 33.458 40.231  8.337   1.00 126.82 ? 347 TYR   A CA   1 
ATOM   2033 C  C    . TYR   A 1 326 ? 34.534 40.132  9.413   1.00 121.12 ? 347 TYR   A C    1 
ATOM   2034 O  O    . TYR   A 1 326 ? 34.558 39.171  10.190  1.00 120.14 ? 347 TYR   A O    1 
ATOM   2035 C  CB   . TYR   A 1 326 ? 33.947 39.610  7.026   1.00 127.14 ? 347 TYR   A CB   1 
ATOM   2036 C  CG   . TYR   A 1 326 ? 34.340 38.152  7.131   1.00 121.66 ? 347 TYR   A CG   1 
ATOM   2037 C  CD1  . TYR   A 1 326 ? 35.632 37.783  7.486   1.00 122.16 ? 347 TYR   A CD1  1 
ATOM   2038 C  CD2  . TYR   A 1 326 ? 33.423 37.144  6.865   1.00 118.44 ? 347 TYR   A CD2  1 
ATOM   2039 C  CE1  . TYR   A 1 326 ? 35.996 36.454  7.583   1.00 121.62 ? 347 TYR   A CE1  1 
ATOM   2040 C  CE2  . TYR   A 1 326 ? 33.778 35.811  6.956   1.00 122.18 ? 347 TYR   A CE2  1 
ATOM   2041 C  CZ   . TYR   A 1 326 ? 35.067 35.472  7.316   1.00 119.94 ? 347 TYR   A CZ   1 
ATOM   2042 O  OH   . TYR   A 1 326 ? 35.427 34.148  7.410   1.00 111.66 ? 347 TYR   A OH   1 
ATOM   2043 N  N    . ASP   A 1 327 ? 35.433 41.116  9.474   1.00 116.89 ? 348 ASP   A N    1 
ATOM   2044 C  CA   . ASP   A 1 327 ? 36.489 41.089  10.477  1.00 118.35 ? 348 ASP   A CA   1 
ATOM   2045 C  C    . ASP   A 1 327 ? 36.003 41.575  11.835  1.00 113.48 ? 348 ASP   A C    1 
ATOM   2046 O  O    . ASP   A 1 327 ? 36.585 41.211  12.862  1.00 107.50 ? 348 ASP   A O    1 
ATOM   2047 C  CB   . ASP   A 1 327 ? 37.675 41.938  10.017  1.00 115.88 ? 348 ASP   A CB   1 
ATOM   2048 N  N    . THR   A 1 328 ? 34.951 42.392  11.865  1.00 112.83 ? 349 THR   A N    1 
ATOM   2049 C  CA   . THR   A 1 328 ? 34.485 42.950  13.128  1.00 115.93 ? 349 THR   A CA   1 
ATOM   2050 C  C    . THR   A 1 328 ? 33.511 42.022  13.839  1.00 112.94 ? 349 THR   A C    1 
ATOM   2051 O  O    . THR   A 1 328 ? 33.487 41.988  15.075  1.00 110.73 ? 349 THR   A O    1 
ATOM   2052 C  CB   . THR   A 1 328 ? 33.826 44.310  12.895  1.00 119.75 ? 349 THR   A CB   1 
ATOM   2053 O  OG1  . THR   A 1 328 ? 32.666 44.146  12.072  1.00 123.61 ? 349 THR   A OG1  1 
ATOM   2054 C  CG2  . THR   A 1 328 ? 34.798 45.259  12.213  1.00 120.35 ? 349 THR   A CG2  1 
ATOM   2055 N  N    . VAL   A 1 329 ? 32.703 41.274  13.085  1.00 111.19 ? 350 VAL   A N    1 
ATOM   2056 C  CA   . VAL   A 1 329 ? 31.722 40.385  13.700  1.00 112.22 ? 350 VAL   A CA   1 
ATOM   2057 C  C    . VAL   A 1 329 ? 32.424 39.304  14.512  1.00 109.86 ? 350 VAL   A C    1 
ATOM   2058 O  O    . VAL   A 1 329 ? 32.042 39.009  15.652  1.00 106.17 ? 350 VAL   A O    1 
ATOM   2059 C  CB   . VAL   A 1 329 ? 30.803 39.779  12.626  1.00 111.41 ? 350 VAL   A CB   1 
ATOM   2060 C  CG1  . VAL   A 1 329 ? 29.921 38.710  13.237  1.00 106.13 ? 350 VAL   A CG1  1 
ATOM   2061 C  CG2  . VAL   A 1 329 ? 29.958 40.866  11.980  1.00 113.92 ? 350 VAL   A CG2  1 
ATOM   2062 N  N    . LEU   A 1 330 ? 33.470 38.705  13.941  1.00 109.44 ? 351 LEU   A N    1 
ATOM   2063 C  CA   . LEU   A 1 330 ? 34.231 37.679  14.642  1.00 106.94 ? 351 LEU   A CA   1 
ATOM   2064 C  C    . LEU   A 1 330 ? 35.034 38.236  15.810  1.00 107.30 ? 351 LEU   A C    1 
ATOM   2065 O  O    . LEU   A 1 330 ? 35.631 37.453  16.557  1.00 109.39 ? 351 LEU   A O    1 
ATOM   2066 C  CB   . LEU   A 1 330 ? 35.164 36.967  13.663  1.00 96.94  ? 351 LEU   A CB   1 
ATOM   2067 N  N    . GLN   A 1 331 ? 35.065 39.556  15.985  1.00 100.13 ? 352 GLN   A N    1 
ATOM   2068 C  CA   . GLN   A 1 331 ? 35.805 40.165  17.081  1.00 97.92  ? 352 GLN   A CA   1 
ATOM   2069 C  C    . GLN   A 1 331 ? 34.970 40.276  18.350  1.00 100.53 ? 352 GLN   A C    1 
ATOM   2070 O  O    . GLN   A 1 331 ? 35.503 40.117  19.453  1.00 98.72  ? 352 GLN   A O    1 
ATOM   2071 C  CB   . GLN   A 1 331 ? 36.317 41.547  16.670  1.00 103.08 ? 352 GLN   A CB   1 
ATOM   2072 N  N    . MET   A 1 332 ? 33.674 40.549  18.217  1.00 100.88 ? 353 MET   A N    1 
ATOM   2073 C  CA   . MET   A 1 332 ? 32.780 40.644  19.370  1.00 98.66  ? 353 MET   A CA   1 
ATOM   2074 C  C    . MET   A 1 332 ? 32.658 39.268  20.012  1.00 98.58  ? 353 MET   A C    1 
ATOM   2075 O  O    . MET   A 1 332 ? 31.899 38.415  19.548  1.00 100.67 ? 353 MET   A O    1 
ATOM   2076 C  CB   . MET   A 1 332 ? 31.419 41.181  18.943  1.00 94.96  ? 353 MET   A CB   1 
ATOM   2077 N  N    . GLU   A 1 333 ? 33.415 39.047  21.091  1.00 101.04 ? 354 GLU   A N    1 
ATOM   2078 C  CA   . GLU   A 1 333 ? 33.456 37.728  21.715  1.00 103.31 ? 354 GLU   A CA   1 
ATOM   2079 C  C    . GLU   A 1 333 ? 32.134 37.368  22.381  1.00 100.53 ? 354 GLU   A C    1 
ATOM   2080 O  O    . GLU   A 1 333 ? 31.744 36.195  22.382  1.00 98.87  ? 354 GLU   A O    1 
ATOM   2081 C  CB   . GLU   A 1 333 ? 34.590 37.674  22.738  1.00 103.19 ? 354 GLU   A CB   1 
ATOM   2082 C  CG   . GLU   A 1 333 ? 35.949 38.007  22.156  1.00 107.41 ? 354 GLU   A CG   1 
ATOM   2083 C  CD   . GLU   A 1 333 ? 36.775 38.875  23.079  1.00 113.09 ? 354 GLU   A CD   1 
ATOM   2084 O  OE1  . GLU   A 1 333 ? 36.841 38.568  24.288  1.00 111.21 ? 354 GLU   A OE1  1 
ATOM   2085 O  OE2  . GLU   A 1 333 ? 37.348 39.872  22.594  1.00 113.37 ? 354 GLU   A OE2  1 
ATOM   2086 N  N    . TYR   A 1 334 ? 31.432 38.352  22.943  1.00 103.15 ? 355 TYR   A N    1 
ATOM   2087 C  CA   . TYR   A 1 334 ? 30.212 38.047  23.682  1.00 102.90 ? 355 TYR   A CA   1 
ATOM   2088 C  C    . TYR   A 1 334 ? 29.069 37.660  22.753  1.00 100.82 ? 355 TYR   A C    1 
ATOM   2089 O  O    . TYR   A 1 334 ? 28.205 36.865  23.138  1.00 102.78 ? 355 TYR   A O    1 
ATOM   2090 C  CB   . TYR   A 1 334 ? 29.817 39.237  24.557  1.00 106.71 ? 355 TYR   A CB   1 
ATOM   2091 C  CG   . TYR   A 1 334 ? 29.058 38.852  25.808  1.00 104.40 ? 355 TYR   A CG   1 
ATOM   2092 C  CD1  . TYR   A 1 334 ? 29.613 37.981  26.736  1.00 104.24 ? 355 TYR   A CD1  1 
ATOM   2093 C  CD2  . TYR   A 1 334 ? 27.796 39.371  26.068  1.00 106.06 ? 355 TYR   A CD2  1 
ATOM   2094 C  CE1  . TYR   A 1 334 ? 28.929 37.628  27.883  1.00 109.72 ? 355 TYR   A CE1  1 
ATOM   2095 C  CE2  . TYR   A 1 334 ? 27.105 39.024  27.214  1.00 109.80 ? 355 TYR   A CE2  1 
ATOM   2096 C  CZ   . TYR   A 1 334 ? 27.676 38.152  28.118  1.00 111.72 ? 355 TYR   A CZ   1 
ATOM   2097 O  OH   . TYR   A 1 334 ? 26.993 37.802  29.260  1.00 108.04 ? 355 TYR   A OH   1 
ATOM   2098 N  N    . LEU   A 1 335 ? 29.041 38.209  21.535  1.00 98.01  ? 356 LEU   A N    1 
ATOM   2099 C  CA   . LEU   A 1 335 ? 27.999 37.832  20.585  1.00 97.16  ? 356 LEU   A CA   1 
ATOM   2100 C  C    . LEU   A 1 335 ? 28.106 36.360  20.211  1.00 97.27  ? 356 LEU   A C    1 
ATOM   2101 O  O    . LEU   A 1 335 ? 27.088 35.680  20.031  1.00 96.04  ? 356 LEU   A O    1 
ATOM   2102 C  CB   . LEU   A 1 335 ? 28.078 38.713  19.338  1.00 99.94  ? 356 LEU   A CB   1 
ATOM   2103 C  CG   . LEU   A 1 335 ? 27.034 38.444  18.251  1.00 95.51  ? 356 LEU   A CG   1 
ATOM   2104 C  CD1  . LEU   A 1 335 ? 25.630 38.514  18.829  1.00 92.73  ? 356 LEU   A CD1  1 
ATOM   2105 C  CD2  . LEU   A 1 335 ? 27.189 39.423  17.095  1.00 94.73  ? 356 LEU   A CD2  1 
ATOM   2106 N  N    . ASP   A 1 336 ? 29.332 35.846  20.093  1.00 98.80  ? 357 ASP   A N    1 
ATOM   2107 C  CA   . ASP   A 1 336 ? 29.503 34.423  19.826  1.00 98.98  ? 357 ASP   A CA   1 
ATOM   2108 C  C    . ASP   A 1 336 ? 29.128 33.581  21.039  1.00 94.66  ? 357 ASP   A C    1 
ATOM   2109 O  O    . ASP   A 1 336 ? 28.686 32.439  20.884  1.00 95.93  ? 357 ASP   A O    1 
ATOM   2110 C  CB   . ASP   A 1 336 ? 30.940 34.133  19.394  1.00 102.50 ? 357 ASP   A CB   1 
ATOM   2111 C  CG   . ASP   A 1 336 ? 31.110 32.731  18.837  1.00 100.59 ? 357 ASP   A CG   1 
ATOM   2112 O  OD1  . ASP   A 1 336 ? 30.525 32.438  17.773  1.00 98.71  ? 357 ASP   A OD1  1 
ATOM   2113 O  OD2  . ASP   A 1 336 ? 31.830 31.924  19.461  1.00 102.46 ? 357 ASP   A OD2  1 
ATOM   2114 N  N    . MET   A 1 337 ? 29.292 34.123  22.249  1.00 94.06  ? 358 MET   A N    1 
ATOM   2115 C  CA   . MET   A 1 337 ? 28.865 33.398  23.441  1.00 91.78  ? 358 MET   A CA   1 
ATOM   2116 C  C    . MET   A 1 337 ? 27.348 33.368  23.563  1.00 88.84  ? 358 MET   A C    1 
ATOM   2117 O  O    . MET   A 1 337 ? 26.788 32.400  24.089  1.00 85.57  ? 358 MET   A O    1 
ATOM   2118 C  CB   . MET   A 1 337 ? 29.473 34.023  24.697  1.00 98.88  ? 358 MET   A CB   1 
ATOM   2119 C  CG   . MET   A 1 337 ? 30.988 34.121  24.693  1.00 102.28 ? 358 MET   A CG   1 
ATOM   2120 S  SD   . MET   A 1 337 ? 31.635 34.760  26.251  1.00 94.89  ? 358 MET   A SD   1 
ATOM   2121 C  CE   . MET   A 1 337 ? 33.316 35.162  25.780  1.00 102.14 ? 358 MET   A CE   1 
ATOM   2122 N  N    . VAL   A 1 338 ? 26.670 34.415  23.088  1.00 93.35  ? 359 VAL   A N    1 
ATOM   2123 C  CA   . VAL   A 1 338 ? 25.217 34.478  23.209  1.00 93.69  ? 359 VAL   A CA   1 
ATOM   2124 C  C    . VAL   A 1 338 ? 24.556 33.505  22.242  1.00 91.86  ? 359 VAL   A C    1 
ATOM   2125 O  O    . VAL   A 1 338 ? 23.584 32.825  22.592  1.00 93.95  ? 359 VAL   A O    1 
ATOM   2126 C  CB   . VAL   A 1 338 ? 24.725 35.919  22.986  1.00 92.20  ? 359 VAL   A CB   1 
ATOM   2127 N  N    . VAL   A 1 339 ? 25.069 33.419  21.012  1.00 87.36  ? 360 VAL   A N    1 
ATOM   2128 C  CA   . VAL   A 1 339 ? 24.476 32.513  20.037  1.00 85.80  ? 360 VAL   A CA   1 
ATOM   2129 C  C    . VAL   A 1 339 ? 24.764 31.061  20.398  1.00 84.25  ? 360 VAL   A C    1 
ATOM   2130 O  O    . VAL   A 1 339 ? 23.958 30.170  20.103  1.00 84.54  ? 360 VAL   A O    1 
ATOM   2131 C  CB   . VAL   A 1 339 ? 24.971 32.855  18.619  1.00 92.23  ? 360 VAL   A CB   1 
ATOM   2132 C  CG1  . VAL   A 1 339 ? 24.503 34.245  18.216  1.00 89.47  ? 360 VAL   A CG1  1 
ATOM   2133 C  CG2  . VAL   A 1 339 ? 26.486 32.760  18.541  1.00 92.63  ? 360 VAL   A CG2  1 
ATOM   2134 N  N    . ASN   A 1 340 ? 25.897 30.795  21.052  1.00 84.91  ? 361 ASN   A N    1 
ATOM   2135 C  CA   . ASN   A 1 340 ? 26.241 29.419  21.396  1.00 81.60  ? 361 ASN   A CA   1 
ATOM   2136 C  C    . ASN   A 1 340 ? 25.328 28.871  22.487  1.00 82.05  ? 361 ASN   A C    1 
ATOM   2137 O  O    . ASN   A 1 340 ? 24.848 27.735  22.388  1.00 81.12  ? 361 ASN   A O    1 
ATOM   2138 C  CB   . ASN   A 1 340 ? 27.705 29.334  21.829  1.00 81.66  ? 361 ASN   A CB   1 
ATOM   2139 C  CG   . ASN   A 1 340 ? 28.666 29.473  20.664  1.00 89.37  ? 361 ASN   A CG   1 
ATOM   2140 O  OD1  . ASN   A 1 340 ? 28.289 29.922  19.581  1.00 92.76  ? 361 ASN   A OD1  1 
ATOM   2141 N  ND2  . ASN   A 1 340 ? 29.920 29.091  20.884  1.00 91.15  ? 361 ASN   A ND2  1 
ATOM   2142 N  N    . GLU   A 1 341 ? 25.074 29.661  23.532  1.00 85.64  ? 362 GLU   A N    1 
ATOM   2143 C  CA   . GLU   A 1 341 ? 24.253 29.179  24.638  1.00 89.26  ? 362 GLU   A CA   1 
ATOM   2144 C  C    . GLU   A 1 341 ? 22.797 29.009  24.219  1.00 89.05  ? 362 GLU   A C    1 
ATOM   2145 O  O    . GLU   A 1 341 ? 22.129 28.062  24.653  1.00 88.41  ? 362 GLU   A O    1 
ATOM   2146 C  CB   . GLU   A 1 341 ? 24.370 30.132  25.829  1.00 92.43  ? 362 GLU   A CB   1 
ATOM   2147 C  CG   . GLU   A 1 341 ? 23.591 29.702  27.068  1.00 91.84  ? 362 GLU   A CG   1 
ATOM   2148 C  CD   . GLU   A 1 341 ? 24.191 28.492  27.765  1.00 88.14  ? 362 GLU   A CD   1 
ATOM   2149 O  OE1  . GLU   A 1 341 ? 25.306 28.070  27.394  1.00 84.65  ? 362 GLU   A OE1  1 
ATOM   2150 O  OE2  . GLU   A 1 341 ? 23.543 27.964  28.693  1.00 93.11  ? 362 GLU   A OE2  1 
ATOM   2151 N  N    . THR   A 1 342 ? 22.287 29.912  23.377  1.00 88.92  ? 363 THR   A N    1 
ATOM   2152 C  CA   . THR   A 1 342 ? 20.918 29.769  22.889  1.00 83.72  ? 363 THR   A CA   1 
ATOM   2153 C  C    . THR   A 1 342 ? 20.771 28.518  22.033  1.00 83.86  ? 363 THR   A C    1 
ATOM   2154 O  O    . THR   A 1 342 ? 19.771 27.797  22.142  1.00 80.37  ? 363 THR   A O    1 
ATOM   2155 C  CB   . THR   A 1 342 ? 20.505 31.011  22.097  1.00 79.13  ? 363 THR   A CB   1 
ATOM   2156 O  OG1  . THR   A 1 342 ? 20.767 32.184  22.875  1.00 92.02  ? 363 THR   A OG1  1 
ATOM   2157 C  CG2  . THR   A 1 342 ? 19.025 30.962  21.769  1.00 78.00  ? 363 THR   A CG2  1 
ATOM   2158 N  N    . LEU   A 1 343 ? 21.760 28.242  21.178  1.00 84.86  ? 364 LEU   A N    1 
ATOM   2159 C  CA   . LEU   A 1 343 ? 21.746 27.005  20.406  1.00 77.12  ? 364 LEU   A CA   1 
ATOM   2160 C  C    . LEU   A 1 343 ? 21.843 25.785  21.308  1.00 76.72  ? 364 LEU   A C    1 
ATOM   2161 O  O    . LEU   A 1 343 ? 21.289 24.729  20.983  1.00 76.41  ? 364 LEU   A O    1 
ATOM   2162 C  CB   . LEU   A 1 343 ? 22.887 27.007  19.390  1.00 72.48  ? 364 LEU   A CB   1 
ATOM   2163 C  CG   . LEU   A 1 343 ? 22.706 27.961  18.212  1.00 70.60  ? 364 LEU   A CG   1 
ATOM   2164 C  CD1  . LEU   A 1 343 ? 23.979 28.036  17.386  1.00 76.97  ? 364 LEU   A CD1  1 
ATOM   2165 C  CD2  . LEU   A 1 343 ? 21.532 27.520  17.357  1.00 76.64  ? 364 LEU   A CD2  1 
ATOM   2166 N  N    . ARG   A 1 344 ? 22.542 25.905  22.438  1.00 80.16  ? 365 ARG   A N    1 
ATOM   2167 C  CA   . ARG   A 1 344 ? 22.578 24.808  23.399  1.00 79.29  ? 365 ARG   A CA   1 
ATOM   2168 C  C    . ARG   A 1 344 ? 21.199 24.570  23.997  1.00 76.75  ? 365 ARG   A C    1 
ATOM   2169 O  O    . ARG   A 1 344 ? 20.687 23.446  23.979  1.00 74.84  ? 365 ARG   A O    1 
ATOM   2170 C  CB   . ARG   A 1 344 ? 23.597 25.099  24.502  1.00 78.56  ? 365 ARG   A CB   1 
ATOM   2171 C  CG   . ARG   A 1 344 ? 23.822 23.931  25.451  1.00 78.99  ? 365 ARG   A CG   1 
ATOM   2172 C  CD   . ARG   A 1 344 ? 24.590 24.355  26.691  1.00 83.10  ? 365 ARG   A CD   1 
ATOM   2173 N  NE   . ARG   A 1 344 ? 23.816 25.265  27.527  1.00 85.27  ? 365 ARG   A NE   1 
ATOM   2174 C  CZ   . ARG   A 1 344 ? 22.984 24.877  28.483  1.00 82.39  ? 365 ARG   A CZ   1 
ATOM   2175 N  NH1  . ARG   A 1 344 ? 22.794 23.596  28.756  1.00 80.71  ? 365 ARG   A NH1  1 
ATOM   2176 N  NH2  . ARG   A 1 344 ? 22.325 25.796  29.184  1.00 88.68  ? 365 ARG   A NH2  1 
ATOM   2177 N  N    . LEU   A 1 345 ? 20.573 25.626  24.522  1.00 80.14  ? 366 LEU   A N    1 
ATOM   2178 C  CA   . LEU   A 1 345 ? 19.254 25.473  25.122  1.00 84.15  ? 366 LEU   A CA   1 
ATOM   2179 C  C    . LEU   A 1 345 ? 18.208 25.071  24.091  1.00 85.73  ? 366 LEU   A C    1 
ATOM   2180 O  O    . LEU   A 1 345 ? 17.195 24.457  24.443  1.00 82.87  ? 366 LEU   A O    1 
ATOM   2181 C  CB   . LEU   A 1 345 ? 18.840 26.769  25.821  1.00 81.81  ? 366 LEU   A CB   1 
ATOM   2182 N  N    . PHE   A 1 346 ? 18.432 25.399  22.819  1.00 84.66  ? 367 PHE   A N    1 
ATOM   2183 C  CA   . PHE   A 1 346 ? 17.471 25.111  21.754  1.00 80.44  ? 367 PHE   A CA   1 
ATOM   2184 C  C    . PHE   A 1 346 ? 18.209 24.673  20.500  1.00 78.32  ? 367 PHE   A C    1 
ATOM   2185 O  O    . PHE   A 1 346 ? 18.368 25.445  19.547  1.00 79.60  ? 367 PHE   A O    1 
ATOM   2186 C  CB   . PHE   A 1 346 ? 16.587 26.328  21.471  1.00 81.93  ? 367 PHE   A CB   1 
ATOM   2187 C  CG   . PHE   A 1 346 ? 15.922 26.885  22.695  1.00 85.51  ? 367 PHE   A CG   1 
ATOM   2188 C  CD1  . PHE   A 1 346 ? 14.863 26.218  23.286  1.00 92.10  ? 367 PHE   A CD1  1 
ATOM   2189 C  CD2  . PHE   A 1 346 ? 16.362 28.069  23.260  1.00 85.99  ? 367 PHE   A CD2  1 
ATOM   2190 C  CE1  . PHE   A 1 346 ? 14.251 26.722  24.418  1.00 94.53  ? 367 PHE   A CE1  1 
ATOM   2191 C  CE2  . PHE   A 1 346 ? 15.753 28.582  24.390  1.00 93.32  ? 367 PHE   A CE2  1 
ATOM   2192 C  CZ   . PHE   A 1 346 ? 14.696 27.907  24.970  1.00 94.07  ? 367 PHE   A CZ   1 
ATOM   2193 N  N    . PRO   A 1 347 ? 18.678 23.424  20.461  1.00 77.32  ? 368 PRO   A N    1 
ATOM   2194 C  CA   . PRO   A 1 347 ? 19.244 22.899  19.212  1.00 74.96  ? 368 PRO   A CA   1 
ATOM   2195 C  C    . PRO   A 1 347 ? 18.154 22.446  18.252  1.00 75.08  ? 368 PRO   A C    1 
ATOM   2196 O  O    . PRO   A 1 347 ? 17.690 21.306  18.333  1.00 77.39  ? 368 PRO   A O    1 
ATOM   2197 C  CB   . PRO   A 1 347 ? 20.104 21.724  19.685  1.00 74.48  ? 368 PRO   A CB   1 
ATOM   2198 C  CG   . PRO   A 1 347 ? 19.428 21.250  20.930  1.00 70.67  ? 368 PRO   A CG   1 
ATOM   2199 C  CD   . PRO   A 1 347 ? 18.770 22.451  21.565  1.00 76.07  ? 368 PRO   A CD   1 
ATOM   2200 N  N    . ILE   A 1 348 ? 17.751 23.323  17.330  1.00 78.78  ? 369 ILE   A N    1 
ATOM   2201 C  CA   . ILE   A 1 348 ? 16.599 23.088  16.465  1.00 83.16  ? 369 ILE   A CA   1 
ATOM   2202 C  C    . ILE   A 1 348 ? 16.646 21.751  15.729  1.00 75.33  ? 369 ILE   A C    1 
ATOM   2203 O  O    . ILE   A 1 348 ? 15.599 21.270  15.289  1.00 77.30  ? 369 ILE   A O    1 
ATOM   2204 C  CB   . ILE   A 1 348 ? 16.436 24.268  15.483  1.00 80.51  ? 369 ILE   A CB   1 
ATOM   2205 C  CG1  . ILE   A 1 348 ? 17.708 24.439  14.659  1.00 82.87  ? 369 ILE   A CG1  1 
ATOM   2206 C  CG2  . ILE   A 1 348 ? 16.112 25.548  16.229  1.00 80.06  ? 369 ILE   A CG2  1 
ATOM   2207 C  CD1  . ILE   A 1 348 ? 17.644 25.585  13.706  1.00 83.16  ? 369 ILE   A CD1  1 
ATOM   2208 N  N    . ALA   A 1 349 ? 17.817 21.124  15.667  1.00 74.92  ? 370 ALA   A N    1 
ATOM   2209 C  CA   . ALA   A 1 349 ? 17.889 19.774  15.063  1.00 76.28  ? 370 ALA   A CA   1 
ATOM   2210 C  C    . ALA   A 1 349 ? 17.243 18.751  15.994  1.00 79.29  ? 370 ALA   A C    1 
ATOM   2211 O  O    . ALA   A 1 349 ? 16.465 17.911  15.503  1.00 82.86  ? 370 ALA   A O    1 
ATOM   2212 C  CB   . ALA   A 1 349 ? 19.323 19.424  14.780  1.00 73.06  ? 370 ALA   A CB   1 
ATOM   2213 N  N    . MET   A 1 350 ? 17.568 18.811  17.286  1.00 73.64  ? 371 MET   A N    1 
ATOM   2214 C  CA   . MET   A 1 350 ? 16.951 17.905  18.285  1.00 68.02  ? 371 MET   A CA   1 
ATOM   2215 C  C    . MET   A 1 350 ? 17.519 16.493  18.148  1.00 66.44  ? 371 MET   A C    1 
ATOM   2216 O  O    . MET   A 1 350 ? 17.348 15.718  19.102  1.00 75.10  ? 371 MET   A O    1 
ATOM   2217 C  CB   . MET   A 1 350 ? 15.436 17.832  18.088  1.00 72.46  ? 371 MET   A CB   1 
ATOM   2218 C  CG   . MET   A 1 350 ? 14.679 18.967  18.736  1.00 84.32  ? 371 MET   A CG   1 
ATOM   2219 S  SD   . MET   A 1 350 ? 12.992 19.069  18.111  1.00 102.80 ? 371 MET   A SD   1 
ATOM   2220 C  CE   . MET   A 1 350 ? 13.332 19.034  16.346  1.00 93.91  ? 371 MET   A CE   1 
ATOM   2221 N  N    . ARG   A 1 351 ? 18.180 16.182  17.033  1.00 71.66  ? 372 ARG   A N    1 
ATOM   2222 C  CA   . ARG   A 1 351 ? 18.665 14.829  16.797  1.00 68.33  ? 372 ARG   A CA   1 
ATOM   2223 C  C    . ARG   A 1 351 ? 19.611 14.835  15.605  1.00 71.55  ? 372 ARG   A C    1 
ATOM   2224 O  O    . ARG   A 1 351 ? 19.448 15.624  14.671  1.00 69.72  ? 372 ARG   A O    1 
ATOM   2225 C  CB   . ARG   A 1 351 ? 17.507 13.854  16.538  1.00 68.79  ? 372 ARG   A CB   1 
ATOM   2226 C  CG   . ARG   A 1 351 ? 17.023 13.110  17.769  1.00 64.36  ? 372 ARG   A CG   1 
ATOM   2227 C  CD   . ARG   A 1 351 ? 15.751 12.339  17.475  1.00 74.25  ? 372 ARG   A CD   1 
ATOM   2228 N  NE   . ARG   A 1 351 ? 15.291 11.575  18.628  1.00 73.79  ? 372 ARG   A NE   1 
ATOM   2229 C  CZ   . ARG   A 1 351 ? 14.178 10.854  18.648  1.00 78.26  ? 372 ARG   A CZ   1 
ATOM   2230 N  NH1  . ARG   A 1 351 ? 13.380 10.785  17.595  1.00 86.86  ? 372 ARG   A NH1  1 
ATOM   2231 N  NH2  . ARG   A 1 351 ? 13.858 10.186  19.753  1.00 79.65  ? 372 ARG   A NH2  1 
ATOM   2232 N  N    . LEU   A 1 352 ? 20.605 13.951  15.658  1.00 62.42  ? 373 LEU   A N    1 
ATOM   2233 C  CA   . LEU   A 1 352 ? 21.490 13.673  14.536  1.00 52.90  ? 373 LEU   A CA   1 
ATOM   2234 C  C    . LEU   A 1 352 ? 21.434 12.183  14.240  1.00 57.48  ? 373 LEU   A C    1 
ATOM   2235 O  O    . LEU   A 1 352 ? 21.544 11.362  15.156  1.00 59.76  ? 373 LEU   A O    1 
ATOM   2236 C  CB   . LEU   A 1 352 ? 22.927 14.099  14.835  1.00 52.94  ? 373 LEU   A CB   1 
ATOM   2237 C  CG   . LEU   A 1 352 ? 23.138 15.577  15.154  1.00 59.22  ? 373 LEU   A CG   1 
ATOM   2238 C  CD1  . LEU   A 1 352 ? 24.595 15.843  15.494  1.00 66.95  ? 373 LEU   A CD1  1 
ATOM   2239 C  CD2  . LEU   A 1 352 ? 22.686 16.440  13.992  1.00 62.83  ? 373 LEU   A CD2  1 
ATOM   2240 N  N    . GLU   A 1 353 ? 21.262 11.832  12.970  1.00 68.36  ? 374 GLU   A N    1 
ATOM   2241 C  CA   . GLU   A 1 353 ? 21.049 10.444  12.589  1.00 72.48  ? 374 GLU   A CA   1 
ATOM   2242 C  C    . GLU   A 1 353 ? 22.033 10.023  11.507  1.00 67.32  ? 374 GLU   A C    1 
ATOM   2243 O  O    . GLU   A 1 353 ? 22.324 10.787  10.581  1.00 65.94  ? 374 GLU   A O    1 
ATOM   2244 C  CB   . GLU   A 1 353 ? 19.606 10.220  12.113  1.00 78.03  ? 374 GLU   A CB   1 
ATOM   2245 C  CG   . GLU   A 1 353 ? 18.563 10.460  13.199  1.00 76.58  ? 374 GLU   A CG   1 
ATOM   2246 C  CD   . GLU   A 1 353 ? 17.180 9.984   12.803  1.00 92.75  ? 374 GLU   A CD   1 
ATOM   2247 O  OE1  . GLU   A 1 353 ? 16.972 9.681   11.609  1.00 87.32  ? 374 GLU   A OE1  1 
ATOM   2248 O  OE2  . GLU   A 1 353 ? 16.301 9.909   13.690  1.00 92.69  ? 374 GLU   A OE2  1 
ATOM   2249 N  N    . ARG   A 1 354 ? 22.548 8.802   11.647  1.00 62.17  ? 375 ARG   A N    1 
ATOM   2250 C  CA   . ARG   A 1 354 ? 23.426 8.175   10.671  1.00 61.03  ? 375 ARG   A CA   1 
ATOM   2251 C  C    . ARG   A 1 354 ? 23.002 6.723   10.515  1.00 65.93  ? 375 ARG   A C    1 
ATOM   2252 O  O    . ARG   A 1 354 ? 22.717 6.045   11.505  1.00 70.34  ? 375 ARG   A O    1 
ATOM   2253 C  CB   . ARG   A 1 354 ? 24.900 8.244   11.098  1.00 65.14  ? 375 ARG   A CB   1 
ATOM   2254 C  CG   . ARG   A 1 354 ? 25.481 9.648   11.179  1.00 61.96  ? 375 ARG   A CG   1 
ATOM   2255 C  CD   . ARG   A 1 354 ? 25.687 10.247  9.802   1.00 57.62  ? 375 ARG   A CD   1 
ATOM   2256 N  NE   . ARG   A 1 354 ? 26.429 11.500  9.861   1.00 53.51  ? 375 ARG   A NE   1 
ATOM   2257 C  CZ   . ARG   A 1 354 ? 25.873 12.695  10.004  1.00 53.20  ? 375 ARG   A CZ   1 
ATOM   2258 N  NH1  . ARG   A 1 354 ? 24.562 12.838  10.113  1.00 49.87  ? 375 ARG   A NH1  1 
ATOM   2259 N  NH2  . ARG   A 1 354 ? 26.651 13.774  10.040  1.00 57.11  ? 375 ARG   A NH2  1 
ATOM   2260 N  N    . VAL   A 1 355 ? 22.961 6.250   9.275   1.00 73.44  ? 376 VAL   A N    1 
ATOM   2261 C  CA   . VAL   A 1 355 ? 22.530 4.887   8.984   1.00 74.30  ? 376 VAL   A CA   1 
ATOM   2262 C  C    . VAL   A 1 355 ? 23.753 3.979   8.957   1.00 72.05  ? 376 VAL   A C    1 
ATOM   2263 O  O    . VAL   A 1 355 ? 24.703 4.222   8.205   1.00 73.00  ? 376 VAL   A O    1 
ATOM   2264 C  CB   . VAL   A 1 355 ? 21.761 4.818   7.657   1.00 72.16  ? 376 VAL   A CB   1 
ATOM   2265 C  CG1  . VAL   A 1 355 ? 21.468 3.372   7.293   1.00 78.67  ? 376 VAL   A CG1  1 
ATOM   2266 C  CG2  . VAL   A 1 355 ? 20.469 5.615   7.756   1.00 69.47  ? 376 VAL   A CG2  1 
ATOM   2267 N  N    . CYS   A 1 356 ? 23.729 2.936   9.783   1.00 74.02  ? 377 CYS   A N    1 
ATOM   2268 C  CA   . CYS   A 1 356 ? 24.801 1.944   9.821   1.00 78.80  ? 377 CYS   A CA   1 
ATOM   2269 C  C    . CYS   A 1 356 ? 24.603 0.992   8.649   1.00 76.62  ? 377 CYS   A C    1 
ATOM   2270 O  O    . CYS   A 1 356 ? 23.833 0.034   8.733   1.00 80.62  ? 377 CYS   A O    1 
ATOM   2271 C  CB   . CYS   A 1 356 ? 24.798 1.203   11.153  1.00 79.80  ? 377 CYS   A CB   1 
ATOM   2272 S  SG   . CYS   A 1 356 ? 26.200 0.092   11.395  1.00 84.69  ? 377 CYS   A SG   1 
ATOM   2273 N  N    . LYS   A 1 357 ? 25.299 1.257   7.547   1.00 75.47  ? 378 LYS   A N    1 
ATOM   2274 C  CA   . LYS   A 1 357 ? 25.118 0.517   6.306   1.00 76.56  ? 378 LYS   A CA   1 
ATOM   2275 C  C    . LYS   A 1 357 ? 26.034 -0.696  6.192   1.00 76.57  ? 378 LYS   A C    1 
ATOM   2276 O  O    . LYS   A 1 357 ? 26.109 -1.300  5.118   1.00 73.32  ? 378 LYS   A O    1 
ATOM   2277 C  CB   . LYS   A 1 357 ? 25.335 1.447   5.111   1.00 74.62  ? 378 LYS   A CB   1 
ATOM   2278 C  CG   . LYS   A 1 357 ? 26.643 2.218   5.169   1.00 75.16  ? 378 LYS   A CG   1 
ATOM   2279 C  CD   . LYS   A 1 357 ? 26.784 3.164   3.990   1.00 71.75  ? 378 LYS   A CD   1 
ATOM   2280 C  CE   . LYS   A 1 357 ? 28.157 3.807   3.976   1.00 75.40  ? 378 LYS   A CE   1 
ATOM   2281 N  NZ   . LYS   A 1 357 ? 29.239 2.785   3.935   1.00 80.81  ? 378 LYS   A NZ   1 
ATOM   2282 N  N    . LYS   A 1 358 ? 26.725 -1.065  7.267   1.00 80.63  ? 379 LYS   A N    1 
ATOM   2283 C  CA   . LYS   A 1 358 ? 27.595 -2.231  7.251   1.00 85.06  ? 379 LYS   A CA   1 
ATOM   2284 C  C    . LYS   A 1 358 ? 27.855 -2.660  8.686   1.00 84.62  ? 379 LYS   A C    1 
ATOM   2285 O  O    . LYS   A 1 358 ? 27.912 -1.826  9.593   1.00 85.45  ? 379 LYS   A O    1 
ATOM   2286 C  CB   . LYS   A 1 358 ? 28.917 -1.942  6.529   1.00 82.36  ? 379 LYS   A CB   1 
ATOM   2287 N  N    . ASP   A 1 359 ? 28.004 -3.968  8.879   1.00 85.03  ? 380 ASP   A N    1 
ATOM   2288 C  CA   . ASP   A 1 359 ? 28.306 -4.501  10.201  1.00 90.43  ? 380 ASP   A CA   1 
ATOM   2289 C  C    . ASP   A 1 359 ? 29.620 -3.925  10.710  1.00 93.83  ? 380 ASP   A C    1 
ATOM   2290 O  O    . ASP   A 1 359 ? 30.657 -4.042  10.050  1.00 92.55  ? 380 ASP   A O    1 
ATOM   2291 C  CB   . ASP   A 1 359 ? 28.370 -6.026  10.146  1.00 90.07  ? 380 ASP   A CB   1 
ATOM   2292 C  CG   . ASP   A 1 359 ? 27.010 -6.656  9.937   1.00 89.49  ? 380 ASP   A CG   1 
ATOM   2293 O  OD1  . ASP   A 1 359 ? 26.105 -6.400  10.759  1.00 91.47  ? 380 ASP   A OD1  1 
ATOM   2294 O  OD2  . ASP   A 1 359 ? 26.840 -7.396  8.945   1.00 89.50  ? 380 ASP   A OD2  1 
ATOM   2295 N  N    . VAL   A 1 360 ? 29.571 -3.294  11.879  1.00 96.10  ? 381 VAL   A N    1 
ATOM   2296 C  CA   . VAL   A 1 360 ? 30.736 -2.618  12.437  1.00 96.90  ? 381 VAL   A CA   1 
ATOM   2297 C  C    . VAL   A 1 360 ? 30.676 -2.711  13.953  1.00 97.17  ? 381 VAL   A C    1 
ATOM   2298 O  O    . VAL   A 1 360 ? 29.600 -2.628  14.554  1.00 94.50  ? 381 VAL   A O    1 
ATOM   2299 C  CB   . VAL   A 1 360 ? 30.812 -1.147  11.975  1.00 88.01  ? 381 VAL   A CB   1 
ATOM   2300 N  N    . GLU   A 1 361 ? 31.841 -2.888  14.568  1.00 99.12  ? 382 GLU   A N    1 
ATOM   2301 C  CA   . GLU   A 1 361 ? 31.991 -2.867  16.017  1.00 98.92  ? 382 GLU   A CA   1 
ATOM   2302 C  C    . GLU   A 1 361 ? 32.678 -1.557  16.382  1.00 100.73 ? 382 GLU   A C    1 
ATOM   2303 O  O    . GLU   A 1 361 ? 33.883 -1.398  16.159  1.00 99.41  ? 382 GLU   A O    1 
ATOM   2304 C  CB   . GLU   A 1 361 ? 32.790 -4.072  16.508  1.00 99.80  ? 382 GLU   A CB   1 
ATOM   2305 N  N    . ILE   A 1 362 ? 31.911 -0.620  16.930  1.00 97.95  ? 383 ILE   A N    1 
ATOM   2306 C  CA   . ILE   A 1 362 ? 32.393 0.721   17.234  1.00 97.37  ? 383 ILE   A CA   1 
ATOM   2307 C  C    . ILE   A 1 362 ? 32.498 0.850   18.747  1.00 99.70  ? 383 ILE   A C    1 
ATOM   2308 O  O    . ILE   A 1 362 ? 31.483 0.809   19.455  1.00 100.50 ? 383 ILE   A O    1 
ATOM   2309 C  CB   . ILE   A 1 362 ? 31.477 1.802   16.644  1.00 92.99  ? 383 ILE   A CB   1 
ATOM   2310 N  N    . ASN   A 1 363 ? 33.730 1.003   19.240  1.00 100.25 ? 384 ASN   A N    1 
ATOM   2311 C  CA   . ASN   A 1 363 ? 34.007 1.244   20.658  1.00 105.71 ? 384 ASN   A CA   1 
ATOM   2312 C  C    . ASN   A 1 363 ? 33.409 0.148   21.542  1.00 108.17 ? 384 ASN   A C    1 
ATOM   2313 O  O    . ASN   A 1 363 ? 32.724 0.417   22.531  1.00 111.03 ? 384 ASN   A O    1 
ATOM   2314 C  CB   . ASN   A 1 363 ? 33.508 2.627   21.086  1.00 102.54 ? 384 ASN   A CB   1 
ATOM   2315 C  CG   . ASN   A 1 363 ? 34.145 3.749   20.289  1.00 98.60  ? 384 ASN   A CG   1 
ATOM   2316 O  OD1  . ASN   A 1 363 ? 35.217 4.245   20.639  1.00 101.38 ? 384 ASN   A OD1  1 
ATOM   2317 N  ND2  . ASN   A 1 363 ? 33.486 4.159   19.211  1.00 93.21  ? 384 ASN   A ND2  1 
ATOM   2318 N  N    . GLY   A 1 364 ? 33.681 -1.101  21.177  1.00 105.69 ? 385 GLY   A N    1 
ATOM   2319 C  CA   . GLY   A 1 364 ? 33.184 -2.228  21.948  1.00 111.04 ? 385 GLY   A CA   1 
ATOM   2320 C  C    . GLY   A 1 364 ? 31.680 -2.395  21.906  1.00 114.89 ? 385 GLY   A C    1 
ATOM   2321 O  O    . GLY   A 1 364 ? 31.060 -2.665  22.943  1.00 113.46 ? 385 GLY   A O    1 
ATOM   2322 N  N    . MET   A 1 365 ? 31.076 -2.241  20.730  1.00 109.50 ? 386 MET   A N    1 
ATOM   2323 C  CA   . MET   A 1 365 ? 29.632 -2.389  20.583  1.00 103.60 ? 386 MET   A CA   1 
ATOM   2324 C  C    . MET   A 1 365 ? 29.333 -2.776  19.146  1.00 98.85  ? 386 MET   A C    1 
ATOM   2325 O  O    . MET   A 1 365 ? 29.737 -2.070  18.216  1.00 99.12  ? 386 MET   A O    1 
ATOM   2326 C  CB   . MET   A 1 365 ? 28.905 -1.098  20.958  1.00 98.40  ? 386 MET   A CB   1 
ATOM   2327 C  CG   . MET   A 1 365 ? 27.394 -1.195  20.870  1.00 100.49 ? 386 MET   A CG   1 
ATOM   2328 S  SD   . MET   A 1 365 ? 26.578 0.237   21.597  1.00 109.37 ? 386 MET   A SD   1 
ATOM   2329 C  CE   . MET   A 1 365 ? 27.102 0.091   23.305  1.00 95.05  ? 386 MET   A CE   1 
ATOM   2330 N  N    . PHE   A 1 366 ? 28.632 -3.891  18.965  1.00 95.24  ? 387 PHE   A N    1 
ATOM   2331 C  CA   . PHE   A 1 366 ? 28.299 -4.367  17.630  1.00 94.73  ? 387 PHE   A CA   1 
ATOM   2332 C  C    . PHE   A 1 366 ? 27.069 -3.635  17.111  1.00 94.57  ? 387 PHE   A C    1 
ATOM   2333 O  O    . PHE   A 1 366 ? 26.015 -3.639  17.756  1.00 97.30  ? 387 PHE   A O    1 
ATOM   2334 C  CB   . PHE   A 1 366 ? 28.058 -5.873  17.643  1.00 90.55  ? 387 PHE   A CB   1 
ATOM   2335 C  CG   . PHE   A 1 366 ? 27.497 -6.400  16.358  1.00 89.47  ? 387 PHE   A CG   1 
ATOM   2336 C  CD1  . PHE   A 1 366 ? 28.238 -6.342  15.189  1.00 96.41  ? 387 PHE   A CD1  1 
ATOM   2337 C  CD2  . PHE   A 1 366 ? 26.229 -6.953  16.315  1.00 92.85  ? 387 PHE   A CD2  1 
ATOM   2338 C  CE1  . PHE   A 1 366 ? 27.725 -6.825  14.001  1.00 95.85  ? 387 PHE   A CE1  1 
ATOM   2339 C  CE2  . PHE   A 1 366 ? 25.710 -7.441  15.130  1.00 96.87  ? 387 PHE   A CE2  1 
ATOM   2340 C  CZ   . PHE   A 1 366 ? 26.459 -7.377  13.971  1.00 95.08  ? 387 PHE   A CZ   1 
ATOM   2341 N  N    . ILE   A 1 367 ? 27.203 -3.013  15.946  1.00 93.85  ? 388 ILE   A N    1 
ATOM   2342 C  CA   . ILE   A 1 367 ? 26.119 -2.278  15.306  1.00 92.91  ? 388 ILE   A CA   1 
ATOM   2343 C  C    . ILE   A 1 367 ? 25.765 -3.011  14.014  1.00 93.24  ? 388 ILE   A C    1 
ATOM   2344 O  O    . ILE   A 1 367 ? 26.542 -2.970  13.047  1.00 89.74  ? 388 ILE   A O    1 
ATOM   2345 C  CB   . ILE   A 1 367 ? 26.505 -0.820  15.029  1.00 93.27  ? 388 ILE   A CB   1 
ATOM   2346 C  CG1  . ILE   A 1 367 ? 27.325 -0.250  16.188  1.00 91.50  ? 388 ILE   A CG1  1 
ATOM   2347 C  CG2  . ILE   A 1 367 ? 25.258 0.019   14.811  1.00 90.31  ? 388 ILE   A CG2  1 
ATOM   2348 C  CD1  . ILE   A 1 367 ? 26.564 -0.162  17.486  1.00 92.76  ? 388 ILE   A CD1  1 
ATOM   2349 N  N    . PRO   A 1 368 ? 24.625 -3.691  13.946  1.00 90.91  ? 389 PRO   A N    1 
ATOM   2350 C  CA   . PRO   A 1 368 ? 24.250 -4.390  12.712  1.00 83.71  ? 389 PRO   A CA   1 
ATOM   2351 C  C    . PRO   A 1 368 ? 23.860 -3.410  11.615  1.00 83.88  ? 389 PRO   A C    1 
ATOM   2352 O  O    . PRO   A 1 368 ? 23.661 -2.214  11.839  1.00 87.11  ? 389 PRO   A O    1 
ATOM   2353 C  CB   . PRO   A 1 368 ? 23.066 -5.261  13.138  1.00 87.36  ? 389 PRO   A CB   1 
ATOM   2354 C  CG   . PRO   A 1 368 ? 22.500 -4.570  14.333  1.00 91.32  ? 389 PRO   A CG   1 
ATOM   2355 C  CD   . PRO   A 1 368 ? 23.656 -3.913  15.033  1.00 91.20  ? 389 PRO   A CD   1 
ATOM   2356 N  N    . LYS   A 1 369 ? 23.750 -3.948  10.403  1.00 85.72  ? 390 LYS   A N    1 
ATOM   2357 C  CA   . LYS   A 1 369 ? 23.463 -3.128  9.234   1.00 81.85  ? 390 LYS   A CA   1 
ATOM   2358 C  C    . LYS   A 1 369 ? 22.010 -2.667  9.229   1.00 79.91  ? 390 LYS   A C    1 
ATOM   2359 O  O    . LYS   A 1 369 ? 21.116 -3.337  9.753   1.00 84.28  ? 390 LYS   A O    1 
ATOM   2360 C  CB   . LYS   A 1 369 ? 23.766 -3.902  7.952   1.00 77.28  ? 390 LYS   A CB   1 
ATOM   2361 N  N    . GLY   A 1 370 ? 21.781 -1.502  8.622   1.00 75.30  ? 391 GLY   A N    1 
ATOM   2362 C  CA   . GLY   A 1 370 ? 20.455 -0.933  8.511   1.00 75.22  ? 391 GLY   A CA   1 
ATOM   2363 C  C    . GLY   A 1 370 ? 19.933 -0.254  9.757   1.00 77.28  ? 391 GLY   A C    1 
ATOM   2364 O  O    . GLY   A 1 370 ? 18.872 0.381   9.696   1.00 79.50  ? 391 GLY   A O    1 
ATOM   2365 N  N    . VAL   A 1 371 ? 20.636 -0.358  10.880  1.00 76.84  ? 392 VAL   A N    1 
ATOM   2366 C  CA   . VAL   A 1 371 ? 20.171 0.227   12.133  1.00 75.30  ? 392 VAL   A CA   1 
ATOM   2367 C  C    . VAL   A 1 371 ? 20.436 1.725   12.116  1.00 78.68  ? 392 VAL   A C    1 
ATOM   2368 O  O    . VAL   A 1 371 ? 21.540 2.171   11.782  1.00 77.97  ? 392 VAL   A O    1 
ATOM   2369 C  CB   . VAL   A 1 371 ? 20.856 -0.446  13.333  1.00 72.40  ? 392 VAL   A CB   1 
ATOM   2370 C  CG1  . VAL   A 1 371 ? 20.583 0.335   14.609  1.00 73.33  ? 392 VAL   A CG1  1 
ATOM   2371 C  CG2  . VAL   A 1 371 ? 20.370 -1.873  13.474  1.00 79.46  ? 392 VAL   A CG2  1 
ATOM   2372 N  N    . VAL   A 1 372 ? 19.419 2.505   12.469  1.00 77.59  ? 393 VAL   A N    1 
ATOM   2373 C  CA   . VAL   A 1 372 ? 19.566 3.951   12.593  1.00 71.96  ? 393 VAL   A CA   1 
ATOM   2374 C  C    . VAL   A 1 372 ? 20.231 4.257   13.929  1.00 69.96  ? 393 VAL   A C    1 
ATOM   2375 O  O    . VAL   A 1 372 ? 19.733 3.858   14.987  1.00 67.95  ? 393 VAL   A O    1 
ATOM   2376 C  CB   . VAL   A 1 372 ? 18.208 4.658   12.477  1.00 75.45  ? 393 VAL   A CB   1 
ATOM   2377 C  CG1  . VAL   A 1 372 ? 18.352 6.137   12.798  1.00 75.23  ? 393 VAL   A CG1  1 
ATOM   2378 C  CG2  . VAL   A 1 372 ? 17.627 4.467   11.084  1.00 83.67  ? 393 VAL   A CG2  1 
ATOM   2379 N  N    . VAL   A 1 373 ? 21.363 4.952   13.881  1.00 68.35  ? 394 VAL   A N    1 
ATOM   2380 C  CA   . VAL   A 1 373 ? 22.085 5.371   15.076  1.00 63.70  ? 394 VAL   A CA   1 
ATOM   2381 C  C    . VAL   A 1 373 ? 21.744 6.831   15.339  1.00 64.35  ? 394 VAL   A C    1 
ATOM   2382 O  O    . VAL   A 1 373 ? 21.924 7.687   14.465  1.00 59.82  ? 394 VAL   A O    1 
ATOM   2383 C  CB   . VAL   A 1 373 ? 23.600 5.171   14.918  1.00 63.00  ? 394 VAL   A CB   1 
ATOM   2384 C  CG1  . VAL   A 1 373 ? 24.324 5.599   16.185  1.00 74.22  ? 394 VAL   A CG1  1 
ATOM   2385 C  CG2  . VAL   A 1 373 ? 23.909 3.720   14.588  1.00 66.05  ? 394 VAL   A CG2  1 
ATOM   2386 N  N    . MET   A 1 374 ? 21.254 7.118   16.542  1.00 68.58  ? 395 MET   A N    1 
ATOM   2387 C  CA   . MET   A 1 374 ? 20.729 8.431   16.883  1.00 65.37  ? 395 MET   A CA   1 
ATOM   2388 C  C    . MET   A 1 374 ? 21.633 9.115   17.899  1.00 56.07  ? 395 MET   A C    1 
ATOM   2389 O  O    . MET   A 1 374 ? 22.188 8.464   18.789  1.00 64.43  ? 395 MET   A O    1 
ATOM   2390 C  CB   . MET   A 1 374 ? 19.304 8.315   17.436  1.00 60.70  ? 395 MET   A CB   1 
ATOM   2391 C  CG   . MET   A 1 374 ? 18.575 9.638   17.583  1.00 64.65  ? 395 MET   A CG   1 
ATOM   2392 S  SD   . MET   A 1 374 ? 18.729 10.344  19.231  1.00 69.29  ? 395 MET   A SD   1 
ATOM   2393 C  CE   . MET   A 1 374 ? 17.772 9.177   20.199  1.00 69.89  ? 395 MET   A CE   1 
ATOM   2394 N  N    . ILE   A 1 375 ? 21.787 10.427  17.750  1.00 50.78  ? 396 ILE   A N    1 
ATOM   2395 C  CA   . ILE   A 1 375 ? 22.553 11.239  18.691  1.00 56.84  ? 396 ILE   A CA   1 
ATOM   2396 C  C    . ILE   A 1 375 ? 21.645 12.351  19.201  1.00 60.18  ? 396 ILE   A C    1 
ATOM   2397 O  O    . ILE   A 1 375 ? 21.337 13.293  18.454  1.00 54.72  ? 396 ILE   A O    1 
ATOM   2398 C  CB   . ILE   A 1 375 ? 23.825 11.809  18.044  1.00 55.39  ? 396 ILE   A CB   1 
ATOM   2399 C  CG1  . ILE   A 1 375 ? 24.737 10.678  17.567  1.00 51.07  ? 396 ILE   A CG1  1 
ATOM   2400 C  CG2  . ILE   A 1 375 ? 24.561 12.708  19.026  1.00 61.50  ? 396 ILE   A CG2  1 
ATOM   2401 C  CD1  . ILE   A 1 375 ? 25.954 11.161  16.813  1.00 56.22  ? 396 ILE   A CD1  1 
ATOM   2402 N  N    . PRO   A 1 376 ? 21.186 12.281  20.454  1.00 64.24  ? 397 PRO   A N    1 
ATOM   2403 C  CA   . PRO   A 1 376 ? 20.249 13.296  20.954  1.00 60.40  ? 397 PRO   A CA   1 
ATOM   2404 C  C    . PRO   A 1 376 ? 20.944 14.595  21.321  1.00 58.89  ? 397 PRO   A C    1 
ATOM   2405 O  O    . PRO   A 1 376 ? 21.558 14.705  22.386  1.00 62.04  ? 397 PRO   A O    1 
ATOM   2406 C  CB   . PRO   A 1 376 ? 19.623 12.619  22.178  1.00 54.07  ? 397 PRO   A CB   1 
ATOM   2407 C  CG   . PRO   A 1 376 ? 20.670 11.671  22.652  1.00 53.85  ? 397 PRO   A CG   1 
ATOM   2408 C  CD   . PRO   A 1 376 ? 21.434 11.214  21.440  1.00 56.67  ? 397 PRO   A CD   1 
ATOM   2409 N  N    . SER   A 1 377 ? 20.853 15.588  20.435  1.00 66.70  ? 398 SER   A N    1 
ATOM   2410 C  CA   . SER   A 1 377 ? 21.493 16.872  20.699  1.00 64.33  ? 398 SER   A CA   1 
ATOM   2411 C  C    . SER   A 1 377 ? 20.816 17.599  21.852  1.00 64.93  ? 398 SER   A C    1 
ATOM   2412 O  O    . SER   A 1 377 ? 21.494 18.201  22.693  1.00 65.97  ? 398 SER   A O    1 
ATOM   2413 C  CB   . SER   A 1 377 ? 21.480 17.734  19.436  1.00 69.28  ? 398 SER   A CB   1 
ATOM   2414 O  OG   . SER   A 1 377 ? 22.251 17.142  18.404  1.00 62.57  ? 398 SER   A OG   1 
ATOM   2415 N  N    . TYR   A 1 378 ? 19.483 17.549  21.913  1.00 65.72  ? 399 TYR   A N    1 
ATOM   2416 C  CA   . TYR   A 1 378 ? 18.758 18.245  22.973  1.00 68.93  ? 399 TYR   A CA   1 
ATOM   2417 C  C    . TYR   A 1 378 ? 19.109 17.680  24.344  1.00 69.09  ? 399 TYR   A C    1 
ATOM   2418 O  O    . TYR   A 1 378 ? 19.363 18.432  25.292  1.00 70.69  ? 399 TYR   A O    1 
ATOM   2419 C  CB   . TYR   A 1 378 ? 17.251 18.154  22.718  1.00 67.60  ? 399 TYR   A CB   1 
ATOM   2420 C  CG   . TYR   A 1 378 ? 16.395 18.916  23.711  1.00 79.75  ? 399 TYR   A CG   1 
ATOM   2421 C  CD1  . TYR   A 1 378 ? 16.053 18.360  24.940  1.00 79.98  ? 399 TYR   A CD1  1 
ATOM   2422 C  CD2  . TYR   A 1 378 ? 15.916 20.187  23.413  1.00 85.96  ? 399 TYR   A CD2  1 
ATOM   2423 C  CE1  . TYR   A 1 378 ? 15.268 19.050  25.845  1.00 79.00  ? 399 TYR   A CE1  1 
ATOM   2424 C  CE2  . TYR   A 1 378 ? 15.128 20.884  24.314  1.00 84.79  ? 399 TYR   A CE2  1 
ATOM   2425 C  CZ   . TYR   A 1 378 ? 14.809 20.309  25.527  1.00 82.74  ? 399 TYR   A CZ   1 
ATOM   2426 O  OH   . TYR   A 1 378 ? 14.026 20.993  26.428  1.00 86.90  ? 399 TYR   A OH   1 
ATOM   2427 N  N    . ALA   A 1 379 ? 19.119 16.351  24.470  1.00 67.11  ? 400 ALA   A N    1 
ATOM   2428 C  CA   . ALA   A 1 379 ? 19.391 15.734  25.764  1.00 63.16  ? 400 ALA   A CA   1 
ATOM   2429 C  C    . ALA   A 1 379 ? 20.811 16.026  26.229  1.00 68.89  ? 400 ALA   A C    1 
ATOM   2430 O  O    . ALA   A 1 379 ? 21.034 16.345  27.403  1.00 79.44  ? 400 ALA   A O    1 
ATOM   2431 C  CB   . ALA   A 1 379 ? 19.149 14.228  25.690  1.00 63.40  ? 400 ALA   A CB   1 
ATOM   2432 N  N    . LEU   A 1 380 ? 21.785 15.924  25.322  1.00 66.41  ? 401 LEU   A N    1 
ATOM   2433 C  CA   . LEU   A 1 380 ? 23.169 16.199  25.694  1.00 69.52  ? 401 LEU   A CA   1 
ATOM   2434 C  C    . LEU   A 1 380 ? 23.397 17.680  25.966  1.00 72.71  ? 401 LEU   A C    1 
ATOM   2435 O  O    . LEU   A 1 380 ? 24.280 18.035  26.756  1.00 75.91  ? 401 LEU   A O    1 
ATOM   2436 C  CB   . LEU   A 1 380 ? 24.115 15.705  24.599  1.00 65.30  ? 401 LEU   A CB   1 
ATOM   2437 N  N    . HIS   A 1 381 ? 22.621 18.558  25.326  1.00 68.50  ? 402 HIS   A N    1 
ATOM   2438 C  CA   . HIS   A 1 381 ? 22.757 19.987  25.581  1.00 69.46  ? 402 HIS   A CA   1 
ATOM   2439 C  C    . HIS   A 1 381 ? 22.173 20.391  26.926  1.00 74.55  ? 402 HIS   A C    1 
ATOM   2440 O  O    . HIS   A 1 381 ? 22.548 21.440  27.459  1.00 82.32  ? 402 HIS   A O    1 
ATOM   2441 C  CB   . HIS   A 1 381 ? 22.088 20.791  24.468  1.00 72.26  ? 402 HIS   A CB   1 
ATOM   2442 C  CG   . HIS   A 1 381 ? 22.857 20.811  23.184  1.00 73.64  ? 402 HIS   A CG   1 
ATOM   2443 N  ND1  . HIS   A 1 381 ? 22.526 21.638  22.132  1.00 66.82  ? 402 HIS   A ND1  1 
ATOM   2444 C  CD2  . HIS   A 1 381 ? 23.939 20.103  22.780  1.00 70.57  ? 402 HIS   A CD2  1 
ATOM   2445 C  CE1  . HIS   A 1 381 ? 23.372 21.440  21.136  1.00 65.77  ? 402 HIS   A CE1  1 
ATOM   2446 N  NE2  . HIS   A 1 381 ? 24.238 20.513  21.504  1.00 65.98  ? 402 HIS   A NE2  1 
ATOM   2447 N  N    . ARG   A 1 382 ? 21.261 19.591  27.479  1.00 76.02  ? 403 ARG   A N    1 
ATOM   2448 C  CA   . ARG   A 1 382 ? 20.693 19.842  28.797  1.00 80.63  ? 403 ARG   A CA   1 
ATOM   2449 C  C    . ARG   A 1 382 ? 21.080 18.761  29.798  1.00 83.17  ? 403 ARG   A C    1 
ATOM   2450 O  O    . ARG   A 1 382 ? 20.379 18.558  30.794  1.00 89.39  ? 403 ARG   A O    1 
ATOM   2451 C  CB   . ARG   A 1 382 ? 19.172 19.974  28.703  1.00 78.62  ? 403 ARG   A CB   1 
ATOM   2452 C  CG   . ARG   A 1 382 ? 18.725 21.040  27.718  1.00 79.69  ? 403 ARG   A CG   1 
ATOM   2453 C  CD   . ARG   A 1 382 ? 17.294 21.481  27.963  1.00 81.86  ? 403 ARG   A CD   1 
ATOM   2454 N  NE   . ARG   A 1 382 ? 16.924 22.585  27.087  1.00 90.59  ? 403 ARG   A NE   1 
ATOM   2455 C  CZ   . ARG   A 1 382 ? 15.821 23.311  27.216  1.00 94.52  ? 403 ARG   A CZ   1 
ATOM   2456 N  NH1  . ARG   A 1 382 ? 14.951 23.080  28.186  1.00 92.75  ? 403 ARG   A NH1  1 
ATOM   2457 N  NH2  . ARG   A 1 382 ? 15.586 24.294  26.350  1.00 92.11  ? 403 ARG   A NH2  1 
ATOM   2458 N  N    . ASP   A 1 383 ? 22.184 18.066  29.549  1.00 83.71  ? 404 ASP   A N    1 
ATOM   2459 C  CA   . ASP   A 1 383 ? 22.675 17.049  30.469  1.00 90.14  ? 404 ASP   A CA   1 
ATOM   2460 C  C    . ASP   A 1 383 ? 23.384 17.720  31.639  1.00 97.53  ? 404 ASP   A C    1 
ATOM   2461 O  O    . ASP   A 1 383 ? 24.309 18.510  31.416  1.00 99.43  ? 404 ASP   A O    1 
ATOM   2462 C  CB   . ASP   A 1 383 ? 23.625 16.100  29.746  1.00 90.26  ? 404 ASP   A CB   1 
ATOM   2463 C  CG   . ASP   A 1 383 ? 24.116 14.965  30.629  1.00 98.01  ? 404 ASP   A CG   1 
ATOM   2464 O  OD1  . ASP   A 1 383 ? 23.534 14.741  31.711  1.00 101.74 ? 404 ASP   A OD1  1 
ATOM   2465 O  OD2  . ASP   A 1 383 ? 25.093 14.292  30.235  1.00 96.28  ? 404 ASP   A OD2  1 
ATOM   2466 N  N    . PRO   A 1 384 ? 22.983 17.453  32.885  1.00 96.06  ? 405 PRO   A N    1 
ATOM   2467 C  CA   . PRO   A 1 384 ? 23.697 18.049  34.027  1.00 98.57  ? 405 PRO   A CA   1 
ATOM   2468 C  C    . PRO   A 1 384 ? 25.147 17.610  34.140  1.00 98.30  ? 405 PRO   A C    1 
ATOM   2469 O  O    . PRO   A 1 384 ? 25.935 18.302  34.797  1.00 101.82 ? 405 PRO   A O    1 
ATOM   2470 C  CB   . PRO   A 1 384 ? 22.877 17.580  35.237  1.00 97.86  ? 405 PRO   A CB   1 
ATOM   2471 C  CG   . PRO   A 1 384 ? 21.519 17.297  34.685  1.00 100.72 ? 405 PRO   A CG   1 
ATOM   2472 C  CD   . PRO   A 1 384 ? 21.751 16.763  33.302  1.00 92.36  ? 405 PRO   A CD   1 
ATOM   2473 N  N    . LYS   A 1 385 ? 25.526 16.489  33.521  1.00 89.57  ? 406 LYS   A N    1 
ATOM   2474 C  CA   . LYS   A 1 385 ? 26.895 16.000  33.652  1.00 92.33  ? 406 LYS   A CA   1 
ATOM   2475 C  C    . LYS   A 1 385 ? 27.891 16.942  32.985  1.00 93.81  ? 406 LYS   A C    1 
ATOM   2476 O  O    . LYS   A 1 385 ? 28.998 17.148  33.498  1.00 91.22  ? 406 LYS   A O    1 
ATOM   2477 C  CB   . LYS   A 1 385 ? 27.008 14.594  33.063  1.00 95.08  ? 406 LYS   A CB   1 
ATOM   2478 N  N    . TYR   A 1 386 ? 27.520 17.522  31.845  1.00 92.29  ? 407 TYR   A N    1 
ATOM   2479 C  CA   . TYR   A 1 386 ? 28.407 18.414  31.111  1.00 88.21  ? 407 TYR   A CA   1 
ATOM   2480 C  C    . TYR   A 1 386 ? 28.082 19.888  31.312  1.00 92.49  ? 407 TYR   A C    1 
ATOM   2481 O  O    . TYR   A 1 386 ? 28.879 20.740  30.904  1.00 92.55  ? 407 TYR   A O    1 
ATOM   2482 C  CB   . TYR   A 1 386 ? 28.368 18.085  29.613  1.00 79.66  ? 407 TYR   A CB   1 
ATOM   2483 N  N    . TRP   A 1 387 ? 26.945 20.211  31.928  1.00 95.16  ? 408 TRP   A N    1 
ATOM   2484 C  CA   . TRP   A 1 387 ? 26.531 21.596  32.118  1.00 97.77  ? 408 TRP   A CA   1 
ATOM   2485 C  C    . TRP   A 1 387 ? 25.961 21.771  33.516  1.00 98.44  ? 408 TRP   A C    1 
ATOM   2486 O  O    . TRP   A 1 387 ? 25.073 21.016  33.925  1.00 94.59  ? 408 TRP   A O    1 
ATOM   2487 C  CB   . TRP   A 1 387 ? 25.486 22.009  31.076  1.00 94.52  ? 408 TRP   A CB   1 
ATOM   2488 C  CG   . TRP   A 1 387 ? 25.797 21.530  29.700  1.00 86.56  ? 408 TRP   A CG   1 
ATOM   2489 C  CD1  . TRP   A 1 387 ? 25.370 20.372  29.121  1.00 87.36  ? 408 TRP   A CD1  1 
ATOM   2490 C  CD2  . TRP   A 1 387 ? 26.613 22.190  28.726  1.00 85.18  ? 408 TRP   A CD2  1 
ATOM   2491 N  NE1  . TRP   A 1 387 ? 25.867 20.270  27.844  1.00 91.76  ? 408 TRP   A NE1  1 
ATOM   2492 C  CE2  . TRP   A 1 387 ? 26.633 21.374  27.577  1.00 88.00  ? 408 TRP   A CE2  1 
ATOM   2493 C  CE3  . TRP   A 1 387 ? 27.328 23.391  28.714  1.00 83.17  ? 408 TRP   A CE3  1 
ATOM   2494 C  CZ2  . TRP   A 1 387 ? 27.338 21.720  26.428  1.00 84.37  ? 408 TRP   A CZ2  1 
ATOM   2495 C  CZ3  . TRP   A 1 387 ? 28.026 23.734  27.572  1.00 88.14  ? 408 TRP   A CZ3  1 
ATOM   2496 C  CH2  . TRP   A 1 387 ? 28.027 22.902  26.445  1.00 89.89  ? 408 TRP   A CH2  1 
ATOM   2497 N  N    . THR   A 1 388 ? 26.464 22.768  34.239  1.00 99.98  ? 409 THR   A N    1 
ATOM   2498 C  CA   . THR   A 1 388 ? 25.952 23.100  35.561  1.00 103.92 ? 409 THR   A CA   1 
ATOM   2499 C  C    . THR   A 1 388 ? 24.795 24.082  35.424  1.00 98.00  ? 409 THR   A C    1 
ATOM   2500 O  O    . THR   A 1 388 ? 24.921 25.105  34.743  1.00 93.64  ? 409 THR   A O    1 
ATOM   2501 C  CB   . THR   A 1 388 ? 27.052 23.696  36.439  1.00 104.48 ? 409 THR   A CB   1 
ATOM   2502 N  N    . GLU   A 1 389 ? 23.673 23.767  36.079  1.00 94.93  ? 410 GLU   A N    1 
ATOM   2503 C  CA   . GLU   A 1 389 ? 22.439 24.539  35.975  1.00 92.53  ? 410 GLU   A CA   1 
ATOM   2504 C  C    . GLU   A 1 389 ? 22.074 24.702  34.506  1.00 92.83  ? 410 GLU   A C    1 
ATOM   2505 O  O    . GLU   A 1 389 ? 22.133 25.814  33.965  1.00 95.13  ? 410 GLU   A O    1 
ATOM   2506 C  CB   . GLU   A 1 389 ? 22.583 25.900  36.659  1.00 96.50  ? 410 GLU   A CB   1 
ATOM   2507 N  N    . PRO   A 1 390 ? 21.692 23.617  33.827  1.00 97.98  ? 411 PRO   A N    1 
ATOM   2508 C  CA   . PRO   A 1 390 ? 21.540 23.703  32.367  1.00 92.80  ? 411 PRO   A CA   1 
ATOM   2509 C  C    . PRO   A 1 390 ? 20.335 24.513  31.931  1.00 88.66  ? 411 PRO   A C    1 
ATOM   2510 O  O    . PRO   A 1 390 ? 20.433 25.274  30.960  1.00 91.13  ? 411 PRO   A O    1 
ATOM   2511 C  CB   . PRO   A 1 390 ? 21.426 22.232  31.948  1.00 92.47  ? 411 PRO   A CB   1 
ATOM   2512 C  CG   . PRO   A 1 390 ? 20.810 21.561  33.135  1.00 96.67  ? 411 PRO   A CG   1 
ATOM   2513 C  CD   . PRO   A 1 390 ? 21.352 22.280  34.348  1.00 98.75  ? 411 PRO   A CD   1 
ATOM   2514 N  N    . GLU   A 1 391 ? 19.184 24.262  32.550  1.00 86.81  ? 412 GLU   A N    1 
ATOM   2515 C  CA   . GLU   A 1 391 ? 17.945 24.946  32.107  1.00 86.24  ? 412 GLU   A CA   1 
ATOM   2516 C  C    . GLU   A 1 391 ? 18.148 26.456  32.260  1.00 87.18  ? 412 GLU   A C    1 
ATOM   2517 O  O    . GLU   A 1 391 ? 17.243 27.223  31.876  1.00 85.89  ? 412 GLU   A O    1 
ATOM   2518 C  CB   . GLU   A 1 391 ? 16.755 24.464  32.931  1.00 84.64  ? 412 GLU   A CB   1 
ATOM   2519 C  CG   . GLU   A 1 391 ? 16.748 22.953  33.134  1.00 91.07  ? 412 GLU   A CG   1 
ATOM   2520 C  CD   . GLU   A 1 391 ? 16.631 22.172  31.839  1.00 93.82  ? 412 GLU   A CD   1 
ATOM   2521 O  OE1  . GLU   A 1 391 ? 15.599 22.314  31.151  1.00 94.51  ? 412 GLU   A OE1  1 
ATOM   2522 O  OE2  . GLU   A 1 391 ? 17.576 21.422  31.521  1.00 93.44  ? 412 GLU   A OE2  1 
ATOM   2523 N  N    . LYS   A 1 392 ? 19.292 26.856  32.808  1.00 90.42  ? 413 LYS   A N    1 
ATOM   2524 C  CA   . LYS   A 1 392 ? 19.525 28.295  33.063  1.00 91.99  ? 413 LYS   A CA   1 
ATOM   2525 C  C    . LYS   A 1 392 ? 20.349 28.876  31.904  1.00 92.83  ? 413 LYS   A C    1 
ATOM   2526 O  O    . LYS   A 1 392 ? 21.419 28.313  31.610  1.00 94.94  ? 413 LYS   A O    1 
ATOM   2527 C  CB   . LYS   A 1 392 ? 20.260 28.433  34.399  1.00 89.67  ? 413 LYS   A CB   1 
ATOM   2528 C  CG   . LYS   A 1 392 ? 19.465 27.981  35.615  1.00 85.61  ? 413 LYS   A CG   1 
ATOM   2529 C  CD   . LYS   A 1 392 ? 20.169 28.218  36.946  1.00 86.64  ? 413 LYS   A CD   1 
ATOM   2530 C  CE   . LYS   A 1 392 ? 20.326 29.667  37.287  1.00 88.39  ? 413 LYS   A CE   1 
ATOM   2531 N  NZ   . LYS   A 1 392 ? 19.056 30.292  37.662  1.00 82.38  ? 413 LYS   A NZ   1 
ATOM   2532 N  N    . PHE   A 1 393 ? 19.873 29.955  31.275  1.00 94.40  ? 414 PHE   A N    1 
ATOM   2533 C  CA   . PHE   A 1 393 ? 20.615 30.610  30.161  1.00 91.61  ? 414 PHE   A CA   1 
ATOM   2534 C  C    . PHE   A 1 393 ? 21.818 31.324  30.741  1.00 94.21  ? 414 PHE   A C    1 
ATOM   2535 O  O    . PHE   A 1 393 ? 21.715 32.513  31.093  1.00 96.52  ? 414 PHE   A O    1 
ATOM   2536 C  CB   . PHE   A 1 393 ? 19.734 31.615  29.415  1.00 88.14  ? 414 PHE   A CB   1 
ATOM   2537 C  CG   . PHE   A 1 393 ? 20.401 32.378  28.278  1.00 92.80  ? 414 PHE   A CG   1 
ATOM   2538 C  CD1  . PHE   A 1 393 ? 20.738 31.736  27.095  1.00 95.96  ? 414 PHE   A CD1  1 
ATOM   2539 C  CD2  . PHE   A 1 393 ? 20.675 33.735  28.392  1.00 96.54  ? 414 PHE   A CD2  1 
ATOM   2540 C  CE1  . PHE   A 1 393 ? 21.344 32.432  26.061  1.00 93.92  ? 414 PHE   A CE1  1 
ATOM   2541 C  CE2  . PHE   A 1 393 ? 21.281 34.425  27.354  1.00 93.64  ? 414 PHE   A CE2  1 
ATOM   2542 C  CZ   . PHE   A 1 393 ? 21.614 33.774  26.192  1.00 94.28  ? 414 PHE   A CZ   1 
ATOM   2543 N  N    . LEU   A 1 394 ? 22.932 30.608  30.870  1.00 93.00  ? 415 LEU   A N    1 
ATOM   2544 C  CA   . LEU   A 1 394 ? 24.165 31.217  31.420  1.00 95.23  ? 415 LEU   A CA   1 
ATOM   2545 C  C    . LEU   A 1 394 ? 25.186 31.327  30.286  1.00 96.25  ? 415 LEU   A C    1 
ATOM   2546 O  O    . LEU   A 1 394 ? 26.013 30.410  30.138  1.00 99.20  ? 415 LEU   A O    1 
ATOM   2547 C  CB   . LEU   A 1 394 ? 24.681 30.356  32.569  1.00 94.24  ? 415 LEU   A CB   1 
ATOM   2548 N  N    . PRO   A 1 395 ? 25.170 32.408  29.485  1.00 94.52  ? 416 PRO   A N    1 
ATOM   2549 C  CA   . PRO   A 1 395 ? 26.079 32.531  28.333  1.00 91.71  ? 416 PRO   A CA   1 
ATOM   2550 C  C    . PRO   A 1 395 ? 27.561 32.588  28.700  1.00 98.03  ? 416 PRO   A C    1 
ATOM   2551 O  O    . PRO   A 1 395 ? 28.404 32.597  27.795  1.00 95.69  ? 416 PRO   A O    1 
ATOM   2552 C  CB   . PRO   A 1 395 ? 25.620 33.847  27.678  1.00 94.50  ? 416 PRO   A CB   1 
ATOM   2553 C  CG   . PRO   A 1 395 ? 25.019 34.627  28.794  1.00 101.39 ? 416 PRO   A CG   1 
ATOM   2554 C  CD   . PRO   A 1 395 ? 24.353 33.616  29.683  1.00 98.48  ? 416 PRO   A CD   1 
ATOM   2555 N  N    . GLU   A 1 396 ? 27.914 32.628  29.989  1.00 106.45 ? 417 GLU   A N    1 
ATOM   2556 C  CA   . GLU   A 1 396 ? 29.312 32.596  30.407  1.00 107.61 ? 417 GLU   A CA   1 
ATOM   2557 C  C    . GLU   A 1 396 ? 29.935 31.215  30.270  1.00 105.22 ? 417 GLU   A C    1 
ATOM   2558 O  O    . GLU   A 1 396 ? 31.142 31.075  30.496  1.00 109.17 ? 417 GLU   A O    1 
ATOM   2559 C  CB   . GLU   A 1 396 ? 29.444 33.067  31.864  1.00 105.86 ? 417 GLU   A CB   1 
ATOM   2560 C  CG   . GLU   A 1 396 ? 30.782 33.727  32.206  1.00 108.80 ? 417 GLU   A CG   1 
ATOM   2561 C  CD   . GLU   A 1 396 ? 31.002 35.014  31.439  1.00 113.83 ? 417 GLU   A CD   1 
ATOM   2562 O  OE1  . GLU   A 1 396 ? 30.016 35.754  31.227  1.00 106.36 ? 417 GLU   A OE1  1 
ATOM   2563 O  OE2  . GLU   A 1 396 ? 32.153 35.276  31.034  1.00 117.57 ? 417 GLU   A OE2  1 
ATOM   2564 N  N    . ARG   A 1 397 ? 29.144 30.195  29.922  1.00 100.77 ? 418 ARG   A N    1 
ATOM   2565 C  CA   . ARG   A 1 397 ? 29.686 28.854  29.744  1.00 101.44 ? 418 ARG   A CA   1 
ATOM   2566 C  C    . ARG   A 1 397 ? 30.692 28.787  28.604  1.00 99.16  ? 418 ARG   A C    1 
ATOM   2567 O  O    . ARG   A 1 397 ? 31.533 27.881  28.584  1.00 99.07  ? 418 ARG   A O    1 
ATOM   2568 C  CB   . ARG   A 1 397 ? 28.549 27.862  29.498  1.00 94.99  ? 418 ARG   A CB   1 
ATOM   2569 N  N    . PHE   A 1 398 ? 30.630 29.727  27.661  1.00 99.47  ? 419 PHE   A N    1 
ATOM   2570 C  CA   . PHE   A 1 398 ? 31.547 29.772  26.529  1.00 99.23  ? 419 PHE   A CA   1 
ATOM   2571 C  C    . PHE   A 1 398 ? 32.557 30.909  26.657  1.00 107.09 ? 419 PHE   A C    1 
ATOM   2572 O  O    . PHE   A 1 398 ? 32.957 31.508  25.656  1.00 104.46 ? 419 PHE   A O    1 
ATOM   2573 C  CB   . PHE   A 1 398 ? 30.768 29.887  25.221  1.00 94.73  ? 419 PHE   A CB   1 
ATOM   2574 C  CG   . PHE   A 1 398 ? 29.765 28.791  25.024  1.00 94.58  ? 419 PHE   A CG   1 
ATOM   2575 C  CD1  . PHE   A 1 398 ? 30.153 27.563  24.516  1.00 96.06  ? 419 PHE   A CD1  1 
ATOM   2576 C  CD2  . PHE   A 1 398 ? 28.436 28.983  25.358  1.00 89.71  ? 419 PHE   A CD2  1 
ATOM   2577 C  CE1  . PHE   A 1 398 ? 29.233 26.549  24.340  1.00 90.19  ? 419 PHE   A CE1  1 
ATOM   2578 C  CE2  . PHE   A 1 398 ? 27.511 27.973  25.183  1.00 86.17  ? 419 PHE   A CE2  1 
ATOM   2579 C  CZ   . PHE   A 1 398 ? 27.910 26.755  24.674  1.00 85.99  ? 419 PHE   A CZ   1 
ATOM   2580 N  N    . SER   A 1 399 ? 32.969 31.219  27.884  1.00 111.39 ? 420 SER   A N    1 
ATOM   2581 C  CA   . SER   A 1 399 ? 34.042 32.177  28.093  1.00 109.11 ? 420 SER   A CA   1 
ATOM   2582 C  C    . SER   A 1 399 ? 35.376 31.571  27.664  1.00 110.45 ? 420 SER   A C    1 
ATOM   2583 O  O    . SER   A 1 399 ? 35.511 30.356  27.497  1.00 110.98 ? 420 SER   A O    1 
ATOM   2584 C  CB   . SER   A 1 399 ? 34.100 32.610  29.558  1.00 107.02 ? 420 SER   A CB   1 
ATOM   2585 O  OG   . SER   A 1 399 ? 34.278 31.495  30.414  1.00 109.40 ? 420 SER   A OG   1 
ATOM   2586 N  N    . LYS   A 1 400 ? 36.374 32.443  27.490  1.00 112.39 ? 421 LYS   A N    1 
ATOM   2587 C  CA   . LYS   A 1 400 ? 37.663 32.003  26.960  1.00 114.50 ? 421 LYS   A CA   1 
ATOM   2588 C  C    . LYS   A 1 400 ? 38.311 30.937  27.836  1.00 116.22 ? 421 LYS   A C    1 
ATOM   2589 O  O    . LYS   A 1 400 ? 39.048 30.083  27.329  1.00 110.87 ? 421 LYS   A O    1 
ATOM   2590 C  CB   . LYS   A 1 400 ? 38.599 33.201  26.801  1.00 113.16 ? 421 LYS   A CB   1 
ATOM   2591 N  N    . LYS   A 1 401 ? 38.048 30.962  29.143  1.00 117.97 ? 422 LYS   A N    1 
ATOM   2592 C  CA   . LYS   A 1 401 ? 38.614 29.986  30.065  1.00 118.12 ? 422 LYS   A CA   1 
ATOM   2593 C  C    . LYS   A 1 401 ? 37.716 28.775  30.283  1.00 114.08 ? 422 LYS   A C    1 
ATOM   2594 O  O    . LYS   A 1 401 ? 38.187 27.761  30.810  1.00 110.58 ? 422 LYS   A O    1 
ATOM   2595 C  CB   . LYS   A 1 401 ? 38.912 30.646  31.416  1.00 116.57 ? 422 LYS   A CB   1 
ATOM   2596 N  N    . ASN   A 1 402 ? 36.442 28.853  29.896  1.00 114.61 ? 423 ASN   A N    1 
ATOM   2597 C  CA   . ASN   A 1 402 ? 35.515 27.742  30.056  1.00 116.14 ? 423 ASN   A CA   1 
ATOM   2598 C  C    . ASN   A 1 402 ? 35.096 27.104  28.739  1.00 113.48 ? 423 ASN   A C    1 
ATOM   2599 O  O    . ASN   A 1 402 ? 34.493 26.025  28.760  1.00 110.92 ? 423 ASN   A O    1 
ATOM   2600 C  CB   . ASN   A 1 402 ? 34.263 28.200  30.819  1.00 113.13 ? 423 ASN   A CB   1 
ATOM   2601 C  CG   . ASN   A 1 402 ? 34.562 28.569  32.260  1.00 110.57 ? 423 ASN   A CG   1 
ATOM   2602 O  OD1  . ASN   A 1 402 ? 35.478 28.021  32.875  1.00 108.95 ? 423 ASN   A OD1  1 
ATOM   2603 N  ND2  . ASN   A 1 402 ? 33.789 29.502  32.807  1.00 104.31 ? 423 ASN   A ND2  1 
ATOM   2604 N  N    . LYS   A 1 403 ? 35.399 27.731  27.599  1.00 112.33 ? 424 LYS   A N    1 
ATOM   2605 C  CA   . LYS   A 1 403 ? 35.050 27.151  26.306  1.00 111.57 ? 424 LYS   A CA   1 
ATOM   2606 C  C    . LYS   A 1 403 ? 35.935 25.971  25.933  1.00 112.51 ? 424 LYS   A C    1 
ATOM   2607 O  O    . LYS   A 1 403 ? 35.625 25.271  24.963  1.00 114.23 ? 424 LYS   A O    1 
ATOM   2608 C  CB   . LYS   A 1 403 ? 35.125 28.216  25.209  1.00 109.23 ? 424 LYS   A CB   1 
ATOM   2609 N  N    . ASP   A 1 404 ? 37.023 25.740  26.666  1.00 107.47 ? 425 ASP   A N    1 
ATOM   2610 C  CA   . ASP   A 1 404 ? 37.871 24.579  26.444  1.00 108.26 ? 425 ASP   A CA   1 
ATOM   2611 C  C    . ASP   A 1 404 ? 37.412 23.356  27.227  1.00 103.94 ? 425 ASP   A C    1 
ATOM   2612 O  O    . ASP   A 1 404 ? 37.852 22.242  26.919  1.00 97.71  ? 425 ASP   A O    1 
ATOM   2613 C  CB   . ASP   A 1 404 ? 39.322 24.908  26.810  1.00 110.01 ? 425 ASP   A CB   1 
ATOM   2614 N  N    . ASN   A 1 405 ? 36.540 23.534  28.221  1.00 108.71 ? 426 ASN   A N    1 
ATOM   2615 C  CA   . ASN   A 1 405 ? 36.063 22.415  29.025  1.00 110.48 ? 426 ASN   A CA   1 
ATOM   2616 C  C    . ASN   A 1 405 ? 34.896 21.678  28.382  1.00 105.71 ? 426 ASN   A C    1 
ATOM   2617 O  O    . ASN   A 1 405 ? 34.631 20.528  28.748  1.00 107.40 ? 426 ASN   A O    1 
ATOM   2618 C  CB   . ASN   A 1 405 ? 35.650 22.900  30.418  1.00 107.20 ? 426 ASN   A CB   1 
ATOM   2619 C  CG   . ASN   A 1 405 ? 36.783 23.585  31.158  1.00 108.39 ? 426 ASN   A CG   1 
ATOM   2620 O  OD1  . ASN   A 1 405 ? 37.958 23.359  30.865  1.00 105.41 ? 426 ASN   A OD1  1 
ATOM   2621 N  ND2  . ASN   A 1 405 ? 36.435 24.426  32.126  1.00 111.13 ? 426 ASN   A ND2  1 
ATOM   2622 N  N    . ILE   A 1 406 ? 34.194 22.305  27.444  1.00 102.23 ? 427 ILE   A N    1 
ATOM   2623 C  CA   . ILE   A 1 406 ? 33.059 21.664  26.792  1.00 101.97 ? 427 ILE   A CA   1 
ATOM   2624 C  C    . ILE   A 1 406 ? 33.567 20.648  25.779  1.00 104.05 ? 427 ILE   A C    1 
ATOM   2625 O  O    . ILE   A 1 406 ? 34.571 20.875  25.091  1.00 105.55 ? 427 ILE   A O    1 
ATOM   2626 C  CB   . ILE   A 1 406 ? 32.143 22.716  26.137  1.00 101.20 ? 427 ILE   A CB   1 
ATOM   2627 C  CG1  . ILE   A 1 406 ? 32.901 23.539  25.090  1.00 108.25 ? 427 ILE   A CG1  1 
ATOM   2628 C  CG2  . ILE   A 1 406 ? 31.549 23.633  27.197  1.00 94.53  ? 427 ILE   A CG2  1 
ATOM   2629 C  CD1  . ILE   A 1 406 ? 32.656 23.102  23.656  1.00 95.38  ? 427 ILE   A CD1  1 
ATOM   2630 N  N    . ASP   A 1 407 ? 32.883 19.513  25.696  1.00 98.82  ? 428 ASP   A N    1 
ATOM   2631 C  CA   . ASP   A 1 407 ? 33.261 18.468  24.755  1.00 88.77  ? 428 ASP   A CA   1 
ATOM   2632 C  C    . ASP   A 1 407 ? 32.637 18.764  23.397  1.00 80.87  ? 428 ASP   A C    1 
ATOM   2633 O  O    . ASP   A 1 407 ? 31.411 18.897  23.308  1.00 77.46  ? 428 ASP   A O    1 
ATOM   2634 C  CB   . ASP   A 1 407 ? 32.808 17.106  25.266  1.00 83.95  ? 428 ASP   A CB   1 
ATOM   2635 C  CG   . ASP   A 1 407 ? 33.586 15.955  24.653  1.00 83.67  ? 428 ASP   A CG   1 
ATOM   2636 O  OD1  . ASP   A 1 407 ? 33.949 16.038  23.462  1.00 83.39  ? 428 ASP   A OD1  1 
ATOM   2637 O  OD2  . ASP   A 1 407 ? 33.835 14.960  25.366  1.00 87.86  ? 428 ASP   A OD2  1 
ATOM   2638 N  N    . PRO   A 1 408 ? 33.428 18.881  22.326  1.00 82.56  ? 429 PRO   A N    1 
ATOM   2639 C  CA   . PRO   A 1 408 ? 32.846 19.227  21.018  1.00 78.14  ? 429 PRO   A CA   1 
ATOM   2640 C  C    . PRO   A 1 408 ? 31.876 18.189  20.482  1.00 71.11  ? 429 PRO   A C    1 
ATOM   2641 O  O    . PRO   A 1 408 ? 31.112 18.502  19.561  1.00 70.29  ? 429 PRO   A O    1 
ATOM   2642 C  CB   . PRO   A 1 408 ? 34.076 19.364  20.110  1.00 75.57  ? 429 PRO   A CB   1 
ATOM   2643 C  CG   . PRO   A 1 408 ? 35.142 18.563  20.791  1.00 81.13  ? 429 PRO   A CG   1 
ATOM   2644 C  CD   . PRO   A 1 408 ? 34.892 18.741  22.259  1.00 82.29  ? 429 PRO   A CD   1 
ATOM   2645 N  N    . TYR   A 1 409 ? 31.874 16.973  21.025  1.00 73.57  ? 430 TYR   A N    1 
ATOM   2646 C  CA   . TYR   A 1 409 ? 30.955 15.927  20.600  1.00 68.42  ? 430 TYR   A CA   1 
ATOM   2647 C  C    . TYR   A 1 409 ? 29.732 15.825  21.500  1.00 69.88  ? 430 TYR   A C    1 
ATOM   2648 O  O    . TYR   A 1 409 ? 28.920 14.910  21.328  1.00 61.02  ? 430 TYR   A O    1 
ATOM   2649 C  CB   . TYR   A 1 409 ? 31.685 14.585  20.530  1.00 69.30  ? 430 TYR   A CB   1 
ATOM   2650 C  CG   . TYR   A 1 409 ? 32.817 14.598  19.530  1.00 77.80  ? 430 TYR   A CG   1 
ATOM   2651 C  CD1  . TYR   A 1 409 ? 32.567 14.465  18.170  1.00 79.23  ? 430 TYR   A CD1  1 
ATOM   2652 C  CD2  . TYR   A 1 409 ? 34.132 14.764  19.942  1.00 76.26  ? 430 TYR   A CD2  1 
ATOM   2653 C  CE1  . TYR   A 1 409 ? 33.597 14.487  17.248  1.00 73.40  ? 430 TYR   A CE1  1 
ATOM   2654 C  CE2  . TYR   A 1 409 ? 35.169 14.787  19.027  1.00 80.46  ? 430 TYR   A CE2  1 
ATOM   2655 C  CZ   . TYR   A 1 409 ? 34.896 14.647  17.681  1.00 77.87  ? 430 TYR   A CZ   1 
ATOM   2656 O  OH   . TYR   A 1 409 ? 35.925 14.668  16.767  1.00 83.45  ? 430 TYR   A OH   1 
ATOM   2657 N  N    . ILE   A 1 410 ? 29.585 16.740  22.453  1.00 77.89  ? 431 ILE   A N    1 
ATOM   2658 C  CA   . ILE   A 1 410 ? 28.374 16.857  23.256  1.00 71.72  ? 431 ILE   A CA   1 
ATOM   2659 C  C    . ILE   A 1 410 ? 27.544 18.058  22.828  1.00 70.25  ? 431 ILE   A C    1 
ATOM   2660 O  O    . ILE   A 1 410 ? 26.331 17.951  22.644  1.00 72.30  ? 431 ILE   A O    1 
ATOM   2661 C  CB   . ILE   A 1 410 ? 28.732 16.923  24.757  1.00 66.74  ? 431 ILE   A CB   1 
ATOM   2662 C  CG1  . ILE   A 1 410 ? 29.520 15.679  25.170  1.00 67.28  ? 431 ILE   A CG1  1 
ATOM   2663 C  CG2  . ILE   A 1 410 ? 27.474 17.066  25.608  1.00 68.74  ? 431 ILE   A CG2  1 
ATOM   2664 C  CD1  . ILE   A 1 410 ? 28.783 14.380  24.953  1.00 66.96  ? 431 ILE   A CD1  1 
ATOM   2665 N  N    . TYR   A 1 411 ? 28.187 19.211  22.650  1.00 67.39  ? 432 TYR   A N    1 
ATOM   2666 C  CA   . TYR   A 1 411 ? 27.523 20.401  22.127  1.00 71.21  ? 432 TYR   A CA   1 
ATOM   2667 C  C    . TYR   A 1 411 ? 27.703 20.410  20.615  1.00 72.64  ? 432 TYR   A C    1 
ATOM   2668 O  O    . TYR   A 1 411 ? 28.733 20.852  20.099  1.00 70.21  ? 432 TYR   A O    1 
ATOM   2669 C  CB   . TYR   A 1 411 ? 28.083 21.665  22.771  1.00 71.84  ? 432 TYR   A CB   1 
ATOM   2670 C  CG   . TYR   A 1 411 ? 27.548 22.937  22.155  1.00 70.82  ? 432 TYR   A CG   1 
ATOM   2671 C  CD1  . TYR   A 1 411 ? 26.228 23.322  22.346  1.00 73.14  ? 432 TYR   A CD1  1 
ATOM   2672 C  CD2  . TYR   A 1 411 ? 28.361 23.751  21.379  1.00 70.20  ? 432 TYR   A CD2  1 
ATOM   2673 C  CE1  . TYR   A 1 411 ? 25.733 24.482  21.781  1.00 70.18  ? 432 TYR   A CE1  1 
ATOM   2674 C  CE2  . TYR   A 1 411 ? 27.875 24.914  20.813  1.00 71.77  ? 432 TYR   A CE2  1 
ATOM   2675 C  CZ   . TYR   A 1 411 ? 26.561 25.275  21.018  1.00 68.81  ? 432 TYR   A CZ   1 
ATOM   2676 O  OH   . TYR   A 1 411 ? 26.072 26.428  20.453  1.00 75.75  ? 432 TYR   A OH   1 
ATOM   2677 N  N    . THR   A 1 412 ? 26.698 19.909  19.900  1.00 71.26  ? 433 THR   A N    1 
ATOM   2678 C  CA   . THR   A 1 412 ? 26.724 19.812  18.441  1.00 67.48  ? 433 THR   A CA   1 
ATOM   2679 C  C    . THR   A 1 412 ? 25.475 20.479  17.882  1.00 68.88  ? 433 THR   A C    1 
ATOM   2680 O  O    . THR   A 1 412 ? 24.508 19.802  17.504  1.00 71.58  ? 433 THR   A O    1 
ATOM   2681 C  CB   . THR   A 1 412 ? 26.815 18.355  17.986  1.00 72.02  ? 433 THR   A CB   1 
ATOM   2682 O  OG1  . THR   A 1 412 ? 25.713 17.613  18.524  1.00 64.68  ? 433 THR   A OG1  1 
ATOM   2683 C  CG2  . THR   A 1 412 ? 28.119 17.729  18.458  1.00 73.75  ? 433 THR   A CG2  1 
ATOM   2684 N  N    . PRO   A 1 413 ? 25.455 21.814  17.820  1.00 67.19  ? 434 PRO   A N    1 
ATOM   2685 C  CA   . PRO   A 1 413 ? 24.292 22.483  17.214  1.00 73.14  ? 434 PRO   A CA   1 
ATOM   2686 C  C    . PRO   A 1 413 ? 24.281 22.379  15.701  1.00 74.91  ? 434 PRO   A C    1 
ATOM   2687 O  O    . PRO   A 1 413 ? 23.205 22.270  15.101  1.00 74.64  ? 434 PRO   A O    1 
ATOM   2688 C  CB   . PRO   A 1 413 ? 24.440 23.933  17.690  1.00 72.00  ? 434 PRO   A CB   1 
ATOM   2689 C  CG   . PRO   A 1 413 ? 25.912 24.107  17.860  1.00 72.53  ? 434 PRO   A CG   1 
ATOM   2690 C  CD   . PRO   A 1 413 ? 26.441 22.776  18.338  1.00 66.29  ? 434 PRO   A CD   1 
ATOM   2691 N  N    . PHE   A 1 414 ? 25.453 22.413  15.066  1.00 72.46  ? 435 PHE   A N    1 
ATOM   2692 C  CA   . PHE   A 1 414 ? 25.588 22.222  13.630  1.00 73.22  ? 435 PHE   A CA   1 
ATOM   2693 C  C    . PHE   A 1 414 ? 26.099 20.828  13.280  1.00 74.66  ? 435 PHE   A C    1 
ATOM   2694 O  O    . PHE   A 1 414 ? 26.564 20.605  12.156  1.00 71.69  ? 435 PHE   A O    1 
ATOM   2695 C  CB   . PHE   A 1 414 ? 26.519 23.283  13.040  1.00 73.23  ? 435 PHE   A CB   1 
ATOM   2696 C  CG   . PHE   A 1 414 ? 25.997 24.688  13.157  1.00 77.03  ? 435 PHE   A CG   1 
ATOM   2697 C  CD1  . PHE   A 1 414 ? 26.246 25.445  14.290  1.00 77.24  ? 435 PHE   A CD1  1 
ATOM   2698 C  CD2  . PHE   A 1 414 ? 25.269 25.257  12.125  1.00 80.57  ? 435 PHE   A CD2  1 
ATOM   2699 C  CE1  . PHE   A 1 414 ? 25.773 26.741  14.394  1.00 73.21  ? 435 PHE   A CE1  1 
ATOM   2700 C  CE2  . PHE   A 1 414 ? 24.795 26.553  12.222  1.00 81.58  ? 435 PHE   A CE2  1 
ATOM   2701 C  CZ   . PHE   A 1 414 ? 25.046 27.295  13.359  1.00 75.90  ? 435 PHE   A CZ   1 
ATOM   2702 N  N    . GLY   A 1 415 ? 26.028 19.888  14.221  1.00 67.77  ? 436 GLY   A N    1 
ATOM   2703 C  CA   . GLY   A 1 415 ? 26.566 18.568  13.974  1.00 66.50  ? 436 GLY   A CA   1 
ATOM   2704 C  C    . GLY   A 1 415 ? 28.086 18.572  14.024  1.00 69.89  ? 436 GLY   A C    1 
ATOM   2705 O  O    . GLY   A 1 415 ? 28.720 19.427  14.648  1.00 77.16  ? 436 GLY   A O    1 
ATOM   2706 N  N    . SER   A 1 416 ? 28.670 17.586  13.348  1.00 69.36  ? 437 SER   A N    1 
ATOM   2707 C  CA   . SER   A 1 416 ? 30.118 17.478  13.238  1.00 72.02  ? 437 SER   A CA   1 
ATOM   2708 C  C    . SER   A 1 416 ? 30.448 16.509  12.113  1.00 76.00  ? 437 SER   A C    1 
ATOM   2709 O  O    . SER   A 1 416 ? 29.570 15.842  11.560  1.00 77.07  ? 437 SER   A O    1 
ATOM   2710 C  CB   . SER   A 1 416 ? 30.756 17.022  14.554  1.00 77.97  ? 437 SER   A CB   1 
ATOM   2711 O  OG   . SER   A 1 416 ? 32.169 17.001  14.449  1.00 80.41  ? 437 SER   A OG   1 
ATOM   2712 N  N    . GLY   A 1 417 ? 31.734 16.440  11.782  1.00 80.03  ? 438 GLY   A N    1 
ATOM   2713 C  CA   . GLY   A 1 417 ? 32.204 15.550  10.750  1.00 79.73  ? 438 GLY   A CA   1 
ATOM   2714 C  C    . GLY   A 1 417 ? 32.048 16.141  9.366   1.00 74.83  ? 438 GLY   A C    1 
ATOM   2715 O  O    . GLY   A 1 417 ? 31.661 17.301  9.198   1.00 73.63  ? 438 GLY   A O    1 
ATOM   2716 N  N    . PRO   A 1 418 ? 32.346 15.340  8.338   1.00 78.66  ? 439 PRO   A N    1 
ATOM   2717 C  CA   . PRO   A 1 418 ? 32.258 15.845  6.959   1.00 75.14  ? 439 PRO   A CA   1 
ATOM   2718 C  C    . PRO   A 1 418 ? 30.838 16.060  6.467   1.00 74.82  ? 439 PRO   A C    1 
ATOM   2719 O  O    . PRO   A 1 418 ? 30.667 16.597  5.366   1.00 76.85  ? 439 PRO   A O    1 
ATOM   2720 C  CB   . PRO   A 1 418 ? 32.966 14.756  6.144   1.00 76.31  ? 439 PRO   A CB   1 
ATOM   2721 C  CG   . PRO   A 1 418 ? 32.784 13.516  6.951   1.00 82.24  ? 439 PRO   A CG   1 
ATOM   2722 C  CD   . PRO   A 1 418 ? 32.824 13.948  8.392   1.00 84.95  ? 439 PRO   A CD   1 
ATOM   2723 N  N    . ARG   A 1 419 ? 29.818 15.658  7.226   1.00 76.91  ? 440 ARG   A N    1 
ATOM   2724 C  CA   . ARG   A 1 419 ? 28.430 15.917  6.864   1.00 73.87  ? 440 ARG   A CA   1 
ATOM   2725 C  C    . ARG   A 1 419 ? 27.761 16.866  7.856   1.00 76.16  ? 440 ARG   A C    1 
ATOM   2726 O  O    . ARG   A 1 419 ? 26.549 16.799  8.078   1.00 75.20  ? 440 ARG   A O    1 
ATOM   2727 C  CB   . ARG   A 1 419 ? 27.646 14.611  6.744   1.00 72.05  ? 440 ARG   A CB   1 
ATOM   2728 C  CG   . ARG   A 1 419 ? 26.412 14.727  5.858   1.00 71.83  ? 440 ARG   A CG   1 
ATOM   2729 C  CD   . ARG   A 1 419 ? 25.999 13.396  5.258   1.00 71.41  ? 440 ARG   A CD   1 
ATOM   2730 N  NE   . ARG   A 1 419 ? 24.894 13.566  4.321   1.00 71.34  ? 440 ARG   A NE   1 
ATOM   2731 C  CZ   . ARG   A 1 419 ? 24.403 12.604  3.553   1.00 73.93  ? 440 ARG   A CZ   1 
ATOM   2732 N  NH1  . ARG   A 1 419 ? 24.904 11.379  3.573   1.00 74.46  ? 440 ARG   A NH1  1 
ATOM   2733 N  NH2  . ARG   A 1 419 ? 23.386 12.878  2.742   1.00 77.40  ? 440 ARG   A NH2  1 
ATOM   2734 N  N    . ASN   A 1 420 ? 28.543 17.760  8.455   1.00 77.83  ? 441 ASN   A N    1 
ATOM   2735 C  CA   . ASN   A 1 420 ? 27.994 18.792  9.318   1.00 72.88  ? 441 ASN   A CA   1 
ATOM   2736 C  C    . ASN   A 1 420 ? 27.239 19.822  8.478   1.00 72.72  ? 441 ASN   A C    1 
ATOM   2737 O  O    . ASN   A 1 420 ? 27.088 19.687  7.260   1.00 73.12  ? 441 ASN   A O    1 
ATOM   2738 C  CB   . ASN   A 1 420 ? 29.107 19.459  10.121  1.00 74.87  ? 441 ASN   A CB   1 
ATOM   2739 C  CG   . ASN   A 1 420 ? 30.021 20.305  9.255   1.00 77.11  ? 441 ASN   A CG   1 
ATOM   2740 O  OD1  . ASN   A 1 420 ? 30.038 21.530  9.367   1.00 77.44  ? 441 ASN   A OD1  1 
ATOM   2741 N  ND2  . ASN   A 1 420 ? 30.787 19.655  8.384   1.00 77.35  ? 441 ASN   A ND2  1 
ATOM   2742 N  N    . CYS   A 1 421 ? 26.759 20.871  9.140   1.00 74.05  ? 442 CYS   A N    1 
ATOM   2743 C  CA   . CYS   A 1 421 ? 26.057 21.938  8.437   1.00 73.78  ? 442 CYS   A CA   1 
ATOM   2744 C  C    . CYS   A 1 421 ? 27.026 22.670  7.517   1.00 75.97  ? 442 CYS   A C    1 
ATOM   2745 O  O    . CYS   A 1 421 ? 27.980 23.303  7.982   1.00 74.62  ? 442 CYS   A O    1 
ATOM   2746 C  CB   . CYS   A 1 421 ? 25.424 22.906  9.433   1.00 74.07  ? 442 CYS   A CB   1 
ATOM   2747 S  SG   . CYS   A 1 421 ? 24.490 24.254  8.668   1.00 70.94  ? 442 CYS   A SG   1 
ATOM   2748 N  N    . ILE   A 1 422 ? 26.783 22.579  6.207   1.00 77.33  ? 443 ILE   A N    1 
ATOM   2749 C  CA   . ILE   A 1 422 ? 27.666 23.225  5.244   1.00 75.73  ? 443 ILE   A CA   1 
ATOM   2750 C  C    . ILE   A 1 422 ? 27.484 24.736  5.246   1.00 78.38  ? 443 ILE   A C    1 
ATOM   2751 O  O    . ILE   A 1 422 ? 28.350 25.463  4.744   1.00 79.14  ? 443 ILE   A O    1 
ATOM   2752 C  CB   . ILE   A 1 422 ? 27.436 22.644  3.836   1.00 68.57  ? 443 ILE   A CB   1 
ATOM   2753 C  CG1  . ILE   A 1 422 ? 28.693 22.808  2.981   1.00 77.83  ? 443 ILE   A CG1  1 
ATOM   2754 C  CG2  . ILE   A 1 422 ? 26.253 23.318  3.166   1.00 73.97  ? 443 ILE   A CG2  1 
ATOM   2755 C  CD1  . ILE   A 1 422 ? 28.555 22.245  1.586   1.00 86.32  ? 443 ILE   A CD1  1 
ATOM   2756 N  N    . GLY   A 1 423 ? 26.383 25.231  5.804   1.00 77.74  ? 444 GLY   A N    1 
ATOM   2757 C  CA   . GLY   A 1 423 ? 26.161 26.659  5.898   1.00 81.05  ? 444 GLY   A CA   1 
ATOM   2758 C  C    . GLY   A 1 423 ? 26.319 27.185  7.309   1.00 83.24  ? 444 GLY   A C    1 
ATOM   2759 O  O    . GLY   A 1 423 ? 25.729 28.211  7.663   1.00 84.43  ? 444 GLY   A O    1 
ATOM   2760 N  N    . MET   A 1 424 ? 27.111 26.488  8.127   1.00 78.93  ? 445 MET   A N    1 
ATOM   2761 C  CA   . MET   A 1 424 ? 27.322 26.921  9.505   1.00 76.26  ? 445 MET   A CA   1 
ATOM   2762 C  C    . MET   A 1 424 ? 27.927 28.317  9.556   1.00 82.34  ? 445 MET   A C    1 
ATOM   2763 O  O    . MET   A 1 424 ? 27.458 29.182  10.304  1.00 87.48  ? 445 MET   A O    1 
ATOM   2764 C  CB   . MET   A 1 424 ? 28.216 25.923  10.240  1.00 77.96  ? 445 MET   A CB   1 
ATOM   2765 C  CG   . MET   A 1 424 ? 28.865 26.493  11.491  1.00 76.92  ? 445 MET   A CG   1 
ATOM   2766 S  SD   . MET   A 1 424 ? 29.589 25.226  12.545  1.00 68.42  ? 445 MET   A SD   1 
ATOM   2767 C  CE   . MET   A 1 424 ? 30.473 24.247  11.332  1.00 82.89  ? 445 MET   A CE   1 
ATOM   2768 N  N    . ARG   A 1 425 ? 28.973 28.555  8.762   1.00 83.23  ? 446 ARG   A N    1 
ATOM   2769 C  CA   . ARG   A 1 425 ? 29.610 29.868  8.757   1.00 85.18  ? 446 ARG   A CA   1 
ATOM   2770 C  C    . ARG   A 1 425 ? 28.677 30.934  8.195   1.00 86.64  ? 446 ARG   A C    1 
ATOM   2771 O  O    . ARG   A 1 425 ? 28.660 32.070  8.682   1.00 88.34  ? 446 ARG   A O    1 
ATOM   2772 C  CB   . ARG   A 1 425 ? 30.911 29.814  7.957   1.00 81.10  ? 446 ARG   A CB   1 
ATOM   2773 N  N    . PHE   A 1 426 ? 27.890 30.586  7.176   1.00 85.16  ? 447 PHE   A N    1 
ATOM   2774 C  CA   . PHE   A 1 426 ? 26.958 31.549  6.598   1.00 89.58  ? 447 PHE   A CA   1 
ATOM   2775 C  C    . PHE   A 1 426 ? 25.829 31.868  7.569   1.00 90.64  ? 447 PHE   A C    1 
ATOM   2776 O  O    . PHE   A 1 426 ? 25.474 33.037  7.761   1.00 92.99  ? 447 PHE   A O    1 
ATOM   2777 C  CB   . PHE   A 1 426 ? 26.403 31.011  5.278   1.00 98.19  ? 447 PHE   A CB   1 
ATOM   2778 C  CG   . PHE   A 1 426 ? 25.441 31.945  4.595   1.00 99.38  ? 447 PHE   A CG   1 
ATOM   2779 C  CD1  . PHE   A 1 426 ? 25.902 32.919  3.725   1.00 103.76 ? 447 PHE   A CD1  1 
ATOM   2780 C  CD2  . PHE   A 1 426 ? 24.077 31.843  4.817   1.00 96.74  ? 447 PHE   A CD2  1 
ATOM   2781 C  CE1  . PHE   A 1 426 ? 25.021 33.778  3.094   1.00 108.51 ? 447 PHE   A CE1  1 
ATOM   2782 C  CE2  . PHE   A 1 426 ? 23.191 32.698  4.190   1.00 100.52 ? 447 PHE   A CE2  1 
ATOM   2783 C  CZ   . PHE   A 1 426 ? 23.664 33.667  3.327   1.00 108.52 ? 447 PHE   A CZ   1 
ATOM   2784 N  N    . ALA   A 1 427 ? 25.248 30.838  8.188   1.00 89.97  ? 448 ALA   A N    1 
ATOM   2785 C  CA   . ALA   A 1 427 ? 24.150 31.062  9.122   1.00 91.39  ? 448 ALA   A CA   1 
ATOM   2786 C  C    . ALA   A 1 427 ? 24.617 31.829  10.352  1.00 88.06  ? 448 ALA   A C    1 
ATOM   2787 O  O    . ALA   A 1 427 ? 23.893 32.690  10.866  1.00 88.29  ? 448 ALA   A O    1 
ATOM   2788 C  CB   . ALA   A 1 427 ? 23.521 29.729  9.525   1.00 89.27  ? 448 ALA   A CB   1 
ATOM   2789 N  N    . LEU   A 1 428 ? 25.823 31.530  10.841  1.00 80.49  ? 449 LEU   A N    1 
ATOM   2790 C  CA   . LEU   A 1 428 ? 26.358 32.281  11.970  1.00 80.74  ? 449 LEU   A CA   1 
ATOM   2791 C  C    . LEU   A 1 428 ? 26.603 33.736  11.595  1.00 86.97  ? 449 LEU   A C    1 
ATOM   2792 O  O    . LEU   A 1 428 ? 26.360 34.640  12.401  1.00 91.78  ? 449 LEU   A O    1 
ATOM   2793 C  CB   . LEU   A 1 428 ? 27.646 31.631  12.474  1.00 80.73  ? 449 LEU   A CB   1 
ATOM   2794 C  CG   . LEU   A 1 428 ? 27.476 30.379  13.336  1.00 81.16  ? 449 LEU   A CG   1 
ATOM   2795 C  CD1  . LEU   A 1 428 ? 28.830 29.794  13.702  1.00 77.19  ? 449 LEU   A CD1  1 
ATOM   2796 C  CD2  . LEU   A 1 428 ? 26.672 30.702  14.586  1.00 77.40  ? 449 LEU   A CD2  1 
ATOM   2797 N  N    . MET   A 1 429 ? 27.075 33.983  10.372  1.00 85.36  ? 450 MET   A N    1 
ATOM   2798 C  CA   . MET   A 1 429 ? 27.309 35.357  9.943   1.00 88.00  ? 450 MET   A CA   1 
ATOM   2799 C  C    . MET   A 1 429 ? 25.997 36.085  9.678   1.00 93.12  ? 450 MET   A C    1 
ATOM   2800 O  O    . MET   A 1 429 ? 25.849 37.258  10.040  1.00 96.01  ? 450 MET   A O    1 
ATOM   2801 C  CB   . MET   A 1 429 ? 28.196 35.375  8.699   1.00 90.53  ? 450 MET   A CB   1 
ATOM   2802 N  N    . ASN   A 1 430 ? 25.033 35.404  9.050   1.00 95.90  ? 451 ASN   A N    1 
ATOM   2803 C  CA   . ASN   A 1 430 ? 23.750 36.035  8.747   1.00 96.80  ? 451 ASN   A CA   1 
ATOM   2804 C  C    . ASN   A 1 430 ? 23.027 36.455  10.019  1.00 98.27  ? 451 ASN   A C    1 
ATOM   2805 O  O    . ASN   A 1 430 ? 22.454 37.549  10.086  1.00 103.57 ? 451 ASN   A O    1 
ATOM   2806 C  CB   . ASN   A 1 430 ? 22.879 35.083  7.924   1.00 100.69 ? 451 ASN   A CB   1 
ATOM   2807 C  CG   . ASN   A 1 430 ? 21.521 35.675  7.582   1.00 108.45 ? 451 ASN   A CG   1 
ATOM   2808 O  OD1  . ASN   A 1 430 ? 21.365 36.893  7.491   1.00 111.83 ? 451 ASN   A OD1  1 
ATOM   2809 N  ND2  . ASN   A 1 430 ? 20.531 34.810  7.390   1.00 110.20 ? 451 ASN   A ND2  1 
ATOM   2810 N  N    . MET   A 1 431 ? 23.045 35.599  11.042  1.00 96.45  ? 452 MET   A N    1 
ATOM   2811 C  CA   . MET   A 1 431 ? 22.372 35.935  12.291  1.00 99.30  ? 452 MET   A CA   1 
ATOM   2812 C  C    . MET   A 1 431 ? 23.146 36.990  13.071  1.00 97.87  ? 452 MET   A C    1 
ATOM   2813 O  O    . MET   A 1 431 ? 22.548 37.908  13.644  1.00 97.13  ? 452 MET   A O    1 
ATOM   2814 C  CB   . MET   A 1 431 ? 22.175 34.675  13.133  1.00 98.72  ? 452 MET   A CB   1 
ATOM   2815 C  CG   . MET   A 1 431 ? 21.256 33.645  12.495  1.00 92.84  ? 452 MET   A CG   1 
ATOM   2816 S  SD   . MET   A 1 431 ? 20.972 32.221  13.560  1.00 94.43  ? 452 MET   A SD   1 
ATOM   2817 C  CE   . MET   A 1 431 ? 22.644 31.613  13.766  1.00 86.65  ? 452 MET   A CE   1 
ATOM   2818 N  N    . LYS   A 1 432 ? 24.477 36.881  13.100  1.00 97.50  ? 453 LYS   A N    1 
ATOM   2819 C  CA   . LYS   A 1 432 ? 25.278 37.832  13.865  1.00 99.40  ? 453 LYS   A CA   1 
ATOM   2820 C  C    . LYS   A 1 432 ? 25.257 39.216  13.228  1.00 99.89  ? 453 LYS   A C    1 
ATOM   2821 O  O    . LYS   A 1 432 ? 25.244 40.230  13.935  1.00 98.25  ? 453 LYS   A O    1 
ATOM   2822 C  CB   . LYS   A 1 432 ? 26.712 37.324  14.001  1.00 94.28  ? 453 LYS   A CB   1 
ATOM   2823 N  N    . LEU   A 1 433 ? 25.260 39.280  11.894  1.00 98.66  ? 454 LEU   A N    1 
ATOM   2824 C  CA   . LEU   A 1 433 ? 25.149 40.571  11.225  1.00 98.94  ? 454 LEU   A CA   1 
ATOM   2825 C  C    . LEU   A 1 433 ? 23.789 41.207  11.473  1.00 100.18 ? 454 LEU   A C    1 
ATOM   2826 O  O    . LEU   A 1 433 ? 23.683 42.436  11.542  1.00 102.55 ? 454 LEU   A O    1 
ATOM   2827 C  CB   . LEU   A 1 433 ? 25.393 40.413  9.725   1.00 95.85  ? 454 LEU   A CB   1 
ATOM   2828 N  N    . ALA   A 1 434 ? 22.744 40.391  11.611  1.00 96.17  ? 455 ALA   A N    1 
ATOM   2829 C  CA   . ALA   A 1 434 ? 21.424 40.927  11.913  1.00 100.19 ? 455 ALA   A CA   1 
ATOM   2830 C  C    . ALA   A 1 434 ? 21.313 41.341  13.374  1.00 108.47 ? 455 ALA   A C    1 
ATOM   2831 O  O    . ALA   A 1 434 ? 20.631 42.321  13.695  1.00 111.98 ? 455 ALA   A O    1 
ATOM   2832 C  CB   . ALA   A 1 434 ? 20.345 39.902  11.566  1.00 101.57 ? 455 ALA   A CB   1 
ATOM   2833 N  N    . LEU   A 1 435 ? 21.975 40.608  14.271  1.00 105.58 ? 456 LEU   A N    1 
ATOM   2834 C  CA   . LEU   A 1 435 ? 21.886 40.923  15.691  1.00 100.95 ? 456 LEU   A CA   1 
ATOM   2835 C  C    . LEU   A 1 435 ? 22.635 42.205  16.031  1.00 104.90 ? 456 LEU   A C    1 
ATOM   2836 O  O    . LEU   A 1 435 ? 22.193 42.970  16.896  1.00 111.40 ? 456 LEU   A O    1 
ATOM   2837 C  CB   . LEU   A 1 435 ? 22.421 39.755  16.518  1.00 101.83 ? 456 LEU   A CB   1 
ATOM   2838 N  N    . ILE   A 1 436 ? 23.759 42.461  15.358  1.00 104.55 ? 457 ILE   A N    1 
ATOM   2839 C  CA   . ILE   A 1 436 ? 24.559 43.642  15.669  1.00 108.40 ? 457 ILE   A CA   1 
ATOM   2840 C  C    . ILE   A 1 436 ? 23.791 44.915  15.339  1.00 110.81 ? 457 ILE   A C    1 
ATOM   2841 O  O    . ILE   A 1 436 ? 23.834 45.893  16.095  1.00 109.82 ? 457 ILE   A O    1 
ATOM   2842 C  CB   . ILE   A 1 436 ? 25.907 43.583  14.928  1.00 105.63 ? 457 ILE   A CB   1 
ATOM   2843 N  N    . ARG   A 1 437 ? 23.074 44.927  14.213  1.00 116.05 ? 458 ARG   A N    1 
ATOM   2844 C  CA   . ARG   A 1 437 ? 22.331 46.117  13.813  1.00 115.54 ? 458 ARG   A CA   1 
ATOM   2845 C  C    . ARG   A 1 437 ? 21.035 46.282  14.598  1.00 115.54 ? 458 ARG   A C    1 
ATOM   2846 O  O    . ARG   A 1 437 ? 20.623 47.415  14.868  1.00 119.23 ? 458 ARG   A O    1 
ATOM   2847 C  CB   . ARG   A 1 437 ? 22.030 46.072  12.314  1.00 103.66 ? 458 ARG   A CB   1 
ATOM   2848 N  N    . VAL   A 1 438 ? 20.381 45.181  14.967  1.00 112.34 ? 459 VAL   A N    1 
ATOM   2849 C  CA   . VAL   A 1 438 ? 19.120 45.289  15.694  1.00 115.93 ? 459 VAL   A CA   1 
ATOM   2850 C  C    . VAL   A 1 438 ? 19.354 45.667  17.150  1.00 122.79 ? 459 VAL   A C    1 
ATOM   2851 O  O    . VAL   A 1 438 ? 18.495 46.298  17.776  1.00 126.77 ? 459 VAL   A O    1 
ATOM   2852 C  CB   . VAL   A 1 438 ? 18.326 43.977  15.589  1.00 113.05 ? 459 VAL   A CB   1 
ATOM   2853 N  N    . LEU   A 1 439 ? 20.499 45.291  17.716  1.00 124.23 ? 460 LEU   A N    1 
ATOM   2854 C  CA   . LEU   A 1 439 ? 20.754 45.586  19.119  1.00 123.77 ? 460 LEU   A CA   1 
ATOM   2855 C  C    . LEU   A 1 439 ? 21.326 46.982  19.312  1.00 123.96 ? 460 LEU   A C    1 
ATOM   2856 O  O    . LEU   A 1 439 ? 21.174 47.566  20.392  1.00 126.56 ? 460 LEU   A O    1 
ATOM   2857 C  CB   . LEU   A 1 439 ? 21.695 44.541  19.717  1.00 121.84 ? 460 LEU   A CB   1 
ATOM   2858 N  N    . GLN   A 1 440 ? 21.977 47.531  18.290  1.00 122.21 ? 461 GLN   A N    1 
ATOM   2859 C  CA   . GLN   A 1 440 ? 22.553 48.864  18.392  1.00 125.92 ? 461 GLN   A CA   1 
ATOM   2860 C  C    . GLN   A 1 440 ? 21.543 49.971  18.115  1.00 128.58 ? 461 GLN   A C    1 
ATOM   2861 O  O    . GLN   A 1 440 ? 21.918 51.148  18.140  1.00 131.95 ? 461 GLN   A O    1 
ATOM   2862 C  CB   . GLN   A 1 440 ? 23.746 48.994  17.441  1.00 121.77 ? 461 GLN   A CB   1 
ATOM   2863 C  CG   . GLN   A 1 440 ? 23.376 49.059  15.971  1.00 116.22 ? 461 GLN   A CG   1 
ATOM   2864 C  CD   . GLN   A 1 440 ? 24.585 49.269  15.082  1.00 116.18 ? 461 GLN   A CD   1 
ATOM   2865 O  OE1  . GLN   A 1 440 ? 25.723 49.275  15.553  1.00 113.38 ? 461 GLN   A OE1  1 
ATOM   2866 N  NE2  . GLN   A 1 440 ? 24.344 49.444  13.788  1.00 120.87 ? 461 GLN   A NE2  1 
ATOM   2867 N  N    . ASN   A 1 441 ? 20.279 49.628  17.857  1.00 129.67 ? 462 ASN   A N    1 
ATOM   2868 C  CA   . ASN   A 1 441 ? 19.233 50.618  17.624  1.00 131.47 ? 462 ASN   A CA   1 
ATOM   2869 C  C    . ASN   A 1 441 ? 18.007 50.459  18.511  1.00 132.80 ? 462 ASN   A C    1 
ATOM   2870 O  O    . ASN   A 1 441 ? 17.292 51.448  18.716  1.00 133.74 ? 462 ASN   A O    1 
ATOM   2871 C  CB   . ASN   A 1 441 ? 18.772 50.588  16.157  1.00 132.30 ? 462 ASN   A CB   1 
ATOM   2872 C  CG   . ASN   A 1 441 ? 19.698 51.358  15.234  1.00 132.97 ? 462 ASN   A CG   1 
ATOM   2873 O  OD1  . ASN   A 1 441 ? 20.899 51.463  15.482  1.00 129.99 ? 462 ASN   A OD1  1 
ATOM   2874 N  ND2  . ASN   A 1 441 ? 19.137 51.907  14.162  1.00 131.66 ? 462 ASN   A ND2  1 
ATOM   2875 N  N    . PHE   A 1 442 ? 17.734 49.267  19.040  1.00 131.13 ? 463 PHE   A N    1 
ATOM   2876 C  CA   . PHE   A 1 442 ? 16.530 49.026  19.820  1.00 129.40 ? 463 PHE   A CA   1 
ATOM   2877 C  C    . PHE   A 1 442 ? 16.869 48.196  21.050  1.00 129.26 ? 463 PHE   A C    1 
ATOM   2878 O  O    . PHE   A 1 442 ? 17.943 47.597  21.154  1.00 126.42 ? 463 PHE   A O    1 
ATOM   2879 C  CB   . PHE   A 1 442 ? 15.453 48.313  18.991  1.00 133.21 ? 463 PHE   A CB   1 
ATOM   2880 C  CG   . PHE   A 1 442 ? 15.028 49.068  17.764  1.00 136.13 ? 463 PHE   A CG   1 
ATOM   2881 C  CD1  . PHE   A 1 442 ? 14.002 49.997  17.826  1.00 139.05 ? 463 PHE   A CD1  1 
ATOM   2882 C  CD2  . PHE   A 1 442 ? 15.649 48.843  16.547  1.00 133.90 ? 463 PHE   A CD2  1 
ATOM   2883 C  CE1  . PHE   A 1 442 ? 13.608 50.691  16.698  1.00 140.69 ? 463 PHE   A CE1  1 
ATOM   2884 C  CE2  . PHE   A 1 442 ? 15.259 49.534  15.415  1.00 140.66 ? 463 PHE   A CE2  1 
ATOM   2885 C  CZ   . PHE   A 1 442 ? 14.237 50.458  15.491  1.00 143.38 ? 463 PHE   A CZ   1 
ATOM   2886 N  N    . SER   A 1 443 ? 15.926 48.175  21.990  1.00 133.42 ? 464 SER   A N    1 
ATOM   2887 C  CA   . SER   A 1 443 ? 15.982 47.321  23.166  1.00 130.77 ? 464 SER   A CA   1 
ATOM   2888 C  C    . SER   A 1 443 ? 14.682 46.535  23.255  1.00 129.72 ? 464 SER   A C    1 
ATOM   2889 O  O    . SER   A 1 443 ? 13.619 47.018  22.855  1.00 133.26 ? 464 SER   A O    1 
ATOM   2890 C  CB   . SER   A 1 443 ? 16.201 48.132  24.452  1.00 130.65 ? 464 SER   A CB   1 
ATOM   2891 N  N    . PHE   A 1 444 ? 14.772 45.317  23.779  1.00 126.61 ? 465 PHE   A N    1 
ATOM   2892 C  CA   . PHE   A 1 444 ? 13.647 44.391  23.803  1.00 126.02 ? 465 PHE   A CA   1 
ATOM   2893 C  C    . PHE   A 1 444 ? 13.252 44.113  25.246  1.00 126.58 ? 465 PHE   A C    1 
ATOM   2894 O  O    . PHE   A 1 444 ? 14.058 43.596  26.027  1.00 124.17 ? 465 PHE   A O    1 
ATOM   2895 C  CB   . PHE   A 1 444 ? 13.994 43.093  23.071  1.00 125.54 ? 465 PHE   A CB   1 
ATOM   2896 C  CG   . PHE   A 1 444 ? 14.127 43.259  21.583  1.00 128.52 ? 465 PHE   A CG   1 
ATOM   2897 C  CD1  . PHE   A 1 444 ? 15.247 43.866  21.037  1.00 131.25 ? 465 PHE   A CD1  1 
ATOM   2898 C  CD2  . PHE   A 1 444 ? 13.131 42.811  20.729  1.00 126.64 ? 465 PHE   A CD2  1 
ATOM   2899 C  CE1  . PHE   A 1 444 ? 15.372 44.024  19.669  1.00 130.98 ? 465 PHE   A CE1  1 
ATOM   2900 C  CE2  . PHE   A 1 444 ? 13.251 42.965  19.360  1.00 122.16 ? 465 PHE   A CE2  1 
ATOM   2901 C  CZ   . PHE   A 1 444 ? 14.373 43.572  18.830  1.00 128.22 ? 465 PHE   A CZ   1 
ATOM   2902 N  N    . LYS   A 1 445 ? 12.012 44.457  25.593  1.00 125.65 ? 466 LYS   A N    1 
ATOM   2903 C  CA   . LYS   A 1 445 ? 11.483 44.275  26.933  1.00 127.12 ? 466 LYS   A CA   1 
ATOM   2904 C  C    . LYS   A 1 445 ? 10.348 43.258  26.925  1.00 123.69 ? 466 LYS   A C    1 
ATOM   2905 O  O    . LYS   A 1 445 ? 9.594  43.169  25.951  1.00 119.40 ? 466 LYS   A O    1 
ATOM   2906 C  CB   . LYS   A 1 445 ? 10.968 45.597  27.515  1.00 125.65 ? 466 LYS   A CB   1 
ATOM   2907 N  N    . PRO   A 1 446 ? 10.197 42.431  27.990  1.00 121.97 ? 467 PRO   A N    1 
ATOM   2908 C  CA   . PRO   A 1 446 ? 9.108  41.471  28.061  1.00 120.82 ? 467 PRO   A CA   1 
ATOM   2909 C  C    . PRO   A 1 446 ? 7.752  42.144  28.094  1.00 124.83 ? 467 PRO   A C    1 
ATOM   2910 O  O    . PRO   A 1 446 ? 7.519  42.964  29.000  1.00 125.14 ? 467 PRO   A O    1 
ATOM   2911 C  CB   . PRO   A 1 446 ? 9.390  40.735  29.378  1.00 120.60 ? 467 PRO   A CB   1 
ATOM   2912 C  CG   . PRO   A 1 446 ? 10.869 40.900  29.585  1.00 118.04 ? 467 PRO   A CG   1 
ATOM   2913 C  CD   . PRO   A 1 446 ? 11.065 42.340  29.173  1.00 119.76 ? 467 PRO   A CD   1 
ATOM   2914 N  N    . CYS   A 1 447 ? 6.866  41.790  27.160  1.00 125.88 ? 468 CYS   A N    1 
ATOM   2915 C  CA   . CYS   A 1 447 ? 5.487  42.346  27.155  1.00 124.05 ? 468 CYS   A CA   1 
ATOM   2916 C  C    . CYS   A 1 447 ? 4.612  41.496  28.088  1.00 120.13 ? 468 CYS   A C    1 
ATOM   2917 O  O    . CYS   A 1 447 ? 5.172  40.724  28.891  1.00 121.22 ? 468 CYS   A O    1 
ATOM   2918 C  CB   . CYS   A 1 447 ? 4.863  42.259  25.768  1.00 123.53 ? 468 CYS   A CB   1 
ATOM   2919 S  SG   . CYS   A 1 447 ? 4.107  40.652  25.412  1.00 124.75 ? 468 CYS   A SG   1 
ATOM   2920 N  N    . LYS   A 1 448 ? 3.291  41.640  27.984  1.00 118.49 ? 469 LYS   A N    1 
ATOM   2921 C  CA   . LYS   A 1 448 ? 2.355  40.866  28.836  1.00 115.65 ? 469 LYS   A CA   1 
ATOM   2922 C  C    . LYS   A 1 448 ? 2.925  39.477  29.152  1.00 112.77 ? 469 LYS   A C    1 
ATOM   2923 O  O    . LYS   A 1 448 ? 2.671  38.563  28.343  1.00 113.91 ? 469 LYS   A O    1 
ATOM   2924 C  CB   . LYS   A 1 448 ? 0.982  40.753  28.169  1.00 112.85 ? 469 LYS   A CB   1 
ATOM   2925 N  N    . THR   A 1 450 ? 4.264  37.316  25.808  1.00 129.53 ? 471 THR   A N    1 
ATOM   2926 C  CA   . THR   A 1 450 ? 5.341  36.411  26.179  1.00 131.57 ? 471 THR   A CA   1 
ATOM   2927 C  C    . THR   A 1 450 ? 4.925  35.528  27.348  1.00 128.24 ? 471 THR   A C    1 
ATOM   2928 O  O    . THR   A 1 450 ? 3.882  35.731  27.969  1.00 126.56 ? 471 THR   A O    1 
ATOM   2929 C  CB   . THR   A 1 450 ? 6.623  37.183  26.544  1.00 133.41 ? 471 THR   A CB   1 
ATOM   2930 O  OG1  . THR   A 1 450 ? 7.725  36.275  26.624  1.00 137.86 ? 471 THR   A OG1  1 
ATOM   2931 C  CG2  . THR   A 1 450 ? 6.463  37.889  27.880  1.00 124.91 ? 471 THR   A CG2  1 
ATOM   2932 N  N    . GLN   A 1 451 ? 5.776  34.538  27.621  1.00 121.59 ? 472 GLN   A N    1 
ATOM   2933 C  CA   . GLN   A 1 451 ? 5.506  33.614  28.745  1.00 121.12 ? 472 GLN   A CA   1 
ATOM   2934 C  C    . GLN   A 1 451 ? 6.845  33.096  29.278  1.00 123.34 ? 472 GLN   A C    1 
ATOM   2935 O  O    . GLN   A 1 451 ? 7.528  32.351  28.549  1.00 123.33 ? 472 GLN   A O    1 
ATOM   2936 C  CB   . GLN   A 1 451 ? 4.610  32.457  28.309  1.00 118.83 ? 472 GLN   A CB   1 
ATOM   2937 N  N    . ILE   A 1 452 ? 7.188  33.472  30.508  1.00 122.61 ? 473 ILE   A N    1 
ATOM   2938 C  CA   . ILE   A 1 452 ? 8.496  33.058  31.092  1.00 121.67 ? 473 ILE   A CA   1 
ATOM   2939 C  C    . ILE   A 1 452 ? 8.677  31.542  30.907  1.00 128.93 ? 473 ILE   A C    1 
ATOM   2940 O  O    . ILE   A 1 452 ? 9.740  31.149  30.388  1.00 133.99 ? 473 ILE   A O    1 
ATOM   2941 C  CB   . ILE   A 1 452 ? 8.598  33.477  32.569  1.00 117.72 ? 473 ILE   A CB   1 
ATOM   2942 N  N    . PRO   A 1 453 ? 7.724  30.663  31.288  1.00 128.55 ? 474 PRO   A N    1 
ATOM   2943 C  CA   . PRO   A 1 453 ? 7.955  29.232  31.168  1.00 128.79 ? 474 PRO   A CA   1 
ATOM   2944 C  C    . PRO   A 1 453 ? 8.461  28.837  29.782  1.00 127.70 ? 474 PRO   A C    1 
ATOM   2945 O  O    . PRO   A 1 453 ? 9.176  27.824  29.678  1.00 131.67 ? 474 PRO   A O    1 
ATOM   2946 C  CB   . PRO   A 1 453 ? 6.585  28.615  31.487  1.00 124.48 ? 474 PRO   A CB   1 
ATOM   2947 C  CG   . PRO   A 1 453 ? 5.619  29.773  31.386  1.00 124.94 ? 474 PRO   A CG   1 
ATOM   2948 C  CD   . PRO   A 1 453 ? 6.421  30.972  31.852  1.00 124.46 ? 474 PRO   A CD   1 
ATOM   2949 N  N    . LEU   A 1 454 ? 8.099  29.594  28.746  1.00 122.60 ? 475 LEU   A N    1 
ATOM   2950 C  CA   . LEU   A 1 454 ? 8.559  29.337  27.379  1.00 126.09 ? 475 LEU   A CA   1 
ATOM   2951 C  C    . LEU   A 1 454 ? 8.383  27.868  27.009  1.00 127.45 ? 475 LEU   A C    1 
ATOM   2952 O  O    . LEU   A 1 454 ? 9.301  27.211  26.511  1.00 122.81 ? 475 LEU   A O    1 
ATOM   2953 C  CB   . LEU   A 1 454 ? 10.014 29.774  27.197  1.00 125.00 ? 475 LEU   A CB   1 
ATOM   2954 N  N    . LYS   A 1 455 ? 7.184  27.353  27.280  1.00 128.80 ? 476 LYS   A N    1 
ATOM   2955 C  CA   . LYS   A 1 455 ? 6.887  25.943  27.066  1.00 121.37 ? 476 LYS   A CA   1 
ATOM   2956 C  C    . LYS   A 1 455 ? 7.146  25.555  25.617  1.00 119.28 ? 476 LYS   A C    1 
ATOM   2957 O  O    . LYS   A 1 455 ? 6.563  26.135  24.695  1.00 115.28 ? 476 LYS   A O    1 
ATOM   2958 C  CB   . LYS   A 1 455 ? 5.436  25.650  27.447  1.00 117.53 ? 476 LYS   A CB   1 
ATOM   2959 N  N    . LEU   A 1 456 ? 8.036  24.585  25.424  1.00 119.18 ? 477 LEU   A N    1 
ATOM   2960 C  CA   . LEU   A 1 456 ? 8.362  24.114  24.088  1.00 113.30 ? 477 LEU   A CA   1 
ATOM   2961 C  C    . LEU   A 1 456 ? 7.187  23.352  23.486  1.00 115.30 ? 477 LEU   A C    1 
ATOM   2962 O  O    . LEU   A 1 456 ? 6.331  22.811  24.192  1.00 118.37 ? 477 LEU   A O    1 
ATOM   2963 C  CB   . LEU   A 1 456 ? 9.601  23.221  24.123  1.00 106.11 ? 477 LEU   A CB   1 
ATOM   2964 C  CG   . LEU   A 1 456 ? 10.936 23.911  24.398  1.00 102.71 ? 477 LEU   A CG   1 
ATOM   2965 C  CD1  . LEU   A 1 456 ? 12.040 22.881  24.548  1.00 96.53  ? 477 LEU   A CD1  1 
ATOM   2966 C  CD2  . LEU   A 1 456 ? 11.258 24.888  23.279  1.00 101.22 ? 477 LEU   A CD2  1 
ATOM   2967 N  N    . SER   A 1 457 ? 7.152  23.318  22.158  1.00 118.88 ? 478 SER   A N    1 
ATOM   2968 C  CA   . SER   A 1 457 ? 6.122  22.559  21.467  1.00 120.44 ? 478 SER   A CA   1 
ATOM   2969 C  C    . SER   A 1 457 ? 6.395  21.064  21.581  1.00 119.10 ? 478 SER   A C    1 
ATOM   2970 O  O    . SER   A 1 457 ? 7.545  20.616  21.609  1.00 124.81 ? 478 SER   A O    1 
ATOM   2971 C  CB   . SER   A 1 457 ? 6.045  22.966  19.996  1.00 115.85 ? 478 SER   A CB   1 
ATOM   2972 O  OG   . SER   A 1 457 ? 5.102  22.177  19.294  1.00 112.01 ? 478 SER   A OG   1 
ATOM   2973 N  N    . LEU   A 1 458 ? 5.317  20.289  21.648  1.00 115.42 ? 479 LEU   A N    1 
ATOM   2974 C  CA   . LEU   A 1 458 ? 5.401  18.843  21.780  1.00 110.34 ? 479 LEU   A CA   1 
ATOM   2975 C  C    . LEU   A 1 458 ? 5.546  18.133  20.440  1.00 110.79 ? 479 LEU   A C    1 
ATOM   2976 O  O    . LEU   A 1 458 ? 5.571  16.899  20.410  1.00 113.69 ? 479 LEU   A O    1 
ATOM   2977 C  CB   . LEU   A 1 458 ? 4.164  18.315  22.514  1.00 108.46 ? 479 LEU   A CB   1 
ATOM   2978 C  CG   . LEU   A 1 458 ? 3.825  19.022  23.828  1.00 110.23 ? 479 LEU   A CG   1 
ATOM   2979 C  CD1  . LEU   A 1 458 ? 2.534  18.479  24.422  1.00 110.28 ? 479 LEU   A CD1  1 
ATOM   2980 C  CD2  . LEU   A 1 458 ? 4.973  18.895  24.818  1.00 108.22 ? 479 LEU   A CD2  1 
ATOM   2981 N  N    . GLY   A 1 459 ? 5.648  18.874  19.341  1.00 109.66 ? 480 GLY   A N    1 
ATOM   2982 C  CA   . GLY   A 1 459 ? 5.726  18.295  18.016  1.00 115.70 ? 480 GLY   A CA   1 
ATOM   2983 C  C    . GLY   A 1 459 ? 7.134  17.897  17.622  1.00 118.43 ? 480 GLY   A C    1 
ATOM   2984 O  O    . GLY   A 1 459 ? 8.007  17.665  18.463  1.00 114.37 ? 480 GLY   A O    1 
ATOM   2985 N  N    . GLY   A 1 460 ? 7.352  17.819  16.311  1.00 119.37 ? 481 GLY   A N    1 
ATOM   2986 C  CA   . GLY   A 1 460 ? 8.623  17.425  15.745  1.00 112.90 ? 481 GLY   A CA   1 
ATOM   2987 C  C    . GLY   A 1 460 ? 9.541  18.556  15.342  1.00 113.18 ? 481 GLY   A C    1 
ATOM   2988 O  O    . GLY   A 1 460 ? 10.598 18.297  14.760  1.00 113.88 ? 481 GLY   A O    1 
ATOM   2989 N  N    . LEU   A 1 461 ? 9.167  19.802  15.617  1.00 111.31 ? 482 LEU   A N    1 
ATOM   2990 C  CA   . LEU   A 1 461 ? 10.019 20.958  15.382  1.00 109.99 ? 482 LEU   A CA   1 
ATOM   2991 C  C    . LEU   A 1 461 ? 10.382 21.591  16.717  1.00 111.78 ? 482 LEU   A C    1 
ATOM   2992 O  O    . LEU   A 1 461 ? 9.566  21.614  17.644  1.00 118.28 ? 482 LEU   A O    1 
ATOM   2993 C  CB   . LEU   A 1 461 ? 9.324  21.991  14.493  1.00 110.87 ? 482 LEU   A CB   1 
ATOM   2994 C  CG   . LEU   A 1 461 ? 8.834  21.567  13.110  1.00 109.20 ? 482 LEU   A CG   1 
ATOM   2995 C  CD1  . LEU   A 1 461 ? 8.243  22.766  12.387  1.00 110.86 ? 482 LEU   A CD1  1 
ATOM   2996 C  CD2  . LEU   A 1 461 ? 9.964  20.952  12.304  1.00 105.70 ? 482 LEU   A CD2  1 
ATOM   2997 N  N    . LEU   A 1 462 ? 11.606 22.105  16.818  1.00 106.49 ? 483 LEU   A N    1 
ATOM   2998 C  CA   . LEU   A 1 462 ? 12.017 22.822  18.023  1.00 104.70 ? 483 LEU   A CA   1 
ATOM   2999 C  C    . LEU   A 1 462 ? 11.709 24.313  17.877  1.00 105.15 ? 483 LEU   A C    1 
ATOM   3000 O  O    . LEU   A 1 462 ? 12.584 25.178  17.891  1.00 102.36 ? 483 LEU   A O    1 
ATOM   3001 C  CB   . LEU   A 1 462 ? 13.491 22.578  18.326  1.00 95.19  ? 483 LEU   A CB   1 
ATOM   3002 C  CG   . LEU   A 1 462 ? 13.887 22.956  19.758  1.00 96.15  ? 483 LEU   A CG   1 
ATOM   3003 C  CD1  . LEU   A 1 462 ? 12.919 22.342  20.757  1.00 100.43 ? 483 LEU   A CD1  1 
ATOM   3004 C  CD2  . LEU   A 1 462 ? 15.305 22.526  20.075  1.00 88.77  ? 483 LEU   A CD2  1 
ATOM   3005 N  N    . GLN   A 1 463 ? 10.424 24.590  17.714  1.00 108.02 ? 484 GLN   A N    1 
ATOM   3006 C  CA   . GLN   A 1 463 ? 9.855  25.925  17.728  1.00 111.01 ? 484 GLN   A CA   1 
ATOM   3007 C  C    . GLN   A 1 463 ? 8.781  25.988  18.804  1.00 115.15 ? 484 GLN   A C    1 
ATOM   3008 O  O    . GLN   A 1 463 ? 8.210  24.959  19.181  1.00 116.32 ? 484 GLN   A O    1 
ATOM   3009 C  CB   . GLN   A 1 463 ? 9.257  26.288  16.359  1.00 109.22 ? 484 GLN   A CB   1 
ATOM   3010 C  CG   . GLN   A 1 463 ? 8.365  25.213  15.745  1.00 112.59 ? 484 GLN   A CG   1 
ATOM   3011 C  CD   . GLN   A 1 463 ? 6.969  25.179  16.342  1.00 117.40 ? 484 GLN   A CD   1 
ATOM   3012 O  OE1  . GLN   A 1 463 ? 6.324  26.216  16.503  1.00 115.31 ? 484 GLN   A OE1  1 
ATOM   3013 N  NE2  . GLN   A 1 463 ? 6.498  23.983  16.679  1.00 118.37 ? 484 GLN   A NE2  1 
ATOM   3014 N  N    . PRO   A 1 464 ? 8.499  27.167  19.342  1.00 114.40 ? 485 PRO   A N    1 
ATOM   3015 C  CA   . PRO   A 1 464 ? 7.404  27.274  20.313  1.00 113.24 ? 485 PRO   A CA   1 
ATOM   3016 C  C    . PRO   A 1 464 ? 6.058  27.480  19.636  1.00 115.45 ? 485 PRO   A C    1 
ATOM   3017 O  O    . PRO   A 1 464 ? 5.917  28.362  18.783  1.00 115.92 ? 485 PRO   A O    1 
ATOM   3018 C  CB   . PRO   A 1 464 ? 7.807  28.487  21.157  1.00 118.28 ? 485 PRO   A CB   1 
ATOM   3019 C  CG   . PRO   A 1 464 ? 8.577  29.345  20.207  1.00 114.99 ? 485 PRO   A CG   1 
ATOM   3020 C  CD   . PRO   A 1 464 ? 9.283  28.412  19.251  1.00 112.99 ? 485 PRO   A CD   1 
ATOM   3021 N  N    . GLU   A 1 465 ? 5.067  26.660  19.996  1.00 118.96 ? 486 GLU   A N    1 
ATOM   3022 C  CA   . GLU   A 1 465 ? 3.717  26.869  19.481  1.00 120.99 ? 486 GLU   A CA   1 
ATOM   3023 C  C    . GLU   A 1 465 ? 3.194  28.243  19.875  1.00 123.10 ? 486 GLU   A C    1 
ATOM   3024 O  O    . GLU   A 1 465 ? 2.589  28.946  19.057  1.00 122.98 ? 486 GLU   A O    1 
ATOM   3025 C  CB   . GLU   A 1 465 ? 2.783  25.769  19.986  1.00 116.53 ? 486 GLU   A CB   1 
ATOM   3026 N  N    . LYS   A 1 466 ? 3.423  28.643  21.117  1.00 121.97 ? 487 LYS   A N    1 
ATOM   3027 C  CA   . LYS   A 1 466 ? 3.143  30.011  21.530  1.00 123.95 ? 487 LYS   A CA   1 
ATOM   3028 C  C    . LYS   A 1 466 ? 4.153  30.940  20.867  1.00 123.65 ? 487 LYS   A C    1 
ATOM   3029 O  O    . LYS   A 1 466 ? 5.363  30.724  21.012  1.00 120.41 ? 487 LYS   A O    1 
ATOM   3030 C  CB   . LYS   A 1 466 ? 3.213  30.137  23.049  1.00 124.82 ? 487 LYS   A CB   1 
ATOM   3031 N  N    . PRO   A 1 467 ? 3.717  31.962  20.133  1.00 125.39 ? 488 PRO   A N    1 
ATOM   3032 C  CA   . PRO   A 1 467 ? 4.669  32.833  19.432  1.00 124.86 ? 488 PRO   A CA   1 
ATOM   3033 C  C    . PRO   A 1 467 ? 5.526  33.632  20.405  1.00 121.68 ? 488 PRO   A C    1 
ATOM   3034 O  O    . PRO   A 1 467 ? 5.330  33.618  21.621  1.00 123.41 ? 488 PRO   A O    1 
ATOM   3035 C  CB   . PRO   A 1 467 ? 3.770  33.752  18.598  1.00 125.26 ? 488 PRO   A CB   1 
ATOM   3036 C  CG   . PRO   A 1 467 ? 2.457  33.036  18.510  1.00 129.90 ? 488 PRO   A CG   1 
ATOM   3037 C  CD   . PRO   A 1 467 ? 2.322  32.296  19.806  1.00 126.72 ? 488 PRO   A CD   1 
ATOM   3038 N  N    . VAL   A 1 468 ? 6.495  34.345  19.837  1.00 122.37 ? 489 VAL   A N    1 
ATOM   3039 C  CA   . VAL   A 1 468 ? 7.440  35.157  20.595  1.00 124.77 ? 489 VAL   A CA   1 
ATOM   3040 C  C    . VAL   A 1 468 ? 7.099  36.615  20.312  1.00 129.37 ? 489 VAL   A C    1 
ATOM   3041 O  O    . VAL   A 1 468 ? 7.404  37.139  19.235  1.00 130.94 ? 489 VAL   A O    1 
ATOM   3042 C  CB   . VAL   A 1 468 ? 8.894  34.836  20.231  1.00 123.76 ? 489 VAL   A CB   1 
ATOM   3043 C  CG1  . VAL   A 1 468 ? 9.843  35.535  21.192  1.00 121.02 ? 489 VAL   A CG1  1 
ATOM   3044 C  CG2  . VAL   A 1 468 ? 9.123  33.330  20.239  1.00 126.89 ? 489 VAL   A CG2  1 
ATOM   3045 N  N    . VAL   A 1 469 ? 6.455  37.271  21.276  1.00 128.59 ? 490 VAL   A N    1 
ATOM   3046 C  CA   . VAL   A 1 469 ? 6.042  38.665  21.152  1.00 128.98 ? 490 VAL   A CA   1 
ATOM   3047 C  C    . VAL   A 1 469 ? 6.565  39.428  22.361  1.00 130.71 ? 490 VAL   A C    1 
ATOM   3048 O  O    . VAL   A 1 469 ? 6.186  39.128  23.500  1.00 127.83 ? 490 VAL   A O    1 
ATOM   3049 C  CB   . VAL   A 1 469 ? 4.515  38.808  21.043  1.00 130.01 ? 490 VAL   A CB   1 
ATOM   3050 N  N    . LEU   A 1 470 ? 7.424  40.414  22.113  1.00 132.67 ? 491 LEU   A N    1 
ATOM   3051 C  CA   . LEU   A 1 470 ? 8.015  41.235  23.160  1.00 129.67 ? 491 LEU   A CA   1 
ATOM   3052 C  C    . LEU   A 1 470 ? 7.909  42.701  22.767  1.00 131.24 ? 491 LEU   A C    1 
ATOM   3053 O  O    . LEU   A 1 470 ? 7.518  43.042  21.648  1.00 131.93 ? 491 LEU   A O    1 
ATOM   3054 C  CB   . LEU   A 1 470 ? 9.480  40.856  23.413  1.00 125.12 ? 491 LEU   A CB   1 
ATOM   3055 N  N    . LYS   A 1 471 ? 8.273  43.571  23.706  1.00 130.00 ? 492 LYS   A N    1 
ATOM   3056 C  CA   . LYS   A 1 471 ? 8.192  45.011  23.506  1.00 129.47 ? 492 LYS   A CA   1 
ATOM   3057 C  C    . LYS   A 1 471 ? 9.524  45.535  22.984  1.00 125.34 ? 492 LYS   A C    1 
ATOM   3058 O  O    . LYS   A 1 471 ? 10.579 45.234  23.549  1.00 121.18 ? 492 LYS   A O    1 
ATOM   3059 C  CB   . LYS   A 1 471 ? 7.816  45.714  24.811  1.00 125.48 ? 492 LYS   A CB   1 
ATOM   3060 N  N    . VAL   A 1 472 ? 9.468  46.313  21.906  1.00 125.13 ? 493 VAL   A N    1 
ATOM   3061 C  CA   . VAL   A 1 472 ? 10.651 46.882  21.268  1.00 129.38 ? 493 VAL   A CA   1 
ATOM   3062 C  C    . VAL   A 1 472 ? 10.678 48.376  21.564  1.00 136.86 ? 493 VAL   A C    1 
ATOM   3063 O  O    . VAL   A 1 472 ? 9.753  49.108  21.187  1.00 141.01 ? 493 VAL   A O    1 
ATOM   3064 C  CB   . VAL   A 1 472 ? 10.656 46.622  19.754  1.00 127.37 ? 493 VAL   A CB   1 
ATOM   3065 C  CG1  . VAL   A 1 472 ? 11.987 47.036  19.151  1.00 127.80 ? 493 VAL   A CG1  1 
ATOM   3066 C  CG2  . VAL   A 1 472 ? 10.355 45.159  19.463  1.00 128.32 ? 493 VAL   A CG2  1 
ATOM   3067 N  N    . GLU   A 1 473 ? 11.738 48.829  22.229  1.00 137.75 ? 494 GLU   A N    1 
ATOM   3068 C  CA   . GLU   A 1 473 ? 11.920 50.228  22.585  1.00 138.38 ? 494 GLU   A CA   1 
ATOM   3069 C  C    . GLU   A 1 473 ? 13.093 50.813  21.807  1.00 137.39 ? 494 GLU   A C    1 
ATOM   3070 O  O    . GLU   A 1 473 ? 14.086 50.128  21.547  1.00 137.98 ? 494 GLU   A O    1 
ATOM   3071 C  CB   . GLU   A 1 473 ? 12.160 50.384  24.091  1.00 135.92 ? 494 GLU   A CB   1 
ATOM   3072 C  CG   . GLU   A 1 473 ? 11.176 49.622  24.979  1.00 132.91 ? 494 GLU   A CG   1 
ATOM   3073 C  CD   . GLU   A 1 473 ? 9.871  50.368  25.209  1.00 141.57 ? 494 GLU   A CD   1 
ATOM   3074 O  OE1  . GLU   A 1 473 ? 9.309  50.919  24.239  1.00 144.24 ? 494 GLU   A OE1  1 
ATOM   3075 O  OE2  . GLU   A 1 473 ? 9.407  50.406  26.369  1.00 147.59 ? 494 GLU   A OE2  1 
ATOM   3076 N  N    . SER   A 1 474 ? 12.977 52.090  21.444  1.00 136.34 ? 495 SER   A N    1 
ATOM   3077 C  CA   . SER   A 1 474 ? 13.977 52.755  20.618  1.00 132.22 ? 495 SER   A CA   1 
ATOM   3078 C  C    . SER   A 1 474 ? 15.030 53.415  21.512  1.00 129.91 ? 495 SER   A C    1 
ATOM   3079 O  O    . SER   A 1 474 ? 15.129 53.117  22.705  1.00 131.21 ? 495 SER   A O    1 
ATOM   3080 C  CB   . SER   A 1 474 ? 13.294 53.756  19.680  1.00 130.92 ? 495 SER   A CB   1 
ATOM   3081 O  OG   . SER   A 1 474 ? 14.248 54.451  18.894  1.00 125.74 ? 495 SER   A OG   1 
ATOM   3082 N  N    . ARG   A 1 475 ? 15.829 54.316  20.945  1.00 127.35 ? 496 ARG   A N    1 
ATOM   3083 C  CA   . ARG   A 1 475 ? 16.872 55.004  21.697  1.00 126.99 ? 496 ARG   A CA   1 
ATOM   3084 C  C    . ARG   A 1 475 ? 17.086 56.417  21.164  1.00 123.47 ? 496 ARG   A C    1 
ATOM   3085 O  O    . ARG   A 1 475 ? 16.183 57.011  20.575  1.00 114.96 ? 496 ARG   A O    1 
ATOM   3086 C  CB   . ARG   A 1 475 ? 18.182 54.216  21.643  1.00 123.60 ? 496 ARG   A CB   1 
HETATM 3087 C  CHA  . HEM   B 2 .   ? 22.763 20.057  7.881   1.00 72.76  ? 601 HEM   A CHA  1 
HETATM 3088 C  CHB  . HEM   B 2 .   ? 22.167 22.951  11.804  1.00 74.05  ? 601 HEM   A CHB  1 
HETATM 3089 C  CHC  . HEM   B 2 .   ? 21.652 26.699  8.764   1.00 84.54  ? 601 HEM   A CHC  1 
HETATM 3090 C  CHD  . HEM   B 2 .   ? 22.770 23.950  4.962   1.00 77.30  ? 601 HEM   A CHD  1 
HETATM 3091 C  C1A  . HEM   B 2 .   ? 22.615 20.509  9.186   1.00 71.37  ? 601 HEM   A C1A  1 
HETATM 3092 C  C2A  . HEM   B 2 .   ? 22.597 19.676  10.371  1.00 65.46  ? 601 HEM   A C2A  1 
HETATM 3093 C  C3A  . HEM   B 2 .   ? 22.436 20.483  11.432  1.00 66.17  ? 601 HEM   A C3A  1 
HETATM 3094 C  C4A  . HEM   B 2 .   ? 22.342 21.844  10.980  1.00 71.43  ? 601 HEM   A C4A  1 
HETATM 3095 C  CMA  . HEM   B 2 .   ? 22.356 20.063  12.908  1.00 70.20  ? 601 HEM   A CMA  1 
HETATM 3096 C  CAA  . HEM   B 2 .   ? 22.745 18.131  10.417  1.00 61.49  ? 601 HEM   A CAA  1 
HETATM 3097 C  CBA  . HEM   B 2 .   ? 24.207 17.713  10.348  1.00 58.76  ? 601 HEM   A CBA  1 
HETATM 3098 C  CGA  . HEM   B 2 .   ? 24.341 16.266  10.703  1.00 56.35  ? 601 HEM   A CGA  1 
HETATM 3099 O  O1A  . HEM   B 2 .   ? 23.614 15.431  10.076  1.00 56.87  ? 601 HEM   A O1A  1 
HETATM 3100 O  O2A  . HEM   B 2 .   ? 25.271 15.886  11.469  1.00 58.93  ? 601 HEM   A O2A  1 
HETATM 3101 C  C1B  . HEM   B 2 .   ? 21.934 24.219  11.315  1.00 73.66  ? 601 HEM   A C1B  1 
HETATM 3102 C  C2B  . HEM   B 2 .   ? 21.592 25.396  12.092  1.00 78.97  ? 601 HEM   A C2B  1 
HETATM 3103 C  C3B  . HEM   B 2 .   ? 21.454 26.434  11.258  1.00 80.81  ? 601 HEM   A C3B  1 
HETATM 3104 C  C4B  . HEM   B 2 .   ? 21.699 25.938  9.910   1.00 78.25  ? 601 HEM   A C4B  1 
HETATM 3105 C  CMB  . HEM   B 2 .   ? 21.438 25.397  13.638  1.00 81.59  ? 601 HEM   A CMB  1 
HETATM 3106 C  CAB  . HEM   B 2 .   ? 21.099 27.904  11.556  1.00 85.03  ? 601 HEM   A CAB  1 
HETATM 3107 C  CBB  . HEM   B 2 .   ? 21.331 28.556  12.699  1.00 87.41  ? 601 HEM   A CBB  1 
HETATM 3108 C  C1C  . HEM   B 2 .   ? 21.920 26.294  7.487   1.00 83.65  ? 601 HEM   A C1C  1 
HETATM 3109 C  C2C  . HEM   B 2 .   ? 21.904 27.144  6.321   1.00 82.54  ? 601 HEM   A C2C  1 
HETATM 3110 C  C3C  . HEM   B 2 .   ? 22.216 26.384  5.256   1.00 78.40  ? 601 HEM   A C3C  1 
HETATM 3111 C  C4C  . HEM   B 2 .   ? 22.434 25.047  5.723   1.00 78.42  ? 601 HEM   A C4C  1 
HETATM 3112 C  CMC  . HEM   B 2 .   ? 21.579 28.644  6.370   1.00 87.40  ? 601 HEM   A CMC  1 
HETATM 3113 C  CAC  . HEM   B 2 .   ? 22.341 26.773  3.769   1.00 85.45  ? 601 HEM   A CAC  1 
HETATM 3114 C  CBC  . HEM   B 2 .   ? 21.824 27.881  3.237   1.00 87.04  ? 601 HEM   A CBC  1 
HETATM 3115 C  C1D  . HEM   B 2 .   ? 22.823 22.664  5.438   1.00 76.61  ? 601 HEM   A C1D  1 
HETATM 3116 C  C2D  . HEM   B 2 .   ? 23.013 21.493  4.636   1.00 73.20  ? 601 HEM   A C2D  1 
HETATM 3117 C  C3D  . HEM   B 2 .   ? 23.022 20.409  5.407   1.00 77.90  ? 601 HEM   A C3D  1 
HETATM 3118 C  C4D  . HEM   B 2 .   ? 22.823 20.855  6.775   1.00 75.25  ? 601 HEM   A C4D  1 
HETATM 3119 C  CMD  . HEM   B 2 .   ? 23.190 21.559  3.104   1.00 73.16  ? 601 HEM   A CMD  1 
HETATM 3120 C  CAD  . HEM   B 2 .   ? 23.198 18.955  4.946   1.00 75.96  ? 601 HEM   A CAD  1 
HETATM 3121 C  CBD  . HEM   B 2 .   ? 24.677 18.597  4.927   1.00 73.37  ? 601 HEM   A CBD  1 
HETATM 3122 C  CGD  . HEM   B 2 .   ? 24.926 17.402  4.035   1.00 70.70  ? 601 HEM   A CGD  1 
HETATM 3123 O  O1D  . HEM   B 2 .   ? 24.093 16.457  4.101   1.00 71.07  ? 601 HEM   A O1D  1 
HETATM 3124 O  O2D  . HEM   B 2 .   ? 25.985 17.337  3.343   1.00 72.26  ? 601 HEM   A O2D  1 
HETATM 3125 N  NA   . HEM   B 2 .   ? 22.453 21.821  9.601   1.00 69.25  ? 601 HEM   A NA   1 
HETATM 3126 N  NB   . HEM   B 2 .   ? 21.986 24.594  9.994   1.00 73.62  ? 601 HEM   A NB   1 
HETATM 3127 N  NC   . HEM   B 2 .   ? 22.247 25.023  7.077   1.00 77.70  ? 601 HEM   A NC   1 
HETATM 3128 N  ND   . HEM   B 2 .   ? 22.710 22.241  6.742   1.00 78.99  ? 601 HEM   A ND   1 
HETATM 3129 FE FE   . HEM   B 2 .   ? 22.405 23.452  8.368   1.00 65.76  ? 601 HEM   A FE   1 
HETATM 3130 C  C12  . A1BNX C 3 .   ? 16.423 19.255  8.513   1.00 106.36 ? 602 A1BNX A C12  1 
HETATM 3131 C  C13  . A1BNX C 3 .   ? 15.855 20.502  9.186   1.00 101.43 ? 602 A1BNX A C13  1 
HETATM 3132 C  C14  . A1BNX C 3 .   ? 16.668 21.272  9.997   1.00 98.21  ? 602 A1BNX A C14  1 
HETATM 3133 C  C15  . A1BNX C 3 .   ? 16.150 22.398  10.614  1.00 101.70 ? 602 A1BNX A C15  1 
HETATM 3134 C  C16  . A1BNX C 3 .   ? 14.822 22.741  10.428  1.00 105.74 ? 602 A1BNX A C16  1 
HETATM 3135 C  C21  . A1BNX C 3 .   ? 15.932 19.868  5.521   1.00 103.37 ? 602 A1BNX A C21  1 
HETATM 3136 C  C20  . A1BNX C 3 .   ? 16.898 20.395  6.356   1.00 102.03 ? 602 A1BNX A C20  1 
HETATM 3137 C  C17  . A1BNX C 3 .   ? 14.008 21.963  9.624   1.00 105.86 ? 602 A1BNX A C17  1 
HETATM 3138 C  C23  . A1BNX C 3 .   ? 14.358 19.997  3.576   1.00 103.49 ? 602 A1BNX A C23  1 
HETATM 3139 C  C02  . A1BNX C 3 .   ? 18.675 18.881  7.274   1.00 94.86  ? 602 A1BNX A C02  1 
HETATM 3140 C  C04  . A1BNX C 3 .   ? 18.689 17.485  9.447   1.00 96.91  ? 602 A1BNX A C04  1 
HETATM 3141 C  C05  . A1BNX C 3 .   ? 18.943 18.149  10.632  1.00 92.25  ? 602 A1BNX A C05  1 
HETATM 3142 C  C06  . A1BNX C 3 .   ? 18.357 17.706  11.802  1.00 102.23 ? 602 A1BNX A C06  1 
HETATM 3143 C  C07  . A1BNX C 3 .   ? 17.519 16.605  11.789  1.00 105.86 ? 602 A1BNX A C07  1 
HETATM 3144 C  C08  . A1BNX C 3 .   ? 17.265 15.944  10.600  1.00 103.50 ? 602 A1BNX A C08  1 
HETATM 3145 C  C09  . A1BNX C 3 .   ? 17.850 16.384  9.426   1.00 102.80 ? 602 A1BNX A C09  1 
HETATM 3146 C  C19  . A1BNX C 3 .   ? 14.524 20.839  9.004   1.00 99.57  ? 602 A1BNX A C19  1 
HETATM 3147 C  C22  . A1BNX C 3 .   ? 15.422 20.609  4.478   1.00 101.48 ? 602 A1BNX A C22  1 
HETATM 3148 C  C27  . A1BNX C 3 .   ? 15.890 21.893  4.266   1.00 100.74 ? 602 A1BNX A C27  1 
HETATM 3149 C  C28  . A1BNX C 3 .   ? 16.859 22.428  5.103   1.00 97.59  ? 602 A1BNX A C28  1 
HETATM 3150 C  C29  . A1BNX C 3 .   ? 17.372 21.691  6.155   1.00 95.42  ? 602 A1BNX A C29  1 
HETATM 3151 C  C31  . A1BNX C 3 .   ? 18.110 23.179  7.827   1.00 90.24  ? 602 A1BNX A C31  1 
HETATM 3152 C  C32  . A1BNX C 3 .   ? 19.353 23.489  8.358   1.00 86.75  ? 602 A1BNX A C32  1 
HETATM 3153 C  C34  . A1BNX C 3 .   ? 19.598 22.012  6.853   1.00 88.87  ? 602 A1BNX A C34  1 
HETATM 3154 F  F24  . A1BNX C 3 .   ? 14.686 20.228  2.279   1.00 110.85 ? 602 A1BNX A F24  1 
HETATM 3155 F  F25  . A1BNX C 3 .   ? 13.154 20.568  3.851   1.00 95.80  ? 602 A1BNX A F25  1 
HETATM 3156 F  F26  . A1BNX C 3 .   ? 14.295 18.658  3.808   1.00 105.85 ? 602 A1BNX A F26  1 
HETATM 3157 N  N03  . A1BNX C 3 .   ? 19.297 17.953  8.217   1.00 93.88  ? 602 A1BNX A N03  1 
HETATM 3158 N  N11  . A1BNX C 3 .   ? 17.353 19.514  7.417   1.00 105.54 ? 602 A1BNX A N11  1 
HETATM 3159 N  N30  . A1BNX C 3 .   ? 18.301 22.252  6.913   1.00 89.71  ? 602 A1BNX A N30  1 
HETATM 3160 N  N33  . A1BNX C 3 .   ? 20.248 22.749  7.734   1.00 83.67  ? 602 A1BNX A N33  1 
HETATM 3161 O  O01  . A1BNX C 3 .   ? 19.315 19.156  6.318   1.00 88.80  ? 602 A1BNX A O01  1 
HETATM 3162 O  O18  . A1BNX C 3 .   ? 12.667 22.323  9.443   1.00 110.20 ? 602 A1BNX A O18  1 
HETATM 3163 CL CL10 . A1BNX C 3 .   ? 17.520 15.535  7.890   1.00 114.65 ? 602 A1BNX A CL10 1 
# 
