data_9COR
# 
_entry.id   9COR 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9COR         pdb_00009cor 10.2210/pdb9cor/pdb 
WWPDB D_1000285829 ?            ?                   
# 
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 2025-01-08 ? 
2 'Structure model' 1 1 2025-03-05 ? 
# 
_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' 
# 
_pdbx_audit_revision_category.ordinal             1 
_pdbx_audit_revision_category.revision_ordinal    2 
_pdbx_audit_revision_category.data_content_type   'Structure model' 
_pdbx_audit_revision_category.category            citation 
# 
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_DOI'    
5 2 'Structure model' '_citation.pdbx_database_id_PubMed' 
6 2 'Structure model' '_citation.title'                   
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9COR 
_pdbx_database_status.recvd_initial_deposition_date   2024-07-17 
_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_contact_author.id                 2 
_pdbx_contact_author.email              sevrioui@uci.edu 
_pdbx_contact_author.name_first         Irina 
_pdbx_contact_author.name_last          Sevrioukova 
_pdbx_contact_author.name_mi            F 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-4498-6057 
# 
_audit_author.name               'Sevrioukova, I.F.' 
_audit_author.pdbx_ordinal       1 
_audit_author.identifier_ORCID   0000-0002-4498-6057 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Chem.Biol.Drug Des.' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           1747-0285 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            105 
_citation.language                  ? 
_citation.page_first                e70043 
_citation.page_last                 e70043 
_citation.title                     
'Evaluation of Larger Side-Group Functionalities and the Side/End-Group Interplay in Ritonavir-Like Inhibitors of CYP3A4.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1111/cbdd.70043 
_citation.pdbx_database_id_PubMed   39792691 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Samuels, E.R.'     1 ?                   
primary 'Sevrioukova, I.F.' 2 0000-0002-4498-6057 
# 
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' 55757.812 1 1.14.14.1,1.14.14.56,1.14.14.73,1.14.14.55 
'residues 3-22 deleted, C-terminal 4-histidine tag' ? ? 
2 non-polymer nat 'PROTOPORPHYRIN IX CONTAINING FE' 616.487   1 ?                                          ? ? ? 
3 non-polymer syn 
'(2R)-3-phenyl-2-{[(2S)-3-phenyl-2-{[N-(trifluoroacetyl)glycyl]amino}propyl]sulfanyl}-N-[2-(pyridin-3-yl)ethyl]propanamide' 
572.642   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       
;MAYLYGTHSHGLFKKLGIPGPTPLPFLGNILSYHKGFCMFDMECHKKYGKVWGFYDGQQPVLAITDPDMIKTVLVKECYS
VFTNRRPFGPVGFMKSAISIAEDEEWKRLRSLLSPTFTSGKLKEMVPIIAQYGDVLVRNLRREAETGKPVTLKDVFGAYS
MDVITSTSFGVNIDSLNNPQDPFVENTKKLLRFDFLDPFFLSITVFPFLIPILEVLNICVFPREVTNFLRKSVKRMKESR
LEDTQKHRVDFLQLMIDSQNSKETESHKALSDLELVAQSIIFIFAGYETTSSVLSFIMYELATHPDVQQKLQEEIDAVLP
NKAPPTYDTVLQMEYLDMVVNETLRLFPIAMRLERVCKKDVEINGMFIPKGVVVMIPSYALHRDPKYWTEPEKFLPERFS
KKNKDNIDPYIYTPFGSGPRNCIGMRFALMNMKLALIRVLQNFSFKPCKETQIPLKLSLGGLLQPEKPVVLKVESRDGTV
SGAHHHH
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MAYLYGTHSHGLFKKLGIPGPTPLPFLGNILSYHKGFCMFDMECHKKYGKVWGFYDGQQPVLAITDPDMIKTVLVKECYS
VFTNRRPFGPVGFMKSAISIAEDEEWKRLRSLLSPTFTSGKLKEMVPIIAQYGDVLVRNLRREAETGKPVTLKDVFGAYS
MDVITSTSFGVNIDSLNNPQDPFVENTKKLLRFDFLDPFFLSITVFPFLIPILEVLNICVFPREVTNFLRKSVKRMKESR
LEDTQKHRVDFLQLMIDSQNSKETESHKALSDLELVAQSIIFIFAGYETTSSVLSFIMYELATHPDVQQKLQEEIDAVLP
NKAPPTYDTVLQMEYLDMVVNETLRLFPIAMRLERVCKKDVEINGMFIPKGVVVMIPSYALHRDPKYWTEPEKFLPERFS
KKNKDNIDPYIYTPFGSGPRNCIGMRFALMNMKLALIRVLQNFSFKPCKETQIPLKLSLGGLLQPEKPVVLKVESRDGTV
SGAHHHH
;
_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 '(2R)-3-phenyl-2-{[(2S)-3-phenyl-2-{[N-(trifluoroacetyl)glycyl]amino}propyl]sulfanyl}-N-[2-(pyridin-3-yl)ethyl]propanamide' 
A1A07 
# 
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   TYR n 
1 4   LEU n 
1 5   TYR n 
1 6   GLY n 
1 7   THR n 
1 8   HIS n 
1 9   SER n 
1 10  HIS n 
1 11  GLY n 
1 12  LEU n 
1 13  PHE n 
1 14  LYS n 
1 15  LYS n 
1 16  LEU n 
1 17  GLY n 
1 18  ILE n 
1 19  PRO n 
1 20  GLY n 
1 21  PRO n 
1 22  THR n 
1 23  PRO n 
1 24  LEU n 
1 25  PRO n 
1 26  PHE n 
1 27  LEU n 
1 28  GLY n 
1 29  ASN n 
1 30  ILE n 
1 31  LEU n 
1 32  SER n 
1 33  TYR n 
1 34  HIS n 
1 35  LYS n 
1 36  GLY n 
1 37  PHE n 
1 38  CYS n 
1 39  MET n 
1 40  PHE n 
1 41  ASP n 
1 42  MET n 
1 43  GLU n 
1 44  CYS n 
1 45  HIS n 
1 46  LYS n 
1 47  LYS n 
1 48  TYR n 
1 49  GLY n 
1 50  LYS n 
1 51  VAL n 
1 52  TRP n 
1 53  GLY n 
1 54  PHE n 
1 55  TYR n 
1 56  ASP n 
1 57  GLY n 
1 58  GLN n 
1 59  GLN n 
1 60  PRO n 
1 61  VAL n 
1 62  LEU n 
1 63  ALA n 
1 64  ILE n 
1 65  THR n 
1 66  ASP n 
1 67  PRO n 
1 68  ASP n 
1 69  MET n 
1 70  ILE n 
1 71  LYS n 
1 72  THR n 
1 73  VAL n 
1 74  LEU n 
1 75  VAL n 
1 76  LYS n 
1 77  GLU n 
1 78  CYS n 
1 79  TYR n 
1 80  SER n 
1 81  VAL n 
1 82  PHE n 
1 83  THR n 
1 84  ASN n 
1 85  ARG n 
1 86  ARG n 
1 87  PRO n 
1 88  PHE n 
1 89  GLY n 
1 90  PRO n 
1 91  VAL n 
1 92  GLY n 
1 93  PHE n 
1 94  MET n 
1 95  LYS n 
1 96  SER n 
1 97  ALA n 
1 98  ILE n 
1 99  SER n 
1 100 ILE n 
1 101 ALA n 
1 102 GLU n 
1 103 ASP n 
1 104 GLU n 
1 105 GLU n 
1 106 TRP n 
1 107 LYS n 
1 108 ARG n 
1 109 LEU n 
1 110 ARG n 
1 111 SER n 
1 112 LEU n 
1 113 LEU n 
1 114 SER n 
1 115 PRO n 
1 116 THR n 
1 117 PHE n 
1 118 THR n 
1 119 SER n 
1 120 GLY n 
1 121 LYS n 
1 122 LEU n 
1 123 LYS n 
1 124 GLU n 
1 125 MET n 
1 126 VAL n 
1 127 PRO n 
1 128 ILE n 
1 129 ILE n 
1 130 ALA n 
1 131 GLN n 
1 132 TYR n 
1 133 GLY n 
1 134 ASP n 
1 135 VAL n 
1 136 LEU n 
1 137 VAL n 
1 138 ARG n 
1 139 ASN n 
1 140 LEU n 
1 141 ARG n 
1 142 ARG n 
1 143 GLU n 
1 144 ALA n 
1 145 GLU n 
1 146 THR n 
1 147 GLY n 
1 148 LYS n 
1 149 PRO n 
1 150 VAL n 
1 151 THR n 
1 152 LEU n 
1 153 LYS n 
1 154 ASP n 
1 155 VAL n 
1 156 PHE n 
1 157 GLY n 
1 158 ALA n 
1 159 TYR n 
1 160 SER n 
1 161 MET n 
1 162 ASP n 
1 163 VAL n 
1 164 ILE n 
1 165 THR n 
1 166 SER n 
1 167 THR n 
1 168 SER n 
1 169 PHE n 
1 170 GLY n 
1 171 VAL n 
1 172 ASN n 
1 173 ILE n 
1 174 ASP n 
1 175 SER n 
1 176 LEU n 
1 177 ASN n 
1 178 ASN n 
1 179 PRO n 
1 180 GLN n 
1 181 ASP n 
1 182 PRO n 
1 183 PHE n 
1 184 VAL n 
1 185 GLU n 
1 186 ASN n 
1 187 THR n 
1 188 LYS n 
1 189 LYS n 
1 190 LEU n 
1 191 LEU n 
1 192 ARG n 
1 193 PHE n 
1 194 ASP n 
1 195 PHE n 
1 196 LEU n 
1 197 ASP n 
1 198 PRO n 
1 199 PHE n 
1 200 PHE n 
1 201 LEU n 
1 202 SER n 
1 203 ILE n 
1 204 THR n 
1 205 VAL n 
1 206 PHE n 
1 207 PRO n 
1 208 PHE n 
1 209 LEU n 
1 210 ILE n 
1 211 PRO n 
1 212 ILE n 
1 213 LEU n 
1 214 GLU n 
1 215 VAL n 
1 216 LEU n 
1 217 ASN n 
1 218 ILE n 
1 219 CYS n 
1 220 VAL n 
1 221 PHE n 
1 222 PRO n 
1 223 ARG n 
1 224 GLU n 
1 225 VAL n 
1 226 THR n 
1 227 ASN n 
1 228 PHE n 
1 229 LEU n 
1 230 ARG n 
1 231 LYS n 
1 232 SER n 
1 233 VAL n 
1 234 LYS n 
1 235 ARG n 
1 236 MET n 
1 237 LYS n 
1 238 GLU n 
1 239 SER n 
1 240 ARG n 
1 241 LEU n 
1 242 GLU n 
1 243 ASP n 
1 244 THR n 
1 245 GLN n 
1 246 LYS n 
1 247 HIS n 
1 248 ARG n 
1 249 VAL n 
1 250 ASP n 
1 251 PHE n 
1 252 LEU n 
1 253 GLN n 
1 254 LEU n 
1 255 MET n 
1 256 ILE n 
1 257 ASP n 
1 258 SER n 
1 259 GLN n 
1 260 ASN n 
1 261 SER n 
1 262 LYS n 
1 263 GLU n 
1 264 THR n 
1 265 GLU n 
1 266 SER n 
1 267 HIS n 
1 268 LYS n 
1 269 ALA n 
1 270 LEU n 
1 271 SER n 
1 272 ASP n 
1 273 LEU n 
1 274 GLU n 
1 275 LEU n 
1 276 VAL n 
1 277 ALA n 
1 278 GLN n 
1 279 SER n 
1 280 ILE n 
1 281 ILE n 
1 282 PHE n 
1 283 ILE n 
1 284 PHE n 
1 285 ALA n 
1 286 GLY n 
1 287 TYR n 
1 288 GLU n 
1 289 THR n 
1 290 THR n 
1 291 SER n 
1 292 SER n 
1 293 VAL n 
1 294 LEU n 
1 295 SER n 
1 296 PHE n 
1 297 ILE n 
1 298 MET n 
1 299 TYR n 
1 300 GLU n 
1 301 LEU n 
1 302 ALA n 
1 303 THR n 
1 304 HIS n 
1 305 PRO n 
1 306 ASP n 
1 307 VAL n 
1 308 GLN n 
1 309 GLN n 
1 310 LYS n 
1 311 LEU n 
1 312 GLN n 
1 313 GLU n 
1 314 GLU n 
1 315 ILE n 
1 316 ASP n 
1 317 ALA n 
1 318 VAL n 
1 319 LEU n 
1 320 PRO n 
1 321 ASN n 
1 322 LYS n 
1 323 ALA n 
1 324 PRO n 
1 325 PRO n 
1 326 THR n 
1 327 TYR n 
1 328 ASP n 
1 329 THR n 
1 330 VAL n 
1 331 LEU n 
1 332 GLN n 
1 333 MET n 
1 334 GLU n 
1 335 TYR n 
1 336 LEU n 
1 337 ASP n 
1 338 MET n 
1 339 VAL n 
1 340 VAL n 
1 341 ASN n 
1 342 GLU n 
1 343 THR n 
1 344 LEU n 
1 345 ARG n 
1 346 LEU n 
1 347 PHE n 
1 348 PRO n 
1 349 ILE n 
1 350 ALA n 
1 351 MET n 
1 352 ARG n 
1 353 LEU n 
1 354 GLU n 
1 355 ARG n 
1 356 VAL n 
1 357 CYS n 
1 358 LYS n 
1 359 LYS n 
1 360 ASP n 
1 361 VAL n 
1 362 GLU n 
1 363 ILE n 
1 364 ASN n 
1 365 GLY n 
1 366 MET n 
1 367 PHE n 
1 368 ILE n 
1 369 PRO n 
1 370 LYS n 
1 371 GLY n 
1 372 VAL n 
1 373 VAL n 
1 374 VAL n 
1 375 MET n 
1 376 ILE n 
1 377 PRO n 
1 378 SER n 
1 379 TYR n 
1 380 ALA n 
1 381 LEU n 
1 382 HIS n 
1 383 ARG n 
1 384 ASP n 
1 385 PRO n 
1 386 LYS n 
1 387 TYR n 
1 388 TRP n 
1 389 THR n 
1 390 GLU n 
1 391 PRO n 
1 392 GLU n 
1 393 LYS n 
1 394 PHE n 
1 395 LEU n 
1 396 PRO n 
1 397 GLU n 
1 398 ARG n 
1 399 PHE n 
1 400 SER n 
1 401 LYS n 
1 402 LYS n 
1 403 ASN n 
1 404 LYS n 
1 405 ASP n 
1 406 ASN n 
1 407 ILE n 
1 408 ASP n 
1 409 PRO n 
1 410 TYR n 
1 411 ILE n 
1 412 TYR n 
1 413 THR n 
1 414 PRO n 
1 415 PHE n 
1 416 GLY n 
1 417 SER n 
1 418 GLY n 
1 419 PRO n 
1 420 ARG n 
1 421 ASN n 
1 422 CYS n 
1 423 ILE n 
1 424 GLY n 
1 425 MET n 
1 426 ARG n 
1 427 PHE n 
1 428 ALA n 
1 429 LEU n 
1 430 MET n 
1 431 ASN n 
1 432 MET n 
1 433 LYS n 
1 434 LEU n 
1 435 ALA n 
1 436 LEU n 
1 437 ILE n 
1 438 ARG n 
1 439 VAL n 
1 440 LEU n 
1 441 GLN n 
1 442 ASN n 
1 443 PHE n 
1 444 SER n 
1 445 PHE n 
1 446 LYS n 
1 447 PRO n 
1 448 CYS n 
1 449 LYS n 
1 450 GLU n 
1 451 THR n 
1 452 GLN n 
1 453 ILE n 
1 454 PRO n 
1 455 LEU n 
1 456 LYS n 
1 457 LEU n 
1 458 SER n 
1 459 LEU n 
1 460 GLY n 
1 461 GLY n 
1 462 LEU n 
1 463 LEU n 
1 464 GLN n 
1 465 PRO n 
1 466 GLU n 
1 467 LYS n 
1 468 PRO n 
1 469 VAL n 
1 470 VAL n 
1 471 LEU n 
1 472 LYS n 
1 473 VAL n 
1 474 GLU n 
1 475 SER n 
1 476 ARG n 
1 477 ASP n 
1 478 GLY n 
1 479 THR n 
1 480 VAL n 
1 481 SER n 
1 482 GLY n 
1 483 ALA n 
1 484 HIS n 
1 485 HIS n 
1 486 HIS n 
1 487 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                   487 
_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 BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              C41 
_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          pcWori 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
A1A07 non-polymer         . 
'(2R)-3-phenyl-2-{[(2S)-3-phenyl-2-{[N-(trifluoroacetyl)glycyl]amino}propyl]sulfanyl}-N-[2-(pyridin-3-yl)ethyl]propanamide' ?    
'C29 H31 F3 N4 O3 S' 572.642 
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   1   ?   ?   ?   A . n 
A 1 2   ALA 2   2   ?   ?   ?   A . n 
A 1 3   TYR 3   23  ?   ?   ?   A . n 
A 1 4   LEU 4   24  ?   ?   ?   A . n 
A 1 5   TYR 5   25  ?   ?   ?   A . n 
A 1 6   GLY 6   26  ?   ?   ?   A . n 
A 1 7   THR 7   27  ?   ?   ?   A . n 
A 1 8   HIS 8   28  28  HIS HIS A . n 
A 1 9   SER 9   29  29  SER SER A . n 
A 1 10  HIS 10  30  30  HIS HIS A . n 
A 1 11  GLY 11  31  31  GLY GLY A . n 
A 1 12  LEU 12  32  32  LEU LEU A . n 
A 1 13  PHE 13  33  33  PHE PHE A . n 
A 1 14  LYS 14  34  34  LYS LYS A . n 
A 1 15  LYS 15  35  35  LYS LYS A . n 
A 1 16  LEU 16  36  36  LEU LEU A . n 
A 1 17  GLY 17  37  37  GLY GLY A . n 
A 1 18  ILE 18  38  38  ILE ILE A . n 
A 1 19  PRO 19  39  39  PRO PRO A . n 
A 1 20  GLY 20  40  40  GLY GLY A . n 
A 1 21  PRO 21  41  41  PRO PRO A . n 
A 1 22  THR 22  42  42  THR THR A . n 
A 1 23  PRO 23  43  43  PRO PRO A . n 
A 1 24  LEU 24  44  44  LEU LEU A . n 
A 1 25  PRO 25  45  45  PRO PRO A . n 
A 1 26  PHE 26  46  46  PHE PHE A . n 
A 1 27  LEU 27  47  47  LEU LEU A . n 
A 1 28  GLY 28  48  48  GLY GLY A . n 
A 1 29  ASN 29  49  49  ASN ASN A . n 
A 1 30  ILE 30  50  50  ILE ILE A . n 
A 1 31  LEU 31  51  51  LEU LEU A . n 
A 1 32  SER 32  52  52  SER SER A . n 
A 1 33  TYR 33  53  53  TYR TYR A . n 
A 1 34  HIS 34  54  54  HIS HIS A . n 
A 1 35  LYS 35  55  55  LYS LYS A . n 
A 1 36  GLY 36  56  56  GLY GLY A . n 
A 1 37  PHE 37  57  57  PHE PHE A . n 
A 1 38  CYS 38  58  58  CYS CYS A . n 
A 1 39  MET 39  59  59  MET MET A . n 
A 1 40  PHE 40  60  60  PHE PHE A . n 
A 1 41  ASP 41  61  61  ASP ASP A . n 
A 1 42  MET 42  62  62  MET MET A . n 
A 1 43  GLU 43  63  63  GLU GLU A . n 
A 1 44  CYS 44  64  64  CYS CYS A . n 
A 1 45  HIS 45  65  65  HIS HIS A . n 
A 1 46  LYS 46  66  66  LYS LYS A . n 
A 1 47  LYS 47  67  67  LYS LYS A . n 
A 1 48  TYR 48  68  68  TYR TYR A . n 
A 1 49  GLY 49  69  69  GLY GLY A . n 
A 1 50  LYS 50  70  70  LYS LYS A . n 
A 1 51  VAL 51  71  71  VAL VAL A . n 
A 1 52  TRP 52  72  72  TRP TRP A . n 
A 1 53  GLY 53  73  73  GLY GLY A . n 
A 1 54  PHE 54  74  74  PHE PHE A . n 
A 1 55  TYR 55  75  75  TYR TYR A . n 
A 1 56  ASP 56  76  76  ASP ASP A . n 
A 1 57  GLY 57  77  77  GLY GLY A . n 
A 1 58  GLN 58  78  78  GLN GLN A . n 
A 1 59  GLN 59  79  79  GLN GLN A . n 
A 1 60  PRO 60  80  80  PRO PRO A . n 
A 1 61  VAL 61  81  81  VAL VAL A . n 
A 1 62  LEU 62  82  82  LEU LEU A . n 
A 1 63  ALA 63  83  83  ALA ALA A . n 
A 1 64  ILE 64  84  84  ILE ILE A . n 
A 1 65  THR 65  85  85  THR THR A . n 
A 1 66  ASP 66  86  86  ASP ASP A . n 
A 1 67  PRO 67  87  87  PRO PRO A . n 
A 1 68  ASP 68  88  88  ASP ASP A . n 
A 1 69  MET 69  89  89  MET MET A . n 
A 1 70  ILE 70  90  90  ILE ILE A . n 
A 1 71  LYS 71  91  91  LYS LYS A . n 
A 1 72  THR 72  92  92  THR THR A . n 
A 1 73  VAL 73  93  93  VAL VAL A . n 
A 1 74  LEU 74  94  94  LEU LEU A . n 
A 1 75  VAL 75  95  95  VAL VAL A . n 
A 1 76  LYS 76  96  96  LYS LYS A . n 
A 1 77  GLU 77  97  97  GLU GLU A . n 
A 1 78  CYS 78  98  98  CYS CYS A . n 
A 1 79  TYR 79  99  99  TYR TYR A . n 
A 1 80  SER 80  100 100 SER SER A . n 
A 1 81  VAL 81  101 101 VAL VAL A . n 
A 1 82  PHE 82  102 102 PHE PHE A . n 
A 1 83  THR 83  103 103 THR THR A . n 
A 1 84  ASN 84  104 104 ASN ASN A . n 
A 1 85  ARG 85  105 105 ARG ARG A . n 
A 1 86  ARG 86  106 106 ARG ARG A . n 
A 1 87  PRO 87  107 107 PRO PRO A . n 
A 1 88  PHE 88  108 108 PHE PHE A . n 
A 1 89  GLY 89  109 109 GLY GLY A . n 
A 1 90  PRO 90  110 110 PRO PRO A . n 
A 1 91  VAL 91  111 111 VAL VAL A . n 
A 1 92  GLY 92  112 112 GLY GLY A . n 
A 1 93  PHE 93  113 113 PHE PHE A . n 
A 1 94  MET 94  114 114 MET MET A . n 
A 1 95  LYS 95  115 115 LYS LYS A . n 
A 1 96  SER 96  116 116 SER SER A . n 
A 1 97  ALA 97  117 117 ALA ALA A . n 
A 1 98  ILE 98  118 118 ILE ILE A . n 
A 1 99  SER 99  119 119 SER SER A . n 
A 1 100 ILE 100 120 120 ILE ILE A . n 
A 1 101 ALA 101 121 121 ALA ALA A . n 
A 1 102 GLU 102 122 122 GLU GLU A . n 
A 1 103 ASP 103 123 123 ASP ASP A . n 
A 1 104 GLU 104 124 124 GLU GLU A . n 
A 1 105 GLU 105 125 125 GLU GLU A . n 
A 1 106 TRP 106 126 126 TRP TRP A . n 
A 1 107 LYS 107 127 127 LYS LYS A . n 
A 1 108 ARG 108 128 128 ARG ARG A . n 
A 1 109 LEU 109 129 129 LEU LEU A . n 
A 1 110 ARG 110 130 130 ARG ARG A . n 
A 1 111 SER 111 131 131 SER SER A . n 
A 1 112 LEU 112 132 132 LEU LEU A . n 
A 1 113 LEU 113 133 133 LEU LEU A . n 
A 1 114 SER 114 134 134 SER SER A . n 
A 1 115 PRO 115 135 135 PRO PRO A . n 
A 1 116 THR 116 136 136 THR THR A . n 
A 1 117 PHE 117 137 137 PHE PHE A . n 
A 1 118 THR 118 138 138 THR THR A . n 
A 1 119 SER 119 139 139 SER SER A . n 
A 1 120 GLY 120 140 140 GLY GLY A . n 
A 1 121 LYS 121 141 141 LYS LYS A . n 
A 1 122 LEU 122 142 142 LEU LEU A . n 
A 1 123 LYS 123 143 143 LYS LYS A . n 
A 1 124 GLU 124 144 144 GLU GLU A . n 
A 1 125 MET 125 145 145 MET MET A . n 
A 1 126 VAL 126 146 146 VAL VAL A . n 
A 1 127 PRO 127 147 147 PRO PRO A . n 
A 1 128 ILE 128 148 148 ILE ILE A . n 
A 1 129 ILE 129 149 149 ILE ILE A . n 
A 1 130 ALA 130 150 150 ALA ALA A . n 
A 1 131 GLN 131 151 151 GLN GLN A . n 
A 1 132 TYR 132 152 152 TYR TYR A . n 
A 1 133 GLY 133 153 153 GLY GLY A . n 
A 1 134 ASP 134 154 154 ASP ASP A . n 
A 1 135 VAL 135 155 155 VAL VAL A . n 
A 1 136 LEU 136 156 156 LEU LEU A . n 
A 1 137 VAL 137 157 157 VAL VAL A . n 
A 1 138 ARG 138 158 158 ARG ARG A . n 
A 1 139 ASN 139 159 159 ASN ASN A . n 
A 1 140 LEU 140 160 160 LEU LEU A . n 
A 1 141 ARG 141 161 161 ARG ARG A . n 
A 1 142 ARG 142 162 162 ARG ARG A . n 
A 1 143 GLU 143 163 163 GLU GLU A . n 
A 1 144 ALA 144 164 164 ALA ALA A . n 
A 1 145 GLU 145 165 165 GLU GLU A . n 
A 1 146 THR 146 166 166 THR THR A . n 
A 1 147 GLY 147 167 167 GLY GLY A . n 
A 1 148 LYS 148 168 168 LYS LYS A . n 
A 1 149 PRO 149 169 169 PRO PRO A . n 
A 1 150 VAL 150 170 170 VAL VAL A . n 
A 1 151 THR 151 171 171 THR THR A . n 
A 1 152 LEU 152 172 172 LEU LEU A . n 
A 1 153 LYS 153 173 173 LYS LYS A . n 
A 1 154 ASP 154 174 174 ASP ASP A . n 
A 1 155 VAL 155 175 175 VAL VAL A . n 
A 1 156 PHE 156 176 176 PHE PHE A . n 
A 1 157 GLY 157 177 177 GLY GLY A . n 
A 1 158 ALA 158 178 178 ALA ALA A . n 
A 1 159 TYR 159 179 179 TYR TYR A . n 
A 1 160 SER 160 180 180 SER SER A . n 
A 1 161 MET 161 181 181 MET MET A . n 
A 1 162 ASP 162 182 182 ASP ASP A . n 
A 1 163 VAL 163 183 183 VAL VAL A . n 
A 1 164 ILE 164 184 184 ILE ILE A . n 
A 1 165 THR 165 185 185 THR THR A . n 
A 1 166 SER 166 186 186 SER SER A . n 
A 1 167 THR 167 187 187 THR THR A . n 
A 1 168 SER 168 188 188 SER SER A . n 
A 1 169 PHE 169 189 189 PHE PHE A . n 
A 1 170 GLY 170 190 190 GLY GLY A . n 
A 1 171 VAL 171 191 191 VAL VAL A . n 
A 1 172 ASN 172 192 192 ASN ASN A . n 
A 1 173 ILE 173 193 193 ILE ILE A . n 
A 1 174 ASP 174 194 194 ASP ASP A . n 
A 1 175 SER 175 195 195 SER SER A . n 
A 1 176 LEU 176 196 196 LEU LEU A . n 
A 1 177 ASN 177 197 197 ASN ASN A . n 
A 1 178 ASN 178 198 198 ASN ASN A . n 
A 1 179 PRO 179 199 ?   ?   ?   A . n 
A 1 180 GLN 180 200 ?   ?   ?   A . n 
A 1 181 ASP 181 201 ?   ?   ?   A . n 
A 1 182 PRO 182 202 ?   ?   ?   A . n 
A 1 183 PHE 183 203 ?   ?   ?   A . n 
A 1 184 VAL 184 204 ?   ?   ?   A . n 
A 1 185 GLU 185 205 ?   ?   ?   A . n 
A 1 186 ASN 186 206 ?   ?   ?   A . n 
A 1 187 THR 187 207 ?   ?   ?   A . n 
A 1 188 LYS 188 208 ?   ?   ?   A . n 
A 1 189 LYS 189 209 ?   ?   ?   A . n 
A 1 190 LEU 190 210 ?   ?   ?   A . n 
A 1 191 LEU 191 211 ?   ?   ?   A . n 
A 1 192 ARG 192 212 ?   ?   ?   A . n 
A 1 193 PHE 193 213 ?   ?   ?   A . n 
A 1 194 ASP 194 214 ?   ?   ?   A . n 
A 1 195 PHE 195 215 ?   ?   ?   A . n 
A 1 196 LEU 196 216 216 LEU LEU A . n 
A 1 197 ASP 197 217 217 ASP ASP A . n 
A 1 198 PRO 198 218 218 PRO PRO A . n 
A 1 199 PHE 199 219 219 PHE PHE A . n 
A 1 200 PHE 200 220 220 PHE PHE A . n 
A 1 201 LEU 201 221 221 LEU LEU A . n 
A 1 202 SER 202 222 222 SER SER A . n 
A 1 203 ILE 203 223 223 ILE ILE A . n 
A 1 204 THR 204 224 224 THR THR A . n 
A 1 205 VAL 205 225 225 VAL VAL A . n 
A 1 206 PHE 206 226 226 PHE PHE A . n 
A 1 207 PRO 207 227 227 PRO PRO A . n 
A 1 208 PHE 208 228 228 PHE PHE A . n 
A 1 209 LEU 209 229 229 LEU LEU A . n 
A 1 210 ILE 210 230 230 ILE ILE A . n 
A 1 211 PRO 211 231 231 PRO PRO A . n 
A 1 212 ILE 212 232 232 ILE ILE A . n 
A 1 213 LEU 213 233 233 LEU LEU A . n 
A 1 214 GLU 214 234 234 GLU GLU A . n 
A 1 215 VAL 215 235 235 VAL VAL A . n 
A 1 216 LEU 216 236 236 LEU LEU A . n 
A 1 217 ASN 217 237 237 ASN ASN A . n 
A 1 218 ILE 218 238 238 ILE ILE A . n 
A 1 219 CYS 219 239 239 CYS CYS A . n 
A 1 220 VAL 220 240 240 VAL VAL A . n 
A 1 221 PHE 221 241 241 PHE PHE A . n 
A 1 222 PRO 222 242 242 PRO PRO A . n 
A 1 223 ARG 223 243 243 ARG ARG A . n 
A 1 224 GLU 224 244 244 GLU GLU A . n 
A 1 225 VAL 225 245 245 VAL VAL A . n 
A 1 226 THR 226 246 246 THR THR A . n 
A 1 227 ASN 227 247 247 ASN ASN A . n 
A 1 228 PHE 228 248 248 PHE PHE A . n 
A 1 229 LEU 229 249 249 LEU LEU A . n 
A 1 230 ARG 230 250 250 ARG ARG A . n 
A 1 231 LYS 231 251 251 LYS LYS A . n 
A 1 232 SER 232 252 252 SER SER A . n 
A 1 233 VAL 233 253 253 VAL VAL A . n 
A 1 234 LYS 234 254 254 LYS LYS A . n 
A 1 235 ARG 235 255 255 ARG ARG A . n 
A 1 236 MET 236 256 256 MET MET A . n 
A 1 237 LYS 237 257 257 LYS LYS A . n 
A 1 238 GLU 238 258 258 GLU GLU A . n 
A 1 239 SER 239 259 259 SER SER A . n 
A 1 240 ARG 240 260 260 ARG ARG A . n 
A 1 241 LEU 241 261 ?   ?   ?   A . n 
A 1 242 GLU 242 262 ?   ?   ?   A . n 
A 1 243 ASP 243 263 ?   ?   ?   A . n 
A 1 244 THR 244 264 ?   ?   ?   A . n 
A 1 245 GLN 245 265 ?   ?   ?   A . n 
A 1 246 LYS 246 266 ?   ?   ?   A . n 
A 1 247 HIS 247 267 ?   ?   ?   A . n 
A 1 248 ARG 248 268 ?   ?   ?   A . n 
A 1 249 VAL 249 269 ?   ?   ?   A . n 
A 1 250 ASP 250 270 270 ASP ASP A . n 
A 1 251 PHE 251 271 271 PHE PHE A . n 
A 1 252 LEU 252 272 272 LEU LEU A . n 
A 1 253 GLN 253 273 273 GLN GLN A . n 
A 1 254 LEU 254 274 274 LEU LEU A . n 
A 1 255 MET 255 275 275 MET MET A . n 
A 1 256 ILE 256 276 276 ILE ILE A . n 
A 1 257 ASP 257 277 277 ASP ASP A . n 
A 1 258 SER 258 278 278 SER SER A . n 
A 1 259 GLN 259 279 279 GLN GLN A . n 
A 1 260 ASN 260 280 280 ASN ASN A . n 
A 1 261 SER 261 281 ?   ?   ?   A . n 
A 1 262 LYS 262 282 ?   ?   ?   A . n 
A 1 263 GLU 263 283 ?   ?   ?   A . n 
A 1 264 THR 264 284 ?   ?   ?   A . n 
A 1 265 GLU 265 285 ?   ?   ?   A . n 
A 1 266 SER 266 286 286 SER SER A . n 
A 1 267 HIS 267 287 287 HIS HIS A . n 
A 1 268 LYS 268 288 288 LYS LYS A . n 
A 1 269 ALA 269 289 289 ALA ALA A . n 
A 1 270 LEU 270 290 290 LEU LEU A . n 
A 1 271 SER 271 291 291 SER SER A . n 
A 1 272 ASP 272 292 292 ASP ASP A . n 
A 1 273 LEU 273 293 293 LEU LEU A . n 
A 1 274 GLU 274 294 294 GLU GLU A . n 
A 1 275 LEU 275 295 295 LEU LEU A . n 
A 1 276 VAL 276 296 296 VAL VAL A . n 
A 1 277 ALA 277 297 297 ALA ALA A . n 
A 1 278 GLN 278 298 298 GLN GLN A . n 
A 1 279 SER 279 299 299 SER SER A . n 
A 1 280 ILE 280 300 300 ILE ILE A . n 
A 1 281 ILE 281 301 301 ILE ILE A . n 
A 1 282 PHE 282 302 302 PHE PHE A . n 
A 1 283 ILE 283 303 303 ILE ILE A . n 
A 1 284 PHE 284 304 304 PHE PHE A . n 
A 1 285 ALA 285 305 305 ALA ALA A . n 
A 1 286 GLY 286 306 306 GLY GLY A . n 
A 1 287 TYR 287 307 307 TYR TYR A . n 
A 1 288 GLU 288 308 308 GLU GLU A . n 
A 1 289 THR 289 309 309 THR THR A . n 
A 1 290 THR 290 310 310 THR THR A . n 
A 1 291 SER 291 311 311 SER SER A . n 
A 1 292 SER 292 312 312 SER SER A . n 
A 1 293 VAL 293 313 313 VAL VAL A . n 
A 1 294 LEU 294 314 314 LEU LEU A . n 
A 1 295 SER 295 315 315 SER SER A . n 
A 1 296 PHE 296 316 316 PHE PHE A . n 
A 1 297 ILE 297 317 317 ILE ILE A . n 
A 1 298 MET 298 318 318 MET MET A . n 
A 1 299 TYR 299 319 319 TYR TYR A . n 
A 1 300 GLU 300 320 320 GLU GLU A . n 
A 1 301 LEU 301 321 321 LEU LEU A . n 
A 1 302 ALA 302 322 322 ALA ALA A . n 
A 1 303 THR 303 323 323 THR THR A . n 
A 1 304 HIS 304 324 324 HIS HIS A . n 
A 1 305 PRO 305 325 325 PRO PRO A . n 
A 1 306 ASP 306 326 326 ASP ASP A . n 
A 1 307 VAL 307 327 327 VAL VAL A . n 
A 1 308 GLN 308 328 328 GLN GLN A . n 
A 1 309 GLN 309 329 329 GLN GLN A . n 
A 1 310 LYS 310 330 330 LYS LYS A . n 
A 1 311 LEU 311 331 331 LEU LEU A . n 
A 1 312 GLN 312 332 332 GLN GLN A . n 
A 1 313 GLU 313 333 333 GLU GLU A . n 
A 1 314 GLU 314 334 334 GLU GLU A . n 
A 1 315 ILE 315 335 335 ILE ILE A . n 
A 1 316 ASP 316 336 336 ASP ASP A . n 
A 1 317 ALA 317 337 337 ALA ALA A . n 
A 1 318 VAL 318 338 338 VAL VAL A . n 
A 1 319 LEU 319 339 339 LEU LEU A . n 
A 1 320 PRO 320 340 340 PRO PRO A . n 
A 1 321 ASN 321 341 341 ASN ASN A . n 
A 1 322 LYS 322 342 342 LYS LYS A . n 
A 1 323 ALA 323 343 343 ALA ALA A . n 
A 1 324 PRO 324 344 344 PRO PRO A . n 
A 1 325 PRO 325 345 345 PRO PRO A . n 
A 1 326 THR 326 346 346 THR THR A . n 
A 1 327 TYR 327 347 347 TYR TYR A . n 
A 1 328 ASP 328 348 348 ASP ASP A . n 
A 1 329 THR 329 349 349 THR THR A . n 
A 1 330 VAL 330 350 350 VAL VAL A . n 
A 1 331 LEU 331 351 351 LEU LEU A . n 
A 1 332 GLN 332 352 352 GLN GLN A . n 
A 1 333 MET 333 353 353 MET MET A . n 
A 1 334 GLU 334 354 354 GLU GLU A . n 
A 1 335 TYR 335 355 355 TYR TYR A . n 
A 1 336 LEU 336 356 356 LEU LEU A . n 
A 1 337 ASP 337 357 357 ASP ASP A . n 
A 1 338 MET 338 358 358 MET MET A . n 
A 1 339 VAL 339 359 359 VAL VAL A . n 
A 1 340 VAL 340 360 360 VAL VAL A . n 
A 1 341 ASN 341 361 361 ASN ASN A . n 
A 1 342 GLU 342 362 362 GLU GLU A . n 
A 1 343 THR 343 363 363 THR THR A . n 
A 1 344 LEU 344 364 364 LEU LEU A . n 
A 1 345 ARG 345 365 365 ARG ARG A . n 
A 1 346 LEU 346 366 366 LEU LEU A . n 
A 1 347 PHE 347 367 367 PHE PHE A . n 
A 1 348 PRO 348 368 368 PRO PRO A . n 
A 1 349 ILE 349 369 369 ILE ILE A . n 
A 1 350 ALA 350 370 370 ALA ALA A . n 
A 1 351 MET 351 371 371 MET MET A . n 
A 1 352 ARG 352 372 372 ARG ARG A . n 
A 1 353 LEU 353 373 373 LEU LEU A . n 
A 1 354 GLU 354 374 374 GLU GLU A . n 
A 1 355 ARG 355 375 375 ARG ARG A . n 
A 1 356 VAL 356 376 376 VAL VAL A . n 
A 1 357 CYS 357 377 377 CYS CYS A . n 
A 1 358 LYS 358 378 378 LYS LYS A . n 
A 1 359 LYS 359 379 379 LYS LYS A . n 
A 1 360 ASP 360 380 380 ASP ASP A . n 
A 1 361 VAL 361 381 381 VAL VAL A . n 
A 1 362 GLU 362 382 382 GLU GLU A . n 
A 1 363 ILE 363 383 383 ILE ILE A . n 
A 1 364 ASN 364 384 384 ASN ASN A . n 
A 1 365 GLY 365 385 385 GLY GLY A . n 
A 1 366 MET 366 386 386 MET MET A . n 
A 1 367 PHE 367 387 387 PHE PHE A . n 
A 1 368 ILE 368 388 388 ILE ILE A . n 
A 1 369 PRO 369 389 389 PRO PRO A . n 
A 1 370 LYS 370 390 390 LYS LYS A . n 
A 1 371 GLY 371 391 391 GLY GLY A . n 
A 1 372 VAL 372 392 392 VAL VAL A . n 
A 1 373 VAL 373 393 393 VAL VAL A . n 
A 1 374 VAL 374 394 394 VAL VAL A . n 
A 1 375 MET 375 395 395 MET MET A . n 
A 1 376 ILE 376 396 396 ILE ILE A . n 
A 1 377 PRO 377 397 397 PRO PRO A . n 
A 1 378 SER 378 398 398 SER SER A . n 
A 1 379 TYR 379 399 399 TYR TYR A . n 
A 1 380 ALA 380 400 400 ALA ALA A . n 
A 1 381 LEU 381 401 401 LEU LEU A . n 
A 1 382 HIS 382 402 402 HIS HIS A . n 
A 1 383 ARG 383 403 403 ARG ARG A . n 
A 1 384 ASP 384 404 404 ASP ASP A . n 
A 1 385 PRO 385 405 405 PRO PRO A . n 
A 1 386 LYS 386 406 406 LYS LYS A . n 
A 1 387 TYR 387 407 407 TYR TYR A . n 
A 1 388 TRP 388 408 408 TRP TRP A . n 
A 1 389 THR 389 409 409 THR THR A . n 
A 1 390 GLU 390 410 410 GLU GLU A . n 
A 1 391 PRO 391 411 411 PRO PRO A . n 
A 1 392 GLU 392 412 412 GLU GLU A . n 
A 1 393 LYS 393 413 413 LYS LYS A . n 
A 1 394 PHE 394 414 414 PHE PHE A . n 
A 1 395 LEU 395 415 415 LEU LEU A . n 
A 1 396 PRO 396 416 416 PRO PRO A . n 
A 1 397 GLU 397 417 417 GLU GLU A . n 
A 1 398 ARG 398 418 418 ARG ARG A . n 
A 1 399 PHE 399 419 419 PHE PHE A . n 
A 1 400 SER 400 420 420 SER SER A . n 
A 1 401 LYS 401 421 421 LYS LYS A . n 
A 1 402 LYS 402 422 422 LYS LYS A . n 
A 1 403 ASN 403 423 423 ASN ASN A . n 
A 1 404 LYS 404 424 424 LYS LYS A . n 
A 1 405 ASP 405 425 425 ASP ASP A . n 
A 1 406 ASN 406 426 426 ASN ASN A . n 
A 1 407 ILE 407 427 427 ILE ILE A . n 
A 1 408 ASP 408 428 428 ASP ASP A . n 
A 1 409 PRO 409 429 429 PRO PRO A . n 
A 1 410 TYR 410 430 430 TYR TYR A . n 
A 1 411 ILE 411 431 431 ILE ILE A . n 
A 1 412 TYR 412 432 432 TYR TYR A . n 
A 1 413 THR 413 433 433 THR THR A . n 
A 1 414 PRO 414 434 434 PRO PRO A . n 
A 1 415 PHE 415 435 435 PHE PHE A . n 
A 1 416 GLY 416 436 436 GLY GLY A . n 
A 1 417 SER 417 437 437 SER SER A . n 
A 1 418 GLY 418 438 438 GLY GLY A . n 
A 1 419 PRO 419 439 439 PRO PRO A . n 
A 1 420 ARG 420 440 440 ARG ARG A . n 
A 1 421 ASN 421 441 441 ASN ASN A . n 
A 1 422 CYS 422 442 442 CYS CYS A . n 
A 1 423 ILE 423 443 443 ILE ILE A . n 
A 1 424 GLY 424 444 444 GLY GLY A . n 
A 1 425 MET 425 445 445 MET MET A . n 
A 1 426 ARG 426 446 446 ARG ARG A . n 
A 1 427 PHE 427 447 447 PHE PHE A . n 
A 1 428 ALA 428 448 448 ALA ALA A . n 
A 1 429 LEU 429 449 449 LEU LEU A . n 
A 1 430 MET 430 450 450 MET MET A . n 
A 1 431 ASN 431 451 451 ASN ASN A . n 
A 1 432 MET 432 452 452 MET MET A . n 
A 1 433 LYS 433 453 453 LYS LYS A . n 
A 1 434 LEU 434 454 454 LEU LEU A . n 
A 1 435 ALA 435 455 455 ALA ALA A . n 
A 1 436 LEU 436 456 456 LEU LEU A . n 
A 1 437 ILE 437 457 457 ILE ILE A . n 
A 1 438 ARG 438 458 458 ARG ARG A . n 
A 1 439 VAL 439 459 459 VAL VAL A . n 
A 1 440 LEU 440 460 460 LEU LEU A . n 
A 1 441 GLN 441 461 461 GLN GLN A . n 
A 1 442 ASN 442 462 462 ASN ASN A . n 
A 1 443 PHE 443 463 463 PHE PHE A . n 
A 1 444 SER 444 464 464 SER SER A . n 
A 1 445 PHE 445 465 465 PHE PHE A . n 
A 1 446 LYS 446 466 466 LYS LYS A . n 
A 1 447 PRO 447 467 467 PRO PRO A . n 
A 1 448 CYS 448 468 468 CYS CYS A . n 
A 1 449 LYS 449 469 469 LYS LYS A . n 
A 1 450 GLU 450 470 470 GLU GLU A . n 
A 1 451 THR 451 471 471 THR THR A . n 
A 1 452 GLN 452 472 472 GLN GLN A . n 
A 1 453 ILE 453 473 473 ILE ILE A . n 
A 1 454 PRO 454 474 474 PRO PRO A . n 
A 1 455 LEU 455 475 475 LEU LEU A . n 
A 1 456 LYS 456 476 476 LYS LYS A . n 
A 1 457 LEU 457 477 477 LEU LEU A . n 
A 1 458 SER 458 478 478 SER SER A . n 
A 1 459 LEU 459 479 479 LEU LEU A . n 
A 1 460 GLY 460 480 480 GLY GLY A . n 
A 1 461 GLY 461 481 481 GLY GLY A . n 
A 1 462 LEU 462 482 482 LEU LEU A . n 
A 1 463 LEU 463 483 483 LEU LEU A . n 
A 1 464 GLN 464 484 484 GLN GLN A . n 
A 1 465 PRO 465 485 485 PRO PRO A . n 
A 1 466 GLU 466 486 486 GLU GLU A . n 
A 1 467 LYS 467 487 487 LYS LYS A . n 
A 1 468 PRO 468 488 488 PRO PRO A . n 
A 1 469 VAL 469 489 489 VAL VAL A . n 
A 1 470 VAL 470 490 490 VAL VAL A . n 
A 1 471 LEU 471 491 491 LEU LEU A . n 
A 1 472 LYS 472 492 492 LYS LYS A . n 
A 1 473 VAL 473 493 493 VAL VAL A . n 
A 1 474 GLU 474 494 494 GLU GLU A . n 
A 1 475 SER 475 495 495 SER SER A . n 
A 1 476 ARG 476 496 496 ARG ARG A . n 
A 1 477 ASP 477 497 ?   ?   ?   A . n 
A 1 478 GLY 478 498 ?   ?   ?   A . n 
A 1 479 THR 479 499 ?   ?   ?   A . n 
A 1 480 VAL 480 500 ?   ?   ?   A . n 
A 1 481 SER 481 501 ?   ?   ?   A . n 
A 1 482 GLY 482 502 ?   ?   ?   A . n 
A 1 483 ALA 483 503 ?   ?   ?   A . n 
A 1 484 HIS 484 504 ?   ?   ?   A . n 
A 1 485 HIS 485 505 ?   ?   ?   A . n 
A 1 486 HIS 486 506 ?   ?   ?   A . n 
A 1 487 HIS 487 507 ?   ?   ?   A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1A07 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1A07 
_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   1 601 500 HEM   HEM A . 
C 3 A1A07 1 602 700 A1A07 LIG A . 
# 
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 reduction' ? ? ? ? ? ? ? ? ? ? ? MOSFLM ? ? ? .           2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? SCALA  ? ? ? .           3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER ? ? ? .           4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9COR 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     76.020 
_cell.length_a_esd                 ? 
_cell.length_b                     101.310 
_cell.length_b_esd                 ? 
_cell.length_c                     124.750 
_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                         9COR 
_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                   9COR 
_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             2.15 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          42.89 
_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    'PEG3350, taximate' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     103 
_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                      mirrors 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS 300K' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2017-07-18 
_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                    ? 
_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   1.0 
_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                        'ALS BEAMLINE 8.2.2' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.0 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   8.2.2 
_diffrn_source.pdbx_synchrotron_site       ALS 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9COR 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.55 
_reflns.d_resolution_low                               78.64 
_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                                     16009 
_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                           99.6 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                5.5 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          11.0 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                0.030 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.999 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.070 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.55 
_reflns_shell.d_res_low                                     2.69 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.0 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             2312 
_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                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               0.732 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.494 
_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                                  1.596 
_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                                 9COR 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.55 
_refine.ls_d_res_low                             64.92 
_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                     15981 
_refine.ls_number_reflns_R_free                  806 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.38 
_refine.ls_percent_reflns_R_free                 5.04 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2339 
_refine.ls_R_factor_R_free                       0.2814 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2316 
_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                 33.09 
_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                            0.42 
_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        3515 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         83 
_refine_hist.number_atoms_solvent             0 
_refine_hist.number_atoms_total               3598 
_refine_hist.d_res_high                       2.55 
_refine_hist.d_res_low                        64.92 
# 
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  ? 3715 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.663  ? 5040 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 14.217 ? 1406 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.042  ? 553  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.004  ? 633  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.55 2.71  . . 147 2480 100.00 . . . . 0.3706 . . . . . . . . . . . 0.3732 
'X-RAY DIFFRACTION' 2.71 2.92  . . 126 2504 100.00 . . . . 0.3136 . . . . . . . . . . . 0.3542 
'X-RAY DIFFRACTION' 2.92 3.21  . . 129 2510 100.00 . . . . 0.3129 . . . . . . . . . . . 0.3280 
'X-RAY DIFFRACTION' 3.21 3.68  . . 148 2517 100.00 . . . . 0.2645 . . . . . . . . . . . 0.3126 
'X-RAY DIFFRACTION' 3.68 4.63  . . 135 2553 100.00 . . . . 0.2195 . . . . . . . . . . . 0.2549 
'X-RAY DIFFRACTION' 4.63 64.92 . . 121 2611 97.00  . . . . 0.2003 . . . . . . . . . . . 0.2634 
# 
_struct.entry_id                     9COR 
_struct.title                        'Crystal structure of CYP3A4 bound to an inhibitor' 
_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        9COR 
_struct_keywords.text            'cytochrome P450, CYP3A4, inhibitor, complex, 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   
;MALIPDLAMETWLLLAVSLVLLYLYGTHSHGLFKKLGIPGPTPLPFLGNILSYHKGFCMFDMECHKKYGKVWGFYDGQQP
VLAITDPDMIKTVLVKECYSVFTNRRPFGPVGFMKSAISIAEDEEWKRLRSLLSPTFTSGKLKEMVPIIAQYGDVLVRNL
RREAETGKPVTLKDVFGAYSMDVITSTSFGVNIDSLNNPQDPFVENTKKLLRFDFLDPFFLSITVFPFLIPILEVLNICV
FPREVTNFLRKSVKRMKESRLEDTQKHRVDFLQLMIDSQNSKETESHKALSDLELVAQSIIFIFAGYETTSSVLSFIMYE
LATHPDVQQKLQEEIDAVLPNKAPPTYDTVLQMEYLDMVVNETLRLFPIAMRLERVCKKDVEINGMFIPKGVVVMIPSYA
LHRDPKYWTEPEKFLPERFSKKNKDNIDPYIYTPFGSGPRNCIGMRFALMNMKLALIRVLQNFSFKPCKETQIPLKLSLG
GLLQPEKPVVLKVESRDGTVSGA
;
_struct_ref.pdbx_align_begin           1 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9COR 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 483 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             P08684 
_struct_ref_seq.db_align_beg                  1 
_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       1 
_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 9COR ?   A ?   ? UNP P08684 LEU 3  deletion         ?   1  
1 9COR ?   A ?   ? UNP P08684 ILE 4  deletion         ?   2  
1 9COR ?   A ?   ? UNP P08684 PRO 5  deletion         ?   3  
1 9COR ?   A ?   ? UNP P08684 ASP 6  deletion         ?   4  
1 9COR ?   A ?   ? UNP P08684 LEU 7  deletion         ?   5  
1 9COR ?   A ?   ? UNP P08684 ALA 8  deletion         ?   6  
1 9COR ?   A ?   ? UNP P08684 MET 9  deletion         ?   7  
1 9COR ?   A ?   ? UNP P08684 GLU 10 deletion         ?   8  
1 9COR ?   A ?   ? UNP P08684 THR 11 deletion         ?   9  
1 9COR ?   A ?   ? UNP P08684 TRP 12 deletion         ?   10 
1 9COR ?   A ?   ? UNP P08684 LEU 13 deletion         ?   11 
1 9COR ?   A ?   ? UNP P08684 LEU 14 deletion         ?   12 
1 9COR ?   A ?   ? UNP P08684 LEU 15 deletion         ?   13 
1 9COR ?   A ?   ? UNP P08684 ALA 16 deletion         ?   14 
1 9COR ?   A ?   ? UNP P08684 VAL 17 deletion         ?   15 
1 9COR ?   A ?   ? UNP P08684 SER 18 deletion         ?   16 
1 9COR ?   A ?   ? UNP P08684 LEU 19 deletion         ?   17 
1 9COR ?   A ?   ? UNP P08684 VAL 20 deletion         ?   18 
1 9COR ?   A ?   ? UNP P08684 LEU 21 deletion         ?   19 
1 9COR ?   A ?   ? UNP P08684 LEU 22 deletion         ?   20 
1 9COR HIS A 484 ? UNP P08684 ?   ?  'expression tag' 504 21 
1 9COR HIS A 485 ? UNP P08684 ?   ?  'expression tag' 505 22 
1 9COR HIS A 486 ? UNP P08684 ?   ?  'expression tag' 506 23 
1 9COR HIS A 487 ? UNP P08684 ?   ?  'expression tag' 507 24 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,B,C 
1 2 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                ? 
# 
loop_
_pdbx_struct_oper_list.id 
_pdbx_struct_oper_list.type 
_pdbx_struct_oper_list.name 
_pdbx_struct_oper_list.symmetry_operation 
_pdbx_struct_oper_list.matrix[1][1] 
_pdbx_struct_oper_list.matrix[1][2] 
_pdbx_struct_oper_list.matrix[1][3] 
_pdbx_struct_oper_list.vector[1] 
_pdbx_struct_oper_list.matrix[2][1] 
_pdbx_struct_oper_list.matrix[2][2] 
_pdbx_struct_oper_list.matrix[2][3] 
_pdbx_struct_oper_list.vector[2] 
_pdbx_struct_oper_list.matrix[3][1] 
_pdbx_struct_oper_list.matrix[3][2] 
_pdbx_struct_oper_list.matrix[3][3] 
_pdbx_struct_oper_list.vector[3] 
1 'identity operation'         1_555 x,y,z     1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000  
0.0000000000 0.0000000000    0.0000000000 0.0000000000 1.0000000000  0.0000000000 
2 'crystal symmetry operation' 4_545 x,-y-1,-z 1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 -1.0000000000 
0.0000000000 -101.3100000000 0.0000000000 0.0000000000 -1.0000000000 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 HIS A 8   ? HIS A 10  ? HIS A 28  HIS A 30  5 ? 3  
HELX_P HELX_P2  AA2 GLY A 11  ? GLY A 17  ? GLY A 31  GLY A 37  1 ? 7  
HELX_P HELX_P3  AA3 ASN A 29  ? HIS A 34  ? ASN A 49  HIS A 54  5 ? 6  
HELX_P HELX_P4  AA4 LYS A 35  ? GLY A 49  ? LYS A 55  GLY A 69  1 ? 15 
HELX_P HELX_P5  AA5 ASP A 66  ? VAL A 75  ? ASP A 86  VAL A 95  1 ? 10 
HELX_P HELX_P6  AA6 VAL A 91  ? ALA A 97  ? VAL A 111 ALA A 117 5 ? 7  
HELX_P HELX_P7  AA7 GLU A 102 ? SER A 114 ? GLU A 122 SER A 134 1 ? 13 
HELX_P HELX_P8  AA8 PRO A 115 ? PHE A 117 ? PRO A 135 PHE A 137 5 ? 3  
HELX_P HELX_P9  AA9 THR A 118 ? GLY A 147 ? THR A 138 GLY A 167 1 ? 30 
HELX_P HELX_P10 AB1 LEU A 152 ? GLY A 170 ? LEU A 172 GLY A 190 1 ? 19 
HELX_P HELX_P11 AB2 ASP A 174 ? ASN A 178 ? ASP A 194 ASN A 198 5 ? 5  
HELX_P HELX_P12 AB3 ASP A 197 ? PHE A 206 ? ASP A 217 PHE A 226 1 ? 10 
HELX_P HELX_P13 AB4 LEU A 209 ? LEU A 216 ? LEU A 229 LEU A 236 1 ? 8  
HELX_P HELX_P14 AB5 GLU A 224 ? ARG A 240 ? GLU A 244 ARG A 260 1 ? 17 
HELX_P HELX_P15 AB6 PHE A 251 ? GLN A 259 ? PHE A 271 GLN A 279 1 ? 9  
HELX_P HELX_P16 AB7 SER A 271 ? THR A 289 ? SER A 291 THR A 309 1 ? 19 
HELX_P HELX_P17 AB8 THR A 289 ? THR A 303 ? THR A 309 THR A 323 1 ? 15 
HELX_P HELX_P18 AB9 HIS A 304 ? LEU A 319 ? HIS A 324 LEU A 339 1 ? 16 
HELX_P HELX_P19 AC1 THR A 326 ? MET A 333 ? THR A 346 MET A 353 1 ? 8  
HELX_P HELX_P20 AC2 MET A 333 ? PHE A 347 ? MET A 353 PHE A 367 1 ? 15 
HELX_P HELX_P21 AC3 PRO A 377 ? ARG A 383 ? PRO A 397 ARG A 403 1 ? 7  
HELX_P HELX_P22 AC4 LEU A 395 ? SER A 400 ? LEU A 415 SER A 420 5 ? 6  
HELX_P HELX_P23 AC5 LYS A 402 ? ASN A 406 ? LYS A 422 ASN A 426 5 ? 5  
HELX_P HELX_P24 AC6 GLY A 424 ? ASN A 442 ? GLY A 444 ASN A 462 1 ? 19 
# 
_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 422 SG ? ? ? 1_555 B HEM   . FE  ? ? A CYS 442 A HEM   601 1_555 ? ? ? ? ? ? ? 2.395 ? ? 
metalc2 metalc ? ? B HEM .   FE ? ? ? 1_555 C A1A07 . N30 ? ? A HEM 601 A A1A07 602 1_555 ? ? ? ? ? ? ? 2.134 ? ? 
# 
_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 422 ? A CYS 442 ? 1_555 FE ? B HEM . ? A HEM 601 ? 1_555 NA  ? B HEM   . ? A HEM   601 ? 1_555 96.6  ? 
2  SG ? A CYS 422 ? A CYS 442 ? 1_555 FE ? B HEM . ? A HEM 601 ? 1_555 NB  ? B HEM   . ? A HEM   601 ? 1_555 82.0  ? 
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 89.3  ? 
4  SG ? A CYS 422 ? A CYS 442 ? 1_555 FE ? B HEM . ? A HEM 601 ? 1_555 NC  ? B HEM   . ? A HEM   601 ? 1_555 88.9  ? 
5  NA ? B HEM .   ? A HEM 601 ? 1_555 FE ? B HEM . ? A HEM 601 ? 1_555 NC  ? B HEM   . ? A HEM   601 ? 1_555 174.5 ? 
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 90.6  ? 
7  SG ? A CYS 422 ? A CYS 442 ? 1_555 FE ? B HEM . ? A HEM 601 ? 1_555 ND  ? B HEM   . ? A HEM   601 ? 1_555 101.8 ? 
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 90.0  ? 
9  NB ? B HEM .   ? A HEM 601 ? 1_555 FE ? B HEM . ? A HEM 601 ? 1_555 ND  ? B HEM   . ? A HEM   601 ? 1_555 176.2 ? 
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 89.7  ? 
11 SG ? A CYS 422 ? A CYS 442 ? 1_555 FE ? B HEM . ? A HEM 601 ? 1_555 N30 ? C A1A07 . ? A A1A07 602 ? 1_555 174.5 ? 
12 NA ? B HEM .   ? A HEM 601 ? 1_555 FE ? B HEM . ? A HEM 601 ? 1_555 N30 ? C A1A07 . ? A A1A07 602 ? 1_555 85.2  ? 
13 NB ? B HEM .   ? A HEM 601 ? 1_555 FE ? B HEM . ? A HEM 601 ? 1_555 N30 ? C A1A07 . ? A A1A07 602 ? 1_555 92.8  ? 
14 NC ? B HEM .   ? A HEM 601 ? 1_555 FE ? B HEM . ? A HEM 601 ? 1_555 N30 ? C A1A07 . ? A A1A07 602 ? 1_555 89.3  ? 
15 ND ? B HEM .   ? A HEM 601 ? 1_555 FE ? B HEM . ? A HEM 601 ? 1_555 N30 ? C A1A07 . ? A A1A07 602 ? 1_555 83.4  ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 GLY 89  A . ? GLY 109 A PRO 90  A ? PRO 110 A 1 -2.08 
2 ILE 453 A . ? ILE 473 A PRO 454 A ? PRO 474 A 1 1.06  
# 
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 51  ? ASP A 56  ? VAL A 71  ASP A 76  
AA1 2 GLN A 59  ? ILE A 64  ? GLN A 79  ILE A 84  
AA1 3 VAL A 373 ? ILE A 376 ? VAL A 393 ILE A 396 
AA1 4 LEU A 353 ? VAL A 356 ? LEU A 373 VAL A 376 
AA2 1 VAL A 150 ? THR A 151 ? VAL A 170 THR A 171 
AA2 2 VAL A 470 ? SER A 475 ? VAL A 490 SER A 495 
AA2 3 PHE A 443 ? PRO A 447 ? PHE A 463 PRO A 467 
AA3 1 VAL A 361 ? ILE A 363 ? VAL A 381 ILE A 383 
AA3 2 MET A 366 ? ILE A 368 ? MET A 386 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 PHE A 54  ? N PHE A 74  O VAL A 61  ? O VAL A 81  
AA1 2 3 N LEU A 62  ? N LEU A 82  O VAL A 373 ? O VAL A 393 
AA1 3 4 O ILE A 376 ? O ILE A 396 N LEU A 353 ? N LEU A 373 
AA2 1 2 N VAL A 150 ? N VAL A 170 O LEU A 471 ? O LEU A 491 
AA2 2 3 O LYS A 472 ? O LYS A 492 N LYS A 446 ? N LYS A 466 
AA3 1 2 N VAL A 361 ? N VAL A 381 O ILE A 368 ? O ILE A 388 
# 
_pdbx_entry_details.entry_id                   9COR 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 PHE A 46  ? ? 61.86   -3.79   
2  1 VAL A 101 ? ? -121.79 -54.93  
3  1 PHE A 102 ? ? -103.41 68.78   
4  1 PRO A 107 ? ? -57.40  107.31  
5  1 ASP A 123 ? ? 57.51   -125.34 
6  1 LYS A 168 ? ? -37.18  117.93  
7  1 ARG A 243 ? ? -66.35  2.47    
8  1 HIS A 287 ? ? 58.32   -126.86 
9  1 LYS A 288 ? ? -147.39 31.30   
10 1 ALA A 289 ? ? 59.26   -143.75 
11 1 TYR A 307 ? ? -88.25  -76.18  
12 1 LEU A 339 ? ? -118.59 79.67   
13 1 MET A 371 ? ? 67.97   -53.41  
# 
_pdbx_refine_tls.id               1 
_pdbx_refine_tls.pdbx_refine_id   'X-RAY DIFFRACTION' 
_pdbx_refine_tls.details          ? 
_pdbx_refine_tls.method           refined 
_pdbx_refine_tls.origin_x         -19.2630 
_pdbx_refine_tls.origin_y         -27.1865 
_pdbx_refine_tls.origin_z         -12.9007 
_pdbx_refine_tls.T[1][1]          0.6370 
_pdbx_refine_tls.T[1][1]_esd      ? 
_pdbx_refine_tls.T[1][2]          -0.0152 
_pdbx_refine_tls.T[1][2]_esd      ? 
_pdbx_refine_tls.T[1][3]          0.0099 
_pdbx_refine_tls.T[1][3]_esd      ? 
_pdbx_refine_tls.T[2][2]          0.7480 
_pdbx_refine_tls.T[2][2]_esd      ? 
_pdbx_refine_tls.T[2][3]          0.1527 
_pdbx_refine_tls.T[2][3]_esd      ? 
_pdbx_refine_tls.T[3][3]          0.7652 
_pdbx_refine_tls.T[3][3]_esd      ? 
_pdbx_refine_tls.L[1][1]          2.9046 
_pdbx_refine_tls.L[1][1]_esd      ? 
_pdbx_refine_tls.L[1][2]          -1.5638 
_pdbx_refine_tls.L[1][2]_esd      ? 
_pdbx_refine_tls.L[1][3]          0.6084 
_pdbx_refine_tls.L[1][3]_esd      ? 
_pdbx_refine_tls.L[2][2]          4.3742 
_pdbx_refine_tls.L[2][2]_esd      ? 
_pdbx_refine_tls.L[2][3]          -0.3250 
_pdbx_refine_tls.L[2][3]_esd      ? 
_pdbx_refine_tls.L[3][3]          3.4151 
_pdbx_refine_tls.L[3][3]_esd      ? 
_pdbx_refine_tls.S[1][1]          -0.0255 
_pdbx_refine_tls.S[1][1]_esd      ? 
_pdbx_refine_tls.S[1][2]          0.3610 
_pdbx_refine_tls.S[1][2]_esd      ? 
_pdbx_refine_tls.S[1][3]          0.4580 
_pdbx_refine_tls.S[1][3]_esd      ? 
_pdbx_refine_tls.S[2][1]          0.1747 
_pdbx_refine_tls.S[2][1]_esd      ? 
_pdbx_refine_tls.S[2][2]          0.0789 
_pdbx_refine_tls.S[2][2]_esd      ? 
_pdbx_refine_tls.S[2][3]          -0.0165 
_pdbx_refine_tls.S[2][3]_esd      ? 
_pdbx_refine_tls.S[3][1]          -0.5488 
_pdbx_refine_tls.S[3][1]_esd      ? 
_pdbx_refine_tls.S[3][2]          0.0715 
_pdbx_refine_tls.S[3][2]_esd      ? 
_pdbx_refine_tls.S[3][3]          -0.0164 
_pdbx_refine_tls.S[3][3]_esd      ? 
# 
_pdbx_refine_tls_group.id                  1 
_pdbx_refine_tls_group.pdbx_refine_id      'X-RAY DIFFRACTION' 
_pdbx_refine_tls_group.refine_tls_id       1 
_pdbx_refine_tls_group.beg_label_asym_id   ? 
_pdbx_refine_tls_group.beg_label_seq_id    ? 
_pdbx_refine_tls_group.beg_auth_asym_id    ? 
_pdbx_refine_tls_group.beg_auth_seq_id     ? 
_pdbx_refine_tls_group.beg_PDB_ins_code    ? 
_pdbx_refine_tls_group.end_label_asym_id   ? 
_pdbx_refine_tls_group.end_label_seq_id    ? 
_pdbx_refine_tls_group.end_auth_asym_id    ? 
_pdbx_refine_tls_group.end_auth_seq_id     ? 
_pdbx_refine_tls_group.end_PDB_ins_code    ? 
_pdbx_refine_tls_group.selection           ? 
_pdbx_refine_tls_group.selection_details   all 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A MET 1   ? A MET 1   
2  1 Y 1 A ALA 2   ? A ALA 2   
3  1 Y 1 A TYR 23  ? A TYR 3   
4  1 Y 1 A LEU 24  ? A LEU 4   
5  1 Y 1 A TYR 25  ? A TYR 5   
6  1 Y 1 A GLY 26  ? A GLY 6   
7  1 Y 1 A THR 27  ? A THR 7   
8  1 Y 1 A PRO 199 ? A PRO 179 
9  1 Y 1 A GLN 200 ? A GLN 180 
10 1 Y 1 A ASP 201 ? A ASP 181 
11 1 Y 1 A PRO 202 ? A PRO 182 
12 1 Y 1 A PHE 203 ? A PHE 183 
13 1 Y 1 A VAL 204 ? A VAL 184 
14 1 Y 1 A GLU 205 ? A GLU 185 
15 1 Y 1 A ASN 206 ? A ASN 186 
16 1 Y 1 A THR 207 ? A THR 187 
17 1 Y 1 A LYS 208 ? A LYS 188 
18 1 Y 1 A LYS 209 ? A LYS 189 
19 1 Y 1 A LEU 210 ? A LEU 190 
20 1 Y 1 A LEU 211 ? A LEU 191 
21 1 Y 1 A ARG 212 ? A ARG 192 
22 1 Y 1 A PHE 213 ? A PHE 193 
23 1 Y 1 A ASP 214 ? A ASP 194 
24 1 Y 1 A PHE 215 ? A PHE 195 
25 1 Y 1 A LEU 261 ? A LEU 241 
26 1 Y 1 A GLU 262 ? A GLU 242 
27 1 Y 1 A ASP 263 ? A ASP 243 
28 1 Y 1 A THR 264 ? A THR 244 
29 1 Y 1 A GLN 265 ? A GLN 245 
30 1 Y 1 A LYS 266 ? A LYS 246 
31 1 Y 1 A HIS 267 ? A HIS 247 
32 1 Y 1 A ARG 268 ? A ARG 248 
33 1 Y 1 A VAL 269 ? A VAL 249 
34 1 Y 1 A SER 281 ? A SER 261 
35 1 Y 1 A LYS 282 ? A LYS 262 
36 1 Y 1 A GLU 283 ? A GLU 263 
37 1 Y 1 A THR 284 ? A THR 264 
38 1 Y 1 A GLU 285 ? A GLU 265 
39 1 Y 1 A ASP 497 ? A ASP 477 
40 1 Y 1 A GLY 498 ? A GLY 478 
41 1 Y 1 A THR 499 ? A THR 479 
42 1 Y 1 A VAL 500 ? A VAL 480 
43 1 Y 1 A SER 501 ? A SER 481 
44 1 Y 1 A GLY 502 ? A GLY 482 
45 1 Y 1 A ALA 503 ? A ALA 483 
46 1 Y 1 A HIS 504 ? A HIS 484 
47 1 Y 1 A HIS 505 ? A HIS 485 
48 1 Y 1 A HIS 506 ? A HIS 486 
49 1 Y 1 A HIS 507 ? A HIS 487 
# 
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 
A1A07 C13  C  N N 1   
A1A07 C15  C  N R 2   
A1A07 C17  C  Y N 3   
A1A07 C20  C  Y N 4   
A1A07 C21  C  Y N 5   
A1A07 C22  C  Y N 6   
A1A07 C26  C  N N 7   
A1A07 C28  C  Y N 8   
A1A07 C02  C  N N 9   
A1A07 C05  C  N N 10  
A1A07 C08  C  N N 11  
A1A07 C09  C  N N 12  
A1A07 C12  C  N S 13  
A1A07 C16  C  N N 14  
A1A07 C18  C  Y N 15  
A1A07 C19  C  Y N 16  
A1A07 C23  C  N N 17  
A1A07 C27  C  N N 18  
A1A07 C29  C  Y N 19  
A1A07 C31  C  Y N 20  
A1A07 C32  C  Y N 21  
A1A07 C33  C  Y N 22  
A1A07 C34  C  N N 23  
A1A07 C35  C  Y N 24  
A1A07 C36  C  Y N 25  
A1A07 C37  C  Y N 26  
A1A07 C38  C  Y N 27  
A1A07 C39  C  Y N 28  
A1A07 C40  C  Y N 29  
A1A07 F01  F  N N 30  
A1A07 F03  F  N N 31  
A1A07 F04  F  N N 32  
A1A07 N07  N  N N 33  
A1A07 N11  N  N N 34  
A1A07 N25  N  N N 35  
A1A07 N30  N  Y N 36  
A1A07 O06  O  N N 37  
A1A07 O10  O  N N 38  
A1A07 O24  O  N N 39  
A1A07 S14  S  N N 40  
A1A07 H1   H  N N 41  
A1A07 H2   H  N N 42  
A1A07 H3   H  N N 43  
A1A07 H4   H  N N 44  
A1A07 H5   H  N N 45  
A1A07 H6   H  N N 46  
A1A07 H7   H  N N 47  
A1A07 H8   H  N N 48  
A1A07 H9   H  N N 49  
A1A07 H10  H  N N 50  
A1A07 H11  H  N N 51  
A1A07 H12  H  N N 52  
A1A07 H13  H  N N 53  
A1A07 H14  H  N N 54  
A1A07 H15  H  N N 55  
A1A07 H16  H  N N 56  
A1A07 H17  H  N N 57  
A1A07 H18  H  N N 58  
A1A07 H19  H  N N 59  
A1A07 H20  H  N N 60  
A1A07 H21  H  N N 61  
A1A07 H22  H  N N 62  
A1A07 H23  H  N N 63  
A1A07 H24  H  N N 64  
A1A07 H25  H  N N 65  
A1A07 H26  H  N N 66  
A1A07 H27  H  N N 67  
A1A07 H28  H  N N 68  
A1A07 H29  H  N N 69  
A1A07 H30  H  N N 70  
A1A07 H31  H  N N 71  
ALA   N    N  N N 72  
ALA   CA   C  N S 73  
ALA   C    C  N N 74  
ALA   O    O  N N 75  
ALA   CB   C  N N 76  
ALA   OXT  O  N N 77  
ALA   H    H  N N 78  
ALA   H2   H  N N 79  
ALA   HA   H  N N 80  
ALA   HB1  H  N N 81  
ALA   HB2  H  N N 82  
ALA   HB3  H  N N 83  
ALA   HXT  H  N N 84  
ARG   N    N  N N 85  
ARG   CA   C  N S 86  
ARG   C    C  N N 87  
ARG   O    O  N N 88  
ARG   CB   C  N N 89  
ARG   CG   C  N N 90  
ARG   CD   C  N N 91  
ARG   NE   N  N N 92  
ARG   CZ   C  N N 93  
ARG   NH1  N  N N 94  
ARG   NH2  N  N N 95  
ARG   OXT  O  N N 96  
ARG   H    H  N N 97  
ARG   H2   H  N N 98  
ARG   HA   H  N N 99  
ARG   HB2  H  N N 100 
ARG   HB3  H  N N 101 
ARG   HG2  H  N N 102 
ARG   HG3  H  N N 103 
ARG   HD2  H  N N 104 
ARG   HD3  H  N N 105 
ARG   HE   H  N N 106 
ARG   HH11 H  N N 107 
ARG   HH12 H  N N 108 
ARG   HH21 H  N N 109 
ARG   HH22 H  N N 110 
ARG   HXT  H  N N 111 
ASN   N    N  N N 112 
ASN   CA   C  N S 113 
ASN   C    C  N N 114 
ASN   O    O  N N 115 
ASN   CB   C  N N 116 
ASN   CG   C  N N 117 
ASN   OD1  O  N N 118 
ASN   ND2  N  N N 119 
ASN   OXT  O  N N 120 
ASN   H    H  N N 121 
ASN   H2   H  N N 122 
ASN   HA   H  N N 123 
ASN   HB2  H  N N 124 
ASN   HB3  H  N N 125 
ASN   HD21 H  N N 126 
ASN   HD22 H  N N 127 
ASN   HXT  H  N N 128 
ASP   N    N  N N 129 
ASP   CA   C  N S 130 
ASP   C    C  N N 131 
ASP   O    O  N N 132 
ASP   CB   C  N N 133 
ASP   CG   C  N N 134 
ASP   OD1  O  N N 135 
ASP   OD2  O  N N 136 
ASP   OXT  O  N N 137 
ASP   H    H  N N 138 
ASP   H2   H  N N 139 
ASP   HA   H  N N 140 
ASP   HB2  H  N N 141 
ASP   HB3  H  N N 142 
ASP   HD2  H  N N 143 
ASP   HXT  H  N N 144 
CYS   N    N  N N 145 
CYS   CA   C  N R 146 
CYS   C    C  N N 147 
CYS   O    O  N N 148 
CYS   CB   C  N N 149 
CYS   SG   S  N N 150 
CYS   OXT  O  N N 151 
CYS   H    H  N N 152 
CYS   H2   H  N N 153 
CYS   HA   H  N N 154 
CYS   HB2  H  N N 155 
CYS   HB3  H  N N 156 
CYS   HG   H  N N 157 
CYS   HXT  H  N N 158 
GLN   N    N  N N 159 
GLN   CA   C  N S 160 
GLN   C    C  N N 161 
GLN   O    O  N N 162 
GLN   CB   C  N N 163 
GLN   CG   C  N N 164 
GLN   CD   C  N N 165 
GLN   OE1  O  N N 166 
GLN   NE2  N  N N 167 
GLN   OXT  O  N N 168 
GLN   H    H  N N 169 
GLN   H2   H  N N 170 
GLN   HA   H  N N 171 
GLN   HB2  H  N N 172 
GLN   HB3  H  N N 173 
GLN   HG2  H  N N 174 
GLN   HG3  H  N N 175 
GLN   HE21 H  N N 176 
GLN   HE22 H  N N 177 
GLN   HXT  H  N N 178 
GLU   N    N  N N 179 
GLU   CA   C  N S 180 
GLU   C    C  N N 181 
GLU   O    O  N N 182 
GLU   CB   C  N N 183 
GLU   CG   C  N N 184 
GLU   CD   C  N N 185 
GLU   OE1  O  N N 186 
GLU   OE2  O  N N 187 
GLU   OXT  O  N N 188 
GLU   H    H  N N 189 
GLU   H2   H  N N 190 
GLU   HA   H  N N 191 
GLU   HB2  H  N N 192 
GLU   HB3  H  N N 193 
GLU   HG2  H  N N 194 
GLU   HG3  H  N N 195 
GLU   HE2  H  N N 196 
GLU   HXT  H  N N 197 
GLY   N    N  N N 198 
GLY   CA   C  N N 199 
GLY   C    C  N N 200 
GLY   O    O  N N 201 
GLY   OXT  O  N N 202 
GLY   H    H  N N 203 
GLY   H2   H  N N 204 
GLY   HA2  H  N N 205 
GLY   HA3  H  N N 206 
GLY   HXT  H  N N 207 
HEM   CHA  C  N N 208 
HEM   CHB  C  N N 209 
HEM   CHC  C  N N 210 
HEM   CHD  C  N N 211 
HEM   C1A  C  Y N 212 
HEM   C2A  C  Y N 213 
HEM   C3A  C  Y N 214 
HEM   C4A  C  Y N 215 
HEM   CMA  C  N N 216 
HEM   CAA  C  N N 217 
HEM   CBA  C  N N 218 
HEM   CGA  C  N N 219 
HEM   O1A  O  N N 220 
HEM   O2A  O  N N 221 
HEM   C1B  C  N N 222 
HEM   C2B  C  N N 223 
HEM   C3B  C  N N 224 
HEM   C4B  C  N N 225 
HEM   CMB  C  N N 226 
HEM   CAB  C  N N 227 
HEM   CBB  C  N N 228 
HEM   C1C  C  Y N 229 
HEM   C2C  C  Y N 230 
HEM   C3C  C  Y N 231 
HEM   C4C  C  Y N 232 
HEM   CMC  C  N N 233 
HEM   CAC  C  N N 234 
HEM   CBC  C  N N 235 
HEM   C1D  C  N N 236 
HEM   C2D  C  N N 237 
HEM   C3D  C  N N 238 
HEM   C4D  C  N N 239 
HEM   CMD  C  N N 240 
HEM   CAD  C  N N 241 
HEM   CBD  C  N N 242 
HEM   CGD  C  N N 243 
HEM   O1D  O  N N 244 
HEM   O2D  O  N N 245 
HEM   NA   N  Y N 246 
HEM   NB   N  N N 247 
HEM   NC   N  Y N 248 
HEM   ND   N  N N 249 
HEM   FE   FE N N 250 
HEM   HHB  H  N N 251 
HEM   HHC  H  N N 252 
HEM   HHD  H  N N 253 
HEM   HMA  H  N N 254 
HEM   HMAA H  N N 255 
HEM   HMAB H  N N 256 
HEM   HAA  H  N N 257 
HEM   HAAA H  N N 258 
HEM   HBA  H  N N 259 
HEM   HBAA H  N N 260 
HEM   HMB  H  N N 261 
HEM   HMBA H  N N 262 
HEM   HMBB H  N N 263 
HEM   HAB  H  N N 264 
HEM   HBB  H  N N 265 
HEM   HBBA H  N N 266 
HEM   HMC  H  N N 267 
HEM   HMCA H  N N 268 
HEM   HMCB H  N N 269 
HEM   HAC  H  N N 270 
HEM   HBC  H  N N 271 
HEM   HBCA H  N N 272 
HEM   HMD  H  N N 273 
HEM   HMDA H  N N 274 
HEM   HMDB H  N N 275 
HEM   HAD  H  N N 276 
HEM   HADA H  N N 277 
HEM   HBD  H  N N 278 
HEM   HBDA H  N N 279 
HEM   H2A  H  N N 280 
HEM   H2D  H  N N 281 
HEM   HHA  H  N N 282 
HIS   N    N  N N 283 
HIS   CA   C  N S 284 
HIS   C    C  N N 285 
HIS   O    O  N N 286 
HIS   CB   C  N N 287 
HIS   CG   C  Y N 288 
HIS   ND1  N  Y N 289 
HIS   CD2  C  Y N 290 
HIS   CE1  C  Y N 291 
HIS   NE2  N  Y N 292 
HIS   OXT  O  N N 293 
HIS   H    H  N N 294 
HIS   H2   H  N N 295 
HIS   HA   H  N N 296 
HIS   HB2  H  N N 297 
HIS   HB3  H  N N 298 
HIS   HD1  H  N N 299 
HIS   HD2  H  N N 300 
HIS   HE1  H  N N 301 
HIS   HE2  H  N N 302 
HIS   HXT  H  N N 303 
ILE   N    N  N N 304 
ILE   CA   C  N S 305 
ILE   C    C  N N 306 
ILE   O    O  N N 307 
ILE   CB   C  N S 308 
ILE   CG1  C  N N 309 
ILE   CG2  C  N N 310 
ILE   CD1  C  N N 311 
ILE   OXT  O  N N 312 
ILE   H    H  N N 313 
ILE   H2   H  N N 314 
ILE   HA   H  N N 315 
ILE   HB   H  N N 316 
ILE   HG12 H  N N 317 
ILE   HG13 H  N N 318 
ILE   HG21 H  N N 319 
ILE   HG22 H  N N 320 
ILE   HG23 H  N N 321 
ILE   HD11 H  N N 322 
ILE   HD12 H  N N 323 
ILE   HD13 H  N N 324 
ILE   HXT  H  N N 325 
LEU   N    N  N N 326 
LEU   CA   C  N S 327 
LEU   C    C  N N 328 
LEU   O    O  N N 329 
LEU   CB   C  N N 330 
LEU   CG   C  N N 331 
LEU   CD1  C  N N 332 
LEU   CD2  C  N N 333 
LEU   OXT  O  N N 334 
LEU   H    H  N N 335 
LEU   H2   H  N N 336 
LEU   HA   H  N N 337 
LEU   HB2  H  N N 338 
LEU   HB3  H  N N 339 
LEU   HG   H  N N 340 
LEU   HD11 H  N N 341 
LEU   HD12 H  N N 342 
LEU   HD13 H  N N 343 
LEU   HD21 H  N N 344 
LEU   HD22 H  N N 345 
LEU   HD23 H  N N 346 
LEU   HXT  H  N N 347 
LYS   N    N  N N 348 
LYS   CA   C  N S 349 
LYS   C    C  N N 350 
LYS   O    O  N N 351 
LYS   CB   C  N N 352 
LYS   CG   C  N N 353 
LYS   CD   C  N N 354 
LYS   CE   C  N N 355 
LYS   NZ   N  N N 356 
LYS   OXT  O  N N 357 
LYS   H    H  N N 358 
LYS   H2   H  N N 359 
LYS   HA   H  N N 360 
LYS   HB2  H  N N 361 
LYS   HB3  H  N N 362 
LYS   HG2  H  N N 363 
LYS   HG3  H  N N 364 
LYS   HD2  H  N N 365 
LYS   HD3  H  N N 366 
LYS   HE2  H  N N 367 
LYS   HE3  H  N N 368 
LYS   HZ1  H  N N 369 
LYS   HZ2  H  N N 370 
LYS   HZ3  H  N N 371 
LYS   HXT  H  N N 372 
MET   N    N  N N 373 
MET   CA   C  N S 374 
MET   C    C  N N 375 
MET   O    O  N N 376 
MET   CB   C  N N 377 
MET   CG   C  N N 378 
MET   SD   S  N N 379 
MET   CE   C  N N 380 
MET   OXT  O  N N 381 
MET   H    H  N N 382 
MET   H2   H  N N 383 
MET   HA   H  N N 384 
MET   HB2  H  N N 385 
MET   HB3  H  N N 386 
MET   HG2  H  N N 387 
MET   HG3  H  N N 388 
MET   HE1  H  N N 389 
MET   HE2  H  N N 390 
MET   HE3  H  N N 391 
MET   HXT  H  N N 392 
PHE   N    N  N N 393 
PHE   CA   C  N S 394 
PHE   C    C  N N 395 
PHE   O    O  N N 396 
PHE   CB   C  N N 397 
PHE   CG   C  Y N 398 
PHE   CD1  C  Y N 399 
PHE   CD2  C  Y N 400 
PHE   CE1  C  Y N 401 
PHE   CE2  C  Y N 402 
PHE   CZ   C  Y N 403 
PHE   OXT  O  N N 404 
PHE   H    H  N N 405 
PHE   H2   H  N N 406 
PHE   HA   H  N N 407 
PHE   HB2  H  N N 408 
PHE   HB3  H  N N 409 
PHE   HD1  H  N N 410 
PHE   HD2  H  N N 411 
PHE   HE1  H  N N 412 
PHE   HE2  H  N N 413 
PHE   HZ   H  N N 414 
PHE   HXT  H  N N 415 
PRO   N    N  N N 416 
PRO   CA   C  N S 417 
PRO   C    C  N N 418 
PRO   O    O  N N 419 
PRO   CB   C  N N 420 
PRO   CG   C  N N 421 
PRO   CD   C  N N 422 
PRO   OXT  O  N N 423 
PRO   H    H  N N 424 
PRO   HA   H  N N 425 
PRO   HB2  H  N N 426 
PRO   HB3  H  N N 427 
PRO   HG2  H  N N 428 
PRO   HG3  H  N N 429 
PRO   HD2  H  N N 430 
PRO   HD3  H  N N 431 
PRO   HXT  H  N N 432 
SER   N    N  N N 433 
SER   CA   C  N S 434 
SER   C    C  N N 435 
SER   O    O  N N 436 
SER   CB   C  N N 437 
SER   OG   O  N N 438 
SER   OXT  O  N N 439 
SER   H    H  N N 440 
SER   H2   H  N N 441 
SER   HA   H  N N 442 
SER   HB2  H  N N 443 
SER   HB3  H  N N 444 
SER   HG   H  N N 445 
SER   HXT  H  N N 446 
THR   N    N  N N 447 
THR   CA   C  N S 448 
THR   C    C  N N 449 
THR   O    O  N N 450 
THR   CB   C  N R 451 
THR   OG1  O  N N 452 
THR   CG2  C  N N 453 
THR   OXT  O  N N 454 
THR   H    H  N N 455 
THR   H2   H  N N 456 
THR   HA   H  N N 457 
THR   HB   H  N N 458 
THR   HG1  H  N N 459 
THR   HG21 H  N N 460 
THR   HG22 H  N N 461 
THR   HG23 H  N N 462 
THR   HXT  H  N N 463 
TRP   N    N  N N 464 
TRP   CA   C  N S 465 
TRP   C    C  N N 466 
TRP   O    O  N N 467 
TRP   CB   C  N N 468 
TRP   CG   C  Y N 469 
TRP   CD1  C  Y N 470 
TRP   CD2  C  Y N 471 
TRP   NE1  N  Y N 472 
TRP   CE2  C  Y N 473 
TRP   CE3  C  Y N 474 
TRP   CZ2  C  Y N 475 
TRP   CZ3  C  Y N 476 
TRP   CH2  C  Y N 477 
TRP   OXT  O  N N 478 
TRP   H    H  N N 479 
TRP   H2   H  N N 480 
TRP   HA   H  N N 481 
TRP   HB2  H  N N 482 
TRP   HB3  H  N N 483 
TRP   HD1  H  N N 484 
TRP   HE1  H  N N 485 
TRP   HE3  H  N N 486 
TRP   HZ2  H  N N 487 
TRP   HZ3  H  N N 488 
TRP   HH2  H  N N 489 
TRP   HXT  H  N N 490 
TYR   N    N  N N 491 
TYR   CA   C  N S 492 
TYR   C    C  N N 493 
TYR   O    O  N N 494 
TYR   CB   C  N N 495 
TYR   CG   C  Y N 496 
TYR   CD1  C  Y N 497 
TYR   CD2  C  Y N 498 
TYR   CE1  C  Y N 499 
TYR   CE2  C  Y N 500 
TYR   CZ   C  Y N 501 
TYR   OH   O  N N 502 
TYR   OXT  O  N N 503 
TYR   H    H  N N 504 
TYR   H2   H  N N 505 
TYR   HA   H  N N 506 
TYR   HB2  H  N N 507 
TYR   HB3  H  N N 508 
TYR   HD1  H  N N 509 
TYR   HD2  H  N N 510 
TYR   HE1  H  N N 511 
TYR   HE2  H  N N 512 
TYR   HH   H  N N 513 
TYR   HXT  H  N N 514 
VAL   N    N  N N 515 
VAL   CA   C  N S 516 
VAL   C    C  N N 517 
VAL   O    O  N N 518 
VAL   CB   C  N N 519 
VAL   CG1  C  N N 520 
VAL   CG2  C  N N 521 
VAL   OXT  O  N N 522 
VAL   H    H  N N 523 
VAL   H2   H  N N 524 
VAL   HA   H  N N 525 
VAL   HB   H  N N 526 
VAL   HG11 H  N N 527 
VAL   HG12 H  N N 528 
VAL   HG13 H  N N 529 
VAL   HG21 H  N N 530 
VAL   HG22 H  N N 531 
VAL   HG23 H  N N 532 
VAL   HXT  H  N N 533 
# 
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 
A1A07 O10 C09  doub N N 1   
A1A07 C08 N07  sing N N 2   
A1A07 C08 C09  sing N N 3   
A1A07 N07 C05  sing N N 4   
A1A07 C09 N11  sing N N 5   
A1A07 F03 C02  sing N N 6   
A1A07 F04 C02  sing N N 7   
A1A07 C40 C39  doub Y N 8   
A1A07 C40 C35  sing Y N 9   
A1A07 C39 C38  sing Y N 10  
A1A07 C05 C02  sing N N 11  
A1A07 C05 O06  doub N N 12  
A1A07 C34 C35  sing N N 13  
A1A07 C34 C12  sing N N 14  
A1A07 C02 F01  sing N N 15  
A1A07 C31 C32  doub Y N 16  
A1A07 C31 N30  sing Y N 17  
A1A07 C32 C33  sing Y N 18  
A1A07 C35 C36  doub Y N 19  
A1A07 N11 C12  sing N N 20  
A1A07 C38 C37  doub Y N 21  
A1A07 C12 C13  sing N N 22  
A1A07 N30 C29  doub Y N 23  
A1A07 C36 C37  sing Y N 24  
A1A07 C33 C28  doub Y N 25  
A1A07 C13 S14  sing N N 26  
A1A07 C29 C28  sing Y N 27  
A1A07 C28 C27  sing N N 28  
A1A07 S14 C15  sing N N 29  
A1A07 C15 C16  sing N N 30  
A1A07 C15 C23  sing N N 31  
A1A07 C27 C26  sing N N 32  
A1A07 C26 N25  sing N N 33  
A1A07 C16 C17  sing N N 34  
A1A07 C23 N25  sing N N 35  
A1A07 C23 O24  doub N N 36  
A1A07 C17 C18  doub Y N 37  
A1A07 C17 C22  sing Y N 38  
A1A07 C18 C19  sing Y N 39  
A1A07 C22 C21  doub Y N 40  
A1A07 C19 C20  doub Y N 41  
A1A07 C21 C20  sing Y N 42  
A1A07 C13 H1   sing N N 43  
A1A07 C13 H2   sing N N 44  
A1A07 C15 H3   sing N N 45  
A1A07 C20 H4   sing N N 46  
A1A07 C21 H5   sing N N 47  
A1A07 C22 H6   sing N N 48  
A1A07 C26 H7   sing N N 49  
A1A07 C08 H8   sing N N 50  
A1A07 C08 H9   sing N N 51  
A1A07 C12 H10  sing N N 52  
A1A07 C16 H11  sing N N 53  
A1A07 C16 H12  sing N N 54  
A1A07 C18 H13  sing N N 55  
A1A07 C19 H14  sing N N 56  
A1A07 C27 H15  sing N N 57  
A1A07 C27 H16  sing N N 58  
A1A07 C29 H17  sing N N 59  
A1A07 C31 H18  sing N N 60  
A1A07 C32 H19  sing N N 61  
A1A07 C33 H20  sing N N 62  
A1A07 C34 H21  sing N N 63  
A1A07 C34 H22  sing N N 64  
A1A07 C36 H23  sing N N 65  
A1A07 C37 H24  sing N N 66  
A1A07 C38 H25  sing N N 67  
A1A07 C39 H26  sing N N 68  
A1A07 C40 H27  sing N N 69  
A1A07 N07 H28  sing N N 70  
A1A07 N11 H29  sing N N 71  
A1A07 C26 H30  sing N N 72  
A1A07 N25 H31  sing N N 73  
ALA   N   CA   sing N N 74  
ALA   N   H    sing N N 75  
ALA   N   H2   sing N N 76  
ALA   CA  C    sing N N 77  
ALA   CA  CB   sing N N 78  
ALA   CA  HA   sing N N 79  
ALA   C   O    doub N N 80  
ALA   C   OXT  sing N N 81  
ALA   CB  HB1  sing N N 82  
ALA   CB  HB2  sing N N 83  
ALA   CB  HB3  sing N N 84  
ALA   OXT HXT  sing N N 85  
ARG   N   CA   sing N N 86  
ARG   N   H    sing N N 87  
ARG   N   H2   sing N N 88  
ARG   CA  C    sing N N 89  
ARG   CA  CB   sing N N 90  
ARG   CA  HA   sing N N 91  
ARG   C   O    doub N N 92  
ARG   C   OXT  sing N N 93  
ARG   CB  CG   sing N N 94  
ARG   CB  HB2  sing N N 95  
ARG   CB  HB3  sing N N 96  
ARG   CG  CD   sing N N 97  
ARG   CG  HG2  sing N N 98  
ARG   CG  HG3  sing N N 99  
ARG   CD  NE   sing N N 100 
ARG   CD  HD2  sing N N 101 
ARG   CD  HD3  sing N N 102 
ARG   NE  CZ   sing N N 103 
ARG   NE  HE   sing N N 104 
ARG   CZ  NH1  sing N N 105 
ARG   CZ  NH2  doub N N 106 
ARG   NH1 HH11 sing N N 107 
ARG   NH1 HH12 sing N N 108 
ARG   NH2 HH21 sing N N 109 
ARG   NH2 HH22 sing N N 110 
ARG   OXT HXT  sing N N 111 
ASN   N   CA   sing N N 112 
ASN   N   H    sing N N 113 
ASN   N   H2   sing N N 114 
ASN   CA  C    sing N N 115 
ASN   CA  CB   sing N N 116 
ASN   CA  HA   sing N N 117 
ASN   C   O    doub N N 118 
ASN   C   OXT  sing N N 119 
ASN   CB  CG   sing N N 120 
ASN   CB  HB2  sing N N 121 
ASN   CB  HB3  sing N N 122 
ASN   CG  OD1  doub N N 123 
ASN   CG  ND2  sing N N 124 
ASN   ND2 HD21 sing N N 125 
ASN   ND2 HD22 sing N N 126 
ASN   OXT HXT  sing N N 127 
ASP   N   CA   sing N N 128 
ASP   N   H    sing N N 129 
ASP   N   H2   sing N N 130 
ASP   CA  C    sing N N 131 
ASP   CA  CB   sing N N 132 
ASP   CA  HA   sing N N 133 
ASP   C   O    doub N N 134 
ASP   C   OXT  sing N N 135 
ASP   CB  CG   sing N N 136 
ASP   CB  HB2  sing N N 137 
ASP   CB  HB3  sing N N 138 
ASP   CG  OD1  doub N N 139 
ASP   CG  OD2  sing N N 140 
ASP   OD2 HD2  sing N N 141 
ASP   OXT HXT  sing N N 142 
CYS   N   CA   sing N N 143 
CYS   N   H    sing N N 144 
CYS   N   H2   sing N N 145 
CYS   CA  C    sing N N 146 
CYS   CA  CB   sing N N 147 
CYS   CA  HA   sing N N 148 
CYS   C   O    doub N N 149 
CYS   C   OXT  sing N N 150 
CYS   CB  SG   sing N N 151 
CYS   CB  HB2  sing N N 152 
CYS   CB  HB3  sing N N 153 
CYS   SG  HG   sing N N 154 
CYS   OXT HXT  sing N N 155 
GLN   N   CA   sing N N 156 
GLN   N   H    sing N N 157 
GLN   N   H2   sing N N 158 
GLN   CA  C    sing N N 159 
GLN   CA  CB   sing N N 160 
GLN   CA  HA   sing N N 161 
GLN   C   O    doub N N 162 
GLN   C   OXT  sing N N 163 
GLN   CB  CG   sing N N 164 
GLN   CB  HB2  sing N N 165 
GLN   CB  HB3  sing N N 166 
GLN   CG  CD   sing N N 167 
GLN   CG  HG2  sing N N 168 
GLN   CG  HG3  sing N N 169 
GLN   CD  OE1  doub N N 170 
GLN   CD  NE2  sing N N 171 
GLN   NE2 HE21 sing N N 172 
GLN   NE2 HE22 sing N N 173 
GLN   OXT HXT  sing N N 174 
GLU   N   CA   sing N N 175 
GLU   N   H    sing N N 176 
GLU   N   H2   sing N N 177 
GLU   CA  C    sing N N 178 
GLU   CA  CB   sing N N 179 
GLU   CA  HA   sing N N 180 
GLU   C   O    doub N N 181 
GLU   C   OXT  sing N N 182 
GLU   CB  CG   sing N N 183 
GLU   CB  HB2  sing N N 184 
GLU   CB  HB3  sing N N 185 
GLU   CG  CD   sing N N 186 
GLU   CG  HG2  sing N N 187 
GLU   CG  HG3  sing N N 188 
GLU   CD  OE1  doub N N 189 
GLU   CD  OE2  sing N N 190 
GLU   OE2 HE2  sing N N 191 
GLU   OXT HXT  sing N N 192 
GLY   N   CA   sing N N 193 
GLY   N   H    sing N N 194 
GLY   N   H2   sing N N 195 
GLY   CA  C    sing N N 196 
GLY   CA  HA2  sing N N 197 
GLY   CA  HA3  sing N N 198 
GLY   C   O    doub N N 199 
GLY   C   OXT  sing N N 200 
GLY   OXT HXT  sing N N 201 
HEM   CHA C1A  sing N N 202 
HEM   CHA C4D  doub N N 203 
HEM   CHA HHA  sing N N 204 
HEM   CHB C4A  sing N N 205 
HEM   CHB C1B  doub N N 206 
HEM   CHB HHB  sing N N 207 
HEM   CHC C4B  sing N N 208 
HEM   CHC C1C  doub N N 209 
HEM   CHC HHC  sing N N 210 
HEM   CHD C4C  doub N N 211 
HEM   CHD C1D  sing N N 212 
HEM   CHD HHD  sing N N 213 
HEM   C1A C2A  doub Y N 214 
HEM   C1A NA   sing Y N 215 
HEM   C2A C3A  sing Y N 216 
HEM   C2A CAA  sing N N 217 
HEM   C3A C4A  doub Y N 218 
HEM   C3A CMA  sing N N 219 
HEM   C4A NA   sing Y N 220 
HEM   CMA HMA  sing N N 221 
HEM   CMA HMAA sing N N 222 
HEM   CMA HMAB sing N N 223 
HEM   CAA CBA  sing N N 224 
HEM   CAA HAA  sing N N 225 
HEM   CAA HAAA sing N N 226 
HEM   CBA CGA  sing N N 227 
HEM   CBA HBA  sing N N 228 
HEM   CBA HBAA sing N N 229 
HEM   CGA O1A  doub N N 230 
HEM   CGA O2A  sing N N 231 
HEM   C1B C2B  sing N N 232 
HEM   C1B NB   sing N N 233 
HEM   C2B C3B  doub N N 234 
HEM   C2B CMB  sing N N 235 
HEM   C3B C4B  sing N N 236 
HEM   C3B CAB  sing N N 237 
HEM   C4B NB   doub N N 238 
HEM   CMB HMB  sing N N 239 
HEM   CMB HMBA sing N N 240 
HEM   CMB HMBB sing N N 241 
HEM   CAB CBB  doub N N 242 
HEM   CAB HAB  sing N N 243 
HEM   CBB HBB  sing N N 244 
HEM   CBB HBBA sing N N 245 
HEM   C1C C2C  sing Y N 246 
HEM   C1C NC   sing Y N 247 
HEM   C2C C3C  doub Y N 248 
HEM   C2C CMC  sing N N 249 
HEM   C3C C4C  sing Y N 250 
HEM   C3C CAC  sing N N 251 
HEM   C4C NC   sing Y N 252 
HEM   CMC HMC  sing N N 253 
HEM   CMC HMCA sing N N 254 
HEM   CMC HMCB sing N N 255 
HEM   CAC CBC  doub N N 256 
HEM   CAC HAC  sing N N 257 
HEM   CBC HBC  sing N N 258 
HEM   CBC HBCA sing N N 259 
HEM   C1D C2D  sing N N 260 
HEM   C1D ND   doub N N 261 
HEM   C2D C3D  doub N N 262 
HEM   C2D CMD  sing N N 263 
HEM   C3D C4D  sing N N 264 
HEM   C3D CAD  sing N N 265 
HEM   C4D ND   sing N N 266 
HEM   CMD HMD  sing N N 267 
HEM   CMD HMDA sing N N 268 
HEM   CMD HMDB sing N N 269 
HEM   CAD CBD  sing N N 270 
HEM   CAD HAD  sing N N 271 
HEM   CAD HADA sing N N 272 
HEM   CBD CGD  sing N N 273 
HEM   CBD HBD  sing N N 274 
HEM   CBD HBDA sing N N 275 
HEM   CGD O1D  doub N N 276 
HEM   CGD O2D  sing N N 277 
HEM   O2A H2A  sing N N 278 
HEM   O2D H2D  sing N N 279 
HEM   FE  NA   sing N N 280 
HEM   FE  NB   sing N N 281 
HEM   FE  NC   sing N N 282 
HEM   FE  ND   sing N N 283 
HIS   N   CA   sing N N 284 
HIS   N   H    sing N N 285 
HIS   N   H2   sing N N 286 
HIS   CA  C    sing N N 287 
HIS   CA  CB   sing N N 288 
HIS   CA  HA   sing N N 289 
HIS   C   O    doub N N 290 
HIS   C   OXT  sing N N 291 
HIS   CB  CG   sing N N 292 
HIS   CB  HB2  sing N N 293 
HIS   CB  HB3  sing N N 294 
HIS   CG  ND1  sing Y N 295 
HIS   CG  CD2  doub Y N 296 
HIS   ND1 CE1  doub Y N 297 
HIS   ND1 HD1  sing N N 298 
HIS   CD2 NE2  sing Y N 299 
HIS   CD2 HD2  sing N N 300 
HIS   CE1 NE2  sing Y N 301 
HIS   CE1 HE1  sing N N 302 
HIS   NE2 HE2  sing N N 303 
HIS   OXT HXT  sing N N 304 
ILE   N   CA   sing N N 305 
ILE   N   H    sing N N 306 
ILE   N   H2   sing N N 307 
ILE   CA  C    sing N N 308 
ILE   CA  CB   sing N N 309 
ILE   CA  HA   sing N N 310 
ILE   C   O    doub N N 311 
ILE   C   OXT  sing N N 312 
ILE   CB  CG1  sing N N 313 
ILE   CB  CG2  sing N N 314 
ILE   CB  HB   sing N N 315 
ILE   CG1 CD1  sing N N 316 
ILE   CG1 HG12 sing N N 317 
ILE   CG1 HG13 sing N N 318 
ILE   CG2 HG21 sing N N 319 
ILE   CG2 HG22 sing N N 320 
ILE   CG2 HG23 sing N N 321 
ILE   CD1 HD11 sing N N 322 
ILE   CD1 HD12 sing N N 323 
ILE   CD1 HD13 sing N N 324 
ILE   OXT HXT  sing N N 325 
LEU   N   CA   sing N N 326 
LEU   N   H    sing N N 327 
LEU   N   H2   sing N N 328 
LEU   CA  C    sing N N 329 
LEU   CA  CB   sing N N 330 
LEU   CA  HA   sing N N 331 
LEU   C   O    doub N N 332 
LEU   C   OXT  sing N N 333 
LEU   CB  CG   sing N N 334 
LEU   CB  HB2  sing N N 335 
LEU   CB  HB3  sing N N 336 
LEU   CG  CD1  sing N N 337 
LEU   CG  CD2  sing N N 338 
LEU   CG  HG   sing N N 339 
LEU   CD1 HD11 sing N N 340 
LEU   CD1 HD12 sing N N 341 
LEU   CD1 HD13 sing N N 342 
LEU   CD2 HD21 sing N N 343 
LEU   CD2 HD22 sing N N 344 
LEU   CD2 HD23 sing N N 345 
LEU   OXT HXT  sing N N 346 
LYS   N   CA   sing N N 347 
LYS   N   H    sing N N 348 
LYS   N   H2   sing N N 349 
LYS   CA  C    sing N N 350 
LYS   CA  CB   sing N N 351 
LYS   CA  HA   sing N N 352 
LYS   C   O    doub N N 353 
LYS   C   OXT  sing N N 354 
LYS   CB  CG   sing N N 355 
LYS   CB  HB2  sing N N 356 
LYS   CB  HB3  sing N N 357 
LYS   CG  CD   sing N N 358 
LYS   CG  HG2  sing N N 359 
LYS   CG  HG3  sing N N 360 
LYS   CD  CE   sing N N 361 
LYS   CD  HD2  sing N N 362 
LYS   CD  HD3  sing N N 363 
LYS   CE  NZ   sing N N 364 
LYS   CE  HE2  sing N N 365 
LYS   CE  HE3  sing N N 366 
LYS   NZ  HZ1  sing N N 367 
LYS   NZ  HZ2  sing N N 368 
LYS   NZ  HZ3  sing N N 369 
LYS   OXT HXT  sing N N 370 
MET   N   CA   sing N N 371 
MET   N   H    sing N N 372 
MET   N   H2   sing N N 373 
MET   CA  C    sing N N 374 
MET   CA  CB   sing N N 375 
MET   CA  HA   sing N N 376 
MET   C   O    doub N N 377 
MET   C   OXT  sing N N 378 
MET   CB  CG   sing N N 379 
MET   CB  HB2  sing N N 380 
MET   CB  HB3  sing N N 381 
MET   CG  SD   sing N N 382 
MET   CG  HG2  sing N N 383 
MET   CG  HG3  sing N N 384 
MET   SD  CE   sing N N 385 
MET   CE  HE1  sing N N 386 
MET   CE  HE2  sing N N 387 
MET   CE  HE3  sing N N 388 
MET   OXT HXT  sing N N 389 
PHE   N   CA   sing N N 390 
PHE   N   H    sing N N 391 
PHE   N   H2   sing N N 392 
PHE   CA  C    sing N N 393 
PHE   CA  CB   sing N N 394 
PHE   CA  HA   sing N N 395 
PHE   C   O    doub N N 396 
PHE   C   OXT  sing N N 397 
PHE   CB  CG   sing N N 398 
PHE   CB  HB2  sing N N 399 
PHE   CB  HB3  sing N N 400 
PHE   CG  CD1  doub Y N 401 
PHE   CG  CD2  sing Y N 402 
PHE   CD1 CE1  sing Y N 403 
PHE   CD1 HD1  sing N N 404 
PHE   CD2 CE2  doub Y N 405 
PHE   CD2 HD2  sing N N 406 
PHE   CE1 CZ   doub Y N 407 
PHE   CE1 HE1  sing N N 408 
PHE   CE2 CZ   sing Y N 409 
PHE   CE2 HE2  sing N N 410 
PHE   CZ  HZ   sing N N 411 
PHE   OXT HXT  sing N N 412 
PRO   N   CA   sing N N 413 
PRO   N   CD   sing N N 414 
PRO   N   H    sing N N 415 
PRO   CA  C    sing N N 416 
PRO   CA  CB   sing N N 417 
PRO   CA  HA   sing N N 418 
PRO   C   O    doub N N 419 
PRO   C   OXT  sing N N 420 
PRO   CB  CG   sing N N 421 
PRO   CB  HB2  sing N N 422 
PRO   CB  HB3  sing N N 423 
PRO   CG  CD   sing N N 424 
PRO   CG  HG2  sing N N 425 
PRO   CG  HG3  sing N N 426 
PRO   CD  HD2  sing N N 427 
PRO   CD  HD3  sing N N 428 
PRO   OXT HXT  sing N N 429 
SER   N   CA   sing N N 430 
SER   N   H    sing N N 431 
SER   N   H2   sing N N 432 
SER   CA  C    sing N N 433 
SER   CA  CB   sing N N 434 
SER   CA  HA   sing N N 435 
SER   C   O    doub N N 436 
SER   C   OXT  sing N N 437 
SER   CB  OG   sing N N 438 
SER   CB  HB2  sing N N 439 
SER   CB  HB3  sing N N 440 
SER   OG  HG   sing N N 441 
SER   OXT HXT  sing N N 442 
THR   N   CA   sing N N 443 
THR   N   H    sing N N 444 
THR   N   H2   sing N N 445 
THR   CA  C    sing N N 446 
THR   CA  CB   sing N N 447 
THR   CA  HA   sing N N 448 
THR   C   O    doub N N 449 
THR   C   OXT  sing N N 450 
THR   CB  OG1  sing N N 451 
THR   CB  CG2  sing N N 452 
THR   CB  HB   sing N N 453 
THR   OG1 HG1  sing N N 454 
THR   CG2 HG21 sing N N 455 
THR   CG2 HG22 sing N N 456 
THR   CG2 HG23 sing N N 457 
THR   OXT HXT  sing N N 458 
TRP   N   CA   sing N N 459 
TRP   N   H    sing N N 460 
TRP   N   H2   sing N N 461 
TRP   CA  C    sing N N 462 
TRP   CA  CB   sing N N 463 
TRP   CA  HA   sing N N 464 
TRP   C   O    doub N N 465 
TRP   C   OXT  sing N N 466 
TRP   CB  CG   sing N N 467 
TRP   CB  HB2  sing N N 468 
TRP   CB  HB3  sing N N 469 
TRP   CG  CD1  doub Y N 470 
TRP   CG  CD2  sing Y N 471 
TRP   CD1 NE1  sing Y N 472 
TRP   CD1 HD1  sing N N 473 
TRP   CD2 CE2  doub Y N 474 
TRP   CD2 CE3  sing Y N 475 
TRP   NE1 CE2  sing Y N 476 
TRP   NE1 HE1  sing N N 477 
TRP   CE2 CZ2  sing Y N 478 
TRP   CE3 CZ3  doub Y N 479 
TRP   CE3 HE3  sing N N 480 
TRP   CZ2 CH2  doub Y N 481 
TRP   CZ2 HZ2  sing N N 482 
TRP   CZ3 CH2  sing Y N 483 
TRP   CZ3 HZ3  sing N N 484 
TRP   CH2 HH2  sing N N 485 
TRP   OXT HXT  sing N N 486 
TYR   N   CA   sing N N 487 
TYR   N   H    sing N N 488 
TYR   N   H2   sing N N 489 
TYR   CA  C    sing N N 490 
TYR   CA  CB   sing N N 491 
TYR   CA  HA   sing N N 492 
TYR   C   O    doub N N 493 
TYR   C   OXT  sing N N 494 
TYR   CB  CG   sing N N 495 
TYR   CB  HB2  sing N N 496 
TYR   CB  HB3  sing N N 497 
TYR   CG  CD1  doub Y N 498 
TYR   CG  CD2  sing Y N 499 
TYR   CD1 CE1  sing Y N 500 
TYR   CD1 HD1  sing N N 501 
TYR   CD2 CE2  doub Y N 502 
TYR   CD2 HD2  sing N N 503 
TYR   CE1 CZ   doub Y N 504 
TYR   CE1 HE1  sing N N 505 
TYR   CE2 CZ   sing Y N 506 
TYR   CE2 HE2  sing N N 507 
TYR   CZ  OH   sing N N 508 
TYR   OH  HH   sing N N 509 
TYR   OXT HXT  sing N N 510 
VAL   N   CA   sing N N 511 
VAL   N   H    sing N N 512 
VAL   N   H2   sing N N 513 
VAL   CA  C    sing N N 514 
VAL   CA  CB   sing N N 515 
VAL   CA  HA   sing N N 516 
VAL   C   O    doub N N 517 
VAL   C   OXT  sing N N 518 
VAL   CB  CG1  sing N N 519 
VAL   CB  CG2  sing N N 520 
VAL   CB  HB   sing N N 521 
VAL   CG1 HG11 sing N N 522 
VAL   CG1 HG12 sing N N 523 
VAL   CG1 HG13 sing N N 524 
VAL   CG2 HG21 sing N N 525 
VAL   CG2 HG22 sing N N 526 
VAL   CG2 HG23 sing N N 527 
VAL   OXT HXT  sing N N 528 
# 
_pdbx_audit_support.funding_organization   
'National Institutes of Health/National Institute of Environmental Health Sciences (NIH/NIEHS)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           ES025767 
_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   5vcc 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9COR 
_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]   0.013154 
_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]   0.009871 
_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]   0.008016 
_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  
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 8   ? -8.249  -58.823 -15.518 1.00 132.63 ? 28  HIS   A N   1 
ATOM   2    C  CA  . HIS   A 1 8   ? -9.200  -59.890 -15.231 1.00 142.72 ? 28  HIS   A CA  1 
ATOM   3    C  C   . HIS   A 1 8   ? -10.642 -59.407 -15.399 1.00 132.61 ? 28  HIS   A C   1 
ATOM   4    O  O   . HIS   A 1 8   ? -11.428 -60.041 -16.108 1.00 131.84 ? 28  HIS   A O   1 
ATOM   5    C  CB  . HIS   A 1 8   ? -8.978  -60.436 -13.820 1.00 162.95 ? 28  HIS   A CB  1 
ATOM   6    C  CG  . HIS   A 1 8   ? -8.736  -59.375 -12.794 1.00 178.00 ? 28  HIS   A CG  1 
ATOM   7    N  ND1 . HIS   A 1 8   ? -9.754  -58.792 -12.072 1.00 172.34 ? 28  HIS   A ND1 1 
ATOM   8    C  CD2 . HIS   A 1 8   ? -7.591  -58.787 -12.372 1.00 177.55 ? 28  HIS   A CD2 1 
ATOM   9    C  CE1 . HIS   A 1 8   ? -9.247  -57.893 -11.246 1.00 158.48 ? 28  HIS   A CE1 1 
ATOM   10   N  NE2 . HIS   A 1 8   ? -7.937  -57.871 -11.409 1.00 167.95 ? 28  HIS   A NE2 1 
ATOM   11   N  N   . SER   A 1 9   ? -10.981 -58.284 -14.758 1.00 124.52 ? 29  SER   A N   1 
ATOM   12   C  CA  . SER   A 1 9   ? -12.300 -57.683 -14.926 1.00 110.42 ? 29  SER   A CA  1 
ATOM   13   C  C   . SER   A 1 9   ? -12.534 -57.184 -16.351 1.00 106.30 ? 29  SER   A C   1 
ATOM   14   O  O   . SER   A 1 9   ? -13.615 -56.660 -16.632 1.00 96.23  ? 29  SER   A O   1 
ATOM   15   C  CB  . SER   A 1 9   ? -12.484 -56.529 -13.934 1.00 110.68 ? 29  SER   A CB  1 
ATOM   16   O  OG  . SER   A 1 9   ? -11.596 -55.470 -14.236 1.00 109.50 ? 29  SER   A OG  1 
ATOM   17   N  N   . HIS   A 1 10  ? -11.552 -57.329 -17.244 1.00 102.62 ? 30  HIS   A N   1 
ATOM   18   C  CA  . HIS   A 1 10  ? -11.637 -56.861 -18.626 1.00 94.58  ? 30  HIS   A CA  1 
ATOM   19   C  C   . HIS   A 1 10  ? -12.487 -57.758 -19.523 1.00 109.15 ? 30  HIS   A C   1 
ATOM   20   O  O   . HIS   A 1 10  ? -12.658 -57.446 -20.707 1.00 108.72 ? 30  HIS   A O   1 
ATOM   21   C  CB  . HIS   A 1 10  ? -10.226 -56.728 -19.215 1.00 94.60  ? 30  HIS   A CB  1 
ATOM   22   C  CG  . HIS   A 1 10  ? -9.358  -55.757 -18.476 1.00 91.09  ? 30  HIS   A CG  1 
ATOM   23   N  ND1 . HIS   A 1 10  ? -9.876  -54.788 -17.646 1.00 94.34  ? 30  HIS   A ND1 1 
ATOM   24   C  CD2 . HIS   A 1 10  ? -8.012  -55.611 -18.429 1.00 76.95  ? 30  HIS   A CD2 1 
ATOM   25   C  CE1 . HIS   A 1 10  ? -8.889  -54.083 -17.123 1.00 88.14  ? 30  HIS   A CE1 1 
ATOM   26   N  NE2 . HIS   A 1 10  ? -7.747  -54.561 -17.582 1.00 89.48  ? 30  HIS   A NE2 1 
ATOM   27   N  N   . GLY   A 1 11  ? -13.018 -58.860 -18.997 1.00 102.28 ? 31  GLY   A N   1 
ATOM   28   C  CA  . GLY   A 1 11  ? -13.906 -59.713 -19.759 1.00 96.78  ? 31  GLY   A CA  1 
ATOM   29   C  C   . GLY   A 1 11  ? -15.363 -59.333 -19.700 1.00 104.70 ? 31  GLY   A C   1 
ATOM   30   O  O   . GLY   A 1 11  ? -16.161 -59.861 -20.479 1.00 112.56 ? 31  GLY   A O   1 
ATOM   31   N  N   . LEU   A 1 12  ? -15.722 -58.407 -18.813 1.00 102.69 ? 32  LEU   A N   1 
ATOM   32   C  CA  . LEU   A 1 12  ? -17.113 -58.078 -18.524 1.00 103.31 ? 32  LEU   A CA  1 
ATOM   33   C  C   . LEU   A 1 12  ? -17.881 -57.626 -19.759 1.00 101.80 ? 32  LEU   A C   1 
ATOM   34   O  O   . LEU   A 1 12  ? -18.814 -58.308 -20.194 1.00 108.61 ? 32  LEU   A O   1 
ATOM   35   C  CB  . LEU   A 1 12  ? -17.181 -56.993 -17.450 1.00 94.17  ? 32  LEU   A CB  1 
ATOM   36   C  CG  . LEU   A 1 12  ? -18.602 -56.559 -17.092 1.00 91.19  ? 32  LEU   A CG  1 
ATOM   37   C  CD1 . LEU   A 1 12  ? -19.273 -57.620 -16.235 1.00 99.09  ? 32  LEU   A CD1 1 
ATOM   38   C  CD2 . LEU   A 1 12  ? -18.614 -55.202 -16.404 1.00 87.83  ? 32  LEU   A CD2 1 
ATOM   39   N  N   . PHE   A 1 13  ? -17.497 -56.477 -20.326 1.00 95.86  ? 33  PHE   A N   1 
ATOM   40   C  CA  . PHE   A 1 13  ? -18.212 -55.937 -21.480 1.00 99.07  ? 33  PHE   A CA  1 
ATOM   41   C  C   . PHE   A 1 13  ? -18.236 -56.929 -22.636 1.00 103.54 ? 33  PHE   A C   1 
ATOM   42   O  O   . PHE   A 1 13  ? -19.245 -57.048 -23.342 1.00 111.71 ? 33  PHE   A O   1 
ATOM   43   C  CB  . PHE   A 1 13  ? -17.574 -54.621 -21.924 1.00 99.34  ? 33  PHE   A CB  1 
ATOM   44   C  CG  . PHE   A 1 13  ? -17.732 -53.503 -20.933 1.00 100.59 ? 33  PHE   A CG  1 
ATOM   45   C  CD1 . PHE   A 1 13  ? -18.965 -53.230 -20.363 1.00 100.40 ? 33  PHE   A CD1 1 
ATOM   46   C  CD2 . PHE   A 1 13  ? -16.645 -52.724 -20.572 1.00 99.15  ? 33  PHE   A CD2 1 
ATOM   47   C  CE1 . PHE   A 1 13  ? -19.109 -52.198 -19.453 1.00 97.22  ? 33  PHE   A CE1 1 
ATOM   48   C  CE2 . PHE   A 1 13  ? -16.783 -51.695 -19.661 1.00 95.64  ? 33  PHE   A CE2 1 
ATOM   49   C  CZ  . PHE   A 1 13  ? -18.016 -51.431 -19.102 1.00 96.97  ? 33  PHE   A CZ  1 
ATOM   50   N  N   . LYS   A 1 14  ? -17.128 -57.645 -22.845 1.00 121.35 ? 34  LYS   A N   1 
ATOM   51   C  CA  . LYS   A 1 14  ? -17.079 -58.685 -23.868 1.00 120.08 ? 34  LYS   A CA  1 
ATOM   52   C  C   . LYS   A 1 14  ? -18.195 -59.704 -23.673 1.00 123.14 ? 34  LYS   A C   1 
ATOM   53   O  O   . LYS   A 1 14  ? -18.903 -60.058 -24.623 1.00 127.95 ? 34  LYS   A O   1 
ATOM   54   C  CB  . LYS   A 1 14  ? -15.711 -59.368 -23.834 1.00 127.25 ? 34  LYS   A CB  1 
ATOM   55   C  CG  . LYS   A 1 14  ? -15.682 -60.741 -24.472 1.00 139.46 ? 34  LYS   A CG  1 
ATOM   56   C  CD  . LYS   A 1 14  ? -14.491 -61.541 -23.973 1.00 149.50 ? 34  LYS   A CD  1 
ATOM   57   C  CE  . LYS   A 1 14  ? -14.450 -62.918 -24.609 1.00 163.46 ? 34  LYS   A CE  1 
ATOM   58   N  NZ  . LYS   A 1 14  ? -15.729 -63.657 -24.417 1.00 165.75 ? 34  LYS   A NZ  1 
ATOM   59   N  N   . LYS   A 1 15  ? -18.362 -60.190 -22.441 1.00 106.24 ? 35  LYS   A N   1 
ATOM   60   C  CA  . LYS   A 1 15  ? -19.463 -61.100 -22.142 1.00 109.11 ? 35  LYS   A CA  1 
ATOM   61   C  C   . LYS   A 1 15  ? -20.808 -60.434 -22.404 1.00 104.95 ? 35  LYS   A C   1 
ATOM   62   O  O   . LYS   A 1 15  ? -21.703 -61.032 -23.013 1.00 118.62 ? 35  LYS   A O   1 
ATOM   63   C  CB  . LYS   A 1 15  ? -19.375 -61.573 -20.692 1.00 115.65 ? 35  LYS   A CB  1 
ATOM   64   C  CG  . LYS   A 1 15  ? -20.538 -62.448 -20.254 1.00 118.22 ? 35  LYS   A CG  1 
ATOM   65   C  CD  . LYS   A 1 15  ? -20.788 -62.318 -18.762 1.00 126.68 ? 35  LYS   A CD  1 
ATOM   66   C  CE  . LYS   A 1 15  ? -21.218 -60.903 -18.407 1.00 121.62 ? 35  LYS   A CE  1 
ATOM   67   N  NZ  . LYS   A 1 15  ? -21.505 -60.755 -16.955 1.00 128.02 ? 35  LYS   A NZ  1 
ATOM   68   N  N   . LEU   A 1 16  ? -20.968 -59.188 -21.952 1.00 114.83 ? 36  LEU   A N   1 
ATOM   69   C  CA  . LEU   A 1 16  ? -22.198 -58.449 -22.205 1.00 109.84 ? 36  LEU   A CA  1 
ATOM   70   C  C   . LEU   A 1 16  ? -22.382 -58.089 -23.672 1.00 100.67 ? 36  LEU   A C   1 
ATOM   71   O  O   . LEU   A 1 16  ? -23.458 -57.606 -24.038 1.00 100.28 ? 36  LEU   A O   1 
ATOM   72   C  CB  . LEU   A 1 16  ? -22.233 -57.170 -21.363 1.00 102.59 ? 36  LEU   A CB  1 
ATOM   73   C  CG  . LEU   A 1 16  ? -22.529 -57.326 -19.871 1.00 104.93 ? 36  LEU   A CG  1 
ATOM   74   C  CD1 . LEU   A 1 16  ? -22.787 -55.970 -19.233 1.00 102.69 ? 36  LEU   A CD1 1 
ATOM   75   C  CD2 . LEU   A 1 16  ? -23.710 -58.257 -19.660 1.00 109.77 ? 36  LEU   A CD2 1 
ATOM   76   N  N   . GLY   A 1 17  ? -21.371 -58.303 -24.512 1.00 99.19  ? 37  GLY   A N   1 
ATOM   77   C  CA  . GLY   A 1 17  ? -21.486 -57.958 -25.915 1.00 105.89 ? 37  GLY   A CA  1 
ATOM   78   C  C   . GLY   A 1 17  ? -21.556 -56.477 -26.194 1.00 103.65 ? 37  GLY   A C   1 
ATOM   79   O  O   . GLY   A 1 17  ? -22.097 -56.075 -27.228 1.00 111.51 ? 37  GLY   A O   1 
ATOM   80   N  N   . ILE   A 1 18  ? -21.032 -55.651 -25.295 1.00 95.93  ? 38  ILE   A N   1 
ATOM   81   C  CA  . ILE   A 1 18  ? -21.010 -54.200 -25.468 1.00 95.87  ? 38  ILE   A CA  1 
ATOM   82   C  C   . ILE   A 1 18  ? -19.677 -53.810 -26.098 1.00 90.13  ? 38  ILE   A C   1 
ATOM   83   O  O   . ILE   A 1 18  ? -18.617 -54.234 -25.614 1.00 85.46  ? 38  ILE   A O   1 
ATOM   84   C  CB  . ILE   A 1 18  ? -21.244 -53.485 -24.126 1.00 102.27 ? 38  ILE   A CB  1 
ATOM   85   C  CG1 . ILE   A 1 18  ? -22.698 -53.668 -23.682 1.00 102.20 ? 38  ILE   A CG1 1 
ATOM   86   C  CG2 . ILE   A 1 18  ? -20.887 -52.003 -24.224 1.00 98.00  ? 38  ILE   A CG2 1 
ATOM   87   C  CD1 . ILE   A 1 18  ? -22.905 -53.555 -22.185 1.00 101.88 ? 38  ILE   A CD1 1 
ATOM   88   N  N   . PRO   A 1 19  ? -19.675 -53.025 -27.171 1.00 88.48  ? 39  PRO   A N   1 
ATOM   89   C  CA  . PRO   A 1 19  ? -18.420 -52.703 -27.857 1.00 90.32  ? 39  PRO   A CA  1 
ATOM   90   C  C   . PRO   A 1 19  ? -17.587 -51.709 -27.058 1.00 85.79  ? 39  PRO   A C   1 
ATOM   91   O  O   . PRO   A 1 19  ? -18.055 -51.069 -26.117 1.00 82.55  ? 39  PRO   A O   1 
ATOM   92   C  CB  . PRO   A 1 19  ? -18.889 -52.093 -29.181 1.00 85.22  ? 39  PRO   A CB  1 
ATOM   93   C  CG  . PRO   A 1 19  ? -20.208 -51.478 -28.844 1.00 84.01  ? 39  PRO   A CG  1 
ATOM   94   C  CD  . PRO   A 1 19  ? -20.837 -52.385 -27.814 1.00 83.74  ? 39  PRO   A CD  1 
ATOM   95   N  N   . GLY   A 1 20  ? -16.325 -51.588 -27.459 1.00 91.17  ? 40  GLY   A N   1 
ATOM   96   C  CA  . GLY   A 1 20  ? -15.420 -50.664 -26.820 1.00 92.35  ? 40  GLY   A CA  1 
ATOM   97   C  C   . GLY   A 1 20  ? -13.967 -50.946 -27.140 1.00 86.44  ? 40  GLY   A C   1 
ATOM   98   O  O   . GLY   A 1 20  ? -13.619 -51.988 -27.705 1.00 94.83  ? 40  GLY   A O   1 
ATOM   99   N  N   . PRO   A 1 21  ? -13.087 -50.012 -26.785 1.00 88.33  ? 41  PRO   A N   1 
ATOM   100  C  CA  . PRO   A 1 21  ? -11.655 -50.221 -27.027 1.00 79.48  ? 41  PRO   A CA  1 
ATOM   101  C  C   . PRO   A 1 21  ? -11.114 -51.370 -26.188 1.00 95.25  ? 41  PRO   A C   1 
ATOM   102  O  O   . PRO   A 1 21  ? -11.516 -51.570 -25.040 1.00 86.50  ? 41  PRO   A O   1 
ATOM   103  C  CB  . PRO   A 1 21  ? -11.027 -48.882 -26.624 1.00 85.57  ? 41  PRO   A CB  1 
ATOM   104  C  CG  . PRO   A 1 21  ? -12.010 -48.279 -25.669 1.00 80.83  ? 41  PRO   A CG  1 
ATOM   105  C  CD  . PRO   A 1 21  ? -13.361 -48.706 -26.161 1.00 74.40  ? 41  PRO   A CD  1 
ATOM   106  N  N   . THR   A 1 22  ? -10.197 -52.127 -26.778 1.00 96.63  ? 42  THR   A N   1 
ATOM   107  C  CA  . THR   A 1 22  ? -9.610  -53.264 -26.080 1.00 96.97  ? 42  THR   A CA  1 
ATOM   108  C  C   . THR   A 1 22  ? -8.681  -52.765 -24.979 1.00 86.39  ? 42  THR   A C   1 
ATOM   109  O  O   . THR   A 1 22  ? -7.807  -51.931 -25.243 1.00 85.45  ? 42  THR   A O   1 
ATOM   110  C  CB  . THR   A 1 22  ? -8.843  -54.156 -27.055 1.00 92.04  ? 42  THR   A CB  1 
ATOM   111  O  OG1 . THR   A 1 22  ? -9.626  -54.354 -28.239 1.00 108.51 ? 42  THR   A OG1 1 
ATOM   112  C  CG2 . THR   A 1 22  ? -8.553  -55.511 -26.423 1.00 92.87  ? 42  THR   A CG2 1 
ATOM   113  N  N   . PRO   A 1 23  ? -8.836  -53.235 -23.744 1.00 82.15  ? 43  PRO   A N   1 
ATOM   114  C  CA  . PRO   A 1 23  ? -8.015  -52.728 -22.642 1.00 85.80  ? 43  PRO   A CA  1 
ATOM   115  C  C   . PRO   A 1 23  ? -6.670  -53.428 -22.518 1.00 84.98  ? 43  PRO   A C   1 
ATOM   116  O  O   . PRO   A 1 23  ? -6.505  -54.599 -22.863 1.00 91.37  ? 43  PRO   A O   1 
ATOM   117  C  CB  . PRO   A 1 23  ? -8.889  -53.019 -21.413 1.00 86.11  ? 43  PRO   A CB  1 
ATOM   118  C  CG  . PRO   A 1 23  ? -9.627  -54.256 -21.791 1.00 81.82  ? 43  PRO   A CG  1 
ATOM   119  C  CD  . PRO   A 1 23  ? -9.884  -54.160 -23.276 1.00 82.30  ? 43  PRO   A CD  1 
ATOM   120  N  N   . LEU   A 1 24  ? -5.682  -52.666 -22.001 1.00 85.30  ? 44  LEU   A N   1 
ATOM   121  C  CA  . LEU   A 1 24  ? -4.370  -53.158 -21.612 1.00 83.94  ? 44  LEU   A CA  1 
ATOM   122  C  C   . LEU   A 1 24  ? -4.400  -53.629 -20.163 1.00 92.62  ? 44  LEU   A C   1 
ATOM   123  O  O   . LEU   A 1 24  ? -5.124  -53.062 -19.337 1.00 90.17  ? 44  LEU   A O   1 
ATOM   124  C  CB  . LEU   A 1 24  ? -3.317  -52.064 -21.763 1.00 83.49  ? 44  LEU   A CB  1 
ATOM   125  C  CG  . LEU   A 1 24  ? -2.958  -51.571 -23.164 1.00 82.95  ? 44  LEU   A CG  1 
ATOM   126  C  CD1 . LEU   A 1 24  ? -1.875  -50.517 -23.073 1.00 83.45  ? 44  LEU   A CD1 1 
ATOM   127  C  CD2 . LEU   A 1 24  ? -2.513  -52.719 -24.057 1.00 86.63  ? 44  LEU   A CD2 1 
ATOM   128  N  N   . PRO   A 1 25  ? -3.637  -54.670 -19.830 1.00 93.31  ? 45  PRO   A N   1 
ATOM   129  C  CA  . PRO   A 1 25  ? -3.591  -55.130 -18.438 1.00 85.03  ? 45  PRO   A CA  1 
ATOM   130  C  C   . PRO   A 1 25  ? -3.045  -54.051 -17.513 1.00 78.53  ? 45  PRO   A C   1 
ATOM   131  O  O   . PRO   A 1 25  ? -2.172  -53.265 -17.888 1.00 88.69  ? 45  PRO   A O   1 
ATOM   132  C  CB  . PRO   A 1 25  ? -2.654  -56.343 -18.495 1.00 83.66  ? 45  PRO   A CB  1 
ATOM   133  C  CG  . PRO   A 1 25  ? -2.748  -56.819 -19.902 1.00 86.04  ? 45  PRO   A CG  1 
ATOM   134  C  CD  . PRO   A 1 25  ? -2.909  -55.577 -20.733 1.00 86.69  ? 45  PRO   A CD  1 
ATOM   135  N  N   . PHE   A 1 26  ? -3.605  -54.005 -16.301 1.00 79.20  ? 46  PHE   A N   1 
ATOM   136  C  CA  . PHE   A 1 26  ? -3.181  -53.106 -15.230 1.00 93.45  ? 46  PHE   A CA  1 
ATOM   137  C  C   . PHE   A 1 26  ? -3.335  -51.630 -15.579 1.00 90.33  ? 46  PHE   A C   1 
ATOM   138  O  O   . PHE   A 1 26  ? -3.075  -50.761 -14.740 1.00 103.10 ? 46  PHE   A O   1 
ATOM   139  C  CB  . PHE   A 1 26  ? -1.705  -53.327 -14.893 1.00 85.75  ? 46  PHE   A CB  1 
ATOM   140  C  CG  . PHE   A 1 26  ? -1.406  -54.691 -14.345 1.00 98.60  ? 46  PHE   A CG  1 
ATOM   141  C  CD1 . PHE   A 1 26  ? -1.766  -55.025 -13.052 1.00 107.12 ? 46  PHE   A CD1 1 
ATOM   142  C  CD2 . PHE   A 1 26  ? -0.756  -55.635 -15.121 1.00 99.46  ? 46  PHE   A CD2 1 
ATOM   143  C  CE1 . PHE   A 1 26  ? -1.489  -56.278 -12.543 1.00 103.58 ? 46  PHE   A CE1 1 
ATOM   144  C  CE2 . PHE   A 1 26  ? -0.476  -56.890 -14.619 1.00 107.55 ? 46  PHE   A CE2 1 
ATOM   145  C  CZ  . PHE   A 1 26  ? -0.842  -57.212 -13.328 1.00 99.95  ? 46  PHE   A CZ  1 
ATOM   146  N  N   . LEU   A 1 27  ? -3.750  -51.331 -16.810 1.00 84.15  ? 47  LEU   A N   1 
ATOM   147  C  CA  . LEU   A 1 27  ? -4.046  -49.968 -17.221 1.00 81.83  ? 47  LEU   A CA  1 
ATOM   148  C  C   . LEU   A 1 27  ? -5.443  -49.780 -17.782 1.00 79.15  ? 47  LEU   A C   1 
ATOM   149  O  O   . LEU   A 1 27  ? -5.932  -48.648 -17.783 1.00 75.83  ? 47  LEU   A O   1 
ATOM   150  C  CB  . LEU   A 1 27  ? -3.039  -49.488 -18.277 1.00 73.92  ? 47  LEU   A CB  1 
ATOM   151  C  CG  . LEU   A 1 27  ? -1.557  -49.584 -17.926 1.00 84.24  ? 47  LEU   A CG  1 
ATOM   152  C  CD1 . LEU   A 1 27  ? -0.725  -48.947 -19.024 1.00 87.51  ? 47  LEU   A CD1 1 
ATOM   153  C  CD2 . LEU   A 1 27  ? -1.279  -48.930 -16.584 1.00 83.46  ? 47  LEU   A CD2 1 
ATOM   154  N  N   . GLY   A 1 28  ? -6.102  -50.836 -18.244 1.00 75.68  ? 48  GLY   A N   1 
ATOM   155  C  CA  . GLY   A 1 28  ? -7.365  -50.638 -18.933 1.00 78.97  ? 48  GLY   A CA  1 
ATOM   156  C  C   . GLY   A 1 28  ? -7.151  -49.816 -20.191 1.00 80.17  ? 48  GLY   A C   1 
ATOM   157  O  O   . GLY   A 1 28  ? -6.222  -50.057 -20.970 1.00 80.86  ? 48  GLY   A O   1 
ATOM   158  N  N   . ASN   A 1 29  ? -8.008  -48.815 -20.387 1.00 75.69  ? 49  ASN   A N   1 
ATOM   159  C  CA  . ASN   A 1 29  ? -7.933  -47.935 -21.545 1.00 70.39  ? 49  ASN   A CA  1 
ATOM   160  C  C   . ASN   A 1 29  ? -7.424  -46.542 -21.186 1.00 80.47  ? 49  ASN   A C   1 
ATOM   161  O  O   . ASN   A 1 29  ? -7.673  -45.589 -21.931 1.00 82.03  ? 49  ASN   A O   1 
ATOM   162  C  CB  . ASN   A 1 29  ? -9.304  -47.831 -22.216 1.00 74.66  ? 49  ASN   A CB  1 
ATOM   163  C  CG  . ASN   A 1 29  ? -9.992  -49.174 -22.351 1.00 78.45  ? 49  ASN   A CG  1 
ATOM   164  O  OD1 . ASN   A 1 29  ? -10.739 -49.593 -21.467 1.00 76.14  ? 49  ASN   A OD1 1 
ATOM   165  N  ND2 . ASN   A 1 29  ? -9.746  -49.856 -23.463 1.00 84.98  ? 49  ASN   A ND2 1 
ATOM   166  N  N   . ILE   A 1 30  ? -6.704  -46.403 -20.068 1.00 81.25  ? 50  ILE   A N   1 
ATOM   167  C  CA  . ILE   A 1 30  ? -6.392  -45.068 -19.561 1.00 78.84  ? 50  ILE   A CA  1 
ATOM   168  C  C   . ILE   A 1 30  ? -5.377  -44.355 -20.445 1.00 84.96  ? 50  ILE   A C   1 
ATOM   169  O  O   . ILE   A 1 30  ? -5.366  -43.119 -20.504 1.00 90.55  ? 50  ILE   A O   1 
ATOM   170  C  CB  . ILE   A 1 30  ? -5.897  -45.125 -18.104 1.00 76.52  ? 50  ILE   A CB  1 
ATOM   171  C  CG1 . ILE   A 1 30  ? -4.546  -45.843 -18.021 1.00 80.81  ? 50  ILE   A CG1 1 
ATOM   172  C  CG2 . ILE   A 1 30  ? -6.954  -45.757 -17.202 1.00 79.66  ? 50  ILE   A CG2 1 
ATOM   173  C  CD1 . ILE   A 1 30  ? -3.678  -45.378 -16.872 1.00 90.97  ? 50  ILE   A CD1 1 
ATOM   174  N  N   . LEU   A 1 31  ? -4.510  -45.100 -21.139 1.00 90.32  ? 51  LEU   A N   1 
ATOM   175  C  CA  . LEU   A 1 31  ? -3.529  -44.464 -22.013 1.00 88.52  ? 51  LEU   A CA  1 
ATOM   176  C  C   . LEU   A 1 31  ? -4.190  -43.608 -23.083 1.00 92.67  ? 51  LEU   A C   1 
ATOM   177  O  O   . LEU   A 1 31  ? -3.542  -42.712 -23.636 1.00 90.30  ? 51  LEU   A O   1 
ATOM   178  C  CB  . LEU   A 1 31  ? -2.632  -45.514 -22.672 1.00 79.28  ? 51  LEU   A CB  1 
ATOM   179  C  CG  . LEU   A 1 31  ? -1.638  -46.272 -21.787 1.00 85.10  ? 51  LEU   A CG  1 
ATOM   180  C  CD1 . LEU   A 1 31  ? -0.708  -47.118 -22.644 1.00 82.59  ? 51  LEU   A CD1 1 
ATOM   181  C  CD2 . LEU   A 1 31  ? -0.840  -45.319 -20.907 1.00 82.41  ? 51  LEU   A CD2 1 
ATOM   182  N  N   . SER   A 1 32  ? -5.465  -43.857 -23.378 1.00 86.36  ? 52  SER   A N   1 
ATOM   183  C  CA  . SER   A 1 32  ? -6.224  -43.057 -24.330 1.00 97.81  ? 52  SER   A CA  1 
ATOM   184  C  C   . SER   A 1 32  ? -6.647  -41.706 -23.769 1.00 100.65 ? 52  SER   A C   1 
ATOM   185  O  O   . SER   A 1 32  ? -7.298  -40.936 -24.485 1.00 99.82  ? 52  SER   A O   1 
ATOM   186  C  CB  . SER   A 1 32  ? -7.457  -43.835 -24.796 1.00 88.98  ? 52  SER   A CB  1 
ATOM   187  O  OG  . SER   A 1 32  ? -7.081  -45.033 -25.451 1.00 86.75  ? 52  SER   A OG  1 
ATOM   188  N  N   . TYR   A 1 33  ? -6.309  -41.399 -22.518 1.00 93.97  ? 53  TYR   A N   1 
ATOM   189  C  CA  . TYR   A 1 33  ? -6.553  -40.077 -21.957 1.00 101.19 ? 53  TYR   A CA  1 
ATOM   190  C  C   . TYR   A 1 33  ? -5.451  -39.085 -22.300 1.00 108.00 ? 53  TYR   A C   1 
ATOM   191  O  O   . TYR   A 1 33  ? -5.469  -37.959 -21.790 1.00 105.49 ? 53  TYR   A O   1 
ATOM   192  C  CB  . TYR   A 1 33  ? -6.716  -40.166 -20.437 1.00 96.82  ? 53  TYR   A CB  1 
ATOM   193  C  CG  . TYR   A 1 33  ? -8.031  -40.762 -19.987 1.00 94.70  ? 53  TYR   A CG  1 
ATOM   194  C  CD1 . TYR   A 1 33  ? -9.104  -40.867 -20.863 1.00 100.10 ? 53  TYR   A CD1 1 
ATOM   195  C  CD2 . TYR   A 1 33  ? -8.202  -41.214 -18.686 1.00 99.04  ? 53  TYR   A CD2 1 
ATOM   196  C  CE1 . TYR   A 1 33  ? -10.309 -41.409 -20.454 1.00 97.67  ? 53  TYR   A CE1 1 
ATOM   197  C  CE2 . TYR   A 1 33  ? -9.401  -41.757 -18.268 1.00 91.50  ? 53  TYR   A CE2 1 
ATOM   198  C  CZ  . TYR   A 1 33  ? -10.452 -41.852 -19.157 1.00 88.23  ? 53  TYR   A CZ  1 
ATOM   199  O  OH  . TYR   A 1 33  ? -11.649 -42.392 -18.748 1.00 81.05  ? 53  TYR   A OH  1 
ATOM   200  N  N   . HIS   A 1 34  ? -4.493  -39.480 -23.144 1.00 103.39 ? 54  HIS   A N   1 
ATOM   201  C  CA  . HIS   A 1 34  ? -3.427  -38.568 -23.545 1.00 110.77 ? 54  HIS   A CA  1 
ATOM   202  C  C   . HIS   A 1 34  ? -3.978  -37.350 -24.274 1.00 114.02 ? 54  HIS   A C   1 
ATOM   203  O  O   . HIS   A 1 34  ? -3.384  -36.267 -24.210 1.00 119.11 ? 54  HIS   A O   1 
ATOM   204  C  CB  . HIS   A 1 34  ? -2.415  -39.302 -24.425 1.00 115.90 ? 54  HIS   A CB  1 
ATOM   205  C  CG  . HIS   A 1 34  ? -2.970  -39.740 -25.745 1.00 123.18 ? 54  HIS   A CG  1 
ATOM   206  N  ND1 . HIS   A 1 34  ? -3.819  -40.818 -25.875 1.00 121.26 ? 54  HIS   A ND1 1 
ATOM   207  C  CD2 . HIS   A 1 34  ? -2.798  -39.244 -26.993 1.00 125.12 ? 54  HIS   A CD2 1 
ATOM   208  C  CE1 . HIS   A 1 34  ? -4.146  -40.967 -27.146 1.00 123.83 ? 54  HIS   A CE1 1 
ATOM   209  N  NE2 . HIS   A 1 34  ? -3.540  -40.025 -27.846 1.00 122.69 ? 54  HIS   A NE2 1 
ATOM   210  N  N   . LYS   A 1 35  ? -5.100  -37.506 -24.972 1.00 110.64 ? 55  LYS   A N   1 
ATOM   211  C  CA  . LYS   A 1 35  ? -5.777  -36.398 -25.628 1.00 110.65 ? 55  LYS   A CA  1 
ATOM   212  C  C   . LYS   A 1 35  ? -6.949  -35.870 -24.816 1.00 110.53 ? 55  LYS   A C   1 
ATOM   213  O  O   . LYS   A 1 35  ? -7.755  -35.092 -25.337 1.00 112.15 ? 55  LYS   A O   1 
ATOM   214  C  CB  . LYS   A 1 35  ? -6.235  -36.821 -27.028 1.00 109.56 ? 55  LYS   A CB  1 
ATOM   215  C  CG  . LYS   A 1 35  ? -5.095  -36.881 -28.038 1.00 122.62 ? 55  LYS   A CG  1 
ATOM   216  C  CD  . LYS   A 1 35  ? -5.458  -37.664 -29.291 1.00 128.56 ? 55  LYS   A CD  1 
ATOM   217  C  CE  . LYS   A 1 35  ? -4.261  -37.757 -30.230 1.00 135.02 ? 55  LYS   A CE  1 
ATOM   218  N  NZ  . LYS   A 1 35  ? -4.502  -38.674 -31.379 1.00 139.27 ? 55  LYS   A NZ  1 
ATOM   219  N  N   . GLY   A 1 36  ? -7.061  -36.266 -23.552 1.00 113.13 ? 56  GLY   A N   1 
ATOM   220  C  CA  . GLY   A 1 36  ? -8.085  -35.750 -22.667 1.00 113.47 ? 56  GLY   A CA  1 
ATOM   221  C  C   . GLY   A 1 36  ? -9.341  -36.606 -22.660 1.00 111.92 ? 56  GLY   A C   1 
ATOM   222  O  O   . GLY   A 1 36  ? -9.620  -37.368 -23.585 1.00 108.67 ? 56  GLY   A O   1 
ATOM   223  N  N   . PHE   A 1 37  ? -10.105 -36.471 -21.571 1.00 113.18 ? 57  PHE   A N   1 
ATOM   224  C  CA  . PHE   A 1 37  ? -11.388 -37.161 -21.465 1.00 106.70 ? 57  PHE   A CA  1 
ATOM   225  C  C   . PHE   A 1 37  ? -12.280 -36.862 -22.663 1.00 103.66 ? 57  PHE   A C   1 
ATOM   226  O  O   . PHE   A 1 37  ? -12.957 -37.754 -23.187 1.00 103.31 ? 57  PHE   A O   1 
ATOM   227  C  CB  . PHE   A 1 37  ? -12.122 -36.746 -20.185 1.00 108.48 ? 57  PHE   A CB  1 
ATOM   228  C  CG  . PHE   A 1 37  ? -11.371 -37.025 -18.915 1.00 108.85 ? 57  PHE   A CG  1 
ATOM   229  C  CD1 . PHE   A 1 37  ? -11.381 -38.289 -18.348 1.00 107.87 ? 57  PHE   A CD1 1 
ATOM   230  C  CD2 . PHE   A 1 37  ? -10.692 -36.011 -18.263 1.00 122.69 ? 57  PHE   A CD2 1 
ATOM   231  C  CE1 . PHE   A 1 37  ? -10.703 -38.540 -17.168 1.00 114.64 ? 57  PHE   A CE1 1 
ATOM   232  C  CE2 . PHE   A 1 37  ? -10.016 -36.257 -17.085 1.00 134.76 ? 57  PHE   A CE2 1 
ATOM   233  C  CZ  . PHE   A 1 37  ? -10.022 -37.522 -16.537 1.00 132.22 ? 57  PHE   A CZ  1 
ATOM   234  N  N   . CYS   A 1 38  ? -12.284 -35.605 -23.111 1.00 100.08 ? 58  CYS   A N   1 
ATOM   235  C  CA  . CYS   A 1 38  ? -13.283 -35.153 -24.072 1.00 97.69  ? 58  CYS   A CA  1 
ATOM   236  C  C   . CYS   A 1 38  ? -13.011 -35.704 -25.466 1.00 96.77  ? 58  CYS   A C   1 
ATOM   237  O  O   . CYS   A 1 38  ? -13.912 -36.252 -26.112 1.00 94.88  ? 58  CYS   A O   1 
ATOM   238  C  CB  . CYS   A 1 38  ? -13.320 -33.626 -24.088 1.00 98.64  ? 58  CYS   A CB  1 
ATOM   239  S  SG  . CYS   A 1 38  ? -13.772 -32.899 -22.499 1.00 106.97 ? 58  CYS   A SG  1 
ATOM   240  N  N   . MET   A 1 39  ? -11.778 -35.549 -25.958 1.00 97.28  ? 59  MET   A N   1 
ATOM   241  C  CA  . MET   A 1 39  ? -11.431 -36.091 -27.269 1.00 98.52  ? 59  MET   A CA  1 
ATOM   242  C  C   . MET   A 1 39  ? -11.655 -37.597 -27.313 1.00 98.96  ? 59  MET   A C   1 
ATOM   243  O  O   . MET   A 1 39  ? -12.161 -38.131 -28.307 1.00 100.23 ? 59  MET   A O   1 
ATOM   244  C  CB  . MET   A 1 39  ? -9.978  -35.756 -27.608 1.00 100.60 ? 59  MET   A CB  1 
ATOM   245  C  CG  . MET   A 1 39  ? -9.686  -34.267 -27.721 1.00 113.73 ? 59  MET   A CG  1 
ATOM   246  S  SD  . MET   A 1 39  ? -10.186 -33.570 -29.305 1.00 142.17 ? 59  MET   A SD  1 
ATOM   247  C  CE  . MET   A 1 39  ? -9.100  -34.459 -30.419 1.00 119.59 ? 59  MET   A CE  1 
ATOM   248  N  N   . PHE   A 1 40  ? -11.293 -38.294 -26.235 1.00 94.20  ? 60  PHE   A N   1 
ATOM   249  C  CA  . PHE   A 1 40  ? -11.507 -39.735 -26.162 1.00 86.59  ? 60  PHE   A CA  1 
ATOM   250  C  C   . PHE   A 1 40  ? -12.993 -40.076 -26.147 1.00 95.86  ? 60  PHE   A C   1 
ATOM   251  O  O   . PHE   A 1 40  ? -13.409 -41.083 -26.731 1.00 92.93  ? 60  PHE   A O   1 
ATOM   252  C  CB  . PHE   A 1 40  ? -10.802 -40.293 -24.926 1.00 98.14  ? 60  PHE   A CB  1 
ATOM   253  C  CG  . PHE   A 1 40  ? -11.152 -41.718 -24.611 1.00 93.83  ? 60  PHE   A CG  1 
ATOM   254  C  CD1 . PHE   A 1 40  ? -10.722 -42.749 -25.427 1.00 91.18  ? 60  PHE   A CD1 1 
ATOM   255  C  CD2 . PHE   A 1 40  ? -11.895 -42.027 -23.484 1.00 94.39  ? 60  PHE   A CD2 1 
ATOM   256  C  CE1 . PHE   A 1 40  ? -11.036 -44.062 -25.132 1.00 88.65  ? 60  PHE   A CE1 1 
ATOM   257  C  CE2 . PHE   A 1 40  ? -12.214 -43.337 -23.183 1.00 91.18  ? 60  PHE   A CE2 1 
ATOM   258  C  CZ  . PHE   A 1 40  ? -11.784 -44.356 -24.009 1.00 86.28  ? 60  PHE   A CZ  1 
ATOM   259  N  N   . ASP   A 1 41  ? -13.808 -39.247 -25.488 1.00 92.96  ? 61  ASP   A N   1 
ATOM   260  C  CA  . ASP   A 1 41  ? -15.250 -39.479 -25.473 1.00 90.57  ? 61  ASP   A CA  1 
ATOM   261  C  C   . ASP   A 1 41  ? -15.842 -39.346 -26.871 1.00 92.27  ? 61  ASP   A C   1 
ATOM   262  O  O   . ASP   A 1 41  ? -16.652 -40.178 -27.296 1.00 87.80  ? 61  ASP   A O   1 
ATOM   263  C  CB  . ASP   A 1 41  ? -15.932 -38.507 -24.509 1.00 90.88  ? 61  ASP   A CB  1 
ATOM   264  C  CG  . ASP   A 1 41  ? -15.817 -38.940 -23.062 1.00 84.94  ? 61  ASP   A CG  1 
ATOM   265  O  OD1 . ASP   A 1 41  ? -15.372 -40.080 -22.816 1.00 84.82  ? 61  ASP   A OD1 1 
ATOM   266  O  OD2 . ASP   A 1 41  ? -16.170 -38.138 -22.172 1.00 88.60  ? 61  ASP   A OD2 1 
ATOM   267  N  N   . MET   A 1 42  ? -15.451 -38.299 -27.601 1.00 94.21  ? 62  MET   A N   1 
ATOM   268  C  CA  . MET   A 1 42  ? -16.002 -38.080 -28.935 1.00 95.61  ? 62  MET   A CA  1 
ATOM   269  C  C   . MET   A 1 42  ? -15.558 -39.168 -29.904 1.00 92.93  ? 62  MET   A C   1 
ATOM   270  O  O   . MET   A 1 42  ? -16.360 -39.652 -30.712 1.00 88.22  ? 62  MET   A O   1 
ATOM   271  C  CB  . MET   A 1 42  ? -15.592 -36.703 -29.453 1.00 92.41  ? 62  MET   A CB  1 
ATOM   272  C  CG  . MET   A 1 42  ? -16.017 -35.549 -28.560 1.00 93.86  ? 62  MET   A CG  1 
ATOM   273  S  SD  . MET   A 1 42  ? -15.829 -33.955 -29.377 1.00 112.75 ? 62  MET   A SD  1 
ATOM   274  C  CE  . MET   A 1 42  ? -16.930 -34.166 -30.774 1.00 81.03  ? 62  MET   A CE  1 
ATOM   275  N  N   . GLU   A 1 43  ? -14.284 -39.562 -29.840 1.00 94.74  ? 63  GLU   A N   1 
ATOM   276  C  CA  . GLU   A 1 43  ? -13.794 -40.626 -30.710 1.00 90.10  ? 63  GLU   A CA  1 
ATOM   277  C  C   . GLU   A 1 43  ? -14.541 -41.929 -30.458 1.00 99.69  ? 63  GLU   A C   1 
ATOM   278  O  O   . GLU   A 1 43  ? -14.852 -42.668 -31.399 1.00 96.91  ? 63  GLU   A O   1 
ATOM   279  C  CB  . GLU   A 1 43  ? -12.291 -40.819 -30.507 1.00 101.10 ? 63  GLU   A CB  1 
ATOM   280  C  CG  . GLU   A 1 43  ? -11.441 -39.657 -30.996 1.00 115.43 ? 63  GLU   A CG  1 
ATOM   281  C  CD  . GLU   A 1 43  ? -9.996  -39.764 -30.548 1.00 135.93 ? 63  GLU   A CD  1 
ATOM   282  O  OE1 . GLU   A 1 43  ? -9.682  -40.688 -29.769 1.00 128.78 ? 63  GLU   A OE1 1 
ATOM   283  O  OE2 . GLU   A 1 43  ? -9.175  -38.922 -30.972 1.00 147.62 ? 63  GLU   A OE2 1 
ATOM   284  N  N   . CYS   A 1 44  ? -14.842 -42.226 -29.192 1.00 97.61  ? 64  CYS   A N   1 
ATOM   285  C  CA  . CYS   A 1 44  ? -15.602 -43.432 -28.879 1.00 91.87  ? 64  CYS   A CA  1 
ATOM   286  C  C   . CYS   A 1 44  ? -17.062 -43.287 -29.289 1.00 88.35  ? 64  CYS   A C   1 
ATOM   287  O  O   . CYS   A 1 44  ? -17.683 -44.255 -29.744 1.00 91.41  ? 64  CYS   A O   1 
ATOM   288  C  CB  . CYS   A 1 44  ? -15.488 -43.751 -27.390 1.00 85.43  ? 64  CYS   A CB  1 
ATOM   289  S  SG  . CYS   A 1 44  ? -13.898 -44.445 -26.895 1.00 90.25  ? 64  CYS   A SG  1 
ATOM   290  N  N   . HIS   A 1 45  ? -17.628 -42.088 -29.131 1.00 92.06  ? 65  HIS   A N   1 
ATOM   291  C  CA  . HIS   A 1 45  ? -18.998 -41.845 -29.576 1.00 91.12  ? 65  HIS   A CA  1 
ATOM   292  C  C   . HIS   A 1 45  ? -19.143 -42.130 -31.067 1.00 94.01  ? 65  HIS   A C   1 
ATOM   293  O  O   . HIS   A 1 45  ? -20.091 -42.797 -31.499 1.00 102.06 ? 65  HIS   A O   1 
ATOM   294  C  CB  . HIS   A 1 45  ? -19.396 -40.402 -29.256 1.00 90.03  ? 65  HIS   A CB  1 
ATOM   295  C  CG  . HIS   A 1 45  ? -20.849 -40.113 -29.466 1.00 89.43  ? 65  HIS   A CG  1 
ATOM   296  N  ND1 . HIS   A 1 45  ? -21.798 -41.108 -29.557 1.00 87.07  ? 65  HIS   A ND1 1 
ATOM   297  C  CD2 . HIS   A 1 45  ? -21.517 -38.943 -29.604 1.00 91.32  ? 65  HIS   A CD2 1 
ATOM   298  C  CE1 . HIS   A 1 45  ? -22.988 -40.564 -29.740 1.00 87.79  ? 65  HIS   A CE1 1 
ATOM   299  N  NE2 . HIS   A 1 45  ? -22.845 -39.252 -29.773 1.00 90.30  ? 65  HIS   A NE2 1 
ATOM   300  N  N   . LYS   A 1 46  ? -18.193 -41.637 -31.865 1.00 96.32  ? 66  LYS   A N   1 
ATOM   301  C  CA  . LYS   A 1 46  ? -18.197 -41.853 -33.308 1.00 99.94  ? 66  LYS   A CA  1 
ATOM   302  C  C   . LYS   A 1 46  ? -18.035 -43.330 -33.653 1.00 100.44 ? 66  LYS   A C   1 
ATOM   303  O  O   . LYS   A 1 46  ? -18.887 -43.921 -34.328 1.00 105.24 ? 66  LYS   A O   1 
ATOM   304  C  CB  . LYS   A 1 46  ? -17.079 -41.021 -33.942 1.00 103.85 ? 66  LYS   A CB  1 
ATOM   305  C  CG  . LYS   A 1 46  ? -16.814 -41.288 -35.413 1.00 104.34 ? 66  LYS   A CG  1 
ATOM   306  C  CD  . LYS   A 1 46  ? -15.598 -40.498 -35.873 1.00 122.65 ? 66  LYS   A CD  1 
ATOM   307  C  CE  . LYS   A 1 46  ? -15.282 -40.737 -37.339 1.00 118.95 ? 66  LYS   A CE  1 
ATOM   308  N  NZ  . LYS   A 1 46  ? -16.363 -40.229 -38.227 1.00 123.77 ? 66  LYS   A NZ  1 
ATOM   309  N  N   . LYS   A 1 47  ? -16.947 -43.949 -33.184 1.00 101.45 ? 67  LYS   A N   1 
ATOM   310  C  CA  . LYS   A 1 47  ? -16.583 -45.300 -33.598 1.00 98.99  ? 67  LYS   A CA  1 
ATOM   311  C  C   . LYS   A 1 47  ? -17.523 -46.375 -33.070 1.00 102.02 ? 67  LYS   A C   1 
ATOM   312  O  O   . LYS   A 1 47  ? -17.452 -47.512 -33.549 1.00 96.45  ? 67  LYS   A O   1 
ATOM   313  C  CB  . LYS   A 1 47  ? -15.163 -45.638 -33.135 1.00 107.34 ? 67  LYS   A CB  1 
ATOM   314  C  CG  . LYS   A 1 47  ? -14.059 -44.754 -33.677 1.00 111.93 ? 67  LYS   A CG  1 
ATOM   315  C  CD  . LYS   A 1 47  ? -12.720 -45.188 -33.101 1.00 118.62 ? 67  LYS   A CD  1 
ATOM   316  C  CE  . LYS   A 1 47  ? -11.610 -44.217 -33.456 1.00 133.19 ? 67  LYS   A CE  1 
ATOM   317  N  NZ  . LYS   A 1 47  ? -10.324 -44.606 -32.815 1.00 134.93 ? 67  LYS   A NZ  1 
ATOM   318  N  N   . TYR   A 1 48  ? -18.382 -46.064 -32.098 1.00 104.78 ? 68  TYR   A N   1 
ATOM   319  C  CA  . TYR   A 1 48  ? -19.116 -47.128 -31.419 1.00 99.98  ? 68  TYR   A CA  1 
ATOM   320  C  C   . TYR   A 1 48  ? -20.628 -46.921 -31.388 1.00 102.63 ? 68  TYR   A C   1 
ATOM   321  O  O   . TYR   A 1 48  ? -21.380 -47.900 -31.423 1.00 103.25 ? 68  TYR   A O   1 
ATOM   322  C  CB  . TYR   A 1 48  ? -18.573 -47.300 -29.998 1.00 95.83  ? 68  TYR   A CB  1 
ATOM   323  C  CG  . TYR   A 1 48  ? -17.132 -47.758 -29.973 1.00 98.17  ? 68  TYR   A CG  1 
ATOM   324  C  CD1 . TYR   A 1 48  ? -16.774 -48.998 -30.484 1.00 96.98  ? 68  TYR   A CD1 1 
ATOM   325  C  CD2 . TYR   A 1 48  ? -16.131 -46.953 -29.445 1.00 94.23  ? 68  TYR   A CD2 1 
ATOM   326  C  CE1 . TYR   A 1 48  ? -15.461 -49.423 -30.471 1.00 88.60  ? 68  TYR   A CE1 1 
ATOM   327  C  CE2 . TYR   A 1 48  ? -14.813 -47.370 -29.427 1.00 89.52  ? 68  TYR   A CE2 1 
ATOM   328  C  CZ  . TYR   A 1 48  ? -14.484 -48.606 -29.942 1.00 94.77  ? 68  TYR   A CZ  1 
ATOM   329  O  OH  . TYR   A 1 48  ? -13.175 -49.030 -29.927 1.00 88.41  ? 68  TYR   A OH  1 
ATOM   330  N  N   . GLY   A 1 49  ? -21.095 -45.684 -31.306 1.00 102.27 ? 69  GLY   A N   1 
ATOM   331  C  CA  . GLY   A 1 49  ? -22.518 -45.400 -31.407 1.00 103.11 ? 69  GLY   A CA  1 
ATOM   332  C  C   . GLY   A 1 49  ? -23.141 -45.064 -30.056 1.00 97.92  ? 69  GLY   A C   1 
ATOM   333  O  O   . GLY   A 1 49  ? -22.647 -44.198 -29.337 1.00 96.17  ? 69  GLY   A O   1 
ATOM   334  N  N   . LYS   A 1 50  ? -24.233 -45.758 -29.718 1.00 101.19 ? 70  LYS   A N   1 
ATOM   335  C  CA  . LYS   A 1 50  ? -25.073 -45.323 -28.606 1.00 101.26 ? 70  LYS   A CA  1 
ATOM   336  C  C   . LYS   A 1 50  ? -24.536 -45.756 -27.246 1.00 92.29  ? 70  LYS   A C   1 
ATOM   337  O  O   . LYS   A 1 50  ? -24.731 -45.039 -26.257 1.00 83.66  ? 70  LYS   A O   1 
ATOM   338  C  CB  . LYS   A 1 50  ? -26.501 -45.846 -28.782 1.00 95.37  ? 70  LYS   A CB  1 
ATOM   339  C  CG  . LYS   A 1 50  ? -26.659 -47.340 -28.554 1.00 114.14 ? 70  LYS   A CG  1 
ATOM   340  C  CD  . LYS   A 1 50  ? -28.089 -47.692 -28.182 1.00 123.49 ? 70  LYS   A CD  1 
ATOM   341  C  CE  . LYS   A 1 50  ? -28.160 -49.045 -27.490 1.00 124.65 ? 70  LYS   A CE  1 
ATOM   342  N  NZ  . LYS   A 1 50  ? -27.528 -50.127 -28.294 1.00 110.80 ? 70  LYS   A NZ  1 
ATOM   343  N  N   . VAL   A 1 51  ? -23.877 -46.909 -27.164 1.00 91.17  ? 71  VAL   A N   1 
ATOM   344  C  CA  A VAL   A 1 51  ? -23.393 -47.455 -25.902 0.64 93.03  ? 71  VAL   A CA  1 
ATOM   345  C  CA  B VAL   A 1 51  ? -23.383 -47.439 -25.898 0.36 90.04  ? 71  VAL   A CA  1 
ATOM   346  C  C   . VAL   A 1 51  ? -22.032 -48.096 -26.135 1.00 93.83  ? 71  VAL   A C   1 
ATOM   347  O  O   . VAL   A 1 51  ? -21.814 -48.755 -27.157 1.00 92.09  ? 71  VAL   A O   1 
ATOM   348  C  CB  A VAL   A 1 51  ? -24.399 -48.471 -25.317 0.64 95.49  ? 71  VAL   A CB  1 
ATOM   349  C  CB  B VAL   A 1 51  ? -24.368 -48.442 -25.257 0.36 92.16  ? 71  VAL   A CB  1 
ATOM   350  C  CG1 A VAL   A 1 51  ? -23.699 -49.511 -24.455 0.64 93.72  ? 71  VAL   A CG1 1 
ATOM   351  C  CG1 B VAL   A 1 51  ? -25.586 -47.721 -24.692 0.36 97.03  ? 71  VAL   A CG1 1 
ATOM   352  C  CG2 A VAL   A 1 51  ? -25.469 -47.748 -24.514 0.64 96.61  ? 71  VAL   A CG2 1 
ATOM   353  C  CG2 B VAL   A 1 51  ? -24.782 -49.511 -26.259 0.36 97.75  ? 71  VAL   A CG2 1 
ATOM   354  N  N   . TRP   A 1 52  ? -21.117 -47.900 -25.188 1.00 88.97  ? 72  TRP   A N   1 
ATOM   355  C  CA  . TRP   A 1 52  ? -19.817 -48.549 -25.240 1.00 88.26  ? 72  TRP   A CA  1 
ATOM   356  C  C   . TRP   A 1 52  ? -19.223 -48.557 -23.842 1.00 87.48  ? 72  TRP   A C   1 
ATOM   357  O  O   . TRP   A 1 52  ? -19.583 -47.742 -22.988 1.00 77.75  ? 72  TRP   A O   1 
ATOM   358  C  CB  . TRP   A 1 52  ? -18.870 -47.860 -26.229 1.00 88.23  ? 72  TRP   A CB  1 
ATOM   359  C  CG  . TRP   A 1 52  ? -18.446 -46.489 -25.815 1.00 75.81  ? 72  TRP   A CG  1 
ATOM   360  C  CD1 . TRP   A 1 52  ? -17.318 -46.154 -25.125 1.00 81.38  ? 72  TRP   A CD1 1 
ATOM   361  C  CD2 . TRP   A 1 52  ? -19.141 -45.264 -26.069 1.00 86.45  ? 72  TRP   A CD2 1 
ATOM   362  N  NE1 . TRP   A 1 52  ? -17.270 -44.795 -24.930 1.00 76.86  ? 72  TRP   A NE1 1 
ATOM   363  C  CE2 . TRP   A 1 52  ? -18.376 -44.225 -25.504 1.00 80.89  ? 72  TRP   A CE2 1 
ATOM   364  C  CE3 . TRP   A 1 52  ? -20.337 -44.944 -26.719 1.00 90.61  ? 72  TRP   A CE3 1 
ATOM   365  C  CZ2 . TRP   A 1 52  ? -18.768 -42.890 -25.567 1.00 82.24  ? 72  TRP   A CZ2 1 
ATOM   366  C  CZ3 . TRP   A 1 52  ? -20.724 -43.619 -26.782 1.00 89.00  ? 72  TRP   A CZ3 1 
ATOM   367  C  CH2 . TRP   A 1 52  ? -19.942 -42.608 -26.208 1.00 88.96  ? 72  TRP   A CH2 1 
ATOM   368  N  N   . GLY   A 1 53  ? -18.312 -49.497 -23.620 1.00 87.15  ? 73  GLY   A N   1 
ATOM   369  C  CA  . GLY   A 1 53  ? -17.642 -49.602 -22.343 1.00 76.79  ? 73  GLY   A CA  1 
ATOM   370  C  C   . GLY   A 1 53  ? -16.138 -49.481 -22.457 1.00 76.99  ? 73  GLY   A C   1 
ATOM   371  O  O   . GLY   A 1 53  ? -15.570 -49.671 -23.538 1.00 88.74  ? 73  GLY   A O   1 
ATOM   372  N  N   . PHE   A 1 54  ? -15.487 -49.155 -21.347 1.00 79.81  ? 74  PHE   A N   1 
ATOM   373  C  CA  . PHE   A 1 54  ? -14.033 -49.106 -21.275 1.00 76.51  ? 74  PHE   A CA  1 
ATOM   374  C  C   . PHE   A 1 54  ? -13.639 -49.296 -19.815 1.00 71.62  ? 74  PHE   A C   1 
ATOM   375  O  O   . PHE   A 1 54  ? -14.491 -49.516 -18.949 1.00 70.11  ? 74  PHE   A O   1 
ATOM   376  C  CB  . PHE   A 1 54  ? -13.486 -47.804 -21.871 1.00 74.73  ? 74  PHE   A CB  1 
ATOM   377  C  CG  . PHE   A 1 54  ? -13.985 -46.558 -21.194 1.00 76.94  ? 74  PHE   A CG  1 
ATOM   378  C  CD1 . PHE   A 1 54  ? -15.240 -46.048 -21.486 1.00 74.87  ? 74  PHE   A CD1 1 
ATOM   379  C  CD2 . PHE   A 1 54  ? -13.188 -45.882 -20.286 1.00 72.39  ? 74  PHE   A CD2 1 
ATOM   380  C  CE1 . PHE   A 1 54  ? -15.698 -44.900 -20.872 1.00 71.93  ? 74  PHE   A CE1 1 
ATOM   381  C  CE2 . PHE   A 1 54  ? -13.640 -44.729 -19.670 1.00 72.49  ? 74  PHE   A CE2 1 
ATOM   382  C  CZ  . PHE   A 1 54  ? -14.897 -44.238 -19.964 1.00 65.48  ? 74  PHE   A CZ  1 
ATOM   383  N  N   . TYR   A 1 55  ? -12.339 -49.211 -19.540 1.00 73.89  ? 75  TYR   A N   1 
ATOM   384  C  CA  . TYR   A 1 55  ? -11.815 -49.601 -18.234 1.00 67.14  ? 75  TYR   A CA  1 
ATOM   385  C  C   . TYR   A 1 55  ? -10.827 -48.558 -17.733 1.00 73.36  ? 75  TYR   A C   1 
ATOM   386  O  O   . TYR   A 1 55  ? -9.728  -48.425 -18.281 1.00 81.61  ? 75  TYR   A O   1 
ATOM   387  C  CB  . TYR   A 1 55  ? -11.154 -50.977 -18.303 1.00 77.90  ? 75  TYR   A CB  1 
ATOM   388  C  CG  . TYR   A 1 55  ? -12.109 -52.090 -18.666 1.00 77.11  ? 75  TYR   A CG  1 
ATOM   389  C  CD1 . TYR   A 1 55  ? -12.370 -52.402 -19.994 1.00 75.71  ? 75  TYR   A CD1 1 
ATOM   390  C  CD2 . TYR   A 1 55  ? -12.750 -52.829 -17.680 1.00 75.44  ? 75  TYR   A CD2 1 
ATOM   391  C  CE1 . TYR   A 1 55  ? -13.243 -53.418 -20.329 1.00 79.22  ? 75  TYR   A CE1 1 
ATOM   392  C  CE2 . TYR   A 1 55  ? -13.624 -53.847 -18.006 1.00 79.22  ? 75  TYR   A CE2 1 
ATOM   393  C  CZ  . TYR   A 1 55  ? -13.866 -54.138 -19.332 1.00 85.89  ? 75  TYR   A CZ  1 
ATOM   394  O  OH  . TYR   A 1 55  ? -14.735 -55.151 -19.664 1.00 97.51  ? 75  TYR   A OH  1 
ATOM   395  N  N   . ASP   A 1 56  ? -11.220 -47.822 -16.697 1.00 71.75  ? 76  ASP   A N   1 
ATOM   396  C  CA  . ASP   A 1 56  ? -10.277 -47.043 -15.898 1.00 75.35  ? 76  ASP   A CA  1 
ATOM   397  C  C   . ASP   A 1 56  ? -9.532  -48.013 -14.991 1.00 78.15  ? 76  ASP   A C   1 
ATOM   398  O  O   . ASP   A 1 56  ? -10.017 -48.376 -13.917 1.00 73.74  ? 76  ASP   A O   1 
ATOM   399  C  CB  . ASP   A 1 56  ? -11.011 -45.981 -15.088 1.00 73.92  ? 76  ASP   A CB  1 
ATOM   400  C  CG  . ASP   A 1 56  ? -11.591 -44.881 -15.948 1.00 77.04  ? 76  ASP   A CG  1 
ATOM   401  O  OD1 . ASP   A 1 56  ? -11.139 -44.719 -17.101 1.00 74.49  ? 76  ASP   A OD1 1 
ATOM   402  O  OD2 . ASP   A 1 56  ? -12.495 -44.171 -15.462 1.00 89.76  ? 76  ASP   A OD2 1 
ATOM   403  N  N   . GLY   A 1 57  ? -8.349  -48.443 -15.418 1.00 78.57  ? 77  GLY   A N   1 
ATOM   404  C  CA  . GLY   A 1 57  ? -7.678  -49.541 -14.752 1.00 65.00  ? 77  GLY   A CA  1 
ATOM   405  C  C   . GLY   A 1 57  ? -8.499  -50.809 -14.837 1.00 75.78  ? 77  GLY   A C   1 
ATOM   406  O  O   . GLY   A 1 57  ? -8.821  -51.278 -15.932 1.00 73.58  ? 77  GLY   A O   1 
ATOM   407  N  N   . GLN   A 1 58  ? -8.863  -51.366 -13.684 1.00 74.57  ? 78  GLN   A N   1 
ATOM   408  C  CA  . GLN   A 1 58  ? -9.767  -52.506 -13.638 1.00 75.35  ? 78  GLN   A CA  1 
ATOM   409  C  C   . GLN   A 1 58  ? -11.230 -52.095 -13.549 1.00 82.34  ? 78  GLN   A C   1 
ATOM   410  O  O   . GLN   A 1 58  ? -12.104 -52.967 -13.586 1.00 84.65  ? 78  GLN   A O   1 
ATOM   411  C  CB  . GLN   A 1 58  ? -9.426  -53.410 -12.449 1.00 92.37  ? 78  GLN   A CB  1 
ATOM   412  C  CG  . GLN   A 1 58  ? -8.037  -54.020 -12.493 1.00 102.36 ? 78  GLN   A CG  1 
ATOM   413  C  CD  . GLN   A 1 58  ? -7.947  -55.216 -13.420 1.00 113.45 ? 78  GLN   A CD  1 
ATOM   414  O  OE1 . GLN   A 1 58  ? -8.932  -55.920 -13.643 1.00 118.21 ? 78  GLN   A OE1 1 
ATOM   415  N  NE2 . GLN   A 1 58  ? -6.759  -55.453 -13.964 1.00 114.50 ? 78  GLN   A NE2 1 
ATOM   416  N  N   . GLN   A 1 59  ? -11.516 -50.799 -13.440 1.00 66.64  ? 79  GLN   A N   1 
ATOM   417  C  CA  . GLN   A 1 59  ? -12.865 -50.295 -13.221 1.00 72.00  ? 79  GLN   A CA  1 
ATOM   418  C  C   . GLN   A 1 59  ? -13.639 -50.196 -14.530 1.00 62.04  ? 79  GLN   A C   1 
ATOM   419  O  O   . GLN   A 1 59  ? -13.306 -49.369 -15.388 1.00 64.89  ? 79  GLN   A O   1 
ATOM   420  C  CB  . GLN   A 1 59  ? -12.811 -48.929 -12.534 1.00 59.92  ? 79  GLN   A CB  1 
ATOM   421  C  CG  . GLN   A 1 59  ? -14.147 -48.210 -12.466 1.00 64.55  ? 79  GLN   A CG  1 
ATOM   422  C  CD  . GLN   A 1 59  ? -15.181 -48.979 -11.669 1.00 68.12  ? 79  GLN   A CD  1 
ATOM   423  O  OE1 . GLN   A 1 59  ? -15.036 -49.167 -10.462 1.00 74.67  ? 79  GLN   A OE1 1 
ATOM   424  N  NE2 . GLN   A 1 59  ? -16.231 -49.434 -12.344 1.00 73.56  ? 79  GLN   A NE2 1 
ATOM   425  N  N   . PRO   A 1 60  ? -14.678 -51.010 -14.718 1.00 63.07  ? 80  PRO   A N   1 
ATOM   426  C  CA  . PRO   A 1 60  ? -15.489 -50.897 -15.938 1.00 75.80  ? 80  PRO   A CA  1 
ATOM   427  C  C   . PRO   A 1 60  ? -16.356 -49.646 -15.904 1.00 71.88  ? 80  PRO   A C   1 
ATOM   428  O  O   . PRO   A 1 60  ? -17.051 -49.379 -14.921 1.00 67.20  ? 80  PRO   A O   1 
ATOM   429  C  CB  . PRO   A 1 60  ? -16.339 -52.173 -15.917 1.00 68.71  ? 80  PRO   A CB  1 
ATOM   430  C  CG  . PRO   A 1 60  ? -16.435 -52.528 -14.468 1.00 65.28  ? 80  PRO   A CG  1 
ATOM   431  C  CD  . PRO   A 1 60  ? -15.122 -52.119 -13.855 1.00 67.72  ? 80  PRO   A CD  1 
ATOM   432  N  N   . VAL   A 1 61  ? -16.303 -48.873 -16.987 1.00 75.32  ? 81  VAL   A N   1 
ATOM   433  C  CA  . VAL   A 1 61  ? -17.124 -47.681 -17.158 1.00 72.34  ? 81  VAL   A CA  1 
ATOM   434  C  C   . VAL   A 1 61  ? -17.970 -47.869 -18.408 1.00 76.62  ? 81  VAL   A C   1 
ATOM   435  O  O   . VAL   A 1 61  ? -17.446 -48.235 -19.467 1.00 79.95  ? 81  VAL   A O   1 
ATOM   436  C  CB  . VAL   A 1 61  ? -16.267 -46.405 -17.261 1.00 65.18  ? 81  VAL   A CB  1 
ATOM   437  C  CG1 . VAL   A 1 61  ? -17.153 -45.169 -17.300 1.00 71.87  ? 81  VAL   A CG1 1 
ATOM   438  C  CG2 . VAL   A 1 61  ? -15.289 -46.325 -16.101 1.00 69.59  ? 81  VAL   A CG2 1 
ATOM   439  N  N   . LEU   A 1 62  ? -19.274 -47.624 -18.286 1.00 71.62  ? 82  LEU   A N   1 
ATOM   440  C  CA  . LEU   A 1 62  ? -20.222 -47.814 -19.379 1.00 71.48  ? 82  LEU   A CA  1 
ATOM   441  C  C   . LEU   A 1 62  ? -20.781 -46.460 -19.793 1.00 74.79  ? 82  LEU   A C   1 
ATOM   442  O  O   . LEU   A 1 62  ? -21.538 -45.838 -19.040 1.00 80.60  ? 82  LEU   A O   1 
ATOM   443  C  CB  . LEU   A 1 62  ? -21.349 -48.761 -18.974 1.00 76.89  ? 82  LEU   A CB  1 
ATOM   444  C  CG  . LEU   A 1 62  ? -22.447 -48.925 -20.026 1.00 80.88  ? 82  LEU   A CG  1 
ATOM   445  C  CD1 . LEU   A 1 62  ? -21.884 -49.539 -21.300 1.00 86.54  ? 82  LEU   A CD1 1 
ATOM   446  C  CD2 . LEU   A 1 62  ? -23.594 -49.758 -19.480 1.00 81.31  ? 82  LEU   A CD2 1 
ATOM   447  N  N   . ALA   A 1 63  ? -20.418 -46.011 -20.990 1.00 76.83  ? 83  ALA   A N   1 
ATOM   448  C  CA  . ALA   A 1 63  ? -20.955 -44.768 -21.522 1.00 73.20  ? 83  ALA   A CA  1 
ATOM   449  C  C   . ALA   A 1 63  ? -22.314 -45.018 -22.161 1.00 74.58  ? 83  ALA   A C   1 
ATOM   450  O  O   . ALA   A 1 63  ? -22.485 -45.972 -22.927 1.00 80.98  ? 83  ALA   A O   1 
ATOM   451  C  CB  . ALA   A 1 63  ? -19.994 -44.164 -22.542 1.00 74.97  ? 83  ALA   A CB  1 
ATOM   452  N  N   . ILE   A 1 64  ? -23.281 -44.165 -21.839 1.00 72.06  ? 84  ILE   A N   1 
ATOM   453  C  CA  . ILE   A 1 64  ? -24.606 -44.214 -22.441 1.00 68.87  ? 84  ILE   A CA  1 
ATOM   454  C  C   . ILE   A 1 64  ? -24.906 -42.849 -23.041 1.00 77.00  ? 84  ILE   A C   1 
ATOM   455  O  O   . ILE   A 1 64  ? -24.490 -41.816 -22.504 1.00 79.10  ? 84  ILE   A O   1 
ATOM   456  C  CB  . ILE   A 1 64  ? -25.691 -44.624 -21.422 1.00 77.47  ? 84  ILE   A CB  1 
ATOM   457  C  CG1 . ILE   A 1 64  ? -25.853 -43.557 -20.337 1.00 75.11  ? 84  ILE   A CG1 1 
ATOM   458  C  CG2 . ILE   A 1 64  ? -25.347 -45.970 -20.798 1.00 77.73  ? 84  ILE   A CG2 1 
ATOM   459  C  CD1 . ILE   A 1 64  ? -27.032 -43.789 -19.415 1.00 86.90  ? 84  ILE   A CD1 1 
ATOM   460  N  N   . THR   A 1 65  ? -25.609 -42.846 -24.175 1.00 77.86  ? 85  THR   A N   1 
ATOM   461  C  CA  . THR   A 1 65  ? -25.926 -41.611 -24.875 1.00 83.95  ? 85  THR   A CA  1 
ATOM   462  C  C   . THR   A 1 65  ? -27.395 -41.484 -25.254 1.00 81.75  ? 85  THR   A C   1 
ATOM   463  O  O   . THR   A 1 65  ? -27.774 -40.469 -25.847 1.00 86.70  ? 85  THR   A O   1 
ATOM   464  C  CB  . THR   A 1 65  ? -25.068 -41.474 -26.145 1.00 82.42  ? 85  THR   A CB  1 
ATOM   465  O  OG1 . THR   A 1 65  ? -25.309 -42.587 -27.012 1.00 85.63  ? 85  THR   A OG1 1 
ATOM   466  C  CG2 . THR   A 1 65  ? -23.584 -41.421 -25.795 1.00 76.21  ? 85  THR   A CG2 1 
ATOM   467  N  N   . ASP   A 1 66  ? -28.228 -42.467 -24.932 1.00 82.72  ? 86  ASP   A N   1 
ATOM   468  C  CA  . ASP   A 1 66  ? -29.640 -42.397 -25.284 1.00 87.24  ? 86  ASP   A CA  1 
ATOM   469  C  C   . ASP   A 1 66  ? -30.384 -41.587 -24.229 1.00 89.72  ? 86  ASP   A C   1 
ATOM   470  O  O   . ASP   A 1 66  ? -30.329 -41.938 -23.045 1.00 84.52  ? 86  ASP   A O   1 
ATOM   471  C  CB  . ASP   A 1 66  ? -30.231 -43.796 -25.405 1.00 98.97  ? 86  ASP   A CB  1 
ATOM   472  C  CG  . ASP   A 1 66  ? -31.662 -43.786 -25.899 1.00 98.48  ? 86  ASP   A CG  1 
ATOM   473  O  OD1 . ASP   A 1 66  ? -32.563 -43.477 -25.094 1.00 100.88 ? 86  ASP   A OD1 1 
ATOM   474  O  OD2 . ASP   A 1 66  ? -31.887 -44.076 -27.092 1.00 105.88 ? 86  ASP   A OD2 1 
ATOM   475  N  N   . PRO   A 1 67  ? -31.068 -40.499 -24.606 1.00 92.78  ? 87  PRO   A N   1 
ATOM   476  C  CA  . PRO   A 1 67  ? -31.711 -39.644 -23.589 1.00 91.27  ? 87  PRO   A CA  1 
ATOM   477  C  C   . PRO   A 1 67  ? -32.700 -40.375 -22.693 1.00 90.89  ? 87  PRO   A C   1 
ATOM   478  O  O   . PRO   A 1 67  ? -32.797 -40.045 -21.504 1.00 90.51  ? 87  PRO   A O   1 
ATOM   479  C  CB  . PRO   A 1 67  ? -32.398 -38.554 -24.431 1.00 76.99  ? 87  PRO   A CB  1 
ATOM   480  C  CG  . PRO   A 1 67  ? -32.386 -39.061 -25.846 1.00 89.67  ? 87  PRO   A CG  1 
ATOM   481  C  CD  . PRO   A 1 67  ? -31.177 -39.928 -25.957 1.00 86.46  ? 87  PRO   A CD  1 
ATOM   482  N  N   . ASP   A 1 68  ? -33.440 -41.354 -23.221 1.00 90.43  ? 88  ASP   A N   1 
ATOM   483  C  CA  . ASP   A 1 68  ? -34.316 -42.151 -22.366 1.00 92.81  ? 88  ASP   A CA  1 
ATOM   484  C  C   . ASP   A 1 68  ? -33.511 -42.896 -21.310 1.00 81.33  ? 88  ASP   A C   1 
ATOM   485  O  O   . ASP   A 1 68  ? -33.878 -42.917 -20.129 1.00 89.10  ? 88  ASP   A O   1 
ATOM   486  C  CB  . ASP   A 1 68  ? -35.133 -43.132 -23.208 1.00 105.35 ? 88  ASP   A CB  1 
ATOM   487  C  CG  . ASP   A 1 68  ? -36.292 -42.466 -23.919 1.00 109.62 ? 88  ASP   A CG  1 
ATOM   488  O  OD1 . ASP   A 1 68  ? -36.851 -41.496 -23.365 1.00 117.19 ? 88  ASP   A OD1 1 
ATOM   489  O  OD2 . ASP   A 1 68  ? -36.645 -42.914 -25.030 1.00 93.84  ? 88  ASP   A OD2 1 
ATOM   490  N  N   . MET   A 1 69  ? -32.402 -43.514 -21.723 1.00 93.10  ? 89  MET   A N   1 
ATOM   491  C  CA  . MET   A 1 69  ? -31.524 -44.185 -20.772 1.00 96.58  ? 89  MET   A CA  1 
ATOM   492  C  C   . MET   A 1 69  ? -30.911 -43.187 -19.798 1.00 82.97  ? 89  MET   A C   1 
ATOM   493  O  O   . MET   A 1 69  ? -30.759 -43.482 -18.606 1.00 87.41  ? 89  MET   A O   1 
ATOM   494  C  CB  . MET   A 1 69  ? -30.434 -44.945 -21.530 1.00 97.57  ? 89  MET   A CB  1 
ATOM   495  C  CG  . MET   A 1 69  ? -30.116 -46.317 -20.974 1.00 98.98  ? 89  MET   A CG  1 
ATOM   496  S  SD  . MET   A 1 69  ? -29.099 -47.293 -22.098 1.00 106.67 ? 89  MET   A SD  1 
ATOM   497  C  CE  . MET   A 1 69  ? -30.230 -47.512 -23.471 1.00 106.76 ? 89  MET   A CE  1 
ATOM   498  N  N   . ILE   A 1 70  ? -30.561 -41.996 -20.288 1.00 86.16  ? 90  ILE   A N   1 
ATOM   499  C  CA  . ILE   A 1 70  ? -29.999 -40.964 -19.421 1.00 82.70  ? 90  ILE   A CA  1 
ATOM   500  C  C   . ILE   A 1 70  ? -31.032 -40.504 -18.401 1.00 84.76  ? 90  ILE   A C   1 
ATOM   501  O  O   . ILE   A 1 70  ? -30.711 -40.286 -17.226 1.00 82.92  ? 90  ILE   A O   1 
ATOM   502  C  CB  . ILE   A 1 70  ? -29.468 -39.792 -20.268 1.00 78.59  ? 90  ILE   A CB  1 
ATOM   503  C  CG1 . ILE   A 1 70  ? -28.249 -40.237 -21.079 1.00 77.85  ? 90  ILE   A CG1 1 
ATOM   504  C  CG2 . ILE   A 1 70  ? -29.127 -38.597 -19.389 1.00 75.82  ? 90  ILE   A CG2 1 
ATOM   505  C  CD1 . ILE   A 1 70  ? -27.671 -39.155 -21.964 1.00 79.97  ? 90  ILE   A CD1 1 
ATOM   506  N  N   . LYS   A 1 71  ? -32.289 -40.355 -18.827 1.00 89.97  ? 91  LYS   A N   1 
ATOM   507  C  CA  . LYS   A 1 71  ? -33.347 -40.021 -17.880 1.00 86.96  ? 91  LYS   A CA  1 
ATOM   508  C  C   . LYS   A 1 71  ? -33.551 -41.145 -16.872 1.00 86.03  ? 91  LYS   A C   1 
ATOM   509  O  O   . LYS   A 1 71  ? -33.793 -40.889 -15.686 1.00 79.12  ? 91  LYS   A O   1 
ATOM   510  C  CB  . LYS   A 1 71  ? -34.650 -39.723 -18.622 1.00 84.23  ? 91  LYS   A CB  1 
ATOM   511  C  CG  . LYS   A 1 71  ? -35.821 -39.409 -17.701 1.00 92.64  ? 91  LYS   A CG  1 
ATOM   512  C  CD  . LYS   A 1 71  ? -37.068 -39.021 -18.477 1.00 98.27  ? 91  LYS   A CD  1 
ATOM   513  C  CE  . LYS   A 1 71  ? -38.166 -38.543 -17.542 1.00 101.03 ? 91  LYS   A CE  1 
ATOM   514  N  NZ  . LYS   A 1 71  ? -39.361 -38.067 -18.290 1.00 114.81 ? 91  LYS   A NZ  1 
ATOM   515  N  N   . THR   A 1 72  ? -33.449 -42.396 -17.324 1.00 85.37  ? 92  THR   A N   1 
ATOM   516  C  CA  . THR   A 1 72  ? -33.569 -43.531 -16.414 1.00 91.27  ? 92  THR   A CA  1 
ATOM   517  C  C   . THR   A 1 72  ? -32.489 -43.482 -15.339 1.00 95.41  ? 92  THR   A C   1 
ATOM   518  O  O   . THR   A 1 72  ? -32.776 -43.625 -14.144 1.00 93.16  ? 92  THR   A O   1 
ATOM   519  C  CB  . THR   A 1 72  ? -33.486 -44.842 -17.197 1.00 93.03  ? 92  THR   A CB  1 
ATOM   520  O  OG1 . THR   A 1 72  ? -34.248 -44.730 -18.406 1.00 94.00  ? 92  THR   A OG1 1 
ATOM   521  C  CG2 . THR   A 1 72  ? -34.035 -45.991 -16.367 1.00 88.28  ? 92  THR   A CG2 1 
ATOM   522  N  N   . VAL   A 1 73  ? -31.238 -43.265 -15.748 1.00 86.20  ? 93  VAL   A N   1 
ATOM   523  C  CA  . VAL   A 1 73  ? -30.130 -43.251 -14.798 1.00 83.75  ? 93  VAL   A CA  1 
ATOM   524  C  C   . VAL   A 1 73  ? -30.204 -42.020 -13.903 1.00 88.73  ? 93  VAL   A C   1 
ATOM   525  O  O   . VAL   A 1 73  ? -30.204 -42.128 -12.671 1.00 78.71  ? 93  VAL   A O   1 
ATOM   526  C  CB  . VAL   A 1 73  ? -28.786 -43.323 -15.543 1.00 84.03  ? 93  VAL   A CB  1 
ATOM   527  C  CG1 . VAL   A 1 73  ? -27.645 -42.904 -14.627 1.00 75.71  ? 93  VAL   A CG1 1 
ATOM   528  C  CG2 . VAL   A 1 73  ? -28.551 -44.723 -16.073 1.00 77.00  ? 93  VAL   A CG2 1 
ATOM   529  N  N   . LEU   A 1 74  ? -30.274 -40.832 -14.507 1.00 89.09  ? 94  LEU   A N   1 
ATOM   530  C  CA  . LEU   A 1 74  ? -30.129 -39.607 -13.728 1.00 74.50  ? 94  LEU   A CA  1 
ATOM   531  C  C   . LEU   A 1 74  ? -31.370 -39.290 -12.904 1.00 78.30  ? 94  LEU   A C   1 
ATOM   532  O  O   . LEU   A 1 74  ? -31.259 -38.656 -11.849 1.00 83.61  ? 94  LEU   A O   1 
ATOM   533  C  CB  . LEU   A 1 74  ? -29.796 -38.430 -14.646 1.00 73.88  ? 94  LEU   A CB  1 
ATOM   534  C  CG  . LEU   A 1 74  ? -28.363 -38.369 -15.177 1.00 76.93  ? 94  LEU   A CG  1 
ATOM   535  C  CD1 . LEU   A 1 74  ? -28.091 -37.027 -15.838 1.00 77.89  ? 94  LEU   A CD1 1 
ATOM   536  C  CD2 . LEU   A 1 74  ? -27.370 -38.629 -14.055 1.00 69.67  ? 94  LEU   A CD2 1 
ATOM   537  N  N   . VAL   A 1 75  ? -32.551 -39.713 -13.351 1.00 85.11  ? 95  VAL   A N   1 
ATOM   538  C  CA  . VAL   A 1 75  ? -33.785 -39.300 -12.692 1.00 93.24  ? 95  VAL   A CA  1 
ATOM   539  C  C   . VAL   A 1 75  ? -34.526 -40.496 -12.107 1.00 101.15 ? 95  VAL   A C   1 
ATOM   540  O  O   . VAL   A 1 75  ? -34.694 -40.598 -10.887 1.00 105.85 ? 95  VAL   A O   1 
ATOM   541  C  CB  . VAL   A 1 75  ? -34.698 -38.527 -13.662 1.00 93.58  ? 95  VAL   A CB  1 
ATOM   542  C  CG1 . VAL   A 1 75  ? -35.924 -38.004 -12.928 1.00 98.46  ? 95  VAL   A CG1 1 
ATOM   543  C  CG2 . VAL   A 1 75  ? -33.935 -37.391 -14.328 1.00 87.82  ? 95  VAL   A CG2 1 
ATOM   544  N  N   . LYS   A 1 76  ? -34.968 -41.407 -12.977 1.00 104.74 ? 96  LYS   A N   1 
ATOM   545  C  CA  . LYS   A 1 76  ? -35.949 -42.413 -12.576 1.00 108.05 ? 96  LYS   A CA  1 
ATOM   546  C  C   . LYS   A 1 76  ? -35.398 -43.345 -11.502 1.00 106.90 ? 96  LYS   A C   1 
ATOM   547  O  O   . LYS   A 1 76  ? -36.044 -43.571 -10.472 1.00 102.47 ? 96  LYS   A O   1 
ATOM   548  C  CB  . LYS   A 1 76  ? -36.406 -43.206 -13.800 1.00 110.09 ? 96  LYS   A CB  1 
ATOM   549  C  CG  . LYS   A 1 76  ? -36.876 -42.331 -14.950 1.00 114.18 ? 96  LYS   A CG  1 
ATOM   550  C  CD  . LYS   A 1 76  ? -37.698 -43.117 -15.954 1.00 126.27 ? 96  LYS   A CD  1 
ATOM   551  C  CE  . LYS   A 1 76  ? -38.327 -42.189 -16.979 1.00 129.43 ? 96  LYS   A CE  1 
ATOM   552  N  NZ  . LYS   A 1 76  ? -39.325 -42.888 -17.833 1.00 134.12 ? 96  LYS   A NZ  1 
ATOM   553  N  N   . GLU   A 1 77  ? -34.206 -43.897 -11.723 1.00 100.99 ? 97  GLU   A N   1 
ATOM   554  C  CA  . GLU   A 1 77  ? -33.628 -44.888 -10.824 1.00 91.70  ? 97  GLU   A CA  1 
ATOM   555  C  C   . GLU   A 1 77  ? -32.522 -44.312 -9.944  1.00 88.65  ? 97  GLU   A C   1 
ATOM   556  O  O   . GLU   A 1 77  ? -31.661 -45.063 -9.473  1.00 89.89  ? 97  GLU   A O   1 
ATOM   557  C  CB  . GLU   A 1 77  ? -33.098 -46.076 -11.628 1.00 93.05  ? 97  GLU   A CB  1 
ATOM   558  C  CG  . GLU   A 1 77  ? -34.089 -46.621 -12.644 1.00 95.25  ? 97  GLU   A CG  1 
ATOM   559  C  CD  . GLU   A 1 77  ? -35.356 -47.146 -12.000 1.00 109.41 ? 97  GLU   A CD  1 
ATOM   560  O  OE1 . GLU   A 1 77  ? -35.250 -47.924 -11.028 1.00 110.43 ? 97  GLU   A OE1 1 
ATOM   561  O  OE2 . GLU   A 1 77  ? -36.457 -46.775 -12.459 1.00 105.03 ? 97  GLU   A OE2 1 
ATOM   562  N  N   . CYS   A 1 78  ? -32.536 -42.998 -9.705  1.00 88.56  ? 98  CYS   A N   1 
ATOM   563  C  CA  . CYS   A 1 78  ? -31.480 -42.364 -8.921  1.00 89.20  ? 98  CYS   A CA  1 
ATOM   564  C  C   . CYS   A 1 78  ? -31.455 -42.892 -7.491  1.00 84.05  ? 98  CYS   A C   1 
ATOM   565  O  O   . CYS   A 1 78  ? -30.431 -43.399 -7.019  1.00 79.05  ? 98  CYS   A O   1 
ATOM   566  C  CB  . CYS   A 1 78  ? -31.667 -40.846 -8.926  1.00 77.78  ? 98  CYS   A CB  1 
ATOM   567  S  SG  . CYS   A 1 78  ? -30.630 -39.963 -7.734  1.00 74.06  ? 98  CYS   A SG  1 
ATOM   568  N  N   . TYR   A 1 79  ? -32.580 -42.772 -6.782  1.00 92.00  ? 99  TYR   A N   1 
ATOM   569  C  CA  . TYR   A 1 79  ? -32.617 -43.181 -5.381  1.00 97.75  ? 99  TYR   A CA  1 
ATOM   570  C  C   . TYR   A 1 79  ? -32.377 -44.677 -5.227  1.00 90.23  ? 99  TYR   A C   1 
ATOM   571  O  O   . TYR   A 1 79  ? -31.748 -45.115 -4.257  1.00 81.81  ? 99  TYR   A O   1 
ATOM   572  C  CB  . TYR   A 1 79  ? -33.959 -42.800 -4.754  1.00 89.65  ? 99  TYR   A CB  1 
ATOM   573  C  CG  . TYR   A 1 79  ? -34.153 -41.318 -4.557  1.00 106.70 ? 99  TYR   A CG  1 
ATOM   574  C  CD1 . TYR   A 1 79  ? -33.453 -40.632 -3.574  1.00 99.14  ? 99  TYR   A CD1 1 
ATOM   575  C  CD2 . TYR   A 1 79  ? -35.049 -40.604 -5.342  1.00 102.70 ? 99  TYR   A CD2 1 
ATOM   576  C  CE1 . TYR   A 1 79  ? -33.631 -39.277 -3.385  1.00 101.92 ? 99  TYR   A CE1 1 
ATOM   577  C  CE2 . TYR   A 1 79  ? -35.235 -39.247 -5.158  1.00 110.95 ? 99  TYR   A CE2 1 
ATOM   578  C  CZ  . TYR   A 1 79  ? -34.524 -38.590 -4.178  1.00 108.92 ? 99  TYR   A CZ  1 
ATOM   579  O  OH  . TYR   A 1 79  ? -34.704 -37.240 -3.990  1.00 102.94 ? 99  TYR   A OH  1 
ATOM   580  N  N   . SER   A 1 80  ? -32.866 -45.477 -6.174  1.00 89.51  ? 100 SER   A N   1 
ATOM   581  C  CA  . SER   A 1 80  ? -32.833 -46.926 -6.008  1.00 89.88  ? 100 SER   A CA  1 
ATOM   582  C  C   . SER   A 1 80  ? -31.466 -47.513 -6.350  1.00 96.36  ? 100 SER   A C   1 
ATOM   583  O  O   . SER   A 1 80  ? -30.932 -48.334 -5.595  1.00 103.93 ? 100 SER   A O   1 
ATOM   584  C  CB  . SER   A 1 80  ? -33.928 -47.572 -6.861  1.00 89.53  ? 100 SER   A CB  1 
ATOM   585  O  OG  . SER   A 1 80  ? -33.980 -46.990 -8.151  1.00 94.88  ? 100 SER   A OG  1 
ATOM   586  N  N   . VAL   A 1 81  ? -30.879 -47.104 -7.476  1.00 88.13  ? 101 VAL   A N   1 
ATOM   587  C  CA  . VAL   A 1 81  ? -29.703 -47.762 -8.035  1.00 89.83  ? 101 VAL   A CA  1 
ATOM   588  C  C   . VAL   A 1 81  ? -28.531 -46.797 -8.179  1.00 84.72  ? 101 VAL   A C   1 
ATOM   589  O  O   . VAL   A 1 81  ? -27.433 -47.058 -7.678  1.00 85.99  ? 101 VAL   A O   1 
ATOM   590  C  CB  . VAL   A 1 81  ? -30.025 -48.426 -9.391  1.00 88.42  ? 101 VAL   A CB  1 
ATOM   591  C  CG1 . VAL   A 1 81  ? -28.928 -49.412 -9.765  1.00 92.00  ? 101 VAL   A CG1 1 
ATOM   592  C  CG2 . VAL   A 1 81  ? -31.389 -49.094 -9.345  1.00 82.36  ? 101 VAL   A CG2 1 
ATOM   593  N  N   . PHE   A 1 82  ? -28.742 -45.684 -8.874  1.00 85.10  ? 102 PHE   A N   1 
ATOM   594  C  CA  . PHE   A 1 82  ? -27.663 -44.776 -9.250  1.00 71.24  ? 102 PHE   A CA  1 
ATOM   595  C  C   . PHE   A 1 82  ? -27.688 -43.550 -8.342  1.00 73.05  ? 102 PHE   A C   1 
ATOM   596  O  O   . PHE   A 1 82  ? -27.983 -42.431 -8.760  1.00 90.95  ? 102 PHE   A O   1 
ATOM   597  C  CB  . PHE   A 1 82  ? -27.802 -44.393 -10.730 1.00 77.58  ? 102 PHE   A CB  1 
ATOM   598  C  CG  . PHE   A 1 82  ? -28.023 -45.571 -11.629 1.00 76.51  ? 102 PHE   A CG  1 
ATOM   599  C  CD1 . PHE   A 1 82  ? -26.952 -46.304 -12.100 1.00 74.05  ? 102 PHE   A CD1 1 
ATOM   600  C  CD2 . PHE   A 1 82  ? -29.303 -45.951 -11.994 1.00 85.55  ? 102 PHE   A CD2 1 
ATOM   601  C  CE1 . PHE   A 1 82  ? -27.146 -47.394 -12.924 1.00 82.34  ? 102 PHE   A CE1 1 
ATOM   602  C  CE2 . PHE   A 1 82  ? -29.508 -47.045 -12.821 1.00 84.80  ? 102 PHE   A CE2 1 
ATOM   603  C  CZ  . PHE   A 1 82  ? -28.426 -47.767 -13.287 1.00 88.38  ? 102 PHE   A CZ  1 
ATOM   604  N  N   . THR   A 1 83  ? -27.353 -43.777 -7.069  1.00 73.08  ? 103 THR   A N   1 
ATOM   605  C  CA  . THR   A 1 83  ? -27.413 -42.727 -6.054  1.00 74.63  ? 103 THR   A CA  1 
ATOM   606  C  C   . THR   A 1 83  ? -26.114 -41.938 -5.934  1.00 61.18  ? 103 THR   A C   1 
ATOM   607  O  O   . THR   A 1 83  ? -26.155 -40.738 -5.642  1.00 65.96  ? 103 THR   A O   1 
ATOM   608  C  CB  . THR   A 1 83  ? -27.763 -43.339 -4.688  1.00 79.57  ? 103 THR   A CB  1 
ATOM   609  O  OG1 . THR   A 1 83  ? -28.942 -44.146 -4.806  1.00 86.29  ? 103 THR   A OG1 1 
ATOM   610  C  CG2 . THR   A 1 83  ? -28.010 -42.246 -3.638  1.00 79.22  ? 103 THR   A CG2 1 
ATOM   611  N  N   . ASN   A 1 84  ? -24.968 -42.575 -6.167  1.00 62.02  ? 104 ASN   A N   1 
ATOM   612  C  CA  . ASN   A 1 84  ? -23.677 -42.027 -5.787  1.00 69.62  ? 104 ASN   A CA  1 
ATOM   613  C  C   . ASN   A 1 84  ? -22.742 -41.914 -6.982  1.00 61.05  ? 104 ASN   A C   1 
ATOM   614  O  O   . ASN   A 1 84  ? -22.859 -42.655 -7.966  1.00 68.44  ? 104 ASN   A O   1 
ATOM   615  C  CB  . ASN   A 1 84  ? -23.018 -42.899 -4.717  1.00 58.76  ? 104 ASN   A CB  1 
ATOM   616  C  CG  . ASN   A 1 84  ? -24.001 -43.351 -3.660  1.00 69.78  ? 104 ASN   A CG  1 
ATOM   617  O  OD1 . ASN   A 1 84  ? -24.812 -42.565 -3.177  1.00 77.03  ? 104 ASN   A OD1 1 
ATOM   618  N  ND2 . ASN   A 1 84  ? -23.940 -44.629 -3.301  1.00 73.36  ? 104 ASN   A ND2 1 
ATOM   619  N  N   . ARG   A 1 85  ? -21.801 -40.977 -6.869  1.00 65.69  ? 105 ARG   A N   1 
ATOM   620  C  CA  . ARG   A 1 85  ? -20.729 -40.833 -7.840  1.00 59.43  ? 105 ARG   A CA  1 
ATOM   621  C  C   . ARG   A 1 85  ? -19.621 -41.830 -7.518  1.00 66.95  ? 105 ARG   A C   1 
ATOM   622  O  O   . ARG   A 1 85  ? -19.667 -42.551 -6.516  1.00 71.94  ? 105 ARG   A O   1 
ATOM   623  C  CB  . ARG   A 1 85  ? -20.201 -39.398 -7.846  1.00 66.48  ? 105 ARG   A CB  1 
ATOM   624  C  CG  . ARG   A 1 85  ? -21.308 -38.354 -7.916  1.00 72.73  ? 105 ARG   A CG  1 
ATOM   625  C  CD  . ARG   A 1 85  ? -20.776 -36.944 -8.152  1.00 71.37  ? 105 ARG   A CD  1 
ATOM   626  N  NE  . ARG   A 1 85  ? -21.816 -36.081 -8.700  1.00 73.32  ? 105 ARG   A NE  1 
ATOM   627  C  CZ  . ARG   A 1 85  ? -22.588 -35.277 -7.981  1.00 76.42  ? 105 ARG   A CZ  1 
ATOM   628  N  NH1 . ARG   A 1 85  ? -22.443 -35.165 -6.672  1.00 77.16  ? 105 ARG   A NH1 1 
ATOM   629  N  NH2 . ARG   A 1 85  ? -23.533 -34.568 -8.593  1.00 69.42  ? 105 ARG   A NH2 1 
ATOM   630  N  N   . ARG   A 1 86  ? -18.617 -41.891 -8.382  1.00 73.65  ? 106 ARG   A N   1 
ATOM   631  C  CA  . ARG   A 1 86  ? -17.626 -42.941 -8.203  1.00 78.64  ? 106 ARG   A CA  1 
ATOM   632  C  C   . ARG   A 1 86  ? -16.757 -42.618 -6.986  1.00 77.23  ? 106 ARG   A C   1 
ATOM   633  O  O   . ARG   A 1 86  ? -16.455 -41.446 -6.723  1.00 68.20  ? 106 ARG   A O   1 
ATOM   634  C  CB  . ARG   A 1 86  ? -16.788 -43.133 -9.464  1.00 82.14  ? 106 ARG   A CB  1 
ATOM   635  C  CG  . ARG   A 1 86  ? -15.752 -42.074 -9.732  1.00 93.40  ? 106 ARG   A CG  1 
ATOM   636  C  CD  . ARG   A 1 86  ? -14.664 -42.642 -10.623 1.00 96.19  ? 106 ARG   A CD  1 
ATOM   637  N  NE  . ARG   A 1 86  ? -15.008 -42.548 -12.037 1.00 101.74 ? 106 ARG   A NE  1 
ATOM   638  C  CZ  . ARG   A 1 86  ? -14.438 -43.267 -12.994 1.00 89.95  ? 106 ARG   A CZ  1 
ATOM   639  N  NH1 . ARG   A 1 86  ? -13.499 -44.158 -12.720 1.00 82.77  ? 106 ARG   A NH1 1 
ATOM   640  N  NH2 . ARG   A 1 86  ? -14.826 -43.096 -14.254 1.00 81.95  ? 106 ARG   A NH2 1 
ATOM   641  N  N   . PRO   A 1 87  ? -16.379 -43.621 -6.190  1.00 81.12  ? 107 PRO   A N   1 
ATOM   642  C  CA  . PRO   A 1 87  ? -15.710 -43.345 -4.906  1.00 79.36  ? 107 PRO   A CA  1 
ATOM   643  C  C   . PRO   A 1 87  ? -14.438 -42.527 -5.052  1.00 87.61  ? 107 PRO   A C   1 
ATOM   644  O  O   . PRO   A 1 87  ? -13.408 -43.036 -5.504  1.00 96.58  ? 107 PRO   A O   1 
ATOM   645  C  CB  . PRO   A 1 87  ? -15.415 -44.752 -4.355  1.00 85.29  ? 107 PRO   A CB  1 
ATOM   646  C  CG  . PRO   A 1 87  ? -15.486 -45.668 -5.529  1.00 92.93  ? 107 PRO   A CG  1 
ATOM   647  C  CD  . PRO   A 1 87  ? -16.536 -45.068 -6.427  1.00 84.06  ? 107 PRO   A CD  1 
ATOM   648  N  N   . PHE   A 1 88  ? -14.505 -41.263 -4.648  1.00 102.49 ? 108 PHE   A N   1 
ATOM   649  C  CA  . PHE   A 1 88  ? -13.372 -40.350 -4.706  1.00 106.66 ? 108 PHE   A CA  1 
ATOM   650  C  C   . PHE   A 1 88  ? -12.686 -40.283 -3.349  1.00 122.65 ? 108 PHE   A C   1 
ATOM   651  O  O   . PHE   A 1 88  ? -13.348 -40.130 -2.317  1.00 121.87 ? 108 PHE   A O   1 
ATOM   652  C  CB  . PHE   A 1 88  ? -13.819 -38.952 -5.140  1.00 114.03 ? 108 PHE   A CB  1 
ATOM   653  C  CG  . PHE   A 1 88  ? -12.751 -37.909 -5.008  1.00 119.17 ? 108 PHE   A CG  1 
ATOM   654  C  CD1 . PHE   A 1 88  ? -11.540 -38.057 -5.663  1.00 122.25 ? 108 PHE   A CD1 1 
ATOM   655  C  CD2 . PHE   A 1 88  ? -12.958 -36.777 -4.237  1.00 110.65 ? 108 PHE   A CD2 1 
ATOM   656  C  CE1 . PHE   A 1 88  ? -10.553 -37.102 -5.547  1.00 133.42 ? 108 PHE   A CE1 1 
ATOM   657  C  CE2 . PHE   A 1 88  ? -11.974 -35.815 -4.118  1.00 126.70 ? 108 PHE   A CE2 1 
ATOM   658  C  CZ  . PHE   A 1 88  ? -10.769 -35.978 -4.775  1.00 134.51 ? 108 PHE   A CZ  1 
ATOM   659  N  N   . GLY   A 1 89  ? -11.361 -40.397 -3.359  1.00 114.03 ? 109 GLY   A N   1 
ATOM   660  C  CA  . GLY   A 1 89  ? -10.568 -40.332 -2.157  1.00 113.77 ? 109 GLY   A CA  1 
ATOM   661  C  C   . GLY   A 1 89  ? -9.093  -40.232 -2.488  1.00 110.84 ? 109 GLY   A C   1 
ATOM   662  O  O   . GLY   A 1 89  ? -8.694  -40.278 -3.653  1.00 115.13 ? 109 GLY   A O   1 
ATOM   663  N  N   . PRO   A 1 90  ? -8.246  -40.083 -1.459  1.00 115.19 ? 110 PRO   A N   1 
ATOM   664  C  CA  . PRO   A 1 90  ? -8.575  -39.961 -0.029  1.00 108.57 ? 110 PRO   A CA  1 
ATOM   665  C  C   . PRO   A 1 90  ? -9.144  -38.585 0.303   1.00 109.46 ? 110 PRO   A C   1 
ATOM   666  O  O   . PRO   A 1 90  ? -8.626  -37.563 -0.145  1.00 115.82 ? 110 PRO   A O   1 
ATOM   667  C  CB  . PRO   A 1 90  ? -7.221  -40.211 0.651   1.00 113.91 ? 110 PRO   A CB  1 
ATOM   668  C  CG  . PRO   A 1 90  ? -6.222  -39.704 -0.345  1.00 107.47 ? 110 PRO   A CG  1 
ATOM   669  C  CD  . PRO   A 1 90  ? -6.792  -40.095 -1.687  1.00 110.65 ? 110 PRO   A CD  1 
ATOM   670  N  N   . VAL   A 1 91  ? -10.214 -38.528 1.092   1.00 101.65 ? 111 VAL   A N   1 
ATOM   671  C  CA  . VAL   A 1 91  ? -10.916 -37.277 1.356   1.00 106.82 ? 111 VAL   A CA  1 
ATOM   672  C  C   . VAL   A 1 91  ? -10.933 -36.896 2.827   1.00 106.88 ? 111 VAL   A C   1 
ATOM   673  O  O   . VAL   A 1 91  ? -11.238 -35.736 3.143   1.00 108.36 ? 111 VAL   A O   1 
ATOM   674  C  CB  . VAL   A 1 91  ? -12.360 -37.318 0.808   1.00 100.30 ? 111 VAL   A CB  1 
ATOM   675  C  CG1 . VAL   A 1 91  ? -12.347 -37.311 -0.714  1.00 106.87 ? 111 VAL   A CG1 1 
ATOM   676  C  CG2 . VAL   A 1 91  ? -13.086 -38.544 1.332   1.00 92.20  ? 111 VAL   A CG2 1 
ATOM   677  N  N   . GLY   A 1 92  ? -10.613 -37.812 3.736   1.00 101.23 ? 112 GLY   A N   1 
ATOM   678  C  CA  . GLY   A 1 92  ? -10.633 -37.468 5.147   1.00 108.06 ? 112 GLY   A CA  1 
ATOM   679  C  C   . GLY   A 1 92  ? -12.033 -37.127 5.614   1.00 99.60  ? 112 GLY   A C   1 
ATOM   680  O  O   . GLY   A 1 92  ? -13.022 -37.745 5.204   1.00 96.55  ? 112 GLY   A O   1 
ATOM   681  N  N   . PHE   A 1 93  ? -12.126 -36.111 6.476   1.00 104.13 ? 113 PHE   A N   1 
ATOM   682  C  CA  . PHE   A 1 93  ? -13.428 -35.682 6.976   1.00 102.83 ? 113 PHE   A CA  1 
ATOM   683  C  C   . PHE   A 1 93  ? -14.327 -35.155 5.867   1.00 100.28 ? 113 PHE   A C   1 
ATOM   684  O  O   . PHE   A 1 93  ? -15.546 -35.080 6.059   1.00 103.87 ? 113 PHE   A O   1 
ATOM   685  C  CB  . PHE   A 1 93  ? -13.258 -34.605 8.048   1.00 100.02 ? 113 PHE   A CB  1 
ATOM   686  C  CG  . PHE   A 1 93  ? -12.959 -33.245 7.492   1.00 108.13 ? 113 PHE   A CG  1 
ATOM   687  C  CD1 . PHE   A 1 93  ? -11.668 -32.901 7.141   1.00 118.86 ? 113 PHE   A CD1 1 
ATOM   688  C  CD2 . PHE   A 1 93  ? -13.969 -32.312 7.314   1.00 109.97 ? 113 PHE   A CD2 1 
ATOM   689  C  CE1 . PHE   A 1 93  ? -11.390 -31.660 6.626   1.00 118.54 ? 113 PHE   A CE1 1 
ATOM   690  C  CE2 . PHE   A 1 93  ? -13.695 -31.064 6.798   1.00 114.19 ? 113 PHE   A CE2 1 
ATOM   691  C  CZ  . PHE   A 1 93  ? -12.403 -30.736 6.453   1.00 122.42 ? 113 PHE   A CZ  1 
ATOM   692  N  N   . MET   A 1 94  ? -13.757 -34.788 4.714   1.00 94.23  ? 114 MET   A N   1 
ATOM   693  C  CA  . MET   A 1 94  ? -14.533 -34.279 3.588   1.00 95.23  ? 114 MET   A CA  1 
ATOM   694  C  C   . MET   A 1 94  ? -15.449 -35.360 3.030   1.00 92.90  ? 114 MET   A C   1 
ATOM   695  O  O   . MET   A 1 94  ? -16.236 -35.098 2.114   1.00 92.11  ? 114 MET   A O   1 
ATOM   696  C  CB  . MET   A 1 94  ? -13.613 -33.737 2.489   1.00 102.72 ? 114 MET   A CB  1 
ATOM   697  C  CG  . MET   A 1 94  ? -12.898 -32.438 2.856   1.00 110.38 ? 114 MET   A CG  1 
ATOM   698  S  SD  . MET   A 1 94  ? -14.035 -31.091 3.255   1.00 97.16  ? 114 MET   A SD  1 
ATOM   699  C  CE  . MET   A 1 94  ? -14.951 -30.943 1.725   1.00 87.91  ? 114 MET   A CE  1 
ATOM   700  N  N   . LYS   A 1 95  ? -15.344 -36.578 3.567   1.00 85.12  ? 115 LYS   A N   1 
ATOM   701  C  CA  . LYS   A 1 95  ? -16.341 -37.606 3.303   1.00 89.54  ? 115 LYS   A CA  1 
ATOM   702  C  C   . LYS   A 1 95  ? -17.743 -37.140 3.673   1.00 84.47  ? 115 LYS   A C   1 
ATOM   703  O  O   . LYS   A 1 95  ? -18.723 -37.646 3.115   1.00 84.15  ? 115 LYS   A O   1 
ATOM   704  C  CB  . LYS   A 1 95  ? -15.990 -38.877 4.083   1.00 92.29  ? 115 LYS   A CB  1 
ATOM   705  C  CG  . LYS   A 1 95  ? -16.173 -38.731 5.588   1.00 104.55 ? 115 LYS   A CG  1 
ATOM   706  C  CD  . LYS   A 1 95  ? -15.853 -40.015 6.325   1.00 119.01 ? 115 LYS   A CD  1 
ATOM   707  C  CE  . LYS   A 1 95  ? -16.138 -39.874 7.811   1.00 122.49 ? 115 LYS   A CE  1 
ATOM   708  N  NZ  . LYS   A 1 95  ? -15.414 -38.715 8.408   1.00 125.21 ? 115 LYS   A NZ  1 
ATOM   709  N  N   . SER   A 1 96  ? -17.855 -36.185 4.597   1.00 86.08  ? 116 SER   A N   1 
ATOM   710  C  CA  . SER   A 1 96  ? -19.132 -35.664 5.068   1.00 87.06  ? 116 SER   A CA  1 
ATOM   711  C  C   . SER   A 1 96  ? -19.673 -34.535 4.202   1.00 88.56  ? 116 SER   A C   1 
ATOM   712  O  O   . SER   A 1 96  ? -20.708 -33.955 4.543   1.00 83.49  ? 116 SER   A O   1 
ATOM   713  C  CB  . SER   A 1 96  ? -19.002 -35.175 6.515   1.00 89.01  ? 116 SER   A CB  1 
ATOM   714  O  OG  . SER   A 1 96  ? -18.410 -36.163 7.338   1.00 106.34 ? 116 SER   A OG  1 
ATOM   715  N  N   . ALA   A 1 97  ? -19.003 -34.206 3.104   1.00 83.49  ? 117 ALA   A N   1 
ATOM   716  C  CA  . ALA   A 1 97  ? -19.470 -33.171 2.196   1.00 84.15  ? 117 ALA   A CA  1 
ATOM   717  C  C   . ALA   A 1 97  ? -20.467 -33.759 1.204   1.00 82.12  ? 117 ALA   A C   1 
ATOM   718  O  O   . ALA   A 1 97  ? -20.359 -34.921 0.805   1.00 78.49  ? 117 ALA   A O   1 
ATOM   719  C  CB  . ALA   A 1 97  ? -18.290 -32.540 1.464   1.00 92.04  ? 117 ALA   A CB  1 
ATOM   720  N  N   . ILE   A 1 98  ? -21.432 -32.930 0.793   1.00 73.93  ? 118 ILE   A N   1 
ATOM   721  C  CA  . ILE   A 1 98  ? -22.632 -33.445 0.132   1.00 79.19  ? 118 ILE   A CA  1 
ATOM   722  C  C   . ILE   A 1 98  ? -22.298 -34.078 -1.213  1.00 73.51  ? 118 ILE   A C   1 
ATOM   723  O  O   . ILE   A 1 98  ? -22.778 -35.174 -1.533  1.00 73.12  ? 118 ILE   A O   1 
ATOM   724  C  CB  . ILE   A 1 98  ? -23.691 -32.332 -0.006  1.00 77.79  ? 118 ILE   A CB  1 
ATOM   725  C  CG1 . ILE   A 1 98  ? -24.851 -32.813 -0.880  1.00 75.34  ? 118 ILE   A CG1 1 
ATOM   726  C  CG2 . ILE   A 1 98  ? -23.076 -31.049 -0.554  1.00 77.19  ? 118 ILE   A CG2 1 
ATOM   727  C  CD1 . ILE   A 1 98  ? -26.056 -31.910 -0.845  1.00 88.32  ? 118 ILE   A CD1 1 
ATOM   728  N  N   . SER   A 1 99  ? -21.473 -33.412 -2.021  1.00 78.59  ? 119 SER   A N   1 
ATOM   729  C  CA  . SER   A 1 99  ? -21.134 -33.953 -3.336  1.00 81.27  ? 119 SER   A CA  1 
ATOM   730  C  C   . SER   A 1 99  ? -20.307 -35.234 -3.256  1.00 77.36  ? 119 SER   A C   1 
ATOM   731  O  O   . SER   A 1 99  ? -20.130 -35.906 -4.274  1.00 74.59  ? 119 SER   A O   1 
ATOM   732  C  CB  . SER   A 1 99  ? -20.397 -32.893 -4.155  1.00 80.07  ? 119 SER   A CB  1 
ATOM   733  O  OG  . SER   A 1 99  ? -19.104 -32.684 -3.641  1.00 74.24  ? 119 SER   A OG  1 
ATOM   734  N  N   . ILE   A 1 100 ? -19.820 -35.586 -2.067  1.00 75.85  ? 120 ILE   A N   1 
ATOM   735  C  CA  . ILE   A 1 100 ? -19.049 -36.795 -1.865  1.00 75.98  ? 120 ILE   A CA  1 
ATOM   736  C  C   . ILE   A 1 100 ? -19.844 -37.861 -1.117  1.00 76.89  ? 120 ILE   A C   1 
ATOM   737  O  O   . ILE   A 1 100 ? -19.635 -39.055 -1.361  1.00 64.35  ? 120 ILE   A O   1 
ATOM   738  C  CB  . ILE   A 1 100 ? -17.727 -36.483 -1.133  1.00 79.03  ? 120 ILE   A CB  1 
ATOM   739  C  CG1 . ILE   A 1 100 ? -16.846 -35.571 -1.980  1.00 83.82  ? 120 ILE   A CG1 1 
ATOM   740  C  CG2 . ILE   A 1 100 ? -16.976 -37.760 -0.728  1.00 76.20  ? 120 ILE   A CG2 1 
ATOM   741  C  CD1 . ILE   A 1 100 ? -15.629 -35.044 -1.304  1.00 99.77  ? 120 ILE   A CD1 1 
ATOM   742  N  N   . ALA   A 1 101 ? -20.789 -37.467 -0.262  1.00 78.96  ? 121 ALA   A N   1 
ATOM   743  C  CA  . ALA   A 1 101 ? -21.543 -38.420 0.545   1.00 75.21  ? 121 ALA   A CA  1 
ATOM   744  C  C   . ALA   A 1 101 ? -22.395 -39.349 -0.319  1.00 76.10  ? 121 ALA   A C   1 
ATOM   745  O  O   . ALA   A 1 101 ? -22.766 -39.032 -1.453  1.00 61.88  ? 121 ALA   A O   1 
ATOM   746  C  CB  . ALA   A 1 101 ? -22.452 -37.699 1.543   1.00 76.77  ? 121 ALA   A CB  1 
ATOM   747  N  N   . GLU   A 1 102 ? -22.750 -40.499 0.260   1.00 71.62  ? 122 GLU   A N   1 
ATOM   748  C  CA  . GLU   A 1 102 ? -23.475 -41.543 -0.456  1.00 72.03  ? 122 GLU   A CA  1 
ATOM   749  C  C   . GLU   A 1 102 ? -24.789 -41.887 0.235   1.00 81.33  ? 122 GLU   A C   1 
ATOM   750  O  O   . GLU   A 1 102 ? -24.926 -41.738 1.451   1.00 86.93  ? 122 GLU   A O   1 
ATOM   751  C  CB  . GLU   A 1 102 ? -22.646 -42.831 -0.578  1.00 76.41  ? 122 GLU   A CB  1 
ATOM   752  C  CG  . GLU   A 1 102 ? -21.150 -42.618 -0.634  1.00 77.40  ? 122 GLU   A CG  1 
ATOM   753  C  CD  . GLU   A 1 102 ? -20.411 -43.869 -1.050  1.00 84.91  ? 122 GLU   A CD  1 
ATOM   754  O  OE1 . GLU   A 1 102 ? -20.465 -44.871 -0.306  1.00 95.04  ? 122 GLU   A OE1 1 
ATOM   755  O  OE2 . GLU   A 1 102 ? -19.804 -43.861 -2.141  1.00 75.50  ? 122 GLU   A OE2 1 
ATOM   756  N  N   . ASP   A 1 103 ? -25.757 -42.336 -0.565  1.00 82.93  ? 123 ASP   A N   1 
ATOM   757  C  CA  . ASP   A 1 103 ? -26.955 -43.050 -0.090  1.00 91.94  ? 123 ASP   A CA  1 
ATOM   758  C  C   . ASP   A 1 103 ? -27.705 -42.180 0.918   1.00 92.99  ? 123 ASP   A C   1 
ATOM   759  O  O   . ASP   A 1 103 ? -28.043 -41.030 0.595   1.00 89.34  ? 123 ASP   A O   1 
ATOM   760  C  CB  . ASP   A 1 103 ? -26.517 -44.417 0.420   1.00 98.65  ? 123 ASP   A CB  1 
ATOM   761  C  CG  . ASP   A 1 103 ? -25.925 -45.284 -0.673  1.00 101.59 ? 123 ASP   A CG  1 
ATOM   762  O  OD1 . ASP   A 1 103 ? -26.341 -45.142 -1.842  1.00 96.74  ? 123 ASP   A OD1 1 
ATOM   763  O  OD2 . ASP   A 1 103 ? -25.045 -46.113 -0.359  1.00 98.86  ? 123 ASP   A OD2 1 
ATOM   764  N  N   . GLU   A 1 104 ? -27.983 -42.671 2.129   1.00 93.55  ? 124 GLU   A N   1 
ATOM   765  C  CA  . GLU   A 1 104 ? -28.867 -41.949 3.035   1.00 97.22  ? 124 GLU   A CA  1 
ATOM   766  C  C   . GLU   A 1 104 ? -28.178 -40.747 3.661   1.00 95.67  ? 124 GLU   A C   1 
ATOM   767  O  O   . GLU   A 1 104 ? -28.843 -39.756 3.983   1.00 91.46  ? 124 GLU   A O   1 
ATOM   768  C  CB  . GLU   A 1 104 ? -29.387 -42.892 4.117   1.00 105.80 ? 124 GLU   A CB  1 
ATOM   769  C  CG  . GLU   A 1 104 ? -29.985 -44.171 3.566   1.00 116.71 ? 124 GLU   A CG  1 
ATOM   770  C  CD  . GLU   A 1 104 ? -31.047 -43.909 2.519   1.00 131.61 ? 124 GLU   A CD  1 
ATOM   771  O  OE1 . GLU   A 1 104 ? -32.026 -43.199 2.830   1.00 124.77 ? 124 GLU   A OE1 1 
ATOM   772  O  OE2 . GLU   A 1 104 ? -30.895 -44.401 1.381   1.00 139.43 ? 124 GLU   A OE2 1 
ATOM   773  N  N   . GLU   A 1 105 ? -26.858 -40.815 3.851   1.00 85.12  ? 125 GLU   A N   1 
ATOM   774  C  CA  . GLU   A 1 105 ? -26.131 -39.661 4.371   1.00 89.14  ? 125 GLU   A CA  1 
ATOM   775  C  C   . GLU   A 1 105 ? -26.223 -38.478 3.415   1.00 89.93  ? 125 GLU   A C   1 
ATOM   776  O  O   . GLU   A 1 105 ? -26.463 -37.342 3.841   1.00 94.68  ? 125 GLU   A O   1 
ATOM   777  C  CB  . GLU   A 1 105 ? -24.673 -40.030 4.637   1.00 92.67  ? 125 GLU   A CB  1 
ATOM   778  C  CG  . GLU   A 1 105 ? -24.426 -40.630 6.012   1.00 106.64 ? 125 GLU   A CG  1 
ATOM   779  C  CD  . GLU   A 1 105 ? -24.874 -42.071 6.111   1.00 116.55 ? 125 GLU   A CD  1 
ATOM   780  O  OE1 . GLU   A 1 105 ? -24.924 -42.748 5.064   1.00 116.28 ? 125 GLU   A OE1 1 
ATOM   781  O  OE2 . GLU   A 1 105 ? -25.178 -42.527 7.234   1.00 123.61 ? 125 GLU   A OE2 1 
ATOM   782  N  N   . TRP   A 1 106 ? -26.045 -38.727 2.115   1.00 82.40  ? 126 TRP   A N   1 
ATOM   783  C  CA  . TRP   A 1 106 ? -26.244 -37.665 1.135   1.00 83.41  ? 126 TRP   A CA  1 
ATOM   784  C  C   . TRP   A 1 106 ? -27.695 -37.210 1.106   1.00 81.81  ? 126 TRP   A C   1 
ATOM   785  O  O   . TRP   A 1 106 ? -27.974 -36.008 1.025   1.00 81.87  ? 126 TRP   A O   1 
ATOM   786  C  CB  . TRP   A 1 106 ? -25.816 -38.129 -0.257  1.00 80.42  ? 126 TRP   A CB  1 
ATOM   787  C  CG  . TRP   A 1 106 ? -26.472 -37.324 -1.339  1.00 80.27  ? 126 TRP   A CG  1 
ATOM   788  C  CD1 . TRP   A 1 106 ? -26.060 -36.119 -1.827  1.00 66.96  ? 126 TRP   A CD1 1 
ATOM   789  C  CD2 . TRP   A 1 106 ? -27.674 -37.653 -2.048  1.00 76.78  ? 126 TRP   A CD2 1 
ATOM   790  N  NE1 . TRP   A 1 106 ? -26.924 -35.682 -2.802  1.00 65.20  ? 126 TRP   A NE1 1 
ATOM   791  C  CE2 . TRP   A 1 106 ? -27.924 -36.605 -2.955  1.00 75.05  ? 126 TRP   A CE2 1 
ATOM   792  C  CE3 . TRP   A 1 106 ? -28.561 -38.734 -2.004  1.00 77.14  ? 126 TRP   A CE3 1 
ATOM   793  C  CZ2 . TRP   A 1 106 ? -29.021 -36.607 -3.813  1.00 78.64  ? 126 TRP   A CZ2 1 
ATOM   794  C  CZ3 . TRP   A 1 106 ? -29.650 -38.733 -2.856  1.00 66.15  ? 126 TRP   A CZ3 1 
ATOM   795  C  CH2 . TRP   A 1 106 ? -29.871 -37.677 -3.749  1.00 76.47  ? 126 TRP   A CH2 1 
ATOM   796  N  N   . LYS   A 1 107 ? -28.634 -38.160 1.153   1.00 82.37  ? 127 LYS   A N   1 
ATOM   797  C  CA  . LYS   A 1 107 ? -30.052 -37.814 1.122   1.00 85.25  ? 127 LYS   A CA  1 
ATOM   798  C  C   . LYS   A 1 107 ? -30.429 -36.910 2.287   1.00 94.54  ? 127 LYS   A C   1 
ATOM   799  O  O   . LYS   A 1 107 ? -31.310 -36.054 2.150   1.00 91.86  ? 127 LYS   A O   1 
ATOM   800  C  CB  . LYS   A 1 107 ? -30.895 -39.090 1.130   1.00 77.56  ? 127 LYS   A CB  1 
ATOM   801  C  CG  . LYS   A 1 107 ? -32.389 -38.868 0.968   1.00 93.59  ? 127 LYS   A CG  1 
ATOM   802  C  CD  . LYS   A 1 107 ? -32.981 -39.848 -0.034  1.00 111.36 ? 127 LYS   A CD  1 
ATOM   803  C  CE  . LYS   A 1 107 ? -32.647 -41.288 0.323   1.00 118.13 ? 127 LYS   A CE  1 
ATOM   804  N  NZ  . LYS   A 1 107 ? -33.157 -42.244 -0.700  1.00 123.62 ? 127 LYS   A NZ  1 
ATOM   805  N  N   . ARG   A 1 108 ? -29.766 -37.074 3.432   1.00 95.80  ? 128 ARG   A N   1 
ATOM   806  C  CA  . ARG   A 1 108 ? -29.996 -36.176 4.557   1.00 94.58  ? 128 ARG   A CA  1 
ATOM   807  C  C   . ARG   A 1 108 ? -29.335 -34.823 4.322   1.00 87.86  ? 128 ARG   A C   1 
ATOM   808  O  O   . ARG   A 1 108 ? -29.964 -33.774 4.508   1.00 93.65  ? 128 ARG   A O   1 
ATOM   809  C  CB  . ARG   A 1 108 ? -29.481 -36.811 5.847   1.00 93.42  ? 128 ARG   A CB  1 
ATOM   810  C  CG  . ARG   A 1 108 ? -29.238 -35.821 6.970   1.00 99.00  ? 128 ARG   A CG  1 
ATOM   811  C  CD  . ARG   A 1 108 ? -28.744 -36.526 8.219   1.00 101.19 ? 128 ARG   A CD  1 
ATOM   812  N  NE  . ARG   A 1 108 ? -28.048 -35.614 9.118   1.00 115.13 ? 128 ARG   A NE  1 
ATOM   813  C  CZ  . ARG   A 1 108 ? -26.747 -35.365 9.067   1.00 108.78 ? 128 ARG   A CZ  1 
ATOM   814  N  NH1 . ARG   A 1 108 ? -25.967 -35.948 8.172   1.00 97.28  ? 128 ARG   A NH1 1 
ATOM   815  N  NH2 . ARG   A 1 108 ? -26.216 -34.509 9.935   1.00 111.71 ? 128 ARG   A NH2 1 
ATOM   816  N  N   . LEU   A 1 109 ? -28.063 -34.828 3.913   1.00 93.33  ? 129 LEU   A N   1 
ATOM   817  C  CA  . LEU   A 1 109 ? -27.351 -33.574 3.681   1.00 91.73  ? 129 LEU   A CA  1 
ATOM   818  C  C   . LEU   A 1 109 ? -28.034 -32.738 2.607   1.00 97.26  ? 129 LEU   A C   1 
ATOM   819  O  O   . LEU   A 1 109 ? -28.034 -31.504 2.677   1.00 94.15  ? 129 LEU   A O   1 
ATOM   820  C  CB  . LEU   A 1 109 ? -25.900 -33.858 3.292   1.00 83.07  ? 129 LEU   A CB  1 
ATOM   821  C  CG  . LEU   A 1 109 ? -24.977 -34.419 4.373   1.00 85.60  ? 129 LEU   A CG  1 
ATOM   822  C  CD1 . LEU   A 1 109 ? -23.662 -34.864 3.759   1.00 67.57  ? 129 LEU   A CD1 1 
ATOM   823  C  CD2 . LEU   A 1 109 ? -24.736 -33.378 5.452   1.00 71.99  ? 129 LEU   A CD2 1 
ATOM   824  N  N   . ARG   A 1 110 ? -28.622 -33.394 1.604   1.00 83.87  ? 130 ARG   A N   1 
ATOM   825  C  CA  . ARG   A 1 110 ? -29.339 -32.664 0.563   1.00 87.46  ? 130 ARG   A CA  1 
ATOM   826  C  C   . ARG   A 1 110 ? -30.548 -31.937 1.136   1.00 88.87  ? 130 ARG   A C   1 
ATOM   827  O  O   . ARG   A 1 110 ? -30.787 -30.767 0.814   1.00 91.53  ? 130 ARG   A O   1 
ATOM   828  C  CB  . ARG   A 1 110 ? -29.768 -33.618 -0.550  1.00 82.56  ? 130 ARG   A CB  1 
ATOM   829  C  CG  . ARG   A 1 110 ? -30.367 -32.920 -1.761  1.00 86.16  ? 130 ARG   A CG  1 
ATOM   830  C  CD  . ARG   A 1 110 ? -29.308 -32.616 -2.810  1.00 76.99  ? 130 ARG   A CD  1 
ATOM   831  N  NE  . ARG   A 1 110 ? -29.823 -31.766 -3.877  1.00 81.51  ? 130 ARG   A NE  1 
ATOM   832  C  CZ  . ARG   A 1 110 ? -29.233 -31.596 -5.053  1.00 78.34  ? 130 ARG   A CZ  1 
ATOM   833  N  NH1 . ARG   A 1 110 ? -28.116 -32.233 -5.364  1.00 79.45  ? 130 ARG   A NH1 1 
ATOM   834  N  NH2 . ARG   A 1 110 ? -29.780 -30.772 -5.941  1.00 73.22  ? 130 ARG   A NH2 1 
ATOM   835  N  N   . SER   A 1 111 ? -31.318 -32.613 1.991   1.00 89.46  ? 131 SER   A N   1 
ATOM   836  C  CA  . SER   A 1 111 ? -32.503 -31.994 2.577   1.00 98.67  ? 131 SER   A CA  1 
ATOM   837  C  C   . SER   A 1 111 ? -32.130 -30.800 3.443   1.00 95.09  ? 131 SER   A C   1 
ATOM   838  O  O   . SER   A 1 111 ? -32.770 -29.746 3.377   1.00 97.71  ? 131 SER   A O   1 
ATOM   839  C  CB  . SER   A 1 111 ? -33.286 -33.023 3.393   1.00 101.60 ? 131 SER   A CB  1 
ATOM   840  O  OG  . SER   A 1 111 ? -34.006 -33.908 2.553   1.00 113.02 ? 131 SER   A OG  1 
ATOM   841  N  N   . LEU   A 1 112 ? -31.092 -30.947 4.268   1.00 92.67  ? 132 LEU   A N   1 
ATOM   842  C  CA  . LEU   A 1 112 ? -30.694 -29.857 5.151   1.00 93.09  ? 132 LEU   A CA  1 
ATOM   843  C  C   . LEU   A 1 112 ? -30.130 -28.674 4.375   1.00 91.32  ? 132 LEU   A C   1 
ATOM   844  O  O   . LEU   A 1 112 ? -30.236 -27.530 4.831   1.00 100.53 ? 132 LEU   A O   1 
ATOM   845  C  CB  . LEU   A 1 112 ? -29.674 -30.359 6.167   1.00 98.28  ? 132 LEU   A CB  1 
ATOM   846  C  CG  . LEU   A 1 112 ? -30.197 -31.423 7.128   1.00 105.68 ? 132 LEU   A CG  1 
ATOM   847  C  CD1 . LEU   A 1 112 ? -29.027 -32.194 7.698   1.00 102.69 ? 132 LEU   A CD1 1 
ATOM   848  C  CD2 . LEU   A 1 112 ? -31.023 -30.791 8.243   1.00 106.70 ? 132 LEU   A CD2 1 
ATOM   849  N  N   . LEU   A 1 113 ? -29.536 -28.924 3.208   1.00 95.19  ? 133 LEU   A N   1 
ATOM   850  C  CA  . LEU   A 1 113 ? -28.908 -27.875 2.416   1.00 99.59  ? 133 LEU   A CA  1 
ATOM   851  C  C   . LEU   A 1 113 ? -29.762 -27.396 1.248   1.00 102.59 ? 133 LEU   A C   1 
ATOM   852  O  O   . LEU   A 1 113 ? -29.384 -26.420 0.593   1.00 104.53 ? 133 LEU   A O   1 
ATOM   853  C  CB  . LEU   A 1 113 ? -27.549 -28.355 1.890   1.00 93.53  ? 133 LEU   A CB  1 
ATOM   854  C  CG  . LEU   A 1 113 ? -26.457 -28.450 2.955   1.00 92.25  ? 133 LEU   A CG  1 
ATOM   855  C  CD1 . LEU   A 1 113 ? -25.200 -29.103 2.403   1.00 86.70  ? 133 LEU   A CD1 1 
ATOM   856  C  CD2 . LEU   A 1 113 ? -26.151 -27.065 3.495   1.00 96.87  ? 133 LEU   A CD2 1 
ATOM   857  N  N   . SER   A 1 114 ? -30.896 -28.048 0.970   1.00 98.91  ? 134 SER   A N   1 
ATOM   858  C  CA  . SER   A 1 114 ? -31.735 -27.607 -0.146  1.00 102.35 ? 134 SER   A CA  1 
ATOM   859  C  C   . SER   A 1 114 ? -32.384 -26.251 0.106   1.00 107.71 ? 134 SER   A C   1 
ATOM   860  O  O   . SER   A 1 114 ? -32.328 -25.391 -0.792  1.00 109.34 ? 134 SER   A O   1 
ATOM   861  C  CB  . SER   A 1 114 ? -32.775 -28.683 -0.476  1.00 101.52 ? 134 SER   A CB  1 
ATOM   862  O  OG  . SER   A 1 114 ? -32.167 -29.828 -1.050  1.00 114.50 ? 134 SER   A OG  1 
ATOM   863  N  N   . PRO   A 1 115 ? -33.012 -25.981 1.259   1.00 110.51 ? 135 PRO   A N   1 
ATOM   864  C  CA  . PRO   A 1 115 ? -33.604 -24.647 1.464   1.00 112.80 ? 135 PRO   A CA  1 
ATOM   865  C  C   . PRO   A 1 115 ? -32.589 -23.522 1.412   1.00 113.02 ? 135 PRO   A C   1 
ATOM   866  O  O   . PRO   A 1 115 ? -32.967 -22.369 1.165   1.00 110.15 ? 135 PRO   A O   1 
ATOM   867  C  CB  . PRO   A 1 115 ? -34.245 -24.754 2.856   1.00 118.11 ? 135 PRO   A CB  1 
ATOM   868  C  CG  . PRO   A 1 115 ? -34.418 -26.204 3.093   1.00 117.31 ? 135 PRO   A CG  1 
ATOM   869  C  CD  . PRO   A 1 115 ? -33.255 -26.853 2.422   1.00 109.18 ? 135 PRO   A CD  1 
ATOM   870  N  N   . THR   A 1 116 ? -31.311 -23.823 1.647   1.00 114.10 ? 136 THR   A N   1 
ATOM   871  C  CA  . THR   A 1 116 ? -30.263 -22.820 1.510   1.00 111.36 ? 136 THR   A CA  1 
ATOM   872  C  C   . THR   A 1 116 ? -30.226 -22.238 0.103   1.00 99.00  ? 136 THR   A C   1 
ATOM   873  O  O   . THR   A 1 116 ? -29.911 -21.055 -0.073  1.00 104.42 ? 136 THR   A O   1 
ATOM   874  C  CB  . THR   A 1 116 ? -28.908 -23.439 1.858   1.00 103.28 ? 136 THR   A CB  1 
ATOM   875  O  OG1 . THR   A 1 116 ? -29.030 -24.237 3.043   1.00 115.96 ? 136 THR   A OG1 1 
ATOM   876  C  CG2 . THR   A 1 116 ? -27.871 -22.361 2.095   1.00 111.29 ? 136 THR   A CG2 1 
ATOM   877  N  N   . PHE   A 1 117 ? -30.552 -23.045 -0.908  1.00 104.76 ? 137 PHE   A N   1 
ATOM   878  C  CA  . PHE   A 1 117 ? -30.435 -22.651 -2.306  1.00 108.38 ? 137 PHE   A CA  1 
ATOM   879  C  C   . PHE   A 1 117 ? -31.793 -22.432 -2.963  1.00 109.99 ? 137 PHE   A C   1 
ATOM   880  O  O   . PHE   A 1 117 ? -31.961 -22.711 -4.152  1.00 103.36 ? 137 PHE   A O   1 
ATOM   881  C  CB  . PHE   A 1 117 ? -29.636 -23.691 -3.088  1.00 98.43  ? 137 PHE   A CB  1 
ATOM   882  C  CG  . PHE   A 1 117 ? -28.247 -23.905 -2.566  1.00 96.08  ? 137 PHE   A CG  1 
ATOM   883  C  CD1 . PHE   A 1 117 ? -27.180 -23.189 -3.081  1.00 93.39  ? 137 PHE   A CD1 1 
ATOM   884  C  CD2 . PHE   A 1 117 ? -28.008 -24.823 -1.560  1.00 87.63  ? 137 PHE   A CD2 1 
ATOM   885  C  CE1 . PHE   A 1 117 ? -25.901 -23.386 -2.598  1.00 90.60  ? 137 PHE   A CE1 1 
ATOM   886  C  CE2 . PHE   A 1 117 ? -26.734 -25.024 -1.072  1.00 98.93  ? 137 PHE   A CE2 1 
ATOM   887  C  CZ  . PHE   A 1 117 ? -25.678 -24.305 -1.592  1.00 89.63  ? 137 PHE   A CZ  1 
ATOM   888  N  N   . THR   A 1 118 ? -32.768 -21.930 -2.212  1.00 108.97 ? 138 THR   A N   1 
ATOM   889  C  CA  . THR   A 1 118 ? -34.052 -21.605 -2.813  1.00 117.19 ? 138 THR   A CA  1 
ATOM   890  C  C   . THR   A 1 118 ? -33.966 -20.275 -3.554  1.00 121.90 ? 138 THR   A C   1 
ATOM   891  O  O   . THR   A 1 118 ? -33.073 -19.457 -3.316  1.00 121.70 ? 138 THR   A O   1 
ATOM   892  C  CB  . THR   A 1 118 ? -35.158 -21.541 -1.756  1.00 120.13 ? 138 THR   A CB  1 
ATOM   893  O  OG1 . THR   A 1 118 ? -34.788 -20.625 -0.719  1.00 116.41 ? 138 THR   A OG1 1 
ATOM   894  C  CG2 . THR   A 1 118 ? -35.411 -22.914 -1.156  1.00 123.14 ? 138 THR   A CG2 1 
ATOM   895  N  N   . SER   A 1 119 ? -34.913 -20.070 -4.473  1.00 125.30 ? 139 SER   A N   1 
ATOM   896  C  CA  . SER   A 1 119 ? -34.976 -18.810 -5.205  1.00 135.36 ? 139 SER   A CA  1 
ATOM   897  C  C   . SER   A 1 119 ? -35.166 -17.625 -4.268  1.00 130.43 ? 139 SER   A C   1 
ATOM   898  O  O   . SER   A 1 119 ? -34.678 -16.524 -4.550  1.00 131.32 ? 139 SER   A O   1 
ATOM   899  C  CB  . SER   A 1 119 ? -36.105 -18.868 -6.235  1.00 137.98 ? 139 SER   A CB  1 
ATOM   900  O  OG  . SER   A 1 119 ? -37.306 -19.341 -5.646  1.00 138.49 ? 139 SER   A OG  1 
ATOM   901  N  N   . GLY   A 1 120 ? -35.857 -17.830 -3.147  1.00 124.84 ? 140 GLY   A N   1 
ATOM   902  C  CA  . GLY   A 1 120 ? -36.063 -16.737 -2.210  1.00 130.78 ? 140 GLY   A CA  1 
ATOM   903  C  C   . GLY   A 1 120 ? -34.774 -16.286 -1.549  1.00 124.06 ? 140 GLY   A C   1 
ATOM   904  O  O   . GLY   A 1 120 ? -34.465 -15.092 -1.517  1.00 124.04 ? 140 GLY   A O   1 
ATOM   905  N  N   . LYS   A 1 121 ? -34.008 -17.236 -1.002  1.00 123.55 ? 141 LYS   A N   1 
ATOM   906  C  CA  . LYS   A 1 121 ? -32.730 -16.892 -0.386  1.00 124.01 ? 141 LYS   A CA  1 
ATOM   907  C  C   . LYS   A 1 121 ? -31.772 -16.285 -1.404  1.00 115.85 ? 141 LYS   A C   1 
ATOM   908  O  O   . LYS   A 1 121 ? -30.998 -15.378 -1.076  1.00 119.04 ? 141 LYS   A O   1 
ATOM   909  C  CB  . LYS   A 1 121 ? -32.099 -18.127 0.256   1.00 115.58 ? 141 LYS   A CB  1 
ATOM   910  C  CG  . LYS   A 1 121 ? -33.020 -18.905 1.175   1.00 113.65 ? 141 LYS   A CG  1 
ATOM   911  C  CD  . LYS   A 1 121 ? -33.412 -18.104 2.401   1.00 117.92 ? 141 LYS   A CD  1 
ATOM   912  C  CE  . LYS   A 1 121 ? -34.356 -18.907 3.280   1.00 123.22 ? 141 LYS   A CE  1 
ATOM   913  N  NZ  . LYS   A 1 121 ? -33.819 -20.267 3.566   1.00 116.35 ? 141 LYS   A NZ  1 
ATOM   914  N  N   . LEU   A 1 122 ? -31.814 -16.775 -2.647  1.00 122.67 ? 142 LEU   A N   1 
ATOM   915  C  CA  . LEU   A 1 122 ? -30.932 -16.254 -3.686  1.00 120.91 ? 142 LEU   A CA  1 
ATOM   916  C  C   . LEU   A 1 122 ? -31.195 -14.776 -3.945  1.00 121.42 ? 142 LEU   A C   1 
ATOM   917  O  O   . LEU   A 1 122 ? -30.255 -13.993 -4.129  1.00 122.75 ? 142 LEU   A O   1 
ATOM   918  C  CB  . LEU   A 1 122 ? -31.105 -17.069 -4.970  1.00 115.52 ? 142 LEU   A CB  1 
ATOM   919  C  CG  . LEU   A 1 122 ? -30.361 -16.600 -6.221  1.00 114.87 ? 142 LEU   A CG  1 
ATOM   920  C  CD1 . LEU   A 1 122 ? -28.894 -16.365 -5.919  1.00 110.42 ? 142 LEU   A CD1 1 
ATOM   921  C  CD2 . LEU   A 1 122 ? -30.515 -17.623 -7.333  1.00 113.00 ? 142 LEU   A CD2 1 
ATOM   922  N  N   . LYS   A 1 123 ? -32.468 -14.377 -3.959  1.00 121.00 ? 143 LYS   A N   1 
ATOM   923  C  CA  . LYS   A 1 123 ? -32.803 -12.970 -4.154  1.00 131.37 ? 143 LYS   A CA  1 
ATOM   924  C  C   . LYS   A 1 123 ? -32.216 -12.110 -3.041  1.00 132.56 ? 143 LYS   A C   1 
ATOM   925  O  O   . LYS   A 1 123 ? -31.704 -11.014 -3.296  1.00 137.74 ? 143 LYS   A O   1 
ATOM   926  C  CB  . LYS   A 1 123 ? -34.321 -12.809 -4.230  1.00 132.76 ? 143 LYS   A CB  1 
ATOM   927  C  CG  . LYS   A 1 123 ? -34.792 -11.530 -4.896  1.00 142.05 ? 143 LYS   A CG  1 
ATOM   928  C  CD  . LYS   A 1 123 ? -36.261 -11.627 -5.272  1.00 150.99 ? 143 LYS   A CD  1 
ATOM   929  C  CE  . LYS   A 1 123 ? -37.114 -11.981 -4.064  1.00 156.33 ? 143 LYS   A CE  1 
ATOM   930  N  NZ  . LYS   A 1 123 ? -38.555 -12.107 -4.415  1.00 161.73 ? 143 LYS   A NZ  1 
ATOM   931  N  N   . GLU   A 1 124 ? -32.261 -12.605 -1.801  1.00 129.64 ? 144 GLU   A N   1 
ATOM   932  C  CA  . GLU   A 1 124 ? -31.677 -11.881 -0.679  1.00 126.30 ? 144 GLU   A CA  1 
ATOM   933  C  C   . GLU   A 1 124 ? -30.159 -11.793 -0.771  1.00 126.45 ? 144 GLU   A C   1 
ATOM   934  O  O   . GLU   A 1 124 ? -29.560 -10.943 -0.104  1.00 123.59 ? 144 GLU   A O   1 
ATOM   935  C  CB  . GLU   A 1 124 ? -32.083 -12.544 0.639   1.00 126.17 ? 144 GLU   A CB  1 
ATOM   936  C  CG  . GLU   A 1 124 ? -33.587 -12.613 0.859   1.00 131.85 ? 144 GLU   A CG  1 
ATOM   937  C  CD  . GLU   A 1 124 ? -33.955 -13.053 2.261   1.00 141.85 ? 144 GLU   A CD  1 
ATOM   938  O  OE1 . GLU   A 1 124 ? -33.858 -14.263 2.556   1.00 132.52 ? 144 GLU   A OE1 1 
ATOM   939  O  OE2 . GLU   A 1 124 ? -34.337 -12.182 3.071   1.00 135.50 ? 144 GLU   A OE2 1 
ATOM   940  N  N   . MET   A 1 125 ? -29.525 -12.647 -1.576  1.00 126.31 ? 145 MET   A N   1 
ATOM   941  C  CA  . MET   A 1 125 ? -28.079 -12.611 -1.752  1.00 127.45 ? 145 MET   A CA  1 
ATOM   942  C  C   . MET   A 1 125 ? -27.632 -11.651 -2.844  1.00 133.15 ? 145 MET   A C   1 
ATOM   943  O  O   . MET   A 1 125 ? -26.444 -11.312 -2.900  1.00 138.80 ? 145 MET   A O   1 
ATOM   944  C  CB  . MET   A 1 125 ? -27.548 -14.011 -2.077  1.00 117.34 ? 145 MET   A CB  1 
ATOM   945  C  CG  . MET   A 1 125 ? -27.789 -15.033 -0.986  1.00 112.10 ? 145 MET   A CG  1 
ATOM   946  S  SD  . MET   A 1 125 ? -26.885 -16.566 -1.255  1.00 116.10 ? 145 MET   A SD  1 
ATOM   947  C  CE  . MET   A 1 125 ? -27.251 -17.416 0.276   1.00 122.05 ? 145 MET   A CE  1 
ATOM   948  N  N   . VAL   A 1 126 ? -28.552 -11.204 -3.702  1.00 131.21 ? 146 VAL   A N   1 
ATOM   949  C  CA  . VAL   A 1 126 ? -28.165 -10.394 -4.861  1.00 137.39 ? 146 VAL   A CA  1 
ATOM   950  C  C   . VAL   A 1 126 ? -27.479 -9.089  -4.465  1.00 146.35 ? 146 VAL   A C   1 
ATOM   951  O  O   . VAL   A 1 126 ? -26.415 -8.782  -5.030  1.00 145.84 ? 146 VAL   A O   1 
ATOM   952  C  CB  . VAL   A 1 126 ? -29.376 -10.169 -5.776  1.00 141.00 ? 146 VAL   A CB  1 
ATOM   953  C  CG1 . VAL   A 1 126 ? -29.016 -9.241  -6.929  1.00 136.19 ? 146 VAL   A CG1 1 
ATOM   954  C  CG2 . VAL   A 1 126 ? -29.900 -11.498 -6.302  1.00 134.11 ? 146 VAL   A CG2 1 
ATOM   955  N  N   . PRO   A 1 127 ? -28.014 -8.276  -3.542  1.00 148.14 ? 147 PRO   A N   1 
ATOM   956  C  CA  . PRO   A 1 127 ? -27.350 -6.992  -3.246  1.00 146.65 ? 147 PRO   A CA  1 
ATOM   957  C  C   . PRO   A 1 127 ? -25.923 -7.137  -2.744  1.00 149.63 ? 147 PRO   A C   1 
ATOM   958  O  O   . PRO   A 1 127 ? -25.085 -6.275  -3.040  1.00 153.89 ? 147 PRO   A O   1 
ATOM   959  C  CB  . PRO   A 1 127 ? -28.261 -6.363  -2.183  1.00 144.12 ? 147 PRO   A CB  1 
ATOM   960  C  CG  . PRO   A 1 127 ? -29.587 -6.988  -2.411  1.00 138.27 ? 147 PRO   A CG  1 
ATOM   961  C  CD  . PRO   A 1 127 ? -29.285 -8.400  -2.803  1.00 140.34 ? 147 PRO   A CD  1 
ATOM   962  N  N   . ILE   A 1 128 ? -25.617 -8.194  -1.990  1.00 145.07 ? 148 ILE   A N   1 
ATOM   963  C  CA  . ILE   A 1 128 ? -24.234 -8.429  -1.584  1.00 148.22 ? 148 ILE   A CA  1 
ATOM   964  C  C   . ILE   A 1 128 ? -23.397 -8.839  -2.790  1.00 152.38 ? 148 ILE   A C   1 
ATOM   965  O  O   . ILE   A 1 128 ? -22.236 -8.435  -2.925  1.00 153.22 ? 148 ILE   A O   1 
ATOM   966  C  CB  . ILE   A 1 128 ? -24.170 -9.473  -0.452  1.00 151.91 ? 148 ILE   A CB  1 
ATOM   967  C  CG1 . ILE   A 1 128 ? -24.767 -8.909  0.844   1.00 153.24 ? 148 ILE   A CG1 1 
ATOM   968  C  CG2 . ILE   A 1 128 ? -22.735 -9.917  -0.204  1.00 148.41 ? 148 ILE   A CG2 1 
ATOM   969  C  CD1 . ILE   A 1 128 ? -26.271 -9.075  0.976   1.00 146.76 ? 148 ILE   A CD1 1 
ATOM   970  N  N   . ILE   A 1 129 ? -23.978 -9.632  -3.694  1.00 146.87 ? 149 ILE   A N   1 
ATOM   971  C  CA  . ILE   A 1 129 ? -23.321 -9.915  -4.966  1.00 146.51 ? 149 ILE   A CA  1 
ATOM   972  C  C   . ILE   A 1 129 ? -23.207 -8.646  -5.803  1.00 148.47 ? 149 ILE   A C   1 
ATOM   973  O  O   . ILE   A 1 129 ? -22.252 -8.483  -6.573  1.00 147.25 ? 149 ILE   A O   1 
ATOM   974  C  CB  . ILE   A 1 129 ? -24.081 -11.026 -5.718  1.00 139.39 ? 149 ILE   A CB  1 
ATOM   975  C  CG1 . ILE   A 1 129 ? -24.086 -12.322 -4.904  1.00 141.17 ? 149 ILE   A CG1 1 
ATOM   976  C  CG2 . ILE   A 1 129 ? -23.476 -11.268 -7.095  1.00 130.87 ? 149 ILE   A CG2 1 
ATOM   977  C  CD1 . ILE   A 1 129 ? -24.798 -13.467 -5.591  1.00 130.61 ? 149 ILE   A CD1 1 
ATOM   978  N  N   . ALA   A 1 130 ? -24.160 -7.721  -5.657  1.00 148.02 ? 150 ALA   A N   1 
ATOM   979  C  CA  . ALA   A 1 130 ? -24.156 -6.510  -6.474  1.00 147.36 ? 150 ALA   A CA  1 
ATOM   980  C  C   . ALA   A 1 130 ? -22.982 -5.602  -6.129  1.00 152.89 ? 150 ALA   A C   1 
ATOM   981  O  O   . ALA   A 1 130 ? -22.424 -4.939  -7.011  1.00 158.77 ? 150 ALA   A O   1 
ATOM   982  C  CB  . ALA   A 1 130 ? -25.477 -5.761  -6.303  1.00 148.27 ? 150 ALA   A CB  1 
ATOM   983  N  N   . GLN   A 1 131 ? -22.592 -5.560  -4.853  1.00 150.51 ? 151 GLN   A N   1 
ATOM   984  C  CA  . GLN   A 1 131 ? -21.561 -4.623  -4.416  1.00 156.18 ? 151 GLN   A CA  1 
ATOM   985  C  C   . GLN   A 1 131 ? -20.201 -4.952  -5.022  1.00 154.74 ? 151 GLN   A C   1 
ATOM   986  O  O   . GLN   A 1 131 ? -19.464 -4.047  -5.431  1.00 151.48 ? 151 GLN   A O   1 
ATOM   987  C  CB  . GLN   A 1 131 ? -21.485 -4.619  -2.890  1.00 156.14 ? 151 GLN   A CB  1 
ATOM   988  C  CG  . GLN   A 1 131 ? -20.158 -4.148  -2.325  1.00 156.67 ? 151 GLN   A CG  1 
ATOM   989  C  CD  . GLN   A 1 131 ? -19.800 -4.868  -1.042  1.00 160.01 ? 151 GLN   A CD  1 
ATOM   990  O  OE1 . GLN   A 1 131 ? -20.572 -5.689  -0.545  1.00 157.39 ? 151 GLN   A OE1 1 
ATOM   991  N  NE2 . GLN   A 1 131 ? -18.624 -4.573  -0.503  1.00 156.32 ? 151 GLN   A NE2 1 
ATOM   992  N  N   . TYR   A 1 132 ? -19.848 -6.236  -5.089  1.00 158.24 ? 152 TYR   A N   1 
ATOM   993  C  CA  . TYR   A 1 132 ? -18.524 -6.625  -5.558  1.00 154.46 ? 152 TYR   A CA  1 
ATOM   994  C  C   . TYR   A 1 132 ? -18.366 -6.521  -7.068  1.00 154.37 ? 152 TYR   A C   1 
ATOM   995  O  O   . TYR   A 1 132 ? -17.244 -6.673  -7.565  1.00 154.25 ? 152 TYR   A O   1 
ATOM   996  C  CB  . TYR   A 1 132 ? -18.202 -8.045  -5.097  1.00 152.26 ? 152 TYR   A CB  1 
ATOM   997  C  CG  . TYR   A 1 132 ? -18.100 -8.152  -3.599  1.00 157.35 ? 152 TYR   A CG  1 
ATOM   998  C  CD1 . TYR   A 1 132 ? -16.915 -7.854  -2.942  1.00 160.19 ? 152 TYR   A CD1 1 
ATOM   999  C  CD2 . TYR   A 1 132 ? -19.195 -8.528  -2.840  1.00 154.92 ? 152 TYR   A CD2 1 
ATOM   1000 C  CE1 . TYR   A 1 132 ? -16.821 -7.945  -1.573  1.00 159.67 ? 152 TYR   A CE1 1 
ATOM   1001 C  CE2 . TYR   A 1 132 ? -19.113 -8.617  -1.474  1.00 158.05 ? 152 TYR   A CE2 1 
ATOM   1002 C  CZ  . TYR   A 1 132 ? -17.925 -8.328  -0.846  1.00 158.49 ? 152 TYR   A CZ  1 
ATOM   1003 O  OH  . TYR   A 1 132 ? -17.849 -8.422  0.517   1.00 159.94 ? 152 TYR   A OH  1 
ATOM   1004 N  N   . GLY   A 1 133 ? -19.450 -6.276  -7.805  1.00 152.15 ? 153 GLY   A N   1 
ATOM   1005 C  CA  . GLY   A 1 133 ? -19.305 -5.927  -9.208  1.00 144.73 ? 153 GLY   A CA  1 
ATOM   1006 C  C   . GLY   A 1 133 ? -18.681 -4.557  -9.386  1.00 146.82 ? 153 GLY   A C   1 
ATOM   1007 O  O   . GLY   A 1 133 ? -17.856 -4.351  -10.280 1.00 145.79 ? 153 GLY   A O   1 
ATOM   1008 N  N   . ASP   A 1 134 ? -19.067 -3.602  -8.533  1.00 146.68 ? 154 ASP   A N   1 
ATOM   1009 C  CA  . ASP   A 1 134 ? -18.423 -2.293  -8.533  1.00 150.31 ? 154 ASP   A CA  1 
ATOM   1010 C  C   . ASP   A 1 134 ? -16.927 -2.427  -8.284  1.00 155.24 ? 154 ASP   A C   1 
ATOM   1011 O  O   . ASP   A 1 134 ? -16.117 -1.743  -8.924  1.00 158.57 ? 154 ASP   A O   1 
ATOM   1012 C  CB  . ASP   A 1 134 ? -19.063 -1.395  -7.476  1.00 158.93 ? 154 ASP   A CB  1 
ATOM   1013 C  CG  . ASP   A 1 134 ? -20.574 -1.510  -7.449  1.00 165.59 ? 154 ASP   A CG  1 
ATOM   1014 O  OD1 . ASP   A 1 134 ? -21.167 -1.811  -8.507  1.00 167.65 ? 154 ASP   A OD1 1 
ATOM   1015 O  OD2 . ASP   A 1 134 ? -21.166 -1.299  -6.370  1.00 169.42 ? 154 ASP   A OD2 1 
ATOM   1016 N  N   . VAL   A 1 135 ? -16.544 -3.305  -7.353  1.00 148.38 ? 155 VAL   A N   1 
ATOM   1017 C  CA  . VAL   A 1 135 ? -15.135 -3.639  -7.165  1.00 149.21 ? 155 VAL   A CA  1 
ATOM   1018 C  C   . VAL   A 1 135 ? -14.549 -4.176  -8.463  1.00 147.32 ? 155 VAL   A C   1 
ATOM   1019 O  O   . VAL   A 1 135 ? -13.496 -3.722  -8.927  1.00 145.23 ? 155 VAL   A O   1 
ATOM   1020 C  CB  . VAL   A 1 135 ? -14.975 -4.651  -6.017  1.00 157.40 ? 155 VAL   A CB  1 
ATOM   1021 C  CG1 . VAL   A 1 135 ? -13.514 -5.035  -5.840  1.00 153.56 ? 155 VAL   A CG1 1 
ATOM   1022 C  CG2 . VAL   A 1 135 ? -15.547 -4.091  -4.724  1.00 157.43 ? 155 VAL   A CG2 1 
ATOM   1023 N  N   . LEU   A 1 136 ? -15.235 -5.147  -9.071  1.00 145.38 ? 156 LEU   A N   1 
ATOM   1024 C  CA  . LEU   A 1 136 ? -14.782 -5.715  -10.336 1.00 139.45 ? 156 LEU   A CA  1 
ATOM   1025 C  C   . LEU   A 1 136 ? -14.670 -4.647  -11.416 1.00 139.98 ? 156 LEU   A C   1 
ATOM   1026 O  O   . LEU   A 1 136 ? -13.733 -4.665  -12.222 1.00 140.22 ? 156 LEU   A O   1 
ATOM   1027 C  CB  . LEU   A 1 136 ? -15.739 -6.823  -10.777 1.00 128.24 ? 156 LEU   A CB  1 
ATOM   1028 C  CG  . LEU   A 1 136 ? -15.496 -7.443  -12.151 1.00 123.37 ? 156 LEU   A CG  1 
ATOM   1029 C  CD1 . LEU   A 1 136 ? -14.176 -8.176  -12.153 1.00 120.30 ? 156 LEU   A CD1 1 
ATOM   1030 C  CD2 . LEU   A 1 136 ? -16.631 -8.381  -12.526 1.00 124.91 ? 156 LEU   A CD2 1 
ATOM   1031 N  N   . VAL   A 1 137 ? -15.617 -3.707  -11.446 1.00 143.60 ? 157 VAL   A N   1 
ATOM   1032 C  CA  . VAL   A 1 137 ? -15.586 -2.642  -12.446 1.00 143.88 ? 157 VAL   A CA  1 
ATOM   1033 C  C   . VAL   A 1 137 ? -14.384 -1.733  -12.222 1.00 146.79 ? 157 VAL   A C   1 
ATOM   1034 O  O   . VAL   A 1 137 ? -13.614 -1.456  -13.150 1.00 149.56 ? 157 VAL   A O   1 
ATOM   1035 C  CB  . VAL   A 1 137 ? -16.907 -1.851  -12.425 1.00 145.93 ? 157 VAL   A CB  1 
ATOM   1036 C  CG1 . VAL   A 1 137 ? -16.698 -0.444  -12.964 1.00 140.86 ? 157 VAL   A CG1 1 
ATOM   1037 C  CG2 . VAL   A 1 137 ? -17.970 -2.577  -13.236 1.00 144.50 ? 157 VAL   A CG2 1 
ATOM   1038 N  N   . ARG   A 1 138 ? -14.199 -1.258  -10.987 1.00 142.97 ? 158 ARG   A N   1 
ATOM   1039 C  CA  . ARG   A 1 138 ? -13.116 -0.318  -10.718 1.00 148.46 ? 158 ARG   A CA  1 
ATOM   1040 C  C   . ARG   A 1 138 ? -11.753 -0.980  -10.873 1.00 155.39 ? 158 ARG   A C   1 
ATOM   1041 O  O   . ARG   A 1 138 ? -10.815 -0.362  -11.389 1.00 164.92 ? 158 ARG   A O   1 
ATOM   1042 C  CB  . ARG   A 1 138 ? -13.272 0.281   -9.322  1.00 151.66 ? 158 ARG   A CB  1 
ATOM   1043 C  CG  . ARG   A 1 138 ? -14.482 1.186   -9.179  1.00 159.06 ? 158 ARG   A CG  1 
ATOM   1044 C  CD  . ARG   A 1 138 ? -14.492 1.875   -7.828  1.00 157.92 ? 158 ARG   A CD  1 
ATOM   1045 N  NE  . ARG   A 1 138 ? -14.438 0.912   -6.736  1.00 148.64 ? 158 ARG   A NE  1 
ATOM   1046 C  CZ  . ARG   A 1 138 ? -15.504 0.347   -6.187  1.00 150.73 ? 158 ARG   A CZ  1 
ATOM   1047 N  NH1 . ARG   A 1 138 ? -16.727 0.633   -6.601  1.00 154.85 ? 158 ARG   A NH1 1 
ATOM   1048 N  NH2 . ARG   A 1 138 ? -15.338 -0.526  -5.198  1.00 151.48 ? 158 ARG   A NH2 1 
ATOM   1049 N  N   . ASN   A 1 139 ? -11.620 -2.232  -10.427 1.00 162.57 ? 159 ASN   A N   1 
ATOM   1050 C  CA  . ASN   A 1 139 ? -10.391 -2.973  -10.691 1.00 165.69 ? 159 ASN   A CA  1 
ATOM   1051 C  C   . ASN   A 1 139 ? -10.167 -3.156  -12.185 1.00 169.82 ? 159 ASN   A C   1 
ATOM   1052 O  O   . ASN   A 1 139 ? -9.019  -3.181  -12.644 1.00 177.53 ? 159 ASN   A O   1 
ATOM   1053 C  CB  . ASN   A 1 139 ? -10.429 -4.331  -9.990  1.00 167.03 ? 159 ASN   A CB  1 
ATOM   1054 C  CG  . ASN   A 1 139 ? -10.324 -4.215  -8.481  1.00 177.10 ? 159 ASN   A CG  1 
ATOM   1055 O  OD1 . ASN   A 1 139 ? -9.752  -3.259  -7.958  1.00 177.72 ? 159 ASN   A OD1 1 
ATOM   1056 N  ND2 . ASN   A 1 139 ? -10.871 -5.196  -7.774  1.00 170.75 ? 159 ASN   A ND2 1 
ATOM   1057 N  N   . LEU   A 1 140 ? -11.248 -3.282  -12.959 1.00 161.38 ? 160 LEU   A N   1 
ATOM   1058 C  CA  . LEU   A 1 140 ? -11.113 -3.353  -14.410 1.00 156.77 ? 160 LEU   A CA  1 
ATOM   1059 C  C   . LEU   A 1 140 ? -10.788 -1.988  -15.002 1.00 166.13 ? 160 LEU   A C   1 
ATOM   1060 O  O   . LEU   A 1 140 ? -10.013 -1.891  -15.961 1.00 171.98 ? 160 LEU   A O   1 
ATOM   1061 C  CB  . LEU   A 1 140 ? -12.391 -3.909  -15.035 1.00 147.01 ? 160 LEU   A CB  1 
ATOM   1062 C  CG  . LEU   A 1 140 ? -12.302 -5.329  -15.590 1.00 134.56 ? 160 LEU   A CG  1 
ATOM   1063 C  CD1 . LEU   A 1 140 ? -13.533 -5.650  -16.414 1.00 130.80 ? 160 LEU   A CD1 1 
ATOM   1064 C  CD2 . LEU   A 1 140 ? -11.040 -5.499  -16.419 1.00 138.21 ? 160 LEU   A CD2 1 
ATOM   1065 N  N   . ARG   A 1 141 ? -11.375 -0.923  -14.451 1.00 164.08 ? 161 ARG   A N   1 
ATOM   1066 C  CA  A ARG   A 1 141 ? -11.105 0.413   -14.970 0.55 167.12 ? 161 ARG   A CA  1 
ATOM   1067 C  CA  B ARG   A 1 141 ? -11.106 0.415   -14.967 0.45 167.12 ? 161 ARG   A CA  1 
ATOM   1068 C  C   . ARG   A 1 141 ? -9.662  0.831   -14.718 1.00 179.99 ? 161 ARG   A C   1 
ATOM   1069 O  O   . ARG   A 1 141 ? -9.104  1.623   -15.487 1.00 186.31 ? 161 ARG   A O   1 
ATOM   1070 C  CB  A ARG   A 1 141 ? -12.079 1.415   -14.352 0.55 159.45 ? 161 ARG   A CB  1 
ATOM   1071 C  CB  B ARG   A 1 141 ? -12.078 1.425   -14.349 0.45 159.48 ? 161 ARG   A CB  1 
ATOM   1072 C  CG  A ARG   A 1 141 ? -12.257 2.702   -15.140 0.55 159.05 ? 161 ARG   A CG  1 
ATOM   1073 C  CG  B ARG   A 1 141 ? -11.789 2.879   -14.710 0.45 160.06 ? 161 ARG   A CG  1 
ATOM   1074 C  CD  A ARG   A 1 141 ? -13.657 3.250   -14.924 0.55 155.44 ? 161 ARG   A CD  1 
ATOM   1075 C  CD  B ARG   A 1 141 ? -13.049 3.731   -14.749 0.45 156.35 ? 161 ARG   A CD  1 
ATOM   1076 N  NE  A ARG   A 1 141 ? -14.088 3.068   -13.543 0.55 152.50 ? 161 ARG   A NE  1 
ATOM   1077 N  NE  B ARG   A 1 141 ? -13.949 3.329   -15.824 0.45 151.24 ? 161 ARG   A NE  1 
ATOM   1078 C  CZ  A ARG   A 1 141 ? -15.341 3.185   -13.125 0.55 150.02 ? 161 ARG   A CZ  1 
ATOM   1079 C  CZ  B ARG   A 1 141 ? -15.122 2.740   -15.638 0.45 150.04 ? 161 ARG   A CZ  1 
ATOM   1080 N  NH1 A ARG   A 1 141 ? -16.323 3.487   -13.959 0.55 147.62 ? 161 ARG   A NH1 1 
ATOM   1081 N  NH1 B ARG   A 1 141 ? -15.588 2.494   -14.424 0.45 149.22 ? 161 ARG   A NH1 1 
ATOM   1082 N  NH2 A ARG   A 1 141 ? -15.616 2.990   -11.839 0.55 149.74 ? 161 ARG   A NH2 1 
ATOM   1083 N  NH2 B ARG   A 1 141 ? -15.849 2.393   -16.697 0.45 151.93 ? 161 ARG   A NH2 1 
ATOM   1084 N  N   . ARG   A 1 142 ? -9.036  0.308   -13.660 1.00 194.05 ? 162 ARG   A N   1 
ATOM   1085 C  CA  . ARG   A 1 142 ? -7.627  0.611   -13.428 1.00 203.12 ? 162 ARG   A CA  1 
ATOM   1086 C  C   . ARG   A 1 142 ? -6.749  -0.019  -14.503 1.00 211.88 ? 162 ARG   A C   1 
ATOM   1087 O  O   . ARG   A 1 142 ? -5.769  0.591   -14.949 1.00 213.55 ? 162 ARG   A O   1 
ATOM   1088 C  CB  . ARG   A 1 142 ? -7.196  0.138   -12.038 1.00 199.38 ? 162 ARG   A CB  1 
ATOM   1089 C  CG  . ARG   A 1 142 ? -5.716  0.370   -11.757 1.00 204.21 ? 162 ARG   A CG  1 
ATOM   1090 C  CD  . ARG   A 1 142 ? -5.325  0.046   -10.322 1.00 207.49 ? 162 ARG   A CD  1 
ATOM   1091 N  NE  . ARG   A 1 142 ? -5.578  -1.346  -9.970  1.00 205.36 ? 162 ARG   A NE  1 
ATOM   1092 C  CZ  . ARG   A 1 142 ? -6.486  -1.742  -9.089  1.00 198.63 ? 162 ARG   A CZ  1 
ATOM   1093 N  NH1 . ARG   A 1 142 ? -7.238  -0.873  -8.433  1.00 200.02 ? 162 ARG   A NH1 1 
ATOM   1094 N  NH2 . ARG   A 1 142 ? -6.639  -3.042  -8.853  1.00 196.15 ? 162 ARG   A NH2 1 
ATOM   1095 N  N   . GLU   A 1 143 ? -7.086  -1.235  -14.937 1.00 193.51 ? 163 GLU   A N   1 
ATOM   1096 C  CA  . GLU   A 1 143 ? -6.354  -1.872  -16.024 1.00 196.66 ? 163 GLU   A CA  1 
ATOM   1097 C  C   . GLU   A 1 143 ? -6.786  -1.371  -17.395 1.00 201.38 ? 163 GLU   A C   1 
ATOM   1098 O  O   . GLU   A 1 143 ? -6.032  -1.526  -18.361 1.00 202.52 ? 163 GLU   A O   1 
ATOM   1099 C  CB  . GLU   A 1 143 ? -6.518  -3.393  -15.959 1.00 201.98 ? 163 GLU   A CB  1 
ATOM   1100 C  CG  . GLU   A 1 143 ? -5.642  -4.083  -14.919 1.00 209.21 ? 163 GLU   A CG  1 
ATOM   1101 C  CD  . GLU   A 1 143 ? -4.194  -4.235  -15.362 1.00 216.51 ? 163 GLU   A CD  1 
ATOM   1102 O  OE1 . GLU   A 1 143 ? -3.798  -3.611  -16.370 1.00 210.03 ? 163 GLU   A OE1 1 
ATOM   1103 O  OE2 . GLU   A 1 143 ? -3.449  -4.989  -14.701 1.00 226.11 ? 163 GLU   A OE2 1 
ATOM   1104 N  N   . ALA   A 1 144 ? -7.977  -0.779  -17.504 1.00 192.97 ? 164 ALA   A N   1 
ATOM   1105 C  CA  . ALA   A 1 144 ? -8.414  -0.226  -18.781 1.00 187.32 ? 164 ALA   A CA  1 
ATOM   1106 C  C   . ALA   A 1 144 ? -7.738  1.108   -19.069 1.00 197.59 ? 164 ALA   A C   1 
ATOM   1107 O  O   . ALA   A 1 144 ? -7.345  1.374   -20.211 1.00 197.26 ? 164 ALA   A O   1 
ATOM   1108 C  CB  . ALA   A 1 144 ? -9.935  -0.070  -18.795 1.00 178.03 ? 164 ALA   A CB  1 
ATOM   1109 N  N   . GLU   A 1 145 ? -7.547  1.920   -18.024 1.00 201.34 ? 165 GLU   A N   1 
ATOM   1110 C  CA  . GLU   A 1 145 ? -6.776  3.174   -18.218 1.00 203.76 ? 165 GLU   A CA  1 
ATOM   1111 C  C   . GLU   A 1 145 ? -5.412  2.778   -18.784 1.00 206.75 ? 165 GLU   A C   1 
ATOM   1112 O  O   . GLU   A 1 145 ? -4.992  3.376   -19.793 1.00 215.28 ? 165 GLU   A O   1 
ATOM   1113 C  CB  . GLU   A 1 145 ? -6.576  3.911   -16.896 1.00 206.97 ? 165 GLU   A CB  1 
ATOM   1114 C  CG  . GLU   A 1 145 ? -7.856  4.459   -16.296 1.00 206.46 ? 165 GLU   A CG  1 
ATOM   1115 C  CD  . GLU   A 1 145 ? -7.658  5.128   -14.946 1.00 203.32 ? 165 GLU   A CD  1 
ATOM   1116 O  OE1 . GLU   A 1 145 ? -6.553  5.002   -14.383 1.00 200.59 ? 165 GLU   A OE1 1 
ATOM   1117 O  OE2 . GLU   A 1 145 ? -8.612  5.764   -14.458 1.00 204.86 ? 165 GLU   A OE2 1 
ATOM   1118 N  N   . THR   A 1 146 ? -4.760  1.795   -18.155 1.00 207.11 ? 166 THR   A N   1 
ATOM   1119 C  CA  . THR   A 1 146 ? -3.444  1.310   -18.644 1.00 209.07 ? 166 THR   A CA  1 
ATOM   1120 C  C   . THR   A 1 146 ? -3.617  0.699   -20.034 1.00 204.88 ? 166 THR   A C   1 
ATOM   1121 O  O   . THR   A 1 146 ? -2.731  0.912   -20.883 1.00 199.78 ? 166 THR   A O   1 
ATOM   1122 C  CB  . THR   A 1 146 ? -2.840  0.277   -17.685 1.00 205.70 ? 166 THR   A CB  1 
ATOM   1123 O  OG1 . THR   A 1 146 ? -3.489  -0.976  -17.908 1.00 199.81 ? 166 THR   A OG1 1 
ATOM   1124 C  CG2 . THR   A 1 146 ? -2.977  0.673   -16.231 1.00 206.64 ? 166 THR   A CG2 1 
ATOM   1125 N  N   . GLY   A 1 147 ? -4.710  -0.038  -20.249 1.00 207.34 ? 167 GLY   A N   1 
ATOM   1126 C  CA  . GLY   A 1 147 ? -4.921  -0.718  -21.542 1.00 204.05 ? 167 GLY   A CA  1 
ATOM   1127 C  C   . GLY   A 1 147 ? -4.136  -2.015  -21.612 1.00 201.43 ? 167 GLY   A C   1 
ATOM   1128 O  O   . GLY   A 1 147 ? -4.554  -2.913  -22.370 1.00 199.12 ? 167 GLY   A O   1 
ATOM   1129 N  N   . LYS   A 1 148 ? -3.038  -2.113  -20.853 1.00 204.23 ? 168 LYS   A N   1 
ATOM   1130 C  CA  . LYS   A 1 148 ? -2.233  -3.362  -20.816 1.00 200.65 ? 168 LYS   A CA  1 
ATOM   1131 C  C   . LYS   A 1 148 ? -3.187  -4.556  -20.887 1.00 192.15 ? 168 LYS   A C   1 
ATOM   1132 O  O   . LYS   A 1 148 ? -4.026  -4.690  -19.974 1.00 195.46 ? 168 LYS   A O   1 
ATOM   1133 C  CB  . LYS   A 1 148 ? -1.392  -3.423  -19.539 1.00 204.38 ? 168 LYS   A CB  1 
ATOM   1134 C  CG  . LYS   A 1 148 ? -0.859  -4.804  -19.184 1.00 202.84 ? 168 LYS   A CG  1 
ATOM   1135 C  CD  . LYS   A 1 148 ? -1.530  -5.412  -17.972 1.00 207.07 ? 168 LYS   A CD  1 
ATOM   1136 C  CE  . LYS   A 1 148 ? -0.843  -5.050  -16.673 1.00 203.77 ? 168 LYS   A CE  1 
ATOM   1137 N  NZ  . LYS   A 1 148 ? 0.575   -4.675  -16.885 1.00 204.74 ? 168 LYS   A NZ  1 
ATOM   1138 N  N   . PRO   A 1 149 ? -3.118  -5.416  -21.927 1.00 177.00 ? 169 PRO   A N   1 
ATOM   1139 C  CA  . PRO   A 1 149 ? -4.081  -6.515  -22.073 1.00 165.13 ? 169 PRO   A CA  1 
ATOM   1140 C  C   . PRO   A 1 149 ? -4.195  -7.338  -20.797 1.00 160.41 ? 169 PRO   A C   1 
ATOM   1141 O  O   . PRO   A 1 149 ? -3.239  -7.476  -20.032 1.00 165.05 ? 169 PRO   A O   1 
ATOM   1142 C  CB  . PRO   A 1 149 ? -3.502  -7.334  -23.230 1.00 156.94 ? 169 PRO   A CB  1 
ATOM   1143 C  CG  . PRO   A 1 149 ? -2.749  -6.324  -24.040 1.00 165.32 ? 169 PRO   A CG  1 
ATOM   1144 C  CD  . PRO   A 1 149 ? -2.160  -5.365  -23.044 1.00 175.95 ? 169 PRO   A CD  1 
ATOM   1145 N  N   . VAL   A 1 150 ? -5.387  -7.885  -20.577 1.00 153.10 ? 170 VAL   A N   1 
ATOM   1146 C  CA  . VAL   A 1 150 ? -5.784  -8.436  -19.287 1.00 152.93 ? 170 VAL   A CA  1 
ATOM   1147 C  C   . VAL   A 1 150 ? -5.908  -9.950  -19.392 1.00 149.17 ? 170 VAL   A C   1 
ATOM   1148 O  O   . VAL   A 1 150 ? -6.542  -10.467 -20.320 1.00 144.39 ? 170 VAL   A O   1 
ATOM   1149 C  CB  . VAL   A 1 150 ? -7.111  -7.818  -18.811 1.00 147.23 ? 170 VAL   A CB  1 
ATOM   1150 C  CG1 . VAL   A 1 150 ? -7.546  -8.430  -17.493 1.00 136.72 ? 170 VAL   A CG1 1 
ATOM   1151 C  CG2 . VAL   A 1 150 ? -6.980  -6.308  -18.691 1.00 158.15 ? 170 VAL   A CG2 1 
ATOM   1152 N  N   . THR   A 1 151 ? -5.315  -10.655 -18.431 1.00 153.66 ? 171 THR   A N   1 
ATOM   1153 C  CA  . THR   A 1 151 ? -5.577  -12.077 -18.247 1.00 153.77 ? 171 THR   A CA  1 
ATOM   1154 C  C   . THR   A 1 151 ? -6.861  -12.223 -17.440 1.00 147.35 ? 171 THR   A C   1 
ATOM   1155 O  O   . THR   A 1 151 ? -6.973  -11.670 -16.340 1.00 145.62 ? 171 THR   A O   1 
ATOM   1156 C  CB  . THR   A 1 151 ? -4.410  -12.756 -17.534 1.00 164.39 ? 171 THR   A CB  1 
ATOM   1157 O  OG1 . THR   A 1 151 ? -4.437  -12.415 -16.142 1.00 171.43 ? 171 THR   A OG1 1 
ATOM   1158 C  CG2 . THR   A 1 151 ? -3.087  -12.301 -18.128 1.00 169.08 ? 171 THR   A CG2 1 
ATOM   1159 N  N   . LEU   A 1 152 ? -7.827  -12.966 -17.979 1.00 146.89 ? 172 LEU   A N   1 
ATOM   1160 C  CA  . LEU   A 1 152 ? -9.182  -12.921 -17.438 1.00 143.96 ? 172 LEU   A CA  1 
ATOM   1161 C  C   . LEU   A 1 152 ? -9.331  -13.720 -16.149 1.00 148.31 ? 172 LEU   A C   1 
ATOM   1162 O  O   . LEU   A 1 152 ? -10.095 -13.321 -15.264 1.00 143.73 ? 172 LEU   A O   1 
ATOM   1163 C  CB  . LEU   A 1 152 ? -10.175 -13.415 -18.486 1.00 133.90 ? 172 LEU   A CB  1 
ATOM   1164 C  CG  . LEU   A 1 152 ? -10.405 -12.414 -19.614 1.00 126.61 ? 172 LEU   A CG  1 
ATOM   1165 C  CD1 . LEU   A 1 152 ? -11.311 -13.019 -20.654 1.00 115.33 ? 172 LEU   A CD1 1 
ATOM   1166 C  CD2 . LEU   A 1 152 ? -10.995 -11.124 -19.067 1.00 122.48 ? 172 LEU   A CD2 1 
ATOM   1167 N  N   . LYS   A 1 153 ? -8.624  -14.846 -16.019 1.00 150.28 ? 173 LYS   A N   1 
ATOM   1168 C  CA  . LYS   A 1 153 ? -8.815  -15.695 -14.846 1.00 156.21 ? 173 LYS   A CA  1 
ATOM   1169 C  C   . LYS   A 1 153 ? -8.407  -14.989 -13.558 1.00 158.16 ? 173 LYS   A C   1 
ATOM   1170 O  O   . LYS   A 1 153 ? -8.921  -15.318 -12.483 1.00 153.41 ? 173 LYS   A O   1 
ATOM   1171 C  CB  . LYS   A 1 153 ? -8.040  -17.003 -15.007 1.00 160.77 ? 173 LYS   A CB  1 
ATOM   1172 C  CG  . LYS   A 1 153 ? -6.535  -16.834 -15.097 1.00 157.74 ? 173 LYS   A CG  1 
ATOM   1173 C  CD  . LYS   A 1 153 ? -5.845  -18.182 -15.208 1.00 152.32 ? 173 LYS   A CD  1 
ATOM   1174 C  CE  . LYS   A 1 153 ? -4.335  -18.030 -15.263 1.00 158.91 ? 173 LYS   A CE  1 
ATOM   1175 N  NZ  . LYS   A 1 153 ? -3.655  -19.349 -15.378 1.00 162.22 ? 173 LYS   A NZ  1 
ATOM   1176 N  N   . ASP   A 1 154 ? -7.495  -14.019 -13.640 1.00 150.59 ? 174 ASP   A N   1 
ATOM   1177 C  CA  . ASP   A 1 154 ? -7.100  -13.246 -12.468 1.00 145.00 ? 174 ASP   A CA  1 
ATOM   1178 C  C   . ASP   A 1 154 ? -8.228  -12.327 -12.020 1.00 140.31 ? 174 ASP   A C   1 
ATOM   1179 O  O   . ASP   A 1 154 ? -8.786  -12.497 -10.931 1.00 136.08 ? 174 ASP   A O   1 
ATOM   1180 C  CB  . ASP   A 1 154 ? -5.847  -12.417 -12.760 1.00 147.17 ? 174 ASP   A CB  1 
ATOM   1181 C  CG  . ASP   A 1 154 ? -4.636  -13.273 -13.051 1.00 153.30 ? 174 ASP   A CG  1 
ATOM   1182 O  OD1 . ASP   A 1 154 ? -4.618  -14.445 -12.620 1.00 154.76 ? 174 ASP   A OD1 1 
ATOM   1183 O  OD2 . ASP   A 1 154 ? -3.698  -12.771 -13.706 1.00 154.79 ? 174 ASP   A OD2 1 
ATOM   1184 N  N   . VAL   A 1 155 ? -8.559  -11.348 -12.867 1.00 144.72 ? 175 VAL   A N   1 
ATOM   1185 C  CA  . VAL   A 1 155 ? -9.584  -10.359 -12.540 1.00 143.23 ? 175 VAL   A CA  1 
ATOM   1186 C  C   . VAL   A 1 155 ? -10.905 -11.037 -12.195 1.00 138.65 ? 175 VAL   A C   1 
ATOM   1187 O  O   . VAL   A 1 155 ? -11.604 -10.633 -11.257 1.00 134.48 ? 175 VAL   A O   1 
ATOM   1188 C  CB  . VAL   A 1 155 ? -9.732  -9.360  -13.705 1.00 129.88 ? 175 VAL   A CB  1 
ATOM   1189 C  CG1 . VAL   A 1 155 ? -9.651  -10.086 -15.038 1.00 134.47 ? 175 VAL   A CG1 1 
ATOM   1190 C  CG2 . VAL   A 1 155 ? -11.030 -8.589  -13.602 1.00 128.40 ? 175 VAL   A CG2 1 
ATOM   1191 N  N   . PHE   A 1 156 ? -11.260 -12.093 -12.933 1.00 141.21 ? 176 PHE   A N   1 
ATOM   1192 C  CA  . PHE   A 1 156 ? -12.490 -12.823 -12.637 1.00 142.73 ? 176 PHE   A CA  1 
ATOM   1193 C  C   . PHE   A 1 156 ? -12.344 -13.663 -11.375 1.00 149.14 ? 176 PHE   A C   1 
ATOM   1194 O  O   . PHE   A 1 156 ? -13.222 -13.647 -10.503 1.00 145.21 ? 176 PHE   A O   1 
ATOM   1195 C  CB  . PHE   A 1 156 ? -12.881 -13.704 -13.821 1.00 137.76 ? 176 PHE   A CB  1 
ATOM   1196 C  CG  . PHE   A 1 156 ? -13.630 -12.977 -14.891 1.00 135.90 ? 176 PHE   A CG  1 
ATOM   1197 C  CD1 . PHE   A 1 156 ? -14.300 -11.800 -14.606 1.00 133.32 ? 176 PHE   A CD1 1 
ATOM   1198 C  CD2 . PHE   A 1 156 ? -13.669 -13.471 -16.182 1.00 134.54 ? 176 PHE   A CD2 1 
ATOM   1199 C  CE1 . PHE   A 1 156 ? -14.993 -11.127 -15.587 1.00 127.08 ? 176 PHE   A CE1 1 
ATOM   1200 C  CE2 . PHE   A 1 156 ? -14.360 -12.803 -17.166 1.00 130.08 ? 176 PHE   A CE2 1 
ATOM   1201 C  CZ  . PHE   A 1 156 ? -15.024 -11.628 -16.870 1.00 124.28 ? 176 PHE   A CZ  1 
ATOM   1202 N  N   . GLY   A 1 157 ? -11.247 -14.417 -11.268 1.00 139.07 ? 177 GLY   A N   1 
ATOM   1203 C  CA  . GLY   A 1 157 ? -11.018 -15.217 -10.076 1.00 135.88 ? 177 GLY   A CA  1 
ATOM   1204 C  C   . GLY   A 1 157 ? -11.020 -14.396 -8.804  1.00 133.71 ? 177 GLY   A C   1 
ATOM   1205 O  O   . GLY   A 1 157 ? -11.462 -14.871 -7.755  1.00 133.68 ? 177 GLY   A O   1 
ATOM   1206 N  N   . ALA   A 1 158 ? -10.535 -13.155 -8.878  1.00 134.74 ? 178 ALA   A N   1 
ATOM   1207 C  CA  . ALA   A 1 158 ? -10.627 -12.254 -7.735  1.00 139.36 ? 178 ALA   A CA  1 
ATOM   1208 C  C   . ALA   A 1 158 ? -12.081 -11.942 -7.407  1.00 132.06 ? 178 ALA   A C   1 
ATOM   1209 O  O   . ALA   A 1 158 ? -12.493 -12.005 -6.243  1.00 136.85 ? 178 ALA   A O   1 
ATOM   1210 C  CB  . ALA   A 1 158 ? -9.849  -10.971 -8.015  1.00 155.01 ? 178 ALA   A CB  1 
ATOM   1211 N  N   . TYR   A 1 159 ? -12.874 -11.598 -8.426  1.00 136.13 ? 179 TYR   A N   1 
ATOM   1212 C  CA  . TYR   A 1 159 ? -14.297 -11.352 -8.207  1.00 128.74 ? 179 TYR   A CA  1 
ATOM   1213 C  C   . TYR   A 1 159 ? -14.992 -12.599 -7.678  1.00 129.48 ? 179 TYR   A C   1 
ATOM   1214 O  O   . TYR   A 1 159 ? -15.783 -12.528 -6.730  1.00 126.61 ? 179 TYR   A O   1 
ATOM   1215 C  CB  . TYR   A 1 159 ? -14.968 -10.885 -9.499  1.00 122.07 ? 179 TYR   A CB  1 
ATOM   1216 C  CG  . TYR   A 1 159 ? -16.476 -11.005 -9.445  1.00 121.89 ? 179 TYR   A CG  1 
ATOM   1217 C  CD1 . TYR   A 1 159 ? -17.241 -10.056 -8.781  1.00 121.11 ? 179 TYR   A CD1 1 
ATOM   1218 C  CD2 . TYR   A 1 159 ? -17.133 -12.077 -10.040 1.00 118.61 ? 179 TYR   A CD2 1 
ATOM   1219 C  CE1 . TYR   A 1 159 ? -18.618 -10.164 -8.717  1.00 120.24 ? 179 TYR   A CE1 1 
ATOM   1220 C  CE2 . TYR   A 1 159 ? -18.510 -12.194 -9.979  1.00 110.39 ? 179 TYR   A CE2 1 
ATOM   1221 C  CZ  . TYR   A 1 159 ? -19.247 -11.234 -9.319  1.00 108.48 ? 179 TYR   A CZ  1 
ATOM   1222 O  OH  . TYR   A 1 159 ? -20.617 -11.345 -9.257  1.00 111.33 ? 179 TYR   A OH  1 
ATOM   1223 N  N   . SER   A 1 160 ? -14.725 -13.751 -8.301  1.00 123.93 ? 180 SER   A N   1 
ATOM   1224 C  CA  . SER   A 1 160 ? -15.311 -15.005 -7.839  1.00 122.17 ? 180 SER   A CA  1 
ATOM   1225 C  C   . SER   A 1 160 ? -15.022 -15.237 -6.362  1.00 123.97 ? 180 SER   A C   1 
ATOM   1226 O  O   . SER   A 1 160 ? -15.896 -15.686 -5.612  1.00 119.65 ? 180 SER   A O   1 
ATOM   1227 C  CB  . SER   A 1 160 ? -14.783 -16.171 -8.676  1.00 118.70 ? 180 SER   A CB  1 
ATOM   1228 O  OG  . SER   A 1 160 ? -15.207 -17.412 -8.142  1.00 117.84 ? 180 SER   A OG  1 
ATOM   1229 N  N   . MET   A 1 161 ? -13.801 -14.921 -5.925  1.00 127.60 ? 181 MET   A N   1 
ATOM   1230 C  CA  . MET   A 1 161 ? -13.469 -15.030 -4.509  1.00 129.27 ? 181 MET   A CA  1 
ATOM   1231 C  C   . MET   A 1 161 ? -14.268 -14.035 -3.676  1.00 132.26 ? 181 MET   A C   1 
ATOM   1232 O  O   . MET   A 1 161 ? -14.726 -14.366 -2.576  1.00 132.16 ? 181 MET   A O   1 
ATOM   1233 C  CB  . MET   A 1 161 ? -11.969 -14.816 -4.306  1.00 132.52 ? 181 MET   A CB  1 
ATOM   1234 C  CG  . MET   A 1 161 ? -11.519 -14.924 -2.860  1.00 129.93 ? 181 MET   A CG  1 
ATOM   1235 S  SD  . MET   A 1 161 ? -11.892 -16.538 -2.149  1.00 143.89 ? 181 MET   A SD  1 
ATOM   1236 C  CE  . MET   A 1 161 ? -10.922 -17.605 -3.209  1.00 138.77 ? 181 MET   A CE  1 
ATOM   1237 N  N   . ASP   A 1 162 ? -14.445 -12.812 -4.186  1.00 142.18 ? 182 ASP   A N   1 
ATOM   1238 C  CA  . ASP   A 1 162 ? -15.188 -11.794 -3.450  1.00 146.49 ? 182 ASP   A CA  1 
ATOM   1239 C  C   . ASP   A 1 162 ? -16.611 -12.249 -3.157  1.00 141.84 ? 182 ASP   A C   1 
ATOM   1240 O  O   . ASP   A 1 162 ? -17.119 -12.049 -2.047  1.00 141.64 ? 182 ASP   A O   1 
ATOM   1241 C  CB  . ASP   A 1 162 ? -15.202 -10.483 -4.235  1.00 152.28 ? 182 ASP   A CB  1 
ATOM   1242 C  CG  . ASP   A 1 162 ? -13.845 -9.813  -4.280  1.00 157.35 ? 182 ASP   A CG  1 
ATOM   1243 O  OD1 . ASP   A 1 162 ? -13.005 -10.109 -3.405  1.00 159.65 ? 182 ASP   A OD1 1 
ATOM   1244 O  OD2 . ASP   A 1 162 ? -13.621 -8.983  -5.186  1.00 160.04 ? 182 ASP   A OD2 1 
ATOM   1245 N  N   . VAL   A 1 163 ? -17.271 -12.860 -4.142  1.00 132.85 ? 183 VAL   A N   1 
ATOM   1246 C  CA  . VAL   A 1 163 ? -18.618 -13.381 -3.928  1.00 125.57 ? 183 VAL   A CA  1 
ATOM   1247 C  C   . VAL   A 1 163 ? -18.591 -14.505 -2.899  1.00 125.11 ? 183 VAL   A C   1 
ATOM   1248 O  O   . VAL   A 1 163 ? -19.411 -14.541 -1.973  1.00 130.90 ? 183 VAL   A O   1 
ATOM   1249 C  CB  . VAL   A 1 163 ? -19.228 -13.855 -5.259  1.00 120.82 ? 183 VAL   A CB  1 
ATOM   1250 C  CG1 . VAL   A 1 163 ? -20.666 -14.314 -5.054  1.00 112.74 ? 183 VAL   A CG1 1 
ATOM   1251 C  CG2 . VAL   A 1 163 ? -19.162 -12.744 -6.289  1.00 122.08 ? 183 VAL   A CG2 1 
ATOM   1252 N  N   . ILE   A 1 164 ? -17.638 -15.434 -3.046  1.00 119.09 ? 184 ILE   A N   1 
ATOM   1253 C  CA  . ILE   A 1 164 ? -17.577 -16.615 -2.183  1.00 121.65 ? 184 ILE   A CA  1 
ATOM   1254 C  C   . ILE   A 1 164 ? -17.494 -16.206 -0.720  1.00 127.31 ? 184 ILE   A C   1 
ATOM   1255 O  O   . ILE   A 1 164 ? -18.405 -16.474 0.072   1.00 127.95 ? 184 ILE   A O   1 
ATOM   1256 C  CB  . ILE   A 1 164 ? -16.389 -17.509 -2.570  1.00 113.80 ? 184 ILE   A CB  1 
ATOM   1257 C  CG1 . ILE   A 1 164 ? -16.657 -18.200 -3.902  1.00 116.45 ? 184 ILE   A CG1 1 
ATOM   1258 C  CG2 . ILE   A 1 164 ? -16.132 -18.543 -1.487  1.00 116.52 ? 184 ILE   A CG2 1 
ATOM   1259 C  CD1 . ILE   A 1 164 ? -15.513 -19.055 -4.326  1.00 115.32 ? 184 ILE   A CD1 1 
ATOM   1260 N  N   . THR   A 1 165 ? -16.402 -15.530 -0.345  1.00 124.77 ? 185 THR   A N   1 
ATOM   1261 C  CA  . THR   A 1 165 ? -16.187 -15.175 1.055   1.00 124.06 ? 185 THR   A CA  1 
ATOM   1262 C  C   . THR   A 1 165 ? -17.329 -14.334 1.608   1.00 129.94 ? 185 THR   A C   1 
ATOM   1263 O  O   . THR   A 1 165 ? -17.669 -14.448 2.792   1.00 133.98 ? 185 THR   A O   1 
ATOM   1264 C  CB  . THR   A 1 165 ? -14.862 -14.431 1.209   1.00 131.64 ? 185 THR   A CB  1 
ATOM   1265 O  OG1 . THR   A 1 165 ? -14.914 -13.205 0.470   1.00 144.21 ? 185 THR   A OG1 1 
ATOM   1266 C  CG2 . THR   A 1 165 ? -13.715 -15.282 0.681   1.00 115.15 ? 185 THR   A CG2 1 
ATOM   1267 N  N   . SER   A 1 166 ? -17.943 -13.501 0.768   1.00 131.62 ? 186 SER   A N   1 
ATOM   1268 C  CA  . SER   A 1 166 ? -19.087 -12.714 1.214   1.00 136.64 ? 186 SER   A CA  1 
ATOM   1269 C  C   . SER   A 1 166 ? -20.331 -13.581 1.349   1.00 133.98 ? 186 SER   A C   1 
ATOM   1270 O  O   . SER   A 1 166 ? -20.994 -13.574 2.393   1.00 135.93 ? 186 SER   A O   1 
ATOM   1271 C  CB  . SER   A 1 166 ? -19.339 -11.562 0.245   1.00 137.96 ? 186 SER   A CB  1 
ATOM   1272 O  OG  . SER   A 1 166 ? -19.554 -12.042 -1.071  1.00 132.95 ? 186 SER   A OG  1 
ATOM   1273 N  N   . THR   A 1 167 ? -20.668 -14.334 0.300   1.00 128.51 ? 187 THR   A N   1 
ATOM   1274 C  CA  . THR   A 1 167 ? -21.900 -15.115 0.297   1.00 130.68 ? 187 THR   A CA  1 
ATOM   1275 C  C   . THR   A 1 167 ? -21.841 -16.337 1.199   1.00 130.14 ? 187 THR   A C   1 
ATOM   1276 O  O   . THR   A 1 167 ? -22.872 -16.989 1.391   1.00 129.59 ? 187 THR   A O   1 
ATOM   1277 C  CB  . THR   A 1 167 ? -22.247 -15.565 -1.124  1.00 119.12 ? 187 THR   A CB  1 
ATOM   1278 O  OG1 . THR   A 1 167 ? -21.117 -16.229 -1.707  1.00 111.78 ? 187 THR   A OG1 1 
ATOM   1279 C  CG2 . THR   A 1 167 ? -22.634 -14.372 -1.982  1.00 126.35 ? 187 THR   A CG2 1 
ATOM   1280 N  N   . SER   A 1 168 ? -20.678 -16.669 1.751   1.00 125.78 ? 188 SER   A N   1 
ATOM   1281 C  CA  . SER   A 1 168 ? -20.553 -17.856 2.581   1.00 130.13 ? 188 SER   A CA  1 
ATOM   1282 C  C   . SER   A 1 168 ? -20.194 -17.574 4.033   1.00 134.92 ? 188 SER   A C   1 
ATOM   1283 O  O   . SER   A 1 168 ? -20.531 -18.388 4.887   1.00 135.01 ? 188 SER   A O   1 
ATOM   1284 C  CB  . SER   A 1 168 ? -19.516 -18.823 1.984   1.00 129.94 ? 188 SER   A CB  1 
ATOM   1285 O  OG  . SER   A 1 168 ? -18.367 -18.131 1.531   1.00 129.49 ? 188 SER   A OG  1 
ATOM   1286 N  N   . PHE   A 1 169 ? -19.537 -16.456 4.347   1.00 133.37 ? 189 PHE   A N   1 
ATOM   1287 C  CA  . PHE   A 1 169 ? -19.135 -16.202 5.724   1.00 137.86 ? 189 PHE   A CA  1 
ATOM   1288 C  C   . PHE   A 1 169 ? -19.275 -14.749 6.164   1.00 139.97 ? 189 PHE   A C   1 
ATOM   1289 O  O   . PHE   A 1 169 ? -18.796 -14.416 7.252   1.00 146.07 ? 189 PHE   A O   1 
ATOM   1290 C  CB  . PHE   A 1 169 ? -17.674 -16.649 5.943   1.00 137.86 ? 189 PHE   A CB  1 
ATOM   1291 C  CG  . PHE   A 1 169 ? -17.347 -17.977 5.324   1.00 137.98 ? 189 PHE   A CG  1 
ATOM   1292 C  CD1 . PHE   A 1 169 ? -17.753 -19.154 5.927   1.00 136.10 ? 189 PHE   A CD1 1 
ATOM   1293 C  CD2 . PHE   A 1 169 ? -16.637 -18.049 4.137   1.00 132.91 ? 189 PHE   A CD2 1 
ATOM   1294 C  CE1 . PHE   A 1 169 ? -17.460 -20.378 5.360   1.00 133.92 ? 189 PHE   A CE1 1 
ATOM   1295 C  CE2 . PHE   A 1 169 ? -16.339 -19.271 3.564   1.00 131.63 ? 189 PHE   A CE2 1 
ATOM   1296 C  CZ  . PHE   A 1 169 ? -16.752 -20.438 4.176   1.00 129.10 ? 189 PHE   A CZ  1 
ATOM   1297 N  N   . GLY   A 1 170 ? -19.897 -13.875 5.369   1.00 144.64 ? 190 GLY   A N   1 
ATOM   1298 C  CA  . GLY   A 1 170 ? -19.936 -12.457 5.665   1.00 140.10 ? 190 GLY   A CA  1 
ATOM   1299 C  C   . GLY   A 1 170 ? -18.596 -11.758 5.673   1.00 147.46 ? 190 GLY   A C   1 
ATOM   1300 O  O   . GLY   A 1 170 ? -18.555 -10.548 5.917   1.00 155.32 ? 190 GLY   A O   1 
ATOM   1301 N  N   . VAL   A 1 171 ? -17.500 -12.475 5.423   1.00 141.56 ? 191 VAL   A N   1 
ATOM   1302 C  CA  . VAL   A 1 171 ? -16.193 -11.842 5.301   1.00 148.84 ? 191 VAL   A CA  1 
ATOM   1303 C  C   . VAL   A 1 171 ? -16.126 -11.079 3.981   1.00 149.32 ? 191 VAL   A C   1 
ATOM   1304 O  O   . VAL   A 1 171 ? -16.551 -11.578 2.929   1.00 146.58 ? 191 VAL   A O   1 
ATOM   1305 C  CB  . VAL   A 1 171 ? -15.078 -12.898 5.410   1.00 153.97 ? 191 VAL   A CB  1 
ATOM   1306 C  CG1 . VAL   A 1 171 ? -13.699 -12.321 4.996   1.00 156.43 ? 191 VAL   A CG1 1 
ATOM   1307 C  CG2 . VAL   A 1 171 ? -15.008 -13.450 6.820   1.00 156.99 ? 191 VAL   A CG2 1 
ATOM   1308 N  N   . ASN   A 1 172 ? -15.575 -9.866  4.023   1.00 153.35 ? 192 ASN   A N   1 
ATOM   1309 C  CA  . ASN   A 1 172 ? -15.646 -8.932  2.901   1.00 158.03 ? 192 ASN   A CA  1 
ATOM   1310 C  C   . ASN   A 1 172 ? -14.251 -8.390  2.611   1.00 159.64 ? 192 ASN   A C   1 
ATOM   1311 O  O   . ASN   A 1 172 ? -13.691 -7.645  3.421   1.00 158.75 ? 192 ASN   A O   1 
ATOM   1312 C  CB  . ASN   A 1 172 ? -16.632 -7.801  3.207   1.00 156.15 ? 192 ASN   A CB  1 
ATOM   1313 C  CG  . ASN   A 1 172 ? -18.026 -8.321  3.516   1.00 155.27 ? 192 ASN   A CG  1 
ATOM   1314 O  OD1 . ASN   A 1 172 ? -18.815 -8.589  2.609   1.00 153.80 ? 192 ASN   A OD1 1 
ATOM   1315 N  ND2 . ASN   A 1 172 ? -18.325 -8.492  4.799   1.00 155.28 ? 192 ASN   A ND2 1 
ATOM   1316 N  N   . ILE   A 1 173 ? -13.684 -8.779  1.468   1.00 161.64 ? 193 ILE   A N   1 
ATOM   1317 C  CA  . ILE   A 1 173 ? -12.301 -8.468  1.128   1.00 159.66 ? 193 ILE   A CA  1 
ATOM   1318 C  C   . ILE   A 1 173 ? -12.237 -8.000  -0.320  1.00 156.15 ? 193 ILE   A C   1 
ATOM   1319 O  O   . ILE   A 1 173 ? -13.038 -8.415  -1.162  1.00 156.45 ? 193 ILE   A O   1 
ATOM   1320 C  CB  . ILE   A 1 173 ? -11.369 -9.690  1.337   1.00 166.55 ? 193 ILE   A CB  1 
ATOM   1321 C  CG1 . ILE   A 1 173 ? -11.529 -10.267 2.742   1.00 168.87 ? 193 ILE   A CG1 1 
ATOM   1322 C  CG2 . ILE   A 1 173 ? -9.911  -9.322  1.099   1.00 162.74 ? 193 ILE   A CG2 1 
ATOM   1323 C  CD1 . ILE   A 1 173 ? -10.646 -11.465 3.005   1.00 172.97 ? 193 ILE   A CD1 1 
ATOM   1324 N  N   . ASP   A 1 174 ? -11.284 -7.112  -0.601  1.00 158.12 ? 194 ASP   A N   1 
ATOM   1325 C  CA  . ASP   A 1 174 ? -10.844 -6.846  -1.969  1.00 160.42 ? 194 ASP   A CA  1 
ATOM   1326 C  C   . ASP   A 1 174 ? -9.694  -7.810  -2.236  1.00 166.15 ? 194 ASP   A C   1 
ATOM   1327 O  O   . ASP   A 1 174 ? -8.525  -7.495  -2.013  1.00 166.37 ? 194 ASP   A O   1 
ATOM   1328 C  CB  . ASP   A 1 174 ? -10.429 -5.390  -2.138  1.00 161.29 ? 194 ASP   A CB  1 
ATOM   1329 C  CG  . ASP   A 1 174 ? -10.258 -4.995  -3.592  1.00 169.15 ? 194 ASP   A CG  1 
ATOM   1330 O  OD1 . ASP   A 1 174 ? -10.531 -5.835  -4.475  1.00 171.67 ? 194 ASP   A OD1 1 
ATOM   1331 O  OD2 . ASP   A 1 174 ? -9.853  -3.842  -3.853  1.00 164.42 ? 194 ASP   A OD2 1 
ATOM   1332 N  N   . SER   A 1 175 ? -10.042 -9.010  -2.714  1.00 167.57 ? 195 SER   A N   1 
ATOM   1333 C  CA  A SER   A 1 175 ? -9.049  -10.070 -2.872  0.80 168.01 ? 195 SER   A CA  1 
ATOM   1334 C  CA  B SER   A 1 175 ? -9.048  -10.068 -2.869  0.20 168.00 ? 195 SER   A CA  1 
ATOM   1335 C  C   . SER   A 1 175 ? -7.946  -9.663  -3.842  1.00 175.31 ? 195 SER   A C   1 
ATOM   1336 O  O   . SER   A 1 175 ? -6.761  -9.906  -3.582  1.00 170.56 ? 195 SER   A O   1 
ATOM   1337 C  CB  A SER   A 1 175 ? -9.731  -11.355 -3.341  0.80 160.97 ? 195 SER   A CB  1 
ATOM   1338 C  CB  B SER   A 1 175 ? -9.726  -11.358 -3.327  0.20 160.94 ? 195 SER   A CB  1 
ATOM   1339 O  OG  A SER   A 1 175 ? -10.850 -11.664 -2.528  0.80 155.68 ? 195 SER   A OG  1 
ATOM   1340 O  OG  B SER   A 1 175 ? -10.354 -11.181 -4.584  0.20 158.25 ? 195 SER   A OG  1 
ATOM   1341 N  N   . LEU   A 1 176 ? -8.315  -9.045  -4.967  1.00 207.21 ? 196 LEU   A N   1 
ATOM   1342 C  CA  . LEU   A 1 176 ? -7.317  -8.608  -5.937  1.00 218.32 ? 196 LEU   A CA  1 
ATOM   1343 C  C   . LEU   A 1 176 ? -6.342  -7.604  -5.339  1.00 223.30 ? 196 LEU   A C   1 
ATOM   1344 O  O   . LEU   A 1 176 ? -5.219  -7.473  -5.837  1.00 229.08 ? 196 LEU   A O   1 
ATOM   1345 C  CB  . LEU   A 1 176 ? -8.009  -8.002  -7.161  1.00 225.54 ? 196 LEU   A CB  1 
ATOM   1346 C  CG  . LEU   A 1 176 ? -7.167  -7.807  -8.424  1.00 232.50 ? 196 LEU   A CG  1 
ATOM   1347 C  CD1 . LEU   A 1 176 ? -6.823  -9.148  -9.058  1.00 231.59 ? 196 LEU   A CD1 1 
ATOM   1348 C  CD2 . LEU   A 1 176 ? -7.887  -6.911  -9.417  1.00 234.74 ? 196 LEU   A CD2 1 
ATOM   1349 N  N   . ASN   A 1 177 ? -6.744  -6.898  -4.282  1.00 185.94 ? 197 ASN   A N   1 
ATOM   1350 C  CA  . ASN   A 1 177 ? -5.898  -5.914  -3.620  1.00 177.10 ? 197 ASN   A CA  1 
ATOM   1351 C  C   . ASN   A 1 177 ? -5.478  -6.344  -2.220  1.00 172.64 ? 197 ASN   A C   1 
ATOM   1352 O  O   . ASN   A 1 177 ? -5.008  -5.509  -1.442  1.00 179.86 ? 197 ASN   A O   1 
ATOM   1353 C  CB  . ASN   A 1 177 ? -6.611  -4.561  -3.562  1.00 178.40 ? 197 ASN   A CB  1 
ATOM   1354 C  CG  . ASN   A 1 177 ? -6.790  -3.938  -4.932  1.00 185.91 ? 197 ASN   A CG  1 
ATOM   1355 O  OD1 . ASN   A 1 177 ? -5.879  -3.962  -5.760  1.00 192.61 ? 197 ASN   A OD1 1 
ATOM   1356 N  ND2 . ASN   A 1 177 ? -7.971  -3.383  -5.183  1.00 180.56 ? 197 ASN   A ND2 1 
ATOM   1357 N  N   . ASN   A 1 178 ? -5.636  -7.621  -1.881  1.00 169.98 ? 198 ASN   A N   1 
ATOM   1358 C  CA  . ASN   A 1 178 ? -5.219  -8.132  -0.578  1.00 155.14 ? 198 ASN   A CA  1 
ATOM   1359 C  C   . ASN   A 1 178 ? -4.659  -9.546  -0.697  1.00 156.55 ? 198 ASN   A C   1 
ATOM   1360 O  O   . ASN   A 1 178 ? -4.767  -10.348 0.231   1.00 143.98 ? 198 ASN   A O   1 
ATOM   1361 C  CB  . ASN   A 1 178 ? -6.388  -8.112  0.409   1.00 153.66 ? 198 ASN   A CB  1 
ATOM   1362 C  CG  . ASN   A 1 178 ? -6.688  -6.720  0.931   1.00 150.30 ? 198 ASN   A CG  1 
ATOM   1363 O  OD1 . ASN   A 1 178 ? -6.201  -6.325  1.990   1.00 151.96 ? 198 ASN   A OD1 1 
ATOM   1364 N  ND2 . ASN   A 1 178 ? -7.493  -5.969  0.188   1.00 152.72 ? 198 ASN   A ND2 1 
ATOM   1365 N  N   . LEU   A 1 196 ? -6.019  -35.898 -14.838 1.00 154.48 ? 216 LEU   A N   1 
ATOM   1366 C  CA  . LEU   A 1 196 ? -4.997  -36.506 -15.682 1.00 157.35 ? 216 LEU   A CA  1 
ATOM   1367 C  C   . LEU   A 1 196 ? -3.604  -36.086 -15.231 1.00 167.66 ? 216 LEU   A C   1 
ATOM   1368 O  O   . LEU   A 1 196 ? -2.627  -36.230 -15.966 1.00 165.17 ? 216 LEU   A O   1 
ATOM   1369 C  CB  . LEU   A 1 196 ? -5.221  -36.133 -17.148 1.00 146.25 ? 216 LEU   A CB  1 
ATOM   1370 C  CG  . LEU   A 1 196 ? -6.546  -36.637 -17.724 1.00 137.54 ? 216 LEU   A CG  1 
ATOM   1371 C  CD1 . LEU   A 1 196 ? -6.658  -36.333 -19.211 1.00 131.52 ? 216 LEU   A CD1 1 
ATOM   1372 C  CD2 . LEU   A 1 196 ? -6.702  -38.127 -17.461 1.00 130.74 ? 216 LEU   A CD2 1 
ATOM   1373 N  N   . ASP   A 1 197 ? -3.525  -35.568 -14.015 1.00 182.13 ? 217 ASP   A N   1 
ATOM   1374 C  CA  . ASP   A 1 197 ? -2.256  -35.194 -13.408 1.00 185.18 ? 217 ASP   A CA  1 
ATOM   1375 C  C   . ASP   A 1 197 ? -1.619  -36.466 -12.844 1.00 180.97 ? 217 ASP   A C   1 
ATOM   1376 O  O   . ASP   A 1 197 ? -2.199  -37.554 -12.924 1.00 175.01 ? 217 ASP   A O   1 
ATOM   1377 C  CB  . ASP   A 1 197 ? -2.502  -34.072 -12.395 1.00 176.31 ? 217 ASP   A CB  1 
ATOM   1378 C  CG  . ASP   A 1 197 ? -2.658  -34.569 -10.968 1.00 174.93 ? 217 ASP   A CG  1 
ATOM   1379 O  OD1 . ASP   A 1 197 ? -3.234  -35.654 -10.752 1.00 173.20 ? 217 ASP   A OD1 1 
ATOM   1380 O  OD2 . ASP   A 1 197 ? -2.210  -33.848 -10.050 1.00 174.21 ? 217 ASP   A OD2 1 
ATOM   1381 N  N   . PRO   A 1 198 ? -0.403  -36.382 -12.284 1.00 178.88 ? 218 PRO   A N   1 
ATOM   1382 C  CA  . PRO   A 1 198 ? 0.258   -37.621 -11.830 1.00 179.53 ? 218 PRO   A CA  1 
ATOM   1383 C  C   . PRO   A 1 198 ? -0.499  -38.391 -10.759 1.00 167.06 ? 218 PRO   A C   1 
ATOM   1384 O  O   . PRO   A 1 198 ? -0.524  -39.627 -10.804 1.00 162.02 ? 218 PRO   A O   1 
ATOM   1385 C  CB  . PRO   A 1 198 ? 1.605   -37.115 -11.304 1.00 181.45 ? 218 PRO   A CB  1 
ATOM   1386 C  CG  . PRO   A 1 198 ? 1.864   -35.885 -12.077 1.00 182.98 ? 218 PRO   A CG  1 
ATOM   1387 C  CD  . PRO   A 1 198 ? 0.526   -35.237 -12.241 1.00 178.24 ? 218 PRO   A CD  1 
ATOM   1388 N  N   . PHE   A 1 199 ? -1.114  -37.705 -9.795  1.00 158.73 ? 219 PHE   A N   1 
ATOM   1389 C  CA  . PHE   A 1 199 ? -1.663  -38.405 -8.638  1.00 148.77 ? 219 PHE   A CA  1 
ATOM   1390 C  C   . PHE   A 1 199 ? -2.936  -39.162 -8.992  1.00 139.63 ? 219 PHE   A C   1 
ATOM   1391 O  O   . PHE   A 1 199 ? -3.034  -40.374 -8.770  1.00 136.27 ? 219 PHE   A O   1 
ATOM   1392 C  CB  . PHE   A 1 199 ? -1.925  -37.420 -7.496  1.00 144.95 ? 219 PHE   A CB  1 
ATOM   1393 C  CG  . PHE   A 1 199 ? -2.613  -38.042 -6.314  1.00 136.33 ? 219 PHE   A CG  1 
ATOM   1394 C  CD1 . PHE   A 1 199 ? -1.946  -38.944 -5.502  1.00 138.41 ? 219 PHE   A CD1 1 
ATOM   1395 C  CD2 . PHE   A 1 199 ? -3.928  -37.727 -6.017  1.00 130.14 ? 219 PHE   A CD2 1 
ATOM   1396 C  CE1 . PHE   A 1 199 ? -2.577  -39.520 -4.414  1.00 138.08 ? 219 PHE   A CE1 1 
ATOM   1397 C  CE2 . PHE   A 1 199 ? -4.562  -38.297 -4.929  1.00 133.89 ? 219 PHE   A CE2 1 
ATOM   1398 C  CZ  . PHE   A 1 199 ? -3.887  -39.195 -4.128  1.00 137.01 ? 219 PHE   A CZ  1 
ATOM   1399 N  N   . PHE   A 1 200 ? -3.933  -38.460 -9.532  1.00 145.34 ? 220 PHE   A N   1 
ATOM   1400 C  CA  . PHE   A 1 200 ? -5.217  -39.096 -9.796  1.00 141.07 ? 220 PHE   A CA  1 
ATOM   1401 C  C   . PHE   A 1 200 ? -5.132  -40.127 -10.915 1.00 139.40 ? 220 PHE   A C   1 
ATOM   1402 O  O   . PHE   A 1 200 ? -6.008  -40.994 -11.007 1.00 130.84 ? 220 PHE   A O   1 
ATOM   1403 C  CB  . PHE   A 1 200 ? -6.266  -38.029 -10.107 1.00 118.70 ? 220 PHE   A CB  1 
ATOM   1404 C  CG  . PHE   A 1 200 ? -6.410  -36.996 -9.021  1.00 128.19 ? 220 PHE   A CG  1 
ATOM   1405 C  CD1 . PHE   A 1 200 ? -7.297  -37.186 -7.975  1.00 122.62 ? 220 PHE   A CD1 1 
ATOM   1406 C  CD2 . PHE   A 1 200 ? -5.648  -35.840 -9.041  1.00 126.43 ? 220 PHE   A CD2 1 
ATOM   1407 C  CE1 . PHE   A 1 200 ? -7.425  -36.239 -6.974  1.00 119.22 ? 220 PHE   A CE1 1 
ATOM   1408 C  CE2 . PHE   A 1 200 ? -5.769  -34.892 -8.046  1.00 123.42 ? 220 PHE   A CE2 1 
ATOM   1409 C  CZ  . PHE   A 1 200 ? -6.658  -35.090 -7.012  1.00 120.23 ? 220 PHE   A CZ  1 
ATOM   1410 N  N   . LEU   A 1 201 ? -4.100  -40.056 -11.759 1.00 163.45 ? 221 LEU   A N   1 
ATOM   1411 C  CA  . LEU   A 1 201 ? -3.793  -41.177 -12.642 1.00 165.53 ? 221 LEU   A CA  1 
ATOM   1412 C  C   . LEU   A 1 201 ? -3.345  -42.387 -11.834 1.00 155.02 ? 221 LEU   A C   1 
ATOM   1413 O  O   . LEU   A 1 201 ? -3.833  -43.504 -12.041 1.00 160.28 ? 221 LEU   A O   1 
ATOM   1414 C  CB  . LEU   A 1 201 ? -2.717  -40.778 -13.653 1.00 169.52 ? 221 LEU   A CB  1 
ATOM   1415 C  CG  . LEU   A 1 201 ? -3.165  -40.384 -15.061 1.00 173.78 ? 221 LEU   A CG  1 
ATOM   1416 C  CD1 . LEU   A 1 201 ? -1.951  -40.094 -15.927 1.00 170.96 ? 221 LEU   A CD1 1 
ATOM   1417 C  CD2 . LEU   A 1 201 ? -4.021  -41.477 -15.679 1.00 148.27 ? 221 LEU   A CD2 1 
ATOM   1418 N  N   . SER   A 1 202 ? -2.411  -42.178 -10.901 1.00 133.86 ? 222 SER   A N   1 
ATOM   1419 C  CA  . SER   A 1 202 ? -2.021  -43.240 -9.980  1.00 134.33 ? 222 SER   A CA  1 
ATOM   1420 C  C   . SER   A 1 202 ? -3.195  -43.735 -9.150  1.00 132.01 ? 222 SER   A C   1 
ATOM   1421 O  O   . SER   A 1 202 ? -3.162  -44.871 -8.664  1.00 136.64 ? 222 SER   A O   1 
ATOM   1422 C  CB  . SER   A 1 202 ? -0.904  -42.753 -9.054  1.00 141.24 ? 222 SER   A CB  1 
ATOM   1423 O  OG  . SER   A 1 202 ? 0.374   -42.964 -9.628  1.00 139.74 ? 222 SER   A OG  1 
ATOM   1424 N  N   . ILE   A 1 203 ? -4.227  -42.909 -8.971  1.00 124.80 ? 223 ILE   A N   1 
ATOM   1425 C  CA  . ILE   A 1 203 ? -5.403  -43.352 -8.231  1.00 128.04 ? 223 ILE   A CA  1 
ATOM   1426 C  C   . ILE   A 1 203 ? -6.085  -44.501 -8.959  1.00 128.70 ? 223 ILE   A C   1 
ATOM   1427 O  O   . ILE   A 1 203 ? -6.462  -45.502 -8.348  1.00 124.91 ? 223 ILE   A O   1 
ATOM   1428 C  CB  . ILE   A 1 203 ? -6.378  -42.185 -7.998  1.00 125.76 ? 223 ILE   A CB  1 
ATOM   1429 C  CG1 . ILE   A 1 203 ? -5.875  -41.277 -6.877  1.00 121.13 ? 223 ILE   A CG1 1 
ATOM   1430 C  CG2 . ILE   A 1 203 ? -7.774  -42.711 -7.667  1.00 117.21 ? 223 ILE   A CG2 1 
ATOM   1431 C  CD1 . ILE   A 1 203 ? -6.919  -40.297 -6.394  1.00 125.36 ? 223 ILE   A CD1 1 
ATOM   1432 N  N   . THR   A 1 204 ? -6.267  -44.378 -10.270 1.00 120.81 ? 224 THR   A N   1 
ATOM   1433 C  CA  . THR   A 1 204 ? -7.058  -45.376 -10.978 1.00 116.45 ? 224 THR   A CA  1 
ATOM   1434 C  C   . THR   A 1 204 ? -6.249  -46.591 -11.416 1.00 110.43 ? 224 THR   A C   1 
ATOM   1435 O  O   . THR   A 1 204 ? -6.845  -47.613 -11.774 1.00 103.23 ? 224 THR   A O   1 
ATOM   1436 C  CB  . THR   A 1 204 ? -7.750  -44.746 -12.186 1.00 105.49 ? 224 THR   A CB  1 
ATOM   1437 O  OG1 . THR   A 1 204 ? -7.539  -43.330 -12.170 1.00 112.04 ? 224 THR   A OG1 1 
ATOM   1438 C  CG2 . THR   A 1 204 ? -9.238  -45.012 -12.108 1.00 108.81 ? 224 THR   A CG2 1 
ATOM   1439 N  N   . VAL   A 1 205 ? -4.920  -46.513 -11.401 1.00 113.55 ? 225 VAL   A N   1 
ATOM   1440 C  CA  . VAL   A 1 205 ? -4.112  -47.716 -11.547 1.00 122.51 ? 225 VAL   A CA  1 
ATOM   1441 C  C   . VAL   A 1 205 ? -3.877  -48.378 -10.191 1.00 127.23 ? 225 VAL   A C   1 
ATOM   1442 O  O   . VAL   A 1 205 ? -3.694  -49.599 -10.119 1.00 130.18 ? 225 VAL   A O   1 
ATOM   1443 C  CB  . VAL   A 1 205 ? -2.784  -47.393 -12.259 1.00 127.68 ? 225 VAL   A CB  1 
ATOM   1444 C  CG1 . VAL   A 1 205 ? -1.926  -48.642 -12.413 1.00 121.78 ? 225 VAL   A CG1 1 
ATOM   1445 C  CG2 . VAL   A 1 205 ? -3.062  -46.786 -13.619 1.00 117.96 ? 225 VAL   A CG2 1 
ATOM   1446 N  N   . PHE   A 1 206 ? -3.913  -47.605 -9.106  1.00 129.14 ? 226 PHE   A N   1 
ATOM   1447 C  CA  . PHE   A 1 206 ? -3.812  -48.134 -7.746  1.00 133.82 ? 226 PHE   A CA  1 
ATOM   1448 C  C   . PHE   A 1 206 ? -4.936  -47.575 -6.875  1.00 136.54 ? 226 PHE   A C   1 
ATOM   1449 O  O   . PHE   A 1 206 ? -4.688  -46.817 -5.929  1.00 136.83 ? 226 PHE   A O   1 
ATOM   1450 C  CB  . PHE   A 1 206 ? -2.447  -47.807 -7.140  1.00 137.60 ? 226 PHE   A CB  1 
ATOM   1451 C  CG  . PHE   A 1 206 ? -1.310  -47.836 -8.127  1.00 141.89 ? 226 PHE   A CG  1 
ATOM   1452 C  CD1 . PHE   A 1 206 ? -0.878  -49.029 -8.679  1.00 141.80 ? 226 PHE   A CD1 1 
ATOM   1453 C  CD2 . PHE   A 1 206 ? -0.655  -46.669 -8.478  1.00 139.20 ? 226 PHE   A CD2 1 
ATOM   1454 C  CE1 . PHE   A 1 206 ? 0.175   -49.048 -9.576  1.00 142.00 ? 226 PHE   A CE1 1 
ATOM   1455 C  CE2 . PHE   A 1 206 ? 0.399   -46.685 -9.369  1.00 137.94 ? 226 PHE   A CE2 1 
ATOM   1456 C  CZ  . PHE   A 1 206 ? 0.813   -47.876 -9.920  1.00 140.36 ? 226 PHE   A CZ  1 
ATOM   1457 N  N   . PRO   A 1 207 ? -6.195  -47.930 -7.165  1.00 124.02 ? 227 PRO   A N   1 
ATOM   1458 C  CA  . PRO   A 1 207 ? -7.294  -47.496 -6.290  1.00 117.18 ? 227 PRO   A CA  1 
ATOM   1459 C  C   . PRO   A 1 207 ? -7.394  -48.318 -5.026  1.00 112.38 ? 227 PRO   A C   1 
ATOM   1460 O  O   . PRO   A 1 207 ? -8.080  -47.902 -4.082  1.00 106.26 ? 227 PRO   A O   1 
ATOM   1461 C  CB  . PRO   A 1 207 ? -8.533  -47.670 -7.175  1.00 110.35 ? 227 PRO   A CB  1 
ATOM   1462 C  CG  . PRO   A 1 207 ? -8.181  -48.823 -8.042  1.00 110.37 ? 227 PRO   A CG  1 
ATOM   1463 C  CD  . PRO   A 1 207 ? -6.692  -48.737 -8.295  1.00 120.79 ? 227 PRO   A CD  1 
ATOM   1464 N  N   . PHE   A 1 208 ? -6.723  -49.466 -4.983  1.00 99.49  ? 228 PHE   A N   1 
ATOM   1465 C  CA  . PHE   A 1 208 ? -6.514  -50.197 -3.745  1.00 108.41 ? 228 PHE   A CA  1 
ATOM   1466 C  C   . PHE   A 1 208 ? -5.633  -49.430 -2.765  1.00 112.62 ? 228 PHE   A C   1 
ATOM   1467 O  O   . PHE   A 1 208 ? -5.392  -49.930 -1.660  1.00 118.26 ? 228 PHE   A O   1 
ATOM   1468 C  CB  . PHE   A 1 208 ? -5.903  -51.566 -4.058  1.00 115.37 ? 228 PHE   A CB  1 
ATOM   1469 C  CG  . PHE   A 1 208 ? -4.625  -51.510 -4.850  1.00 120.20 ? 228 PHE   A CG  1 
ATOM   1470 C  CD1 . PHE   A 1 208 ? -4.653  -51.486 -6.233  1.00 116.22 ? 228 PHE   A CD1 1 
ATOM   1471 C  CD2 . PHE   A 1 208 ? -3.397  -51.503 -4.210  1.00 122.14 ? 228 PHE   A CD2 1 
ATOM   1472 C  CE1 . PHE   A 1 208 ? -3.484  -51.446 -6.963  1.00 116.97 ? 228 PHE   A CE1 1 
ATOM   1473 C  CE2 . PHE   A 1 208 ? -2.221  -51.463 -4.934  1.00 124.74 ? 228 PHE   A CE2 1 
ATOM   1474 C  CZ  . PHE   A 1 208 ? -2.265  -51.432 -6.314  1.00 130.37 ? 228 PHE   A CZ  1 
ATOM   1475 N  N   . LEU   A 1 209 ? -5.136  -48.252 -3.153  1.00 107.51 ? 229 LEU   A N   1 
ATOM   1476 C  CA  . LEU   A 1 209 ? -4.338  -47.399 -2.279  1.00 112.98 ? 229 LEU   A CA  1 
ATOM   1477 C  C   . LEU   A 1 209 ? -5.128  -46.246 -1.675  1.00 115.08 ? 229 LEU   A C   1 
ATOM   1478 O  O   . LEU   A 1 209 ? -4.545  -45.426 -0.961  1.00 122.44 ? 229 LEU   A O   1 
ATOM   1479 C  CB  . LEU   A 1 209 ? -3.129  -46.831 -3.032  1.00 116.13 ? 229 LEU   A CB  1 
ATOM   1480 C  CG  . LEU   A 1 209 ? -2.115  -47.836 -3.570  1.00 120.50 ? 229 LEU   A CG  1 
ATOM   1481 C  CD1 . LEU   A 1 209 ? -0.849  -47.132 -4.010  1.00 117.97 ? 229 LEU   A CD1 1 
ATOM   1482 C  CD2 . LEU   A 1 209 ? -1.809  -48.872 -2.518  1.00 119.52 ? 229 LEU   A CD2 1 
ATOM   1483 N  N   . ILE   A 1 210 ? -6.425  -46.149 -1.950  1.00 106.92 ? 230 ILE   A N   1 
ATOM   1484 C  CA  . ILE   A 1 210 ? -7.263  -45.135 -1.313  1.00 105.47 ? 230 ILE   A CA  1 
ATOM   1485 C  C   . ILE   A 1 210 ? -7.365  -45.419 0.183   1.00 107.46 ? 230 ILE   A C   1 
ATOM   1486 O  O   . ILE   A 1 210 ? -7.077  -44.519 0.985   1.00 104.68 ? 230 ILE   A O   1 
ATOM   1487 C  CB  . ILE   A 1 210 ? -8.656  -45.056 -1.957  1.00 104.60 ? 230 ILE   A CB  1 
ATOM   1488 C  CG1 . ILE   A 1 210 ? -8.545  -44.842 -3.465  1.00 108.68 ? 230 ILE   A CG1 1 
ATOM   1489 C  CG2 . ILE   A 1 210 ? -9.455  -43.921 -1.333  1.00 105.19 ? 230 ILE   A CG2 1 
ATOM   1490 C  CD1 . ILE   A 1 210 ? -9.865  -44.993 -4.190  1.00 103.52 ? 230 ILE   A CD1 1 
ATOM   1491 N  N   . PRO   A 1 211 ? -7.757  -46.625 0.625   1.00 111.53 ? 231 PRO   A N   1 
ATOM   1492 C  CA  . PRO   A 1 211 ? -7.796  -46.868 2.076   1.00 113.21 ? 231 PRO   A CA  1 
ATOM   1493 C  C   . PRO   A 1 211 ? -6.418  -46.825 2.704   1.00 111.51 ? 231 PRO   A C   1 
ATOM   1494 O  O   . PRO   A 1 211 ? -6.302  -46.582 3.913   1.00 110.23 ? 231 PRO   A O   1 
ATOM   1495 C  CB  . PRO   A 1 211 ? -8.424  -48.267 2.192   1.00 105.47 ? 231 PRO   A CB  1 
ATOM   1496 C  CG  . PRO   A 1 211 ? -8.844  -48.658 0.814   1.00 104.28 ? 231 PRO   A CG  1 
ATOM   1497 C  CD  . PRO   A 1 211 ? -7.996  -47.875 -0.119  1.00 106.59 ? 231 PRO   A CD  1 
ATOM   1498 N  N   . ILE   A 1 212 ? -5.374  -47.080 1.911   1.00 116.93 ? 232 ILE   A N   1 
ATOM   1499 C  CA  . ILE   A 1 212 ? -3.999  -46.875 2.357   1.00 113.00 ? 232 ILE   A CA  1 
ATOM   1500 C  C   . ILE   A 1 212 ? -3.815  -45.457 2.872   1.00 111.69 ? 232 ILE   A C   1 
ATOM   1501 O  O   . ILE   A 1 212 ? -3.185  -45.231 3.911   1.00 130.87 ? 232 ILE   A O   1 
ATOM   1502 C  CB  . ILE   A 1 212 ? -3.023  -47.186 1.206   1.00 111.48 ? 232 ILE   A CB  1 
ATOM   1503 C  CG1 . ILE   A 1 212 ? -2.906  -48.696 0.979   1.00 120.00 ? 232 ILE   A CG1 1 
ATOM   1504 C  CG2 . ILE   A 1 212 ? -1.668  -46.517 1.441   1.00 114.88 ? 232 ILE   A CG2 1 
ATOM   1505 C  CD1 . ILE   A 1 212 ? -1.495  -49.221 1.085   1.00 133.07 ? 232 ILE   A CD1 1 
ATOM   1506 N  N   . LEU   A 1 213 ? -4.367  -44.480 2.157   1.00 117.78 ? 233 LEU   A N   1 
ATOM   1507 C  CA  . LEU   A 1 213 ? -4.154  -43.079 2.491   1.00 123.73 ? 233 LEU   A CA  1 
ATOM   1508 C  C   . LEU   A 1 213 ? -5.133  -42.559 3.535   1.00 127.67 ? 233 LEU   A C   1 
ATOM   1509 O  O   . LEU   A 1 213 ? -4.804  -41.613 4.259   1.00 134.96 ? 233 LEU   A O   1 
ATOM   1510 C  CB  . LEU   A 1 213 ? -4.238  -42.230 1.222   1.00 113.88 ? 233 LEU   A CB  1 
ATOM   1511 C  CG  . LEU   A 1 213 ? -3.327  -42.753 0.108   1.00 107.44 ? 233 LEU   A CG  1 
ATOM   1512 C  CD1 . LEU   A 1 213 ? -3.499  -41.962 -1.178  1.00 111.24 ? 233 LEU   A CD1 1 
ATOM   1513 C  CD2 . LEU   A 1 213 ? -1.870  -42.769 0.555   1.00 111.18 ? 233 LEU   A CD2 1 
ATOM   1514 N  N   . GLU   A 1 214 ? -6.326  -43.153 3.635   1.00 114.86 ? 234 GLU   A N   1 
ATOM   1515 C  CA  . GLU   A 1 214 ? -7.260  -42.737 4.675   1.00 117.99 ? 234 GLU   A CA  1 
ATOM   1516 C  C   . GLU   A 1 214 ? -6.722  -43.049 6.064   1.00 130.20 ? 234 GLU   A C   1 
ATOM   1517 O  O   . GLU   A 1 214 ? -7.024  -42.331 7.024   1.00 140.03 ? 234 GLU   A O   1 
ATOM   1518 C  CB  . GLU   A 1 214 ? -8.620  -43.408 4.467   1.00 111.35 ? 234 GLU   A CB  1 
ATOM   1519 C  CG  . GLU   A 1 214 ? -9.218  -43.233 3.074   1.00 114.33 ? 234 GLU   A CG  1 
ATOM   1520 C  CD  . GLU   A 1 214 ? -9.787  -41.842 2.825   1.00 115.42 ? 234 GLU   A CD  1 
ATOM   1521 O  OE1 . GLU   A 1 214 ? -9.457  -40.901 3.578   1.00 108.91 ? 234 GLU   A OE1 1 
ATOM   1522 O  OE2 . GLU   A 1 214 ? -10.576 -41.691 1.868   1.00 111.67 ? 234 GLU   A OE2 1 
ATOM   1523 N  N   . VAL   A 1 215 ? -5.928  -44.114 6.193   1.00 134.67 ? 235 VAL   A N   1 
ATOM   1524 C  CA  . VAL   A 1 215 ? -5.277  -44.408 7.465   1.00 130.36 ? 235 VAL   A CA  1 
ATOM   1525 C  C   . VAL   A 1 215 ? -3.978  -43.626 7.621   1.00 134.37 ? 235 VAL   A C   1 
ATOM   1526 O  O   . VAL   A 1 215 ? -3.472  -43.493 8.743   1.00 138.37 ? 235 VAL   A O   1 
ATOM   1527 C  CB  . VAL   A 1 215 ? -5.033  -45.922 7.610   1.00 125.67 ? 235 VAL   A CB  1 
ATOM   1528 C  CG1 . VAL   A 1 215 ? -3.892  -46.373 6.718   1.00 122.36 ? 235 VAL   A CG1 1 
ATOM   1529 C  CG2 . VAL   A 1 215 ? -4.769  -46.298 9.065   1.00 124.65 ? 235 VAL   A CG2 1 
ATOM   1530 N  N   . LEU   A 1 216 ? -3.433  -43.088 6.533   1.00 131.24 ? 236 LEU   A N   1 
ATOM   1531 C  CA  . LEU   A 1 216 ? -2.242  -42.250 6.592   1.00 133.35 ? 236 LEU   A CA  1 
ATOM   1532 C  C   . LEU   A 1 216 ? -2.568  -40.785 6.855   1.00 146.91 ? 236 LEU   A C   1 
ATOM   1533 O  O   . LEU   A 1 216 ? -1.653  -39.955 6.871   1.00 148.78 ? 236 LEU   A O   1 
ATOM   1534 C  CB  . LEU   A 1 216 ? -1.436  -42.374 5.292   1.00 128.73 ? 236 LEU   A CB  1 
ATOM   1535 C  CG  . LEU   A 1 216 ? -0.616  -43.639 5.003   1.00 136.20 ? 236 LEU   A CG  1 
ATOM   1536 C  CD1 . LEU   A 1 216 ? 0.843   -43.288 4.746   1.00 132.83 ? 236 LEU   A CD1 1 
ATOM   1537 C  CD2 . LEU   A 1 216 ? -0.725  -44.656 6.123   1.00 139.69 ? 236 LEU   A CD2 1 
ATOM   1538 N  N   . ASN   A 1 217 ? -3.845  -40.458 7.061   1.00 159.60 ? 237 ASN   A N   1 
ATOM   1539 C  CA  . ASN   A 1 217 ? -4.305  -39.091 7.324   1.00 169.21 ? 237 ASN   A CA  1 
ATOM   1540 C  C   . ASN   A 1 217 ? -3.764  -38.105 6.292   1.00 168.71 ? 237 ASN   A C   1 
ATOM   1541 O  O   . ASN   A 1 217 ? -3.383  -36.978 6.614   1.00 170.61 ? 237 ASN   A O   1 
ATOM   1542 C  CB  . ASN   A 1 217 ? -3.948  -38.639 8.739   1.00 174.79 ? 237 ASN   A CB  1 
ATOM   1543 C  CG  . ASN   A 1 217 ? -4.946  -37.639 9.287   1.00 187.96 ? 237 ASN   A CG  1 
ATOM   1544 O  OD1 . ASN   A 1 217 ? -6.137  -37.714 8.981   1.00 190.11 ? 237 ASN   A OD1 1 
ATOM   1545 N  ND2 . ASN   A 1 217 ? -4.469  -36.690 10.085  1.00 196.42 ? 237 ASN   A ND2 1 
ATOM   1546 N  N   . ILE   A 1 218 ? -3.727  -38.534 5.040   1.00 157.62 ? 238 ILE   A N   1 
ATOM   1547 C  CA  . ILE   A 1 218 ? -3.385  -37.657 3.939   1.00 155.32 ? 238 ILE   A CA  1 
ATOM   1548 C  C   . ILE   A 1 218 ? -4.686  -37.172 3.317   1.00 154.16 ? 238 ILE   A C   1 
ATOM   1549 O  O   . ILE   A 1 218 ? -5.762  -37.736 3.536   1.00 155.47 ? 238 ILE   A O   1 
ATOM   1550 C  CB  . ILE   A 1 218 ? -2.484  -38.358 2.897   1.00 147.90 ? 238 ILE   A CB  1 
ATOM   1551 C  CG1 . ILE   A 1 218 ? -1.482  -39.271 3.598   1.00 148.33 ? 238 ILE   A CG1 1 
ATOM   1552 C  CG2 . ILE   A 1 218 ? -1.725  -37.334 2.060   1.00 148.03 ? 238 ILE   A CG2 1 
ATOM   1553 C  CD1 . ILE   A 1 218 ? -0.552  -39.990 2.656   1.00 140.43 ? 238 ILE   A CD1 1 
ATOM   1554 N  N   . CYS   A 1 219 ? -4.592  -36.107 2.528   1.00 151.78 ? 239 CYS   A N   1 
ATOM   1555 C  CA  . CYS   A 1 219 ? -5.782  -35.499 1.953   1.00 151.91 ? 239 CYS   A CA  1 
ATOM   1556 C  C   . CYS   A 1 219 ? -5.394  -34.695 0.728   1.00 151.74 ? 239 CYS   A C   1 
ATOM   1557 O  O   . CYS   A 1 219 ? -4.392  -33.979 0.747   1.00 153.38 ? 239 CYS   A O   1 
ATOM   1558 C  CB  . CYS   A 1 219 ? -6.467  -34.576 2.958   1.00 157.50 ? 239 CYS   A CB  1 
ATOM   1559 S  SG  . CYS   A 1 219 ? -8.219  -34.863 3.218   1.00 151.89 ? 239 CYS   A SG  1 
ATOM   1560 N  N   . VAL   A 1 220 ? -6.216  -34.794 -0.322  1.00 154.33 ? 240 VAL   A N   1 
ATOM   1561 C  CA  . VAL   A 1 220 ? -6.046  -33.941 -1.493  1.00 155.03 ? 240 VAL   A CA  1 
ATOM   1562 C  C   . VAL   A 1 220 ? -6.515  -32.532 -1.205  1.00 156.90 ? 240 VAL   A C   1 
ATOM   1563 O  O   . VAL   A 1 220 ? -6.448  -31.662 -2.082  1.00 153.59 ? 240 VAL   A O   1 
ATOM   1564 C  CB  . VAL   A 1 220 ? -6.800  -34.517 -2.707  1.00 147.81 ? 240 VAL   A CB  1 
ATOM   1565 C  CG1 . VAL   A 1 220 ? -6.130  -35.768 -3.187  1.00 138.46 ? 240 VAL   A CG1 1 
ATOM   1566 C  CG2 . VAL   A 1 220 ? -8.245  -34.805 -2.325  1.00 143.27 ? 240 VAL   A CG2 1 
ATOM   1567 N  N   . PHE   A 1 221 ? -7.026  -32.292 -0.006  1.00 161.36 ? 241 PHE   A N   1 
ATOM   1568 C  CA  . PHE   A 1 221 ? -7.316  -30.942 0.473   1.00 158.07 ? 241 PHE   A CA  1 
ATOM   1569 C  C   . PHE   A 1 221 ? -6.375  -30.709 1.639   1.00 158.19 ? 241 PHE   A C   1 
ATOM   1570 O  O   . PHE   A 1 221 ? -6.633  -31.208 2.748   1.00 156.17 ? 241 PHE   A O   1 
ATOM   1571 C  CB  . PHE   A 1 221 ? -8.782  -30.791 0.887   1.00 160.25 ? 241 PHE   A CB  1 
ATOM   1572 C  CG  . PHE   A 1 221 ? -9.689  -31.546 -0.003  1.00 166.90 ? 241 PHE   A CG  1 
ATOM   1573 C  CD1 . PHE   A 1 221 ? -9.943  -31.076 -1.273  1.00 162.17 ? 241 PHE   A CD1 1 
ATOM   1574 C  CD2 . PHE   A 1 221 ? -10.183 -32.786 0.365   1.00 162.23 ? 241 PHE   A CD2 1 
ATOM   1575 C  CE1 . PHE   A 1 221 ? -10.715 -31.788 -2.148  1.00 161.20 ? 241 PHE   A CE1 1 
ATOM   1576 C  CE2 . PHE   A 1 221 ? -10.969 -33.514 -0.513  1.00 160.49 ? 241 PHE   A CE2 1 
ATOM   1577 C  CZ  . PHE   A 1 221 ? -11.229 -33.010 -1.774  1.00 159.48 ? 241 PHE   A CZ  1 
ATOM   1578 N  N   . PRO   A 1 222 ? -5.273  -29.977 1.443   1.00 163.73 ? 242 PRO   A N   1 
ATOM   1579 C  CA  . PRO   A 1 222 ? -4.159  -30.039 2.403   1.00 165.45 ? 242 PRO   A CA  1 
ATOM   1580 C  C   . PRO   A 1 222 ? -4.671  -29.934 3.832   1.00 183.03 ? 242 PRO   A C   1 
ATOM   1581 O  O   . PRO   A 1 222 ? -5.636  -29.223 4.117   1.00 184.38 ? 242 PRO   A O   1 
ATOM   1582 C  CB  . PRO   A 1 222 ? -3.240  -28.893 1.960   1.00 164.87 ? 242 PRO   A CB  1 
ATOM   1583 C  CG  . PRO   A 1 222 ? -4.018  -28.127 0.905   1.00 150.32 ? 242 PRO   A CG  1 
ATOM   1584 C  CD  . PRO   A 1 222 ? -4.952  -29.110 0.296   1.00 154.34 ? 242 PRO   A CD  1 
ATOM   1585 N  N   . ARG   A 1 223 ? -3.999  -30.648 4.739   1.00 199.70 ? 243 ARG   A N   1 
ATOM   1586 C  CA  . ARG   A 1 223 ? -4.413  -30.721 6.138   1.00 206.27 ? 243 ARG   A CA  1 
ATOM   1587 C  C   . ARG   A 1 223 ? -4.279  -29.371 6.838   1.00 203.19 ? 243 ARG   A C   1 
ATOM   1588 O  O   . ARG   A 1 223 ? -4.549  -29.257 8.036   1.00 207.18 ? 243 ARG   A O   1 
ATOM   1589 C  CB  . ARG   A 1 223 ? -3.621  -31.819 6.862   1.00 206.67 ? 243 ARG   A CB  1 
ATOM   1590 C  CG  . ARG   A 1 223 ? -4.241  -32.306 8.169   1.00 206.80 ? 243 ARG   A CG  1 
ATOM   1591 C  CD  . ARG   A 1 223 ? -5.724  -32.612 8.010   1.00 210.18 ? 243 ARG   A CD  1 
ATOM   1592 N  NE  . ARG   A 1 223 ? -5.965  -33.821 7.232   1.00 203.05 ? 243 ARG   A NE  1 
ATOM   1593 C  CZ  . ARG   A 1 223 ? -7.168  -34.311 6.965   1.00 195.95 ? 243 ARG   A CZ  1 
ATOM   1594 N  NH1 . ARG   A 1 223 ? -8.269  -33.710 7.388   1.00 195.39 ? 243 ARG   A NH1 1 
ATOM   1595 N  NH2 . ARG   A 1 223 ? -7.270  -35.433 6.258   1.00 191.73 ? 243 ARG   A NH2 1 
ATOM   1596 N  N   . GLU   A 1 224 ? -3.871  -28.340 6.100   1.00 189.06 ? 244 GLU   A N   1 
ATOM   1597 C  CA  . GLU   A 1 224 ? -3.793  -26.973 6.601   1.00 196.29 ? 244 GLU   A CA  1 
ATOM   1598 C  C   . GLU   A 1 224 ? -4.971  -26.111 6.163   1.00 191.58 ? 244 GLU   A C   1 
ATOM   1599 O  O   . GLU   A 1 224 ? -5.517  -25.360 6.978   1.00 190.54 ? 244 GLU   A O   1 
ATOM   1600 C  CB  . GLU   A 1 224 ? -2.485  -26.326 6.140   1.00 200.66 ? 244 GLU   A CB  1 
ATOM   1601 C  CG  . GLU   A 1 224 ? -2.159  -26.594 4.681   1.00 198.98 ? 244 GLU   A CG  1 
ATOM   1602 C  CD  . GLU   A 1 224 ? -1.872  -25.327 3.907   1.00 205.96 ? 244 GLU   A CD  1 
ATOM   1603 O  OE1 . GLU   A 1 224 ? -1.170  -24.447 4.445   1.00 221.88 ? 244 GLU   A OE1 1 
ATOM   1604 O  OE2 . GLU   A 1 224 ? -2.356  -25.211 2.762   1.00 202.96 ? 244 GLU   A OE2 1 
ATOM   1605 N  N   . VAL   A 1 225 ? -5.375  -26.201 4.892   1.00 190.65 ? 245 VAL   A N   1 
ATOM   1606 C  CA  . VAL   A 1 225 ? -6.543  -25.459 4.421   1.00 186.08 ? 245 VAL   A CA  1 
ATOM   1607 C  C   . VAL   A 1 225 ? -7.772  -25.851 5.225   1.00 180.09 ? 245 VAL   A C   1 
ATOM   1608 O  O   . VAL   A 1 225 ? -8.469  -25.001 5.790   1.00 172.52 ? 245 VAL   A O   1 
ATOM   1609 C  CB  . VAL   A 1 225 ? -6.764  -25.696 2.917   1.00 179.49 ? 245 VAL   A CB  1 
ATOM   1610 C  CG1 . VAL   A 1 225 ? -8.093  -25.096 2.477   1.00 180.62 ? 245 VAL   A CG1 1 
ATOM   1611 C  CG2 . VAL   A 1 225 ? -5.620  -25.110 2.113   1.00 178.38 ? 245 VAL   A CG2 1 
ATOM   1612 N  N   . THR   A 1 226 ? -8.050  -27.153 5.288   1.00 195.46 ? 246 THR   A N   1 
ATOM   1613 C  CA  . THR   A 1 226 ? -9.178  -27.629 6.074   1.00 185.44 ? 246 THR   A CA  1 
ATOM   1614 C  C   . THR   A 1 226 ? -9.013  -27.269 7.543   1.00 179.33 ? 246 THR   A C   1 
ATOM   1615 O  O   . THR   A 1 226 ? -9.975  -26.854 8.197   1.00 177.85 ? 246 THR   A O   1 
ATOM   1616 C  CB  . THR   A 1 226 ? -9.329  -29.136 5.902   1.00 179.96 ? 246 THR   A CB  1 
ATOM   1617 O  OG1 . THR   A 1 226 ? -8.168  -29.797 6.418   1.00 187.91 ? 246 THR   A OG1 1 
ATOM   1618 C  CG2 . THR   A 1 226 ? -9.495  -29.487 4.431   1.00 176.32 ? 246 THR   A CG2 1 
ATOM   1619 N  N   . ASN   A 1 227 ? -7.797  -27.413 8.079   1.00 179.89 ? 247 ASN   A N   1 
ATOM   1620 C  CA  . ASN   A 1 227 ? -7.542  -26.979 9.449   1.00 182.28 ? 247 ASN   A CA  1 
ATOM   1621 C  C   . ASN   A 1 227 ? -7.801  -25.488 9.611   1.00 182.78 ? 247 ASN   A C   1 
ATOM   1622 O  O   . ASN   A 1 227 ? -8.364  -25.058 10.624  1.00 180.66 ? 247 ASN   A O   1 
ATOM   1623 C  CB  . ASN   A 1 227 ? -6.108  -27.310 9.860   1.00 186.30 ? 247 ASN   A CB  1 
ATOM   1624 C  CG  . ASN   A 1 227 ? -5.972  -28.703 10.440  1.00 189.88 ? 247 ASN   A CG  1 
ATOM   1625 O  OD1 . ASN   A 1 227 ? -6.939  -29.282 10.935  1.00 189.77 ? 247 ASN   A OD1 1 
ATOM   1626 N  ND2 . ASN   A 1 227 ? -4.763  -29.250 10.383  1.00 190.62 ? 247 ASN   A ND2 1 
ATOM   1627 N  N   . PHE   A 1 228 ? -7.392  -24.685 8.626   1.00 179.82 ? 248 PHE   A N   1 
ATOM   1628 C  CA  . PHE   A 1 228 ? -7.629  -23.247 8.692   1.00 175.07 ? 248 PHE   A CA  1 
ATOM   1629 C  C   . PHE   A 1 228 ? -9.114  -22.944 8.836   1.00 170.24 ? 248 PHE   A C   1 
ATOM   1630 O  O   . PHE   A 1 228 ? -9.529  -22.244 9.766   1.00 168.47 ? 248 PHE   A O   1 
ATOM   1631 C  CB  . PHE   A 1 228 ? -7.057  -22.561 7.450   1.00 171.88 ? 248 PHE   A CB  1 
ATOM   1632 C  CG  . PHE   A 1 228 ? -7.526  -21.144 7.268   1.00 166.01 ? 248 PHE   A CG  1 
ATOM   1633 C  CD1 . PHE   A 1 228 ? -7.113  -20.146 8.134   1.00 171.30 ? 248 PHE   A CD1 1 
ATOM   1634 C  CD2 . PHE   A 1 228 ? -8.375  -20.810 6.225   1.00 155.17 ? 248 PHE   A CD2 1 
ATOM   1635 C  CE1 . PHE   A 1 228 ? -7.543  -18.842 7.969   1.00 168.62 ? 248 PHE   A CE1 1 
ATOM   1636 C  CE2 . PHE   A 1 228 ? -8.807  -19.508 6.053   1.00 159.22 ? 248 PHE   A CE2 1 
ATOM   1637 C  CZ  . PHE   A 1 228 ? -8.390  -18.523 6.926   1.00 165.16 ? 248 PHE   A CZ  1 
ATOM   1638 N  N   . LEU   A 1 229 ? -9.934  -23.489 7.937   1.00 170.08 ? 249 LEU   A N   1 
ATOM   1639 C  CA  . LEU   A 1 229 ? -11.353 -23.153 7.936   1.00 163.67 ? 249 LEU   A CA  1 
ATOM   1640 C  C   . LEU   A 1 229 ? -12.099 -23.851 9.069   1.00 169.13 ? 249 LEU   A C   1 
ATOM   1641 O  O   . LEU   A 1 229 ? -13.039 -23.282 9.633   1.00 164.62 ? 249 LEU   A O   1 
ATOM   1642 C  CB  . LEU   A 1 229 ? -11.965 -23.499 6.580   1.00 148.00 ? 249 LEU   A CB  1 
ATOM   1643 C  CG  . LEU   A 1 229 ? -11.391 -22.691 5.412   1.00 147.37 ? 249 LEU   A CG  1 
ATOM   1644 C  CD1 . LEU   A 1 229 ? -11.729 -23.330 4.077   1.00 133.51 ? 249 LEU   A CD1 1 
ATOM   1645 C  CD2 . LEU   A 1 229 ? -11.893 -21.256 5.459   1.00 137.45 ? 249 LEU   A CD2 1 
ATOM   1646 N  N   . ARG   A 1 230 ? -11.695 -25.079 9.419   1.00 175.02 ? 250 ARG   A N   1 
ATOM   1647 C  CA  . ARG   A 1 230 ? -12.365 -25.796 10.504  1.00 173.93 ? 250 ARG   A CA  1 
ATOM   1648 C  C   . ARG   A 1 230 ? -12.349 -24.990 11.796  1.00 174.56 ? 250 ARG   A C   1 
ATOM   1649 O  O   . ARG   A 1 230 ? -13.357 -24.929 12.511  1.00 174.49 ? 250 ARG   A O   1 
ATOM   1650 C  CB  . ARG   A 1 230 ? -11.718 -27.166 10.721  1.00 170.98 ? 250 ARG   A CB  1 
ATOM   1651 C  CG  . ARG   A 1 230 ? -12.256 -28.268 9.816   1.00 168.25 ? 250 ARG   A CG  1 
ATOM   1652 C  CD  . ARG   A 1 230 ? -11.363 -29.498 9.861   1.00 162.65 ? 250 ARG   A CD  1 
ATOM   1653 N  NE  . ARG   A 1 230 ? -11.402 -30.160 11.160  1.00 164.89 ? 250 ARG   A NE  1 
ATOM   1654 C  CZ  . ARG   A 1 230 ? -10.546 -31.094 11.550  1.00 170.81 ? 250 ARG   A CZ  1 
ATOM   1655 N  NH1 . ARG   A 1 230 ? -9.547  -31.483 10.774  1.00 174.19 ? 250 ARG   A NH1 1 
ATOM   1656 N  NH2 . ARG   A 1 230 ? -10.694 -31.649 12.749  1.00 164.57 ? 250 ARG   A NH2 1 
ATOM   1657 N  N   . LYS   A 1 231 ? -11.217 -24.359 12.111  1.00 180.24 ? 251 LYS   A N   1 
ATOM   1658 C  CA  . LYS   A 1 231 ? -11.168 -23.472 13.267  1.00 183.07 ? 251 LYS   A CA  1 
ATOM   1659 C  C   . LYS   A 1 231 ? -11.659 -22.070 12.928  1.00 180.78 ? 251 LYS   A C   1 
ATOM   1660 O  O   . LYS   A 1 231 ? -12.211 -21.388 13.798  1.00 181.56 ? 251 LYS   A O   1 
ATOM   1661 C  CB  . LYS   A 1 231 ? -9.746  -23.425 13.831  1.00 192.76 ? 251 LYS   A CB  1 
ATOM   1662 C  CG  . LYS   A 1 231 ? -8.702  -22.942 12.847  1.00 195.29 ? 251 LYS   A CG  1 
ATOM   1663 C  CD  . LYS   A 1 231 ? -7.306  -23.347 13.281  1.00 197.47 ? 251 LYS   A CD  1 
ATOM   1664 C  CE  . LYS   A 1 231 ? -6.284  -23.004 12.213  1.00 198.00 ? 251 LYS   A CE  1 
ATOM   1665 N  NZ  . LYS   A 1 231 ? -6.341  -21.562 11.845  1.00 200.31 ? 251 LYS   A NZ  1 
ATOM   1666 N  N   . SER   A 1 232 ? -11.480 -21.625 11.679  1.00 180.27 ? 252 SER   A N   1 
ATOM   1667 C  CA  . SER   A 1 232 ? -12.018 -20.328 11.280  1.00 181.99 ? 252 SER   A CA  1 
ATOM   1668 C  C   . SER   A 1 232 ? -13.536 -20.304 11.371  1.00 180.51 ? 252 SER   A C   1 
ATOM   1669 O  O   . SER   A 1 232 ? -14.124 -19.258 11.672  1.00 180.45 ? 252 SER   A O   1 
ATOM   1670 C  CB  . SER   A 1 232 ? -11.576 -19.978 9.859   1.00 171.70 ? 252 SER   A CB  1 
ATOM   1671 O  OG  . SER   A 1 232 ? -10.167 -19.836 9.772   1.00 171.88 ? 252 SER   A OG  1 
ATOM   1672 N  N   . VAL   A 1 233 ? -14.187 -21.438 11.107  1.00 177.54 ? 253 VAL   A N   1 
ATOM   1673 C  CA  . VAL   A 1 233 ? -15.642 -21.497 11.212  1.00 174.56 ? 253 VAL   A CA  1 
ATOM   1674 C  C   . VAL   A 1 233 ? -16.076 -21.288 12.657  1.00 186.67 ? 253 VAL   A C   1 
ATOM   1675 O  O   . VAL   A 1 233 ? -16.926 -20.440 12.950  1.00 190.92 ? 253 VAL   A O   1 
ATOM   1676 C  CB  . VAL   A 1 233 ? -16.172 -22.827 10.646  1.00 156.52 ? 253 VAL   A CB  1 
ATOM   1677 C  CG1 . VAL   A 1 233 ? -17.608 -23.062 11.088  1.00 155.34 ? 253 VAL   A CG1 1 
ATOM   1678 C  CG2 . VAL   A 1 233 ? -16.088 -22.830 9.127   1.00 151.31 ? 253 VAL   A CG2 1 
ATOM   1679 N  N   . LYS   A 1 234 ? -15.486 -22.046 13.586  1.00 183.00 ? 254 LYS   A N   1 
ATOM   1680 C  CA  . LYS   A 1 234 ? -15.902 -21.957 14.981  1.00 192.10 ? 254 LYS   A CA  1 
ATOM   1681 C  C   . LYS   A 1 234 ? -15.539 -20.623 15.625  1.00 200.93 ? 254 LYS   A C   1 
ATOM   1682 O  O   . LYS   A 1 234 ? -16.062 -20.317 16.702  1.00 203.95 ? 254 LYS   A O   1 
ATOM   1683 C  CB  . LYS   A 1 234 ? -15.307 -23.110 15.794  1.00 193.87 ? 254 LYS   A CB  1 
ATOM   1684 C  CG  . LYS   A 1 234 ? -13.839 -22.963 16.146  1.00 200.43 ? 254 LYS   A CG  1 
ATOM   1685 C  CD  . LYS   A 1 234 ? -13.427 -24.009 17.172  1.00 202.49 ? 254 LYS   A CD  1 
ATOM   1686 C  CE  . LYS   A 1 234 ? -14.268 -23.896 18.437  1.00 203.44 ? 254 LYS   A CE  1 
ATOM   1687 N  NZ  . LYS   A 1 234 ? -13.917 -24.933 19.446  1.00 193.54 ? 254 LYS   A NZ  1 
ATOM   1688 N  N   . ARG   A 1 235 ? -14.659 -19.831 15.007  1.00 205.41 ? 255 ARG   A N   1 
ATOM   1689 C  CA  . ARG   A 1 235 ? -14.497 -18.444 15.431  1.00 207.01 ? 255 ARG   A CA  1 
ATOM   1690 C  C   . ARG   A 1 235 ? -15.748 -17.639 15.107  1.00 210.33 ? 255 ARG   A C   1 
ATOM   1691 O  O   . ARG   A 1 235 ? -16.362 -17.032 15.992  1.00 209.65 ? 255 ARG   A O   1 
ATOM   1692 C  CB  . ARG   A 1 235 ? -13.276 -17.814 14.757  1.00 210.48 ? 255 ARG   A CB  1 
ATOM   1693 C  CG  . ARG   A 1 235 ? -11.930 -18.272 15.278  1.00 214.56 ? 255 ARG   A CG  1 
ATOM   1694 C  CD  . ARG   A 1 235 ? -10.846 -17.299 14.836  1.00 217.32 ? 255 ARG   A CD  1 
ATOM   1695 N  NE  . ARG   A 1 235 ? -9.527  -17.918 14.804  1.00 222.16 ? 255 ARG   A NE  1 
ATOM   1696 C  CZ  . ARG   A 1 235 ? -8.969  -18.428 13.714  1.00 217.11 ? 255 ARG   A CZ  1 
ATOM   1697 N  NH1 . ARG   A 1 235 ? -9.586  -18.400 12.544  1.00 214.33 ? 255 ARG   A NH1 1 
ATOM   1698 N  NH2 . ARG   A 1 235 ? -7.762  -18.978 13.801  1.00 221.99 ? 255 ARG   A NH2 1 
ATOM   1699 N  N   . MET   A 1 236 ? -16.141 -17.630 13.831  1.00 212.75 ? 256 MET   A N   1 
ATOM   1700 C  CA  . MET   A 1 236 ? -17.340 -16.908 13.422  1.00 210.33 ? 256 MET   A CA  1 
ATOM   1701 C  C   . MET   A 1 236 ? -18.593 -17.502 14.050  1.00 207.55 ? 256 MET   A C   1 
ATOM   1702 O  O   . MET   A 1 236 ? -19.560 -16.776 14.309  1.00 200.85 ? 256 MET   A O   1 
ATOM   1703 C  CB  . MET   A 1 236 ? -17.452 -16.914 11.897  1.00 202.60 ? 256 MET   A CB  1 
ATOM   1704 C  CG  . MET   A 1 236 ? -16.147 -16.603 11.182  1.00 205.34 ? 256 MET   A CG  1 
ATOM   1705 S  SD  . MET   A 1 236 ? -16.308 -16.597 9.387   1.00 205.50 ? 256 MET   A SD  1 
ATOM   1706 C  CE  . MET   A 1 236 ? -14.595 -16.398 8.903   1.00 203.65 ? 256 MET   A CE  1 
ATOM   1707 N  N   . LYS   A 1 237 ? -18.596 -18.813 14.304  1.00 212.55 ? 257 LYS   A N   1 
ATOM   1708 C  CA  . LYS   A 1 237 ? -19.750 -19.439 14.940  1.00 208.15 ? 257 LYS   A CA  1 
ATOM   1709 C  C   . LYS   A 1 237 ? -20.001 -18.850 16.322  1.00 208.69 ? 257 LYS   A C   1 
ATOM   1710 O  O   . LYS   A 1 237 ? -21.139 -18.518 16.670  1.00 207.20 ? 257 LYS   A O   1 
ATOM   1711 C  CB  . LYS   A 1 237 ? -19.550 -20.952 15.038  1.00 202.31 ? 257 LYS   A CB  1 
ATOM   1712 C  CG  . LYS   A 1 237 ? -19.703 -21.697 13.726  1.00 191.63 ? 257 LYS   A CG  1 
ATOM   1713 C  CD  . LYS   A 1 237 ? -19.932 -23.180 13.963  1.00 190.92 ? 257 LYS   A CD  1 
ATOM   1714 C  CE  . LYS   A 1 237 ? -21.229 -23.409 14.721  1.00 192.38 ? 257 LYS   A CE  1 
ATOM   1715 N  NZ  . LYS   A 1 237 ? -21.537 -24.855 14.885  1.00 185.51 ? 257 LYS   A NZ  1 
ATOM   1716 N  N   . GLU   A 1 238 ? -18.949 -18.715 17.125  1.00 206.79 ? 258 GLU   A N   1 
ATOM   1717 C  CA  . GLU   A 1 238 ? -19.089 -18.236 18.492  1.00 211.44 ? 258 GLU   A CA  1 
ATOM   1718 C  C   . GLU   A 1 238 ? -18.914 -16.729 18.620  1.00 211.18 ? 258 GLU   A C   1 
ATOM   1719 O  O   . GLU   A 1 238 ? -19.071 -16.194 19.723  1.00 204.08 ? 258 GLU   A O   1 
ATOM   1720 C  CB  . GLU   A 1 238 ? -18.095 -18.956 19.408  1.00 209.85 ? 258 GLU   A CB  1 
ATOM   1721 C  CG  . GLU   A 1 238 ? -18.729 -19.480 20.685  1.00 209.16 ? 258 GLU   A CG  1 
ATOM   1722 C  CD  . GLU   A 1 238 ? -17.760 -20.261 21.545  1.00 211.38 ? 258 GLU   A CD  1 
ATOM   1723 O  OE1 . GLU   A 1 238 ? -16.652 -20.577 21.062  1.00 217.86 ? 258 GLU   A OE1 1 
ATOM   1724 O  OE2 . GLU   A 1 238 ? -18.106 -20.558 22.708  1.00 200.52 ? 258 GLU   A OE2 1 
ATOM   1725 N  N   . SER   A 1 239 ? -18.589 -16.031 17.531  1.00 212.18 ? 259 SER   A N   1 
ATOM   1726 C  CA  . SER   A 1 239 ? -18.621 -14.573 17.559  1.00 211.61 ? 259 SER   A CA  1 
ATOM   1727 C  C   . SER   A 1 239 ? -20.039 -14.063 17.333  1.00 207.98 ? 259 SER   A C   1 
ATOM   1728 O  O   . SER   A 1 239 ? -20.502 -13.155 18.033  1.00 212.22 ? 259 SER   A O   1 
ATOM   1729 C  CB  . SER   A 1 239 ? -17.667 -13.999 16.511  1.00 213.16 ? 259 SER   A CB  1 
ATOM   1730 O  OG  . SER   A 1 239 ? -18.103 -14.306 15.198  1.00 210.86 ? 259 SER   A OG  1 
ATOM   1731 N  N   . ARG   A 1 240 ? -20.743 -14.644 16.366  1.00 207.69 ? 260 ARG   A N   1 
ATOM   1732 C  CA  . ARG   A 1 240 ? -22.133 -14.298 16.105  1.00 201.47 ? 260 ARG   A CA  1 
ATOM   1733 C  C   . ARG   A 1 240 ? -23.028 -14.795 17.235  1.00 187.57 ? 260 ARG   A C   1 
ATOM   1734 O  O   . ARG   A 1 240 ? -23.715 -14.010 17.887  1.00 174.14 ? 260 ARG   A O   1 
ATOM   1735 C  CB  . ARG   A 1 240 ? -22.597 -14.889 14.771  1.00 199.05 ? 260 ARG   A CB  1 
ATOM   1736 C  CG  . ARG   A 1 240 ? -21.709 -14.543 13.588  1.00 195.51 ? 260 ARG   A CG  1 
ATOM   1737 C  CD  . ARG   A 1 240 ? -22.268 -15.120 12.297  1.00 185.01 ? 260 ARG   A CD  1 
ATOM   1738 N  NE  . ARG   A 1 240 ? -21.364 -14.925 11.171  1.00 182.12 ? 260 ARG   A NE  1 
ATOM   1739 C  CZ  . ARG   A 1 240 ? -21.681 -15.163 9.906   1.00 165.91 ? 260 ARG   A CZ  1 
ATOM   1740 N  NH1 . ARG   A 1 240 ? -22.886 -15.589 9.564   1.00 152.12 ? 260 ARG   A NH1 1 
ATOM   1741 N  NH2 . ARG   A 1 240 ? -20.768 -14.965 8.960   1.00 159.00 ? 260 ARG   A NH2 1 
ATOM   1742 N  N   . ASP   A 1 250 ? -25.649 -15.107 4.886   1.00 161.94 ? 270 ASP   A N   1 
ATOM   1743 C  CA  . ASP   A 1 250 ? -24.796 -15.908 4.015   1.00 152.45 ? 270 ASP   A CA  1 
ATOM   1744 C  C   . ASP   A 1 250 ? -25.099 -17.398 4.149   1.00 144.59 ? 270 ASP   A C   1 
ATOM   1745 O  O   . ASP   A 1 250 ? -26.005 -17.792 4.884   1.00 146.82 ? 270 ASP   A O   1 
ATOM   1746 C  CB  . ASP   A 1 250 ? -23.321 -15.639 4.318   1.00 151.42 ? 270 ASP   A CB  1 
ATOM   1747 C  CG  . ASP   A 1 250 ? -23.079 -15.292 5.774   1.00 152.16 ? 270 ASP   A CG  1 
ATOM   1748 O  OD1 . ASP   A 1 250 ? -23.373 -16.133 6.648   1.00 152.27 ? 270 ASP   A OD1 1 
ATOM   1749 O  OD2 . ASP   A 1 250 ? -22.591 -14.175 6.042   1.00 153.74 ? 270 ASP   A OD2 1 
ATOM   1750 N  N   . PHE   A 1 251 ? -24.332 -18.218 3.425   1.00 135.71 ? 271 PHE   A N   1 
ATOM   1751 C  CA  . PHE   A 1 251 ? -24.537 -19.664 3.464   1.00 132.40 ? 271 PHE   A CA  1 
ATOM   1752 C  C   . PHE   A 1 251 ? -24.316 -20.213 4.869   1.00 131.93 ? 271 PHE   A C   1 
ATOM   1753 O  O   . PHE   A 1 251 ? -25.129 -20.995 5.375   1.00 120.74 ? 271 PHE   A O   1 
ATOM   1754 C  CB  . PHE   A 1 251 ? -23.608 -20.352 2.463   1.00 128.84 ? 271 PHE   A CB  1 
ATOM   1755 C  CG  . PHE   A 1 251 ? -24.063 -20.243 1.035   1.00 122.27 ? 271 PHE   A CG  1 
ATOM   1756 C  CD1 . PHE   A 1 251 ? -25.375 -20.515 0.688   1.00 112.36 ? 271 PHE   A CD1 1 
ATOM   1757 C  CD2 . PHE   A 1 251 ? -23.178 -19.867 0.039   1.00 116.77 ? 271 PHE   A CD2 1 
ATOM   1758 C  CE1 . PHE   A 1 251 ? -25.796 -20.421 -0.625  1.00 108.52 ? 271 PHE   A CE1 1 
ATOM   1759 C  CE2 . PHE   A 1 251 ? -23.593 -19.766 -1.276  1.00 110.51 ? 271 PHE   A CE2 1 
ATOM   1760 C  CZ  . PHE   A 1 251 ? -24.905 -20.043 -1.608  1.00 106.96 ? 271 PHE   A CZ  1 
ATOM   1761 N  N   . LEU   A 1 252 ? -23.213 -19.814 5.512   1.00 137.32 ? 272 LEU   A N   1 
ATOM   1762 C  CA  . LEU   A 1 252 ? -22.957 -20.214 6.893   1.00 130.04 ? 272 LEU   A CA  1 
ATOM   1763 C  C   . LEU   A 1 252 ? -24.143 -19.891 7.791   1.00 135.88 ? 272 LEU   A C   1 
ATOM   1764 O  O   . LEU   A 1 252 ? -24.531 -20.703 8.639   1.00 135.27 ? 272 LEU   A O   1 
ATOM   1765 C  CB  . LEU   A 1 252 ? -21.696 -19.522 7.411   1.00 135.32 ? 272 LEU   A CB  1 
ATOM   1766 C  CG  . LEU   A 1 252 ? -21.419 -19.516 8.914   1.00 134.52 ? 272 LEU   A CG  1 
ATOM   1767 C  CD1 . LEU   A 1 252 ? -21.052 -20.902 9.393   1.00 128.25 ? 272 LEU   A CD1 1 
ATOM   1768 C  CD2 . LEU   A 1 252 ? -20.316 -18.524 9.245   1.00 148.44 ? 272 LEU   A CD2 1 
ATOM   1769 N  N   . GLN   A 1 253 ? -24.732 -18.707 7.613   1.00 130.84 ? 273 GLN   A N   1 
ATOM   1770 C  CA  . GLN   A 1 253 ? -25.920 -18.335 8.372   1.00 130.67 ? 273 GLN   A CA  1 
ATOM   1771 C  C   . GLN   A 1 253 ? -27.050 -19.328 8.126   1.00 131.93 ? 273 GLN   A C   1 
ATOM   1772 O  O   . GLN   A 1 253 ? -27.521 -19.992 9.055   1.00 136.24 ? 273 GLN   A O   1 
ATOM   1773 C  CB  . GLN   A 1 253 ? -26.349 -16.913 8.008   1.00 143.72 ? 273 GLN   A CB  1 
ATOM   1774 C  CG  . GLN   A 1 253 ? -27.600 -16.430 8.706   1.00 148.66 ? 273 GLN   A CG  1 
ATOM   1775 C  CD  . GLN   A 1 253 ? -27.931 -14.997 8.345   1.00 156.31 ? 273 GLN   A CD  1 
ATOM   1776 O  OE1 . GLN   A 1 253 ? -27.223 -14.362 7.560   1.00 159.75 ? 273 GLN   A OE1 1 
ATOM   1777 N  NE2 . GLN   A 1 253 ? -29.008 -14.478 8.917   1.00 161.21 ? 273 GLN   A NE2 1 
ATOM   1778 N  N   . LEU   A 1 254 ? -27.464 -19.476 6.861   1.00 143.70 ? 274 LEU   A N   1 
ATOM   1779 C  CA  . LEU   A 1 254 ? -28.558 -20.386 6.529   1.00 138.44 ? 274 LEU   A CA  1 
ATOM   1780 C  C   . LEU   A 1 254 ? -28.274 -21.803 7.013   1.00 140.96 ? 274 LEU   A C   1 
ATOM   1781 O  O   . LEU   A 1 254 ? -29.192 -22.523 7.424   1.00 136.23 ? 274 LEU   A O   1 
ATOM   1782 C  CB  . LEU   A 1 254 ? -28.813 -20.378 5.020   1.00 122.38 ? 274 LEU   A CB  1 
ATOM   1783 C  CG  . LEU   A 1 254 ? -29.164 -19.025 4.400   1.00 123.59 ? 274 LEU   A CG  1 
ATOM   1784 C  CD1 . LEU   A 1 254 ? -29.370 -19.155 2.899   1.00 114.92 ? 274 LEU   A CD1 1 
ATOM   1785 C  CD2 . LEU   A 1 254 ? -30.399 -18.437 5.063   1.00 117.81 ? 274 LEU   A CD2 1 
ATOM   1786 N  N   . MET   A 1 255 ? -27.006 -22.217 6.983   1.00 134.66 ? 275 MET   A N   1 
ATOM   1787 C  CA  . MET   A 1 255 ? -26.652 -23.535 7.500   1.00 137.20 ? 275 MET   A CA  1 
ATOM   1788 C  C   . MET   A 1 255 ? -26.723 -23.570 9.022   1.00 140.37 ? 275 MET   A C   1 
ATOM   1789 O  O   . MET   A 1 255 ? -27.222 -24.542 9.601   1.00 143.11 ? 275 MET   A O   1 
ATOM   1790 C  CB  . MET   A 1 255 ? -25.259 -23.932 7.015   1.00 128.18 ? 275 MET   A CB  1 
ATOM   1791 C  CG  . MET   A 1 255 ? -25.161 -24.149 5.517   1.00 127.25 ? 275 MET   A CG  1 
ATOM   1792 S  SD  . MET   A 1 255 ? -23.600 -24.918 5.060   1.00 137.99 ? 275 MET   A SD  1 
ATOM   1793 C  CE  . MET   A 1 255 ? -23.666 -26.389 6.077   1.00 114.54 ? 275 MET   A CE  1 
ATOM   1794 N  N   . ILE   A 1 256 ? -26.223 -22.525 9.688   1.00 140.26 ? 276 ILE   A N   1 
ATOM   1795 C  CA  . ILE   A 1 256 ? -26.349 -22.445 11.142  1.00 147.77 ? 276 ILE   A CA  1 
ATOM   1796 C  C   . ILE   A 1 256 ? -27.817 -22.374 11.542  1.00 154.67 ? 276 ILE   A C   1 
ATOM   1797 O  O   . ILE   A 1 256 ? -28.243 -23.004 12.518  1.00 159.58 ? 276 ILE   A O   1 
ATOM   1798 C  CB  . ILE   A 1 256 ? -25.549 -21.245 11.687  1.00 141.68 ? 276 ILE   A CB  1 
ATOM   1799 C  CG1 . ILE   A 1 256 ? -24.048 -21.540 11.656  1.00 142.42 ? 276 ILE   A CG1 1 
ATOM   1800 C  CG2 . ILE   A 1 256 ? -25.990 -20.893 13.102  1.00 131.31 ? 276 ILE   A CG2 1 
ATOM   1801 C  CD1 . ILE   A 1 256 ? -23.202 -20.458 12.296  1.00 144.00 ? 276 ILE   A CD1 1 
ATOM   1802 N  N   . ASP   A 1 257 ? -28.617 -21.615 10.788  1.00 151.75 ? 277 ASP   A N   1 
ATOM   1803 C  CA  . ASP   A 1 257 ? -30.053 -21.580 11.042  1.00 152.30 ? 277 ASP   A CA  1 
ATOM   1804 C  C   . ASP   A 1 257 ? -30.689 -22.947 10.825  1.00 158.46 ? 277 ASP   A C   1 
ATOM   1805 O  O   . ASP   A 1 257 ? -31.697 -23.271 11.464  1.00 162.25 ? 277 ASP   A O   1 
ATOM   1806 C  CB  . ASP   A 1 257 ? -30.724 -20.539 10.144  1.00 153.63 ? 277 ASP   A CB  1 
ATOM   1807 C  CG  . ASP   A 1 257 ? -30.069 -19.175 10.239  1.00 151.90 ? 277 ASP   A CG  1 
ATOM   1808 O  OD1 . ASP   A 1 257 ? -29.173 -19.000 11.092  1.00 147.59 ? 277 ASP   A OD1 1 
ATOM   1809 O  OD2 . ASP   A 1 257 ? -30.442 -18.281 9.450   1.00 145.95 ? 277 ASP   A OD2 1 
ATOM   1810 N  N   . SER   A 1 258 ? -30.115 -23.760 9.935   1.00 163.93 ? 278 SER   A N   1 
ATOM   1811 C  CA  . SER   A 1 258 ? -30.676 -25.079 9.661   1.00 167.46 ? 278 SER   A CA  1 
ATOM   1812 C  C   . SER   A 1 258 ? -30.509 -26.008 10.858  1.00 168.24 ? 278 SER   A C   1 
ATOM   1813 O  O   . SER   A 1 258 ? -31.465 -26.672 11.277  1.00 167.31 ? 278 SER   A O   1 
ATOM   1814 C  CB  . SER   A 1 258 ? -30.023 -25.681 8.415   1.00 151.50 ? 278 SER   A CB  1 
ATOM   1815 O  OG  . SER   A 1 258 ? -28.661 -25.990 8.651   1.00 152.85 ? 278 SER   A OG  1 
ATOM   1816 N  N   . GLN   A 1 259 ? -29.303 -26.065 11.429  1.00 166.19 ? 279 GLN   A N   1 
ATOM   1817 C  CA  . GLN   A 1 259 ? -29.089 -26.907 12.601  1.00 160.91 ? 279 GLN   A CA  1 
ATOM   1818 C  C   . GLN   A 1 259 ? -29.809 -26.387 13.840  1.00 174.24 ? 279 GLN   A C   1 
ATOM   1819 O  O   . GLN   A 1 259 ? -29.773 -27.055 14.879  1.00 179.75 ? 279 GLN   A O   1 
ATOM   1820 C  CB  . GLN   A 1 259 ? -27.591 -27.058 12.888  1.00 158.42 ? 279 GLN   A CB  1 
ATOM   1821 C  CG  . GLN   A 1 259 ? -26.864 -25.769 13.224  1.00 158.04 ? 279 GLN   A CG  1 
ATOM   1822 C  CD  . GLN   A 1 259 ? -25.427 -26.008 13.650  1.00 159.71 ? 279 GLN   A CD  1 
ATOM   1823 O  OE1 . GLN   A 1 259 ? -24.685 -25.067 13.933  1.00 166.79 ? 279 GLN   A OE1 1 
ATOM   1824 N  NE2 . GLN   A 1 259 ? -25.028 -27.274 13.700  1.00 151.34 ? 279 GLN   A NE2 1 
ATOM   1825 N  N   . ASN   A 1 260 ? -30.454 -25.225 13.760  1.00 165.53 ? 280 ASN   A N   1 
ATOM   1826 C  CA  . ASN   A 1 260 ? -31.335 -24.760 14.824  1.00 170.42 ? 280 ASN   A CA  1 
ATOM   1827 C  C   . ASN   A 1 260 ? -32.684 -25.466 14.741  1.00 166.52 ? 280 ASN   A C   1 
ATOM   1828 O  O   . ASN   A 1 260 ? -33.579 -25.024 14.020  1.00 162.15 ? 280 ASN   A O   1 
ATOM   1829 C  CB  . ASN   A 1 260 ? -31.538 -23.246 14.750  1.00 167.64 ? 280 ASN   A CB  1 
ATOM   1830 C  CG  . ASN   A 1 260 ? -30.534 -22.482 15.584  1.00 165.29 ? 280 ASN   A CG  1 
ATOM   1831 O  OD1 . ASN   A 1 260 ? -29.871 -23.049 16.452  1.00 161.05 ? 280 ASN   A OD1 1 
ATOM   1832 N  ND2 . ASN   A 1 260 ? -30.424 -21.182 15.335  1.00 161.70 ? 280 ASN   A ND2 1 
ATOM   1833 N  N   . SER   A 1 266 ? -36.872 -33.045 10.610  1.00 164.04 ? 286 SER   A N   1 
ATOM   1834 C  CA  . SER   A 1 266 ? -36.476 -34.359 11.100  1.00 171.20 ? 286 SER   A CA  1 
ATOM   1835 C  C   . SER   A 1 266 ? -34.985 -34.593 10.885  1.00 173.68 ? 286 SER   A C   1 
ATOM   1836 O  O   . SER   A 1 266 ? -34.169 -33.701 11.127  1.00 169.61 ? 286 SER   A O   1 
ATOM   1837 C  CB  . SER   A 1 266 ? -37.289 -35.457 10.409  1.00 165.49 ? 286 SER   A CB  1 
ATOM   1838 O  OG  . SER   A 1 266 ? -37.063 -35.456 9.010   1.00 155.30 ? 286 SER   A OG  1 
ATOM   1839 N  N   . HIS   A 1 267 ? -34.643 -35.799 10.426  1.00 153.73 ? 287 HIS   A N   1 
ATOM   1840 C  CA  . HIS   A 1 267 ? -33.257 -36.223 10.197  1.00 151.58 ? 287 HIS   A CA  1 
ATOM   1841 C  C   . HIS   A 1 267 ? -32.504 -36.101 11.517  1.00 154.35 ? 287 HIS   A C   1 
ATOM   1842 O  O   . HIS   A 1 267 ? -32.948 -36.694 12.516  1.00 163.85 ? 287 HIS   A O   1 
ATOM   1843 C  CB  . HIS   A 1 267 ? -32.673 -35.438 9.018   1.00 140.65 ? 287 HIS   A CB  1 
ATOM   1844 C  CG  . HIS   A 1 267 ? -33.125 -35.931 7.678   1.00 128.54 ? 287 HIS   A CG  1 
ATOM   1845 N  ND1 . HIS   A 1 267 ? -32.906 -37.223 7.250   1.00 122.20 ? 287 HIS   A ND1 1 
ATOM   1846 C  CD2 . HIS   A 1 267 ? -33.777 -35.306 6.668   1.00 122.73 ? 287 HIS   A CD2 1 
ATOM   1847 C  CE1 . HIS   A 1 267 ? -33.408 -37.374 6.038   1.00 123.89 ? 287 HIS   A CE1 1 
ATOM   1848 N  NE2 . HIS   A 1 267 ? -33.942 -36.226 5.661   1.00 120.48 ? 287 HIS   A NE2 1 
ATOM   1849 N  N   . LYS   A 1 268 ? -31.370 -35.390 11.503  1.00 155.21 ? 288 LYS   A N   1 
ATOM   1850 C  CA  . LYS   A 1 268 ? -30.533 -35.238 12.724  1.00 166.43 ? 288 LYS   A CA  1 
ATOM   1851 C  C   . LYS   A 1 268 ? -29.854 -33.864 12.712  1.00 152.59 ? 288 LYS   A C   1 
ATOM   1852 O  O   . LYS   A 1 268 ? -28.729 -33.764 13.240  1.00 159.55 ? 288 LYS   A O   1 
ATOM   1853 C  CB  . LYS   A 1 268 ? -29.462 -36.332 12.787  1.00 160.68 ? 288 LYS   A CB  1 
ATOM   1854 C  CG  . LYS   A 1 268 ? -29.970 -37.753 12.991  1.00 165.83 ? 288 LYS   A CG  1 
ATOM   1855 C  CD  . LYS   A 1 268 ? -28.862 -38.783 13.019  1.00 168.11 ? 288 LYS   A CD  1 
ATOM   1856 C  CE  . LYS   A 1 268 ? -29.365 -40.193 13.246  1.00 160.53 ? 288 LYS   A CE  1 
ATOM   1857 N  NZ  . LYS   A 1 268 ? -28.258 -41.178 13.245  1.00 157.99 ? 288 LYS   A NZ  1 
ATOM   1858 N  N   . ALA   A 1 269 ? -30.505 -32.856 12.123  1.00 136.57 ? 289 ALA   A N   1 
ATOM   1859 C  CA  . ALA   A 1 269 ? -29.932 -31.489 12.056  1.00 140.60 ? 289 ALA   A CA  1 
ATOM   1860 C  C   . ALA   A 1 269 ? -28.584 -31.439 11.327  1.00 136.69 ? 289 ALA   A C   1 
ATOM   1861 O  O   . ALA   A 1 269 ? -28.409 -32.196 10.353  1.00 137.62 ? 289 ALA   A O   1 
ATOM   1862 C  CB  . ALA   A 1 269 ? -29.903 -30.869 13.432  1.00 135.98 ? 289 ALA   A CB  1 
ATOM   1863 N  N   . LEU   A 1 270 ? -27.665 -30.584 11.788  1.00 137.18 ? 290 LEU   A N   1 
ATOM   1864 C  CA  . LEU   A 1 270 ? -26.316 -30.515 11.161  1.00 129.11 ? 290 LEU   A CA  1 
ATOM   1865 C  C   . LEU   A 1 270 ? -25.229 -30.489 12.239  1.00 130.67 ? 290 LEU   A C   1 
ATOM   1866 O  O   . LEU   A 1 270 ? -25.476 -29.901 13.309  1.00 141.69 ? 290 LEU   A O   1 
ATOM   1867 C  CB  . LEU   A 1 270 ? -26.247 -29.261 10.286  1.00 124.73 ? 290 LEU   A CB  1 
ATOM   1868 C  CG  . LEU   A 1 270 ? -26.558 -29.484 8.807   1.00 112.67 ? 290 LEU   A CG  1 
ATOM   1869 C  CD1 . LEU   A 1 270 ? -26.310 -28.218 8.003   1.00 112.58 ? 290 LEU   A CD1 1 
ATOM   1870 C  CD2 . LEU   A 1 270 ? -25.736 -30.639 8.255   1.00 116.71 ? 290 LEU   A CD2 1 
ATOM   1871 N  N   . SER   A 1 271 ? -24.074 -31.103 11.962  1.00 132.16 ? 291 SER   A N   1 
ATOM   1872 C  CA  . SER   A 1 271 ? -22.961 -31.095 12.899  1.00 121.88 ? 291 SER   A CA  1 
ATOM   1873 C  C   . SER   A 1 271 ? -22.075 -29.870 12.679  1.00 142.32 ? 291 SER   A C   1 
ATOM   1874 O  O   . SER   A 1 271 ? -22.346 -29.009 11.837  1.00 137.54 ? 291 SER   A O   1 
ATOM   1875 C  CB  . SER   A 1 271 ? -22.150 -32.382 12.766  1.00 120.62 ? 291 SER   A CB  1 
ATOM   1876 O  OG  . SER   A 1 271 ? -20.838 -32.215 13.277  1.00 118.76 ? 291 SER   A OG  1 
ATOM   1877 N  N   . ASP   A 1 272 ? -20.993 -29.794 13.456  1.00 151.17 ? 292 ASP   A N   1 
ATOM   1878 C  CA  . ASP   A 1 272 ? -20.036 -28.700 13.350  1.00 149.12 ? 292 ASP   A CA  1 
ATOM   1879 C  C   . ASP   A 1 272 ? -18.923 -29.000 12.353  1.00 140.12 ? 292 ASP   A C   1 
ATOM   1880 O  O   . ASP   A 1 272 ? -18.524 -28.114 11.591  1.00 142.21 ? 292 ASP   A O   1 
ATOM   1881 C  CB  . ASP   A 1 272 ? -19.440 -28.388 14.726  1.00 161.85 ? 292 ASP   A CB  1 
ATOM   1882 C  CG  . ASP   A 1 272 ? -20.483 -27.902 15.712  1.00 170.46 ? 292 ASP   A CG  1 
ATOM   1883 O  OD1 . ASP   A 1 272 ? -21.411 -27.182 15.286  1.00 170.95 ? 292 ASP   A OD1 1 
ATOM   1884 O  OD2 . ASP   A 1 272 ? -20.380 -28.244 16.909  1.00 175.75 ? 292 ASP   A OD2 1 
ATOM   1885 N  N   . LEU   A 1 273 ? -18.409 -30.232 12.344  1.00 123.52 ? 293 LEU   A N   1 
ATOM   1886 C  CA  . LEU   A 1 273 ? -17.439 -30.611 11.323  1.00 119.70 ? 293 LEU   A CA  1 
ATOM   1887 C  C   . LEU   A 1 273 ? -18.092 -30.682 9.949   1.00 113.83 ? 293 LEU   A C   1 
ATOM   1888 O  O   . LEU   A 1 273 ? -17.490 -30.283 8.946   1.00 108.97 ? 293 LEU   A O   1 
ATOM   1889 C  CB  . LEU   A 1 273 ? -16.794 -31.951 11.676  1.00 114.44 ? 293 LEU   A CB  1 
ATOM   1890 C  CG  . LEU   A 1 273 ? -15.754 -32.452 10.673  1.00 114.73 ? 293 LEU   A CG  1 
ATOM   1891 C  CD1 . LEU   A 1 273 ? -14.557 -31.515 10.646  1.00 121.87 ? 293 LEU   A CD1 1 
ATOM   1892 C  CD2 . LEU   A 1 273 ? -15.324 -33.874 10.993  1.00 113.37 ? 293 LEU   A CD2 1 
ATOM   1893 N  N   . GLU   A 1 274 ? -19.327 -31.187 9.888   1.00 112.70 ? 294 GLU   A N   1 
ATOM   1894 C  CA  . GLU   A 1 274 ? -20.039 -31.256 8.617   1.00 104.47 ? 294 GLU   A CA  1 
ATOM   1895 C  C   . GLU   A 1 274 ? -20.291 -29.865 8.052   1.00 97.78  ? 294 GLU   A C   1 
ATOM   1896 O  O   . GLU   A 1 274 ? -20.124 -29.639 6.848   1.00 101.39 ? 294 GLU   A O   1 
ATOM   1897 C  CB  . GLU   A 1 274 ? -21.356 -32.010 8.798   1.00 108.47 ? 294 GLU   A CB  1 
ATOM   1898 C  CG  . GLU   A 1 274 ? -21.181 -33.444 9.266   1.00 118.29 ? 294 GLU   A CG  1 
ATOM   1899 C  CD  . GLU   A 1 274 ? -22.489 -34.094 9.669   1.00 118.59 ? 294 GLU   A CD  1 
ATOM   1900 O  OE1 . GLU   A 1 274 ? -23.557 -33.513 9.386   1.00 114.65 ? 294 GLU   A OE1 1 
ATOM   1901 O  OE2 . GLU   A 1 274 ? -22.447 -35.185 10.276  1.00 115.95 ? 294 GLU   A OE2 1 
ATOM   1902 N  N   . LEU   A 1 275 ? -20.684 -28.919 8.909   1.00 105.67 ? 295 LEU   A N   1 
ATOM   1903 C  CA  . LEU   A 1 275 ? -20.936 -27.553 8.458   1.00 105.09 ? 295 LEU   A CA  1 
ATOM   1904 C  C   . LEU   A 1 275 ? -19.698 -26.952 7.802   1.00 103.77 ? 295 LEU   A C   1 
ATOM   1905 O  O   . LEU   A 1 275 ? -19.805 -26.202 6.824   1.00 103.46 ? 295 LEU   A O   1 
ATOM   1906 C  CB  . LEU   A 1 275 ? -21.386 -26.694 9.638   1.00 116.69 ? 295 LEU   A CB  1 
ATOM   1907 C  CG  . LEU   A 1 275 ? -22.253 -25.469 9.352   1.00 121.53 ? 295 LEU   A CG  1 
ATOM   1908 C  CD1 . LEU   A 1 275 ? -23.706 -25.768 9.680   1.00 129.58 ? 295 LEU   A CD1 1 
ATOM   1909 C  CD2 . LEU   A 1 275 ? -21.757 -24.281 10.147  1.00 130.85 ? 295 LEU   A CD2 1 
ATOM   1910 N  N   . VAL   A 1 276 ? -18.514 -27.272 8.327   1.00 104.09 ? 296 VAL   A N   1 
ATOM   1911 C  CA  . VAL   A 1 276 ? -17.278 -26.782 7.725   1.00 102.71 ? 296 VAL   A CA  1 
ATOM   1912 C  C   . VAL   A 1 276 ? -17.047 -27.435 6.368   1.00 102.09 ? 296 VAL   A C   1 
ATOM   1913 O  O   . VAL   A 1 276 ? -16.643 -26.770 5.406   1.00 105.84 ? 296 VAL   A O   1 
ATOM   1914 C  CB  . VAL   A 1 276 ? -16.087 -27.020 8.668   1.00 110.88 ? 296 VAL   A CB  1 
ATOM   1915 C  CG1 . VAL   A 1 276 ? -14.816 -26.473 8.043   1.00 117.52 ? 296 VAL   A CG1 1 
ATOM   1916 C  CG2 . VAL   A 1 276 ? -16.342 -26.390 10.026  1.00 129.16 ? 296 VAL   A CG2 1 
ATOM   1917 N  N   . ALA   A 1 277 ? -17.292 -28.745 6.271   1.00 93.78  ? 297 ALA   A N   1 
ATOM   1918 C  CA  . ALA   A 1 277 ? -17.052 -29.459 5.021   1.00 92.22  ? 297 ALA   A CA  1 
ATOM   1919 C  C   . ALA   A 1 277 ? -17.888 -28.885 3.885   1.00 90.40  ? 297 ALA   A C   1 
ATOM   1920 O  O   . ALA   A 1 277 ? -17.388 -28.703 2.768   1.00 97.56  ? 297 ALA   A O   1 
ATOM   1921 C  CB  . ALA   A 1 277 ? -17.345 -30.947 5.206   1.00 89.77  ? 297 ALA   A CB  1 
ATOM   1922 N  N   . GLN   A 1 278 ? -19.161 -28.588 4.153   1.00 87.67  ? 298 GLN   A N   1 
ATOM   1923 C  CA  . GLN   A 1 278 ? -20.025 -28.023 3.121   1.00 95.04  ? 298 GLN   A CA  1 
ATOM   1924 C  C   . GLN   A 1 278 ? -19.510 -26.665 2.662   1.00 91.60  ? 298 GLN   A C   1 
ATOM   1925 O  O   . GLN   A 1 278 ? -19.473 -26.374 1.461   1.00 88.71  ? 298 GLN   A O   1 
ATOM   1926 C  CB  . GLN   A 1 278 ? -21.459 -27.901 3.639   1.00 96.99  ? 298 GLN   A CB  1 
ATOM   1927 C  CG  . GLN   A 1 278 ? -21.956 -29.090 4.445   1.00 91.66  ? 298 GLN   A CG  1 
ATOM   1928 C  CD  . GLN   A 1 278 ? -21.918 -30.390 3.673   1.00 85.42  ? 298 GLN   A CD  1 
ATOM   1929 O  OE1 . GLN   A 1 278 ? -22.085 -30.408 2.455   1.00 86.90  ? 298 GLN   A OE1 1 
ATOM   1930 N  NE2 . GLN   A 1 278 ? -21.695 -31.491 4.382   1.00 85.69  ? 298 GLN   A NE2 1 
ATOM   1931 N  N   . SER   A 1 279 ? -19.112 -25.815 3.613   1.00 92.67  ? 299 SER   A N   1 
ATOM   1932 C  CA  . SER   A 1 279 ? -18.588 -24.498 3.262   1.00 89.48  ? 299 SER   A CA  1 
ATOM   1933 C  C   . SER   A 1 279 ? -17.369 -24.616 2.356   1.00 91.62  ? 299 SER   A C   1 
ATOM   1934 O  O   . SER   A 1 279 ? -17.213 -23.839 1.407   1.00 94.24  ? 299 SER   A O   1 
ATOM   1935 C  CB  . SER   A 1 279 ? -18.239 -23.721 4.532   1.00 93.88  ? 299 SER   A CB  1 
ATOM   1936 O  OG  . SER   A 1 279 ? -19.278 -23.811 5.492   1.00 105.09 ? 299 SER   A OG  1 
ATOM   1937 N  N   . ILE   A 1 280 ? -16.500 -25.590 2.630   1.00 93.56  ? 300 ILE   A N   1 
ATOM   1938 C  CA  . ILE   A 1 280 ? -15.338 -25.826 1.779   1.00 91.58  ? 300 ILE   A CA  1 
ATOM   1939 C  C   . ILE   A 1 280 ? -15.775 -26.260 0.386   1.00 92.17  ? 300 ILE   A C   1 
ATOM   1940 O  O   . ILE   A 1 280 ? -15.214 -25.813 -0.623  1.00 95.08  ? 300 ILE   A O   1 
ATOM   1941 C  CB  . ILE   A 1 280 ? -14.410 -26.862 2.438   1.00 90.98  ? 300 ILE   A CB  1 
ATOM   1942 C  CG1 . ILE   A 1 280 ? -13.782 -26.272 3.702   1.00 97.29  ? 300 ILE   A CG1 1 
ATOM   1943 C  CG2 . ILE   A 1 280 ? -13.339 -27.336 1.463   1.00 86.67  ? 300 ILE   A CG2 1 
ATOM   1944 C  CD1 . ILE   A 1 280 ? -13.321 -27.308 4.694   1.00 106.32 ? 300 ILE   A CD1 1 
ATOM   1945 N  N   . ILE   A 1 281 ? -16.791 -27.124 0.302   1.00 93.08  ? 301 ILE   A N   1 
ATOM   1946 C  CA  . ILE   A 1 281 ? -17.269 -27.569 -1.000  1.00 93.87  ? 301 ILE   A CA  1 
ATOM   1947 C  C   . ILE   A 1 281 ? -17.993 -26.451 -1.736  1.00 87.70  ? 301 ILE   A C   1 
ATOM   1948 O  O   . ILE   A 1 281 ? -18.113 -26.504 -2.964  1.00 94.76  ? 301 ILE   A O   1 
ATOM   1949 C  CB  . ILE   A 1 281 ? -18.171 -28.811 -0.862  1.00 89.97  ? 301 ILE   A CB  1 
ATOM   1950 C  CG1 . ILE   A 1 281 ? -17.918 -29.772 -2.019  1.00 100.28 ? 301 ILE   A CG1 1 
ATOM   1951 C  CG2 . ILE   A 1 281 ? -19.643 -28.437 -0.857  1.00 90.31  ? 301 ILE   A CG2 1 
ATOM   1952 C  CD1 . ILE   A 1 281 ? -17.618 -31.162 -1.571  1.00 103.46 ? 301 ILE   A CD1 1 
ATOM   1953 N  N   . PHE   A 1 282 ? -18.473 -25.433 -1.019  1.00 85.62  ? 302 PHE   A N   1 
ATOM   1954 C  CA  . PHE   A 1 282 ? -19.098 -24.292 -1.677  1.00 89.93  ? 302 PHE   A CA  1 
ATOM   1955 C  C   . PHE   A 1 282 ? -18.051 -23.342 -2.251  1.00 93.53  ? 302 PHE   A C   1 
ATOM   1956 O  O   . PHE   A 1 282 ? -18.242 -22.791 -3.342  1.00 94.98  ? 302 PHE   A O   1 
ATOM   1957 C  CB  . PHE   A 1 282 ? -20.013 -23.551 -0.699  1.00 88.63  ? 302 PHE   A CB  1 
ATOM   1958 C  CG  . PHE   A 1 282 ? -21.209 -24.351 -0.249  1.00 86.82  ? 302 PHE   A CG  1 
ATOM   1959 C  CD1 . PHE   A 1 282 ? -21.569 -25.522 -0.896  1.00 75.52  ? 302 PHE   A CD1 1 
ATOM   1960 C  CD2 . PHE   A 1 282 ? -21.976 -23.925 0.821   1.00 100.37 ? 302 PHE   A CD2 1 
ATOM   1961 C  CE1 . PHE   A 1 282 ? -22.669 -26.251 -0.486  1.00 89.19  ? 302 PHE   A CE1 1 
ATOM   1962 C  CE2 . PHE   A 1 282 ? -23.076 -24.650 1.239   1.00 103.83 ? 302 PHE   A CE2 1 
ATOM   1963 C  CZ  . PHE   A 1 282 ? -23.423 -25.815 0.584   1.00 96.10  ? 302 PHE   A CZ  1 
ATOM   1964 N  N   . ILE   A 1 283 ? -16.944 -23.143 -1.530  1.00 88.15  ? 303 ILE   A N   1 
ATOM   1965 C  CA  . ILE   A 1 283 ? -15.853 -22.305 -2.030  1.00 93.84  ? 303 ILE   A CA  1 
ATOM   1966 C  C   . ILE   A 1 283 ? -15.247 -22.925 -3.284  1.00 90.74  ? 303 ILE   A C   1 
ATOM   1967 O  O   . ILE   A 1 283 ? -15.184 -22.294 -4.345  1.00 97.42  ? 303 ILE   A O   1 
ATOM   1968 C  CB  . ILE   A 1 283 ? -14.785 -22.100 -0.940  1.00 102.18 ? 303 ILE   A CB  1 
ATOM   1969 C  CG1 . ILE   A 1 283 ? -15.403 -21.483 0.318   1.00 97.13  ? 303 ILE   A CG1 1 
ATOM   1970 C  CG2 . ILE   A 1 283 ? -13.638 -21.240 -1.467  1.00 112.54 ? 303 ILE   A CG2 1 
ATOM   1971 C  CD1 . ILE   A 1 283 ? -14.422 -21.326 1.457   1.00 101.82 ? 303 ILE   A CD1 1 
ATOM   1972 N  N   . PHE   A 1 284 ? -14.776 -24.171 -3.165  1.00 85.04  ? 304 PHE   A N   1 
ATOM   1973 C  CA  . PHE   A 1 284 ? -14.272 -24.918 -4.313  1.00 95.58  ? 304 PHE   A CA  1 
ATOM   1974 C  C   . PHE   A 1 284 ? -15.235 -24.841 -5.490  1.00 100.40 ? 304 PHE   A C   1 
ATOM   1975 O  O   . PHE   A 1 284 ? -14.832 -24.552 -6.624  1.00 111.14 ? 304 PHE   A O   1 
ATOM   1976 C  CB  . PHE   A 1 284 ? -14.066 -26.376 -3.921  1.00 102.32 ? 304 PHE   A CB  1 
ATOM   1977 C  CG  . PHE   A 1 284 ? -12.642 -26.756 -3.635  1.00 110.96 ? 304 PHE   A CG  1 
ATOM   1978 C  CD1 . PHE   A 1 284 ? -11.791 -27.118 -4.666  1.00 108.37 ? 304 PHE   A CD1 1 
ATOM   1979 C  CD2 . PHE   A 1 284 ? -12.172 -26.809 -2.333  1.00 112.00 ? 304 PHE   A CD2 1 
ATOM   1980 C  CE1 . PHE   A 1 284 ? -10.487 -27.493 -4.405  1.00 117.39 ? 304 PHE   A CE1 1 
ATOM   1981 C  CE2 . PHE   A 1 284 ? -10.871 -27.185 -2.066  1.00 109.43 ? 304 PHE   A CE2 1 
ATOM   1982 C  CZ  . PHE   A 1 284 ? -10.027 -27.527 -3.103  1.00 115.99 ? 304 PHE   A CZ  1 
ATOM   1983 N  N   . ALA   A 1 285 ? -16.517 -25.113 -5.232  1.00 96.20  ? 305 ALA   A N   1 
ATOM   1984 C  CA  . ALA   A 1 285 ? -17.539 -25.045 -6.271  1.00 90.98  ? 305 ALA   A CA  1 
ATOM   1985 C  C   . ALA   A 1 285 ? -17.526 -23.695 -6.968  1.00 90.02  ? 305 ALA   A C   1 
ATOM   1986 O  O   . ALA   A 1 285 ? -17.211 -23.594 -8.157  1.00 95.88  ? 305 ALA   A O   1 
ATOM   1987 C  CB  . ALA   A 1 285 ? -18.922 -25.305 -5.671  1.00 83.21  ? 305 ALA   A CB  1 
ATOM   1988 N  N   . GLY   A 1 286 ? -17.866 -22.644 -6.233  1.00 90.57  ? 306 GLY   A N   1 
ATOM   1989 C  CA  . GLY   A 1 286 ? -18.025 -21.327 -6.799  1.00 95.04  ? 306 GLY   A CA  1 
ATOM   1990 C  C   . GLY   A 1 286 ? -16.756 -20.602 -7.175  1.00 107.48 ? 306 GLY   A C   1 
ATOM   1991 O  O   . GLY   A 1 286 ? -16.840 -19.469 -7.658  1.00 114.75 ? 306 GLY   A O   1 
ATOM   1992 N  N   . TYR   A 1 287 ? -15.583 -21.197 -6.976  1.00 102.19 ? 307 TYR   A N   1 
ATOM   1993 C  CA  . TYR   A 1 287 ? -14.364 -20.467 -7.315  1.00 106.61 ? 307 TYR   A CA  1 
ATOM   1994 C  C   . TYR   A 1 287 ? -13.961 -20.678 -8.764  1.00 110.34 ? 307 TYR   A C   1 
ATOM   1995 O  O   . TYR   A 1 287 ? -14.148 -19.790 -9.599  1.00 111.30 ? 307 TYR   A O   1 
ATOM   1996 C  CB  . TYR   A 1 287 ? -13.196 -20.854 -6.407  1.00 113.06 ? 307 TYR   A CB  1 
ATOM   1997 C  CG  . TYR   A 1 287 ? -11.957 -20.044 -6.725  1.00 125.13 ? 307 TYR   A CG  1 
ATOM   1998 C  CD1 . TYR   A 1 287 ? -11.916 -18.679 -6.467  1.00 128.90 ? 307 TYR   A CD1 1 
ATOM   1999 C  CD2 . TYR   A 1 287 ? -10.844 -20.632 -7.313  1.00 122.33 ? 307 TYR   A CD2 1 
ATOM   2000 C  CE1 . TYR   A 1 287 ? -10.793 -17.923 -6.768  1.00 126.02 ? 307 TYR   A CE1 1 
ATOM   2001 C  CE2 . TYR   A 1 287 ? -9.715  -19.884 -7.616  1.00 123.10 ? 307 TYR   A CE2 1 
ATOM   2002 C  CZ  . TYR   A 1 287 ? -9.696  -18.531 -7.341  1.00 129.49 ? 307 TYR   A CZ  1 
ATOM   2003 O  OH  . TYR   A 1 287 ? -8.577  -17.785 -7.640  1.00 140.90 ? 307 TYR   A OH  1 
ATOM   2004 N  N   . GLU   A 1 288 ? -13.393 -21.844 -9.068  1.00 116.37 ? 308 GLU   A N   1 
ATOM   2005 C  CA  . GLU   A 1 288 ? -12.873 -22.096 -10.404 1.00 121.28 ? 308 GLU   A CA  1 
ATOM   2006 C  C   . GLU   A 1 288 ? -13.964 -22.396 -11.423 1.00 117.55 ? 308 GLU   A C   1 
ATOM   2007 O  O   . GLU   A 1 288 ? -13.647 -22.650 -12.587 1.00 118.99 ? 308 GLU   A O   1 
ATOM   2008 C  CB  . GLU   A 1 288 ? -11.864 -23.250 -10.371 1.00 124.68 ? 308 GLU   A CB  1 
ATOM   2009 C  CG  . GLU   A 1 288 ? -10.827 -23.175 -11.482 1.00 135.54 ? 308 GLU   A CG  1 
ATOM   2010 C  CD  . GLU   A 1 288 ? -10.440 -24.537 -12.014 1.00 149.37 ? 308 GLU   A CD  1 
ATOM   2011 O  OE1 . GLU   A 1 288 ? -9.827  -25.318 -11.258 1.00 156.77 ? 308 GLU   A OE1 1 
ATOM   2012 O  OE2 . GLU   A 1 288 ? -10.755 -24.827 -13.187 1.00 150.47 ? 308 GLU   A OE2 1 
ATOM   2013 N  N   . THR   A 1 289 ? -15.234 -22.378 -11.023 1.00 107.86 ? 309 THR   A N   1 
ATOM   2014 C  CA  . THR   A 1 289 ? -16.341 -22.534 -11.963 1.00 107.97 ? 309 THR   A CA  1 
ATOM   2015 C  C   . THR   A 1 289 ? -16.902 -21.193 -12.415 1.00 102.16 ? 309 THR   A C   1 
ATOM   2016 O  O   . THR   A 1 289 ? -17.025 -20.948 -13.618 1.00 98.64  ? 309 THR   A O   1 
ATOM   2017 C  CB  . THR   A 1 289 ? -17.453 -23.383 -11.341 1.00 96.01  ? 309 THR   A CB  1 
ATOM   2018 O  OG1 . THR   A 1 289 ? -17.940 -22.751 -10.149 1.00 96.21  ? 309 THR   A OG1 1 
ATOM   2019 C  CG2 . THR   A 1 289 ? -16.932 -24.774 -11.000 1.00 94.89  ? 309 THR   A CG2 1 
ATOM   2020 N  N   . THR   A 1 290 ? -17.238 -20.317 -11.464 1.00 100.23 ? 310 THR   A N   1 
ATOM   2021 C  CA  . THR   A 1 290 ? -17.664 -18.964 -11.806 1.00 93.85  ? 310 THR   A CA  1 
ATOM   2022 C  C   . THR   A 1 290 ? -16.623 -18.256 -12.664 1.00 100.73 ? 310 THR   A C   1 
ATOM   2023 O  O   . THR   A 1 290 ? -16.963 -17.590 -13.649 1.00 101.47 ? 310 THR   A O   1 
ATOM   2024 C  CB  . THR   A 1 290 ? -17.932 -18.164 -10.528 1.00 100.22 ? 310 THR   A CB  1 
ATOM   2025 O  OG1 . THR   A 1 290 ? -19.054 -18.718 -9.829  1.00 95.89  ? 310 THR   A OG1 1 
ATOM   2026 C  CG2 . THR   A 1 290 ? -18.208 -16.700 -10.850 1.00 101.07 ? 310 THR   A CG2 1 
ATOM   2027 N  N   . SER   A 1 291 ? -15.344 -18.401 -12.312 1.00 104.79 ? 311 SER   A N   1 
ATOM   2028 C  CA  . SER   A 1 291 ? -14.280 -17.722 -13.045 1.00 105.40 ? 311 SER   A CA  1 
ATOM   2029 C  C   . SER   A 1 291 ? -14.022 -18.363 -14.404 1.00 105.91 ? 311 SER   A C   1 
ATOM   2030 O  O   . SER   A 1 291 ? -13.830 -17.650 -15.395 1.00 111.85 ? 311 SER   A O   1 
ATOM   2031 C  CB  . SER   A 1 291 ? -12.997 -17.707 -12.213 1.00 113.42 ? 311 SER   A CB  1 
ATOM   2032 O  OG  . SER   A 1 291 ? -12.493 -19.018 -12.022 1.00 116.18 ? 311 SER   A OG  1 
ATOM   2033 N  N   . SER   A 1 292 ? -14.007 -19.698 -14.475 1.00 105.21 ? 312 SER   A N   1 
ATOM   2034 C  CA  . SER   A 1 292 ? -13.711 -20.359 -15.745 1.00 106.24 ? 312 SER   A CA  1 
ATOM   2035 C  C   . SER   A 1 292 ? -14.781 -20.065 -16.788 1.00 110.14 ? 312 SER   A C   1 
ATOM   2036 O  O   . SER   A 1 292 ? -14.462 -19.794 -17.952 1.00 109.14 ? 312 SER   A O   1 
ATOM   2037 C  CB  . SER   A 1 292 ? -13.569 -21.869 -15.546 1.00 105.41 ? 312 SER   A CB  1 
ATOM   2038 O  OG  . SER   A 1 292 ? -12.402 -22.188 -14.807 1.00 121.96 ? 312 SER   A OG  1 
ATOM   2039 N  N   . VAL   A 1 293 ? -16.056 -20.115 -16.396 1.00 93.98  ? 313 VAL   A N   1 
ATOM   2040 C  CA  . VAL   A 1 293 ? -17.128 -19.860 -17.354 1.00 99.02  ? 313 VAL   A CA  1 
ATOM   2041 C  C   . VAL   A 1 293 ? -17.101 -18.407 -17.813 1.00 104.26 ? 313 VAL   A C   1 
ATOM   2042 O  O   . VAL   A 1 293 ? -17.226 -18.121 -19.009 1.00 111.66 ? 313 VAL   A O   1 
ATOM   2043 C  CB  . VAL   A 1 293 ? -18.492 -20.240 -16.752 1.00 86.20  ? 313 VAL   A CB  1 
ATOM   2044 C  CG1 . VAL   A 1 293 ? -19.606 -19.958 -17.752 1.00 86.77  ? 313 VAL   A CG1 1 
ATOM   2045 C  CG2 . VAL   A 1 293 ? -18.504 -21.704 -16.340 1.00 94.53  ? 313 VAL   A CG2 1 
ATOM   2046 N  N   . LEU   A 1 294 ? -16.928 -17.469 -16.876 1.00 99.95  ? 314 LEU   A N   1 
ATOM   2047 C  CA  . LEU   A 1 294 ? -16.896 -16.058 -17.246 1.00 99.79  ? 314 LEU   A CA  1 
ATOM   2048 C  C   . LEU   A 1 294 ? -15.742 -15.747 -18.189 1.00 106.74 ? 314 LEU   A C   1 
ATOM   2049 O  O   . LEU   A 1 294 ? -15.876 -14.886 -19.065 1.00 110.17 ? 314 LEU   A O   1 
ATOM   2050 C  CB  . LEU   A 1 294 ? -16.818 -15.182 -15.996 1.00 96.52  ? 314 LEU   A CB  1 
ATOM   2051 C  CG  . LEU   A 1 294 ? -18.150 -14.954 -15.282 1.00 92.65  ? 314 LEU   A CG  1 
ATOM   2052 C  CD1 . LEU   A 1 294 ? -17.966 -14.049 -14.076 1.00 105.29 ? 314 LEU   A CD1 1 
ATOM   2053 C  CD2 . LEU   A 1 294 ? -19.170 -14.370 -16.246 1.00 94.08  ? 314 LEU   A CD2 1 
ATOM   2054 N  N   . SER   A 1 295 ? -14.605 -16.428 -18.029 1.00 101.97 ? 315 SER   A N   1 
ATOM   2055 C  CA  . SER   A 1 295 ? -13.534 -16.299 -19.012 1.00 99.10  ? 315 SER   A CA  1 
ATOM   2056 C  C   . SER   A 1 295 ? -13.951 -16.893 -20.352 1.00 98.26  ? 315 SER   A C   1 
ATOM   2057 O  O   . SER   A 1 295 ? -13.707 -16.294 -21.407 1.00 106.96 ? 315 SER   A O   1 
ATOM   2058 C  CB  . SER   A 1 295 ? -12.261 -16.970 -18.498 1.00 110.61 ? 315 SER   A CB  1 
ATOM   2059 O  OG  . SER   A 1 295 ? -11.683 -16.234 -17.433 1.00 126.71 ? 315 SER   A OG  1 
ATOM   2060 N  N   . PHE   A 1 296 ? -14.589 -18.067 -20.328 1.00 97.98  ? 316 PHE   A N   1 
ATOM   2061 C  CA  . PHE   A 1 296 ? -15.098 -18.668 -21.557 1.00 96.22  ? 316 PHE   A CA  1 
ATOM   2062 C  C   . PHE   A 1 296 ? -16.100 -17.759 -22.254 1.00 98.71  ? 316 PHE   A C   1 
ATOM   2063 O  O   . PHE   A 1 296 ? -16.187 -17.764 -23.487 1.00 94.25  ? 316 PHE   A O   1 
ATOM   2064 C  CB  . PHE   A 1 296 ? -15.740 -20.023 -21.254 1.00 95.69  ? 316 PHE   A CB  1 
ATOM   2065 C  CG  . PHE   A 1 296 ? -14.754 -21.146 -21.104 1.00 98.29  ? 316 PHE   A CG  1 
ATOM   2066 C  CD1 . PHE   A 1 296 ? -13.743 -21.328 -22.033 1.00 99.49  ? 316 PHE   A CD1 1 
ATOM   2067 C  CD2 . PHE   A 1 296 ? -14.837 -22.021 -20.033 1.00 93.75  ? 316 PHE   A CD2 1 
ATOM   2068 C  CE1 . PHE   A 1 296 ? -12.836 -22.360 -21.897 1.00 105.20 ? 316 PHE   A CE1 1 
ATOM   2069 C  CE2 . PHE   A 1 296 ? -13.930 -23.054 -19.891 1.00 100.05 ? 316 PHE   A CE2 1 
ATOM   2070 C  CZ  . PHE   A 1 296 ? -12.929 -23.224 -20.825 1.00 104.48 ? 316 PHE   A CZ  1 
ATOM   2071 N  N   . ILE   A 1 297 ? -16.862 -16.975 -21.490 1.00 93.53  ? 317 ILE   A N   1 
ATOM   2072 C  CA  . ILE   A 1 297 ? -17.847 -16.086 -22.096 1.00 92.14  ? 317 ILE   A CA  1 
ATOM   2073 C  C   . ILE   A 1 297 ? -17.172 -14.873 -22.724 1.00 97.99  ? 317 ILE   A C   1 
ATOM   2074 O  O   . ILE   A 1 297 ? -17.517 -14.469 -23.839 1.00 102.69 ? 317 ILE   A O   1 
ATOM   2075 C  CB  . ILE   A 1 297 ? -18.907 -15.675 -21.058 1.00 95.60  ? 317 ILE   A CB  1 
ATOM   2076 C  CG1 . ILE   A 1 297 ? -19.712 -16.898 -20.610 1.00 95.26  ? 317 ILE   A CG1 1 
ATOM   2077 C  CG2 . ILE   A 1 297 ? -19.831 -14.614 -21.631 1.00 97.19  ? 317 ILE   A CG2 1 
ATOM   2078 C  CD1 . ILE   A 1 297 ? -20.810 -16.590 -19.617 1.00 93.14  ? 317 ILE   A CD1 1 
ATOM   2079 N  N   . MET   A 1 298 ? -16.197 -14.276 -22.031 1.00 97.12  ? 318 MET   A N   1 
ATOM   2080 C  CA  . MET   A 1 298 ? -15.535 -13.095 -22.579 1.00 103.17 ? 318 MET   A CA  1 
ATOM   2081 C  C   . MET   A 1 298 ? -14.736 -13.436 -23.829 1.00 105.83 ? 318 MET   A C   1 
ATOM   2082 O  O   . MET   A 1 298 ? -14.694 -12.643 -24.777 1.00 101.34 ? 318 MET   A O   1 
ATOM   2083 C  CB  . MET   A 1 298 ? -14.633 -12.449 -21.531 1.00 103.43 ? 318 MET   A CB  1 
ATOM   2084 C  CG  . MET   A 1 298 ? -15.364 -11.986 -20.296 1.00 102.44 ? 318 MET   A CG  1 
ATOM   2085 S  SD  . MET   A 1 298 ? -17.084 -11.577 -20.627 1.00 117.83 ? 318 MET   A SD  1 
ATOM   2086 C  CE  . MET   A 1 298 ? -16.926 -9.982  -21.422 1.00 112.60 ? 318 MET   A CE  1 
ATOM   2087 N  N   . TYR   A 1 299 ? -14.087 -14.602 -23.847 1.00 107.31 ? 319 TYR   A N   1 
ATOM   2088 C  CA  . TYR   A 1 299 ? -13.434 -15.056 -25.070 1.00 105.16 ? 319 TYR   A CA  1 
ATOM   2089 C  C   . TYR   A 1 299 ? -14.438 -15.152 -26.211 1.00 107.37 ? 319 TYR   A C   1 
ATOM   2090 O  O   . TYR   A 1 299 ? -14.181 -14.677 -27.323 1.00 106.64 ? 319 TYR   A O   1 
ATOM   2091 C  CB  . TYR   A 1 299 ? -12.749 -16.406 -24.842 1.00 102.32 ? 319 TYR   A CB  1 
ATOM   2092 C  CG  . TYR   A 1 299 ? -12.278 -17.060 -26.124 1.00 106.88 ? 319 TYR   A CG  1 
ATOM   2093 C  CD1 . TYR   A 1 299 ? -13.088 -17.962 -26.806 1.00 106.95 ? 319 TYR   A CD1 1 
ATOM   2094 C  CD2 . TYR   A 1 299 ? -11.030 -16.769 -26.658 1.00 112.19 ? 319 TYR   A CD2 1 
ATOM   2095 C  CE1 . TYR   A 1 299 ? -12.669 -18.553 -27.980 1.00 109.95 ? 319 TYR   A CE1 1 
ATOM   2096 C  CE2 . TYR   A 1 299 ? -10.600 -17.359 -27.833 1.00 116.87 ? 319 TYR   A CE2 1 
ATOM   2097 C  CZ  . TYR   A 1 299 ? -11.426 -18.249 -28.489 1.00 117.09 ? 319 TYR   A CZ  1 
ATOM   2098 O  OH  . TYR   A 1 299 ? -11.007 -18.842 -29.657 1.00 118.20 ? 319 TYR   A OH  1 
ATOM   2099 N  N   . GLU   A 1 300 ? -15.597 -15.760 -25.947 1.00 101.32 ? 320 GLU   A N   1 
ATOM   2100 C  CA  . GLU   A 1 300 ? -16.597 -15.930 -26.996 1.00 98.67  ? 320 GLU   A CA  1 
ATOM   2101 C  C   . GLU   A 1 300 ? -17.206 -14.595 -27.408 1.00 100.45 ? 320 GLU   A C   1 
ATOM   2102 O  O   . GLU   A 1 300 ? -17.467 -14.369 -28.595 1.00 104.49 ? 320 GLU   A O   1 
ATOM   2103 C  CB  . GLU   A 1 300 ? -17.681 -16.903 -26.534 1.00 101.55 ? 320 GLU   A CB  1 
ATOM   2104 C  CG  . GLU   A 1 300 ? -17.213 -18.348 -26.473 1.00 98.04  ? 320 GLU   A CG  1 
ATOM   2105 C  CD  . GLU   A 1 300 ? -16.669 -18.837 -27.801 1.00 107.63 ? 320 GLU   A CD  1 
ATOM   2106 O  OE1 . GLU   A 1 300 ? -17.221 -18.447 -28.851 1.00 106.23 ? 320 GLU   A OE1 1 
ATOM   2107 O  OE2 . GLU   A 1 300 ? -15.683 -19.603 -27.797 1.00 111.86 ? 320 GLU   A OE2 1 
ATOM   2108 N  N   . LEU   A 1 301 ? -17.440 -13.699 -26.446 1.00 106.12 ? 321 LEU   A N   1 
ATOM   2109 C  CA  . LEU   A 1 301 ? -17.952 -12.376 -26.790 1.00 108.04 ? 321 LEU   A CA  1 
ATOM   2110 C  C   . LEU   A 1 301 ? -16.927 -11.580 -27.589 1.00 115.14 ? 321 LEU   A C   1 
ATOM   2111 O  O   . LEU   A 1 301 ? -17.288 -10.855 -28.523 1.00 121.47 ? 321 LEU   A O   1 
ATOM   2112 C  CB  . LEU   A 1 301 ? -18.352 -11.613 -25.527 1.00 103.95 ? 321 LEU   A CB  1 
ATOM   2113 C  CG  . LEU   A 1 301 ? -19.516 -12.153 -24.692 1.00 97.82  ? 321 LEU   A CG  1 
ATOM   2114 C  CD1 . LEU   A 1 301 ? -19.834 -11.202 -23.548 1.00 91.65  ? 321 LEU   A CD1 1 
ATOM   2115 C  CD2 . LEU   A 1 301 ? -20.746 -12.395 -25.552 1.00 100.66 ? 321 LEU   A CD2 1 
ATOM   2116 N  N   . ALA   A 1 302 ? -15.644 -11.704 -27.238 1.00 119.31 ? 322 ALA   A N   1 
ATOM   2117 C  CA  . ALA   A 1 302 ? -14.608 -10.968 -27.957 1.00 123.07 ? 322 ALA   A CA  1 
ATOM   2118 C  C   . ALA   A 1 302 ? -14.449 -11.483 -29.381 1.00 121.13 ? 322 ALA   A C   1 
ATOM   2119 O  O   . ALA   A 1 302 ? -14.308 -10.691 -30.321 1.00 127.07 ? 322 ALA   A O   1 
ATOM   2120 C  CB  . ALA   A 1 302 ? -13.280 -11.054 -27.205 1.00 131.82 ? 322 ALA   A CB  1 
ATOM   2121 N  N   . THR   A 1 303 ? -14.469 -12.801 -29.564 1.00 115.99 ? 323 THR   A N   1 
ATOM   2122 C  CA  . THR   A 1 303 ? -14.386 -13.384 -30.898 1.00 109.96 ? 323 THR   A CA  1 
ATOM   2123 C  C   . THR   A 1 303 ? -15.705 -13.312 -31.656 1.00 119.47 ? 323 THR   A C   1 
ATOM   2124 O  O   . THR   A 1 303 ? -15.789 -13.838 -32.771 1.00 118.89 ? 323 THR   A O   1 
ATOM   2125 C  CB  . THR   A 1 303 ? -13.924 -14.841 -30.811 1.00 114.55 ? 323 THR   A CB  1 
ATOM   2126 O  OG1 . THR   A 1 303 ? -14.899 -15.610 -30.096 1.00 104.10 ? 323 THR   A OG1 1 
ATOM   2127 C  CG2 . THR   A 1 303 ? -12.584 -14.934 -30.095 1.00 121.07 ? 323 THR   A CG2 1 
ATOM   2128 N  N   . HIS   A 1 304 ? -16.732 -12.694 -31.075 1.00 117.78 ? 324 HIS   A N   1 
ATOM   2129 C  CA  . HIS   A 1 304 ? -18.016 -12.480 -31.744 1.00 117.43 ? 324 HIS   A CA  1 
ATOM   2130 C  C   . HIS   A 1 304 ? -18.544 -11.120 -31.315 1.00 113.29 ? 324 HIS   A C   1 
ATOM   2131 O  O   . HIS   A 1 304 ? -19.450 -11.019 -30.479 1.00 113.00 ? 324 HIS   A O   1 
ATOM   2132 C  CB  . HIS   A 1 304 ? -19.013 -13.591 -31.407 1.00 114.48 ? 324 HIS   A CB  1 
ATOM   2133 C  CG  . HIS   A 1 304 ? -18.580 -14.951 -31.858 1.00 112.71 ? 324 HIS   A CG  1 
ATOM   2134 N  ND1 . HIS   A 1 304 ? -17.616 -15.684 -31.201 1.00 111.58 ? 324 HIS   A ND1 1 
ATOM   2135 C  CD2 . HIS   A 1 304 ? -18.988 -15.715 -32.899 1.00 112.65 ? 324 HIS   A CD2 1 
ATOM   2136 C  CE1 . HIS   A 1 304 ? -17.445 -16.838 -31.820 1.00 110.22 ? 324 HIS   A CE1 1 
ATOM   2137 N  NE2 . HIS   A 1 304 ? -18.266 -16.882 -32.853 1.00 116.74 ? 324 HIS   A NE2 1 
ATOM   2138 N  N   . PRO   A 1 305 ? -17.987 -10.038 -31.869 1.00 126.95 ? 325 PRO   A N   1 
ATOM   2139 C  CA  . PRO   A 1 305 ? -18.373 -8.695  -31.402 1.00 129.42 ? 325 PRO   A CA  1 
ATOM   2140 C  C   . PRO   A 1 305 ? -19.836 -8.375  -31.633 1.00 126.06 ? 325 PRO   A C   1 
ATOM   2141 O  O   . PRO   A 1 305 ? -20.393 -7.529  -30.922 1.00 113.78 ? 325 PRO   A O   1 
ATOM   2142 C  CB  . PRO   A 1 305 ? -17.460 -7.763  -32.213 1.00 118.36 ? 325 PRO   A CB  1 
ATOM   2143 C  CG  . PRO   A 1 305 ? -16.356 -8.642  -32.734 1.00 118.28 ? 325 PRO   A CG  1 
ATOM   2144 C  CD  . PRO   A 1 305 ? -16.976 -9.986  -32.936 1.00 128.13 ? 325 PRO   A CD  1 
ATOM   2145 N  N   . ASP   A 1 306 ? -20.472 -9.022  -32.610 1.00 128.15 ? 326 ASP   A N   1 
ATOM   2146 C  CA  . ASP   A 1 306 ? -21.900 -8.825  -32.834 1.00 123.72 ? 326 ASP   A CA  1 
ATOM   2147 C  C   . ASP   A 1 306 ? -22.710 -9.264  -31.620 1.00 118.96 ? 326 ASP   A C   1 
ATOM   2148 O  O   . ASP   A 1 306 ? -23.589 -8.534  -31.147 1.00 116.63 ? 326 ASP   A O   1 
ATOM   2149 C  CB  . ASP   A 1 306 ? -22.331 -9.592  -34.081 1.00 127.39 ? 326 ASP   A CB  1 
ATOM   2150 C  CG  . ASP   A 1 306 ? -21.569 -10.892 -34.248 1.00 134.64 ? 326 ASP   A CG  1 
ATOM   2151 O  OD1 . ASP   A 1 306 ? -20.329 -10.879 -34.094 1.00 138.97 ? 326 ASP   A OD1 1 
ATOM   2152 O  OD2 . ASP   A 1 306 ? -22.209 -11.928 -34.522 1.00 138.67 ? 326 ASP   A OD2 1 
ATOM   2153 N  N   . VAL   A 1 307 ? -22.421 -10.460 -31.101 1.00 122.56 ? 327 VAL   A N   1 
ATOM   2154 C  CA  . VAL   A 1 307 ? -23.116 -10.950 -29.913 1.00 105.93 ? 327 VAL   A CA  1 
ATOM   2155 C  C   . VAL   A 1 307 ? -22.860 -10.026 -28.731 1.00 111.49 ? 327 VAL   A C   1 
ATOM   2156 O  O   . VAL   A 1 307 ? -23.754 -9.774  -27.912 1.00 110.89 ? 327 VAL   A O   1 
ATOM   2157 C  CB  . VAL   A 1 307 ? -22.684 -12.395 -29.604 1.00 105.66 ? 327 VAL   A CB  1 
ATOM   2158 C  CG1 . VAL   A 1 307 ? -23.531 -12.981 -28.485 1.00 111.74 ? 327 VAL   A CG1 1 
ATOM   2159 C  CG2 . VAL   A 1 307 ? -22.770 -13.252 -30.857 1.00 98.55  ? 327 VAL   A CG2 1 
ATOM   2160 N  N   . GLN   A 1 308 ? -21.637 -9.502  -28.627 1.00 111.31 ? 328 GLN   A N   1 
ATOM   2161 C  CA  . GLN   A 1 308 ? -21.315 -8.575  -27.548 1.00 114.92 ? 328 GLN   A CA  1 
ATOM   2162 C  C   . GLN   A 1 308 ? -22.147 -7.303  -27.650 1.00 114.84 ? 328 GLN   A C   1 
ATOM   2163 O  O   . GLN   A 1 308 ? -22.612 -6.774  -26.634 1.00 113.40 ? 328 GLN   A O   1 
ATOM   2164 C  CB  . GLN   A 1 308 ? -19.819 -8.255  -27.573 1.00 105.52 ? 328 GLN   A CB  1 
ATOM   2165 C  CG  . GLN   A 1 308 ? -19.323 -7.446  -26.390 1.00 106.09 ? 328 GLN   A CG  1 
ATOM   2166 C  CD  . GLN   A 1 308 ? -17.813 -7.306  -26.381 1.00 115.32 ? 328 GLN   A CD  1 
ATOM   2167 O  OE1 . GLN   A 1 308 ? -17.258 -6.491  -25.644 1.00 121.45 ? 328 GLN   A OE1 1 
ATOM   2168 N  NE2 . GLN   A 1 308 ? -17.140 -8.105  -27.201 1.00 107.41 ? 328 GLN   A NE2 1 
ATOM   2169 N  N   . GLN   A 1 309 ? -22.359 -6.805  -28.870 1.00 119.19 ? 329 GLN   A N   1 
ATOM   2170 C  CA  . GLN   A 1 309 ? -23.173 -5.606  -29.043 1.00 114.21 ? 329 GLN   A CA  1 
ATOM   2171 C  C   . GLN   A 1 309 ? -24.641 -5.887  -28.742 1.00 118.39 ? 329 GLN   A C   1 
ATOM   2172 O  O   . GLN   A 1 309 ? -25.283 -5.138  -27.998 1.00 113.33 ? 329 GLN   A O   1 
ATOM   2173 C  CB  . GLN   A 1 309 ? -23.008 -5.051  -30.458 1.00 127.71 ? 329 GLN   A CB  1 
ATOM   2174 C  CG  . GLN   A 1 309 ? -23.980 -3.930  -30.781 1.00 126.88 ? 329 GLN   A CG  1 
ATOM   2175 C  CD  . GLN   A 1 309 ? -23.556 -3.111  -31.982 1.00 127.76 ? 329 GLN   A CD  1 
ATOM   2176 O  OE1 . GLN   A 1 309 ? -22.381 -3.079  -32.344 1.00 129.16 ? 329 GLN   A OE1 1 
ATOM   2177 N  NE2 . GLN   A 1 309 ? -24.516 -2.439  -32.607 1.00 131.04 ? 329 GLN   A NE2 1 
ATOM   2178 N  N   . LYS   A 1 310 ? -25.189 -6.968  -29.308 1.00 124.36 ? 330 LYS   A N   1 
ATOM   2179 C  CA  . LYS   A 1 310 ? -26.583 -7.313  -29.039 1.00 122.39 ? 330 LYS   A CA  1 
ATOM   2180 C  C   . LYS   A 1 310 ? -26.823 -7.559  -27.555 1.00 121.61 ? 330 LYS   A C   1 
ATOM   2181 O  O   . LYS   A 1 310 ? -27.908 -7.257  -27.044 1.00 123.00 ? 330 LYS   A O   1 
ATOM   2182 C  CB  . LYS   A 1 310 ? -26.993 -8.538  -29.858 1.00 120.19 ? 330 LYS   A CB  1 
ATOM   2183 C  CG  . LYS   A 1 310 ? -28.481 -8.854  -29.777 1.00 125.08 ? 330 LYS   A CG  1 
ATOM   2184 C  CD  . LYS   A 1 310 ? -28.884 -9.953  -30.740 1.00 127.71 ? 330 LYS   A CD  1 
ATOM   2185 C  CE  . LYS   A 1 310 ? -30.385 -10.176 -30.714 1.00 125.11 ? 330 LYS   A CE  1 
ATOM   2186 N  NZ  . LYS   A 1 310 ? -30.804 -11.268 -31.633 1.00 123.95 ? 330 LYS   A NZ  1 
ATOM   2187 N  N   . LEU   A 1 311 ? -25.828 -8.097  -26.849 1.00 110.20 ? 331 LEU   A N   1 
ATOM   2188 C  CA  . LEU   A 1 311 ? -25.944 -8.245  -25.403 1.00 118.16 ? 331 LEU   A CA  1 
ATOM   2189 C  C   . LEU   A 1 311 ? -25.869 -6.889  -24.714 1.00 123.01 ? 331 LEU   A C   1 
ATOM   2190 O  O   . LEU   A 1 311 ? -26.670 -6.590  -23.821 1.00 123.46 ? 331 LEU   A O   1 
ATOM   2191 C  CB  . LEU   A 1 311 ? -24.855 -9.185  -24.883 1.00 105.56 ? 331 LEU   A CB  1 
ATOM   2192 C  CG  . LEU   A 1 311 ? -24.843 -9.541  -23.395 1.00 112.63 ? 331 LEU   A CG  1 
ATOM   2193 C  CD1 . LEU   A 1 311 ? -26.249 -9.789  -22.880 1.00 111.88 ? 331 LEU   A CD1 1 
ATOM   2194 C  CD2 . LEU   A 1 311 ? -23.978 -10.771 -23.170 1.00 106.22 ? 331 LEU   A CD2 1 
ATOM   2195 N  N   . GLN   A 1 312 ? -24.909 -6.051  -25.119 1.00 120.40 ? 332 GLN   A N   1 
ATOM   2196 C  CA  . GLN   A 1 312 ? -24.814 -4.706  -24.562 1.00 118.25 ? 332 GLN   A CA  1 
ATOM   2197 C  C   . GLN   A 1 312 ? -26.065 -3.888  -24.854 1.00 120.44 ? 332 GLN   A C   1 
ATOM   2198 O  O   . GLN   A 1 312 ? -26.443 -3.026  -24.053 1.00 122.66 ? 332 GLN   A O   1 
ATOM   2199 C  CB  . GLN   A 1 312 ? -23.577 -3.993  -25.108 1.00 117.89 ? 332 GLN   A CB  1 
ATOM   2200 C  CG  . GLN   A 1 312 ? -22.263 -4.453  -24.493 1.00 122.00 ? 332 GLN   A CG  1 
ATOM   2201 C  CD  . GLN   A 1 312 ? -21.060 -3.770  -25.117 1.00 130.73 ? 332 GLN   A CD  1 
ATOM   2202 O  OE1 . GLN   A 1 312 ? -21.160 -3.165  -26.184 1.00 128.19 ? 332 GLN   A OE1 1 
ATOM   2203 N  NE2 . GLN   A 1 312 ? -19.915 -3.861  -24.450 1.00 126.59 ? 332 GLN   A NE2 1 
ATOM   2204 N  N   . GLU   A 1 313 ? -26.719 -4.140  -25.991 1.00 118.52 ? 333 GLU   A N   1 
ATOM   2205 C  CA  . GLU   A 1 313 ? -27.971 -3.454  -26.293 1.00 121.94 ? 333 GLU   A CA  1 
ATOM   2206 C  C   . GLU   A 1 313 ? -29.072 -3.873  -25.327 1.00 120.82 ? 333 GLU   A C   1 
ATOM   2207 O  O   . GLU   A 1 313 ? -29.813 -3.028  -24.809 1.00 120.55 ? 333 GLU   A O   1 
ATOM   2208 C  CB  . GLU   A 1 313 ? -28.390 -3.735  -27.737 1.00 131.76 ? 333 GLU   A CB  1 
ATOM   2209 C  CG  . GLU   A 1 313 ? -27.516 -3.072  -28.786 1.00 126.91 ? 333 GLU   A CG  1 
ATOM   2210 C  CD  . GLU   A 1 313 ? -27.819 -3.564  -30.187 1.00 129.28 ? 333 GLU   A CD  1 
ATOM   2211 O  OE1 . GLU   A 1 313 ? -28.751 -4.381  -30.343 1.00 144.71 ? 333 GLU   A OE1 1 
ATOM   2212 O  OE2 . GLU   A 1 313 ? -27.124 -3.136  -31.132 1.00 130.22 ? 333 GLU   A OE2 1 
ATOM   2213 N  N   . GLU   A 1 314 ? -29.195 -5.178  -25.075 1.00 130.66 ? 334 GLU   A N   1 
ATOM   2214 C  CA  . GLU   A 1 314 ? -30.223 -5.667  -24.160 1.00 129.63 ? 334 GLU   A CA  1 
ATOM   2215 C  C   . GLU   A 1 314 ? -29.979 -5.176  -22.739 1.00 132.65 ? 334 GLU   A C   1 
ATOM   2216 O  O   . GLU   A 1 314 ? -30.924 -4.819  -22.026 1.00 136.32 ? 334 GLU   A O   1 
ATOM   2217 C  CB  . GLU   A 1 314 ? -30.274 -7.195  -24.206 1.00 137.68 ? 334 GLU   A CB  1 
ATOM   2218 C  CG  . GLU   A 1 314 ? -31.078 -7.839  -23.088 1.00 142.18 ? 334 GLU   A CG  1 
ATOM   2219 C  CD  . GLU   A 1 314 ? -31.428 -9.283  -23.390 1.00 130.32 ? 334 GLU   A CD  1 
ATOM   2220 O  OE1 . GLU   A 1 314 ? -32.284 -9.513  -24.270 1.00 133.23 ? 334 GLU   A OE1 1 
ATOM   2221 O  OE2 . GLU   A 1 314 ? -30.841 -10.187 -22.761 1.00 123.05 ? 334 GLU   A OE2 1 
ATOM   2222 N  N   . ILE   A 1 315 ? -28.715 -5.146  -22.313 1.00 128.97 ? 335 ILE   A N   1 
ATOM   2223 C  CA  . ILE   A 1 315 ? -28.393 -4.688  -20.966 1.00 132.87 ? 335 ILE   A CA  1 
ATOM   2224 C  C   . ILE   A 1 315 ? -28.716 -3.206  -20.811 1.00 134.93 ? 335 ILE   A C   1 
ATOM   2225 O  O   . ILE   A 1 315 ? -29.249 -2.778  -19.781 1.00 136.05 ? 335 ILE   A O   1 
ATOM   2226 C  CB  . ILE   A 1 315 ? -26.919 -4.990  -20.644 1.00 128.88 ? 335 ILE   A CB  1 
ATOM   2227 C  CG1 . ILE   A 1 315 ? -26.663 -6.498  -20.683 1.00 121.61 ? 335 ILE   A CG1 1 
ATOM   2228 C  CG2 . ILE   A 1 315 ? -26.548 -4.439  -19.285 1.00 127.38 ? 335 ILE   A CG2 1 
ATOM   2229 C  CD1 . ILE   A 1 315 ? -25.198 -6.869  -20.660 1.00 118.38 ? 335 ILE   A CD1 1 
ATOM   2230 N  N   . ASP   A 1 316 ? -28.411 -2.402  -21.833 1.00 130.06 ? 336 ASP   A N   1 
ATOM   2231 C  CA  . ASP   A 1 316 ? -28.704 -0.974  -21.759 1.00 129.80 ? 336 ASP   A CA  1 
ATOM   2232 C  C   . ASP   A 1 316 ? -30.205 -0.712  -21.800 1.00 134.99 ? 336 ASP   A C   1 
ATOM   2233 O  O   . ASP   A 1 316 ? -30.698 0.202   -21.130 1.00 133.80 ? 336 ASP   A O   1 
ATOM   2234 C  CB  . ASP   A 1 316 ? -28.005 -0.233  -22.900 1.00 133.65 ? 336 ASP   A CB  1 
ATOM   2235 C  CG  . ASP   A 1 316 ? -26.494 -0.298  -22.799 1.00 129.62 ? 336 ASP   A CG  1 
ATOM   2236 O  OD1 . ASP   A 1 316 ? -25.984 -0.700  -21.732 1.00 121.41 ? 336 ASP   A OD1 1 
ATOM   2237 O  OD2 . ASP   A 1 316 ? -25.815 0.044   -23.791 1.00 123.57 ? 336 ASP   A OD2 1 
ATOM   2238 N  N   . ALA   A 1 317 ? -30.946 -1.503  -22.578 1.00 135.00 ? 337 ALA   A N   1 
ATOM   2239 C  CA  . ALA   A 1 317 ? -32.378 -1.263  -22.729 1.00 120.51 ? 337 ALA   A CA  1 
ATOM   2240 C  C   . ALA   A 1 317 ? -33.129 -1.564  -21.437 1.00 133.27 ? 337 ALA   A C   1 
ATOM   2241 O  O   . ALA   A 1 317 ? -33.986 -0.782  -21.009 1.00 138.35 ? 337 ALA   A O   1 
ATOM   2242 C  CB  . ALA   A 1 317 ? -32.932 -2.101  -23.882 1.00 119.66 ? 337 ALA   A CB  1 
ATOM   2243 N  N   . VAL   A 1 318 ? -32.826 -2.699  -20.806 1.00 132.40 ? 338 VAL   A N   1 
ATOM   2244 C  CA  . VAL   A 1 318 ? -33.520 -3.067  -19.576 1.00 130.73 ? 338 VAL   A CA  1 
ATOM   2245 C  C   . VAL   A 1 318 ? -32.991 -2.271  -18.387 1.00 137.79 ? 338 VAL   A C   1 
ATOM   2246 O  O   . VAL   A 1 318 ? -33.749 -1.947  -17.464 1.00 140.79 ? 338 VAL   A O   1 
ATOM   2247 C  CB  . VAL   A 1 318 ? -33.407 -4.584  -19.345 1.00 135.26 ? 338 VAL   A CB  1 
ATOM   2248 C  CG1 . VAL   A 1 318 ? -34.053 -4.981  -18.029 1.00 135.48 ? 338 VAL   A CG1 1 
ATOM   2249 C  CG2 . VAL   A 1 318 ? -34.047 -5.340  -20.500 1.00 127.58 ? 338 VAL   A CG2 1 
ATOM   2250 N  N   . LEU   A 1 319 ? -31.702 -1.924  -18.392 1.00 133.34 ? 339 LEU   A N   1 
ATOM   2251 C  CA  . LEU   A 1 319 ? -31.078 -1.133  -17.333 1.00 142.27 ? 339 LEU   A CA  1 
ATOM   2252 C  C   . LEU   A 1 319 ? -30.556 0.163   -17.943 1.00 146.78 ? 339 LEU   A C   1 
ATOM   2253 O  O   . LEU   A 1 319 ? -29.353 0.290   -18.218 1.00 147.38 ? 339 LEU   A O   1 
ATOM   2254 C  CB  . LEU   A 1 319 ? -29.955 -1.908  -16.651 1.00 144.99 ? 339 LEU   A CB  1 
ATOM   2255 C  CG  . LEU   A 1 319 ? -30.325 -3.290  -16.118 1.00 139.47 ? 339 LEU   A CG  1 
ATOM   2256 C  CD1 . LEU   A 1 319 ? -29.093 -3.969  -15.575 1.00 138.77 ? 339 LEU   A CD1 1 
ATOM   2257 C  CD2 . LEU   A 1 319 ? -31.401 -3.193  -15.048 1.00 136.93 ? 339 LEU   A CD2 1 
ATOM   2258 N  N   . PRO   A 1 320 ? -31.427 1.145   -18.166 1.00 151.85 ? 340 PRO   A N   1 
ATOM   2259 C  CA  . PRO   A 1 320 ? -30.983 2.390   -18.801 1.00 153.67 ? 340 PRO   A CA  1 
ATOM   2260 C  C   . PRO   A 1 320 ? -30.040 3.178   -17.906 1.00 163.34 ? 340 PRO   A C   1 
ATOM   2261 O  O   . PRO   A 1 320 ? -30.151 3.161   -16.678 1.00 164.97 ? 340 PRO   A O   1 
ATOM   2262 C  CB  . PRO   A 1 320 ? -32.292 3.153   -19.040 1.00 145.31 ? 340 PRO   A CB  1 
ATOM   2263 C  CG  . PRO   A 1 320 ? -33.243 2.597   -18.026 1.00 149.24 ? 340 PRO   A CG  1 
ATOM   2264 C  CD  . PRO   A 1 320 ? -32.868 1.155   -17.860 1.00 147.16 ? 340 PRO   A CD  1 
ATOM   2265 N  N   . ASN   A 1 321 ? -29.096 3.872   -18.550 1.00 170.20 ? 341 ASN   A N   1 
ATOM   2266 C  CA  . ASN   A 1 321 ? -28.089 4.688   -17.867 1.00 174.83 ? 341 ASN   A CA  1 
ATOM   2267 C  C   . ASN   A 1 321 ? -27.188 3.836   -16.976 1.00 168.49 ? 341 ASN   A C   1 
ATOM   2268 O  O   . ASN   A 1 321 ? -26.753 4.277   -15.909 1.00 167.14 ? 341 ASN   A O   1 
ATOM   2269 C  CB  . ASN   A 1 321 ? -28.733 5.812   -17.047 1.00 176.91 ? 341 ASN   A CB  1 
ATOM   2270 C  CG  . ASN   A 1 321 ? -29.656 6.685   -17.876 1.00 174.94 ? 341 ASN   A CG  1 
ATOM   2271 O  OD1 . ASN   A 1 321 ? -30.838 6.840   -17.557 1.00 173.16 ? 341 ASN   A OD1 1 
ATOM   2272 N  ND2 . ASN   A 1 321 ? -29.124 7.256   -18.948 1.00 184.25 ? 341 ASN   A ND2 1 
ATOM   2273 N  N   . LYS   A 1 322 ? -26.895 2.613   -17.424 1.00 170.88 ? 342 LYS   A N   1 
ATOM   2274 C  CA  . LYS   A 1 322 ? -26.123 1.645   -16.642 1.00 166.06 ? 342 LYS   A CA  1 
ATOM   2275 C  C   . LYS   A 1 322 ? -26.778 1.409   -15.281 1.00 162.32 ? 342 LYS   A C   1 
ATOM   2276 O  O   . LYS   A 1 322 ? -26.121 1.440   -14.238 1.00 162.91 ? 342 LYS   A O   1 
ATOM   2277 C  CB  . LYS   A 1 322 ? -24.670 2.095   -16.466 1.00 167.60 ? 342 LYS   A CB  1 
ATOM   2278 C  CG  . LYS   A 1 322 ? -23.956 2.558   -17.721 1.00 167.30 ? 342 LYS   A CG  1 
ATOM   2279 C  CD  . LYS   A 1 322 ? -22.625 3.182   -17.325 1.00 167.63 ? 342 LYS   A CD  1 
ATOM   2280 C  CE  . LYS   A 1 322 ? -21.720 3.429   -18.515 1.00 168.72 ? 342 LYS   A CE  1 
ATOM   2281 N  NZ  . LYS   A 1 322 ? -20.350 3.810   -18.070 1.00 169.78 ? 342 LYS   A NZ  1 
ATOM   2282 N  N   . ALA   A 1 323 ? -28.091 1.195   -15.298 1.00 158.79 ? 343 ALA   A N   1 
ATOM   2283 C  CA  . ALA   A 1 323 ? -28.834 1.037   -14.059 1.00 155.42 ? 343 ALA   A CA  1 
ATOM   2284 C  C   . ALA   A 1 323 ? -28.324 -0.179  -13.286 1.00 153.24 ? 343 ALA   A C   1 
ATOM   2285 O  O   . ALA   A 1 323 ? -27.850 -1.150  -13.882 1.00 146.89 ? 343 ALA   A O   1 
ATOM   2286 C  CB  . ALA   A 1 323 ? -30.328 0.891   -14.342 1.00 154.59 ? 343 ALA   A CB  1 
ATOM   2287 N  N   . PRO   A 1 324 ? -28.393 -0.144  -11.957 1.00 151.31 ? 344 PRO   A N   1 
ATOM   2288 C  CA  . PRO   A 1 324 ? -27.946 -1.289  -11.161 1.00 145.03 ? 344 PRO   A CA  1 
ATOM   2289 C  C   . PRO   A 1 324 ? -28.800 -2.508  -11.448 1.00 151.48 ? 344 PRO   A C   1 
ATOM   2290 O  O   . PRO   A 1 324 ? -30.031 -2.464  -11.296 1.00 148.80 ? 344 PRO   A O   1 
ATOM   2291 C  CB  . PRO   A 1 324 ? -28.128 -0.811  -9.712  1.00 142.41 ? 344 PRO   A CB  1 
ATOM   2292 C  CG  . PRO   A 1 324 ? -28.196 0.678   -9.797  1.00 147.90 ? 344 PRO   A CG  1 
ATOM   2293 C  CD  . PRO   A 1 324 ? -28.844 0.973   -11.111 1.00 154.69 ? 344 PRO   A CD  1 
ATOM   2294 N  N   . PRO   A 1 325 ? -28.190 -3.610  -11.880 1.00 150.78 ? 345 PRO   A N   1 
ATOM   2295 C  CA  . PRO   A 1 325 ? -28.969 -4.828  -12.124 1.00 144.20 ? 345 PRO   A CA  1 
ATOM   2296 C  C   . PRO   A 1 325 ? -29.612 -5.337  -10.845 1.00 132.73 ? 345 PRO   A C   1 
ATOM   2297 O  O   . PRO   A 1 325 ? -29.009 -5.315  -9.770  1.00 130.16 ? 345 PRO   A O   1 
ATOM   2298 C  CB  . PRO   A 1 325 ? -27.927 -5.815  -12.663 1.00 133.25 ? 345 PRO   A CB  1 
ATOM   2299 C  CG  . PRO   A 1 325 ? -26.617 -5.292  -12.177 1.00 136.75 ? 345 PRO   A CG  1 
ATOM   2300 C  CD  . PRO   A 1 325 ? -26.761 -3.801  -12.174 1.00 152.94 ? 345 PRO   A CD  1 
ATOM   2301 N  N   . THR   A 1 326 ? -30.855 -5.781  -10.970 1.00 133.59 ? 346 THR   A N   1 
ATOM   2302 C  CA  . THR   A 1 326 ? -31.585 -6.408  -9.882  1.00 131.61 ? 346 THR   A CA  1 
ATOM   2303 C  C   . THR   A 1 326 ? -31.799 -7.879  -10.204 1.00 134.00 ? 346 THR   A C   1 
ATOM   2304 O  O   . THR   A 1 326 ? -31.534 -8.339  -11.317 1.00 130.79 ? 346 THR   A O   1 
ATOM   2305 C  CB  . THR   A 1 326 ? -32.932 -5.713  -9.650  1.00 130.40 ? 346 THR   A CB  1 
ATOM   2306 O  OG1 . THR   A 1 326 ? -33.863 -6.121  -10.660 1.00 138.62 ? 346 THR   A OG1 1 
ATOM   2307 C  CG2 . THR   A 1 326 ? -32.768 -4.202  -9.707  1.00 141.03 ? 346 THR   A CG2 1 
ATOM   2308 N  N   . TYR   A 1 327 ? -32.275 -8.618  -9.201  1.00 135.24 ? 347 TYR   A N   1 
ATOM   2309 C  CA  . TYR   A 1 327 ? -32.634 -10.017 -9.400  1.00 126.61 ? 347 TYR   A CA  1 
ATOM   2310 C  C   . TYR   A 1 327 ? -33.610 -10.168 -10.562 1.00 129.25 ? 347 TYR   A C   1 
ATOM   2311 O  O   . TYR   A 1 327 ? -33.358 -10.913 -11.517 1.00 131.04 ? 347 TYR   A O   1 
ATOM   2312 C  CB  . TYR   A 1 327 ? -33.233 -10.580 -8.106  1.00 130.56 ? 347 TYR   A CB  1 
ATOM   2313 C  CG  . TYR   A 1 327 ? -33.748 -12.002 -8.204  1.00 129.69 ? 347 TYR   A CG  1 
ATOM   2314 C  CD1 . TYR   A 1 327 ? -35.014 -12.274 -8.714  1.00 127.69 ? 347 TYR   A CD1 1 
ATOM   2315 C  CD2 . TYR   A 1 327 ? -32.978 -13.071 -7.765  1.00 122.60 ? 347 TYR   A CD2 1 
ATOM   2316 C  CE1 . TYR   A 1 327 ? -35.487 -13.567 -8.802  1.00 121.38 ? 347 TYR   A CE1 1 
ATOM   2317 C  CE2 . TYR   A 1 327 ? -33.444 -14.369 -7.846  1.00 121.10 ? 347 TYR   A CE2 1 
ATOM   2318 C  CZ  . TYR   A 1 327 ? -34.699 -14.611 -8.366  1.00 118.07 ? 347 TYR   A CZ  1 
ATOM   2319 O  OH  . TYR   A 1 327 ? -35.169 -15.901 -8.449  1.00 117.35 ? 347 TYR   A OH  1 
ATOM   2320 N  N   . ASP   A 1 328 ? -34.732 -9.448  -10.494 1.00 130.78 ? 348 ASP   A N   1 
ATOM   2321 C  CA  . ASP   A 1 328 ? -35.803 -9.619  -11.470 1.00 138.38 ? 348 ASP   A CA  1 
ATOM   2322 C  C   . ASP   A 1 328 ? -35.384 -9.180  -12.868 1.00 142.44 ? 348 ASP   A C   1 
ATOM   2323 O  O   . ASP   A 1 328 ? -35.810 -9.785  -13.858 1.00 141.90 ? 348 ASP   A O   1 
ATOM   2324 C  CB  . ASP   A 1 328 ? -37.038 -8.846  -11.009 1.00 135.79 ? 348 ASP   A CB  1 
ATOM   2325 C  CG  . ASP   A 1 328 ? -37.510 -9.275  -9.635  1.00 139.30 ? 348 ASP   A CG  1 
ATOM   2326 O  OD1 . ASP   A 1 328 ? -38.040 -10.400 -9.513  1.00 137.68 ? 348 ASP   A OD1 1 
ATOM   2327 O  OD2 . ASP   A 1 328 ? -37.328 -8.496  -8.675  1.00 142.50 ? 348 ASP   A OD2 1 
ATOM   2328 N  N   . THR   A 1 329 ? -34.559 -8.137  -12.974 1.00 143.67 ? 349 THR   A N   1 
ATOM   2329 C  CA  . THR   A 1 329 ? -34.092 -7.704  -14.287 1.00 139.95 ? 349 THR   A CA  1 
ATOM   2330 C  C   . THR   A 1 329 ? -33.149 -8.721  -14.917 1.00 131.40 ? 349 THR   A C   1 
ATOM   2331 O  O   . THR   A 1 329 ? -33.114 -8.852  -16.146 1.00 129.94 ? 349 THR   A O   1 
ATOM   2332 C  CB  . THR   A 1 329 ? -33.404 -6.341  -14.182 1.00 143.18 ? 349 THR   A CB  1 
ATOM   2333 O  OG1 . THR   A 1 329 ? -32.580 -6.303  -13.009 1.00 146.66 ? 349 THR   A OG1 1 
ATOM   2334 C  CG2 . THR   A 1 329 ? -34.429 -5.217  -14.119 1.00 148.21 ? 349 THR   A CG2 1 
ATOM   2335 N  N   . VAL   A 1 330 ? -32.377 -9.442  -14.099 1.00 124.12 ? 350 VAL   A N   1 
ATOM   2336 C  CA  . VAL   A 1 330 ? -31.470 -10.458 -14.631 1.00 118.09 ? 350 VAL   A CA  1 
ATOM   2337 C  C   . VAL   A 1 330 ? -32.256 -11.547 -15.350 1.00 120.03 ? 350 VAL   A C   1 
ATOM   2338 O  O   . VAL   A 1 330 ? -31.910 -11.955 -16.465 1.00 120.50 ? 350 VAL   A O   1 
ATOM   2339 C  CB  . VAL   A 1 330 ? -30.595 -11.040 -13.506 1.00 118.66 ? 350 VAL   A CB  1 
ATOM   2340 C  CG1 . VAL   A 1 330 ? -29.919 -12.325 -13.961 1.00 112.64 ? 350 VAL   A CG1 1 
ATOM   2341 C  CG2 . VAL   A 1 330 ? -29.553 -10.031 -13.071 1.00 121.58 ? 350 VAL   A CG2 1 
ATOM   2342 N  N   . LEU   A 1 331 ? -33.326 -12.036 -14.721 1.00 112.96 ? 351 LEU   A N   1 
ATOM   2343 C  CA  . LEU   A 1 331 ? -34.176 -13.031 -15.364 1.00 116.01 ? 351 LEU   A CA  1 
ATOM   2344 C  C   . LEU   A 1 331 ? -34.949 -12.450 -16.540 1.00 121.71 ? 351 LEU   A C   1 
ATOM   2345 O  O   . LEU   A 1 331 ? -35.418 -13.208 -17.396 1.00 124.14 ? 351 LEU   A O   1 
ATOM   2346 C  CB  . LEU   A 1 331 ? -35.149 -13.627 -14.347 1.00 114.98 ? 351 LEU   A CB  1 
ATOM   2347 C  CG  . LEU   A 1 331 ? -34.531 -14.123 -13.038 1.00 118.36 ? 351 LEU   A CG  1 
ATOM   2348 C  CD1 . LEU   A 1 331 ? -35.592 -14.764 -12.159 1.00 125.32 ? 351 LEU   A CD1 1 
ATOM   2349 C  CD2 . LEU   A 1 331 ? -33.391 -15.093 -13.308 1.00 112.55 ? 351 LEU   A CD2 1 
ATOM   2350 N  N   . GLN   A 1 332 ? -35.090 -11.125 -16.596 1.00 118.76 ? 352 GLN   A N   1 
ATOM   2351 C  CA  . GLN   A 1 332 ? -35.800 -10.487 -17.698 1.00 120.37 ? 352 GLN   A CA  1 
ATOM   2352 C  C   . GLN   A 1 332 ? -35.003 -10.557 -18.995 1.00 117.48 ? 352 GLN   A C   1 
ATOM   2353 O  O   . GLN   A 1 332 ? -35.585 -10.509 -20.085 1.00 119.55 ? 352 GLN   A O   1 
ATOM   2354 C  CB  . GLN   A 1 332 ? -36.104 -9.034  -17.327 1.00 128.11 ? 352 GLN   A CB  1 
ATOM   2355 C  CG  . GLN   A 1 332 ? -37.006 -8.282  -18.287 1.00 130.15 ? 352 GLN   A CG  1 
ATOM   2356 C  CD  . GLN   A 1 332 ? -37.451 -6.949  -17.716 1.00 137.22 ? 352 GLN   A CD  1 
ATOM   2357 O  OE1 . GLN   A 1 332 ? -37.446 -6.750  -16.501 1.00 138.60 ? 352 GLN   A OE1 1 
ATOM   2358 N  NE2 . GLN   A 1 332 ? -37.833 -6.025  -18.591 1.00 142.89 ? 352 GLN   A NE2 1 
ATOM   2359 N  N   . MET   A 1 333 ? -33.682 -10.689 -18.898 1.00 116.36 ? 353 MET   A N   1 
ATOM   2360 C  CA  . MET   A 1 333 ? -32.797 -10.645 -20.058 1.00 114.41 ? 353 MET   A CA  1 
ATOM   2361 C  C   . MET   A 1 333 ? -32.696 -12.039 -20.665 1.00 115.14 ? 353 MET   A C   1 
ATOM   2362 O  O   . MET   A 1 333 ? -32.077 -12.937 -20.083 1.00 114.25 ? 353 MET   A O   1 
ATOM   2363 C  CB  . MET   A 1 333 ? -31.425 -10.115 -19.654 1.00 107.89 ? 353 MET   A CB  1 
ATOM   2364 C  CG  . MET   A 1 333 ? -31.500 -8.813  -18.885 1.00 116.07 ? 353 MET   A CG  1 
ATOM   2365 S  SD  . MET   A 1 333 ? -29.900 -8.112  -18.465 1.00 117.00 ? 353 MET   A SD  1 
ATOM   2366 C  CE  . MET   A 1 333 ? -30.427 -6.697  -17.506 1.00 133.40 ? 353 MET   A CE  1 
ATOM   2367 N  N   . GLU   A 1 334 ? -33.296 -12.216 -21.843 1.00 112.17 ? 354 GLU   A N   1 
ATOM   2368 C  CA  . GLU   A 1 334 ? -33.298 -13.520 -22.494 1.00 105.19 ? 354 GLU   A CA  1 
ATOM   2369 C  C   . GLU   A 1 334 ? -32.017 -13.761 -23.283 1.00 102.38 ? 354 GLU   A C   1 
ATOM   2370 O  O   . GLU   A 1 334 ? -31.459 -14.863 -23.238 1.00 104.46 ? 354 GLU   A O   1 
ATOM   2371 C  CB  . GLU   A 1 334 ? -34.520 -13.647 -23.404 1.00 114.15 ? 354 GLU   A CB  1 
ATOM   2372 C  CG  . GLU   A 1 334 ? -35.844 -13.599 -22.661 1.00 130.01 ? 354 GLU   A CG  1 
ATOM   2373 C  CD  . GLU   A 1 334 ? -37.033 -13.469 -23.592 1.00 147.40 ? 354 GLU   A CD  1 
ATOM   2374 O  OE1 . GLU   A 1 334 ? -36.828 -13.461 -24.824 1.00 150.50 ? 354 GLU   A OE1 1 
ATOM   2375 O  OE2 . GLU   A 1 334 ? -38.173 -13.370 -23.091 1.00 152.37 ? 354 GLU   A OE2 1 
ATOM   2376 N  N   . TYR   A 1 335 ? -31.534 -12.747 -24.008 1.00 108.11 ? 355 TYR   A N   1 
ATOM   2377 C  CA  . TYR   A 1 335 ? -30.326 -12.932 -24.807 1.00 102.80 ? 355 TYR   A CA  1 
ATOM   2378 C  C   . TYR   A 1 335 ? -29.103 -13.166 -23.931 1.00 102.90 ? 355 TYR   A C   1 
ATOM   2379 O  O   . TYR   A 1 335 ? -28.186 -13.892 -24.333 1.00 98.46  ? 355 TYR   A O   1 
ATOM   2380 C  CB  . TYR   A 1 335 ? -30.101 -11.729 -25.722 1.00 99.98  ? 355 TYR   A CB  1 
ATOM   2381 C  CG  . TYR   A 1 335 ? -29.116 -12.004 -26.836 1.00 101.97 ? 355 TYR   A CG  1 
ATOM   2382 C  CD1 . TYR   A 1 335 ? -29.489 -12.753 -27.944 1.00 96.72  ? 355 TYR   A CD1 1 
ATOM   2383 C  CD2 . TYR   A 1 335 ? -27.815 -11.521 -26.780 1.00 107.57 ? 355 TYR   A CD2 1 
ATOM   2384 C  CE1 . TYR   A 1 335 ? -28.596 -13.014 -28.966 1.00 105.64 ? 355 TYR   A CE1 1 
ATOM   2385 C  CE2 . TYR   A 1 335 ? -26.913 -11.775 -27.799 1.00 103.80 ? 355 TYR   A CE2 1 
ATOM   2386 C  CZ  . TYR   A 1 335 ? -27.310 -12.522 -28.889 1.00 102.47 ? 355 TYR   A CZ  1 
ATOM   2387 O  OH  . TYR   A 1 335 ? -26.420 -12.780 -29.906 1.00 97.79  ? 355 TYR   A OH  1 
ATOM   2388 N  N   . LEU   A 1 336 ? -29.066 -12.562 -22.741 1.00 97.57  ? 356 LEU   A N   1 
ATOM   2389 C  CA  . LEU   A 1 336 ? -27.996 -12.869 -21.797 1.00 99.63  ? 356 LEU   A CA  1 
ATOM   2390 C  C   . LEU   A 1 336 ? -28.040 -14.334 -21.386 1.00 100.38 ? 356 LEU   A C   1 
ATOM   2391 O  O   . LEU   A 1 336 ? -26.999 -14.996 -21.304 1.00 95.99  ? 356 LEU   A O   1 
ATOM   2392 C  CB  . LEU   A 1 336 ? -28.097 -11.963 -20.571 1.00 97.64  ? 356 LEU   A CB  1 
ATOM   2393 C  CG  . LEU   A 1 336 ? -27.199 -12.334 -19.388 1.00 94.01  ? 356 LEU   A CG  1 
ATOM   2394 C  CD1 . LEU   A 1 336 ? -25.728 -12.296 -19.782 1.00 93.52  ? 356 LEU   A CD1 1 
ATOM   2395 C  CD2 . LEU   A 1 336 ? -27.465 -11.419 -18.203 1.00 101.76 ? 356 LEU   A CD2 1 
ATOM   2396 N  N   . ASP   A 1 337 ? -29.241 -14.857 -21.124 1.00 95.91  ? 357 ASP   A N   1 
ATOM   2397 C  CA  . ASP   A 1 337 ? -29.382 -16.277 -20.824 1.00 96.00  ? 357 ASP   A CA  1 
ATOM   2398 C  C   . ASP   A 1 337 ? -28.959 -17.133 -22.010 1.00 91.55  ? 357 ASP   A C   1 
ATOM   2399 O  O   . ASP   A 1 337 ? -28.369 -18.206 -21.833 1.00 84.86  ? 357 ASP   A O   1 
ATOM   2400 C  CB  . ASP   A 1 337 ? -30.826 -16.581 -20.418 1.00 100.44 ? 357 ASP   A CB  1 
ATOM   2401 C  CG  . ASP   A 1 337 ? -31.113 -18.068 -20.334 1.00 100.62 ? 357 ASP   A CG  1 
ATOM   2402 O  OD1 . ASP   A 1 337 ? -31.370 -18.691 -21.387 1.00 100.81 ? 357 ASP   A OD1 1 
ATOM   2403 O  OD2 . ASP   A 1 337 ? -31.072 -18.617 -19.214 1.00 105.10 ? 357 ASP   A OD2 1 
ATOM   2404 N  N   . MET   A 1 338 ? -29.247 -16.672 -23.230 1.00 94.88  ? 358 MET   A N   1 
ATOM   2405 C  CA  . MET   A 1 338 ? -28.861 -17.420 -24.422 1.00 83.72  ? 358 MET   A CA  1 
ATOM   2406 C  C   . MET   A 1 338 ? -27.345 -17.495 -24.564 1.00 87.69  ? 358 MET   A C   1 
ATOM   2407 O  O   . MET   A 1 338 ? -26.807 -18.528 -24.981 1.00 90.04  ? 358 MET   A O   1 
ATOM   2408 C  CB  . MET   A 1 338 ? -29.489 -16.783 -25.661 1.00 84.45  ? 358 MET   A CB  1 
ATOM   2409 C  CG  . MET   A 1 338 ? -31.006 -16.868 -25.696 1.00 94.01  ? 358 MET   A CG  1 
ATOM   2410 S  SD  . MET   A 1 338 ? -31.746 -15.722 -26.874 1.00 100.08 ? 358 MET   A SD  1 
ATOM   2411 C  CE  . MET   A 1 338 ? -30.875 -16.171 -28.372 1.00 93.67  ? 358 MET   A CE  1 
ATOM   2412 N  N   . VAL   A 1 339 ? -26.641 -16.413 -24.224 1.00 87.60  ? 359 VAL   A N   1 
ATOM   2413 C  CA  . VAL   A 1 339 ? -25.180 -16.420 -24.283 1.00 90.61  ? 359 VAL   A CA  1 
ATOM   2414 C  C   . VAL   A 1 339 ? -24.614 -17.407 -23.270 1.00 92.27  ? 359 VAL   A C   1 
ATOM   2415 O  O   . VAL   A 1 339 ? -23.711 -18.194 -23.579 1.00 88.55  ? 359 VAL   A O   1 
ATOM   2416 C  CB  . VAL   A 1 339 ? -24.626 -15.001 -24.058 1.00 92.10  ? 359 VAL   A CB  1 
ATOM   2417 C  CG1 . VAL   A 1 339 ? -23.139 -15.051 -23.729 1.00 91.19  ? 359 VAL   A CG1 1 
ATOM   2418 C  CG2 . VAL   A 1 339 ? -24.873 -14.131 -25.280 1.00 86.52  ? 359 VAL   A CG2 1 
ATOM   2419 N  N   . VAL   A 1 340 ? -25.143 -17.380 -22.043 1.00 86.78  ? 360 VAL   A N   1 
ATOM   2420 C  CA  . VAL   A 1 340 ? -24.635 -18.245 -20.980 1.00 86.11  ? 360 VAL   A CA  1 
ATOM   2421 C  C   . VAL   A 1 340 ? -24.785 -19.712 -21.366 1.00 85.68  ? 360 VAL   A C   1 
ATOM   2422 O  O   . VAL   A 1 340 ? -23.823 -20.487 -21.315 1.00 79.41  ? 360 VAL   A O   1 
ATOM   2423 C  CB  . VAL   A 1 340 ? -25.350 -17.939 -19.652 1.00 89.07  ? 360 VAL   A CB  1 
ATOM   2424 C  CG1 . VAL   A 1 340 ? -25.033 -19.010 -18.619 1.00 79.86  ? 360 VAL   A CG1 1 
ATOM   2425 C  CG2 . VAL   A 1 340 ? -24.952 -16.564 -19.137 1.00 82.12  ? 360 VAL   A CG2 1 
ATOM   2426 N  N   . ASN   A 1 341 ? -25.996 -20.111 -21.763 1.00 81.56  ? 361 ASN   A N   1 
ATOM   2427 C  CA  . ASN   A 1 341 ? -26.246 -21.515 -22.077 1.00 81.54  ? 361 ASN   A CA  1 
ATOM   2428 C  C   . ASN   A 1 341 ? -25.378 -21.992 -23.234 1.00 82.17  ? 361 ASN   A C   1 
ATOM   2429 O  O   . ASN   A 1 341 ? -24.861 -23.115 -23.208 1.00 77.77  ? 361 ASN   A O   1 
ATOM   2430 C  CB  . ASN   A 1 341 ? -27.724 -21.730 -22.397 1.00 77.54  ? 361 ASN   A CB  1 
ATOM   2431 C  CG  . ASN   A 1 341 ? -28.627 -21.384 -21.234 1.00 89.26  ? 361 ASN   A CG  1 
ATOM   2432 O  OD1 . ASN   A 1 341 ? -28.172 -21.262 -20.098 1.00 95.96  ? 361 ASN   A OD1 1 
ATOM   2433 N  ND2 . ASN   A 1 341 ? -29.917 -21.229 -21.510 1.00 93.15  ? 361 ASN   A ND2 1 
ATOM   2434 N  N   . GLU   A 1 342 ? -25.206 -21.153 -24.258 1.00 89.10  ? 362 GLU   A N   1 
ATOM   2435 C  CA  . GLU   A 1 342 ? -24.401 -21.552 -25.408 1.00 81.88  ? 362 GLU   A CA  1 
ATOM   2436 C  C   . GLU   A 1 342 ? -22.934 -21.711 -25.031 1.00 85.82  ? 362 GLU   A C   1 
ATOM   2437 O  O   . GLU   A 1 342 ? -22.257 -22.621 -25.523 1.00 92.44  ? 362 GLU   A O   1 
ATOM   2438 C  CB  . GLU   A 1 342 ? -24.564 -20.540 -26.544 1.00 93.74  ? 362 GLU   A CB  1 
ATOM   2439 C  CG  . GLU   A 1 342 ? -23.612 -20.736 -27.726 1.00 92.81  ? 362 GLU   A CG  1 
ATOM   2440 C  CD  . GLU   A 1 342 ? -23.941 -21.948 -28.591 1.00 96.43  ? 362 GLU   A CD  1 
ATOM   2441 O  OE1 . GLU   A 1 342 ? -24.692 -22.840 -28.144 1.00 97.25  ? 362 GLU   A OE1 1 
ATOM   2442 O  OE2 . GLU   A 1 342 ? -23.441 -22.006 -29.734 1.00 101.44 ? 362 GLU   A OE2 1 
ATOM   2443 N  N   . THR   A 1 343 ? -22.423 -20.836 -24.162 1.00 85.11  ? 363 THR   A N   1 
ATOM   2444 C  CA  . THR   A 1 343 ? -21.062 -21.006 -23.665 1.00 83.05  ? 363 THR   A CA  1 
ATOM   2445 C  C   . THR   A 1 343 ? -20.932 -22.307 -22.884 1.00 84.95  ? 363 THR   A C   1 
ATOM   2446 O  O   . THR   A 1 343 ? -19.970 -23.062 -23.062 1.00 83.60  ? 363 THR   A O   1 
ATOM   2447 C  CB  . THR   A 1 343 ? -20.663 -19.816 -22.792 1.00 82.55  ? 363 THR   A CB  1 
ATOM   2448 O  OG1 . THR   A 1 343 ? -20.832 -18.598 -23.528 1.00 90.61  ? 363 THR   A OG1 1 
ATOM   2449 C  CG2 . THR   A 1 343 ? -19.210 -19.945 -22.361 1.00 84.28  ? 363 THR   A CG2 1 
ATOM   2450 N  N   . LEU   A 1 344 ? -21.907 -22.589 -22.016 1.00 87.05  ? 364 LEU   A N   1 
ATOM   2451 C  CA  . LEU   A 1 344 ? -21.890 -23.821 -21.239 1.00 85.18  ? 364 LEU   A CA  1 
ATOM   2452 C  C   . LEU   A 1 344 ? -22.068 -25.057 -22.109 1.00 84.79  ? 364 LEU   A C   1 
ATOM   2453 O  O   . LEU   A 1 344 ? -21.665 -26.151 -21.698 1.00 81.38  ? 364 LEU   A O   1 
ATOM   2454 C  CB  . LEU   A 1 344 ? -22.971 -23.775 -20.160 1.00 71.47  ? 364 LEU   A CB  1 
ATOM   2455 C  CG  . LEU   A 1 344 ? -22.687 -22.805 -19.012 1.00 70.49  ? 364 LEU   A CG  1 
ATOM   2456 C  CD1 . LEU   A 1 344 ? -23.861 -22.755 -18.049 1.00 71.06  ? 364 LEU   A CD1 1 
ATOM   2457 C  CD2 . LEU   A 1 344 ? -21.407 -23.197 -18.282 1.00 74.14  ? 364 LEU   A CD2 1 
ATOM   2458 N  N   . ARG   A 1 345 ? -22.659 -24.913 -23.297 1.00 85.98  ? 365 ARG   A N   1 
ATOM   2459 C  CA  . ARG   A 1 345 ? -22.721 -26.040 -24.221 1.00 87.37  ? 365 ARG   A CA  1 
ATOM   2460 C  C   . ARG   A 1 345 ? -21.343 -26.358 -24.787 1.00 82.44  ? 365 ARG   A C   1 
ATOM   2461 O  O   . ARG   A 1 345 ? -20.960 -27.529 -24.885 1.00 84.80  ? 365 ARG   A O   1 
ATOM   2462 C  CB  . ARG   A 1 345 ? -23.707 -25.747 -25.350 1.00 87.62  ? 365 ARG   A CB  1 
ATOM   2463 C  CG  . ARG   A 1 345 ? -23.905 -26.913 -26.302 1.00 87.98  ? 365 ARG   A CG  1 
ATOM   2464 C  CD  . ARG   A 1 345 ? -24.661 -26.489 -27.546 1.00 84.68  ? 365 ARG   A CD  1 
ATOM   2465 N  NE  . ARG   A 1 345 ? -23.922 -25.498 -28.317 1.00 90.90  ? 365 ARG   A NE  1 
ATOM   2466 C  CZ  . ARG   A 1 345 ? -23.052 -25.791 -29.275 1.00 94.80  ? 365 ARG   A CZ  1 
ATOM   2467 N  NH1 . ARG   A 1 345 ? -22.791 -27.043 -29.611 1.00 93.53  ? 365 ARG   A NH1 1 
ATOM   2468 N  NH2 . ARG   A 1 345 ? -22.430 -24.802 -29.910 1.00 102.48 ? 365 ARG   A NH2 1 
ATOM   2469 N  N   . LEU   A 1 346 ? -20.580 -25.329 -25.157 1.00 81.62  ? 366 LEU   A N   1 
ATOM   2470 C  CA  . LEU   A 1 346 ? -19.244 -25.554 -25.695 1.00 90.83  ? 366 LEU   A CA  1 
ATOM   2471 C  C   . LEU   A 1 346 ? -18.235 -25.903 -24.610 1.00 87.35  ? 366 LEU   A C   1 
ATOM   2472 O  O   . LEU   A 1 346 ? -17.255 -26.604 -24.886 1.00 88.70  ? 366 LEU   A O   1 
ATOM   2473 C  CB  . LEU   A 1 346 ? -18.775 -24.322 -26.468 1.00 82.21  ? 366 LEU   A CB  1 
ATOM   2474 C  CG  . LEU   A 1 346 ? -19.368 -24.156 -27.867 1.00 94.66  ? 366 LEU   A CG  1 
ATOM   2475 C  CD1 . LEU   A 1 346 ? -19.029 -22.789 -28.438 1.00 87.14  ? 366 LEU   A CD1 1 
ATOM   2476 C  CD2 . LEU   A 1 346 ? -18.860 -25.259 -28.780 1.00 89.57  ? 366 LEU   A CD2 1 
ATOM   2477 N  N   . PHE   A 1 347 ? -18.449 -25.433 -23.383 1.00 83.90  ? 367 PHE   A N   1 
ATOM   2478 C  CA  . PHE   A 1 347 ? -17.512 -25.644 -22.280 1.00 84.60  ? 367 PHE   A CA  1 
ATOM   2479 C  C   . PHE   A 1 347 ? -18.267 -26.127 -21.047 1.00 79.71  ? 367 PHE   A C   1 
ATOM   2480 O  O   . PHE   A 1 347 ? -18.460 -25.376 -20.083 1.00 85.02  ? 367 PHE   A O   1 
ATOM   2481 C  CB  . PHE   A 1 347 ? -16.727 -24.365 -21.988 1.00 89.82  ? 367 PHE   A CB  1 
ATOM   2482 C  CG  . PHE   A 1 347 ? -16.110 -23.747 -23.211 1.00 95.01  ? 367 PHE   A CG  1 
ATOM   2483 C  CD1 . PHE   A 1 347 ? -15.087 -24.392 -23.887 1.00 96.10  ? 367 PHE   A CD1 1 
ATOM   2484 C  CD2 . PHE   A 1 347 ? -16.555 -22.525 -23.688 1.00 94.05  ? 367 PHE   A CD2 1 
ATOM   2485 C  CE1 . PHE   A 1 347 ? -14.518 -23.830 -25.014 1.00 100.13 ? 367 PHE   A CE1 1 
ATOM   2486 C  CE2 . PHE   A 1 347 ? -15.989 -21.956 -24.815 1.00 94.63  ? 367 PHE   A CE2 1 
ATOM   2487 C  CZ  . PHE   A 1 347 ? -14.970 -22.610 -25.479 1.00 99.87  ? 367 PHE   A CZ  1 
ATOM   2488 N  N   . PRO   A 1 348 ? -18.711 -27.392 -21.045 1.00 81.97  ? 368 PRO   A N   1 
ATOM   2489 C  CA  . PRO   A 1 348 ? -19.342 -27.949 -19.841 1.00 79.58  ? 368 PRO   A CA  1 
ATOM   2490 C  C   . PRO   A 1 348 ? -18.162 -28.290 -18.944 1.00 88.17  ? 368 PRO   A C   1 
ATOM   2491 O  O   . PRO   A 1 348 ? -17.404 -29.220 -19.233 1.00 94.60  ? 368 PRO   A O   1 
ATOM   2492 C  CB  . PRO   A 1 348 ? -20.133 -29.144 -20.386 1.00 74.35  ? 368 PRO   A CB  1 
ATOM   2493 C  CG  . PRO   A 1 348 ? -19.353 -29.584 -21.579 1.00 77.62  ? 368 PRO   A CG  1 
ATOM   2494 C  CD  . PRO   A 1 348 ? -18.686 -28.358 -22.158 1.00 77.96  ? 368 PRO   A CD  1 
ATOM   2495 N  N   . ILE   A 1 349 ? -17.931 -27.451 -17.930 1.00 82.79  ? 369 ILE   A N   1 
ATOM   2496 C  CA  . ILE   A 1 349 ? -16.824 -27.699 -16.954 1.00 89.52  ? 369 ILE   A CA  1 
ATOM   2497 C  C   . ILE   A 1 349 ? -16.781 -29.149 -16.467 1.00 78.32  ? 369 ILE   A C   1 
ATOM   2498 O  O   . ILE   A 1 349 ? -15.661 -29.667 -16.302 1.00 91.68  ? 369 ILE   A O   1 
ATOM   2499 C  CB  . ILE   A 1 349 ? -16.939 -26.719 -15.768 1.00 84.27  ? 369 ILE   A CB  1 
ATOM   2500 C  CG1 . ILE   A 1 349 ? -18.365 -26.661 -15.215 1.00 87.20  ? 369 ILE   A CG1 1 
ATOM   2501 C  CG2 . ILE   A 1 349 ? -16.430 -25.340 -16.160 1.00 97.18  ? 369 ILE   A CG2 1 
ATOM   2502 C  CD1 . ILE   A 1 349 ? -18.527 -27.309 -13.859 1.00 96.74  ? 369 ILE   A CD1 1 
ATOM   2503 N  N   . ALA   A 1 350 ? -17.932 -29.786 -16.251 1.00 69.56  ? 370 ALA   A N   1 
ATOM   2504 C  CA  . ALA   A 1 350 ? -17.910 -31.114 -15.648 1.00 82.54  ? 370 ALA   A CA  1 
ATOM   2505 C  C   . ALA   A 1 350 ? -17.426 -32.194 -16.604 1.00 83.60  ? 370 ALA   A C   1 
ATOM   2506 O  O   . ALA   A 1 350 ? -16.952 -33.241 -16.147 1.00 92.98  ? 370 ALA   A O   1 
ATOM   2507 C  CB  . ALA   A 1 350 ? -19.300 -31.499 -15.132 1.00 81.74  ? 370 ALA   A CB  1 
ATOM   2508 N  N   . MET   A 1 351 ? -17.558 -31.960 -17.915 1.00 73.16  ? 371 MET   A N   1 
ATOM   2509 C  CA  . MET   A 1 351 ? -17.154 -32.882 -18.975 1.00 81.39  ? 371 MET   A CA  1 
ATOM   2510 C  C   . MET   A 1 351 ? -18.021 -34.137 -19.002 1.00 70.61  ? 371 MET   A C   1 
ATOM   2511 O  O   . MET   A 1 351 ? -18.574 -34.486 -20.050 1.00 69.22  ? 371 MET   A O   1 
ATOM   2512 C  CB  . MET   A 1 351 ? -15.674 -33.256 -18.840 1.00 80.54  ? 371 MET   A CB  1 
ATOM   2513 C  CG  . MET   A 1 351 ? -14.714 -32.108 -19.120 1.00 91.94  ? 371 MET   A CG  1 
ATOM   2514 S  SD  . MET   A 1 351 ? -13.099 -32.338 -18.345 1.00 128.95 ? 371 MET   A SD  1 
ATOM   2515 C  CE  . MET   A 1 351 ? -13.513 -32.051 -16.626 1.00 112.30 ? 371 MET   A CE  1 
ATOM   2516 N  N   . ARG   A 1 352 ? -18.143 -34.824 -17.868 1.00 74.37  ? 372 ARG   A N   1 
ATOM   2517 C  CA  . ARG   A 1 352 ? -18.919 -36.050 -17.780 1.00 71.84  ? 372 ARG   A CA  1 
ATOM   2518 C  C   . ARG   A 1 352 ? -19.791 -36.029 -16.532 1.00 69.03  ? 372 ARG   A C   1 
ATOM   2519 O  O   . ARG   A 1 352 ? -19.554 -35.269 -15.590 1.00 73.90  ? 372 ARG   A O   1 
ATOM   2520 C  CB  . ARG   A 1 352 ? -18.020 -37.293 -17.734 1.00 74.54  ? 372 ARG   A CB  1 
ATOM   2521 C  CG  . ARG   A 1 352 ? -16.942 -37.367 -18.798 1.00 76.58  ? 372 ARG   A CG  1 
ATOM   2522 C  CD  . ARG   A 1 352 ? -15.791 -38.216 -18.285 1.00 83.28  ? 372 ARG   A CD  1 
ATOM   2523 N  NE  . ARG   A 1 352 ? -15.130 -38.978 -19.337 1.00 84.31  ? 372 ARG   A NE  1 
ATOM   2524 C  CZ  . ARG   A 1 352 ? -14.319 -40.003 -19.113 1.00 86.18  ? 372 ARG   A CZ  1 
ATOM   2525 N  NH1 . ARG   A 1 352 ? -14.068 -40.430 -17.886 1.00 85.78  ? 372 ARG   A NH1 1 
ATOM   2526 N  NH2 . ARG   A 1 352 ? -13.756 -40.624 -20.145 1.00 82.24  ? 372 ARG   A NH2 1 
ATOM   2527 N  N   . LEU   A 1 353 ? -20.806 -36.889 -16.542 1.00 63.32  ? 373 LEU   A N   1 
ATOM   2528 C  CA  . LEU   A 1 353 ? -21.625 -37.185 -15.377 1.00 58.14  ? 373 LEU   A CA  1 
ATOM   2529 C  C   . LEU   A 1 353 ? -21.513 -38.673 -15.084 1.00 70.87  ? 373 LEU   A C   1 
ATOM   2530 O  O   . LEU   A 1 353 ? -21.517 -39.494 -16.007 1.00 67.16  ? 373 LEU   A O   1 
ATOM   2531 C  CB  . LEU   A 1 353 ? -23.089 -36.798 -15.607 1.00 66.13  ? 373 LEU   A CB  1 
ATOM   2532 C  CG  . LEU   A 1 353 ? -23.352 -35.358 -16.051 1.00 67.57  ? 373 LEU   A CG  1 
ATOM   2533 C  CD1 . LEU   A 1 353 ? -24.821 -35.162 -16.394 1.00 73.93  ? 373 LEU   A CD1 1 
ATOM   2534 C  CD2 . LEU   A 1 353 ? -22.914 -34.380 -14.976 1.00 56.41  ? 373 LEU   A CD2 1 
ATOM   2535 N  N   . GLU   A 1 354 ? -21.404 -39.026 -13.804 1.00 70.85  ? 374 GLU   A N   1 
ATOM   2536 C  CA  . GLU   A 1 354 ? -21.136 -40.406 -13.428 1.00 62.69  ? 374 GLU   A CA  1 
ATOM   2537 C  C   . GLU   A 1 354 ? -22.024 -40.833 -12.270 1.00 65.39  ? 374 GLU   A C   1 
ATOM   2538 O  O   . GLU   A 1 354 ? -22.328 -40.037 -11.377 1.00 71.37  ? 374 GLU   A O   1 
ATOM   2539 C  CB  . GLU   A 1 354 ? -19.663 -40.604 -13.045 1.00 60.80  ? 374 GLU   A CB  1 
ATOM   2540 C  CG  . GLU   A 1 354 ? -18.691 -40.418 -14.198 1.00 68.50  ? 374 GLU   A CG  1 
ATOM   2541 C  CD  . GLU   A 1 354 ? -17.266 -40.758 -13.815 1.00 87.51  ? 374 GLU   A CD  1 
ATOM   2542 O  OE1 . GLU   A 1 354 ? -17.032 -41.099 -12.637 1.00 87.82  ? 374 GLU   A OE1 1 
ATOM   2543 O  OE2 . GLU   A 1 354 ? -16.381 -40.686 -14.693 1.00 92.65  ? 374 GLU   A OE2 1 
ATOM   2544 N  N   . ARG   A 1 355 ? -22.431 -42.102 -12.299 1.00 55.51  ? 375 ARG   A N   1 
ATOM   2545 C  CA  . ARG   A 1 355 ? -23.182 -42.736 -11.226 1.00 65.82  ? 375 ARG   A CA  1 
ATOM   2546 C  C   . ARG   A 1 355 ? -22.688 -44.166 -11.072 1.00 64.77  ? 375 ARG   A C   1 
ATOM   2547 O  O   . ARG   A 1 355 ? -22.482 -44.866 -12.068 1.00 70.47  ? 375 ARG   A O   1 
ATOM   2548 C  CB  . ARG   A 1 355 ? -24.691 -42.744 -11.510 1.00 66.79  ? 375 ARG   A CB  1 
ATOM   2549 C  CG  . ARG   A 1 355 ? -25.328 -41.377 -11.671 1.00 68.48  ? 375 ARG   A CG  1 
ATOM   2550 C  CD  . ARG   A 1 355 ? -25.346 -40.612 -10.361 1.00 59.11  ? 375 ARG   A CD  1 
ATOM   2551 N  NE  . ARG   A 1 355 ? -26.145 -39.397 -10.465 1.00 67.82  ? 375 ARG   A NE  1 
ATOM   2552 C  CZ  . ARG   A 1 355 ? -25.696 -38.246 -10.946 1.00 61.46  ? 375 ARG   A CZ  1 
ATOM   2553 N  NH1 . ARG   A 1 355 ? -24.450 -38.114 -11.369 1.00 71.50  ? 375 ARG   A NH1 1 
ATOM   2554 N  NH2 . ARG   A 1 355 ? -26.519 -37.204 -11.005 1.00 58.44  ? 375 ARG   A NH2 1 
ATOM   2555 N  N   . VAL   A 1 356 ? -22.493 -44.598 -9.829  1.00 78.73  ? 376 VAL   A N   1 
ATOM   2556 C  CA  . VAL   A 1 356 ? -22.129 -45.983 -9.545  1.00 69.86  ? 376 VAL   A CA  1 
ATOM   2557 C  C   . VAL   A 1 356 ? -23.397 -46.820 -9.470  1.00 75.68  ? 376 VAL   A C   1 
ATOM   2558 O  O   . VAL   A 1 356 ? -24.316 -46.515 -8.701  1.00 78.89  ? 376 VAL   A O   1 
ATOM   2559 C  CB  . VAL   A 1 356 ? -21.320 -46.095 -8.243  1.00 66.55  ? 376 VAL   A CB  1 
ATOM   2560 C  CG1 . VAL   A 1 356 ? -21.084 -47.560 -7.894  1.00 62.62  ? 376 VAL   A CG1 1 
ATOM   2561 C  CG2 . VAL   A 1 356 ? -20.003 -45.392 -8.392  1.00 60.47  ? 376 VAL   A CG2 1 
ATOM   2562 N  N   . CYS   A 1 357 ? -23.439 -47.879 -10.271 1.00 70.63  ? 377 CYS   A N   1 
ATOM   2563 C  CA  . CYS   A 1 357 ? -24.577 -48.788 -10.330 1.00 76.15  ? 377 CYS   A CA  1 
ATOM   2564 C  C   . CYS   A 1 357 ? -24.533 -49.713 -9.118  1.00 85.51  ? 377 CYS   A C   1 
ATOM   2565 O  O   . CYS   A 1 357 ? -23.721 -50.643 -9.068  1.00 82.94  ? 377 CYS   A O   1 
ATOM   2566 C  CB  . CYS   A 1 357 ? -24.527 -49.559 -11.646 1.00 78.65  ? 377 CYS   A CB  1 
ATOM   2567 S  SG  . CYS   A 1 357 ? -25.613 -50.970 -11.786 1.00 85.30  ? 377 CYS   A SG  1 
ATOM   2568 N  N   . LYS   A 1 358 ? -25.403 -49.462 -8.134  1.00 84.65  ? 378 LYS   A N   1 
ATOM   2569 C  CA  . LYS   A 1 358 ? -25.310 -50.149 -6.851  1.00 86.58  ? 378 LYS   A CA  1 
ATOM   2570 C  C   . LYS   A 1 358 ? -25.980 -51.520 -6.843  1.00 93.23  ? 378 LYS   A C   1 
ATOM   2571 O  O   . LYS   A 1 358 ? -25.771 -52.281 -5.892  1.00 93.75  ? 378 LYS   A O   1 
ATOM   2572 C  CB  . LYS   A 1 358 ? -25.905 -49.279 -5.736  1.00 82.94  ? 378 LYS   A CB  1 
ATOM   2573 C  CG  . LYS   A 1 358 ? -27.414 -49.393 -5.571  1.00 99.58  ? 378 LYS   A CG  1 
ATOM   2574 C  CD  . LYS   A 1 358 ? -27.898 -48.716 -4.289  1.00 94.91  ? 378 LYS   A CD  1 
ATOM   2575 C  CE  . LYS   A 1 358 ? -27.704 -47.207 -4.330  1.00 92.44  ? 378 LYS   A CE  1 
ATOM   2576 N  NZ  . LYS   A 1 358 ? -28.299 -46.536 -3.137  1.00 91.37  ? 378 LYS   A NZ  1 
ATOM   2577 N  N   . LYS   A 1 359 ? -26.776 -51.855 -7.859  1.00 90.10  ? 379 LYS   A N   1 
ATOM   2578 C  CA  . LYS   A 1 359 ? -27.372 -53.181 -7.971  1.00 98.89  ? 379 LYS   A CA  1 
ATOM   2579 C  C   . LYS   A 1 359 ? -27.429 -53.577 -9.438  1.00 99.85  ? 379 LYS   A C   1 
ATOM   2580 O  O   . LYS   A 1 359 ? -27.403 -52.726 -10.327 1.00 107.90 ? 379 LYS   A O   1 
ATOM   2581 C  CB  . LYS   A 1 359 ? -28.795 -53.243 -7.401  1.00 107.21 ? 379 LYS   A CB  1 
ATOM   2582 C  CG  . LYS   A 1 359 ? -29.012 -52.648 -6.028  1.00 105.50 ? 379 LYS   A CG  1 
ATOM   2583 C  CD  . LYS   A 1 359 ? -30.493 -52.709 -5.697  1.00 112.48 ? 379 LYS   A CD  1 
ATOM   2584 C  CE  . LYS   A 1 359 ? -30.784 -52.279 -4.276  1.00 128.12 ? 379 LYS   A CE  1 
ATOM   2585 N  NZ  . LYS   A 1 359 ? -32.215 -52.512 -3.934  1.00 130.36 ? 379 LYS   A NZ  1 
ATOM   2586 N  N   . ASP   A 1 360 ? -27.538 -54.881 -9.685  1.00 105.21 ? 380 ASP   A N   1 
ATOM   2587 C  CA  . ASP   A 1 360 ? -27.853 -55.349 -11.029 1.00 98.17  ? 380 ASP   A CA  1 
ATOM   2588 C  C   . ASP   A 1 360 ? -29.189 -54.771 -11.476 1.00 96.57  ? 380 ASP   A C   1 
ATOM   2589 O  O   . ASP   A 1 360 ? -30.185 -54.856 -10.752 1.00 93.58  ? 380 ASP   A O   1 
ATOM   2590 C  CB  . ASP   A 1 360 ? -27.909 -56.877 -11.070 1.00 90.33  ? 380 ASP   A CB  1 
ATOM   2591 C  CG  . ASP   A 1 360 ? -26.537 -57.513 -11.096 1.00 109.64 ? 380 ASP   A CG  1 
ATOM   2592 O  OD1 . ASP   A 1 360 ? -25.533 -56.777 -11.000 1.00 108.24 ? 380 ASP   A OD1 1 
ATOM   2593 O  OD2 . ASP   A 1 360 ? -26.464 -58.754 -11.219 1.00 116.71 ? 380 ASP   A OD2 1 
ATOM   2594 N  N   . VAL   A 1 361 ? -29.211 -54.179 -12.671 1.00 100.75 ? 381 VAL   A N   1 
ATOM   2595 C  CA  . VAL   A 1 361 ? -30.414 -53.531 -13.180 1.00 106.07 ? 381 VAL   A CA  1 
ATOM   2596 C  C   . VAL   A 1 361 ? -30.472 -53.669 -14.693 1.00 104.85 ? 381 VAL   A C   1 
ATOM   2597 O  O   . VAL   A 1 361 ? -29.449 -53.807 -15.369 1.00 103.49 ? 381 VAL   A O   1 
ATOM   2598 C  CB  . VAL   A 1 361 ? -30.486 -52.038 -12.782 1.00 99.48  ? 381 VAL   A CB  1 
ATOM   2599 C  CG1 . VAL   A 1 361 ? -31.066 -51.892 -11.393 1.00 106.41 ? 381 VAL   A CG1 1 
ATOM   2600 C  CG2 . VAL   A 1 361 ? -29.110 -51.392 -12.875 1.00 91.17  ? 381 VAL   A CG2 1 
ATOM   2601 N  N   . GLU   A 1 362 ? -31.693 -53.629 -15.214 1.00 106.11 ? 382 GLU   A N   1 
ATOM   2602 C  CA  . GLU   A 1 362 ? -31.966 -53.516 -16.639 1.00 111.02 ? 382 GLU   A CA  1 
ATOM   2603 C  C   . GLU   A 1 362 ? -32.653 -52.182 -16.886 1.00 106.75 ? 382 GLU   A C   1 
ATOM   2604 O  O   . GLU   A 1 362 ? -33.666 -51.877 -16.249 1.00 113.46 ? 382 GLU   A O   1 
ATOM   2605 C  CB  . GLU   A 1 362 ? -32.855 -54.664 -17.120 1.00 122.22 ? 382 GLU   A CB  1 
ATOM   2606 C  CG  . GLU   A 1 362 ? -32.162 -55.679 -18.007 1.00 128.84 ? 382 GLU   A CG  1 
ATOM   2607 C  CD  . GLU   A 1 362 ? -33.054 -56.860 -18.332 1.00 145.53 ? 382 GLU   A CD  1 
ATOM   2608 O  OE1 . GLU   A 1 362 ? -33.539 -57.517 -17.386 1.00 148.14 ? 382 GLU   A OE1 1 
ATOM   2609 O  OE2 . GLU   A 1 362 ? -33.282 -57.123 -19.531 1.00 147.99 ? 382 GLU   A OE2 1 
ATOM   2610 N  N   . ILE   A 1 363 ? -32.098 -51.382 -17.792 1.00 112.14 ? 383 ILE   A N   1 
ATOM   2611 C  CA  . ILE   A 1 363 ? -32.675 -50.086 -18.131 1.00 111.86 ? 383 ILE   A CA  1 
ATOM   2612 C  C   . ILE   A 1 363 ? -32.796 -49.995 -19.647 1.00 112.61 ? 383 ILE   A C   1 
ATOM   2613 O  O   . ILE   A 1 363 ? -31.787 -50.049 -20.362 1.00 102.16 ? 383 ILE   A O   1 
ATOM   2614 C  CB  . ILE   A 1 363 ? -31.857 -48.912 -17.560 1.00 108.90 ? 383 ILE   A CB  1 
ATOM   2615 C  CG1 . ILE   A 1 363 ? -30.388 -48.980 -17.985 1.00 93.42  ? 383 ILE   A CG1 1 
ATOM   2616 C  CG2 . ILE   A 1 363 ? -31.942 -48.901 -16.040 1.00 111.86 ? 383 ILE   A CG2 1 
ATOM   2617 C  CD1 . ILE   A 1 363 ? -29.625 -47.712 -17.694 1.00 98.58  ? 383 ILE   A CD1 1 
ATOM   2618 N  N   . ASN   A 1 364 ? -34.032 -49.887 -20.133 1.00 114.65 ? 384 ASN   A N   1 
ATOM   2619 C  CA  . ASN   A 1 364 ? -34.320 -49.725 -21.556 1.00 119.06 ? 384 ASN   A CA  1 
ATOM   2620 C  C   . ASN   A 1 364 ? -33.680 -50.839 -22.385 1.00 117.19 ? 384 ASN   A C   1 
ATOM   2621 O  O   . ASN   A 1 364 ? -33.070 -50.603 -23.431 1.00 111.95 ? 384 ASN   A O   1 
ATOM   2622 C  CB  . ASN   A 1 364 ? -33.877 -48.344 -22.042 1.00 119.31 ? 384 ASN   A CB  1 
ATOM   2623 C  CG  . ASN   A 1 364 ? -34.485 -47.220 -21.227 1.00 109.53 ? 384 ASN   A CG  1 
ATOM   2624 O  OD1 . ASN   A 1 364 ? -35.589 -46.756 -21.513 1.00 118.84 ? 384 ASN   A OD1 1 
ATOM   2625 N  ND2 . ASN   A 1 364 ? -33.769 -46.780 -20.198 1.00 104.90 ? 384 ASN   A ND2 1 
ATOM   2626 N  N   . GLY   A 1 365 ? -33.818 -52.072 -21.898 1.00 118.05 ? 385 GLY   A N   1 
ATOM   2627 C  CA  . GLY   A 1 365 ? -33.380 -53.247 -22.623 1.00 119.50 ? 385 GLY   A CA  1 
ATOM   2628 C  C   . GLY   A 1 365 ? -31.935 -53.648 -22.422 1.00 124.14 ? 385 GLY   A C   1 
ATOM   2629 O  O   . GLY   A 1 365 ? -31.509 -54.663 -22.990 1.00 124.92 ? 385 GLY   A O   1 
ATOM   2630 N  N   . MET   A 1 366 ? -31.169 -52.903 -21.631 1.00 116.02 ? 386 MET   A N   1 
ATOM   2631 C  CA  . MET   A 1 366 ? -29.745 -53.152 -21.451 1.00 109.42 ? 386 MET   A CA  1 
ATOM   2632 C  C   . MET   A 1 366 ? -29.483 -53.612 -20.024 1.00 107.55 ? 386 MET   A C   1 
ATOM   2633 O  O   . MET   A 1 366 ? -29.839 -52.914 -19.068 1.00 96.44  ? 386 MET   A O   1 
ATOM   2634 C  CB  . MET   A 1 366 ? -28.932 -51.897 -21.764 1.00 108.66 ? 386 MET   A CB  1 
ATOM   2635 C  CG  . MET   A 1 366 ? -27.430 -52.082 -21.657 1.00 101.70 ? 386 MET   A CG  1 
ATOM   2636 S  SD  . MET   A 1 366 ? -26.576 -50.741 -22.498 1.00 109.24 ? 386 MET   A SD  1 
ATOM   2637 C  CE  . MET   A 1 366 ? -27.485 -50.729 -24.042 1.00 117.00 ? 386 MET   A CE  1 
ATOM   2638 N  N   . PHE   A 1 367 ? -28.857 -54.778 -19.882 1.00 109.52 ? 387 PHE   A N   1 
ATOM   2639 C  CA  . PHE   A 1 367 ? -28.454 -55.261 -18.570 1.00 102.32 ? 387 PHE   A CA  1 
ATOM   2640 C  C   . PHE   A 1 367 ? -27.167 -54.571 -18.137 1.00 101.58 ? 387 PHE   A C   1 
ATOM   2641 O  O   . PHE   A 1 367 ? -26.222 -54.449 -18.923 1.00 100.98 ? 387 PHE   A O   1 
ATOM   2642 C  CB  . PHE   A 1 367 ? -28.259 -56.776 -18.580 1.00 96.17  ? 387 PHE   A CB  1 
ATOM   2643 C  CG  . PHE   A 1 367 ? -27.648 -57.308 -17.315 1.00 111.47 ? 387 PHE   A CG  1 
ATOM   2644 C  CD1 . PHE   A 1 367 ? -28.358 -57.282 -16.127 1.00 113.39 ? 387 PHE   A CD1 1 
ATOM   2645 C  CD2 . PHE   A 1 367 ? -26.363 -57.826 -17.310 1.00 114.41 ? 387 PHE   A CD2 1 
ATOM   2646 C  CE1 . PHE   A 1 367 ? -27.801 -57.762 -14.960 1.00 113.73 ? 387 PHE   A CE1 1 
ATOM   2647 C  CE2 . PHE   A 1 367 ? -25.801 -58.311 -16.144 1.00 114.86 ? 387 PHE   A CE2 1 
ATOM   2648 C  CZ  . PHE   A 1 367 ? -26.522 -58.280 -14.968 1.00 111.79 ? 387 PHE   A CZ  1 
ATOM   2649 N  N   . ILE   A 1 368 ? -27.135 -54.117 -16.884 1.00 99.03  ? 388 ILE   A N   1 
ATOM   2650 C  CA  . ILE   A 1 368 ? -25.976 -53.446 -16.318 1.00 96.66  ? 388 ILE   A CA  1 
ATOM   2651 C  C   . ILE   A 1 368 ? -25.628 -54.134 -15.005 1.00 100.11 ? 388 ILE   A C   1 
ATOM   2652 O  O   . ILE   A 1 368 ? -26.458 -54.176 -14.092 1.00 102.11 ? 388 ILE   A O   1 
ATOM   2653 C  CB  . ILE   A 1 368 ? -26.223 -51.944 -16.085 1.00 96.51  ? 388 ILE   A CB  1 
ATOM   2654 C  CG1 . ILE   A 1 368 ? -26.539 -51.248 -17.409 1.00 96.89  ? 388 ILE   A CG1 1 
ATOM   2655 C  CG2 . ILE   A 1 368 ? -25.017 -51.302 -15.418 1.00 96.19  ? 388 ILE   A CG2 1 
ATOM   2656 C  CD1 . ILE   A 1 368 ? -26.745 -49.763 -17.275 1.00 89.04  ? 388 ILE   A CD1 1 
ATOM   2657 N  N   . PRO   A 1 369 ? -24.429 -54.684 -14.854 1.00 100.56 ? 389 PRO   A N   1 
ATOM   2658 C  CA  . PRO   A 1 369 ? -24.083 -55.394 -13.621 1.00 90.42  ? 389 PRO   A CA  1 
ATOM   2659 C  C   . PRO   A 1 369 ? -23.731 -54.421 -12.502 1.00 97.37  ? 389 PRO   A C   1 
ATOM   2660 O  O   . PRO   A 1 369 ? -23.488 -53.234 -12.716 1.00 99.23  ? 389 PRO   A O   1 
ATOM   2661 C  CB  . PRO   A 1 369 ? -22.868 -56.246 -14.019 1.00 93.37  ? 389 PRO   A CB  1 
ATOM   2662 C  CG  . PRO   A 1 369 ? -22.558 -55.892 -15.469 1.00 95.09  ? 389 PRO   A CG  1 
ATOM   2663 C  CD  . PRO   A 1 369 ? -23.297 -54.635 -15.790 1.00 91.96  ? 389 PRO   A CD  1 
ATOM   2664 N  N   . LYS   A 1 370 ? -23.710 -54.962 -11.287 1.00 97.00  ? 390 LYS   A N   1 
ATOM   2665 C  CA  . LYS   A 1 370 ? -23.397 -54.180 -10.101 1.00 91.84  ? 390 LYS   A CA  1 
ATOM   2666 C  C   . LYS   A 1 370 ? -21.952 -53.686 -10.142 1.00 90.92  ? 390 LYS   A C   1 
ATOM   2667 O  O   . LYS   A 1 370 ? -21.079 -54.294 -10.768 1.00 93.81  ? 390 LYS   A O   1 
ATOM   2668 C  CB  . LYS   A 1 370 ? -23.641 -55.022 -8.847  1.00 90.71  ? 390 LYS   A CB  1 
ATOM   2669 C  CG  . LYS   A 1 370 ? -23.486 -54.293 -7.524  1.00 89.00  ? 390 LYS   A CG  1 
ATOM   2670 C  CD  . LYS   A 1 370 ? -23.648 -55.262 -6.367  1.00 88.97  ? 390 LYS   A CD  1 
ATOM   2671 C  CE  . LYS   A 1 370 ? -23.253 -54.632 -5.046  1.00 92.84  ? 390 LYS   A CE  1 
ATOM   2672 N  NZ  . LYS   A 1 370 ? -23.280 -55.630 -3.941  1.00 123.37 ? 390 LYS   A NZ  1 
ATOM   2673 N  N   . GLY   A 1 371 ? -21.709 -52.554 -9.478  1.00 93.43  ? 391 GLY   A N   1 
ATOM   2674 C  CA  . GLY   A 1 371 ? -20.382 -51.985 -9.381  1.00 84.55  ? 391 GLY   A CA  1 
ATOM   2675 C  C   . GLY   A 1 371 ? -19.913 -51.216 -10.595 1.00 78.17  ? 391 GLY   A C   1 
ATOM   2676 O  O   . GLY   A 1 371 ? -18.905 -50.503 -10.502 1.00 80.33  ? 391 GLY   A O   1 
ATOM   2677 N  N   . VAL   A 1 372 ? -20.602 -51.334 -11.730 1.00 75.53  ? 392 VAL   A N   1 
ATOM   2678 C  CA  . VAL   A 1 372 ? -20.210 -50.614 -12.934 1.00 76.69  ? 392 VAL   A CA  1 
ATOM   2679 C  C   . VAL   A 1 372 ? -20.451 -49.123 -12.745 1.00 76.14  ? 392 VAL   A C   1 
ATOM   2680 O  O   . VAL   A 1 372 ? -21.441 -48.705 -12.130 1.00 77.81  ? 392 VAL   A O   1 
ATOM   2681 C  CB  . VAL   A 1 372 ? -20.982 -51.159 -14.150 1.00 69.25  ? 392 VAL   A CB  1 
ATOM   2682 C  CG1 . VAL   A 1 372 ? -20.844 -50.231 -15.350 1.00 66.00  ? 392 VAL   A CG1 1 
ATOM   2683 C  CG2 . VAL   A 1 372 ? -20.499 -52.556 -14.502 1.00 74.10  ? 392 VAL   A CG2 1 
ATOM   2684 N  N   . VAL   A 1 373 ? -19.532 -48.311 -13.258 1.00 71.29  ? 393 VAL   A N   1 
ATOM   2685 C  CA  . VAL   A 1 373 ? -19.713 -46.865 -13.310 1.00 70.18  ? 393 VAL   A CA  1 
ATOM   2686 C  C   . VAL   A 1 373 ? -20.390 -46.520 -14.630 1.00 72.11  ? 393 VAL   A C   1 
ATOM   2687 O  O   . VAL   A 1 373 ? -19.830 -46.759 -15.706 1.00 73.89  ? 393 VAL   A O   1 
ATOM   2688 C  CB  . VAL   A 1 373 ? -18.372 -46.129 -13.169 1.00 65.53  ? 393 VAL   A CB  1 
ATOM   2689 C  CG1 . VAL   A 1 373 ? -18.569 -44.632 -13.352 1.00 64.23  ? 393 VAL   A CG1 1 
ATOM   2690 C  CG2 . VAL   A 1 373 ? -17.741 -46.426 -11.820 1.00 68.00  ? 393 VAL   A CG2 1 
ATOM   2691 N  N   . VAL   A 1 374 ? -21.597 -45.971 -14.552 1.00 66.17  ? 394 VAL   A N   1 
ATOM   2692 C  CA  . VAL   A 1 374 ? -22.322 -45.507 -15.730 1.00 67.17  ? 394 VAL   A CA  1 
ATOM   2693 C  C   . VAL   A 1 374 ? -21.984 -44.039 -15.950 1.00 62.19  ? 394 VAL   A C   1 
ATOM   2694 O  O   . VAL   A 1 374 ? -22.117 -43.218 -15.035 1.00 61.75  ? 394 VAL   A O   1 
ATOM   2695 C  CB  . VAL   A 1 374 ? -23.836 -45.716 -15.566 1.00 71.77  ? 394 VAL   A CB  1 
ATOM   2696 C  CG1 . VAL   A 1 374 ? -24.592 -44.949 -16.639 1.00 70.55  ? 394 VAL   A CG1 1 
ATOM   2697 C  CG2 . VAL   A 1 374 ? -24.169 -47.200 -15.637 1.00 76.27  ? 394 VAL   A CG2 1 
ATOM   2698 N  N   . MET   A 1 375 ? -21.543 -43.707 -17.162 1.00 60.47  ? 395 MET   A N   1 
ATOM   2699 C  CA  A MET   A 1 375 ? -21.038 -42.378 -17.482 0.64 71.06  ? 395 MET   A CA  1 
ATOM   2700 C  CA  B MET   A 1 375 ? -21.039 -42.379 -17.484 0.36 70.15  ? 395 MET   A CA  1 
ATOM   2701 C  C   . MET   A 1 375 ? -21.869 -41.759 -18.597 1.00 69.08  ? 395 MET   A C   1 
ATOM   2702 O  O   . MET   A 1 375 ? -22.186 -42.425 -19.588 1.00 69.73  ? 395 MET   A O   1 
ATOM   2703 C  CB  A MET   A 1 375 ? -19.560 -42.445 -17.884 0.64 65.12  ? 395 MET   A CB  1 
ATOM   2704 C  CB  B MET   A 1 375 ? -19.570 -42.444 -17.904 0.36 61.60  ? 395 MET   A CB  1 
ATOM   2705 C  CG  A MET   A 1 375 ? -18.907 -41.096 -18.150 0.64 68.80  ? 395 MET   A CG  1 
ATOM   2706 C  CG  B MET   A 1 375 ? -18.984 -41.103 -18.303 0.36 69.39  ? 395 MET   A CG  1 
ATOM   2707 S  SD  A MET   A 1 375 ? -18.966 -40.609 -19.885 0.64 65.24  ? 395 MET   A SD  1 
ATOM   2708 S  SD  B MET   A 1 375 ? -17.368 -41.269 -19.078 0.36 83.79  ? 395 MET   A SD  1 
ATOM   2709 C  CE  A MET   A 1 375 ? -17.926 -41.861 -20.630 0.64 73.30  ? 395 MET   A CE  1 
ATOM   2710 C  CE  B MET   A 1 375 ? -17.819 -41.868 -20.703 0.36 73.49  ? 395 MET   A CE  1 
ATOM   2711 N  N   . ILE   A 1 376 ? -22.213 -40.487 -18.435 1.00 63.39  ? 396 ILE   A N   1 
ATOM   2712 C  CA  . ILE   A 1 376 ? -22.930 -39.713 -19.441 1.00 71.13  ? 396 ILE   A CA  1 
ATOM   2713 C  C   . ILE   A 1 376 ? -21.940 -38.709 -20.023 1.00 67.43  ? 396 ILE   A C   1 
ATOM   2714 O  O   . ILE   A 1 376 ? -21.566 -37.749 -19.331 1.00 65.20  ? 396 ILE   A O   1 
ATOM   2715 C  CB  . ILE   A 1 376 ? -24.155 -38.999 -18.851 1.00 68.37  ? 396 ILE   A CB  1 
ATOM   2716 C  CG1 . ILE   A 1 376 ? -25.203 -40.008 -18.393 1.00 59.44  ? 396 ILE   A CG1 1 
ATOM   2717 C  CG2 . ILE   A 1 376 ? -24.776 -38.064 -19.873 1.00 62.41  ? 396 ILE   A CG2 1 
ATOM   2718 C  CD1 . ILE   A 1 376 ? -25.087 -40.430 -16.944 1.00 67.76  ? 396 ILE   A CD1 1 
ATOM   2719 N  N   . PRO   A 1 377 ? -21.473 -38.889 -21.249 1.00 69.04  ? 397 PRO   A N   1 
ATOM   2720 C  CA  . PRO   A 1 377 ? -20.447 -37.980 -21.787 1.00 69.90  ? 397 PRO   A CA  1 
ATOM   2721 C  C   . PRO   A 1 377 ? -21.013 -36.616 -22.176 1.00 71.93  ? 397 PRO   A C   1 
ATOM   2722 O  O   . PRO   A 1 377 ? -21.405 -36.415 -23.327 1.00 74.65  ? 397 PRO   A O   1 
ATOM   2723 C  CB  . PRO   A 1 377 ? -19.909 -38.747 -22.997 1.00 73.49  ? 397 PRO   A CB  1 
ATOM   2724 C  CG  . PRO   A 1 377 ? -21.046 -39.606 -23.429 1.00 66.34  ? 397 PRO   A CG  1 
ATOM   2725 C  CD  . PRO   A 1 377 ? -21.790 -39.987 -22.178 1.00 65.39  ? 397 PRO   A CD  1 
ATOM   2726 N  N   . SER   A 1 378 ? -21.063 -35.672 -21.227 1.00 68.44  ? 398 SER   A N   1 
ATOM   2727 C  CA  . SER   A 1 378 ? -21.698 -34.378 -21.485 1.00 62.78  ? 398 SER   A CA  1 
ATOM   2728 C  C   . SER   A 1 378 ? -21.033 -33.648 -22.650 1.00 73.01  ? 398 SER   A C   1 
ATOM   2729 O  O   . SER   A 1 378 ? -21.705 -33.210 -23.591 1.00 75.73  ? 398 SER   A O   1 
ATOM   2730 C  CB  . SER   A 1 378 ? -21.670 -33.511 -20.225 1.00 71.62  ? 398 SER   A CB  1 
ATOM   2731 O  OG  . SER   A 1 378 ? -22.545 -34.014 -19.231 1.00 78.64  ? 398 SER   A OG  1 
ATOM   2732 N  N   . TYR   A 1 379 ? -19.705 -33.502 -22.595 1.00 67.78  ? 399 TYR   A N   1 
ATOM   2733 C  CA  . TYR   A 1 379 ? -18.983 -32.774 -23.638 1.00 79.06  ? 399 TYR   A CA  1 
ATOM   2734 C  C   . TYR   A 1 379 ? -19.233 -33.380 -25.012 1.00 82.85  ? 399 TYR   A C   1 
ATOM   2735 O  O   . TYR   A 1 379 ? -19.433 -32.655 -25.995 1.00 82.42  ? 399 TYR   A O   1 
ATOM   2736 C  CB  . TYR   A 1 379 ? -17.486 -32.763 -23.324 1.00 74.35  ? 399 TYR   A CB  1 
ATOM   2737 C  CG  . TYR   A 1 379 ? -16.624 -32.025 -24.331 1.00 84.31  ? 399 TYR   A CG  1 
ATOM   2738 C  CD1 . TYR   A 1 379 ? -16.195 -32.647 -25.498 1.00 83.94  ? 399 TYR   A CD1 1 
ATOM   2739 C  CD2 . TYR   A 1 379 ? -16.231 -30.710 -24.110 1.00 88.38  ? 399 TYR   A CD2 1 
ATOM   2740 C  CE1 . TYR   A 1 379 ? -15.407 -31.982 -26.417 1.00 95.11  ? 399 TYR   A CE1 1 
ATOM   2741 C  CE2 . TYR   A 1 379 ? -15.441 -30.035 -25.027 1.00 85.12  ? 399 TYR   A CE2 1 
ATOM   2742 C  CZ  . TYR   A 1 379 ? -15.031 -30.678 -26.178 1.00 80.53  ? 399 TYR   A CZ  1 
ATOM   2743 O  OH  . TYR   A 1 379 ? -14.247 -30.017 -27.096 1.00 88.24  ? 399 TYR   A OH  1 
ATOM   2744 N  N   . ALA   A 1 380 ? -19.224 -34.712 -25.099 1.00 81.11  ? 400 ALA   A N   1 
ATOM   2745 C  CA  . ALA   A 1 380 ? -19.387 -35.375 -26.387 1.00 77.80  ? 400 ALA   A CA  1 
ATOM   2746 C  C   . ALA   A 1 380 ? -20.812 -35.261 -26.912 1.00 85.03  ? 400 ALA   A C   1 
ATOM   2747 O  O   . ALA   A 1 380 ? -21.022 -35.302 -28.129 1.00 94.72  ? 400 ALA   A O   1 
ATOM   2748 C  CB  . ALA   A 1 380 ? -18.975 -36.843 -26.281 1.00 67.77  ? 400 ALA   A CB  1 
ATOM   2749 N  N   . LEU   A 1 381 ? -21.801 -35.125 -26.025 1.00 80.75  ? 401 LEU   A N   1 
ATOM   2750 C  CA  . LEU   A 1 381 ? -23.175 -34.914 -26.471 1.00 80.68  ? 401 LEU   A CA  1 
ATOM   2751 C  C   . LEU   A 1 381 ? -23.440 -33.454 -26.818 1.00 81.99  ? 401 LEU   A C   1 
ATOM   2752 O  O   . LEU   A 1 381 ? -24.205 -33.168 -27.748 1.00 89.40  ? 401 LEU   A O   1 
ATOM   2753 C  CB  . LEU   A 1 381 ? -24.154 -35.384 -25.394 1.00 80.53  ? 401 LEU   A CB  1 
ATOM   2754 C  CG  . LEU   A 1 381 ? -24.065 -36.856 -24.985 1.00 79.58  ? 401 LEU   A CG  1 
ATOM   2755 C  CD1 . LEU   A 1 381 ? -24.913 -37.118 -23.751 1.00 75.83  ? 401 LEU   A CD1 1 
ATOM   2756 C  CD2 . LEU   A 1 381 ? -24.476 -37.769 -26.132 1.00 84.95  ? 401 LEU   A CD2 1 
ATOM   2757 N  N   . HIS   A 1 382 ? -22.818 -32.525 -26.089 1.00 80.26  ? 402 HIS   A N   1 
ATOM   2758 C  CA  . HIS   A 1 382 ? -22.969 -31.105 -26.382 1.00 84.24  ? 402 HIS   A CA  1 
ATOM   2759 C  C   . HIS   A 1 382 ? -22.383 -30.725 -27.735 1.00 91.10  ? 402 HIS   A C   1 
ATOM   2760 O  O   . HIS   A 1 382 ? -22.695 -29.646 -28.250 1.00 93.04  ? 402 HIS   A O   1 
ATOM   2761 C  CB  . HIS   A 1 382 ? -22.310 -30.267 -25.286 1.00 83.08  ? 402 HIS   A CB  1 
ATOM   2762 C  CG  . HIS   A 1 382 ? -23.058 -30.263 -23.989 1.00 82.13  ? 402 HIS   A CG  1 
ATOM   2763 N  ND1 . HIS   A 1 382 ? -22.771 -29.383 -22.967 1.00 76.51  ? 402 HIS   A ND1 1 
ATOM   2764 C  CD2 . HIS   A 1 382 ? -24.083 -31.029 -23.548 1.00 77.74  ? 402 HIS   A CD2 1 
ATOM   2765 C  CE1 . HIS   A 1 382 ? -23.587 -29.608 -21.952 1.00 77.78  ? 402 HIS   A CE1 1 
ATOM   2766 N  NE2 . HIS   A 1 382 ? -24.393 -30.602 -22.279 1.00 74.09  ? 402 HIS   A NE2 1 
ATOM   2767 N  N   . ARG   A 1 383 ? -21.533 -31.575 -28.314 1.00 98.43  ? 403 ARG   A N   1 
ATOM   2768 C  CA  . ARG   A 1 383 ? -20.945 -31.327 -29.624 1.00 92.64  ? 403 ARG   A CA  1 
ATOM   2769 C  C   . ARG   A 1 383 ? -21.288 -32.431 -30.617 1.00 100.29 ? 403 ARG   A C   1 
ATOM   2770 O  O   . ARG   A 1 383 ? -20.544 -32.655 -31.576 1.00 112.39 ? 403 ARG   A O   1 
ATOM   2771 C  CB  . ARG   A 1 383 ? -19.429 -31.163 -29.503 1.00 84.20  ? 403 ARG   A CB  1 
ATOM   2772 C  CG  . ARG   A 1 383 ? -19.014 -29.936 -28.712 1.00 83.87  ? 403 ARG   A CG  1 
ATOM   2773 C  CD  . ARG   A 1 383 ? -17.543 -29.984 -28.349 1.00 91.48  ? 403 ARG   A CD  1 
ATOM   2774 N  NE  . ARG   A 1 383 ? -17.117 -28.789 -27.631 1.00 94.16  ? 403 ARG   A NE  1 
ATOM   2775 C  CZ  . ARG   A 1 383 ? -16.396 -27.812 -28.164 1.00 89.01  ? 403 ARG   A CZ  1 
ATOM   2776 N  NH1 . ARG   A 1 383 ? -15.987 -27.863 -29.421 1.00 92.78  ? 403 ARG   A NH1 1 
ATOM   2777 N  NH2 . ARG   A 1 383 ? -16.074 -26.760 -27.417 1.00 86.67  ? 403 ARG   A NH2 1 
ATOM   2778 N  N   . ASP   A 1 384 ? -22.399 -33.125 -30.400 1.00 99.92  ? 404 ASP   A N   1 
ATOM   2779 C  CA  . ASP   A 1 384 ? -22.838 -34.170 -31.316 1.00 109.66 ? 404 ASP   A CA  1 
ATOM   2780 C  C   . ASP   A 1 384 ? -23.539 -33.537 -32.511 1.00 118.21 ? 404 ASP   A C   1 
ATOM   2781 O  O   . ASP   A 1 384 ? -24.573 -32.883 -32.332 1.00 115.50 ? 404 ASP   A O   1 
ATOM   2782 C  CB  . ASP   A 1 384 ? -23.775 -35.138 -30.601 1.00 106.89 ? 404 ASP   A CB  1 
ATOM   2783 C  CG  . ASP   A 1 384 ? -24.241 -36.279 -31.493 1.00 120.44 ? 404 ASP   A CG  1 
ATOM   2784 O  OD1 . ASP   A 1 384 ? -23.669 -36.467 -32.588 1.00 123.27 ? 404 ASP   A OD1 1 
ATOM   2785 O  OD2 . ASP   A 1 384 ? -25.187 -36.991 -31.094 1.00 121.98 ? 404 ASP   A OD2 1 
ATOM   2786 N  N   . PRO   A 1 385 ? -23.016 -33.692 -33.730 1.00 121.99 ? 405 PRO   A N   1 
ATOM   2787 C  CA  . PRO   A 1 385 ? -23.713 -33.125 -34.896 1.00 128.69 ? 405 PRO   A CA  1 
ATOM   2788 C  C   . PRO   A 1 385 ? -25.090 -33.721 -35.116 1.00 129.56 ? 405 PRO   A C   1 
ATOM   2789 O  O   . PRO   A 1 385 ? -25.963 -33.051 -35.684 1.00 124.53 ? 405 PRO   A O   1 
ATOM   2790 C  CB  . PRO   A 1 385 ? -22.767 -33.446 -36.063 1.00 115.11 ? 405 PRO   A CB  1 
ATOM   2791 C  CG  . PRO   A 1 385 ? -21.434 -33.689 -35.427 1.00 127.72 ? 405 PRO   A CG  1 
ATOM   2792 C  CD  . PRO   A 1 385 ? -21.730 -34.307 -34.096 1.00 114.89 ? 405 PRO   A CD  1 
ATOM   2793 N  N   . LYS   A 1 386 ? -25.315 -34.961 -34.674 1.00 130.50 ? 406 LYS   A N   1 
ATOM   2794 C  CA  . LYS   A 1 386 ? -26.619 -35.593 -34.842 1.00 139.17 ? 406 LYS   A CA  1 
ATOM   2795 C  C   . LYS   A 1 386 ? -27.709 -34.881 -34.051 1.00 133.77 ? 406 LYS   A C   1 
ATOM   2796 O  O   . LYS   A 1 386 ? -28.896 -35.107 -34.309 1.00 136.01 ? 406 LYS   A O   1 
ATOM   2797 C  CB  . LYS   A 1 386 ? -26.538 -37.066 -34.438 1.00 145.57 ? 406 LYS   A CB  1 
ATOM   2798 C  CG  . LYS   A 1 386 ? -25.416 -37.818 -35.136 1.00 151.50 ? 406 LYS   A CG  1 
ATOM   2799 C  CD  . LYS   A 1 386 ? -25.614 -39.322 -35.079 1.00 168.87 ? 406 LYS   A CD  1 
ATOM   2800 C  CE  . LYS   A 1 386 ? -24.582 -40.036 -35.937 1.00 174.13 ? 406 LYS   A CE  1 
ATOM   2801 N  NZ  . LYS   A 1 386 ? -24.885 -41.485 -36.084 1.00 179.15 ? 406 LYS   A NZ  1 
ATOM   2802 N  N   . TYR   A 1 387 ? -27.334 -34.031 -33.095 1.00 129.89 ? 407 TYR   A N   1 
ATOM   2803 C  CA  . TYR   A 1 387 ? -28.275 -33.168 -32.396 1.00 123.94 ? 407 TYR   A CA  1 
ATOM   2804 C  C   . TYR   A 1 387 ? -28.074 -31.690 -32.687 1.00 119.02 ? 407 TYR   A C   1 
ATOM   2805 O  O   . TYR   A 1 387 ? -29.051 -30.938 -32.689 1.00 122.86 ? 407 TYR   A O   1 
ATOM   2806 C  CB  . TYR   A 1 387 ? -28.176 -33.378 -30.880 1.00 115.29 ? 407 TYR   A CB  1 
ATOM   2807 C  CG  . TYR   A 1 387 ? -28.875 -34.615 -30.368 1.00 121.83 ? 407 TYR   A CG  1 
ATOM   2808 C  CD1 . TYR   A 1 387 ? -30.244 -34.614 -30.134 1.00 114.63 ? 407 TYR   A CD1 1 
ATOM   2809 C  CD2 . TYR   A 1 387 ? -28.165 -35.777 -30.101 1.00 129.21 ? 407 TYR   A CD2 1 
ATOM   2810 C  CE1 . TYR   A 1 387 ? -30.888 -35.738 -29.660 1.00 127.66 ? 407 TYR   A CE1 1 
ATOM   2811 C  CE2 . TYR   A 1 387 ? -28.800 -36.908 -29.625 1.00 126.52 ? 407 TYR   A CE2 1 
ATOM   2812 C  CZ  . TYR   A 1 387 ? -30.161 -36.882 -29.407 1.00 129.75 ? 407 TYR   A CZ  1 
ATOM   2813 O  OH  . TYR   A 1 387 ? -30.802 -38.003 -28.933 1.00 127.49 ? 407 TYR   A OH  1 
ATOM   2814 N  N   . TRP   A 1 388 ? -26.841 -31.259 -32.938 1.00 118.31 ? 408 TRP   A N   1 
ATOM   2815 C  CA  . TRP   A 1 388 ? -26.500 -29.846 -33.054 1.00 118.01 ? 408 TRP   A CA  1 
ATOM   2816 C  C   . TRP   A 1 388 ? -26.050 -29.536 -34.475 1.00 122.14 ? 408 TRP   A C   1 
ATOM   2817 O  O   . TRP   A 1 388 ? -25.072 -30.114 -34.961 1.00 124.66 ? 408 TRP   A O   1 
ATOM   2818 C  CB  . TRP   A 1 388 ? -25.402 -29.472 -32.057 1.00 107.95 ? 408 TRP   A CB  1 
ATOM   2819 C  CG  . TRP   A 1 388 ? -25.731 -29.832 -30.643 1.00 106.01 ? 408 TRP   A CG  1 
ATOM   2820 C  CD1 . TRP   A 1 388 ? -25.360 -30.962 -29.976 1.00 100.77 ? 408 TRP   A CD1 1 
ATOM   2821 C  CD2 . TRP   A 1 388 ? -26.505 -29.057 -29.722 1.00 107.13 ? 408 TRP   A CD2 1 
ATOM   2822 N  NE1 . TRP   A 1 388 ? -25.854 -30.938 -28.694 1.00 94.21  ? 408 TRP   A NE1 1 
ATOM   2823 C  CE2 . TRP   A 1 388 ? -26.561 -29.779 -28.513 1.00 101.01 ? 408 TRP   A CE2 1 
ATOM   2824 C  CE3 . TRP   A 1 388 ? -27.156 -27.822 -29.801 1.00 99.45  ? 408 TRP   A CE3 1 
ATOM   2825 C  CZ2 . TRP   A 1 388 ? -27.241 -29.306 -27.393 1.00 88.56  ? 408 TRP   A CZ2 1 
ATOM   2826 C  CZ3 . TRP   A 1 388 ? -27.832 -27.355 -28.688 1.00 99.17  ? 408 TRP   A CZ3 1 
ATOM   2827 C  CH2 . TRP   A 1 388 ? -27.868 -28.095 -27.500 1.00 98.69  ? 408 TRP   A CH2 1 
ATOM   2828 N  N   . THR   A 1 389 ? -26.758 -28.621 -35.132 1.00 112.49 ? 409 THR   A N   1 
ATOM   2829 C  CA  . THR   A 1 389 ? -26.322 -28.125 -36.431 1.00 123.48 ? 409 THR   A CA  1 
ATOM   2830 C  C   . THR   A 1 389 ? -25.121 -27.206 -36.250 1.00 124.63 ? 409 THR   A C   1 
ATOM   2831 O  O   . THR   A 1 389 ? -25.162 -26.272 -35.443 1.00 127.33 ? 409 THR   A O   1 
ATOM   2832 C  CB  . THR   A 1 389 ? -27.456 -27.375 -37.127 1.00 123.05 ? 409 THR   A CB  1 
ATOM   2833 O  OG1 . THR   A 1 389 ? -27.705 -26.141 -36.440 1.00 126.94 ? 409 THR   A OG1 1 
ATOM   2834 C  CG2 . THR   A 1 389 ? -28.726 -28.209 -37.124 1.00 114.91 ? 409 THR   A CG2 1 
ATOM   2835 N  N   . GLU   A 1 390 ? -24.058 -27.470 -37.006 1.00 121.15 ? 410 GLU   A N   1 
ATOM   2836 C  CA  . GLU   A 1 390 ? -22.806 -26.729 -36.903 1.00 124.60 ? 410 GLU   A CA  1 
ATOM   2837 C  C   . GLU   A 1 390 ? -22.349 -26.635 -35.442 1.00 125.43 ? 410 GLU   A C   1 
ATOM   2838 O  O   . GLU   A 1 390 ? -22.250 -25.542 -34.886 1.00 123.74 ? 410 GLU   A O   1 
ATOM   2839 C  CB  . GLU   A 1 390 ? -22.946 -25.342 -37.517 1.00 125.22 ? 410 GLU   A CB  1 
ATOM   2840 C  CG  . GLU   A 1 390 ? -23.321 -25.363 -38.994 1.00 128.41 ? 410 GLU   A CG  1 
ATOM   2841 C  CD  . GLU   A 1 390 ? -23.410 -23.976 -39.604 1.00 139.48 ? 410 GLU   A CD  1 
ATOM   2842 O  OE1 . GLU   A 1 390 ? -24.299 -23.197 -39.200 1.00 126.12 ? 410 GLU   A OE1 1 
ATOM   2843 O  OE2 . GLU   A 1 390 ? -22.584 -23.665 -40.488 1.00 150.41 ? 410 GLU   A OE2 1 
ATOM   2844 N  N   . PRO   A 1 391 ? -22.059 -27.775 -34.803 1.00 139.99 ? 411 PRO   A N   1 
ATOM   2845 C  CA  . PRO   A 1 391 ? -21.907 -27.775 -33.338 1.00 131.98 ? 411 PRO   A CA  1 
ATOM   2846 C  C   . PRO   A 1 391 ? -20.651 -27.085 -32.834 1.00 126.24 ? 411 PRO   A C   1 
ATOM   2847 O  O   . PRO   A 1 391 ? -20.645 -26.625 -31.686 1.00 124.88 ? 411 PRO   A O   1 
ATOM   2848 C  CB  . PRO   A 1 391 ? -21.898 -29.269 -32.989 1.00 130.44 ? 411 PRO   A CB  1 
ATOM   2849 C  CG  . PRO   A 1 391 ? -21.375 -29.931 -34.216 1.00 137.02 ? 411 PRO   A CG  1 
ATOM   2850 C  CD  . PRO   A 1 391 ? -21.870 -29.118 -35.381 1.00 143.66 ? 411 PRO   A CD  1 
ATOM   2851 N  N   . GLU   A 1 392 ? -19.589 -26.999 -33.637 1.00 124.20 ? 412 GLU   A N   1 
ATOM   2852 C  CA  . GLU   A 1 392 ? -18.382 -26.318 -33.183 1.00 119.69 ? 412 GLU   A CA  1 
ATOM   2853 C  C   . GLU   A 1 392 ? -18.536 -24.804 -33.137 1.00 114.71 ? 412 GLU   A C   1 
ATOM   2854 O  O   . GLU   A 1 392 ? -17.643 -24.127 -32.617 1.00 97.31  ? 412 GLU   A O   1 
ATOM   2855 C  CB  . GLU   A 1 392 ? -17.195 -26.678 -34.080 1.00 124.56 ? 412 GLU   A CB  1 
ATOM   2856 C  CG  . GLU   A 1 392 ? -16.386 -27.874 -33.606 1.00 126.94 ? 412 GLU   A CG  1 
ATOM   2857 C  CD  . GLU   A 1 392 ? -15.071 -28.015 -34.348 1.00 148.96 ? 412 GLU   A CD  1 
ATOM   2858 O  OE1 . GLU   A 1 392 ? -14.813 -27.203 -35.262 1.00 147.34 ? 412 GLU   A OE1 1 
ATOM   2859 O  OE2 . GLU   A 1 392 ? -14.293 -28.934 -34.016 1.00 157.43 ? 412 GLU   A OE2 1 
ATOM   2860 N  N   . LYS   A 1 393 ? -19.636 -24.261 -33.653 1.00 107.11 ? 413 LYS   A N   1 
ATOM   2861 C  CA  . LYS   A 1 393 ? -19.802 -22.820 -33.769 1.00 110.93 ? 413 LYS   A CA  1 
ATOM   2862 C  C   . LYS   A 1 393 ? -20.557 -22.256 -32.572 1.00 104.48 ? 413 LYS   A C   1 
ATOM   2863 O  O   . LYS   A 1 393 ? -21.509 -22.864 -32.073 1.00 98.13  ? 413 LYS   A O   1 
ATOM   2864 C  CB  . LYS   A 1 393 ? -20.537 -22.466 -35.063 1.00 113.74 ? 413 LYS   A CB  1 
ATOM   2865 C  CG  . LYS   A 1 393 ? -19.835 -22.960 -36.319 1.00 123.59 ? 413 LYS   A CG  1 
ATOM   2866 C  CD  . LYS   A 1 393 ? -20.613 -22.615 -37.581 1.00 126.03 ? 413 LYS   A CD  1 
ATOM   2867 C  CE  . LYS   A 1 393 ? -20.203 -21.265 -38.147 1.00 124.96 ? 413 LYS   A CE  1 
ATOM   2868 N  NZ  . LYS   A 1 393 ? -20.953 -20.942 -39.394 1.00 134.71 ? 413 LYS   A NZ  1 
ATOM   2869 N  N   . PHE   A 1 394 ? -20.115 -21.088 -32.114 1.00 107.25 ? 414 PHE   A N   1 
ATOM   2870 C  CA  . PHE   A 1 394 ? -20.780 -20.348 -31.046 1.00 97.37  ? 414 PHE   A CA  1 
ATOM   2871 C  C   . PHE   A 1 394 ? -21.990 -19.645 -31.646 1.00 103.10 ? 414 PHE   A C   1 
ATOM   2872 O  O   . PHE   A 1 394 ? -21.857 -18.621 -32.320 1.00 106.32 ? 414 PHE   A O   1 
ATOM   2873 C  CB  . PHE   A 1 394 ? -19.809 -19.360 -30.409 1.00 98.81  ? 414 PHE   A CB  1 
ATOM   2874 C  CG  . PHE   A 1 394 ? -20.429 -18.467 -29.370 1.00 96.14  ? 414 PHE   A CG  1 
ATOM   2875 C  CD1 . PHE   A 1 394 ? -20.587 -18.903 -28.065 1.00 92.34  ? 414 PHE   A CD1 1 
ATOM   2876 C  CD2 . PHE   A 1 394 ? -20.830 -17.181 -29.694 1.00 93.54  ? 414 PHE   A CD2 1 
ATOM   2877 C  CE1 . PHE   A 1 394 ? -21.149 -18.080 -27.106 1.00 91.70  ? 414 PHE   A CE1 1 
ATOM   2878 C  CE2 . PHE   A 1 394 ? -21.391 -16.352 -28.742 1.00 88.22  ? 414 PHE   A CE2 1 
ATOM   2879 C  CZ  . PHE   A 1 394 ? -21.551 -16.802 -27.446 1.00 95.02  ? 414 PHE   A CZ  1 
ATOM   2880 N  N   . LEU   A 1 395 ? -23.179 -20.202 -31.415 1.00 91.58  ? 415 LEU   A N   1 
ATOM   2881 C  CA  . LEU   A 1 395 ? -24.421 -19.681 -31.984 1.00 100.65 ? 415 LEU   A CA  1 
ATOM   2882 C  C   . LEU   A 1 395 ? -25.470 -19.592 -30.883 1.00 96.97  ? 415 LEU   A C   1 
ATOM   2883 O  O   . LEU   A 1 395 ? -26.220 -20.547 -30.643 1.00 101.50 ? 415 LEU   A O   1 
ATOM   2884 C  CB  . LEU   A 1 395 ? -24.903 -20.551 -33.144 1.00 98.09  ? 415 LEU   A CB  1 
ATOM   2885 C  CG  . LEU   A 1 395 ? -24.050 -20.472 -34.411 1.00 113.23 ? 415 LEU   A CG  1 
ATOM   2886 C  CD1 . LEU   A 1 395 ? -24.598 -21.393 -35.487 1.00 112.69 ? 415 LEU   A CD1 1 
ATOM   2887 C  CD2 . LEU   A 1 395 ? -23.992 -19.037 -34.906 1.00 97.62  ? 415 LEU   A CD2 1 
ATOM   2888 N  N   . PRO   A 1 396 ? -25.551 -18.452 -30.190 1.00 95.65  ? 416 PRO   A N   1 
ATOM   2889 C  CA  . PRO   A 1 396 ? -26.534 -18.301 -29.105 1.00 95.52  ? 416 PRO   A CA  1 
ATOM   2890 C  C   . PRO   A 1 396 ? -27.977 -18.533 -29.527 1.00 92.32  ? 416 PRO   A C   1 
ATOM   2891 O  O   . PRO   A 1 396 ? -28.824 -18.842 -28.680 1.00 99.78  ? 416 PRO   A O   1 
ATOM   2892 C  CB  . PRO   A 1 396 ? -26.324 -16.854 -28.651 1.00 87.51  ? 416 PRO   A CB  1 
ATOM   2893 C  CG  . PRO   A 1 396 ? -24.898 -16.576 -28.963 1.00 91.05  ? 416 PRO   A CG  1 
ATOM   2894 C  CD  . PRO   A 1 396 ? -24.605 -17.322 -30.238 1.00 89.39  ? 416 PRO   A CD  1 
ATOM   2895 N  N   . GLU   A 1 397 ? -28.275 -18.396 -30.818 1.00 96.97  ? 417 GLU   A N   1 
ATOM   2896 C  CA  . GLU   A 1 397 ? -29.652 -18.506 -31.282 1.00 107.24 ? 417 GLU   A CA  1 
ATOM   2897 C  C   . GLU   A 1 397 ? -30.209 -19.922 -31.189 1.00 106.28 ? 417 GLU   A C   1 
ATOM   2898 O  O   . GLU   A 1 397 ? -31.408 -20.107 -31.427 1.00 109.08 ? 417 GLU   A O   1 
ATOM   2899 C  CB  . GLU   A 1 397 ? -29.765 -17.995 -32.720 1.00 114.57 ? 417 GLU   A CB  1 
ATOM   2900 C  CG  . GLU   A 1 397 ? -29.589 -16.488 -32.857 1.00 117.99 ? 417 GLU   A CG  1 
ATOM   2901 C  CD  . GLU   A 1 397 ? -30.685 -15.701 -32.158 1.00 129.81 ? 417 GLU   A CD  1 
ATOM   2902 O  OE1 . GLU   A 1 397 ? -31.838 -16.181 -32.117 1.00 130.48 ? 417 GLU   A OE1 1 
ATOM   2903 O  OE2 . GLU   A 1 397 ? -30.390 -14.599 -31.648 1.00 135.89 ? 417 GLU   A OE2 1 
ATOM   2904 N  N   . ARG   A 1 398 ? -29.382 -20.923 -30.865 1.00 102.84 ? 418 ARG   A N   1 
ATOM   2905 C  CA  . ARG   A 1 398 ? -29.925 -22.243 -30.559 1.00 86.24  ? 418 ARG   A CA  1 
ATOM   2906 C  C   . ARG   A 1 398 ? -30.860 -22.187 -29.363 1.00 95.31  ? 418 ARG   A C   1 
ATOM   2907 O  O   . ARG   A 1 398 ? -31.821 -22.961 -29.286 1.00 90.51  ? 418 ARG   A O   1 
ATOM   2908 C  CB  . ARG   A 1 398 ? -28.808 -23.244 -30.266 1.00 102.90 ? 418 ARG   A CB  1 
ATOM   2909 C  CG  . ARG   A 1 398 ? -27.633 -23.215 -31.209 1.00 106.08 ? 418 ARG   A CG  1 
ATOM   2910 C  CD  . ARG   A 1 398 ? -26.491 -24.028 -30.620 1.00 102.30 ? 418 ARG   A CD  1 
ATOM   2911 N  NE  . ARG   A 1 398 ? -25.244 -23.860 -31.354 1.00 106.54 ? 418 ARG   A NE  1 
ATOM   2912 C  CZ  . ARG   A 1 398 ? -24.922 -24.543 -32.443 1.00 108.78 ? 418 ARG   A CZ  1 
ATOM   2913 N  NH1 . ARG   A 1 398 ? -25.753 -25.424 -32.975 1.00 110.40 ? 418 ARG   A NH1 1 
ATOM   2914 N  NH2 . ARG   A 1 398 ? -23.740 -24.335 -33.014 1.00 115.37 ? 418 ARG   A NH2 1 
ATOM   2915 N  N   . PHE   A 1 399 ? -30.587 -21.289 -28.417 1.00 92.70  ? 419 PHE   A N   1 
ATOM   2916 C  CA  . PHE   A 1 399 ? -31.380 -21.144 -27.207 1.00 92.57  ? 419 PHE   A CA  1 
ATOM   2917 C  C   . PHE   A 1 399 ? -32.388 -20.009 -27.310 1.00 99.11  ? 419 PHE   A C   1 
ATOM   2918 O  O   . PHE   A 1 399 ? -32.865 -19.516 -26.282 1.00 102.68 ? 419 PHE   A O   1 
ATOM   2919 C  CB  . PHE   A 1 399 ? -30.465 -20.935 -26.001 1.00 87.59  ? 419 PHE   A CB  1 
ATOM   2920 C  CG  . PHE   A 1 399 ? -29.559 -22.096 -25.728 1.00 90.98  ? 419 PHE   A CG  1 
ATOM   2921 C  CD1 . PHE   A 1 399 ? -29.995 -23.166 -24.965 1.00 86.67  ? 419 PHE   A CD1 1 
ATOM   2922 C  CD2 . PHE   A 1 399 ? -28.274 -22.123 -26.241 1.00 94.48  ? 419 PHE   A CD2 1 
ATOM   2923 C  CE1 . PHE   A 1 399 ? -29.162 -24.239 -24.713 1.00 87.85  ? 419 PHE   A CE1 1 
ATOM   2924 C  CE2 . PHE   A 1 399 ? -27.438 -23.193 -25.994 1.00 90.77  ? 419 PHE   A CE2 1 
ATOM   2925 C  CZ  . PHE   A 1 399 ? -27.882 -24.253 -25.229 1.00 85.39  ? 419 PHE   A CZ  1 
ATOM   2926 N  N   . SER   A 1 400 ? -32.710 -19.574 -28.525 1.00 110.58 ? 420 SER   A N   1 
ATOM   2927 C  CA  . SER   A 1 400 ? -33.793 -18.620 -28.694 1.00 119.20 ? 420 SER   A CA  1 
ATOM   2928 C  C   . SER   A 1 400 ? -35.097 -19.238 -28.208 1.00 130.02 ? 420 SER   A C   1 
ATOM   2929 O  O   . SER   A 1 400 ? -35.290 -20.456 -28.263 1.00 126.92 ? 420 SER   A O   1 
ATOM   2930 C  CB  . SER   A 1 400 ? -33.921 -18.201 -30.160 1.00 122.65 ? 420 SER   A CB  1 
ATOM   2931 O  OG  . SER   A 1 400 ? -34.393 -19.270 -30.962 1.00 133.41 ? 420 SER   A OG  1 
ATOM   2932 N  N   . LYS   A 1 401 ? -35.998 -18.379 -27.721 1.00 140.19 ? 421 LYS   A N   1 
ATOM   2933 C  CA  . LYS   A 1 401 ? -37.300 -18.821 -27.232 1.00 141.85 ? 421 LYS   A CA  1 
ATOM   2934 C  C   . LYS   A 1 401 ? -38.025 -19.695 -28.246 1.00 147.68 ? 421 LYS   A C   1 
ATOM   2935 O  O   . LYS   A 1 401 ? -38.877 -20.505 -27.863 1.00 150.56 ? 421 LYS   A O   1 
ATOM   2936 C  CB  . LYS   A 1 401 ? -38.145 -17.600 -26.872 1.00 146.54 ? 421 LYS   A CB  1 
ATOM   2937 C  CG  . LYS   A 1 401 ? -39.271 -17.858 -25.887 1.00 154.43 ? 421 LYS   A CG  1 
ATOM   2938 C  CD  . LYS   A 1 401 ? -39.783 -16.539 -25.334 1.00 161.80 ? 421 LYS   A CD  1 
ATOM   2939 C  CE  . LYS   A 1 401 ? -39.996 -15.527 -26.450 1.00 162.46 ? 421 LYS   A CE  1 
ATOM   2940 N  NZ  . LYS   A 1 401 ? -40.122 -14.135 -25.936 1.00 166.20 ? 421 LYS   A NZ  1 
ATOM   2941 N  N   . LYS   A 1 402 ? -37.695 -19.550 -29.530 1.00 154.49 ? 422 LYS   A N   1 
ATOM   2942 C  CA  . LYS   A 1 402 ? -38.241 -20.435 -30.551 1.00 152.66 ? 422 LYS   A CA  1 
ATOM   2943 C  C   . LYS   A 1 402 ? -37.556 -21.796 -30.522 1.00 155.26 ? 422 LYS   A C   1 
ATOM   2944 O  O   . LYS   A 1 402 ? -38.223 -22.838 -30.508 1.00 158.50 ? 422 LYS   A O   1 
ATOM   2945 C  CB  . LYS   A 1 402 ? -38.095 -19.784 -31.928 1.00 151.14 ? 422 LYS   A CB  1 
ATOM   2946 C  CG  . LYS   A 1 402 ? -38.118 -20.763 -33.092 1.00 158.94 ? 422 LYS   A CG  1 
ATOM   2947 C  CD  . LYS   A 1 402 ? -37.512 -20.135 -34.340 1.00 161.86 ? 422 LYS   A CD  1 
ATOM   2948 C  CE  . LYS   A 1 402 ? -37.442 -21.131 -35.485 1.00 165.91 ? 422 LYS   A CE  1 
ATOM   2949 N  NZ  . LYS   A 1 402 ? -36.725 -20.576 -36.666 1.00 168.81 ? 422 LYS   A NZ  1 
ATOM   2950 N  N   . ASN   A 1 403 ? -36.222 -21.810 -30.508 1.00 146.95 ? 423 ASN   A N   1 
ATOM   2951 C  CA  . ASN   A 1 403 ? -35.470 -23.051 -30.644 1.00 134.16 ? 423 ASN   A CA  1 
ATOM   2952 C  C   . ASN   A 1 403 ? -35.163 -23.734 -29.318 1.00 132.61 ? 423 ASN   A C   1 
ATOM   2953 O  O   . ASN   A 1 403 ? -34.767 -24.906 -29.323 1.00 130.86 ? 423 ASN   A O   1 
ATOM   2954 C  CB  . ASN   A 1 403 ? -34.155 -22.795 -31.385 1.00 121.77 ? 423 ASN   A CB  1 
ATOM   2955 C  CG  . ASN   A 1 403 ? -34.370 -22.298 -32.796 1.00 144.16 ? 423 ASN   A CG  1 
ATOM   2956 O  OD1 . ASN   A 1 403 ? -35.354 -22.646 -33.448 1.00 140.69 ? 423 ASN   A OD1 1 
ATOM   2957 N  ND2 . ASN   A 1 403 ? -33.446 -21.477 -33.279 1.00 134.21 ? 423 ASN   A ND2 1 
ATOM   2958 N  N   . LYS   A 1 404 ? -35.331 -23.039 -28.190 1.00 129.59 ? 424 LYS   A N   1 
ATOM   2959 C  CA  . LYS   A 1 404 ? -35.114 -23.651 -26.883 1.00 131.68 ? 424 LYS   A CA  1 
ATOM   2960 C  C   . LYS   A 1 404 ? -36.032 -24.839 -26.638 1.00 134.39 ? 424 LYS   A C   1 
ATOM   2961 O  O   . LYS   A 1 404 ? -35.768 -25.632 -25.728 1.00 128.55 ? 424 LYS   A O   1 
ATOM   2962 C  CB  . LYS   A 1 404 ? -35.315 -22.621 -25.771 1.00 133.53 ? 424 LYS   A CB  1 
ATOM   2963 C  CG  . LYS   A 1 404 ? -36.743 -22.110 -25.670 1.00 134.73 ? 424 LYS   A CG  1 
ATOM   2964 C  CD  . LYS   A 1 404 ? -37.099 -21.690 -24.253 1.00 139.88 ? 424 LYS   A CD  1 
ATOM   2965 C  CE  . LYS   A 1 404 ? -36.344 -20.445 -23.826 1.00 142.10 ? 424 LYS   A CE  1 
ATOM   2966 N  NZ  . LYS   A 1 404 ? -36.851 -19.931 -22.522 1.00 145.18 ? 424 LYS   A NZ  1 
ATOM   2967 N  N   . ASP   A 1 405 ? -37.099 -24.977 -27.426 1.00 134.25 ? 425 ASP   A N   1 
ATOM   2968 C  CA  . ASP   A 1 405 ? -38.038 -26.075 -27.263 1.00 138.54 ? 425 ASP   A CA  1 
ATOM   2969 C  C   . ASP   A 1 405 ? -37.542 -27.370 -27.892 1.00 134.23 ? 425 ASP   A C   1 
ATOM   2970 O  O   . ASP   A 1 405 ? -37.983 -28.449 -27.481 1.00 121.58 ? 425 ASP   A O   1 
ATOM   2971 C  CB  . ASP   A 1 405 ? -39.390 -25.696 -27.873 1.00 143.76 ? 425 ASP   A CB  1 
ATOM   2972 C  CG  . ASP   A 1 405 ? -39.782 -24.259 -27.575 1.00 151.64 ? 425 ASP   A CG  1 
ATOM   2973 O  OD1 . ASP   A 1 405 ? -39.386 -23.741 -26.511 1.00 158.22 ? 425 ASP   A OD1 1 
ATOM   2974 O  OD2 . ASP   A 1 405 ? -40.484 -23.647 -28.409 1.00 150.82 ? 425 ASP   A OD2 1 
ATOM   2975 N  N   . ASN   A 1 406 ? -36.640 -27.293 -28.871 1.00 144.28 ? 426 ASN   A N   1 
ATOM   2976 C  CA  . ASN   A 1 406 ? -36.175 -28.484 -29.569 1.00 139.72 ? 426 ASN   A CA  1 
ATOM   2977 C  C   . ASN   A 1 406 ? -35.025 -29.183 -28.858 1.00 138.41 ? 426 ASN   A C   1 
ATOM   2978 O  O   . ASN   A 1 406 ? -34.655 -30.293 -29.257 1.00 143.01 ? 426 ASN   A O   1 
ATOM   2979 C  CB  . ASN   A 1 406 ? -35.738 -28.125 -30.992 1.00 140.15 ? 426 ASN   A CB  1 
ATOM   2980 C  CG  . ASN   A 1 406 ? -36.539 -26.981 -31.581 1.00 153.15 ? 426 ASN   A CG  1 
ATOM   2981 O  OD1 . ASN   A 1 406 ? -35.973 -26.009 -32.082 1.00 155.89 ? 426 ASN   A OD1 1 
ATOM   2982 N  ND2 . ASN   A 1 406 ? -37.863 -27.089 -31.526 1.00 156.79 ? 426 ASN   A ND2 1 
ATOM   2983 N  N   . ILE   A 1 407 ? -34.454 -28.570 -27.829 1.00 123.68 ? 427 ILE   A N   1 
ATOM   2984 C  CA  . ILE   A 1 407 ? -33.275 -29.116 -27.170 1.00 112.93 ? 427 ILE   A CA  1 
ATOM   2985 C  C   . ILE   A 1 407 ? -33.707 -30.132 -26.121 1.00 112.60 ? 427 ILE   A C   1 
ATOM   2986 O  O   . ILE   A 1 407 ? -34.590 -29.860 -25.299 1.00 111.17 ? 427 ILE   A O   1 
ATOM   2987 C  CB  . ILE   A 1 407 ? -32.433 -27.991 -26.549 1.00 113.62 ? 427 ILE   A CB  1 
ATOM   2988 C  CG1 . ILE   A 1 407 ? -31.842 -27.112 -27.654 1.00 105.20 ? 427 ILE   A CG1 1 
ATOM   2989 C  CG2 . ILE   A 1 407 ? -31.335 -28.567 -25.670 1.00 96.97  ? 427 ILE   A CG2 1 
ATOM   2990 C  CD1 . ILE   A 1 407 ? -31.074 -25.917 -27.147 1.00 101.43 ? 427 ILE   A CD1 1 
ATOM   2991 N  N   . ASP   A 1 408 ? -33.083 -31.305 -26.149 1.00 108.91 ? 428 ASP   A N   1 
ATOM   2992 C  CA  . ASP   A 1 408 ? -33.411 -32.368 -25.210 1.00 90.66  ? 428 ASP   A CA  1 
ATOM   2993 C  C   . ASP   A 1 408 ? -32.673 -32.130 -23.899 1.00 97.75  ? 428 ASP   A C   1 
ATOM   2994 O  O   . ASP   A 1 408 ? -31.440 -32.036 -23.905 1.00 90.53  ? 428 ASP   A O   1 
ATOM   2995 C  CB  . ASP   A 1 408 ? -33.031 -33.725 -25.799 1.00 87.37  ? 428 ASP   A CB  1 
ATOM   2996 C  CG  . ASP   A 1 408 ? -33.639 -34.892 -25.042 1.00 93.90  ? 428 ASP   A CG  1 
ATOM   2997 O  OD1 . ASP   A 1 408 ? -33.548 -34.921 -23.797 1.00 92.41  ? 428 ASP   A OD1 1 
ATOM   2998 O  OD2 . ASP   A 1 408 ? -34.208 -35.789 -25.698 1.00 94.75  ? 428 ASP   A OD2 1 
ATOM   2999 N  N   . PRO   A 1 409 ? -33.372 -32.027 -22.763 1.00 100.00 ? 429 PRO   A N   1 
ATOM   3000 C  CA  . PRO   A 1 409 ? -32.686 -31.773 -21.487 1.00 87.67  ? 429 PRO   A CA  1 
ATOM   3001 C  C   . PRO   A 1 409 ? -31.848 -32.940 -20.996 1.00 85.05  ? 429 PRO   A C   1 
ATOM   3002 O  O   . PRO   A 1 409 ? -31.218 -32.823 -19.938 1.00 88.76  ? 429 PRO   A O   1 
ATOM   3003 C  CB  . PRO   A 1 409 ? -33.845 -31.486 -20.523 1.00 90.02  ? 429 PRO   A CB  1 
ATOM   3004 C  CG  . PRO   A 1 409 ? -34.986 -32.257 -21.088 1.00 94.12  ? 429 PRO   A CG  1 
ATOM   3005 C  CD  . PRO   A 1 409 ? -34.827 -32.179 -22.587 1.00 87.15  ? 429 PRO   A CD  1 
ATOM   3006 N  N   . TYR   A 1 410 ? -31.833 -34.060 -21.713 1.00 76.25  ? 430 TYR   A N   1 
ATOM   3007 C  CA  . TYR   A 1 410 ? -30.942 -35.169 -21.416 1.00 87.34  ? 430 TYR   A CA  1 
ATOM   3008 C  C   . TYR   A 1 410 ? -29.808 -35.278 -22.423 1.00 85.40  ? 430 TYR   A C   1 
ATOM   3009 O  O   . TYR   A 1 410 ? -28.985 -36.193 -22.321 1.00 84.96  ? 430 TYR   A O   1 
ATOM   3010 C  CB  . TYR   A 1 410 ? -31.740 -36.474 -21.343 1.00 92.99  ? 430 TYR   A CB  1 
ATOM   3011 C  CG  . TYR   A 1 410 ? -32.842 -36.385 -20.314 1.00 87.72  ? 430 TYR   A CG  1 
ATOM   3012 C  CD1 . TYR   A 1 410 ? -32.541 -36.210 -18.969 1.00 83.36  ? 430 TYR   A CD1 1 
ATOM   3013 C  CD2 . TYR   A 1 410 ? -34.178 -36.444 -20.685 1.00 86.98  ? 430 TYR   A CD2 1 
ATOM   3014 C  CE1 . TYR   A 1 410 ? -33.538 -36.111 -18.020 1.00 98.91  ? 430 TYR   A CE1 1 
ATOM   3015 C  CE2 . TYR   A 1 410 ? -35.183 -36.346 -19.742 1.00 86.58  ? 430 TYR   A CE2 1 
ATOM   3016 C  CZ  . TYR   A 1 410 ? -34.858 -36.180 -18.412 1.00 91.63  ? 430 TYR   A CZ  1 
ATOM   3017 O  OH  . TYR   A 1 410 ? -35.859 -36.084 -17.473 1.00 100.11 ? 430 TYR   A OH  1 
ATOM   3018 N  N   . ILE   A 1 411 ? -29.748 -34.367 -23.390 1.00 87.89  ? 431 ILE   A N   1 
ATOM   3019 C  CA  . ILE   A 1 411 ? -28.564 -34.170 -24.212 1.00 86.50  ? 431 ILE   A CA  1 
ATOM   3020 C  C   . ILE   A 1 411 ? -27.777 -32.948 -23.757 1.00 83.33  ? 431 ILE   A C   1 
ATOM   3021 O  O   . ILE   A 1 411 ? -26.547 -32.984 -23.703 1.00 82.76  ? 431 ILE   A O   1 
ATOM   3022 C  CB  . ILE   A 1 411 ? -28.961 -34.060 -25.700 1.00 91.13  ? 431 ILE   A CB  1 
ATOM   3023 C  CG1 . ILE   A 1 411 ? -29.702 -35.321 -26.148 1.00 96.25  ? 431 ILE   A CG1 1 
ATOM   3024 C  CG2 . ILE   A 1 411 ? -27.734 -33.813 -26.566 1.00 81.29  ? 431 ILE   A CG2 1 
ATOM   3025 C  CD1 . ILE   A 1 411 ? -28.980 -36.609 -25.806 1.00 99.36  ? 431 ILE   A CD1 1 
ATOM   3026 N  N   . TYR   A 1 412 ? -28.483 -31.872 -23.408 1.00 82.37  ? 432 TYR   A N   1 
ATOM   3027 C  CA  . TYR   A 1 412 ? -27.883 -30.663 -22.851 1.00 76.96  ? 432 TYR   A CA  1 
ATOM   3028 C  C   . TYR   A 1 412 ? -28.031 -30.710 -21.331 1.00 76.98  ? 432 TYR   A C   1 
ATOM   3029 O  O   . TYR   A 1 412 ? -29.143 -30.598 -20.801 1.00 77.58  ? 432 TYR   A O   1 
ATOM   3030 C  CB  . TYR   A 1 412 ? -28.535 -29.413 -23.440 1.00 75.60  ? 432 TYR   A CB  1 
ATOM   3031 C  CG  . TYR   A 1 412 ? -27.911 -28.126 -22.962 1.00 74.66  ? 432 TYR   A CG  1 
ATOM   3032 C  CD1 . TYR   A 1 412 ? -26.604 -27.806 -23.295 1.00 74.42  ? 432 TYR   A CD1 1 
ATOM   3033 C  CD2 . TYR   A 1 412 ? -28.628 -27.230 -22.178 1.00 72.27  ? 432 TYR   A CD2 1 
ATOM   3034 C  CE1 . TYR   A 1 412 ? -26.024 -26.639 -22.861 1.00 73.28  ? 432 TYR   A CE1 1 
ATOM   3035 C  CE2 . TYR   A 1 412 ? -28.054 -26.052 -21.739 1.00 66.83  ? 432 TYR   A CE2 1 
ATOM   3036 C  CZ  . TYR   A 1 412 ? -26.750 -25.764 -22.084 1.00 72.51  ? 432 TYR   A CZ  1 
ATOM   3037 O  OH  . TYR   A 1 412 ? -26.163 -24.601 -21.655 1.00 73.10  ? 432 TYR   A OH  1 
ATOM   3038 N  N   . THR   A 1 413 ? -26.911 -30.883 -20.636 1.00 80.96  ? 433 THR   A N   1 
ATOM   3039 C  CA  . THR   A 1 413 ? -26.899 -31.045 -19.182 1.00 80.32  ? 433 THR   A CA  1 
ATOM   3040 C  C   . THR   A 1 413 ? -25.684 -30.344 -18.589 1.00 79.66  ? 433 THR   A C   1 
ATOM   3041 O  O   . THR   A 1 413 ? -24.775 -30.995 -18.059 1.00 80.42  ? 433 THR   A O   1 
ATOM   3042 C  CB  . THR   A 1 413 ? -26.889 -32.530 -18.802 1.00 86.74  ? 433 THR   A CB  1 
ATOM   3043 O  OG1 . THR   A 1 413 ? -25.834 -33.199 -19.507 1.00 81.58  ? 433 THR   A OG1 1 
ATOM   3044 C  CG2 . THR   A 1 413 ? -28.214 -33.190 -19.119 1.00 80.83  ? 433 THR   A CG2 1 
ATOM   3045 N  N   . PRO   A 1 414 ? -25.634 -29.007 -18.654 1.00 81.69  ? 434 PRO   A N   1 
ATOM   3046 C  CA  . PRO   A 1 414 ? -24.513 -28.296 -18.016 1.00 77.49  ? 434 PRO   A CA  1 
ATOM   3047 C  C   . PRO   A 1 414 ? -24.496 -28.438 -16.501 1.00 72.06  ? 434 PRO   A C   1 
ATOM   3048 O  O   . PRO   A 1 414 ? -23.421 -28.355 -15.893 1.00 69.96  ? 434 PRO   A O   1 
ATOM   3049 C  CB  . PRO   A 1 414 ? -24.731 -26.835 -18.448 1.00 75.30  ? 434 PRO   A CB  1 
ATOM   3050 C  CG  . PRO   A 1 414 ? -26.199 -26.752 -18.701 1.00 69.69  ? 434 PRO   A CG  1 
ATOM   3051 C  CD  . PRO   A 1 414 ? -26.610 -28.078 -19.252 1.00 80.77  ? 434 PRO   A CD  1 
ATOM   3052 N  N   . PHE   A 1 415 ? -25.650 -28.683 -15.874 1.00 76.22  ? 435 PHE   A N   1 
ATOM   3053 C  CA  . PHE   A 1 415 ? -25.745 -28.813 -14.422 1.00 76.41  ? 435 PHE   A CA  1 
ATOM   3054 C  C   . PHE   A 1 415 ? -26.222 -30.196 -13.992 1.00 63.22  ? 435 PHE   A C   1 
ATOM   3055 O  O   . PHE   A 1 415 ? -26.703 -30.357 -12.866 1.00 70.23  ? 435 PHE   A O   1 
ATOM   3056 C  CB  . PHE   A 1 415 ? -26.675 -27.744 -13.844 1.00 70.48  ? 435 PHE   A CB  1 
ATOM   3057 C  CG  . PHE   A 1 415 ? -26.228 -26.343 -14.114 1.00 70.06  ? 435 PHE   A CG  1 
ATOM   3058 C  CD1 . PHE   A 1 415 ? -26.647 -25.679 -15.253 1.00 70.93  ? 435 PHE   A CD1 1 
ATOM   3059 C  CD2 . PHE   A 1 415 ? -25.386 -25.688 -13.232 1.00 73.25  ? 435 PHE   A CD2 1 
ATOM   3060 C  CE1 . PHE   A 1 415 ? -26.236 -24.389 -15.509 1.00 73.85  ? 435 PHE   A CE1 1 
ATOM   3061 C  CE2 . PHE   A 1 415 ? -24.972 -24.398 -13.480 1.00 81.62  ? 435 PHE   A CE2 1 
ATOM   3062 C  CZ  . PHE   A 1 415 ? -25.397 -23.747 -14.620 1.00 74.59  ? 435 PHE   A CZ  1 
ATOM   3063 N  N   . GLY   A 1 416 ? -26.087 -31.200 -14.857 1.00 69.34  ? 436 GLY   A N   1 
ATOM   3064 C  CA  . GLY   A 1 416 ? -26.650 -32.508 -14.594 1.00 68.31  ? 436 GLY   A CA  1 
ATOM   3065 C  C   . GLY   A 1 416 ? -28.170 -32.452 -14.540 1.00 79.57  ? 436 GLY   A C   1 
ATOM   3066 O  O   . GLY   A 1 416 ? -28.809 -31.481 -14.944 1.00 76.07  ? 436 GLY   A O   1 
ATOM   3067 N  N   . SER   A 1 417 ? -28.747 -33.529 -14.009 1.00 78.08  ? 437 SER   A N   1 
ATOM   3068 C  CA  . SER   A 1 417 ? -30.195 -33.619 -13.907 1.00 83.74  ? 437 SER   A CA  1 
ATOM   3069 C  C   . SER   A 1 417 ? -30.561 -34.598 -12.802 1.00 84.23  ? 437 SER   A C   1 
ATOM   3070 O  O   . SER   A 1 417 ? -29.741 -35.409 -12.363 1.00 82.21  ? 437 SER   A O   1 
ATOM   3071 C  CB  . SER   A 1 417 ? -30.824 -34.048 -15.240 1.00 93.26  ? 437 SER   A CB  1 
ATOM   3072 O  OG  . SER   A 1 417 ? -32.239 -33.959 -15.199 1.00 106.36 ? 437 SER   A OG  1 
ATOM   3073 N  N   . GLY   A 1 418 ? -31.808 -34.508 -12.352 1.00 79.33  ? 438 GLY   A N   1 
ATOM   3074 C  CA  . GLY   A 1 418 ? -32.322 -35.424 -11.365 1.00 79.05  ? 438 GLY   A CA  1 
ATOM   3075 C  C   . GLY   A 1 418 ? -32.139 -34.936 -9.943  1.00 73.42  ? 438 GLY   A C   1 
ATOM   3076 O  O   . GLY   A 1 418 ? -31.773 -33.782 -9.693  1.00 67.94  ? 438 GLY   A O   1 
ATOM   3077 N  N   . PRO   A 1 419 ? -32.394 -35.825 -8.979  1.00 65.48  ? 439 PRO   A N   1 
ATOM   3078 C  CA  . PRO   A 1 419 ? -32.311 -35.429 -7.562  1.00 73.20  ? 439 PRO   A CA  1 
ATOM   3079 C  C   . PRO   A 1 419 ? -30.927 -34.991 -7.132  1.00 79.42  ? 439 PRO   A C   1 
ATOM   3080 O  O   . PRO   A 1 419 ? -30.799 -34.350 -6.080  1.00 77.87  ? 439 PRO   A O   1 
ATOM   3081 C  CB  . PRO   A 1 419 ? -32.746 -36.699 -6.816  1.00 81.40  ? 439 PRO   A CB  1 
ATOM   3082 C  CG  . PRO   A 1 419 ? -33.497 -37.506 -7.827  1.00 90.36  ? 439 PRO   A CG  1 
ATOM   3083 C  CD  . PRO   A 1 419 ? -32.847 -37.214 -9.143  1.00 81.76  ? 439 PRO   A CD  1 
ATOM   3084 N  N   . ARG   A 1 420 ? -29.915 -35.337 -7.879  1.00 73.20  ? 440 ARG   A N   1 
ATOM   3085 C  CA  . ARG   A 1 420 ? -28.546 -35.001 -7.509  1.00 73.79  ? 440 ARG   A CA  1 
ATOM   3086 C  C   . ARG   A 1 420 ? -27.885 -34.144 -8.584  1.00 70.33  ? 440 ARG   A C   1 
ATOM   3087 O  O   . ARG   A 1 420 ? -26.743 -34.380 -8.984  1.00 72.54  ? 440 ARG   A O   1 
ATOM   3088 C  CB  . ARG   A 1 420 ? -27.731 -36.265 -7.239  1.00 71.21  ? 440 ARG   A CB  1 
ATOM   3089 C  CG  . ARG   A 1 420 ? -26.501 -36.033 -6.374  1.00 73.32  ? 440 ARG   A CG  1 
ATOM   3090 C  CD  . ARG   A 1 420 ? -25.947 -37.332 -5.815  1.00 74.54  ? 440 ARG   A CD  1 
ATOM   3091 N  NE  . ARG   A 1 420 ? -24.848 -37.089 -4.889  1.00 68.54  ? 440 ARG   A NE  1 
ATOM   3092 C  CZ  . ARG   A 1 420 ? -24.296 -38.017 -4.120  1.00 69.20  ? 440 ARG   A CZ  1 
ATOM   3093 N  NH1 . ARG   A 1 420 ? -24.723 -39.269 -4.132  1.00 56.35  ? 440 ARG   A NH1 1 
ATOM   3094 N  NH2 . ARG   A 1 420 ? -23.292 -37.680 -3.315  1.00 73.27  ? 440 ARG   A NH2 1 
ATOM   3095 N  N   . ASN   A 1 421 ? -28.602 -33.133 -9.067  1.00 79.33  ? 441 ASN   A N   1 
ATOM   3096 C  CA  . ASN   A 1 421 ? -28.037 -32.185 -10.017 1.00 73.03  ? 441 ASN   A CA  1 
ATOM   3097 C  C   . ASN   A 1 421 ? -27.258 -31.118 -9.250  1.00 74.18  ? 441 ASN   A C   1 
ATOM   3098 O  O   . ASN   A 1 421 ? -27.012 -31.237 -8.046  1.00 79.25  ? 441 ASN   A O   1 
ATOM   3099 C  CB  . ASN   A 1 421 ? -29.137 -31.591 -10.895 1.00 70.93  ? 441 ASN   A CB  1 
ATOM   3100 C  CG  . ASN   A 1 421 ? -30.275 -30.988 -10.088 1.00 79.83  ? 441 ASN   A CG  1 
ATOM   3101 O  OD1 . ASN   A 1 421 ? -30.145 -30.739 -8.889  1.00 83.38  ? 441 ASN   A OD1 1 
ATOM   3102 N  ND2 . ASN   A 1 421 ? -31.401 -30.747 -10.749 1.00 100.19 ? 441 ASN   A ND2 1 
ATOM   3103 N  N   . CYS   A 1 422 ? -26.858 -30.055 -9.942  1.00 77.14  ? 442 CYS   A N   1 
ATOM   3104 C  CA  . CYS   A 1 422 ? -26.142 -28.957 -9.301  1.00 70.25  ? 442 CYS   A CA  1 
ATOM   3105 C  C   . CYS   A 1 422 ? -27.079 -28.234 -8.343  1.00 69.64  ? 442 CYS   A C   1 
ATOM   3106 O  O   . CYS   A 1 422 ? -28.032 -27.577 -8.772  1.00 73.61  ? 442 CYS   A O   1 
ATOM   3107 C  CB  . CYS   A 1 422 ? -25.588 -28.000 -10.352 1.00 65.77  ? 442 CYS   A CB  1 
ATOM   3108 S  SG  . CYS   A 1 422 ? -24.771 -26.541 -9.669  1.00 66.48  ? 442 CYS   A SG  1 
ATOM   3109 N  N   . ILE   A 1 423 ? -26.765 -28.475 -7.033  1.00 72.06  ? 443 ILE   A N   1 
ATOM   3110 C  CA  . ILE   A 1 423 ? -27.603 -27.804 -6.049  1.00 78.26  ? 443 ILE   A CA  1 
ATOM   3111 C  C   . ILE   A 1 423 ? -27.458 -26.293 -6.137  1.00 79.88  ? 443 ILE   A C   1 
ATOM   3112 O  O   . ILE   A 1 423 ? -28.360 -25.560 -5.720  1.00 80.90  ? 443 ILE   A O   1 
ATOM   3113 C  CB  . ILE   A 1 423 ? -27.267 -28.304 -4.627  1.00 67.79  ? 443 ILE   A CB  1 
ATOM   3114 C  CG1 . ILE   A 1 423 ? -28.405 -27.978 -3.658  1.00 75.14  ? 443 ILE   A CG1 1 
ATOM   3115 C  CG2 . ILE   A 1 423 ? -25.983 -27.666 -4.126  1.00 66.63  ? 443 ILE   A CG2 1 
ATOM   3116 C  CD1 . ILE   A 1 423 ? -28.113 -28.340 -2.216  1.00 82.95  ? 443 ILE   A CD1 1 
ATOM   3117 N  N   . GLY   A 1 424 ? -26.345 -25.802 -6.679  1.00 65.48  ? 444 GLY   A N   1 
ATOM   3118 C  CA  . GLY   A 1 424 ? -26.123 -24.374 -6.766  1.00 78.00  ? 444 GLY   A CA  1 
ATOM   3119 C  C   . GLY   A 1 424 ? -26.264 -23.811 -8.167  1.00 78.17  ? 444 GLY   A C   1 
ATOM   3120 O  O   . GLY   A 1 424 ? -25.623 -22.810 -8.506  1.00 80.21  ? 444 GLY   A O   1 
ATOM   3121 N  N   . MET   A 1 425 ? -27.108 -24.443 -8.985  1.00 77.22  ? 445 MET   A N   1 
ATOM   3122 C  CA  . MET   A 1 425 ? -27.301 -24.003 -10.364 1.00 76.70  ? 445 MET   A CA  1 
ATOM   3123 C  C   . MET   A 1 425 ? -27.829 -22.575 -10.422 1.00 80.89  ? 445 MET   A C   1 
ATOM   3124 O  O   . MET   A 1 425 ? -27.212 -21.694 -11.034 1.00 83.92  ? 445 MET   A O   1 
ATOM   3125 C  CB  . MET   A 1 425 ? -28.256 -24.950 -11.091 1.00 76.93  ? 445 MET   A CB  1 
ATOM   3126 C  CG  . MET   A 1 425 ? -28.772 -24.405 -12.421 1.00 81.86  ? 445 MET   A CG  1 
ATOM   3127 S  SD  . MET   A 1 425 ? -29.790 -25.589 -13.322 1.00 90.48  ? 445 MET   A SD  1 
ATOM   3128 C  CE  . MET   A 1 425 ? -31.050 -25.950 -12.100 1.00 95.59  ? 445 MET   A CE  1 
ATOM   3129 N  N   . ARG   A 1 426 ? -28.982 -22.331 -9.792  1.00 87.11  ? 446 ARG   A N   1 
ATOM   3130 C  CA  . ARG   A 1 426 ? -29.615 -21.017 -9.869  1.00 90.53  ? 446 ARG   A CA  1 
ATOM   3131 C  C   . ARG   A 1 426 ? -28.699 -19.930 -9.321  1.00 89.92  ? 446 ARG   A C   1 
ATOM   3132 O  O   . ARG   A 1 426 ? -28.647 -18.819 -9.863  1.00 91.07  ? 446 ARG   A O   1 
ATOM   3133 C  CB  . ARG   A 1 426 ? -30.944 -21.034 -9.113  1.00 96.05  ? 446 ARG   A CB  1 
ATOM   3134 C  CG  . ARG   A 1 426 ? -31.529 -22.426 -8.930  1.00 118.54 ? 446 ARG   A CG  1 
ATOM   3135 C  CD  . ARG   A 1 426 ? -32.914 -22.386 -8.299  1.00 121.06 ? 446 ARG   A CD  1 
ATOM   3136 N  NE  . ARG   A 1 426 ? -33.962 -22.141 -9.283  1.00 128.33 ? 446 ARG   A NE  1 
ATOM   3137 C  CZ  . ARG   A 1 426 ? -34.519 -20.959 -9.510  1.00 140.39 ? 446 ARG   A CZ  1 
ATOM   3138 N  NH1 . ARG   A 1 426 ? -34.158 -19.882 -8.833  1.00 141.17 ? 446 ARG   A NH1 1 
ATOM   3139 N  NH2 . ARG   A 1 426 ? -35.466 -20.857 -10.440 1.00 137.60 ? 446 ARG   A NH2 1 
ATOM   3140 N  N   . PHE   A 1 427 ? -27.962 -20.235 -8.251  1.00 95.82  ? 447 PHE   A N   1 
ATOM   3141 C  CA  . PHE   A 1 427 ? -27.039 -19.260 -7.679  1.00 91.09  ? 447 PHE   A CA  1 
ATOM   3142 C  C   . PHE   A 1 427 ? -25.908 -18.943 -8.650  1.00 89.66  ? 447 PHE   A C   1 
ATOM   3143 O  O   . PHE   A 1 427 ? -25.556 -17.775 -8.852  1.00 93.06  ? 447 PHE   A O   1 
ATOM   3144 C  CB  . PHE   A 1 427 ? -26.487 -19.782 -6.351  1.00 91.58  ? 447 PHE   A CB  1 
ATOM   3145 C  CG  . PHE   A 1 427 ? -25.455 -18.883 -5.722  1.00 94.06  ? 447 PHE   A CG  1 
ATOM   3146 C  CD1 . PHE   A 1 427 ? -25.831 -17.707 -5.095  1.00 99.12  ? 447 PHE   A CD1 1 
ATOM   3147 C  CD2 . PHE   A 1 427 ? -24.112 -19.223 -5.744  1.00 85.20  ? 447 PHE   A CD2 1 
ATOM   3148 C  CE1 . PHE   A 1 427 ? -24.888 -16.881 -4.512  1.00 109.85 ? 447 PHE   A CE1 1 
ATOM   3149 C  CE2 . PHE   A 1 427 ? -23.163 -18.401 -5.161  1.00 88.78  ? 447 PHE   A CE2 1 
ATOM   3150 C  CZ  . PHE   A 1 427 ? -23.553 -17.228 -4.544  1.00 101.53 ? 447 PHE   A CZ  1 
ATOM   3151 N  N   . ALA   A 1 428 ? -25.334 -19.977 -9.270  1.00 86.81  ? 448 ALA   A N   1 
ATOM   3152 C  CA  . ALA   A 1 428 ? -24.211 -19.776 -10.182 1.00 88.18  ? 448 ALA   A CA  1 
ATOM   3153 C  C   . ALA   A 1 428 ? -24.620 -18.935 -11.386 1.00 90.88  ? 448 ALA   A C   1 
ATOM   3154 O  O   . ALA   A 1 428 ? -23.897 -18.017 -11.791 1.00 91.38  ? 448 ALA   A O   1 
ATOM   3155 C  CB  . ALA   A 1 428 ? -23.656 -21.127 -10.632 1.00 74.71  ? 448 ALA   A CB  1 
ATOM   3156 N  N   . LEU   A 1 429 ? -25.778 -19.241 -11.975 1.00 87.82  ? 449 LEU   A N   1 
ATOM   3157 C  CA  . LEU   A 1 429 ? -26.265 -18.464 -13.111 1.00 84.96  ? 449 LEU   A CA  1 
ATOM   3158 C  C   . LEU   A 1 429 ? -26.498 -17.011 -12.718 1.00 90.24  ? 449 LEU   A C   1 
ATOM   3159 O  O   . LEU   A 1 429 ? -26.070 -16.088 -13.421 1.00 91.48  ? 449 LEU   A O   1 
ATOM   3160 C  CB  . LEU   A 1 429 ? -27.549 -19.089 -13.655 1.00 83.30  ? 449 LEU   A CB  1 
ATOM   3161 C  CG  . LEU   A 1 429 ? -27.439 -20.522 -14.175 1.00 93.10  ? 449 LEU   A CG  1 
ATOM   3162 C  CD1 . LEU   A 1 429 ? -28.819 -21.120 -14.387 1.00 82.50  ? 449 LEU   A CD1 1 
ATOM   3163 C  CD2 . LEU   A 1 429 ? -26.638 -20.552 -15.465 1.00 87.81  ? 449 LEU   A CD2 1 
ATOM   3164 N  N   . MET   A 1 430 ? -27.181 -16.791 -11.592 1.00 94.30  ? 450 MET   A N   1 
ATOM   3165 C  CA  . MET   A 1 430 ? -27.394 -15.435 -11.095 1.00 94.68  ? 450 MET   A CA  1 
ATOM   3166 C  C   . MET   A 1 430 ? -26.067 -14.731 -10.842 1.00 98.58  ? 450 MET   A C   1 
ATOM   3167 O  O   . MET   A 1 430 ? -25.892 -13.561 -11.200 1.00 100.07 ? 450 MET   A O   1 
ATOM   3168 C  CB  . MET   A 1 430 ? -28.232 -15.477 -9.816  1.00 95.60  ? 450 MET   A CB  1 
ATOM   3169 C  CG  . MET   A 1 430 ? -28.454 -14.121 -9.168  1.00 106.87 ? 450 MET   A CG  1 
ATOM   3170 S  SD  . MET   A 1 430 ? -29.419 -13.017 -10.213 1.00 115.31 ? 450 MET   A SD  1 
ATOM   3171 C  CE  . MET   A 1 430 ? -30.848 -14.044 -10.546 1.00 108.04 ? 450 MET   A CE  1 
ATOM   3172 N  N   . ASN   A 1 431 ? -25.118 -15.438 -10.224 1.00 99.65  ? 451 ASN   A N   1 
ATOM   3173 C  CA  . ASN   A 1 431 ? -23.811 -14.857 -9.935  1.00 100.56 ? 451 ASN   A CA  1 
ATOM   3174 C  C   . ASN   A 1 431 ? -23.114 -14.409 -11.214 1.00 99.18  ? 451 ASN   A C   1 
ATOM   3175 O  O   . ASN   A 1 431 ? -22.623 -13.277 -11.306 1.00 94.49  ? 451 ASN   A O   1 
ATOM   3176 C  CB  . ASN   A 1 431 ? -22.954 -15.875 -9.179  1.00 96.28  ? 451 ASN   A CB  1 
ATOM   3177 C  CG  . ASN   A 1 431 ? -21.632 -15.300 -8.718  1.00 105.38 ? 451 ASN   A CG  1 
ATOM   3178 O  OD1 . ASN   A 1 431 ? -21.527 -14.111 -8.419  1.00 109.17 ? 451 ASN   A OD1 1 
ATOM   3179 N  ND2 . ASN   A 1 431 ? -20.610 -16.146 -8.656  1.00 99.58  ? 451 ASN   A ND2 1 
ATOM   3180 N  N   . MET   A 1 432 ? -23.074 -15.283 -12.222 1.00 93.39  ? 452 MET   A N   1 
ATOM   3181 C  CA  . MET   A 1 432 ? -22.365 -14.958 -13.456 1.00 96.18  ? 452 MET   A CA  1 
ATOM   3182 C  C   . MET   A 1 432 ? -23.081 -13.869 -14.243 1.00 95.18  ? 452 MET   A C   1 
ATOM   3183 O  O   . MET   A 1 432 ? -22.436 -12.967 -14.791 1.00 93.49  ? 452 MET   A O   1 
ATOM   3184 C  CB  . MET   A 1 432 ? -22.197 -16.214 -14.309 1.00 89.79  ? 452 MET   A CB  1 
ATOM   3185 C  CG  . MET   A 1 432 ? -21.329 -17.279 -13.666 1.00 90.08  ? 452 MET   A CG  1 
ATOM   3186 S  SD  . MET   A 1 432 ? -21.033 -18.685 -14.753 1.00 96.54  ? 452 MET   A SD  1 
ATOM   3187 C  CE  . MET   A 1 432 ? -22.694 -19.323 -14.956 1.00 89.82  ? 452 MET   A CE  1 
ATOM   3188 N  N   . LYS   A 1 433 ? -24.413 -13.937 -14.317 1.00 98.45  ? 453 LYS   A N   1 
ATOM   3189 C  CA  . LYS   A 1 433 ? -25.160 -12.935 -15.069 1.00 97.90  ? 453 LYS   A CA  1 
ATOM   3190 C  C   . LYS   A 1 433 ? -25.010 -11.551 -14.450 1.00 101.63 ? 453 LYS   A C   1 
ATOM   3191 O  O   . LYS   A 1 433 ? -24.882 -10.554 -15.168 1.00 107.72 ? 453 LYS   A O   1 
ATOM   3192 C  CB  . LYS   A 1 433 ? -26.632 -13.336 -15.158 1.00 91.51  ? 453 LYS   A CB  1 
ATOM   3193 C  CG  . LYS   A 1 433 ? -26.891 -14.513 -16.084 1.00 89.73  ? 453 LYS   A CG  1 
ATOM   3194 C  CD  . LYS   A 1 433 ? -28.365 -14.876 -16.127 1.00 88.82  ? 453 LYS   A CD  1 
ATOM   3195 C  CE  . LYS   A 1 433 ? -28.610 -16.024 -17.091 1.00 87.83  ? 453 LYS   A CE  1 
ATOM   3196 N  NZ  . LYS   A 1 433 ? -30.041 -16.430 -17.134 1.00 95.14  ? 453 LYS   A NZ  1 
ATOM   3197 N  N   . LEU   A 1 434 ? -25.011 -11.471 -13.117 1.00 100.31 ? 454 LEU   A N   1 
ATOM   3198 C  CA  . LEU   A 1 434 ? -24.776 -10.191 -12.456 1.00 103.27 ? 454 LEU   A CA  1 
ATOM   3199 C  C   . LEU   A 1 434 ? -23.379 -9.657  -12.745 1.00 103.23 ? 454 LEU   A C   1 
ATOM   3200 O  O   . LEU   A 1 434 ? -23.180 -8.438  -12.800 1.00 109.50 ? 454 LEU   A O   1 
ATOM   3201 C  CB  . LEU   A 1 434 ? -24.994 -10.332 -10.950 1.00 105.06 ? 454 LEU   A CB  1 
ATOM   3202 C  CG  . LEU   A 1 434 ? -26.460 -10.385 -10.520 1.00 108.81 ? 454 LEU   A CG  1 
ATOM   3203 C  CD1 . LEU   A 1 434 ? -26.581 -10.875 -9.091  1.00 121.07 ? 454 LEU   A CD1 1 
ATOM   3204 C  CD2 . LEU   A 1 434 ? -27.095 -9.013  -10.674 1.00 108.22 ? 454 LEU   A CD2 1 
ATOM   3205 N  N   . ALA   A 1 435 ? -22.403 -10.547 -12.931 1.00 101.79 ? 455 ALA   A N   1 
ATOM   3206 C  CA  . ALA   A 1 435 ? -21.059 -10.103 -13.281 1.00 106.98 ? 455 ALA   A CA  1 
ATOM   3207 C  C   . ALA   A 1 435 ? -21.017 -9.565  -14.706 1.00 104.05 ? 455 ALA   A C   1 
ATOM   3208 O  O   . ALA   A 1 435 ? -20.458 -8.491  -14.957 1.00 111.56 ? 455 ALA   A O   1 
ATOM   3209 C  CB  . ALA   A 1 435 ? -20.064 -11.249 -13.107 1.00 102.21 ? 455 ALA   A CB  1 
ATOM   3210 N  N   . LEU   A 1 436 ? -21.607 -10.299 -15.652 1.00 100.93 ? 456 LEU   A N   1 
ATOM   3211 C  CA  . LEU   A 1 436 ? -21.561 -9.889  -17.053 1.00 105.66 ? 456 LEU   A CA  1 
ATOM   3212 C  C   . LEU   A 1 436 ? -22.276 -8.564  -17.275 1.00 112.49 ? 456 LEU   A C   1 
ATOM   3213 O  O   . LEU   A 1 436 ? -21.824 -7.733  -18.071 1.00 116.03 ? 456 LEU   A O   1 
ATOM   3214 C  CB  . LEU   A 1 436 ? -22.179 -10.970 -17.937 1.00 100.54 ? 456 LEU   A CB  1 
ATOM   3215 C  CG  . LEU   A 1 436 ? -21.302 -12.181 -18.230 1.00 101.84 ? 456 LEU   A CG  1 
ATOM   3216 C  CD1 . LEU   A 1 436 ? -22.019 -13.149 -19.154 1.00 105.82 ? 456 LEU   A CD1 1 
ATOM   3217 C  CD2 . LEU   A 1 436 ? -20.000 -11.720 -18.841 1.00 95.25  ? 456 LEU   A CD2 1 
ATOM   3218 N  N   . ILE   A 1 437 ? -23.398 -8.353  -16.585 1.00 112.13 ? 457 ILE   A N   1 
ATOM   3219 C  CA  . ILE   A 1 437 ? -24.207 -7.156  -16.811 1.00 118.49 ? 457 ILE   A CA  1 
ATOM   3220 C  C   . ILE   A 1 437 ? -23.406 -5.902  -16.484 1.00 123.81 ? 457 ILE   A C   1 
ATOM   3221 O  O   . ILE   A 1 437 ? -23.218 -5.021  -17.331 1.00 126.39 ? 457 ILE   A O   1 
ATOM   3222 C  CB  . ILE   A 1 437 ? -25.505 -7.221  -15.989 1.00 119.01 ? 457 ILE   A CB  1 
ATOM   3223 C  CG1 . ILE   A 1 437 ? -26.466 -8.253  -16.580 1.00 115.01 ? 457 ILE   A CG1 1 
ATOM   3224 C  CG2 . ILE   A 1 437 ? -26.155 -5.858  -15.931 1.00 122.89 ? 457 ILE   A CG2 1 
ATOM   3225 C  CD1 . ILE   A 1 437 ? -27.686 -8.496  -15.725 1.00 111.17 ? 457 ILE   A CD1 1 
ATOM   3226 N  N   . ARG   A 1 438 ? -22.922 -5.806  -15.243 1.00 132.53 ? 458 ARG   A N   1 
ATOM   3227 C  CA  . ARG   A 1 438 ? -22.195 -4.614  -14.821 1.00 139.06 ? 458 ARG   A CA  1 
ATOM   3228 C  C   . ARG   A 1 438 ? -20.878 -4.461  -15.573 1.00 138.64 ? 458 ARG   A C   1 
ATOM   3229 O  O   . ARG   A 1 438 ? -20.378 -3.341  -15.720 1.00 147.25 ? 458 ARG   A O   1 
ATOM   3230 C  CB  . ARG   A 1 438 ? -21.943 -4.665  -13.314 1.00 144.61 ? 458 ARG   A CB  1 
ATOM   3231 C  CG  . ARG   A 1 438 ? -22.169 -3.350  -12.591 1.00 151.44 ? 458 ARG   A CG  1 
ATOM   3232 C  CD  . ARG   A 1 438 ? -23.242 -3.507  -11.528 1.00 149.90 ? 458 ARG   A CD  1 
ATOM   3233 N  NE  . ARG   A 1 438 ? -23.414 -2.304  -10.723 1.00 161.75 ? 458 ARG   A NE  1 
ATOM   3234 C  CZ  . ARG   A 1 438 ? -24.145 -1.258  -11.085 1.00 170.41 ? 458 ARG   A CZ  1 
ATOM   3235 N  NH1 . ARG   A 1 438 ? -24.764 -1.218  -12.253 1.00 174.05 ? 458 ARG   A NH1 1 
ATOM   3236 N  NH2 . ARG   A 1 438 ? -24.254 -0.225  -10.255 1.00 175.64 ? 458 ARG   A NH2 1 
ATOM   3237 N  N   . VAL   A 1 439 ? -20.308 -5.566  -16.054 1.00 121.20 ? 459 VAL   A N   1 
ATOM   3238 C  CA  . VAL   A 1 439 ? -19.046 -5.492  -16.783 1.00 123.06 ? 459 VAL   A CA  1 
ATOM   3239 C  C   . VAL   A 1 439 ? -19.272 -5.060  -18.229 1.00 127.51 ? 459 VAL   A C   1 
ATOM   3240 O  O   . VAL   A 1 439 ? -18.383 -4.460  -18.847 1.00 130.63 ? 459 VAL   A O   1 
ATOM   3241 C  CB  . VAL   A 1 439 ? -18.306 -6.840  -16.693 1.00 120.27 ? 459 VAL   A CB  1 
ATOM   3242 C  CG1 . VAL   A 1 439 ? -18.174 -7.500  -18.066 1.00 117.20 ? 459 VAL   A CG1 1 
ATOM   3243 C  CG2 . VAL   A 1 439 ? -16.942 -6.652  -16.057 1.00 122.52 ? 459 VAL   A CG2 1 
ATOM   3244 N  N   . LEU   A 1 440 ? -20.452 -5.334  -18.787 1.00 120.22 ? 460 LEU   A N   1 
ATOM   3245 C  CA  . LEU   A 1 440 ? -20.773 -4.899  -20.139 1.00 122.23 ? 460 LEU   A CA  1 
ATOM   3246 C  C   . LEU   A 1 440 ? -21.458 -3.541  -20.178 1.00 128.19 ? 460 LEU   A C   1 
ATOM   3247 O  O   . LEU   A 1 440 ? -21.531 -2.931  -21.250 1.00 128.29 ? 460 LEU   A O   1 
ATOM   3248 C  CB  . LEU   A 1 440 ? -21.653 -5.941  -20.834 1.00 116.48 ? 460 LEU   A CB  1 
ATOM   3249 C  CG  . LEU   A 1 440 ? -20.918 -7.245  -21.145 1.00 114.65 ? 460 LEU   A CG  1 
ATOM   3250 C  CD1 . LEU   A 1 440 ? -21.876 -8.298  -21.656 1.00 100.84 ? 460 LEU   A CD1 1 
ATOM   3251 C  CD2 . LEU   A 1 440 ? -19.806 -6.995  -22.150 1.00 113.59 ? 460 LEU   A CD2 1 
ATOM   3252 N  N   . GLN   A 1 441 ? -21.964 -3.059  -19.040 1.00 130.68 ? 461 GLN   A N   1 
ATOM   3253 C  CA  . GLN   A 1 441 ? -22.453 -1.687  -18.977 1.00 134.62 ? 461 GLN   A CA  1 
ATOM   3254 C  C   . GLN   A 1 441 ? -21.315 -0.685  -19.094 1.00 145.03 ? 461 GLN   A C   1 
ATOM   3255 O  O   . GLN   A 1 441 ? -21.526 0.439   -19.562 1.00 152.13 ? 461 GLN   A O   1 
ATOM   3256 C  CB  . GLN   A 1 441 ? -23.216 -1.454  -17.672 1.00 138.44 ? 461 GLN   A CB  1 
ATOM   3257 C  CG  . GLN   A 1 441 ? -24.648 -1.947  -17.681 1.00 133.71 ? 461 GLN   A CG  1 
ATOM   3258 C  CD  . GLN   A 1 441 ? -25.291 -1.900  -16.309 1.00 145.23 ? 461 GLN   A CD  1 
ATOM   3259 O  OE1 . GLN   A 1 441 ? -24.606 -1.932  -15.287 1.00 140.54 ? 461 GLN   A OE1 1 
ATOM   3260 N  NE2 . GLN   A 1 441 ? -26.616 -1.821  -16.280 1.00 147.89 ? 461 GLN   A NE2 1 
ATOM   3261 N  N   . ASN   A 1 442 ? -20.109 -1.072  -18.685 1.00 143.99 ? 462 ASN   A N   1 
ATOM   3262 C  CA  . ASN   A 1 442 ? -18.969 -0.166  -18.613 1.00 148.49 ? 462 ASN   A CA  1 
ATOM   3263 C  C   . ASN   A 1 442 ? -17.907 -0.423  -19.669 1.00 149.05 ? 462 ASN   A C   1 
ATOM   3264 O  O   . ASN   A 1 442 ? -17.304 0.530   -20.165 1.00 156.58 ? 462 ASN   A O   1 
ATOM   3265 C  CB  . ASN   A 1 442 ? -18.319 -0.249  -17.226 1.00 147.77 ? 462 ASN   A CB  1 
ATOM   3266 C  CG  . ASN   A 1 442 ? -19.064 0.559   -16.183 1.00 158.37 ? 462 ASN   A CG  1 
ATOM   3267 O  OD1 . ASN   A 1 442 ? -18.688 1.689   -15.874 1.00 158.62 ? 462 ASN   A OD1 1 
ATOM   3268 N  ND2 . ASN   A 1 442 ? -20.128 -0.017  -15.634 1.00 161.01 ? 462 ASN   A ND2 1 
ATOM   3269 N  N   . PHE   A 1 443 ? -17.652 -1.678  -20.031 1.00 135.90 ? 463 PHE   A N   1 
ATOM   3270 C  CA  . PHE   A 1 443 ? -16.529 -2.002  -20.896 1.00 141.19 ? 463 PHE   A CA  1 
ATOM   3271 C  C   . PHE   A 1 443 ? -16.981 -2.809  -22.104 1.00 135.39 ? 463 PHE   A C   1 
ATOM   3272 O  O   . PHE   A 1 443 ? -18.030 -3.459  -22.097 1.00 131.18 ? 463 PHE   A O   1 
ATOM   3273 C  CB  . PHE   A 1 443 ? -15.444 -2.792  -20.147 1.00 141.28 ? 463 PHE   A CB  1 
ATOM   3274 C  CG  . PHE   A 1 443 ? -15.014 -2.162  -18.856 1.00 142.98 ? 463 PHE   A CG  1 
ATOM   3275 C  CD1 . PHE   A 1 443 ? -14.085 -1.136  -18.843 1.00 148.89 ? 463 PHE   A CD1 1 
ATOM   3276 C  CD2 . PHE   A 1 443 ? -15.531 -2.607  -17.651 1.00 140.27 ? 463 PHE   A CD2 1 
ATOM   3277 C  CE1 . PHE   A 1 443 ? -13.686 -0.559  -17.652 1.00 149.97 ? 463 PHE   A CE1 1 
ATOM   3278 C  CE2 . PHE   A 1 443 ? -15.137 -2.035  -16.457 1.00 143.76 ? 463 PHE   A CE2 1 
ATOM   3279 C  CZ  . PHE   A 1 443 ? -14.213 -1.010  -16.457 1.00 146.50 ? 463 PHE   A CZ  1 
ATOM   3280 N  N   . SER   A 1 444 ? -16.162 -2.746  -23.150 1.00 135.33 ? 464 SER   A N   1 
ATOM   3281 C  CA  . SER   A 1 444 ? -16.220 -3.658  -24.278 1.00 129.61 ? 464 SER   A CA  1 
ATOM   3282 C  C   . SER   A 1 444 ? -14.899 -4.411  -24.354 1.00 131.29 ? 464 SER   A C   1 
ATOM   3283 O  O   . SER   A 1 444 ? -13.876 -3.962  -23.831 1.00 135.29 ? 464 SER   A O   1 
ATOM   3284 C  CB  . SER   A 1 444 ? -16.494 -2.920  -25.594 1.00 135.65 ? 464 SER   A CB  1 
ATOM   3285 O  OG  . SER   A 1 444 ? -17.802 -2.377  -25.606 1.00 132.28 ? 464 SER   A OG  1 
ATOM   3286 N  N   . PHE   A 1 445 ? -14.925 -5.570  -25.005 1.00 130.80 ? 465 PHE   A N   1 
ATOM   3287 C  CA  . PHE   A 1 445 ? -13.783 -6.474  -24.998 1.00 131.06 ? 465 PHE   A CA  1 
ATOM   3288 C  C   . PHE   A 1 445 ? -13.380 -6.818  -26.422 1.00 132.92 ? 465 PHE   A C   1 
ATOM   3289 O  O   . PHE   A 1 445 ? -14.221 -7.221  -27.232 1.00 129.94 ? 465 PHE   A O   1 
ATOM   3290 C  CB  . PHE   A 1 445 ? -14.102 -7.740  -24.198 1.00 113.18 ? 465 PHE   A CB  1 
ATOM   3291 C  CG  . PHE   A 1 445 ? -14.278 -7.490  -22.726 1.00 117.89 ? 465 PHE   A CG  1 
ATOM   3292 C  CD1 . PHE   A 1 445 ? -15.454 -6.944  -22.235 1.00 124.03 ? 465 PHE   A CD1 1 
ATOM   3293 C  CD2 . PHE   A 1 445 ? -13.263 -7.791  -21.833 1.00 121.21 ? 465 PHE   A CD2 1 
ATOM   3294 C  CE1 . PHE   A 1 445 ? -15.616 -6.707  -20.884 1.00 125.52 ? 465 PHE   A CE1 1 
ATOM   3295 C  CE2 . PHE   A 1 445 ? -13.419 -7.557  -20.480 1.00 118.37 ? 465 PHE   A CE2 1 
ATOM   3296 C  CZ  . PHE   A 1 445 ? -14.597 -7.015  -20.006 1.00 119.85 ? 465 PHE   A CZ  1 
ATOM   3297 N  N   . LYS   A 1 446 ? -12.092 -6.659  -26.718 1.00 135.86 ? 466 LYS   A N   1 
ATOM   3298 C  CA  . LYS   A 1 446 ? -11.510 -6.891  -28.027 1.00 145.68 ? 466 LYS   A CA  1 
ATOM   3299 C  C   . LYS   A 1 446 ? -10.377 -7.903  -27.926 1.00 140.23 ? 466 LYS   A C   1 
ATOM   3300 O  O   . LYS   A 1 446 ? -9.680  -7.959  -26.908 1.00 136.26 ? 466 LYS   A O   1 
ATOM   3301 C  CB  . LYS   A 1 446 ? -10.966 -5.589  -28.628 1.00 140.19 ? 466 LYS   A CB  1 
ATOM   3302 C  CG  . LYS   A 1 446 ? -11.979 -4.461  -28.711 1.00 150.60 ? 466 LYS   A CG  1 
ATOM   3303 C  CD  . LYS   A 1 446 ? -12.837 -4.573  -29.958 1.00 162.11 ? 466 LYS   A CD  1 
ATOM   3304 C  CE  . LYS   A 1 446 ? -13.796 -3.399  -30.066 1.00 178.04 ? 466 LYS   A CE  1 
ATOM   3305 N  NZ  . LYS   A 1 446 ? -14.480 -3.365  -31.387 1.00 168.89 ? 466 LYS   A NZ  1 
ATOM   3306 N  N   . PRO   A 1 447 ? -10.173 -8.721  -28.957 1.00 144.11 ? 467 PRO   A N   1 
ATOM   3307 C  CA  . PRO   A 1 447 ? -9.020  -9.626  -28.958 1.00 141.51 ? 467 PRO   A CA  1 
ATOM   3308 C  C   . PRO   A 1 447 ? -7.713  -8.849  -29.002 1.00 155.20 ? 467 PRO   A C   1 
ATOM   3309 O  O   . PRO   A 1 447 ? -7.651  -7.701  -29.447 1.00 151.41 ? 467 PRO   A O   1 
ATOM   3310 C  CB  . PRO   A 1 447 ? -9.214  -10.457 -30.234 1.00 138.17 ? 467 PRO   A CB  1 
ATOM   3311 C  CG  . PRO   A 1 447 ? -10.663 -10.314 -30.576 1.00 126.50 ? 467 PRO   A CG  1 
ATOM   3312 C  CD  . PRO   A 1 447 ? -11.048 -8.939  -30.121 1.00 137.70 ? 467 PRO   A CD  1 
ATOM   3313 N  N   . CYS   A 1 448 ? -6.660  -9.491  -28.513 1.00 157.27 ? 468 CYS   A N   1 
ATOM   3314 C  CA  . CYS   A 1 448 ? -5.304  -8.989  -28.648 1.00 164.03 ? 468 CYS   A CA  1 
ATOM   3315 C  C   . CYS   A 1 448 ? -4.497  -9.976  -29.478 1.00 163.63 ? 468 CYS   A C   1 
ATOM   3316 O  O   . CYS   A 1 448 ? -4.902  -11.124 -29.676 1.00 156.96 ? 468 CYS   A O   1 
ATOM   3317 C  CB  . CYS   A 1 448 ? -4.641  -8.771  -27.281 1.00 167.79 ? 468 CYS   A CB  1 
ATOM   3318 S  SG  . CYS   A 1 448 ? -5.275  -7.355  -26.359 1.00 170.65 ? 468 CYS   A SG  1 
ATOM   3319 N  N   . LYS   A 1 449 ? -3.346  -9.516  -29.975 1.00 180.59 ? 469 LYS   A N   1 
ATOM   3320 C  CA  . LYS   A 1 449 ? -2.495  -10.387 -30.779 1.00 180.79 ? 469 LYS   A CA  1 
ATOM   3321 C  C   . LYS   A 1 449 ? -2.070  -11.634 -30.014 1.00 176.45 ? 469 LYS   A C   1 
ATOM   3322 O  O   . LYS   A 1 449 ? -1.716  -12.642 -30.635 1.00 171.35 ? 469 LYS   A O   1 
ATOM   3323 C  CB  . LYS   A 1 449 ? -1.263  -9.621  -31.268 1.00 166.61 ? 469 LYS   A CB  1 
ATOM   3324 C  CG  . LYS   A 1 449 ? 0.003   -9.912  -30.482 1.00 174.54 ? 469 LYS   A CG  1 
ATOM   3325 C  CD  . LYS   A 1 449 ? 1.098   -8.908  -30.785 1.00 168.45 ? 469 LYS   A CD  1 
ATOM   3326 C  CE  . LYS   A 1 449 ? 2.344   -9.202  -29.968 1.00 171.93 ? 469 LYS   A CE  1 
ATOM   3327 N  NZ  . LYS   A 1 449 ? 3.388   -8.158  -30.151 1.00 187.70 ? 469 LYS   A NZ  1 
ATOM   3328 N  N   . GLU   A 1 450 ? -2.111  -11.590 -28.682 1.00 178.49 ? 470 GLU   A N   1 
ATOM   3329 C  CA  . GLU   A 1 450 ? -1.799  -12.741 -27.847 1.00 178.88 ? 470 GLU   A CA  1 
ATOM   3330 C  C   . GLU   A 1 450 ? -3.008  -13.627 -27.579 1.00 170.80 ? 470 GLU   A C   1 
ATOM   3331 O  O   . GLU   A 1 450 ? -2.834  -14.760 -27.117 1.00 171.49 ? 470 GLU   A O   1 
ATOM   3332 C  CB  . GLU   A 1 450 ? -1.200  -12.276 -26.513 1.00 187.11 ? 470 GLU   A CB  1 
ATOM   3333 C  CG  . GLU   A 1 450 ? -1.942  -11.123 -25.839 1.00 193.57 ? 470 GLU   A CG  1 
ATOM   3334 C  CD  . GLU   A 1 450 ? -1.546  -9.760  -26.380 1.00 204.16 ? 470 GLU   A CD  1 
ATOM   3335 O  OE1 . GLU   A 1 450 ? -1.121  -9.677  -27.550 1.00 209.83 ? 470 GLU   A OE1 1 
ATOM   3336 O  OE2 . GLU   A 1 450 ? -1.661  -8.768  -25.634 1.00 207.65 ? 470 GLU   A OE2 1 
ATOM   3337 N  N   . THR   A 1 451 ? -4.220  -13.142 -27.856 1.00 170.63 ? 471 THR   A N   1 
ATOM   3338 C  CA  . THR   A 1 451 ? -5.420  -13.947 -27.661 1.00 157.64 ? 471 THR   A CA  1 
ATOM   3339 C  C   . THR   A 1 451 ? -5.359  -15.201 -28.523 1.00 158.06 ? 471 THR   A C   1 
ATOM   3340 O  O   . THR   A 1 451 ? -5.257  -15.120 -29.750 1.00 154.42 ? 471 THR   A O   1 
ATOM   3341 C  CB  . THR   A 1 451 ? -6.670  -13.136 -28.000 1.00 153.65 ? 471 THR   A CB  1 
ATOM   3342 O  OG1 . THR   A 1 451 ? -6.605  -11.856 -27.361 1.00 154.73 ? 471 THR   A OG1 1 
ATOM   3343 C  CG2 . THR   A 1 451 ? -7.924  -13.869 -27.538 1.00 140.88 ? 471 THR   A CG2 1 
ATOM   3344 N  N   . GLN   A 1 452 ? -5.420  -16.360 -27.873 1.00 159.84 ? 472 GLN   A N   1 
ATOM   3345 C  CA  . GLN   A 1 452 ? -5.342  -17.647 -28.557 1.00 153.66 ? 472 GLN   A CA  1 
ATOM   3346 C  C   . GLN   A 1 452 ? -6.616  -17.863 -29.362 1.00 144.79 ? 472 GLN   A C   1 
ATOM   3347 O  O   . GLN   A 1 452 ? -7.636  -18.306 -28.830 1.00 145.83 ? 472 GLN   A O   1 
ATOM   3348 C  CB  . GLN   A 1 452 ? -5.133  -18.766 -27.545 1.00 158.65 ? 472 GLN   A CB  1 
ATOM   3349 C  CG  . GLN   A 1 452 ? -4.995  -20.145 -28.160 1.00 156.47 ? 472 GLN   A CG  1 
ATOM   3350 C  CD  . GLN   A 1 452 ? -5.115  -21.249 -27.131 1.00 155.68 ? 472 GLN   A CD  1 
ATOM   3351 O  OE1 . GLN   A 1 452 ? -5.991  -21.214 -26.266 1.00 154.97 ? 472 GLN   A OE1 1 
ATOM   3352 N  NE2 . GLN   A 1 452 ? -4.231  -22.236 -27.216 1.00 155.38 ? 472 GLN   A NE2 1 
ATOM   3353 N  N   . ILE   A 1 453 ? -6.563  -17.547 -30.649 1.00 144.32 ? 473 ILE   A N   1 
ATOM   3354 C  CA  . ILE   A 1 453 ? -7.679  -17.735 -31.570 1.00 147.51 ? 473 ILE   A CA  1 
ATOM   3355 C  C   . ILE   A 1 453 ? -7.276  -18.811 -32.575 1.00 148.66 ? 473 ILE   A C   1 
ATOM   3356 O  O   . ILE   A 1 453 ? -6.347  -18.596 -33.364 1.00 151.44 ? 473 ILE   A O   1 
ATOM   3357 C  CB  . ILE   A 1 453 ? -8.059  -16.428 -32.281 1.00 153.28 ? 473 ILE   A CB  1 
ATOM   3358 C  CG1 . ILE   A 1 453 ? -8.146  -15.276 -31.277 1.00 154.12 ? 473 ILE   A CG1 1 
ATOM   3359 C  CG2 . ILE   A 1 453 ? -9.382  -16.588 -33.011 1.00 145.38 ? 473 ILE   A CG2 1 
ATOM   3360 C  CD1 . ILE   A 1 453 ? -8.370  -13.926 -31.922 1.00 162.96 ? 473 ILE   A CD1 1 
ATOM   3361 N  N   . PRO   A 1 454 ? -7.935  -19.975 -32.587 1.00 146.43 ? 474 PRO   A N   1 
ATOM   3362 C  CA  . PRO   A 1 454 ? -9.064  -20.378 -31.739 1.00 134.54 ? 474 PRO   A CA  1 
ATOM   3363 C  C   . PRO   A 1 454 ? -8.616  -20.848 -30.360 1.00 131.92 ? 474 PRO   A C   1 
ATOM   3364 O  O   . PRO   A 1 454 ? -7.438  -21.118 -30.140 1.00 132.19 ? 474 PRO   A O   1 
ATOM   3365 C  CB  . PRO   A 1 454 ? -9.699  -21.510 -32.551 1.00 126.49 ? 474 PRO   A CB  1 
ATOM   3366 C  CG  . PRO   A 1 454 ? -8.517  -22.171 -33.202 1.00 134.66 ? 474 PRO   A CG  1 
ATOM   3367 C  CD  . PRO   A 1 454 ? -7.563  -21.043 -33.532 1.00 139.21 ? 474 PRO   A CD  1 
ATOM   3368 N  N   . LEU   A 1 455 ? -9.541  -20.956 -29.412 1.00 125.47 ? 475 LEU   A N   1 
ATOM   3369 C  CA  . LEU   A 1 455 ? -9.192  -21.420 -28.076 1.00 126.22 ? 475 LEU   A CA  1 
ATOM   3370 C  C   . LEU   A 1 455 ? -8.934  -22.921 -28.094 1.00 126.76 ? 475 LEU   A C   1 
ATOM   3371 O  O   . LEU   A 1 455 ? -9.781  -23.702 -28.536 1.00 122.94 ? 475 LEU   A O   1 
ATOM   3372 C  CB  . LEU   A 1 455 ? -10.313 -21.092 -27.092 1.00 123.21 ? 475 LEU   A CB  1 
ATOM   3373 C  CG  . LEU   A 1 455 ? -10.029 -21.366 -25.616 1.00 120.57 ? 475 LEU   A CG  1 
ATOM   3374 C  CD1 . LEU   A 1 455 ? -9.662  -20.077 -24.896 1.00 121.13 ? 475 LEU   A CD1 1 
ATOM   3375 C  CD2 . LEU   A 1 455 ? -11.221 -22.040 -24.960 1.00 106.51 ? 475 LEU   A CD2 1 
ATOM   3376 N  N   . LYS   A 1 456 ? -7.760  -23.323 -27.616 1.00 125.84 ? 476 LYS   A N   1 
ATOM   3377 C  CA  . LYS   A 1 456 ? -7.423  -24.731 -27.456 1.00 132.53 ? 476 LYS   A CA  1 
ATOM   3378 C  C   . LYS   A 1 456 ? -7.597  -25.115 -25.994 1.00 132.28 ? 476 LYS   A C   1 
ATOM   3379 O  O   . LYS   A 1 456 ? -7.141  -24.396 -25.098 1.00 132.04 ? 476 LYS   A O   1 
ATOM   3380 C  CB  . LYS   A 1 456 ? -5.993  -25.016 -27.919 1.00 137.39 ? 476 LYS   A CB  1 
ATOM   3381 C  CG  . LYS   A 1 456 ? -5.720  -24.661 -29.373 1.00 141.25 ? 476 LYS   A CG  1 
ATOM   3382 C  CD  . LYS   A 1 456 ? -4.339  -25.129 -29.808 1.00 145.27 ? 476 LYS   A CD  1 
ATOM   3383 C  CE  . LYS   A 1 456 ? -3.935  -24.523 -31.145 1.00 144.47 ? 476 LYS   A CE  1 
ATOM   3384 N  NZ  . LYS   A 1 456 ? -4.879  -24.872 -32.243 1.00 145.28 ? 476 LYS   A NZ  1 
ATOM   3385 N  N   . LEU   A 1 457 ? -8.260  -26.242 -25.757 1.00 125.74 ? 477 LEU   A N   1 
ATOM   3386 C  CA  . LEU   A 1 457 ? -8.573  -26.663 -24.403 1.00 126.40 ? 477 LEU   A CA  1 
ATOM   3387 C  C   . LEU   A 1 457 ? -7.386  -27.384 -23.770 1.00 132.84 ? 477 LEU   A C   1 
ATOM   3388 O  O   . LEU   A 1 457 ? -6.465  -27.846 -24.450 1.00 147.33 ? 477 LEU   A O   1 
ATOM   3389 C  CB  . LEU   A 1 457 ? -9.807  -27.564 -24.399 1.00 121.53 ? 477 LEU   A CB  1 
ATOM   3390 C  CG  . LEU   A 1 457 ? -11.125 -26.876 -24.761 1.00 120.49 ? 477 LEU   A CG  1 
ATOM   3391 C  CD1 . LEU   A 1 457 ? -12.131 -27.880 -25.299 1.00 120.59 ? 477 LEU   A CD1 1 
ATOM   3392 C  CD2 . LEU   A 1 457 ? -11.693 -26.147 -23.552 1.00 111.07 ? 477 LEU   A CD2 1 
ATOM   3393 N  N   . SER   A 1 458 ? -7.421  -27.473 -22.443 1.00 139.91 ? 478 SER   A N   1 
ATOM   3394 C  CA  . SER   A 1 458 ? -6.351  -28.108 -21.686 1.00 145.52 ? 478 SER   A CA  1 
ATOM   3395 C  C   . SER   A 1 458 ? -6.411  -29.622 -21.849 1.00 147.61 ? 478 SER   A C   1 
ATOM   3396 O  O   . SER   A 1 458 ? -7.446  -30.243 -21.589 1.00 137.63 ? 478 SER   A O   1 
ATOM   3397 C  CB  . SER   A 1 458 ? -6.454  -27.732 -20.209 1.00 135.06 ? 478 SER   A CB  1 
ATOM   3398 O  OG  . SER   A 1 458 ? -5.628  -28.561 -19.409 1.00 132.47 ? 478 SER   A OG  1 
ATOM   3399 N  N   . LEU   A 1 459 ? -5.292  -30.215 -22.273 1.00 175.97 ? 479 LEU   A N   1 
ATOM   3400 C  CA  . LEU   A 1 459 ? -5.204  -31.660 -22.454 1.00 168.64 ? 479 LEU   A CA  1 
ATOM   3401 C  C   . LEU   A 1 459 ? -5.304  -32.438 -21.146 1.00 165.74 ? 479 LEU   A C   1 
ATOM   3402 O  O   . LEU   A 1 459 ? -5.380  -33.670 -21.189 1.00 159.73 ? 479 LEU   A O   1 
ATOM   3403 C  CB  . LEU   A 1 459 ? -3.895  -32.031 -23.158 1.00 164.77 ? 479 LEU   A CB  1 
ATOM   3404 C  CG  . LEU   A 1 459 ? -3.807  -31.898 -24.682 1.00 178.47 ? 479 LEU   A CG  1 
ATOM   3405 C  CD1 . LEU   A 1 459 ? -3.789  -30.441 -25.124 1.00 169.27 ? 479 LEU   A CD1 1 
ATOM   3406 C  CD2 . LEU   A 1 459 ? -2.582  -32.634 -25.205 1.00 177.38 ? 479 LEU   A CD2 1 
ATOM   3407 N  N   . GLY   A 1 460 ? -5.303  -31.766 -19.996 1.00 150.65 ? 480 GLY   A N   1 
ATOM   3408 C  CA  . GLY   A 1 460 ? -5.355  -32.435 -18.710 1.00 140.71 ? 480 GLY   A CA  1 
ATOM   3409 C  C   . GLY   A 1 460 ? -6.747  -32.894 -18.329 1.00 144.29 ? 480 GLY   A C   1 
ATOM   3410 O  O   . GLY   A 1 460 ? -7.606  -33.142 -19.184 1.00 143.79 ? 480 GLY   A O   1 
ATOM   3411 N  N   . GLY   A 1 461 ? -6.975  -33.009 -17.023 1.00 134.22 ? 481 GLY   A N   1 
ATOM   3412 C  CA  . GLY   A 1 461 ? -8.249  -33.433 -16.486 1.00 135.65 ? 481 GLY   A CA  1 
ATOM   3413 C  C   . GLY   A 1 461 ? -9.220  -32.327 -16.149 1.00 137.31 ? 481 GLY   A C   1 
ATOM   3414 O  O   . GLY   A 1 461 ? -10.311 -32.606 -15.641 1.00 132.12 ? 481 GLY   A O   1 
ATOM   3415 N  N   . LEU   A 1 462 ? -8.861  -31.076 -16.415 1.00 142.91 ? 482 LEU   A N   1 
ATOM   3416 C  CA  . LEU   A 1 462 ? -9.711  -29.929 -16.136 1.00 139.96 ? 482 LEU   A CA  1 
ATOM   3417 C  C   . LEU   A 1 462 ? -10.224 -29.336 -17.438 1.00 140.97 ? 482 LEU   A C   1 
ATOM   3418 O  O   . LEU   A 1 462 ? -9.496  -29.280 -18.434 1.00 143.96 ? 482 LEU   A O   1 
ATOM   3419 C  CB  . LEU   A 1 462 ? -8.948  -28.858 -15.351 1.00 139.45 ? 482 LEU   A CB  1 
ATOM   3420 C  CG  . LEU   A 1 462 ? -8.691  -29.160 -13.877 1.00 146.13 ? 482 LEU   A CG  1 
ATOM   3421 C  CD1 . LEU   A 1 462 ? -7.733  -28.143 -13.282 1.00 145.42 ? 482 LEU   A CD1 1 
ATOM   3422 C  CD2 . LEU   A 1 462 ? -10.007 -29.166 -13.120 1.00 151.73 ? 482 LEU   A CD2 1 
ATOM   3423 N  N   . LEU   A 1 463 ? -11.478 -28.892 -17.432 1.00 120.13 ? 483 LEU   A N   1 
ATOM   3424 C  CA  . LEU   A 1 463 ? -12.006 -28.167 -18.584 1.00 117.80 ? 483 LEU   A CA  1 
ATOM   3425 C  C   . LEU   A 1 463 ? -11.575 -26.714 -18.448 1.00 120.95 ? 483 LEU   A C   1 
ATOM   3426 O  O   . LEU   A 1 463 ? -12.256 -25.886 -17.840 1.00 114.27 ? 483 LEU   A O   1 
ATOM   3427 C  CB  . LEU   A 1 463 ? -13.517 -28.298 -18.692 1.00 109.82 ? 483 LEU   A CB  1 
ATOM   3428 C  CG  . LEU   A 1 463 ? -13.936 -27.775 -20.067 1.00 110.25 ? 483 LEU   A CG  1 
ATOM   3429 C  CD1 . LEU   A 1 463 ? -13.214 -28.548 -21.158 1.00 104.89 ? 483 LEU   A CD1 1 
ATOM   3430 C  CD2 . LEU   A 1 463 ? -15.419 -27.860 -20.270 1.00 102.45 ? 483 LEU   A CD2 1 
ATOM   3431 N  N   . GLN   A 1 464 ? -10.417 -26.414 -19.014 1.00 120.86 ? 484 GLN   A N   1 
ATOM   3432 C  CA  . GLN   A 1 464 ? -9.814  -25.093 -18.984 1.00 116.89 ? 484 GLN   A CA  1 
ATOM   3433 C  C   . GLN   A 1 464 ? -9.129  -24.856 -20.319 1.00 119.04 ? 484 GLN   A C   1 
ATOM   3434 O  O   . GLN   A 1 464 ? -8.874  -25.804 -21.069 1.00 123.74 ? 484 GLN   A O   1 
ATOM   3435 C  CB  . GLN   A 1 464 ? -8.798  -24.963 -17.840 1.00 117.96 ? 484 GLN   A CB  1 
ATOM   3436 C  CG  . GLN   A 1 464 ? -9.418  -24.854 -16.460 1.00 129.56 ? 484 GLN   A CG  1 
ATOM   3437 C  CD  . GLN   A 1 464 ? -8.376  -24.771 -15.364 1.00 137.49 ? 484 GLN   A CD  1 
ATOM   3438 O  OE1 . GLN   A 1 464 ? -7.416  -25.541 -15.343 1.00 138.72 ? 484 GLN   A OE1 1 
ATOM   3439 N  NE2 . GLN   A 1 464 ? -8.557  -23.828 -14.448 1.00 139.22 ? 484 GLN   A NE2 1 
ATOM   3440 N  N   . PRO   A 1 465 ? -8.842  -23.602 -20.655 1.00 129.06 ? 485 PRO   A N   1 
ATOM   3441 C  CA  . PRO   A 1 465 ? -8.061  -23.335 -21.864 1.00 129.14 ? 485 PRO   A CA  1 
ATOM   3442 C  C   . PRO   A 1 465 ? -6.603  -23.718 -21.677 1.00 132.49 ? 485 PRO   A C   1 
ATOM   3443 O  O   . PRO   A 1 465 ? -6.071  -23.724 -20.564 1.00 128.06 ? 485 PRO   A O   1 
ATOM   3444 C  CB  . PRO   A 1 465 ? -8.217  -21.821 -22.064 1.00 126.48 ? 485 PRO   A CB  1 
ATOM   3445 C  CG  . PRO   A 1 465 ? -9.408  -21.439 -21.239 1.00 124.28 ? 485 PRO   A CG  1 
ATOM   3446 C  CD  . PRO   A 1 465 ? -9.395  -22.368 -20.074 1.00 121.34 ? 485 PRO   A CD  1 
ATOM   3447 N  N   . GLU   A 1 466 ? -5.963  -24.058 -22.795 1.00 144.57 ? 486 GLU   A N   1 
ATOM   3448 C  CA  . GLU   A 1 466 ? -4.532  -24.332 -22.823 1.00 148.75 ? 486 GLU   A CA  1 
ATOM   3449 C  C   . GLU   A 1 466 ? -3.776  -23.139 -22.256 1.00 150.48 ? 486 GLU   A C   1 
ATOM   3450 O  O   . GLU   A 1 466 ? -3.163  -23.229 -21.187 1.00 150.22 ? 486 GLU   A O   1 
ATOM   3451 C  CB  . GLU   A 1 466 ? -4.078  -24.627 -24.253 1.00 156.16 ? 486 GLU   A CB  1 
ATOM   3452 C  CG  . GLU   A 1 466 ? -3.055  -25.739 -24.390 1.00 160.42 ? 486 GLU   A CG  1 
ATOM   3453 C  CD  . GLU   A 1 466 ? -2.693  -26.003 -25.839 1.00 167.99 ? 486 GLU   A CD  1 
ATOM   3454 O  OE1 . GLU   A 1 466 ? -2.927  -25.110 -26.682 1.00 162.27 ? 486 GLU   A OE1 1 
ATOM   3455 O  OE2 . GLU   A 1 466 ? -2.183  -27.102 -26.138 1.00 171.84 ? 486 GLU   A OE2 1 
ATOM   3456 N  N   . LYS   A 1 467 ? -3.828  -22.016 -22.965 1.00 146.15 ? 487 LYS   A N   1 
ATOM   3457 C  CA  . LYS   A 1 467 ? -3.304  -20.727 -22.545 1.00 146.54 ? 487 LYS   A CA  1 
ATOM   3458 C  C   . LYS   A 1 467 ? -4.417  -19.875 -21.951 1.00 143.77 ? 487 LYS   A C   1 
ATOM   3459 O  O   . LYS   A 1 467 ? -5.566  -19.959 -22.397 1.00 139.82 ? 487 LYS   A O   1 
ATOM   3460 C  CB  . LYS   A 1 467 ? -2.676  -19.983 -23.726 1.00 150.71 ? 487 LYS   A CB  1 
ATOM   3461 C  CG  . LYS   A 1 467 ? -1.192  -19.709 -23.563 1.00 166.92 ? 487 LYS   A CG  1 
ATOM   3462 C  CD  . LYS   A 1 467 ? -0.394  -21.001 -23.553 1.00 176.51 ? 487 LYS   A CD  1 
ATOM   3463 C  CE  . LYS   A 1 467 ? 1.053   -20.753 -23.162 1.00 190.06 ? 487 LYS   A CE  1 
ATOM   3464 N  NZ  . LYS   A 1 467 ? 1.170   -20.287 -21.752 1.00 188.10 ? 487 LYS   A NZ  1 
ATOM   3465 N  N   . PRO   A 1 468 ? -4.113  -19.062 -20.939 1.00 147.74 ? 488 PRO   A N   1 
ATOM   3466 C  CA  . PRO   A 1 468 ? -5.139  -18.183 -20.367 1.00 133.93 ? 488 PRO   A CA  1 
ATOM   3467 C  C   . PRO   A 1 468 ? -5.662  -17.200 -21.402 1.00 126.92 ? 488 PRO   A C   1 
ATOM   3468 O  O   . PRO   A 1 468 ? -4.995  -16.876 -22.387 1.00 125.38 ? 488 PRO   A O   1 
ATOM   3469 C  CB  . PRO   A 1 468 ? -4.399  -17.461 -19.234 1.00 135.34 ? 488 PRO   A CB  1 
ATOM   3470 C  CG  . PRO   A 1 468 ? -3.244  -18.353 -18.905 1.00 138.12 ? 488 PRO   A CG  1 
ATOM   3471 C  CD  . PRO   A 1 468 ? -2.840  -18.980 -20.205 1.00 144.34 ? 488 PRO   A CD  1 
ATOM   3472 N  N   . VAL   A 1 469 ? -6.882  -16.725 -21.168 1.00 121.15 ? 489 VAL   A N   1 
ATOM   3473 C  CA  . VAL   A 1 469 ? -7.536  -15.817 -22.104 1.00 127.94 ? 489 VAL   A CA  1 
ATOM   3474 C  C   . VAL   A 1 469 ? -7.063  -14.397 -21.824 1.00 133.41 ? 489 VAL   A C   1 
ATOM   3475 O  O   . VAL   A 1 469 ? -7.265  -13.867 -20.726 1.00 140.75 ? 489 VAL   A O   1 
ATOM   3476 C  CB  . VAL   A 1 469 ? -9.064  -15.922 -22.007 1.00 121.90 ? 489 VAL   A CB  1 
ATOM   3477 C  CG1 . VAL   A 1 469 ? -9.713  -15.073 -23.087 1.00 116.45 ? 489 VAL   A CG1 1 
ATOM   3478 C  CG2 . VAL   A 1 469 ? -9.500  -17.373 -22.130 1.00 111.22 ? 489 VAL   A CG2 1 
ATOM   3479 N  N   . VAL   A 1 470 ? -6.429  -13.782 -22.818 1.00 126.10 ? 490 VAL   A N   1 
ATOM   3480 C  CA  . VAL   A 1 470 ? -5.917  -12.420 -22.721 1.00 134.30 ? 490 VAL   A CA  1 
ATOM   3481 C  C   . VAL   A 1 470 ? -6.667  -11.565 -23.733 1.00 136.82 ? 490 VAL   A C   1 
ATOM   3482 O  O   . VAL   A 1 470 ? -6.628  -11.843 -24.938 1.00 143.14 ? 490 VAL   A O   1 
ATOM   3483 C  CB  . VAL   A 1 470 ? -4.401  -12.364 -22.962 1.00 150.56 ? 490 VAL   A CB  1 
ATOM   3484 C  CG1 . VAL   A 1 470 ? -3.656  -12.639 -21.670 1.00 145.35 ? 490 VAL   A CG1 1 
ATOM   3485 C  CG2 . VAL   A 1 470 ? -4.002  -13.381 -24.016 1.00 153.47 ? 490 VAL   A CG2 1 
ATOM   3486 N  N   . LEU   A 1 471 ? -7.348  -10.530 -23.247 1.00 142.07 ? 491 LEU   A N   1 
ATOM   3487 C  CA  . LEU   A 1 471 ? -8.193  -9.701  -24.094 1.00 138.55 ? 491 LEU   A CA  1 
ATOM   3488 C  C   . LEU   A 1 471 ? -7.961  -8.230  -23.781 1.00 145.34 ? 491 LEU   A C   1 
ATOM   3489 O  O   . LEU   A 1 471 ? -7.392  -7.872  -22.747 1.00 147.99 ? 491 LEU   A O   1 
ATOM   3490 C  CB  . LEU   A 1 471 ? -9.676  -10.053 -23.918 1.00 125.24 ? 491 LEU   A CB  1 
ATOM   3491 C  CG  . LEU   A 1 471 ? -10.091 -11.461 -24.348 1.00 122.53 ? 491 LEU   A CG  1 
ATOM   3492 C  CD1 . LEU   A 1 471 ? -11.558 -11.704 -24.042 1.00 117.50 ? 491 LEU   A CD1 1 
ATOM   3493 C  CD2 . LEU   A 1 471 ? -9.812  -11.669 -25.826 1.00 128.13 ? 491 LEU   A CD2 1 
ATOM   3494 N  N   . LYS   A 1 472 ? -8.419  -7.378  -24.696 1.00 140.10 ? 492 LYS   A N   1 
ATOM   3495 C  CA  . LYS   A 1 472 ? -8.309  -5.931  -24.567 1.00 139.35 ? 492 LYS   A CA  1 
ATOM   3496 C  C   . LYS   A 1 472 ? -9.589  -5.372  -23.960 1.00 139.23 ? 492 LYS   A C   1 
ATOM   3497 O  O   . LYS   A 1 472 ? -10.693 -5.742  -24.368 1.00 128.35 ? 492 LYS   A O   1 
ATOM   3498 C  CB  . LYS   A 1 472 ? -8.047  -5.284  -25.929 1.00 140.02 ? 492 LYS   A CB  1 
ATOM   3499 C  CG  . LYS   A 1 472 ? -7.583  -3.838  -25.868 1.00 153.61 ? 492 LYS   A CG  1 
ATOM   3500 C  CD  . LYS   A 1 472 ? -6.725  -3.487  -27.076 1.00 160.91 ? 492 LYS   A CD  1 
ATOM   3501 C  CE  . LYS   A 1 472 ? -7.412  -3.873  -28.376 1.00 161.83 ? 492 LYS   A CE  1 
ATOM   3502 N  NZ  . LYS   A 1 472 ? -6.579  -3.536  -29.563 1.00 149.72 ? 492 LYS   A NZ  1 
ATOM   3503 N  N   . VAL   A 1 473 ? -9.435  -4.478  -22.987 1.00 150.51 ? 493 VAL   A N   1 
ATOM   3504 C  CA  . VAL   A 1 473 ? -10.552 -3.917  -22.235 1.00 148.04 ? 493 VAL   A CA  1 
ATOM   3505 C  C   . VAL   A 1 473 ? -10.659 -2.436  -22.566 1.00 151.67 ? 493 VAL   A C   1 
ATOM   3506 O  O   . VAL   A 1 473 ? -9.751  -1.655  -22.255 1.00 155.87 ? 493 VAL   A O   1 
ATOM   3507 C  CB  . VAL   A 1 473 ? -10.382 -4.136  -20.725 1.00 133.30 ? 493 VAL   A CB  1 
ATOM   3508 C  CG1 . VAL   A 1 473 ? -11.583 -3.592  -19.970 1.00 137.67 ? 493 VAL   A CG1 1 
ATOM   3509 C  CG2 . VAL   A 1 473 ? -10.180 -5.616  -20.426 1.00 125.73 ? 493 VAL   A CG2 1 
ATOM   3510 N  N   . GLU   A 1 474 ? -11.764 -2.051  -23.199 1.00 160.24 ? 494 GLU   A N   1 
ATOM   3511 C  CA  . GLU   A 1 474 ? -12.018 -0.674  -23.592 1.00 167.08 ? 494 GLU   A CA  1 
ATOM   3512 C  C   . GLU   A 1 474 ? -13.203 -0.124  -22.810 1.00 164.00 ? 494 GLU   A C   1 
ATOM   3513 O  O   . GLU   A 1 474 ? -14.202 -0.821  -22.611 1.00 163.58 ? 494 GLU   A O   1 
ATOM   3514 C  CB  . GLU   A 1 474 ? -12.293 -0.578  -25.095 1.00 175.26 ? 494 GLU   A CB  1 
ATOM   3515 C  CG  . GLU   A 1 474 ? -11.228 -1.232  -25.958 1.00 179.27 ? 494 GLU   A CG  1 
ATOM   3516 C  CD  . GLU   A 1 474 ? -11.486 -1.048  -27.439 1.00 184.59 ? 494 GLU   A CD  1 
ATOM   3517 O  OE1 . GLU   A 1 474 ? -12.602 -0.619  -27.800 1.00 183.64 ? 494 GLU   A OE1 1 
ATOM   3518 O  OE2 . GLU   A 1 474 ? -10.571 -1.326  -28.242 1.00 185.02 ? 494 GLU   A OE2 1 
ATOM   3519 N  N   . SER   A 1 475 ? -13.092 1.129   -22.377 1.00 157.80 ? 495 SER   A N   1 
ATOM   3520 C  CA  . SER   A 1 475 ? -14.112 1.755   -21.545 1.00 152.24 ? 495 SER   A CA  1 
ATOM   3521 C  C   . SER   A 1 475 ? -15.180 2.409   -22.414 1.00 150.52 ? 495 SER   A C   1 
ATOM   3522 O  O   . SER   A 1 475 ? -14.865 3.217   -23.293 1.00 152.07 ? 495 SER   A O   1 
ATOM   3523 C  CB  . SER   A 1 475 ? -13.481 2.792   -20.615 1.00 150.89 ? 495 SER   A CB  1 
ATOM   3524 O  OG  . SER   A 1 475 ? -14.457 3.402   -19.789 1.00 162.65 ? 495 SER   A OG  1 
ATOM   3525 N  N   . ARG   A 1 476 ? -16.439 2.058   -22.164 1.00 152.59 ? 496 ARG   A N   1 
ATOM   3526 C  CA  . ARG   A 1 476 ? -17.563 2.693   -22.848 1.00 147.91 ? 496 ARG   A CA  1 
ATOM   3527 C  C   . ARG   A 1 476 ? -17.862 4.053   -22.226 1.00 141.55 ? 496 ARG   A C   1 
ATOM   3528 O  O   . ARG   A 1 476 ? -17.872 5.074   -22.914 1.00 158.76 ? 496 ARG   A O   1 
ATOM   3529 C  CB  . ARG   A 1 476 ? -18.812 1.807   -22.795 1.00 142.90 ? 496 ARG   A CB  1 
ATOM   3530 C  CG  . ARG   A 1 476 ? -18.717 0.520   -23.602 1.00 135.85 ? 496 ARG   A CG  1 
ATOM   3531 C  CD  . ARG   A 1 476 ? -19.944 -0.357  -23.378 1.00 128.82 ? 496 ARG   A CD  1 
ATOM   3532 N  NE  . ARG   A 1 476 ? -21.088 0.057   -24.181 1.00 125.76 ? 496 ARG   A NE  1 
ATOM   3533 C  CZ  . ARG   A 1 476 ? -22.348 -0.259  -23.909 1.00 128.55 ? 496 ARG   A CZ  1 
ATOM   3534 N  NH1 . ARG   A 1 476 ? -22.669 -0.949  -22.827 1.00 122.61 ? 496 ARG   A NH1 1 
ATOM   3535 N  NH2 . ARG   A 1 476 ? -23.309 0.132   -24.741 1.00 128.38 ? 496 ARG   A NH2 1 
HETATM 3536 C  CHA . HEM   B 2 .   ? -23.146 -30.747 -8.813  1.00 73.00  ? 601 HEM   A CHA 1 
HETATM 3537 C  CHB . HEM   B 2 .   ? -22.445 -27.978 -12.750 1.00 66.19  ? 601 HEM   A CHB 1 
HETATM 3538 C  CHC . HEM   B 2 .   ? -21.786 -24.114 -9.897  1.00 82.41  ? 601 HEM   A CHC 1 
HETATM 3539 C  CHD . HEM   B 2 .   ? -22.521 -26.862 -5.957  1.00 72.03  ? 601 HEM   A CHD 1 
HETATM 3540 C  C1A . HEM   B 2 .   ? -22.982 -30.347 -10.123 1.00 76.60  ? 601 HEM   A C1A 1 
HETATM 3541 C  C2A . HEM   B 2 .   ? -23.003 -31.205 -11.291 1.00 72.25  ? 601 HEM   A C2A 1 
HETATM 3542 C  C3A . HEM   B 2 .   ? -22.810 -30.443 -12.371 1.00 72.57  ? 601 HEM   A C3A 1 
HETATM 3543 C  C4A . HEM   B 2 .   ? -22.660 -29.070 -11.936 1.00 70.49  ? 601 HEM   A C4A 1 
HETATM 3544 C  CMA . HEM   B 2 .   ? -22.756 -30.936 -13.832 1.00 68.59  ? 601 HEM   A CMA 1 
HETATM 3545 C  CAA . HEM   B 2 .   ? -23.209 -32.735 -11.288 1.00 54.44  ? 601 HEM   A CAA 1 
HETATM 3546 C  CBA . HEM   B 2 .   ? -24.678 -33.048 -11.551 1.00 61.74  ? 601 HEM   A CBA 1 
HETATM 3547 C  CGA . HEM   B 2 .   ? -24.866 -34.538 -11.655 1.00 67.87  ? 601 HEM   A CGA 1 
HETATM 3548 O  O1A . HEM   B 2 .   ? -26.006 -34.977 -11.957 1.00 73.96  ? 601 HEM   A O1A 1 
HETATM 3549 O  O2A . HEM   B 2 .   ? -23.879 -35.287 -11.440 1.00 68.37  ? 601 HEM   A O2A 1 
HETATM 3550 C  C1B . HEM   B 2 .   ? -22.192 -26.690 -12.329 1.00 73.51  ? 601 HEM   A C1B 1 
HETATM 3551 C  C2B . HEM   B 2 .   ? -21.885 -25.556 -13.179 1.00 81.90  ? 601 HEM   A C2B 1 
HETATM 3552 C  C3B . HEM   B 2 .   ? -21.702 -24.481 -12.387 1.00 76.17  ? 601 HEM   A C3B 1 
HETATM 3553 C  C4B . HEM   B 2 .   ? -21.888 -24.914 -11.015 1.00 67.36  ? 601 HEM   A C4B 1 
HETATM 3554 C  CMB . HEM   B 2 .   ? -21.805 -25.649 -14.720 1.00 67.46  ? 601 HEM   A CMB 1 
HETATM 3555 C  CAB . HEM   B 2 .   ? -21.357 -23.013 -12.754 1.00 77.97  ? 601 HEM   A CAB 1 
HETATM 3556 C  CBB . HEM   B 2 .   ? -21.193 -22.548 -13.998 1.00 85.96  ? 601 HEM   A CBB 1 
HETATM 3557 C  C1C . HEM   B 2 .   ? -21.987 -24.502 -8.589  1.00 80.90  ? 601 HEM   A C1C 1 
HETATM 3558 C  C2C . HEM   B 2 .   ? -22.061 -23.620 -7.444  1.00 80.41  ? 601 HEM   A C2C 1 
HETATM 3559 C  C3C . HEM   B 2 .   ? -22.266 -24.358 -6.351  1.00 82.61  ? 601 HEM   A C3C 1 
HETATM 3560 C  C4C . HEM   B 2 .   ? -22.327 -25.755 -6.760  1.00 74.53  ? 601 HEM   A C4C 1 
HETATM 3561 C  CMC . HEM   B 2 .   ? -21.930 -22.082 -7.478  1.00 80.63  ? 601 HEM   A CMC 1 
HETATM 3562 C  CAC . HEM   B 2 .   ? -22.398 -23.757 -4.930  1.00 73.17  ? 601 HEM   A CAC 1 
HETATM 3563 C  CBC . HEM   B 2 .   ? -22.665 -24.497 -3.850  1.00 82.34  ? 601 HEM   A CBC 1 
HETATM 3564 C  C1D . HEM   B 2 .   ? -22.724 -28.159 -6.380  1.00 72.60  ? 601 HEM   A C1D 1 
HETATM 3565 C  C2D . HEM   B 2 .   ? -22.888 -29.322 -5.531  1.00 77.14  ? 601 HEM   A C2D 1 
HETATM 3566 C  C3D . HEM   B 2 .   ? -23.058 -30.390 -6.317  1.00 74.24  ? 601 HEM   A C3D 1 
HETATM 3567 C  C4D . HEM   B 2 .   ? -23.011 -29.948 -7.696  1.00 70.35  ? 601 HEM   A C4D 1 
HETATM 3568 C  CMD . HEM   B 2 .   ? -22.864 -29.318 -3.986  1.00 72.92  ? 601 HEM   A CMD 1 
HETATM 3569 C  CAD . HEM   B 2 .   ? -23.277 -31.846 -5.850  1.00 66.71  ? 601 HEM   A CAD 1 
HETATM 3570 C  CBD . HEM   B 2 .   ? -24.721 -32.008 -5.385  1.00 66.33  ? 601 HEM   A CBD 1 
HETATM 3571 C  CGD . HEM   B 2 .   ? -24.933 -33.389 -4.824  1.00 71.21  ? 601 HEM   A CGD 1 
HETATM 3572 O  O1D . HEM   B 2 .   ? -26.012 -33.630 -4.223  1.00 64.59  ? 601 HEM   A O1D 1 
HETATM 3573 O  O2D . HEM   B 2 .   ? -24.025 -34.246 -4.973  1.00 69.44  ? 601 HEM   A O2D 1 
HETATM 3574 N  NA  . HEM   B 2 .   ? -22.772 -29.050 -10.557 1.00 72.95  ? 601 HEM   A NA  1 
HETATM 3575 N  NB  . HEM   B 2 .   ? -22.184 -26.262 -11.017 1.00 76.66  ? 601 HEM   A NB  1 
HETATM 3576 N  NC  . HEM   B 2 .   ? -22.153 -25.796 -8.133  1.00 70.66  ? 601 HEM   A NC  1 
HETATM 3577 N  ND  . HEM   B 2 .   ? -22.804 -28.581 -7.695  1.00 73.00  ? 601 HEM   A ND  1 
HETATM 3578 FE FE  . HEM   B 2 .   ? -22.559 -27.402 -9.351  1.00 65.77  ? 601 HEM   A FE  1 
HETATM 3579 C  C13 . A1A07 C 3 .   ? -15.377 -35.124 -8.205  1.00 136.42 ? 602 A1A07 A C13 1 
HETATM 3580 C  C15 . A1A07 C 3 .   ? -14.837 -32.418 -6.574  1.00 131.22 ? 602 A1A07 A C15 1 
HETATM 3581 C  C17 . A1A07 C 3 .   ? -13.712 -31.349 -4.415  1.00 126.55 ? 602 A1A07 A C17 1 
HETATM 3582 C  C20 . A1A07 C 3 .   ? -13.831 -30.739 -1.612  1.00 126.43 ? 602 A1A07 A C20 1 
HETATM 3583 C  C21 . A1A07 C 3 .   ? -14.156 -32.013 -2.085  1.00 128.49 ? 602 A1A07 A C21 1 
HETATM 3584 C  C22 . A1A07 C 3 .   ? -14.094 -32.314 -3.452  1.00 127.07 ? 602 A1A07 A C22 1 
HETATM 3585 C  C26 . A1A07 C 3 .   ? -16.650 -29.698 -6.528  1.00 98.77  ? 602 A1A07 A C26 1 
HETATM 3586 C  C28 . A1A07 C 3 .   ? -18.449 -28.267 -7.879  1.00 81.64  ? 602 A1A07 A C28 1 
HETATM 3587 C  C02 . A1A07 C 3 .   ? -10.863 -39.112 -10.379 1.00 171.11 ? 602 A1A07 A C02 1 
HETATM 3588 C  C05 . A1A07 C 3 .   ? -11.626 -37.695 -10.537 1.00 172.99 ? 602 A1A07 A C05 1 
HETATM 3589 C  C08 . A1A07 C 3 .   ? -11.921 -35.442 -11.726 1.00 161.91 ? 602 A1A07 A C08 1 
HETATM 3590 C  C09 . A1A07 C 3 .   ? -13.451 -35.296 -11.262 1.00 159.40 ? 602 A1A07 A C09 1 
HETATM 3591 C  C12 . A1A07 C 3 .   ? -15.251 -34.262 -9.537  1.00 128.05 ? 602 A1A07 A C12 1 
HETATM 3592 C  C16 . A1A07 C 3 .   ? -13.648 -31.672 -5.907  1.00 129.82 ? 602 A1A07 A C16 1 
HETATM 3593 C  C18 . A1A07 C 3 .   ? -13.396 -30.079 -3.914  1.00 121.91 ? 602 A1A07 A C18 1 
HETATM 3594 C  C19 . A1A07 C 3 .   ? -13.453 -29.779 -2.548  1.00 123.38 ? 602 A1A07 A C19 1 
HETATM 3595 C  C23 . A1A07 C 3 .   ? -16.242 -32.198 -5.866  1.00 119.45 ? 602 A1A07 A C23 1 
HETATM 3596 C  C27 . A1A07 C 3 .   ? -17.779 -28.573 -6.538  1.00 87.90  ? 602 A1A07 A C27 1 
HETATM 3597 C  C29 . A1A07 C 3 .   ? -19.853 -28.269 -8.030  1.00 83.25  ? 602 A1A07 A C29 1 
HETATM 3598 C  C31 . A1A07 C 3 .   ? -19.821 -27.729 -10.309 1.00 87.71  ? 602 A1A07 A C31 1 
HETATM 3599 C  C32 . A1A07 C 3 .   ? -18.421 -27.701 -10.289 1.00 91.02  ? 602 A1A07 A C32 1 
HETATM 3600 C  C33 . A1A07 C 3 .   ? -17.752 -27.969 -9.080  1.00 84.22  ? 602 A1A07 A C33 1 
HETATM 3601 C  C34 . A1A07 C 3 .   ? -16.512 -34.456 -10.512 1.00 123.71 ? 602 A1A07 A C34 1 
HETATM 3602 C  C35 . A1A07 C 3 .   ? -17.769 -33.658 -10.197 1.00 104.57 ? 602 A1A07 A C35 1 
HETATM 3603 C  C36 . A1A07 C 3 .   ? -18.653 -34.018 -9.156  1.00 94.41  ? 602 A1A07 A C36 1 
HETATM 3604 C  C37 . A1A07 C 3 .   ? -19.814 -33.271 -8.864  1.00 87.31  ? 602 A1A07 A C37 1 
HETATM 3605 C  C38 . A1A07 C 3 .   ? -20.138 -32.127 -9.604  1.00 88.79  ? 602 A1A07 A C38 1 
HETATM 3606 C  C39 . A1A07 C 3 .   ? -19.275 -31.752 -10.640 1.00 80.96  ? 602 A1A07 A C39 1 
HETATM 3607 C  C40 . A1A07 C 3 .   ? -18.119 -32.501 -10.925 1.00 93.44  ? 602 A1A07 A C40 1 
HETATM 3608 F  F01 . A1A07 C 3 .   ? -10.684 -39.408 -9.100  1.00 166.53 ? 602 A1A07 A F01 1 
HETATM 3609 F  F03 . A1A07 C 3 .   ? -9.626  -39.110 -10.950 1.00 170.52 ? 602 A1A07 A F03 1 
HETATM 3610 F  F04 . A1A07 C 3 .   ? -11.523 -40.130 -10.928 1.00 158.54 ? 602 A1A07 A F04 1 
HETATM 3611 N  N07 . A1A07 C 3 .   ? -11.256 -36.751 -11.548 1.00 169.20 ? 602 A1A07 A N07 1 
HETATM 3612 N  N11 . A1A07 C 3 .   ? -13.853 -34.484 -10.126 1.00 143.22 ? 602 A1A07 A N11 1 
HETATM 3613 N  N25 . A1A07 C 3 .   ? -17.014 -30.998 -5.859  1.00 106.06 ? 602 A1A07 A N25 1 
HETATM 3614 N  N30 . A1A07 C 3 .   ? -20.521 -28.013 -9.182  1.00 76.03  ? 602 A1A07 A N30 1 
HETATM 3615 O  O06 . A1A07 C 3 .   ? -12.498 -37.539 -9.708  1.00 173.19 ? 602 A1A07 A O06 1 
HETATM 3616 O  O10 . A1A07 C 3 .   ? -14.281 -35.906 -11.908 1.00 162.45 ? 602 A1A07 A O10 1 
HETATM 3617 O  O24 . A1A07 C 3 .   ? -16.681 -33.175 -5.271  1.00 110.35 ? 602 A1A07 A O24 1 
HETATM 3618 S  S14 . A1A07 C 3 .   ? -14.517 -34.291 -6.733  1.00 153.11 ? 602 A1A07 A S14 1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N  N   . HIS   A 8   ? 1.7568 1.6264 1.6559 0.2980  -0.1904 -0.1633 28  HIS   A N   
2    C  CA  . HIS   A 8   ? 1.9161 1.7060 1.8006 0.2864  -0.2068 -0.1652 28  HIS   A CA  
3    C  C   . HIS   A 8   ? 1.7855 1.5684 1.6846 0.2469  -0.2060 -0.1554 28  HIS   A C   
4    O  O   . HIS   A 8   ? 1.7915 1.5360 1.6819 0.2396  -0.2204 -0.1697 28  HIS   A O   
5    C  CB  . HIS   A 8   ? 2.1875 1.9353 2.0686 0.2889  -0.2104 -0.1487 28  HIS   A CB  
6    C  CG  . HIS   A 8   ? 2.3580 2.1475 2.2579 0.2761  -0.1963 -0.1246 28  HIS   A CG  
7    N  ND1 . HIS   A 8   ? 2.2850 2.0665 2.1968 0.2420  -0.1882 -0.1024 28  HIS   A ND1 
8    C  CD2 . HIS   A 8   ? 2.3325 2.1718 2.2420 0.2935  -0.1901 -0.1207 28  HIS   A CD2 
9    C  CE1 . HIS   A 8   ? 2.0936 1.9129 2.0151 0.2404  -0.1783 -0.0872 28  HIS   A CE1 
10   N  NE2 . HIS   A 8   ? 2.2014 2.0563 2.1237 0.2698  -0.1808 -0.0980 28  HIS   A NE2 
11   N  N   . SER   A 9   ? 1.6629 1.4829 1.5852 0.2227  -0.1908 -0.1323 29  SER   A N   
12   C  CA  . SER   A 9   ? 1.4766 1.3011 1.4177 0.1882  -0.1876 -0.1219 29  SER   A CA  
13   C  C   . SER   A 9   ? 1.4128 1.2735 1.3526 0.1886  -0.1894 -0.1378 29  SER   A C   
14   O  O   . SER   A 9   ? 1.2772 1.1459 1.2332 0.1630  -0.1895 -0.1312 29  SER   A O   
15   C  CB  . SER   A 9   ? 1.4621 1.3195 1.4237 0.1684  -0.1698 -0.0954 29  SER   A CB  
16   O  OG  . SER   A 9   ? 1.4239 1.3452 1.3916 0.1787  -0.1580 -0.0955 29  SER   A OG  
17   N  N   . HIS   A 10  ? 1.3652 1.2487 1.2851 0.2190  -0.1902 -0.1574 30  HIS   A N   
18   C  CA  . HIS   A 10  ? 1.2556 1.1733 1.1646 0.2252  -0.1897 -0.1719 30  HIS   A CA  
19   C  C   . HIS   A 10  ? 1.4628 1.3325 1.3520 0.2243  -0.2131 -0.1943 30  HIS   A C   
20   O  O   . HIS   A 10  ? 1.4558 1.3467 1.3285 0.2309  -0.2165 -0.2080 30  HIS   A O   
21   C  CB  . HIS   A 10  ? 1.2464 1.2073 1.1405 0.2606  -0.1784 -0.1831 30  HIS   A CB  
22   C  CG  . HIS   A 10  ? 1.1755 1.1906 1.0950 0.2596  -0.1582 -0.1630 30  HIS   A CG  
23   N  ND1 . HIS   A 10  ? 1.2023 1.2337 1.1483 0.2296  -0.1494 -0.1389 30  HIS   A ND1 
24   C  CD2 . HIS   A 10  ? 0.9809 1.0372 0.9057 0.2850  -0.1467 -0.1644 30  HIS   A CD2 
25   C  CE1 . HIS   A 10  ? 1.1030 1.1791 1.0668 0.2355  -0.1358 -0.1277 30  HIS   A CE1 
26   N  NE2 . HIS   A 10  ? 1.1166 1.2114 1.0719 0.2676  -0.1341 -0.1420 30  HIS   A NE2 
27   N  N   . GLY   A 11  ? 1.3979 1.2013 1.2869 0.2164  -0.2304 -0.1981 31  GLY   A N   
28   C  CA  . GLY   A 11  ? 1.3490 1.1023 1.2259 0.2103  -0.2565 -0.2192 31  GLY   A CA  
29   C  C   . GLY   A 11  ? 1.4396 1.1899 1.3485 0.1708  -0.2636 -0.2070 31  GLY   A C   
30   O  O   . GLY   A 11  ? 1.5509 1.2705 1.4552 0.1631  -0.2878 -0.2255 31  GLY   A O   
31   N  N   . LEU   A 12  ? 1.3923 1.1753 1.3341 0.1470  -0.2442 -0.1775 32  LEU   A N   
32   C  CA  . LEU   A 12  ? 1.3882 1.1694 1.3677 0.1101  -0.2471 -0.1618 32  LEU   A CA  
33   C  C   . LEU   A 12  ? 1.3604 1.1654 1.3419 0.1029  -0.2616 -0.1753 32  LEU   A C   
34   O  O   . LEU   A 12  ? 1.4550 1.2247 1.4470 0.0883  -0.2864 -0.1880 32  LEU   A O   
35   C  CB  . LEU   A 12  ? 1.2508 1.0707 1.2564 0.0943  -0.2202 -0.1301 32  LEU   A CB  
36   C  CG  . LEU   A 12  ? 1.1974 1.0228 1.2446 0.0591  -0.2182 -0.1116 32  LEU   A CG  
37   C  CD1 . LEU   A 12  ? 1.3104 1.0780 1.3765 0.0406  -0.2240 -0.1022 32  LEU   A CD1 
38   C  CD2 . LEU   A 12  ? 1.1328 1.0074 1.1968 0.0504  -0.1921 -0.0864 32  LEU   A CD2 
39   N  N   . PHE   A 13  ? 1.2690 1.1321 1.2411 0.1126  -0.2477 -0.1721 33  PHE   A N   
40   C  CA  . PHE   A 13  ? 1.3025 1.1900 1.2718 0.1081  -0.2606 -0.1818 33  PHE   A CA  
41   C  C   . PHE   A 13  ? 1.3836 1.2336 1.3170 0.1259  -0.2905 -0.2163 33  PHE   A C   
42   O  O   . PHE   A 13  ? 1.4880 1.3281 1.4282 0.1132  -0.3152 -0.2279 33  PHE   A O   
43   C  CB  . PHE   A 13  ? 1.2895 1.2391 1.2457 0.1208  -0.2386 -0.1720 33  PHE   A CB  
44   C  CG  . PHE   A 13  ? 1.2822 1.2671 1.2727 0.1014  -0.2140 -0.1409 33  PHE   A CG  
45   C  CD1 . PHE   A 13  ? 1.2673 1.2493 1.2981 0.0717  -0.2161 -0.1248 33  PHE   A CD1 
46   C  CD2 . PHE   A 13  ? 1.2540 1.2751 1.2381 0.1135  -0.1892 -0.1284 33  PHE   A CD2 
47   C  CE1 . PHE   A 13  ? 1.2088 1.2197 1.2656 0.0575  -0.1932 -0.0981 33  PHE   A CE1 
48   C  CE2 . PHE   A 13  ? 1.1917 1.2391 1.2032 0.0967  -0.1696 -0.1027 33  PHE   A CE2 
49   C  CZ  . PHE   A 13  ? 1.1999 1.2403 1.2442 0.0702  -0.1712 -0.0882 33  PHE   A CZ  
50   N  N   . LYS   A 14  ? 1.6291 1.4580 1.5236 0.1572  -0.2901 -0.2342 34  LYS   A N   
51   C  CA  . LYS   A 14  ? 1.6414 1.4257 1.4953 0.1785  -0.3187 -0.2697 34  LYS   A CA  
52   C  C   . LYS   A 14  ? 1.6931 1.4151 1.5705 0.1530  -0.3502 -0.2794 34  LYS   A C   
53   O  O   . LYS   A 14  ? 1.7652 1.4657 1.6306 0.1506  -0.3809 -0.3027 34  LYS   A O   
54   C  CB  . LYS   A 14  ? 1.7502 1.5178 1.5668 0.2159  -0.3100 -0.2837 34  LYS   A CB  
55   C  CG  . LYS   A 14  ? 1.9400 1.6396 1.7192 0.2362  -0.3406 -0.3193 34  LYS   A CG  
56   C  CD  . LYS   A 14  ? 2.0826 1.7559 1.8418 0.2665  -0.3315 -0.3258 34  LYS   A CD  
57   C  CE  . LYS   A 14  ? 2.2978 1.8967 2.0162 0.2893  -0.3627 -0.3629 34  LYS   A CE  
58   N  NZ  . LYS   A 14  ? 2.3397 1.8753 2.0827 0.2546  -0.3949 -0.3681 34  LYS   A NZ  
59   N  N   . LYS   A 15  ? 1.4779 1.1695 1.3890 0.1335  -0.3437 -0.2610 35  LYS   A N   
60   C  CA  . LYS   A 15  ? 1.5222 1.1577 1.4658 0.1037  -0.3690 -0.2636 35  LYS   A CA  
61   C  C   . LYS   A 15  ? 1.4447 1.1105 1.4325 0.0705  -0.3789 -0.2541 35  LYS   A C   
62   O  O   . LYS   A 15  ? 1.6243 1.2584 1.6243 0.0558  -0.4127 -0.2728 35  LYS   A O   
63   C  CB  . LYS   A 15  ? 1.6065 1.2109 1.5768 0.0891  -0.3526 -0.2382 35  LYS   A CB  
64   C  CG  . LYS   A 15  ? 1.6432 1.1931 1.6554 0.0537  -0.3722 -0.2332 35  LYS   A CG  
65   C  CD  . LYS   A 15  ? 1.7383 1.2869 1.7882 0.0305  -0.3450 -0.1946 35  LYS   A CD  
66   C  CE  . LYS   A 15  ? 1.6393 1.2612 1.7206 0.0148  -0.3190 -0.1681 35  LYS   A CE  
67   N  NZ  . LYS   A 15  ? 1.7109 1.3303 1.8230 -0.0053 -0.2917 -0.1316 35  LYS   A NZ  
68   N  N   . LEU   A 16  ? 1.5408 1.2676 1.5545 0.0590  -0.3517 -0.2259 36  LEU   A N   
69   C  CA  . LEU   A 16  ? 1.4516 1.2139 1.5078 0.0320  -0.3589 -0.2157 36  LEU   A CA  
70   C  C   . LEU   A 16  ? 1.3388 1.1217 1.3644 0.0470  -0.3824 -0.2404 36  LEU   A C   
71   O  O   . LEU   A 16  ? 1.3147 1.1219 1.3734 0.0272  -0.3967 -0.2369 36  LEU   A O   
72   C  CB  . LEU   A 16  ? 1.3318 1.1502 1.4159 0.0213  -0.3231 -0.1808 36  LEU   A CB  
73   C  CG  . LEU   A 16  ? 1.3525 1.1572 1.4770 -0.0016 -0.3014 -0.1514 36  LEU   A CG  
74   C  CD1 . LEU   A 16  ? 1.2968 1.1575 1.4475 -0.0119 -0.2717 -0.1218 36  LEU   A CD1 
75   C  CD2 . LEU   A 16  ? 1.4118 1.1763 1.5824 -0.0322 -0.3225 -0.1514 36  LEU   A CD2 
76   N  N   . GLY   A 17  ? 1.3436 1.1188 1.3065 0.0832  -0.3862 -0.2645 37  GLY   A N   
77   C  CA  . GLY   A 17  ? 1.4359 1.2283 1.3590 0.1017  -0.4062 -0.2870 37  GLY   A CA  
78   C  C   . GLY   A 17  ? 1.3841 1.2445 1.3098 0.1026  -0.3853 -0.2664 37  GLY   A C   
79   O  O   . GLY   A 17  ? 1.4839 1.3603 1.3927 0.1072  -0.4055 -0.2778 37  GLY   A O   
80   N  N   . ILE   A 18  ? 1.2678 1.1650 1.2122 0.0987  -0.3474 -0.2365 38  ILE   A N   
81   C  CA  . ILE   A 18  ? 1.2462 1.2031 1.1933 0.0993  -0.3252 -0.2148 38  ILE   A CA  
82   C  C   . ILE   A 18  ? 1.1844 1.1643 1.0759 0.1340  -0.3052 -0.2200 38  ILE   A C   
83   O  O   . ILE   A 18  ? 1.1327 1.1031 1.0111 0.1489  -0.2883 -0.2211 38  ILE   A O   
84   C  CB  . ILE   A 18  ? 1.3017 1.2829 1.3014 0.0745  -0.2973 -0.1805 38  ILE   A CB  
85   C  CG1 . ILE   A 18  ? 1.2846 1.2563 1.3423 0.0411  -0.3138 -0.1723 38  ILE   A CG1 
86   C  CG2 . ILE   A 18  ? 1.2310 1.2672 1.2255 0.0801  -0.2705 -0.1591 38  ILE   A CG2 
87   C  CD1 . ILE   A 18  ? 1.2653 1.2367 1.3692 0.0189  -0.2892 -0.1444 38  ILE   A CD1 
88   N  N   . PRO   A 19  ? 1.1640 1.1750 1.0229 0.1487  -0.3056 -0.2222 39  PRO   A N   
89   C  CA  . PRO   A 19  ? 1.1972 1.2311 1.0034 0.1822  -0.2844 -0.2261 39  PRO   A CA  
90   C  C   . PRO   A 19  ? 1.1180 1.1953 0.9463 0.1785  -0.2442 -0.1957 39  PRO   A C   
91   O  O   . PRO   A 19  ? 1.0563 1.1482 0.9319 0.1523  -0.2336 -0.1718 39  PRO   A O   
92   C  CB  . PRO   A 19  ? 1.1395 1.1910 0.9074 0.1943  -0.2978 -0.2326 39  PRO   A CB  
93   C  CG  . PRO   A 19  ? 1.1037 1.1668 0.9214 0.1626  -0.3107 -0.2162 39  PRO   A CG  
94   C  CD  . PRO   A 19  ? 1.0947 1.1226 0.9643 0.1362  -0.3252 -0.2193 39  PRO   A CD  
95   N  N   . GLY   A 20  ? 1.1908 1.2889 0.9845 0.2062  -0.2223 -0.1979 40  GLY   A N   
96   C  CA  . GLY   A 20  ? 1.1845 1.3254 0.9992 0.2040  -0.1869 -0.1718 40  GLY   A CA  
97   C  C   . GLY   A 20  ? 1.1136 1.2712 0.8994 0.2355  -0.1666 -0.1794 40  GLY   A C   
98   O  O   . GLY   A 20  ? 1.2413 1.3716 0.9902 0.2611  -0.1789 -0.2061 40  GLY   A O   
99   N  N   . PRO   A 21  ? 1.1160 1.3197 0.9206 0.2346  -0.1354 -0.1563 41  PRO   A N   
100  C  CA  . PRO   A 21  ? 1.0004 1.2300 0.7893 0.2633  -0.1133 -0.1606 41  PRO   A CA  
101  C  C   . PRO   A 21  ? 1.2055 1.4066 1.0068 0.2721  -0.1206 -0.1750 41  PRO   A C   
102  O  O   . PRO   A 21  ? 1.0905 1.2691 0.9269 0.2498  -0.1293 -0.1680 41  PRO   A O   
103  C  CB  . PRO   A 21  ? 1.0486 1.3318 0.8709 0.2500  -0.0826 -0.1293 41  PRO   A CB  
104  C  CG  . PRO   A 21  ? 0.9792 1.2510 0.8408 0.2143  -0.0910 -0.1122 41  PRO   A CG  
105  C  CD  . PRO   A 21  ? 0.9165 1.1506 0.7597 0.2075  -0.1197 -0.1258 41  PRO   A CD  
106  N  N   . THR   A 22  ? 1.2338 1.4349 1.0030 0.3074  -0.1161 -0.1945 42  THR   A N   
107  C  CA  . THR   A 22  ? 1.2457 1.4175 1.0214 0.3218  -0.1238 -0.2095 42  THR   A CA  
108  C  C   . THR   A 22  ? 1.0831 1.2931 0.9061 0.3144  -0.1027 -0.1879 42  THR   A C   
109  O  O   . THR   A 22  ? 1.0482 1.3158 0.8827 0.3215  -0.0760 -0.1734 42  THR   A O   
110  C  CB  . THR   A 22  ? 1.2020 1.3659 0.9292 0.3660  -0.1233 -0.2370 42  THR   A CB  
111  O  OG1 . THR   A 22  ? 1.4360 1.5740 1.1128 0.3748  -0.1407 -0.2558 42  THR   A OG1 
112  C  CG2 . THR   A 22  ? 1.2296 1.3434 0.9557 0.3810  -0.1408 -0.2572 42  THR   A CG2 
113  N  N   . PRO   A 23  ? 1.0305 1.2098 0.8812 0.2998  -0.1142 -0.1845 43  PRO   A N   
114  C  CA  . PRO   A 23  ? 1.0517 1.2640 0.9444 0.2922  -0.0990 -0.1650 43  PRO   A CA  
115  C  C   . PRO   A 23  ? 1.0362 1.2631 0.9295 0.3260  -0.0923 -0.1760 43  PRO   A C   
116  O  O   . PRO   A 23  ? 1.1393 1.3296 1.0028 0.3530  -0.1049 -0.1997 43  PRO   A O   
117  C  CB  . PRO   A 23  ? 1.0648 1.2301 0.9768 0.2650  -0.1161 -0.1575 43  PRO   A CB  
118  C  CG  . PRO   A 23  ? 1.0413 1.1441 0.9233 0.2722  -0.1406 -0.1803 43  PRO   A CG  
119  C  CD  . PRO   A 23  ? 1.0562 1.1683 0.9026 0.2857  -0.1423 -0.1954 43  PRO   A CD  
120  N  N   . LEU   A 24  ? 1.0092 1.2916 0.9402 0.3246  -0.0732 -0.1586 44  LEU   A N   
121  C  CA  . LEU   A 24  ? 0.9780 1.2848 0.9263 0.3520  -0.0673 -0.1638 44  LEU   A CA  
122  C  C   . LEU   A 24  ? 1.0935 1.3647 1.0611 0.3425  -0.0846 -0.1597 44  LEU   A C   
123  O  O   . LEU   A 24  ? 1.0624 1.3182 1.0454 0.3102  -0.0899 -0.1436 44  LEU   A O   
124  C  CB  . LEU   A 24  ? 0.9329 1.3201 0.9194 0.3519  -0.0405 -0.1462 44  LEU   A CB  
125  C  CG  . LEU   A 24  ? 0.9159 1.3498 0.8862 0.3671  -0.0158 -0.1457 44  LEU   A CG  
126  C  CD1 . LEU   A 24  ? 0.8792 1.3912 0.9002 0.3617  0.0104  -0.1241 44  LEU   A CD1 
127  C  CD2 . LEU   A 24  ? 0.9803 1.4016 0.9098 0.4114  -0.0156 -0.1722 44  LEU   A CD2 
128  N  N   . PRO   A 25  ? 1.1089 1.3640 1.0723 0.3725  -0.0931 -0.1735 45  PRO   A N   
129  C  CA  . PRO   A 25  ? 1.0114 1.2313 0.9879 0.3669  -0.1094 -0.1677 45  PRO   A CA  
130  C  C   . PRO   A 25  ? 0.8980 1.1667 0.9189 0.3484  -0.1013 -0.1459 45  PRO   A C   
131  O  O   . PRO   A 25  ? 0.9938 1.3313 1.0448 0.3526  -0.0838 -0.1394 45  PRO   A O   
132  C  CB  . PRO   A 25  ? 1.0028 1.2090 0.9669 0.4100  -0.1169 -0.1872 45  PRO   A CB  
133  C  CG  . PRO   A 25  ? 1.0466 1.2474 0.9750 0.4332  -0.1119 -0.2084 45  PRO   A CG  
134  C  CD  . PRO   A 25  ? 1.0327 1.2904 0.9708 0.4155  -0.0902 -0.1967 45  PRO   A CD  
135  N  N   . PHE   A 26  ? 0.9181 1.1488 0.9423 0.3266  -0.1142 -0.1342 46  PHE   A N   
136  C  CA  . PHE   A 26  ? 1.0774 1.3382 1.1349 0.3100  -0.1132 -0.1164 46  PHE   A CA  
137  C  C   . PHE   A 26  ? 1.0146 1.3218 1.0957 0.2812  -0.0969 -0.1011 46  PHE   A C   
138  O  O   . PHE   A 26  ? 1.1634 1.4860 1.2679 0.2618  -0.0978 -0.0867 46  PHE   A O   
139  C  CB  . PHE   A 26  ? 0.9565 1.2600 1.0414 0.3381  -0.1152 -0.1206 46  PHE   A CB  
140  C  CG  . PHE   A 26  ? 1.1428 1.3977 1.2059 0.3673  -0.1337 -0.1327 46  PHE   A CG  
141  C  CD1 . PHE   A 26  ? 1.2724 1.4755 1.3222 0.3595  -0.1509 -0.1244 46  PHE   A CD1 
142  C  CD2 . PHE   A 26  ? 1.1561 1.4145 1.2083 0.4048  -0.1330 -0.1516 46  PHE   A CD2 
143  C  CE1 . PHE   A 26  ? 1.2517 1.4054 1.2786 0.3869  -0.1678 -0.1329 46  PHE   A CE1 
144  C  CE2 . PHE   A 26  ? 1.2822 1.4910 1.3131 0.4334  -0.1509 -0.1624 46  PHE   A CE2 
145  C  CZ  . PHE   A 26  ? 1.2078 1.3633 1.2265 0.4237  -0.1687 -0.1522 46  PHE   A CZ  
146  N  N   . LEU   A 27  ? 0.9332 1.2593 1.0047 0.2797  -0.0832 -0.1042 47  LEU   A N   
147  C  CA  . LEU   A 27  ? 0.8856 1.2492 0.9742 0.2539  -0.0675 -0.0886 47  LEU   A CA  
148  C  C   . LEU   A 27  ? 0.8721 1.2018 0.9336 0.2350  -0.0682 -0.0870 47  LEU   A C   
149  O  O   . LEU   A 27  ? 0.8208 1.1658 0.8944 0.2099  -0.0600 -0.0714 47  LEU   A O   
150  C  CB  . LEU   A 27  ? 0.7567 1.1879 0.8640 0.2685  -0.0461 -0.0879 47  LEU   A CB  
151  C  CG  . LEU   A 27  ? 0.8577 1.3395 1.0036 0.2883  -0.0423 -0.0888 47  LEU   A CG  
152  C  CD1 . LEU   A 27  ? 0.8680 1.4203 1.0366 0.2967  -0.0155 -0.0829 47  LEU   A CD1 
153  C  CD2 . LEU   A 27  ? 0.8339 1.3224 1.0147 0.2676  -0.0533 -0.0762 47  LEU   A CD2 
154  N  N   . GLY   A 28  ? 0.8549 1.1382 0.8823 0.2463  -0.0796 -0.1029 48  GLY   A N   
155  C  CA  . GLY   A 28  ? 0.9112 1.1713 0.9180 0.2301  -0.0821 -0.1030 48  GLY   A CA  
156  C  C   . GLY   A 28  ? 0.9122 1.2193 0.9146 0.2335  -0.0647 -0.0998 48  GLY   A C   
157  O  O   . GLY   A 28  ? 0.9129 1.2514 0.9080 0.2597  -0.0538 -0.1086 48  GLY   A O   
158  N  N   . ASN   A 29  ? 0.8524 1.1649 0.8585 0.2087  -0.0603 -0.0855 49  ASN   A N   
159  C  CA  . ASN   A 29  ? 0.7750 1.1263 0.7731 0.2095  -0.0437 -0.0780 49  ASN   A CA  
160  C  C   . ASN   A 29  ? 0.8758 1.2720 0.9096 0.1910  -0.0257 -0.0541 49  ASN   A C   
161  O  O   . ASN   A 29  ? 0.8897 1.3078 0.9194 0.1822  -0.0132 -0.0413 49  ASN   A O   
162  C  CB  . ASN   A 29  ? 0.8473 1.1700 0.8196 0.1983  -0.0545 -0.0802 49  ASN   A CB  
163  C  CG  . ASN   A 29  ? 0.9218 1.1916 0.8675 0.2080  -0.0780 -0.1031 49  ASN   A CG  
164  O  OD1 . ASN   A 29  ? 0.9015 1.1326 0.8587 0.1920  -0.0928 -0.1030 49  ASN   A OD1 
165  N  ND2 . ASN   A 29  ? 1.0180 1.2839 0.9269 0.2346  -0.0811 -0.1227 49  ASN   A ND2 
166  N  N   . ILE   A 30  ? 0.8709 1.2783 0.9379 0.1854  -0.0259 -0.0482 50  ILE   A N   
167  C  CA  . ILE   A 30  ? 0.8185 1.2567 0.9204 0.1628  -0.0151 -0.0273 50  ILE   A CA  
168  C  C   . ILE   A 30  ? 0.8706 1.3678 0.9896 0.1690  0.0082  -0.0171 50  ILE   A C   
169  O  O   . ILE   A 30  ? 0.9275 1.4466 1.0664 0.1485  0.0199  0.0022  50  ILE   A O   
170  C  CB  . ILE   A 30  ? 0.7822 1.2137 0.9116 0.1562  -0.0258 -0.0258 50  ILE   A CB  
171  C  CG1 . ILE   A 30  ? 0.8211 1.2824 0.9671 0.1811  -0.0250 -0.0360 50  ILE   A CG1 
172  C  CG2 . ILE   A 30  ? 0.8480 1.2202 0.9583 0.1489  -0.0442 -0.0312 50  ILE   A CG2 
173  C  CD1 . ILE   A 30  ? 0.9294 1.4119 1.1151 0.1730  -0.0306 -0.0291 50  ILE   A CD1 
174  N  N   . LEU   A 31  ? 0.9321 1.4551 1.0444 0.1975  0.0169  -0.0285 51  LEU   A N   
175  C  CA  . LEU   A 31  ? 0.8833 1.4666 1.0134 0.2048  0.0438  -0.0165 51  LEU   A CA  
176  C  C   . LEU   A 31  ? 0.9433 1.5299 1.0479 0.1955  0.0582  -0.0024 51  LEU   A C   
177  O  O   . LEU   A 31  ? 0.8912 1.5238 1.0158 0.1905  0.0825  0.0165  51  LEU   A O   
178  C  CB  . LEU   A 31  ? 0.7624 1.3689 0.8809 0.2424  0.0522  -0.0332 51  LEU   A CB  
179  C  CG  . LEU   A 31  ? 0.8208 1.4409 0.9718 0.2581  0.0431  -0.0443 51  LEU   A CG  
180  C  CD1 . LEU   A 31  ? 0.7817 1.4338 0.9227 0.2981  0.0578  -0.0580 51  LEU   A CD1 
181  C  CD2 . LEU   A 31  ? 0.7517 1.4140 0.9654 0.2360  0.0467  -0.0266 51  LEU   A CD2 
182  N  N   . SER   A 32  ? 0.8929 1.4324 0.9562 0.1926  0.0434  -0.0099 52  SER   A N   
183  C  CA  . SER   A 32  ? 1.0478 1.5847 1.0837 0.1848  0.0517  0.0029  52  SER   A CA  
184  C  C   . SER   A 32  ? 1.0745 1.6113 1.1383 0.1520  0.0541  0.0265  52  SER   A C   
185  O  O   . SER   A 32  ? 1.0722 1.6050 1.1156 0.1446  0.0601  0.0398  52  SER   A O   
186  C  CB  . SER   A 32  ? 0.9683 1.4562 0.9562 0.1933  0.0301  -0.0153 52  SER   A CB  
187  O  OG  . SER   A 32  ? 0.9527 1.4355 0.9078 0.2254  0.0272  -0.0385 52  SER   A OG  
188  N  N   . TYR   A 33  ? 0.9757 1.5132 1.0814 0.1342  0.0479  0.0310  53  TYR   A N   
189  C  CA  . TYR   A 33  ? 1.0585 1.5955 1.1909 0.1052  0.0506  0.0517  53  TYR   A CA  
190  C  C   . TYR   A 33  ? 1.1167 1.7034 1.2836 0.0969  0.0744  0.0723  53  TYR   A C   
191  O  O   . TYR   A 33  ? 1.0760 1.6622 1.2700 0.0721  0.0761  0.0890  53  TYR   A O   
192  C  CB  . TYR   A 33  ? 1.0041 1.5146 1.1599 0.0911  0.0318  0.0461  53  TYR   A CB  
193  C  CG  . TYR   A 33  ? 1.0034 1.4624 1.1324 0.0895  0.0122  0.0349  53  TYR   A CG  
194  C  CD1 . TYR   A 33  ? 1.0892 1.5291 1.1850 0.0931  0.0095  0.0333  53  TYR   A CD1 
195  C  CD2 . TYR   A 33  ? 1.0647 1.4954 1.2029 0.0846  -0.0035 0.0270  53  TYR   A CD2 
196  C  CE1 . TYR   A 33  ? 1.0772 1.4754 1.1584 0.0893  -0.0081 0.0243  53  TYR   A CE1 
197  C  CE2 . TYR   A 33  ? 0.9905 1.3771 1.1090 0.0817  -0.0176 0.0200  53  TYR   A CE2 
198  C  CZ  . TYR   A 33  ? 0.9618 1.3344 1.0562 0.0829  -0.0196 0.0188  53  TYR   A CZ  
199  O  OH  . TYR   A 33  ? 0.8872 1.2211 0.9714 0.0778  -0.0335 0.0129  53  TYR   A OH  
200  N  N   . HIS   A 34  ? 1.0441 1.6728 1.2115 0.1172  0.0934  0.0716  54  HIS   A N   
201  C  CA  . HIS   A 34  ? 1.1073 1.7887 1.3129 0.1086  0.1198  0.0940  54  HIS   A CA  
202  C  C   . HIS   A 34  ? 1.1553 1.8310 1.3458 0.0923  0.1344  0.1191  54  HIS   A C   
203  O  O   . HIS   A 34  ? 1.1981 1.8995 1.4281 0.0712  0.1497  0.1421  54  HIS   A O   
204  C  CB  . HIS   A 34  ? 1.1576 1.8856 1.3604 0.1383  0.1412  0.0888  54  HIS   A CB  
205  C  CG  . HIS   A 34  ? 1.2753 1.9915 1.4135 0.1630  0.1509  0.0840  54  HIS   A CG  
206  N  ND1 . HIS   A 34  ? 1.2824 1.9543 1.3707 0.1821  0.1291  0.0584  54  HIS   A ND1 
207  C  CD2 . HIS   A 34  ? 1.3001 2.0408 1.4130 0.1721  0.1788  0.1016  54  HIS   A CD2 
208  C  CE1 . HIS   A 34  ? 1.3337 2.0030 1.3683 0.2024  0.1401  0.0577  54  HIS   A CE1 
209  N  NE2 . HIS   A 34  ? 1.3021 2.0125 1.3470 0.1982  0.1711  0.0842  54  HIS   A NE2 
210  N  N   . LYS   A 35  ? 1.1426 1.7836 1.2778 0.1015  0.1284  0.1154  55  LYS   A N   
211  C  CA  . LYS   A 35  ? 1.1539 1.7818 1.2683 0.0891  0.1374  0.1383  55  LYS   A CA  
212  C  C   . LYS   A 35  ? 1.1683 1.7487 1.2825 0.0686  0.1144  0.1383  55  LYS   A C   
213  O  O   . LYS   A 35  ? 1.2035 1.7642 1.2936 0.0625  0.1158  0.1531  55  LYS   A O   
214  C  CB  . LYS   A 35  ? 1.1623 1.7864 1.2139 0.1154  0.1452  0.1356  55  LYS   A CB  
215  C  CG  . LYS   A 35  ? 1.3127 1.9866 1.3596 0.1341  0.1784  0.1466  55  LYS   A CG  
216  C  CD  . LYS   A 35  ? 1.4140 2.0803 1.3903 0.1685  0.1811  0.1337  55  LYS   A CD  
217  C  CE  . LYS   A 35  ? 1.4802 2.1987 1.4511 0.1905  0.2181  0.1446  55  LYS   A CE  
218  N  NZ  . LYS   A 35  ? 1.5619 2.2708 1.4588 0.2295  0.2193  0.1262  55  LYS   A NZ  
219  N  N   . GLY   A 36  ? 1.1993 1.7612 1.3379 0.0600  0.0941  0.1230  56  GLY   A N   
220  C  CA  . GLY   A 36  ? 1.2165 1.7368 1.3579 0.0420  0.0760  0.1236  56  GLY   A CA  
221  C  C   . GLY   A 36  ? 1.2208 1.7046 1.3272 0.0530  0.0559  0.1057  56  GLY   A C   
222  O  O   . GLY   A 36  ? 1.1910 1.6753 1.2627 0.0726  0.0546  0.0955  56  GLY   A O   
223  N  N   . PHE   A 37  ? 1.2441 1.6953 1.3611 0.0399  0.0398  0.1015  57  PHE   A N   
224  C  CA  . PHE   A 37  ? 1.1806 1.5987 1.2748 0.0454  0.0220  0.0882  57  PHE   A CA  
225  C  C   . PHE   A 37  ? 1.1542 1.5677 1.2169 0.0522  0.0219  0.0948  57  PHE   A C   
226  O  O   . PHE   A 37  ? 1.1620 1.5638 1.1996 0.0652  0.0090  0.0801  57  PHE   A O   
227  C  CB  . PHE   A 37  ? 1.2076 1.5954 1.3188 0.0294  0.0115  0.0897  57  PHE   A CB  
228  C  CG  . PHE   A 37  ? 1.2053 1.5906 1.3398 0.0242  0.0076  0.0826  57  PHE   A CG  
229  C  CD1 . PHE   A 37  ? 1.1988 1.5710 1.3286 0.0339  -0.0038 0.0649  57  PHE   A CD1 
230  C  CD2 . PHE   A 37  ? 1.3700 1.7618 1.5297 0.0097  0.0128  0.0934  57  PHE   A CD2 
231  C  CE1 . PHE   A 37  ? 1.2807 1.6482 1.4269 0.0316  -0.0092 0.0593  57  PHE   A CE1 
232  C  CE2 . PHE   A 37  ? 1.5179 1.9063 1.6960 0.0064  0.0050  0.0854  57  PHE   A CE2 
233  C  CZ  . PHE   A 37  ? 1.4925 1.8692 1.6620 0.0185  -0.0057 0.0688  57  PHE   A CZ  
234  N  N   . CYS   A 38  ? 1.1064 1.5266 1.1695 0.0437  0.0341  0.1170  58  CYS   A N   
235  C  CA  . CYS   A 38  ? 1.0895 1.4993 1.1229 0.0493  0.0306  0.1258  58  CYS   A CA  
236  C  C   . CYS   A 38  ? 1.0854 1.5125 1.0792 0.0709  0.0358  0.1218  58  CYS   A C   
237  O  O   . CYS   A 38  ? 1.0760 1.4896 1.0394 0.0836  0.0197  0.1104  58  CYS   A O   
238  C  CB  . CYS   A 38  ? 1.0994 1.5057 1.1427 0.0349  0.0422  0.1521  58  CYS   A CB  
239  S  SG  . CYS   A 38  ? 1.2022 1.5806 1.2817 0.0138  0.0343  0.1545  58  CYS   A SG  
240  N  N   . MET   A 39  ? 1.0815 1.5393 1.0754 0.0760  0.0582  0.1310  59  MET   A N   
241  C  CA  . MET   A 39  ? 1.1057 1.5807 1.0567 0.1005  0.0670  0.1269  59  MET   A CA  
242  C  C   . MET   A 39  ? 1.1213 1.5856 1.0530 0.1187  0.0482  0.0953  59  MET   A C   
243  O  O   . MET   A 39  ? 1.1558 1.6110 1.0415 0.1384  0.0383  0.0840  59  MET   A O   
244  C  CB  . MET   A 39  ? 1.1141 1.6295 1.0789 0.1025  0.0978  0.1421  59  MET   A CB  
245  C  CG  . MET   A 39  ? 1.2713 1.7957 1.2541 0.0836  0.1181  0.1757  59  MET   A CG  
246  S  SD  . MET   A 39  ? 1.6531 2.1731 1.5757 0.0986  0.1305  0.1983  59  MET   A SD  
247  C  CE  . MET   A 39  ? 1.3654 1.9244 1.2541 0.1290  0.1545  0.1920  59  MET   A CE  
248  N  N   . PHE   A 40  ? 1.0513 1.5125 1.0154 0.1128  0.0410  0.0803  60  PHE   A N   
249  C  CA  . PHE   A 40  ? 0.9658 1.4097 0.9147 0.1281  0.0222  0.0514  60  PHE   A CA  
250  C  C   . PHE   A 40  ? 1.0998 1.5075 1.0351 0.1242  -0.0052 0.0403  60  PHE   A C   
251  O  O   . PHE   A 40  ? 1.0781 1.4695 0.9832 0.1403  -0.0222 0.0190  60  PHE   A O   
252  C  CB  . PHE   A 40  ? 1.0988 1.5443 1.0858 0.1218  0.0208  0.0422  60  PHE   A CB  
253  C  CG  . PHE   A 40  ? 1.0572 1.4746 1.0335 0.1328  -0.0005 0.0154  60  PHE   A CG  
254  C  CD1 . PHE   A 40  ? 1.0338 1.4531 0.9777 0.1594  -0.0022 -0.0039 60  PHE   A CD1 
255  C  CD2 . PHE   A 40  ? 1.0674 1.4540 1.0649 0.1174  -0.0177 0.0100  60  PHE   A CD2 
256  C  CE1 . PHE   A 40  ? 1.0156 1.4027 0.9500 0.1687  -0.0232 -0.0286 60  PHE   A CE1 
257  C  CE2 . PHE   A 40  ? 1.0393 1.3964 1.0287 0.1255  -0.0361 -0.0117 60  PHE   A CE2 
258  C  CZ  . PHE   A 40  ? 0.9880 1.3435 0.9467 0.1503  -0.0402 -0.0314 60  PHE   A CZ  
259  N  N   . ASP   A 41  ? 1.0593 1.4543 1.0187 0.1035  -0.0103 0.0538  61  ASP   A N   
260  C  CA  . ASP   A 41  ? 1.0390 1.4074 0.9948 0.0991  -0.0342 0.0462  61  ASP   A CA  
261  C  C   . ASP   A 41  ? 1.0747 1.4434 0.9878 0.1142  -0.0430 0.0457  61  ASP   A C   
262  O  O   . ASP   A 41  ? 1.0296 1.3807 0.9255 0.1222  -0.0672 0.0267  61  ASP   A O   
263  C  CB  . ASP   A 41  ? 1.0346 1.3939 1.0246 0.0775  -0.0335 0.0627  61  ASP   A CB  
264  C  CG  . ASP   A 41  ? 0.9524 1.2988 0.9762 0.0649  -0.0352 0.0566  61  ASP   A CG  
265  O  OD1 . ASP   A 41  ? 0.9534 1.2942 0.9753 0.0721  -0.0407 0.0392  61  ASP   A OD1 
266  O  OD2 . ASP   A 41  ? 0.9930 1.3320 1.0413 0.0498  -0.0312 0.0691  61  ASP   A OD2 
267  N  N   . MET   A 42  ? 1.0995 1.4860 0.9941 0.1182  -0.0248 0.0671  62  MET   A N   
268  C  CA  . MET   A 42  ? 1.1336 1.5185 0.9806 0.1349  -0.0328 0.0695  62  MET   A CA  
269  C  C   . MET   A 42  ? 1.1149 1.5011 0.9149 0.1612  -0.0377 0.0474  62  MET   A C   
270  O  O   . MET   A 42  ? 1.0726 1.4430 0.8364 0.1752  -0.0620 0.0321  62  MET   A O   
271  C  CB  . MET   A 42  ? 1.0917 1.4921 0.9273 0.1334  -0.0086 0.1010  62  MET   A CB  
272  C  CG  . MET   A 42  ? 1.0988 1.4922 0.9754 0.1100  -0.0045 0.1220  62  MET   A CG  
273  S  SD  . MET   A 42  ? 1.3434 1.7426 1.1980 0.1101  0.0169  0.1590  62  MET   A SD  
274  C  CE  . MET   A 42  ? 0.9657 1.3531 0.7600 0.1350  -0.0068 0.1532  62  MET   A CE  
275  N  N   . GLU   A 43  ? 1.1315 1.5364 0.9316 0.1697  -0.0162 0.0443  63  GLU   A N   
276  C  CA  . GLU   A 43  ? 1.0880 1.4930 0.8422 0.1983  -0.0186 0.0217  63  GLU   A CA  
277  C  C   . GLU   A 43  ? 1.2212 1.5932 0.9734 0.2014  -0.0529 -0.0110 63  GLU   A C   
278  O  O   . GLU   A 43  ? 1.2077 1.5633 0.9111 0.2234  -0.0711 -0.0324 63  GLU   A O   
279  C  CB  . GLU   A 43  ? 1.2129 1.6480 0.9803 0.2062  0.0112  0.0247  63  GLU   A CB  
280  C  CG  . GLU   A 43  ? 1.3831 1.8539 1.1490 0.2058  0.0471  0.0564  63  GLU   A CG  
281  C  CD  . GLU   A 43  ? 1.6190 2.1260 1.4198 0.2065  0.0750  0.0615  63  GLU   A CD  
282  O  OE1 . GLU   A 43  ? 1.5217 2.0238 1.3474 0.2075  0.0648  0.0409  63  GLU   A OE1 
283  O  OE2 . GLU   A 43  ? 1.7542 2.2950 1.5598 0.2060  0.1067  0.0872  63  GLU   A OE2 
284  N  N   . CYS   A 44  ? 1.1822 1.5413 0.9853 0.1797  -0.0623 -0.0149 64  CYS   A N   
285  C  CA  . CYS   A 44  ? 1.1191 1.4446 0.9268 0.1783  -0.0933 -0.0419 64  CYS   A CA  
286  C  C   . CYS   A 44  ? 1.0823 1.3898 0.8849 0.1712  -0.1221 -0.0452 64  CYS   A C   
287  O  O   . CYS   A 44  ? 1.1359 1.4182 0.9191 0.1794  -0.1512 -0.0703 64  CYS   A O   
288  C  CB  . CYS   A 44  ? 1.0229 1.3396 0.8835 0.1579  -0.0916 -0.0411 64  CYS   A CB  
289  S  SG  . CYS   A 44  ? 1.0780 1.4070 0.9442 0.1713  -0.0719 -0.0488 64  CYS   A SG  
290  N  N   . HIS   A 45  ? 1.1186 1.4384 0.9408 0.1565  -0.1163 -0.0209 65  HIS   A N   
291  C  CA  . HIS   A 45  ? 1.1107 1.4202 0.9311 0.1524  -0.1432 -0.0219 65  HIS   A CA  
292  C  C   . HIS   A 45  ? 1.1704 1.4746 0.9268 0.1788  -0.1601 -0.0360 65  HIS   A C   
293  O  O   . HIS   A 45  ? 1.2819 1.5667 1.0293 0.1820  -0.1951 -0.0569 65  HIS   A O   
294  C  CB  . HIS   A 45  ? 1.0837 1.4083 0.9287 0.1382  -0.1298 0.0085  65  HIS   A CB  
295  C  CG  . HIS   A 45  ? 1.0739 1.3921 0.9319 0.1324  -0.1568 0.0094  65  HIS   A CG  
296  N  ND1 . HIS   A 45  ? 1.0457 1.3478 0.9145 0.1304  -0.1905 -0.0141 65  HIS   A ND1 
297  C  CD2 . HIS   A 45  ? 1.0924 1.4190 0.9582 0.1287  -0.1561 0.0311  65  HIS   A CD2 
298  C  CE1 . HIS   A 45  ? 1.0476 1.3539 0.9343 0.1253  -0.2094 -0.0070 65  HIS   A CE1 
299  N  NE2 . HIS   A 45  ? 1.0758 1.3962 0.9590 0.1258  -0.1890 0.0202  65  HIS   A NE2 
300  N  N   . LYS   A 46  ? 1.2092 1.5304 0.9202 0.1983  -0.1356 -0.0248 66  LYS   A N   
301  C  CA  . LYS   A 46  ? 1.2810 1.5969 0.9196 0.2280  -0.1465 -0.0363 66  LYS   A CA  
302  C  C   . LYS   A 46  ? 1.3051 1.5972 0.9140 0.2458  -0.1677 -0.0738 66  LYS   A C   
303  O  O   . LYS   A 46  ? 1.3834 1.6518 0.9633 0.2556  -0.2046 -0.0969 66  LYS   A O   
304  C  CB  . LYS   A 46  ? 1.3341 1.6760 0.9358 0.2437  -0.1074 -0.0121 66  LYS   A CB  
305  C  CG  . LYS   A 46  ? 1.3696 1.7078 0.8870 0.2796  -0.1091 -0.0223 66  LYS   A CG  
306  C  CD  . LYS   A 46  ? 1.5997 1.9684 1.0923 0.2916  -0.0626 0.0058  66  LYS   A CD  
307  C  CE  . LYS   A 46  ? 1.5838 1.9499 0.9860 0.3307  -0.0586 -0.0016 66  LYS   A CE  
308  N  NZ  . LYS   A 46  ? 1.6668 2.0149 1.0210 0.3406  -0.0853 0.0028  66  LYS   A NZ  
309  N  N   . LYS   A 47  ? 1.3137 1.6100 0.9309 0.2506  -0.1471 -0.0812 67  LYS   A N   
310  C  CA  . LYS   A 47  ? 1.3028 1.5751 0.8833 0.2736  -0.1618 -0.1158 67  LYS   A CA  
311  C  C   . LYS   A 47  ? 1.3442 1.5786 0.9534 0.2591  -0.2015 -0.1426 67  LYS   A C   
312  O  O   . LYS   A 47  ? 1.2956 1.5001 0.8689 0.2781  -0.2226 -0.1745 67  LYS   A O   
313  C  CB  . LYS   A 47  ? 1.3995 1.6893 0.9897 0.2829  -0.1287 -0.1145 67  LYS   A CB  
314  C  CG  . LYS   A 47  ? 1.4517 1.7824 1.0187 0.2981  -0.0865 -0.0896 67  LYS   A CG  
315  C  CD  . LYS   A 47  ? 1.5215 1.8731 1.1123 0.3052  -0.0585 -0.0907 67  LYS   A CD  
316  C  CE  . LYS   A 47  ? 1.6908 2.0905 1.2791 0.3126  -0.0138 -0.0611 67  LYS   A CE  
317  N  NZ  . LYS   A 47  ? 1.6921 2.1187 1.3158 0.3175  0.0110  -0.0616 67  LYS   A NZ  
318  N  N   . TYR   A 48  ? 1.3584 1.5917 1.0309 0.2267  -0.2110 -0.1304 68  TYR   A N   
319  C  CA  . TYR   A 48  ? 1.2963 1.4966 1.0059 0.2097  -0.2406 -0.1513 68  TYR   A CA  
320  C  C   . TYR   A 48  ? 1.3211 1.5146 1.0636 0.1887  -0.2725 -0.1504 68  TYR   A C   
321  O  O   . TYR   A 48  ? 1.3356 1.4986 1.0889 0.1822  -0.3073 -0.1745 68  TYR   A O   
322  C  CB  . TYR   A 48  ? 1.2250 1.4276 0.9883 0.1908  -0.2188 -0.1402 68  TYR   A CB  
323  C  CG  . TYR   A 48  ? 1.2611 1.4686 1.0003 0.2121  -0.1946 -0.1465 68  TYR   A CG  
324  C  CD1 . TYR   A 48  ? 1.2690 1.4462 0.9695 0.2353  -0.2104 -0.1779 68  TYR   A CD1 
325  C  CD2 . TYR   A 48  ? 1.1935 1.4360 0.9508 0.2099  -0.1576 -0.1220 68  TYR   A CD2 
326  C  CE1 . TYR   A 48  ? 1.1669 1.3517 0.8478 0.2582  -0.1879 -0.1839 68  TYR   A CE1 
327  C  CE2 . TYR   A 48  ? 1.1350 1.3884 0.8779 0.2299  -0.1363 -0.1274 68  TYR   A CE2 
328  C  CZ  . TYR   A 48  ? 1.2232 1.4494 0.9282 0.2553  -0.1505 -0.1580 68  TYR   A CZ  
329  O  OH  . TYR   A 48  ? 1.1419 1.3820 0.8351 0.2784  -0.1287 -0.1636 68  TYR   A OH  
330  N  N   . GLY   A 49  ? 1.3008 1.5216 1.0634 0.1778  -0.2621 -0.1232 69  GLY   A N   
331  C  CA  . GLY   A 49  ? 1.3013 1.5226 1.0940 0.1630  -0.2919 -0.1215 69  GLY   A CA  
332  C  C   . GLY   A 49  ? 1.2065 1.4370 1.0770 0.1314  -0.2829 -0.1026 69  GLY   A C   
333  O  O   . GLY   A 49  ? 1.1714 1.4210 1.0615 0.1236  -0.2500 -0.0774 69  GLY   A O   
334  N  N   . LYS   A 50  ? 1.2378 1.4541 1.1529 0.1133  -0.3124 -0.1150 70  LYS   A N   
335  C  CA  . LYS   A 50  ? 1.2102 1.4400 1.1973 0.0861  -0.3054 -0.0953 70  LYS   A CA  
336  C  C   . LYS   A 50  ? 1.0888 1.3079 1.1100 0.0704  -0.2802 -0.0883 70  LYS   A C   
337  O  O   . LYS   A 50  ? 0.9610 1.1954 1.0223 0.0555  -0.2579 -0.0651 70  LYS   A O   
338  C  CB  . LYS   A 50  ? 1.1230 1.3483 1.1524 0.0717  -0.3448 -0.1080 70  LYS   A CB  
339  C  CG  . LYS   A 50  ? 1.3668 1.5574 1.4128 0.0609  -0.3675 -0.1333 70  LYS   A CG  
340  C  CD  . LYS   A 50  ? 1.4596 1.6541 1.5784 0.0348  -0.3936 -0.1342 70  LYS   A CD  
341  C  CE  . LYS   A 50  ? 1.4754 1.6344 1.6263 0.0161  -0.4021 -0.1480 70  LYS   A CE  
342  N  NZ  . LYS   A 50  ? 1.3327 1.4507 1.4267 0.0331  -0.4257 -0.1809 70  LYS   A NZ  
343  N  N   . VAL   A 51  ? 1.0903 1.2806 1.0930 0.0755  -0.2844 -0.1082 71  VAL   A N   
344  C  CA  A VAL   A 51  ? 1.1099 1.2845 1.1403 0.0629  -0.2652 -0.1031 71  VAL   A CA  
345  C  CA  B VAL   A 51  ? 1.0720 1.2470 1.1022 0.0630  -0.2647 -0.1028 71  VAL   A CA  
346  C  C   . VAL   A 51  ? 1.1414 1.2998 1.1241 0.0842  -0.2555 -0.1177 71  VAL   A C   
347  O  O   . VAL   A 51  ? 1.1394 1.2811 1.0783 0.1032  -0.2753 -0.1419 71  VAL   A O   
348  C  CB  A VAL   A 51  ? 1.1332 1.2824 1.2126 0.0403  -0.2869 -0.1116 71  VAL   A CB  
349  C  CB  B VAL   A 51  ? 1.0906 1.2403 1.1708 0.0400  -0.2850 -0.1104 71  VAL   A CB  
350  C  CG1 A VAL   A 51  ? 1.1215 1.2372 1.2023 0.0374  -0.2775 -0.1177 71  VAL   A CG1 
351  C  CG1 B VAL   A 51  ? 1.1243 1.2984 1.2639 0.0182  -0.2832 -0.0896 71  VAL   A CG1 
352  C  CG2 A VAL   A 51  ? 1.1193 1.2916 1.2599 0.0174  -0.2787 -0.0879 71  VAL   A CG2 
353  C  CG2 B VAL   A 51  ? 1.1773 1.2988 1.2380 0.0460  -0.3252 -0.1416 71  VAL   A CG2 
354  N  N   . TRP   A 52  ? 1.0755 1.2391 1.0659 0.0829  -0.2259 -0.1039 72  TRP   A N   
355  C  CA  . TRP   A 52  ? 1.0816 1.2338 1.0380 0.1027  -0.2157 -0.1163 72  TRP   A CA  
356  C  C   . TRP   A 52  ? 1.0629 1.2130 1.0478 0.0925  -0.1929 -0.1014 72  TRP   A C   
357  O  O   . TRP   A 52  ? 0.9234 1.0886 0.9420 0.0749  -0.1783 -0.0792 72  TRP   A O   
358  C  CB  . TRP   A 52  ? 1.0873 1.2678 0.9971 0.1272  -0.2002 -0.1147 72  TRP   A CB  
359  C  CG  . TRP   A 52  ? 0.9129 1.1300 0.8377 0.1206  -0.1705 -0.0860 72  TRP   A CG  
360  C  CD1 . TRP   A 52  ? 0.9752 1.2086 0.9080 0.1225  -0.1436 -0.0739 72  TRP   A CD1 
361  C  CD2 . TRP   A 52  ? 1.0368 1.2765 0.9715 0.1114  -0.1671 -0.0665 72  TRP   A CD2 
362  N  NE1 . TRP   A 52  ? 0.9037 1.1656 0.8510 0.1129  -0.1243 -0.0488 72  TRP   A NE1 
363  C  CE2 . TRP   A 52  ? 0.9541 1.2186 0.9009 0.1069  -0.1372 -0.0434 72  TRP   A CE2 
364  C  CE3 . TRP   A 52  ? 1.0889 1.3293 1.0246 0.1072  -0.1885 -0.0668 72  TRP   A CE3 
365  C  CZ2 . TRP   A 52  ? 0.9610 1.2457 0.9178 0.0986  -0.1270 -0.0206 72  TRP   A CZ2 
366  C  CZ3 . TRP   A 52  ? 1.0573 1.3213 1.0030 0.1011  -0.1778 -0.0433 72  TRP   A CZ3 
367  C  CH2 . TRP   A 52  ? 1.0474 1.3307 1.0021 0.0969  -0.1466 -0.0204 72  TRP   A CH2 
368  N  N   . GLY   A 53  ? 1.0715 1.2007 1.0393 0.1062  -0.1913 -0.1150 73  GLY   A N   
369  C  CA  . GLY   A 53  ? 0.9351 1.0599 0.9228 0.1011  -0.1732 -0.1033 73  GLY   A CA  
370  C  C   . GLY   A 53  ? 0.9385 1.0840 0.9027 0.1237  -0.1547 -0.1049 73  GLY   A C   
371  O  O   . GLY   A 53  ? 1.0962 1.2508 1.0249 0.1466  -0.1563 -0.1194 73  GLY   A O   
372  N  N   . PHE   A 54  ? 0.9642 1.1193 0.9487 0.1185  -0.1370 -0.0899 74  PHE   A N   
373  C  CA  . PHE   A 54  ? 0.9183 1.0959 0.8927 0.1379  -0.1211 -0.0907 74  PHE   A CA  
374  C  C   . PHE   A 54  ? 0.8530 1.0179 0.8503 0.1302  -0.1153 -0.0810 74  PHE   A C   
375  O  O   . PHE   A 54  ? 0.8377 0.9740 0.8520 0.1121  -0.1216 -0.0739 74  PHE   A O   
376  C  CB  . PHE   A 54  ? 0.8799 1.1070 0.8524 0.1405  -0.1012 -0.0766 74  PHE   A CB  
377  C  CG  . PHE   A 54  ? 0.8933 1.1358 0.8943 0.1166  -0.0909 -0.0528 74  PHE   A CG  
378  C  CD1 . PHE   A 54  ? 0.8671 1.1044 0.8733 0.1017  -0.0986 -0.0461 74  PHE   A CD1 
379  C  CD2 . PHE   A 54  ? 0.8220 1.0839 0.8445 0.1107  -0.0751 -0.0383 74  PHE   A CD2 
380  C  CE1 . PHE   A 54  ? 0.8179 1.0671 0.8481 0.0832  -0.0886 -0.0253 74  PHE   A CE1 
381  C  CE2 . PHE   A 54  ? 0.8133 1.0837 0.8572 0.0907  -0.0670 -0.0188 74  PHE   A CE2 
382  C  CZ  . PHE   A 54  ? 0.7261 0.9892 0.7727 0.0780  -0.0725 -0.0122 74  PHE   A CZ  
383  N  N   . TYR   A 55  ? 0.8739 1.0618 0.8718 0.1452  -0.1033 -0.0800 75  TYR   A N   
384  C  CA  . TYR   A 55  ? 0.7893 0.9613 0.8004 0.1450  -0.1028 -0.0754 75  TYR   A CA  
385  C  C   . TYR   A 55  ? 0.8474 1.0622 0.8780 0.1437  -0.0865 -0.0612 75  TYR   A C   
386  O  O   . TYR   A 55  ? 0.9397 1.1906 0.9703 0.1609  -0.0776 -0.0654 75  TYR   A O   
387  C  CB  . TYR   A 55  ? 0.9407 1.0859 0.9332 0.1698  -0.1135 -0.0949 75  TYR   A CB  
388  C  CG  . TYR   A 55  ? 0.9535 1.0472 0.9291 0.1687  -0.1331 -0.1100 75  TYR   A CG  
389  C  CD1 . TYR   A 55  ? 0.9444 1.0363 0.8960 0.1801  -0.1421 -0.1279 75  TYR   A CD1 
390  C  CD2 . TYR   A 55  ? 0.9463 0.9912 0.9290 0.1561  -0.1433 -0.1061 75  TYR   A CD2 
391  C  CE1 . TYR   A 55  ? 1.0096 1.0522 0.9483 0.1775  -0.1642 -0.1439 75  TYR   A CE1 
392  C  CE2 . TYR   A 55  ? 1.0131 1.0100 0.9869 0.1517  -0.1622 -0.1190 75  TYR   A CE2 
393  C  CZ  . TYR   A 55  ? 1.1047 1.1003 1.0583 0.1616  -0.1744 -0.1391 75  TYR   A CZ  
394  O  OH  . TYR   A 55  ? 1.2706 1.2163 1.2179 0.1556  -0.1973 -0.1541 75  TYR   A OH  
395  N  N   . ASP   A 56  ? 0.8223 1.0332 0.8707 0.1237  -0.0827 -0.0447 76  ASP   A N   
396  C  CA  . ASP   A 56  ? 0.8527 1.0905 0.9197 0.1217  -0.0742 -0.0341 76  ASP   A CA  
397  C  C   . ASP   A 56  ? 0.8961 1.1136 0.9598 0.1368  -0.0833 -0.0413 76  ASP   A C   
398  O  O   . ASP   A 56  ? 0.8545 1.0340 0.9131 0.1301  -0.0899 -0.0365 76  ASP   A O   
399  C  CB  . ASP   A 56  ? 0.8323 1.0645 0.9116 0.0983  -0.0695 -0.0171 76  ASP   A CB  
400  C  CG  . ASP   A 56  ? 0.8624 1.1178 0.9470 0.0858  -0.0604 -0.0081 76  ASP   A CG  
401  O  OD1 . ASP   A 56  ? 0.8218 1.1064 0.9021 0.0948  -0.0547 -0.0118 76  ASP   A OD1 
402  O  OD2 . ASP   A 56  ? 1.0254 1.2689 1.1162 0.0690  -0.0580 0.0035  76  ASP   A OD2 
403  N  N   . GLY   A 57  ? 0.8923 1.1353 0.9578 0.1592  -0.0827 -0.0518 77  GLY   A N   
404  C  CA  . GLY   A 57  ? 0.7302 0.9508 0.7887 0.1792  -0.0939 -0.0612 77  GLY   A CA  
405  C  C   . GLY   A 57  ? 0.8945 1.0580 0.9267 0.1845  -0.1062 -0.0717 77  GLY   A C   
406  O  O   . GLY   A 57  ? 0.8734 1.0313 0.8910 0.1921  -0.1081 -0.0844 77  GLY   A O   
407  N  N   . GLN   A 58  ? 0.8969 1.0149 0.9215 0.1802  -0.1150 -0.0662 78  GLN   A N   
408  C  CA  . GLN   A 58  ? 0.9329 0.9918 0.9381 0.1786  -0.1258 -0.0717 78  GLN   A CA  
409  C  C   . GLN   A 58  ? 1.0258 1.0663 1.0366 0.1496  -0.1225 -0.0601 78  GLN   A C   
410  O  O   . GLN   A 58  ? 1.0726 1.0680 1.0756 0.1432  -0.1311 -0.0633 78  GLN   A O   
411  C  CB  . GLN   A 58  ? 1.1673 1.1825 1.1597 0.1900  -0.1352 -0.0688 78  GLN   A CB  
412  C  CG  . GLN   A 58  ? 1.2911 1.3189 1.2791 0.2225  -0.1421 -0.0814 78  GLN   A CG  
413  C  CD  . GLN   A 58  ? 1.4466 1.4475 1.4163 0.2438  -0.1514 -0.1021 78  GLN   A CD  
414  O  OE1 . GLN   A 58  ? 1.5281 1.4796 1.4837 0.2341  -0.1590 -0.1060 78  GLN   A OE1 
415  N  NE2 . GLN   A 58  ? 1.4487 1.4821 1.4199 0.2735  -0.1514 -0.1161 78  GLN   A NE2 
416  N  N   . GLN   A 59  ? 0.8104 0.8843 0.8371 0.1323  -0.1108 -0.0469 79  GLN   A N   
417  C  CA  . GLN   A 59  ? 0.8793 0.9411 0.9153 0.1072  -0.1059 -0.0341 79  GLN   A CA  
418  C  C   . GLN   A 59  ? 0.7481 0.8212 0.7878 0.1004  -0.1090 -0.0419 79  GLN   A C   
419  O  O   . GLN   A 59  ? 0.7696 0.8836 0.8122 0.1030  -0.1030 -0.0437 79  GLN   A O   
420  C  CB  . GLN   A 59  ? 0.7132 0.8020 0.7614 0.0951  -0.0936 -0.0181 79  GLN   A CB  
421  C  CG  . GLN   A 59  ? 0.7686 0.8552 0.8289 0.0729  -0.0860 -0.0054 79  GLN   A CG  
422  C  CD  . GLN   A 59  ? 0.8292 0.8708 0.8881 0.0629  -0.0867 0.0026  79  GLN   A CD  
423  O  OE1 . GLN   A 59  ? 0.9239 0.9410 0.9721 0.0647  -0.0830 0.0120  79  GLN   A OE1 
424  N  NE2 . GLN   A 59  ? 0.8981 0.9287 0.9681 0.0524  -0.0918 -0.0004 79  GLN   A NE2 
425  N  N   . PRO   A 60  ? 0.7730 0.8102 0.8130 0.0914  -0.1191 -0.0460 80  PRO   A N   
426  C  CA  . PRO   A 60  ? 0.9297 0.9769 0.9734 0.0847  -0.1267 -0.0546 80  PRO   A CA  
427  C  C   . PRO   A 60  ? 0.8641 0.9385 0.9286 0.0651  -0.1166 -0.0383 80  PRO   A C   
428  O  O   . PRO   A 60  ? 0.8031 0.8661 0.8840 0.0494  -0.1089 -0.0223 80  PRO   A O   
429  C  CB  . PRO   A 60  ? 0.8562 0.8531 0.9012 0.0777  -0.1430 -0.0626 80  PRO   A CB  
430  C  CG  . PRO   A 60  ? 0.8212 0.7869 0.8722 0.0700  -0.1356 -0.0465 80  PRO   A CG  
431  C  CD  . PRO   A 60  ? 0.8506 0.8348 0.8878 0.0872  -0.1257 -0.0430 80  PRO   A CD  
432  N  N   . VAL   A 61  ? 0.8971 1.0065 0.9581 0.0684  -0.1154 -0.0418 81  VAL   A N   
433  C  CA  . VAL   A 61  ? 0.8455 0.9797 0.9233 0.0535  -0.1083 -0.0279 81  VAL   A CA  
434  C  C   . VAL   A 61  ? 0.8998 1.0364 0.9750 0.0523  -0.1240 -0.0388 81  VAL   A C   
435  O  O   . VAL   A 61  ? 0.9486 1.0904 0.9988 0.0688  -0.1323 -0.0550 81  VAL   A O   
436  C  CB  . VAL   A 61  ? 0.7429 0.9158 0.8179 0.0579  -0.0926 -0.0182 81  VAL   A CB  
437  C  CG1 . VAL   A 61  ? 0.8164 1.0067 0.9076 0.0433  -0.0855 -0.0025 81  VAL   A CG1 
438  C  CG2 . VAL   A 61  ? 0.7990 0.9697 0.8754 0.0614  -0.0832 -0.0122 81  VAL   A CG2 
439  N  N   . LEU   A 62  ? 0.8289 0.9627 0.9294 0.0346  -0.1284 -0.0304 82  LEU   A N   
440  C  CA  . LEU   A 62  ? 0.8254 0.9610 0.9293 0.0315  -0.1481 -0.0407 82  LEU   A CA  
441  C  C   . LEU   A 62  ? 0.8527 1.0225 0.9666 0.0266  -0.1419 -0.0270 82  LEU   A C   
442  O  O   . LEU   A 62  ? 0.9143 1.0904 1.0579 0.0123  -0.1323 -0.0101 82  LEU   A O   
443  C  CB  . LEU   A 62  ? 0.8941 0.9998 1.0276 0.0144  -0.1626 -0.0431 82  LEU   A CB  
444  C  CG  . LEU   A 62  ? 0.9390 1.0488 1.0852 0.0081  -0.1874 -0.0540 82  LEU   A CG  
445  C  CD1 . LEU   A 62  ? 1.0278 1.1279 1.1325 0.0278  -0.2078 -0.0800 82  LEU   A CD1 
446  C  CD2 . LEU   A 62  ? 0.9382 1.0239 1.1273 -0.0139 -0.1988 -0.0519 82  LEU   A CD2 
447  N  N   . ALA   A 63  ? 0.8810 1.0707 0.9674 0.0405  -0.1463 -0.0336 83  ALA   A N   
448  C  CA  . ALA   A 63  ? 0.8245 1.0419 0.9149 0.0384  -0.1429 -0.0205 83  ALA   A CA  
449  C  C   . ALA   A 63  ? 0.8371 1.0525 0.9442 0.0315  -0.1675 -0.0272 83  ALA   A C   
450  O  O   . ALA   A 63  ? 0.9283 1.1279 1.0206 0.0375  -0.1907 -0.0479 83  ALA   A O   
451  C  CB  . ALA   A 63  ? 0.8527 1.0914 0.9044 0.0564  -0.1354 -0.0214 83  ALA   A CB  
452  N  N   . ILE   A 64  ? 0.7892 1.0202 0.9284 0.0199  -0.1639 -0.0107 84  ILE   A N   
453  C  CA  . ILE   A 64  ? 0.7383 0.9767 0.9016 0.0136  -0.1874 -0.0143 84  ILE   A CA  
454  C  C   . ILE   A 64  ? 0.8345 1.1003 0.9908 0.0208  -0.1837 -0.0002 84  ILE   A C   
455  O  O   . ILE   A 64  ? 0.8582 1.1340 1.0135 0.0211  -0.1596 0.0180  84  ILE   A O   
456  C  CB  . ILE   A 64  ? 0.8303 1.0630 1.0503 -0.0073 -0.1878 -0.0069 84  ILE   A CB  
457  C  CG1 . ILE   A 64  ? 0.7882 1.0347 1.0309 -0.0134 -0.1595 0.0174  84  ILE   A CG1 
458  C  CG2 . ILE   A 64  ? 0.8436 1.0432 1.0667 -0.0143 -0.1898 -0.0178 84  ILE   A CG2 
459  C  CD1 . ILE   A 64  ? 0.9183 1.1666 1.2168 -0.0309 -0.1555 0.0282  84  ILE   A CD1 
460  N  N   . THR   A 65  ? 0.8451 1.1194 0.9938 0.0274  -0.2099 -0.0091 85  THR   A N   
461  C  CA  . THR   A 65  ? 0.9191 1.2154 1.0552 0.0372  -0.2100 0.0043  85  THR   A CA  
462  C  C   . THR   A 65  ? 0.8741 1.1852 1.0469 0.0326  -0.2361 0.0041  85  THR   A C   
463  O  O   . THR   A 65  ? 0.9342 1.2623 1.0978 0.0425  -0.2395 0.0156  85  THR   A O   
464  C  CB  . THR   A 65  ? 0.9213 1.2173 0.9930 0.0589  -0.2142 -0.0034 85  THR   A CB  
465  O  OG1 . THR   A 65  ? 0.9732 1.2555 1.0248 0.0661  -0.2455 -0.0296 85  THR   A OG1 
466  C  CG2 . THR   A 65  ? 0.8537 1.1449 0.8971 0.0642  -0.1855 0.0004  85  THR   A CG2 
467  N  N   . ASP   A 66  ? 0.8735 1.1793 1.0903 0.0177  -0.2549 -0.0074 86  ASP   A N   
468  C  CA  . ASP   A 66  ? 0.9089 1.2346 1.1710 0.0117  -0.2818 -0.0081 86  ASP   A CA  
469  C  C   . ASP   A 66  ? 0.9145 1.2618 1.2326 0.0010  -0.2598 0.0158  86  ASP   A C   
470  O  O   . ASP   A 66  ? 0.8412 1.1805 1.1896 -0.0134 -0.2380 0.0229  86  ASP   A O   
471  C  CB  . ASP   A 66  ? 1.0522 1.3639 1.3443 -0.0023 -0.3120 -0.0301 86  ASP   A CB  
472  C  CG  . ASP   A 66  ? 1.0208 1.3570 1.3639 -0.0090 -0.3456 -0.0337 86  ASP   A CG  
473  O  OD1 . ASP   A 66  ? 1.0212 1.3809 1.4310 -0.0235 -0.3353 -0.0171 86  ASP   A OD1 
474  O  OD2 . ASP   A 66  ? 1.1245 1.4579 1.4407 0.0018  -0.3827 -0.0533 86  ASP   A OD2 
475  N  N   . PRO   A 67  ? 0.9411 1.3137 1.2704 0.0102  -0.2640 0.0289  87  PRO   A N   
476  C  CA  . PRO   A 67  ? 0.8998 1.2911 1.2769 0.0047  -0.2400 0.0513  87  PRO   A CA  
477  C  C   . PRO   A 67  ? 0.8666 1.2694 1.3175 -0.0156 -0.2394 0.0527  87  PRO   A C   
478  O  O   . PRO   A 67  ? 0.8524 1.2571 1.3295 -0.0220 -0.2084 0.0687  87  PRO   A O   
479  C  CB  . PRO   A 67  ? 0.7115 1.1265 1.0873 0.0211  -0.2553 0.0602  87  PRO   A CB  
480  C  CG  . PRO   A 67  ? 0.8853 1.2970 1.2246 0.0311  -0.2933 0.0407  87  PRO   A CG  
481  C  CD  . PRO   A 67  ? 0.8714 1.2527 1.1611 0.0298  -0.2879 0.0252  87  PRO   A CD  
482  N  N   . ASP   A 68  ? 0.8472 1.2566 1.3321 -0.0261 -0.2725 0.0367  88  ASP   A N   
483  C  CA  . ASP   A 68  ? 0.8496 1.2684 1.4084 -0.0491 -0.2699 0.0398  88  ASP   A CA  
484  C  C   . ASP   A 68  ? 0.7195 1.1053 1.2654 -0.0610 -0.2424 0.0414  88  ASP   A C   
485  O  O   . ASP   A 68  ? 0.8028 1.1934 1.3894 -0.0724 -0.2147 0.0579  88  ASP   A O   
486  C  CB  . ASP   A 68  ? 0.9937 1.4200 1.5891 -0.0604 -0.3150 0.0197  88  ASP   A CB  
487  C  CG  . ASP   A 68  ? 1.0199 1.4886 1.6566 -0.0533 -0.3417 0.0224  88  ASP   A CG  
488  O  OD1 . ASP   A 68  ? 1.0941 1.5928 1.7657 -0.0481 -0.3199 0.0439  88  ASP   A OD1 
489  O  OD2 . ASP   A 68  ? 0.8207 1.2915 1.4533 -0.0510 -0.3860 0.0020  88  ASP   A OD2 
490  N  N   . MET   A 69  ? 0.8996 1.2514 1.3863 -0.0559 -0.2492 0.0249  89  MET   A N   
491  C  CA  . MET   A 69  ? 0.9609 1.2799 1.4287 -0.0629 -0.2253 0.0260  89  MET   A CA  
492  C  C   . MET   A 69  ? 0.7953 1.1145 1.2427 -0.0549 -0.1860 0.0459  89  MET   A C   
493  O  O   . MET   A 69  ? 0.8522 1.1573 1.3116 -0.0638 -0.1608 0.0565  89  MET   A O   
494  C  CB  . MET   A 69  ? 1.0044 1.2914 1.4116 -0.0538 -0.2418 0.0032  89  MET   A CB  
495  C  CG  . MET   A 69  ? 1.0326 1.2834 1.4447 -0.0671 -0.2427 -0.0065 89  MET   A CG  
496  S  SD  . MET   A 69  ? 1.1634 1.3790 1.5107 -0.0528 -0.2704 -0.0383 89  MET   A SD  
497  C  CE  . MET   A 69  ? 1.1528 1.3832 1.5205 -0.0544 -0.3190 -0.0577 89  MET   A CE  
498  N  N   . ILE   A 70  ? 0.8424 1.1745 1.2569 -0.0380 -0.1813 0.0516  90  ILE   A N   
499  C  CA  . ILE   A 70  ? 0.8056 1.1353 1.2014 -0.0309 -0.1481 0.0688  90  ILE   A CA  
500  C  C   . ILE   A 70  ? 0.8083 1.1553 1.2568 -0.0373 -0.1287 0.0870  90  ILE   A C   
501  O  O   . ILE   A 70  ? 0.7908 1.1249 1.2349 -0.0386 -0.1000 0.0982  90  ILE   A O   
502  C  CB  . ILE   A 70  ? 0.7654 1.1025 1.1183 -0.0133 -0.1496 0.0719  90  ILE   A CB  
503  C  CG1 . ILE   A 70  ? 0.7804 1.1004 1.0771 -0.0054 -0.1587 0.0569  90  ILE   A CG1 
504  C  CG2 . ILE   A 70  ? 0.7341 1.0688 1.0781 -0.0079 -0.1196 0.0899  90  ILE   A CG2 
505  C  CD1 . ILE   A 70  ? 0.8195 1.1463 1.0729 0.0108  -0.1574 0.0625  90  ILE   A CD1 
506  N  N   . LYS   A 71  ? 0.8472 1.2251 1.3460 -0.0397 -0.1443 0.0899  91  LYS   A N   
507  C  CA  . LYS   A 71  ? 0.7827 1.1827 1.3389 -0.0447 -0.1243 0.1073  91  LYS   A CA  
508  C  C   . LYS   A 71  ? 0.7644 1.1520 1.3525 -0.0635 -0.1101 0.1106  91  LYS   A C   
509  O  O   . LYS   A 71  ? 0.6716 1.0591 1.2756 -0.0643 -0.0783 0.1269  91  LYS   A O   
510  C  CB  . LYS   A 71  ? 0.7162 1.1571 1.3270 -0.0431 -0.1474 0.1088  91  LYS   A CB  
511  C  CG  . LYS   A 71  ? 0.7897 1.2616 1.4688 -0.0466 -0.1258 0.1272  91  LYS   A CG  
512  C  CD  . LYS   A 71  ? 0.8266 1.3444 1.5628 -0.0420 -0.1506 0.1286  91  LYS   A CD  
513  C  CE  . LYS   A 71  ? 0.8276 1.3806 1.6305 -0.0404 -0.1239 0.1486  91  LYS   A CE  
514  N  NZ  . LYS   A 71  ? 0.9661 1.5684 1.8278 -0.0324 -0.1484 0.1507  91  LYS   A NZ  
515  N  N   . THR   A 72  ? 0.7591 1.1320 1.3525 -0.0773 -0.1329 0.0955  92  THR   A N   
516  C  CA  . THR   A 72  ? 0.8318 1.1853 1.4509 -0.0959 -0.1204 0.0997  92  THR   A CA  
517  C  C   . THR   A 72  ? 0.9127 1.2316 1.4810 -0.0898 -0.0895 0.1068  92  THR   A C   
518  O  O   . THR   A 72  ? 0.8799 1.1931 1.4667 -0.0957 -0.0608 0.1234  92  THR   A O   
519  C  CB  . THR   A 72  ? 0.8592 1.1934 1.4819 -0.1092 -0.1543 0.0790  92  THR   A CB  
520  O  OG1 . THR   A 72  ? 0.8526 1.2153 1.5035 -0.1091 -0.1904 0.0670  92  THR   A OG1 
521  C  CG2 . THR   A 72  ? 0.7872 1.1082 1.4590 -0.1328 -0.1456 0.0870  92  THR   A CG2 
522  N  N   . VAL   A 73  ? 0.8247 1.1219 1.3287 -0.0769 -0.0949 0.0949  93  VAL   A N   
523  C  CA  . VAL   A 73  ? 0.8197 1.0858 1.2767 -0.0708 -0.0714 0.0990  93  VAL   A CA  
524  C  C   . VAL   A 73  ? 0.8820 1.1567 1.3326 -0.0604 -0.0423 0.1160  93  VAL   A C   
525  O  O   . VAL   A 73  ? 0.7607 1.0201 1.2096 -0.0618 -0.0167 0.1283  93  VAL   A O   
526  C  CB  . VAL   A 73  ? 0.8486 1.0969 1.2474 -0.0598 -0.0855 0.0819  93  VAL   A CB  
527  C  CG1 . VAL   A 73  ? 0.7648 0.9922 1.1198 -0.0505 -0.0628 0.0873  93  VAL   A CG1 
528  C  CG2 . VAL   A 73  ? 0.7680 0.9944 1.1635 -0.0674 -0.1083 0.0645  93  VAL   A CG2 
529  N  N   . LEU   A 74  ? 0.8823 1.1775 1.3250 -0.0484 -0.0461 0.1170  94  LEU   A N   
530  C  CA  . LEU   A 74  ? 0.7039 0.9978 1.1291 -0.0362 -0.0216 0.1295  94  LEU   A CA  
531  C  C   . LEU   A 74  ? 0.7302 1.0429 1.2019 -0.0366 -0.0008 0.1460  94  LEU   A C   
532  O  O   . LEU   A 74  ? 0.8073 1.1077 1.2617 -0.0276 0.0251  0.1561  94  LEU   A O   
533  C  CB  . LEU   A 74  ? 0.7004 1.0049 1.1017 -0.0234 -0.0320 0.1269  94  LEU   A CB  
534  C  CG  . LEU   A 74  ? 0.7629 1.0489 1.1110 -0.0189 -0.0401 0.1161  94  LEU   A CG  
535  C  CD1 . LEU   A 74  ? 0.7798 1.0733 1.1062 -0.0072 -0.0420 0.1204  94  LEU   A CD1 
536  C  CD2 . LEU   A 74  ? 0.6908 0.9477 1.0087 -0.0197 -0.0229 0.1161  94  LEU   A CD2 
537  N  N   . VAL   A 75  ? 0.7866 1.1297 1.3175 -0.0457 -0.0118 0.1485  95  VAL   A N   
538  C  CA  . VAL   A 75  ? 0.8628 1.2340 1.4459 -0.0437 0.0088  0.1654  95  VAL   A CA  
539  C  C   . VAL   A 75  ? 0.9439 1.3212 1.5781 -0.0627 0.0179  0.1735  95  VAL   A C   
540  O  O   . VAL   A 75  ? 1.0062 1.3736 1.6421 -0.0623 0.0502  0.1883  95  VAL   A O   
541  C  CB  . VAL   A 75  ? 0.8408 1.2524 1.4623 -0.0360 -0.0093 0.1658  95  VAL   A CB  
542  C  CG1 . VAL   A 75  ? 0.8737 1.3176 1.5499 -0.0296 0.0151  0.1836  95  VAL   A CG1 
543  C  CG2 . VAL   A 75  ? 0.7893 1.1898 1.3577 -0.0187 -0.0189 0.1599  95  VAL   A CG2 
544  N  N   . LYS   A 76  ? 0.9714 1.3625 1.6457 -0.0794 -0.0109 0.1642  96  LYS   A N   
545  C  CA  . LYS   A 76  ? 0.9855 1.3918 1.7281 -0.1004 -0.0053 0.1743  96  LYS   A CA  
546  C  C   . LYS   A 76  ? 0.9928 1.3580 1.7108 -0.1102 0.0174  0.1818  96  LYS   A C   
547  O  O   . LYS   A 76  ? 0.9237 1.2952 1.6746 -0.1161 0.0486  0.2022  96  LYS   A O   
548  C  CB  . LYS   A 76  ? 0.9925 1.4142 1.7763 -0.1168 -0.0476 0.1584  96  LYS   A CB  
549  C  CG  . LYS   A 76  ? 1.0273 1.4854 1.8258 -0.1046 -0.0750 0.1498  96  LYS   A CG  
550  C  CD  . LYS   A 76  ? 1.1527 1.6347 2.0104 -0.1219 -0.1151 0.1375  96  LYS   A CD  
551  C  CE  . LYS   A 76  ? 1.1727 1.6953 2.0497 -0.1073 -0.1409 0.1326  96  LYS   A CE  
552  N  NZ  . LYS   A 76  ? 1.1987 1.7519 2.1454 -0.1240 -0.1808 0.1221  96  LYS   A NZ  
553  N  N   . GLU   A 77  ? 0.9515 1.2748 1.6108 -0.1101 0.0033  0.1667  97  GLU   A N   
554  C  CA  . GLU   A 77  ? 0.8569 1.1373 1.4901 -0.1181 0.0184  0.1720  97  GLU   A CA  
555  C  C   . GLU   A 77  ? 0.8530 1.1021 1.4131 -0.0990 0.0406  0.1747  97  GLU   A C   
556  O  O   . GLU   A 77  ? 0.8958 1.1042 1.4152 -0.1000 0.0426  0.1720  97  GLU   A O   
557  C  CB  . GLU   A 77  ? 0.8863 1.1393 1.5097 -0.1306 -0.0146 0.1525  97  GLU   A CB  
558  C  CG  . GLU   A 77  ? 0.8835 1.1630 1.5726 -0.1487 -0.0456 0.1438  97  GLU   A CG  
559  C  CD  . GLU   A 77  ? 1.0297 1.3296 1.7979 -0.1702 -0.0288 0.1649  97  GLU   A CD  
560  O  OE1 . GLU   A 77  ? 1.0537 1.3227 1.8194 -0.1802 -0.0062 0.1793  97  GLU   A OE1 
561  O  OE2 . GLU   A 77  ? 0.9362 1.2840 1.7703 -0.1764 -0.0376 0.1684  97  GLU   A OE2 
562  N  N   . CYS   A 78  ? 0.8521 1.1174 1.3954 -0.0811 0.0552  0.1794  98  CYS   A N   
563  C  CA  . CYS   A 78  ? 0.8928 1.1281 1.3683 -0.0637 0.0711  0.1792  98  CYS   A CA  
564  C  C   . CYS   A 78  ? 0.8431 1.0495 1.3009 -0.0634 0.1015  0.1954  98  CYS   A C   
565  O  O   . CYS   A 78  ? 0.8093 0.9770 1.2171 -0.0603 0.1006  0.1909  98  CYS   A O   
566  C  CB  . CYS   A 78  ? 0.7443 0.9995 1.2114 -0.0460 0.0801  0.1816  98  CYS   A CB  
567  S  SG  . CYS   A 78  ? 0.7342 0.9524 1.1274 -0.0257 0.1019  0.1832  98  CYS   A SG  
568  N  N   . TYR   A 79  ? 0.9240 1.1500 1.4218 -0.0647 0.1295  0.2155  99  TYR   A N   
569  C  CA  . TYR   A 79  ? 1.0135 1.2120 1.4885 -0.0612 0.1631  0.2341  99  TYR   A CA  
570  C  C   . TYR   A 79  ? 0.9276 1.0956 1.4050 -0.0793 0.1577  0.2376  99  TYR   A C   
571  O  O   . TYR   A 79  ? 0.8515 0.9781 1.2786 -0.0728 0.1726  0.2449  99  TYR   A O   
572  C  CB  . TYR   A 79  ? 0.8833 1.1152 1.4079 -0.0589 0.1969  0.2566  99  TYR   A CB  
573  C  CG  . TYR   A 79  ? 1.0985 1.3481 1.6073 -0.0350 0.2098  0.2558  99  TYR   A CG  
574  C  CD1 . TYR   A 79  ? 1.0385 1.2535 1.4750 -0.0127 0.2276  0.2555  99  TYR   A CD1 
575  C  CD2 . TYR   A 79  ? 1.0130 1.3109 1.5782 -0.0336 0.2022  0.2547  99  TYR   A CD2 
576  C  CE1 . TYR   A 79  ? 1.0760 1.3003 1.4961 0.0095  0.2377  0.2532  99  TYR   A CE1 
577  C  CE2 . TYR   A 79  ? 1.1192 1.4281 1.6685 -0.0100 0.2137  0.2542  99  TYR   A CE2 
578  C  CZ  . TYR   A 79  ? 1.1306 1.4008 1.6071 0.0111  0.2317  0.2531  99  TYR   A CZ  
579  O  OH  . TYR   A 79  ? 1.0594 1.3338 1.5179 0.0348  0.2414  0.2509  99  TYR   A OH  
580  N  N   . SER   A 80  ? 0.8947 1.0788 1.4276 -0.1009 0.1344  0.2319  100 SER   A N   
581  C  CA  . SER   A 80  ? 0.9059 1.0588 1.4503 -0.1200 0.1303  0.2374  100 SER   A CA  
582  C  C   . SER   A 80  ? 1.0222 1.1315 1.5074 -0.1154 0.1041  0.2170  100 SER   A C   
583  O  O   . SER   A 80  ? 1.1445 1.2095 1.5948 -0.1152 0.1129  0.2245  100 SER   A O   
584  C  CB  . SER   A 80  ? 0.8625 1.0467 1.4924 -0.1460 0.1129  0.2376  100 SER   A CB  
585  O  OG  . SER   A 80  ? 0.9137 1.1303 1.5610 -0.1438 0.0801  0.2159  100 SER   A OG  
586  N  N   . VAL   A 81  ? 0.9184 1.0397 1.3905 -0.1096 0.0730  0.1925  101 VAL   A N   
587  C  CA  . VAL   A 81  ? 0.9647 1.0538 1.3946 -0.1064 0.0459  0.1716  101 VAL   A CA  
588  C  C   . VAL   A 81  ? 0.9192 1.0082 1.2917 -0.0846 0.0403  0.1577  101 VAL   A C   
589  O  O   . VAL   A 81  ? 0.9633 1.0196 1.2842 -0.0735 0.0406  0.1534  101 VAL   A O   
590  C  CB  . VAL   A 81  ? 0.9306 1.0303 1.3986 -0.1212 0.0109  0.1534  101 VAL   A CB  
591  C  CG1 . VAL   A 81  ? 1.0036 1.0614 1.4304 -0.1179 -0.0117 0.1350  101 VAL   A CG1 
592  C  CG2 . VAL   A 81  ? 0.8247 0.9380 1.3665 -0.1457 0.0144  0.1675  101 VAL   A CG2 
593  N  N   . PHE   A 82  ? 0.9082 1.0337 1.2916 -0.0787 0.0342  0.1513  102 PHE   A N   
594  C  CA  . PHE   A 82  ? 0.7466 0.8750 1.0850 -0.0624 0.0253  0.1379  102 PHE   A CA  
595  C  C   . PHE   A 82  ? 0.7746 0.9077 1.0933 -0.0493 0.0497  0.1495  102 PHE   A C   
596  O  O   . PHE   A 82  ? 0.9896 1.1489 1.3172 -0.0433 0.0498  0.1489  102 PHE   A O   
597  C  CB  . PHE   A 82  ? 0.8108 0.9695 1.1675 -0.0637 0.0000  0.1230  102 PHE   A CB  
598  C  CG  . PHE   A 82  ? 0.7913 0.9451 1.1705 -0.0760 -0.0254 0.1103  102 PHE   A CG  
599  C  CD1 . PHE   A 82  ? 0.7803 0.9096 1.1238 -0.0711 -0.0430 0.0931  102 PHE   A CD1 
600  C  CD2 . PHE   A 82  ? 0.8798 1.0531 1.3174 -0.0918 -0.0326 0.1147  102 PHE   A CD2 
601  C  CE1 . PHE   A 82  ? 0.8837 1.0022 1.2424 -0.0802 -0.0679 0.0789  102 PHE   A CE1 
602  C  CE2 . PHE   A 82  ? 0.8670 1.0309 1.3243 -0.1040 -0.0600 0.1005  102 PHE   A CE2 
603  C  CZ  . PHE   A 82  ? 0.9368 1.0701 1.3511 -0.0974 -0.0778 0.0818  102 PHE   A CZ  
604  N  N   . THR   A 83  ? 0.7958 0.8985 1.0824 -0.0431 0.0694  0.1596  103 THR   A N   
605  C  CA  . THR   A 83  ? 0.8251 0.9240 1.0863 -0.0289 0.0929  0.1696  103 THR   A CA  
606  C  C   . THR   A 83  ? 0.6768 0.7617 0.8859 -0.0148 0.0838  0.1569  103 THR   A C   
607  O  O   . THR   A 83  ? 0.7400 0.8304 0.9358 -0.0044 0.0924  0.1581  103 THR   A O   
608  C  CB  . THR   A 83  ? 0.9016 0.9728 1.1488 -0.0270 0.1198  0.1881  103 THR   A CB  
609  O  OG1 . THR   A 83  ? 0.9633 1.0488 1.2666 -0.0438 0.1290  0.2019  103 THR   A OG1 
610  C  CG2 . THR   A 83  ? 0.9077 0.9750 1.1275 -0.0097 0.1458  0.1979  103 THR   A CG2 
611  N  N   . ASN   A 84  ? 0.7020 0.7695 0.8848 -0.0142 0.0658  0.1445  104 ASN   A N   
612  C  CA  . ASN   A 84  ? 0.8187 0.8710 0.9556 -0.0019 0.0589  0.1349  104 ASN   A CA  
613  C  C   . ASN   A 84  ? 0.7037 0.7736 0.8422 -0.0034 0.0353  0.1182  104 ASN   A C   
614  O  O   . ASN   A 84  ? 0.7862 0.8675 0.9469 -0.0111 0.0220  0.1116  104 ASN   A O   
615  C  CB  . ASN   A 84  ? 0.7066 0.7208 0.8052 0.0050  0.0619  0.1377  104 ASN   A CB  
616  C  CG  . ASN   A 84  ? 0.8526 0.8477 0.9509 0.0048  0.0873  0.1573  104 ASN   A CG  
617  O  OD1 . ASN   A 84  ? 0.9400 0.9432 1.0436 0.0088  0.1073  0.1677  104 ASN   A OD1 
618  N  ND2 . ASN   A 84  ? 0.9089 0.8776 1.0010 0.0013  0.0880  0.1637  104 ASN   A ND2 
619  N  N   . ARG   A 85  ? 0.7704 0.8411 0.8843 0.0043  0.0305  0.1114  105 ARG   A N   
620  C  CA  . ARG   A 85  ? 0.6861 0.7736 0.7983 0.0044  0.0125  0.0982  105 ARG   A CA  
621  C  C   . ARG   A 85  ? 0.7944 0.8647 0.8847 0.0103  0.0021  0.0898  105 ARG   A C   
622  O  O   . ARG   A 85  ? 0.8732 0.9148 0.9454 0.0145  0.0076  0.0949  105 ARG   A O   
623  C  CB  . ARG   A 85  ? 0.7757 0.8720 0.8782 0.0075  0.0123  0.0966  105 ARG   A CB  
624  C  CG  . ARG   A 85  ? 0.8469 0.9517 0.9647 0.0062  0.0240  0.1059  105 ARG   A CG  
625  C  CD  . ARG   A 85  ? 0.8302 0.9406 0.9409 0.0076  0.0209  0.1041  105 ARG   A CD  
626  N  NE  . ARG   A 85  ? 0.8434 0.9678 0.9746 0.0069  0.0273  0.1120  105 ARG   A NE  
627  C  CZ  . ARG   A 85  ? 0.8879 1.0001 1.0156 0.0135  0.0406  0.1191  105 ARG   A CZ  
628  N  NH1 . ARG   A 85  ? 0.9162 0.9997 1.0157 0.0214  0.0496  0.1191  105 ARG   A NH1 
629  N  NH2 . ARG   A 85  ? 0.7864 0.9146 0.9366 0.0147  0.0445  0.1261  105 ARG   A NH2 
630  N  N   . ARG   A 86  ? 0.8729 0.9611 0.9643 0.0122  -0.0119 0.0781  106 ARG   A N   
631  C  CA  . ARG   A 86  ? 0.9455 1.0209 1.0215 0.0202  -0.0226 0.0694  106 ARG   A CA  
632  C  C   . ARG   A 86  ? 0.9427 1.0006 0.9910 0.0294  -0.0236 0.0695  106 ARG   A C   
633  O  O   . ARG   A 86  ? 0.8268 0.8930 0.8714 0.0288  -0.0223 0.0700  106 ARG   A O   
634  C  CB  . ARG   A 86  ? 0.9777 1.0802 1.0629 0.0230  -0.0349 0.0567  106 ARG   A CB  
635  C  CG  . ARG   A 86  ? 1.1113 1.2399 1.1974 0.0248  -0.0372 0.0534  106 ARG   A CG  
636  C  CD  . ARG   A 86  ? 1.1384 1.2886 1.2276 0.0331  -0.0468 0.0415  106 ARG   A CD  
637  N  NE  . ARG   A 86  ? 1.1970 1.3709 1.2978 0.0303  -0.0467 0.0388  106 ARG   A NE  
638  C  CZ  . ARG   A 86  ? 1.0436 1.2314 1.1426 0.0395  -0.0530 0.0278  106 ARG   A CZ  
639  N  NH1 . ARG   A 86  ? 0.9572 1.1394 1.0482 0.0522  -0.0596 0.0184  106 ARG   A NH1 
640  N  NH2 . ARG   A 86  ? 0.9350 1.1414 1.0372 0.0386  -0.0532 0.0257  106 ARG   A NH2 
641  N  N   . PRO   A 87  ? 1.0087 1.0383 1.0354 0.0383  -0.0275 0.0692  107 PRO   A N   
642  C  CA  . PRO   A 87  ? 1.0043 1.0121 0.9988 0.0489  -0.0302 0.0701  107 PRO   A CA  
643  C  C   . PRO   A 87  ? 1.0999 1.1316 1.0972 0.0523  -0.0440 0.0592  107 PRO   A C   
644  O  O   . PRO   A 87  ? 1.2055 1.2534 1.2107 0.0586  -0.0571 0.0494  107 PRO   A O   
645  C  CB  . PRO   A 87  ? 1.0969 1.0734 1.0705 0.0595  -0.0357 0.0709  107 PRO   A CB  
646  C  CG  . PRO   A 87  ? 1.1815 1.1699 1.1794 0.0556  -0.0414 0.0643  107 PRO   A CG  
647  C  CD  . PRO   A 87  ? 1.0514 1.0633 1.0791 0.0403  -0.0318 0.0677  107 PRO   A CD  
648  N  N   . PHE   A 88  ? 1.2892 1.3227 1.2822 0.0485  -0.0409 0.0609  108 PHE   A N   
649  C  CA  . PHE   A 88  ? 1.3328 1.3866 1.3334 0.0476  -0.0542 0.0521  108 PHE   A CA  
650  C  C   . PHE   A 88  ? 1.5554 1.5822 1.5227 0.0592  -0.0667 0.0477  108 PHE   A C   
651  O  O   . PHE   A 88  ? 1.5684 1.5600 1.5019 0.0650  -0.0591 0.0535  108 PHE   A O   
652  C  CB  . PHE   A 88  ? 1.4165 1.4836 1.4325 0.0357  -0.0468 0.0557  108 PHE   A CB  
653  C  CG  . PHE   A 88  ? 1.4750 1.5543 1.4986 0.0317  -0.0600 0.0486  108 PHE   A CG  
654  C  CD1 . PHE   A 88  ? 1.4939 1.6075 1.5437 0.0298  -0.0716 0.0418  108 PHE   A CD1 
655  C  CD2 . PHE   A 88  ? 1.3803 1.4369 1.3871 0.0300  -0.0608 0.0487  108 PHE   A CD2 
656  C  CE1 . PHE   A 88  ? 1.6252 1.7534 1.6909 0.0229  -0.0839 0.0368  108 PHE   A CE1 
657  C  CE2 . PHE   A 88  ? 1.5772 1.6419 1.5948 0.0236  -0.0758 0.0414  108 PHE   A CE2 
658  C  CZ  . PHE   A 88  ? 1.6527 1.7550 1.7032 0.0183  -0.0875 0.0363  108 PHE   A CZ  
659  N  N   . GLY   A 89  ? 1.4370 1.4819 1.4136 0.0641  -0.0858 0.0374  109 GLY   A N   
660  C  CA  . GLY   A 89  ? 1.4500 1.4741 1.3985 0.0760  -0.1040 0.0306  109 GLY   A CA  
661  C  C   . GLY   A 89  ? 1.3904 1.4516 1.3696 0.0767  -0.1253 0.0191  109 GLY   A C   
662  O  O   . GLY   A 89  ? 1.4175 1.5200 1.4372 0.0693  -0.1220 0.0178  109 GLY   A O   
663  N  N   . PRO   A 90  ? 1.4557 1.5043 1.4165 0.0866  -0.1477 0.0107  110 PRO   A N   
664  C  CA  . PRO   A 90  ? 1.4074 1.4055 1.3122 0.0987  -0.1544 0.0106  110 PRO   A CA  
665  C  C   . PRO   A 90  ? 1.4281 1.4093 1.3215 0.0881  -0.1493 0.0102  110 PRO   A C   
666  O  O   . PRO   A 90  ? 1.4888 1.4953 1.4165 0.0735  -0.1581 0.0040  110 PRO   A O   
667  C  CB  . PRO   A 90  ? 1.4744 1.4781 1.3758 0.1122  -0.1864 -0.0018 110 PRO   A CB  
668  C  CG  . PRO   A 90  ? 1.3515 1.4138 1.3181 0.0980  -0.1958 -0.0090 110 PRO   A CG  
669  C  CD  . PRO   A 90  ? 1.3728 1.4615 1.3697 0.0886  -0.1700 -0.0001 110 PRO   A CD  
670  N  N   . VAL   A 91  ? 1.3597 1.2970 1.2055 0.0959  -0.1341 0.0176  111 VAL   A N   
671  C  CA  . VAL   A 91  ? 1.4360 1.3544 1.2684 0.0894  -0.1252 0.0177  111 VAL   A CA  
672  C  C   . VAL   A 91  ? 1.4743 1.3430 1.2435 0.1065  -0.1361 0.0111  111 VAL   A C   
673  O  O   . VAL   A 91  ? 1.5040 1.3539 1.2593 0.1037  -0.1364 0.0057  111 VAL   A O   
674  C  CB  . VAL   A 91  ? 1.3518 1.2688 1.1905 0.0835  -0.0921 0.0329  111 VAL   A CB  
675  C  CG1 . VAL   A 91  ? 1.3996 1.3637 1.2971 0.0658  -0.0853 0.0363  111 VAL   A CG1 
676  C  CG2 . VAL   A 91  ? 1.2681 1.1601 1.0751 0.0966  -0.0757 0.0450  111 VAL   A CG2 
677  N  N   . GLY   A 92  ? 1.4257 1.2688 1.1518 0.1260  -0.1458 0.0110  112 GLY   A N   
678  C  CA  . GLY   A 92  ? 1.5522 1.3448 1.2088 0.1455  -0.1566 0.0046  112 GLY   A CA  
679  C  C   . GLY   A 92  ? 1.4699 1.2280 1.0863 0.1524  -0.1242 0.0163  112 GLY   A C   
680  O  O   . GLY   A 92  ? 1.4255 1.1895 1.0532 0.1493  -0.0932 0.0339  112 GLY   A O   
681  N  N   . PHE   A 93  ? 1.5543 1.2767 1.1255 0.1623  -0.1322 0.0054  113 PHE   A N   
682  C  CA  . PHE   A 93  ? 1.5619 1.2523 1.0930 0.1727  -0.1004 0.0151  113 PHE   A CA  
683  C  C   . PHE   A 93  ? 1.5004 1.2222 1.0876 0.1535  -0.0745 0.0244  113 PHE   A C   
684  O  O   . PHE   A 93  ? 1.5554 1.2645 1.1266 0.1606  -0.0420 0.0376  113 PHE   A O   
685  C  CB  . PHE   A 93  ? 1.5618 1.2061 1.0323 0.1889  -0.1175 -0.0025 113 PHE   A CB  
686  C  CG  . PHE   A 93  ? 1.6484 1.3036 1.1563 0.1713  -0.1336 -0.0181 113 PHE   A CG  
687  C  CD1 . PHE   A 93  ? 1.7642 1.4413 1.3105 0.1559  -0.1719 -0.0346 113 PHE   A CD1 
688  C  CD2 . PHE   A 93  ? 1.6756 1.3196 1.1832 0.1704  -0.1100 -0.0150 113 PHE   A CD2 
689  C  CE1 . PHE   A 93  ? 1.7455 1.4299 1.3285 0.1374  -0.1854 -0.0461 113 PHE   A CE1 
690  C  CE2 . PHE   A 93  ? 1.7168 1.3649 1.2568 0.1545  -0.1251 -0.0277 113 PHE   A CE2 
691  C  CZ  . PHE   A 93  ? 1.8025 1.4692 1.3799 0.1367  -0.1624 -0.0426 113 PHE   A CZ  
692  N  N   . MET   A 94  ? 1.3880 1.1520 1.0406 0.1306  -0.0877 0.0188  114 MET   A N   
693  C  CA  . MET   A 94  ? 1.3735 1.1673 1.0773 0.1134  -0.0670 0.0276  114 MET   A CA  
694  C  C   . MET   A 94  ? 1.3298 1.1442 1.0558 0.1107  -0.0386 0.0469  114 MET   A C   
695  O  O   . MET   A 94  ? 1.2980 1.1375 1.0642 0.0988  -0.0207 0.0557  114 MET   A O   
696  C  CB  . MET   A 94  ? 1.4355 1.2686 1.1989 0.0909  -0.0871 0.0194  114 MET   A CB  
697  C  CG  . MET   A 94  ? 1.5412 1.3555 1.2970 0.0869  -0.1126 0.0022  114 MET   A CG  
698  S  SD  . MET   A 94  ? 1.3979 1.1715 1.1223 0.0946  -0.0959 0.0014  114 MET   A SD  
699  C  CE  . MET   A 94  ? 1.2458 1.0623 1.0321 0.0772  -0.0682 0.0195  114 MET   A CE  
700  N  N   . LYS   A 95  ? 1.2437 1.0459 0.9444 0.1214  -0.0364 0.0536  115 LYS   A N   
701  C  CA  . LYS   A 95  ? 1.2932 1.1023 1.0063 0.1201  -0.0086 0.0728  115 LYS   A CA  
702  C  C   . LYS   A 95  ? 1.2383 1.0335 0.9377 0.1264  0.0238  0.0853  115 LYS   A C   
703  O  O   . LYS   A 95  ? 1.2164 1.0312 0.9497 0.1180  0.0471  0.1006  115 LYS   A O   
704  C  CB  . LYS   A 95  ? 1.3492 1.1332 1.0242 0.1339  -0.0117 0.0788  115 LYS   A CB  
705  C  CG  . LYS   A 95  ? 1.5468 1.2802 1.1454 0.1580  -0.0061 0.0810  115 LYS   A CG  
706  C  CD  . LYS   A 95  ? 1.7527 1.4584 1.3108 0.1726  -0.0084 0.0903  115 LYS   A CD  
707  C  CE  . LYS   A 95  ? 1.8421 1.4953 1.3166 0.1989  0.0012  0.0952  115 LYS   A CE  
708  N  NZ  . LYS   A 95  ? 1.8950 1.5301 1.3324 0.2100  -0.0261 0.0723  115 LYS   A NZ  
709  N  N   . SER   A 96  ? 1.2854 1.0478 0.9374 0.1418  0.0246  0.0783  116 SER   A N   
710  C  CA  . SER   A 96  ? 1.3089 1.0566 0.9422 0.1534  0.0564  0.0888  116 SER   A CA  
711  C  C   . SER   A 96  ? 1.3055 1.0770 0.9823 0.1427  0.0615  0.0857  116 SER   A C   
712  O  O   . SER   A 96  ? 1.2484 1.0102 0.9137 0.1543  0.0863  0.0924  116 SER   A O   
713  C  CB  . SER   A 96  ? 1.3782 1.0736 0.9301 0.1801  0.0551  0.0810  116 SER   A CB  
714  O  OG  . SER   A 96  ? 1.6219 1.2916 1.1269 0.1924  0.0464  0.0835  116 SER   A OG  
715  N  N   . ALA   A 97  ? 1.2154 1.0170 0.9399 0.1229  0.0401  0.0770  117 ALA   A N   
716  C  CA  . ALA   A 97  ? 1.2033 1.0259 0.9681 0.1126  0.0437  0.0764  117 ALA   A CA  
717  C  C   . ALA   A 97  ? 1.1465 1.0088 0.9648 0.1013  0.0643  0.0930  117 ALA   A C   
718  O  O   . ALA   A 97  ? 1.0871 0.9686 0.9266 0.0924  0.0641  0.0995  117 ALA   A O   
719  C  CB  . ALA   A 97  ? 1.2902 1.1264 1.0805 0.0964  0.0134  0.0624  117 ALA   A CB  
720  N  N   . ILE   A 98  ? 1.0320 0.9047 0.8723 0.1024  0.0794  0.0985  118 ILE   A N   
721  C  CA  . ILE   A 98  ? 1.0724 0.9785 0.9579 0.0968  0.1014  0.1150  118 ILE   A CA  
722  C  C   . ILE   A 98  ? 0.9708 0.9157 0.9065 0.0757  0.0872  0.1158  118 ILE   A C   
723  O  O   . ILE   A 98  ? 0.9510 0.9151 0.9122 0.0686  0.0953  0.1254  118 ILE   A O   
724  C  CB  . ILE   A 98  ? 1.0491 0.9591 0.9476 0.1060  0.1177  0.1195  118 ILE   A CB  
725  C  CG1 . ILE   A 98  ? 0.9842 0.9373 0.9411 0.0975  0.1335  0.1348  118 ILE   A CG1 
726  C  CG2 . ILE   A 98  ? 1.0433 0.9461 0.9436 0.1018  0.0973  0.1072  118 ILE   A CG2 
727  C  CD1 . ILE   A 98  ? 1.1412 1.1015 1.1130 0.1111  0.1537  0.1421  118 ILE   A CD1 
728  N  N   . SER   A 99  ? 1.0271 0.9824 0.9766 0.0655  0.0662  0.1060  119 SER   A N   
729  C  CA  . SER   A 99  ? 1.0352 1.0267 1.0259 0.0488  0.0545  0.1064  119 SER   A CA  
730  C  C   . SER   A 99  ? 0.9870 0.9804 0.9721 0.0446  0.0439  0.1024  119 SER   A C   
731  O  O   . SER   A 99  ? 0.9329 0.9535 0.9477 0.0341  0.0367  0.1024  119 SER   A O   
732  C  CB  . SER   A 99  ? 1.0129 1.0135 1.0159 0.0402  0.0383  0.0996  119 SER   A CB  
733  O  OG  . SER   A 99  ? 0.9527 0.9359 0.9322 0.0392  0.0208  0.0878  119 SER   A OG  
734  N  N   . ILE   A 100 ? 0.9919 0.9544 0.9358 0.0551  0.0422  0.0987  120 ILE   A N   
735  C  CA  . ILE   A 100 ? 0.9981 0.9569 0.9320 0.0551  0.0318  0.0957  120 ILE   A CA  
736  C  C   . ILE   A 100 ? 1.0209 0.9616 0.9392 0.0622  0.0504  0.1083  120 ILE   A C   
737  O  O   . ILE   A 100 ? 0.8578 0.8021 0.7851 0.0581  0.0463  0.1106  120 ILE   A O   
738  C  CB  . ILE   A 100 ? 1.0549 0.9932 0.9548 0.0619  0.0107  0.0823  120 ILE   A CB  
739  C  CG1 . ILE   A 100 ? 1.0991 1.0603 1.0253 0.0503  -0.0073 0.0722  120 ILE   A CG1 
740  C  CG2 . ILE   A 100 ? 1.0275 0.9570 0.9108 0.0674  0.0001  0.0801  120 ILE   A CG2 
741  C  CD1 . ILE   A 100 ? 1.3138 1.2592 1.2179 0.0537  -0.0297 0.0586  120 ILE   A CD1 
742  N  N   . ALA   A 101 ? 1.0605 0.9820 0.9577 0.0729  0.0723  0.1177  121 ALA   A N   
743  C  CA  . ALA   A 101 ? 1.0244 0.9279 0.9055 0.0797  0.0943  0.1332  121 ALA   A CA  
744  C  C   . ALA   A 101 ? 1.0088 0.9400 0.9427 0.0642  0.1041  0.1449  121 ALA   A C   
745  O  O   . ALA   A 101 ? 0.8021 0.7670 0.7822 0.0521  0.0994  0.1426  121 ALA   A O   
746  C  CB  . ALA   A 101 ? 1.0604 0.9440 0.9123 0.0957  0.1202  0.1418  121 ALA   A CB  
747  N  N   . GLU   A 102 ? 0.9609 0.8745 0.8857 0.0651  0.1174  0.1583  122 GLU   A N   
748  C  CA  . GLU   A 102 ? 0.9437 0.8759 0.9172 0.0487  0.1229  0.1685  122 GLU   A CA  
749  C  C   . GLU   A 102 ? 1.0593 0.9873 1.0435 0.0491  0.1564  0.1913  122 GLU   A C   
750  O  O   . GLU   A 102 ? 1.1549 1.0544 1.0936 0.0651  0.1763  0.2013  122 GLU   A O   
751  C  CB  . GLU   A 102 ? 1.0082 0.9229 0.9723 0.0449  0.1058  0.1648  122 GLU   A CB  
752  C  CG  . GLU   A 102 ? 1.0334 0.9405 0.9670 0.0531  0.0786  0.1460  122 GLU   A CG  
753  C  CD  . GLU   A 102 ? 1.1300 1.0292 1.0668 0.0499  0.0606  0.1405  122 GLU   A CD  
754  O  OE1 . GLU   A 102 ? 1.2773 1.1434 1.1903 0.0550  0.0675  0.1517  122 GLU   A OE1 
755  O  OE2 . GLU   A 102 ? 0.9939 0.9187 0.9560 0.0435  0.0411  0.1261  122 GLU   A OE2 
756  N  N   . ASP   A 103 ? 1.0492 1.0071 1.0948 0.0318  0.1622  0.1995  123 ASP   A N   
757  C  CA  . ASP   A 103 ? 1.1537 1.1128 1.2270 0.0249  0.1913  0.2233  123 ASP   A CA  
758  C  C   . ASP   A 103 ? 1.1739 1.1316 1.2276 0.0420  0.2243  0.2366  123 ASP   A C   
759  O  O   . ASP   A 103 ? 1.1150 1.0971 1.1826 0.0482  0.2253  0.2297  123 ASP   A O   
760  C  CB  . ASP   A 103 ? 1.2591 1.1807 1.3085 0.0216  0.1904  0.2318  123 ASP   A CB  
761  C  CG  . ASP   A 103 ? 1.2868 1.2116 1.3615 0.0063  0.1592  0.2176  123 ASP   A CG  
762  O  OD1 . ASP   A 103 ? 1.1959 1.1566 1.3234 -0.0078 0.1461  0.2090  123 ASP   A OD1 
763  O  OD2 . ASP   A 103 ? 1.2758 1.1659 1.3146 0.0109  0.1471  0.2147  123 ASP   A OD2 
764  N  N   . GLU   A 104 ? 1.2028 1.1308 1.2211 0.0520  0.2523  0.2560  124 GLU   A N   
765  C  CA  . GLU   A 104 ? 1.2529 1.1835 1.2574 0.0693  0.2889  0.2709  124 GLU   A CA  
766  C  C   . GLU   A 104 ? 1.2640 1.1706 1.2004 0.0952  0.2833  0.2547  124 GLU   A C   
767  O  O   . GLU   A 104 ? 1.2078 1.1254 1.1419 0.1102  0.3035  0.2568  124 GLU   A O   
768  C  CB  . GLU   A 104 ? 1.3765 1.2819 1.3615 0.0724  0.3236  0.2992  124 GLU   A CB  
769  C  CG  . GLU   A 104 ? 1.4876 1.4081 1.5388 0.0441  0.3265  0.3155  124 GLU   A CG  
770  C  CD  . GLU   A 104 ? 1.6259 1.6050 1.7698 0.0251  0.3268  0.3162  124 GLU   A CD  
771  O  OE1 . GLU   A 104 ? 1.5217 1.5297 1.6894 0.0342  0.3562  0.3280  124 GLU   A OE1 
772  O  OE2 . GLU   A 104 ? 1.7036 1.6997 1.8944 0.0035  0.2965  0.3041  124 GLU   A OE2 
773  N  N   . GLU   A 105 ? 1.1594 1.0328 1.0421 0.1014  0.2552  0.2379  125 GLU   A N   
774  C  CA  . GLU   A 105 ? 1.2377 1.0878 1.0615 0.1224  0.2431  0.2195  125 GLU   A CA  
775  C  C   . GLU   A 105 ? 1.2244 1.1063 1.0862 0.1174  0.2285  0.2036  125 GLU   A C   
776  O  O   . GLU   A 105 ? 1.2955 1.1694 1.1325 0.1348  0.2373  0.1980  125 GLU   A O   
777  C  CB  . GLU   A 105 ? 1.3104 1.1269 1.0835 0.1265  0.2113  0.2043  125 GLU   A CB  
778  C  CG  . GLU   A 105 ? 1.5280 1.2960 1.2277 0.1462  0.2245  0.2157  125 GLU   A CG  
779  C  CD  . GLU   A 105 ? 1.6493 1.4119 1.3670 0.1352  0.2419  0.2397  125 GLU   A CD  
780  O  OE1 . GLU   A 105 ? 1.6168 1.4057 1.3957 0.1115  0.2294  0.2394  125 GLU   A OE1 
781  O  OE2 . GLU   A 105 ? 1.7666 1.4955 1.4346 0.1505  0.2678  0.2590  125 GLU   A OE2 
782  N  N   . TRP   A 106 ? 1.0993 1.0140 1.0176 0.0955  0.2064  0.1965  126 TRP   A N   
783  C  CA  . TRP   A 106 ? 1.0893 1.0348 1.0452 0.0905  0.1950  0.1857  126 TRP   A CA  
784  C  C   . TRP   A 106 ? 1.0465 1.0197 1.0422 0.0948  0.2239  0.2002  126 TRP   A C   
785  O  O   . TRP   A 106 ? 1.0460 1.0243 1.0403 0.1063  0.2262  0.1941  126 TRP   A O   
786  C  CB  . TRP   A 106 ? 1.0260 1.0004 1.0292 0.0684  0.1679  0.1772  126 TRP   A CB  
787  C  CG  . TRP   A 106 ? 0.9947 1.0070 1.0482 0.0618  0.1642  0.1751  126 TRP   A CG  
788  C  CD1 . TRP   A 106 ? 0.8268 0.8425 0.8750 0.0656  0.1496  0.1628  126 TRP   A CD1 
789  C  CD2 . TRP   A 106 ? 0.9166 0.9673 1.0335 0.0507  0.1740  0.1867  126 TRP   A CD2 
790  N  NE1 . TRP   A 106 ? 0.7755 0.8272 0.8747 0.0598  0.1503  0.1667  126 TRP   A NE1 
791  C  CE2 . TRP   A 106 ? 0.8776 0.9533 1.0206 0.0511  0.1637  0.1803  126 TRP   A CE2 
792  C  CE3 . TRP   A 106 ? 0.9029 0.9686 1.0593 0.0397  0.1890  0.2023  126 TRP   A CE3 
793  C  CZ2 . TRP   A 106 ? 0.8889 1.0056 1.0934 0.0432  0.1658  0.1877  126 TRP   A CZ2 
794  C  CZ3 . TRP   A 106 ? 0.7272 0.8357 0.9506 0.0291  0.1907  0.2088  126 TRP   A CZ3 
795  C  CH2 . TRP   A 106 ? 0.8418 0.9761 1.0875 0.0321  0.1781  0.2009  126 TRP   A CH2 
796  N  N   . LYS   A 107 ? 1.0340 1.0260 1.0695 0.0854  0.2455  0.2198  127 LYS   A N   
797  C  CA  . LYS   A 107 ? 1.0428 1.0693 1.1271 0.0887  0.2738  0.2352  127 LYS   A CA  
798  C  C   . LYS   A 107 ? 1.1832 1.1888 1.2199 0.1179  0.3028  0.2397  127 LYS   A C   
799  O  O   . LYS   A 107 ? 1.1315 1.1622 1.1965 0.1287  0.3180  0.2429  127 LYS   A O   
800  C  CB  . LYS   A 107 ? 0.9220 0.9684 1.0566 0.0716  0.2925  0.2569  127 LYS   A CB  
801  C  CG  . LYS   A 107 ? 1.0865 1.1798 1.2897 0.0705  0.3195  0.2740  127 LYS   A CG  
802  C  CD  . LYS   A 107 ? 1.2717 1.4029 1.5565 0.0409  0.3077  0.2808  127 LYS   A CD  
803  C  CE  . LYS   A 107 ? 1.3694 1.4736 1.6454 0.0246  0.3091  0.2910  127 LYS   A CE  
804  N  NZ  . LYS   A 107 ? 1.4034 1.5375 1.7561 -0.0051 0.2920  0.2935  127 LYS   A NZ  
805  N  N   . ARG   A 108 ? 1.2403 1.1982 1.2013 0.1336  0.3095  0.2388  128 ARG   A N   
806  C  CA  . ARG   A 108 ? 1.2541 1.1838 1.1559 0.1649  0.3331  0.2387  128 ARG   A CA  
807  C  C   . ARG   A 108 ? 1.1847 1.0972 1.0564 0.1763  0.3073  0.2134  128 ARG   A C   
808  O  O   . ARG   A 108 ? 1.2582 1.1732 1.1268 0.1955  0.3221  0.2113  128 ARG   A O   
809  C  CB  . ARG   A 108 ? 1.2814 1.1623 1.1056 0.1795  0.3452  0.2452  128 ARG   A CB  
810  C  CG  . ARG   A 108 ? 1.3952 1.2317 1.1347 0.2136  0.3538  0.2345  128 ARG   A CG  
811  C  CD  . ARG   A 108 ? 1.4662 1.2538 1.1249 0.2294  0.3640  0.2421  128 ARG   A CD  
812  N  NE  . ARG   A 108 ? 1.6898 1.4263 1.2584 0.2583  0.3519  0.2215  128 ARG   A NE  
813  C  CZ  . ARG   A 108 ? 1.6316 1.3389 1.1625 0.2559  0.3086  0.1970  128 ARG   A CZ  
814  N  NH1 . ARG   A 108 ? 1.4663 1.1913 1.0386 0.2285  0.2761  0.1905  128 ARG   A NH1 
815  N  NH2 . ARG   A 108 ? 1.7113 1.3711 1.1622 0.2823  0.2972  0.1778  128 ARG   A NH2 
816  N  N   . LEU   A 109 ? 1.2666 1.1611 1.1183 0.1648  0.2690  0.1947  129 LEU   A N   
817  C  CA  . LEU   A 109 ? 1.2606 1.1368 1.0878 0.1713  0.2431  0.1722  129 LEU   A CA  
818  C  C   . LEU   A 109 ? 1.2984 1.2116 1.1852 0.1654  0.2412  0.1716  129 LEU   A C   
819  O  O   . LEU   A 109 ? 1.2711 1.1675 1.1385 0.1799  0.2369  0.1604  129 LEU   A O   
820  C  CB  . LEU   A 109 ? 1.1603 1.0230 0.9730 0.1557  0.2042  0.1559  129 LEU   A CB  
821  C  CG  . LEU   A 109 ? 1.2296 1.0491 0.9739 0.1658  0.1960  0.1507  129 LEU   A CG  
822  C  CD1 . LEU   A 109 ? 0.9973 0.8199 0.7500 0.1475  0.1591  0.1375  129 LEU   A CD1 
823  C  CD2 . LEU   A 109 ? 1.0965 0.8694 0.7691 0.1925  0.1958  0.1372  129 LEU   A CD2 
824  N  N   . ARG   A 110 ? 1.0896 1.0499 1.0472 0.1452  0.2421  0.1830  130 ARG   A N   
825  C  CA  . ARG   A 110 ? 1.1041 1.1012 1.1179 0.1414  0.2389  0.1839  130 ARG   A CA  
826  C  C   . ARG   A 110 ? 1.1178 1.1219 1.1369 0.1658  0.2712  0.1936  130 ARG   A C   
827  O  O   . ARG   A 110 ? 1.1506 1.1538 1.1732 0.1779  0.2668  0.1866  130 ARG   A O   
828  C  CB  . ARG   A 110 ? 1.0027 1.0470 1.0873 0.1165  0.2316  0.1932  130 ARG   A CB  
829  C  CG  . ARG   A 110 ? 1.0176 1.0994 1.1567 0.1119  0.2206  0.1926  130 ARG   A CG  
830  C  CD  . ARG   A 110 ? 0.9040 0.9824 1.0390 0.0978  0.1852  0.1779  130 ARG   A CD  
831  N  NE  . ARG   A 110 ? 0.9398 1.0446 1.1124 0.0984  0.1752  0.1780  130 ARG   A NE  
832  C  CZ  . ARG   A 110 ? 0.8922 1.0074 1.0768 0.0850  0.1486  0.1711  130 ARG   A CZ  
833  N  NH1 . ARG   A 110 ? 0.9147 1.0212 1.0827 0.0698  0.1301  0.1625  130 ARG   A NH1 
834  N  NH2 . ARG   A 110 ? 0.8113 0.9466 1.0240 0.0892  0.1415  0.1736  130 ARG   A NH2 
835  N  N   . SER   A 111 ? 1.1231 1.1333 1.1426 0.1746  0.3054  0.2108  131 SER   A N   
836  C  CA  . SER   A 111 ? 1.2330 1.2554 1.2606 0.2002  0.3413  0.2218  131 SER   A CA  
837  C  C   . SER   A 111 ? 1.2303 1.2014 1.1814 0.2311  0.3439  0.2064  131 SER   A C   
838  O  O   . SER   A 111 ? 1.2590 1.2350 1.2184 0.2513  0.3533  0.2037  131 SER   A O   
839  C  CB  . SER   A 111 ? 1.2615 1.2984 1.3005 0.2024  0.3804  0.2457  131 SER   A CB  
840  O  OG  . SER   A 111 ? 1.3590 1.4502 1.4850 0.1766  0.3820  0.2612  131 SER   A OG  
841  N  N   . LEU   A 112 ? 1.2421 1.1615 1.1173 0.2364  0.3335  0.1950  132 LEU   A N   
842  C  CA  . LEU   A 112 ? 1.2917 1.1564 1.0891 0.2655  0.3318  0.1775  132 LEU   A CA  
843  C  C   . LEU   A 112 ? 1.2726 1.1235 1.0737 0.2614  0.2977  0.1572  132 LEU   A C   
844  O  O   . LEU   A 112 ? 1.4141 1.2304 1.1752 0.2866  0.2998  0.1448  132 LEU   A O   
845  C  CB  . LEU   A 112 ? 1.4007 1.2150 1.1185 0.2705  0.3227  0.1692  132 LEU   A CB  
846  C  CG  . LEU   A 112 ? 1.5017 1.3161 1.1978 0.2802  0.3597  0.1909  132 LEU   A CG  
847  C  CD1 . LEU   A 112 ? 1.4963 1.2717 1.1338 0.2742  0.3389  0.1846  132 LEU   A CD1 
848  C  CD2 . LEU   A 112 ? 1.5384 1.3312 1.1843 0.3198  0.3989  0.1955  132 LEU   A CD2 
849  N  N   . LEU   A 113 ? 1.2985 1.1732 1.1449 0.2310  0.2672  0.1540  133 LEU   A N   
850  C  CA  . LEU   A 113 ? 1.3570 1.2188 1.2081 0.2235  0.2357  0.1383  133 LEU   A CA  
851  C  C   . LEU   A 113 ? 1.3579 1.2628 1.2772 0.2186  0.2368  0.1472  133 LEU   A C   
852  O  O   . LEU   A 113 ? 1.3860 1.2777 1.3080 0.2156  0.2149  0.1376  133 LEU   A O   
853  C  CB  . LEU   A 113 ? 1.2825 1.1395 1.1318 0.1957  0.2006  0.1285  133 LEU   A CB  
854  C  CG  . LEU   A 113 ? 1.3070 1.1135 1.0846 0.2021  0.1870  0.1134  133 LEU   A CG  
855  C  CD1 . LEU   A 113 ? 1.2305 1.0447 1.0190 0.1752  0.1559  0.1068  133 LEU   A CD1 
856  C  CD2 . LEU   A 113 ? 1.3992 1.1545 1.1268 0.2210  0.1758  0.0949  133 LEU   A CD2 
857  N  N   . SER   A 114 ? 1.2759 1.2310 1.2513 0.2176  0.2605  0.1659  134 SER   A N   
858  C  CA  . SER   A 114 ? 1.2832 1.2814 1.3242 0.2148  0.2580  0.1738  134 SER   A CA  
859  C  C   . SER   A 114 ? 1.3613 1.3417 1.3894 0.2455  0.2692  0.1702  134 SER   A C   
860  O  O   . SER   A 114 ? 1.3760 1.3564 1.4220 0.2437  0.2493  0.1660  134 SER   A O   
861  C  CB  . SER   A 114 ? 1.2299 1.2879 1.3394 0.2044  0.2769  0.1934  134 SER   A CB  
862  O  OG  . SER   A 114 ? 1.3825 1.4562 1.5116 0.1741  0.2585  0.1944  134 SER   A OG  
863  N  N   . PRO   A 115 ? 1.4136 1.3765 1.4090 0.2760  0.3009  0.1721  135 PRO   A N   
864  C  CA  . PRO   A 115 ? 1.4546 1.3965 1.4350 0.3085  0.3102  0.1664  135 PRO   A CA  
865  C  C   . PRO   A 115 ? 1.4963 1.3755 1.4226 0.3109  0.2797  0.1451  135 PRO   A C   
866  O  O   . PRO   A 115 ? 1.4658 1.3279 1.3917 0.3303  0.2768  0.1405  135 PRO   A O   
867  C  CB  . PRO   A 115 ? 1.5395 1.4680 1.4803 0.3406  0.3510  0.1707  135 PRO   A CB  
868  C  CG  . PRO   A 115 ? 1.5085 1.4738 1.4750 0.3221  0.3687  0.1875  135 PRO   A CG  
869  C  CD  . PRO   A 115 ? 1.4067 1.3667 1.3749 0.2852  0.3320  0.1807  135 PRO   A CD  
870  N  N   . THR   A 116 ? 1.5360 1.3801 1.4192 0.2919  0.2562  0.1325  136 THR   A N   
871  C  CA  . THR   A 116 ? 1.5326 1.3224 1.3761 0.2872  0.2238  0.1133  136 THR   A CA  
872  C  C   . THR   A 116 ? 1.3528 1.1624 1.2462 0.2704  0.2021  0.1180  136 THR   A C   
873  O  O   . THR   A 116 ? 1.4425 1.2098 1.3151 0.2769  0.1857  0.1080  136 THR   A O   
874  C  CB  . THR   A 116 ? 1.4506 1.2162 1.2575 0.2651  0.2011  0.1020  136 THR   A CB  
875  O  OG1 . THR   A 116 ? 1.6277 1.3844 1.3940 0.2789  0.2228  0.1030  136 THR   A OG1 
876  C  CG2 . THR   A 116 ? 1.5894 1.2917 1.3474 0.2651  0.1715  0.0802  136 THR   A CG2 
877  N  N   . PHE   A 117 ? 1.3847 1.2545 1.3412 0.2494  0.2010  0.1335  137 PHE   A N   
878  C  CA  . PHE   A 117 ? 1.4096 1.3002 1.4081 0.2323  0.1791  0.1392  137 PHE   A CA  
879  C  C   . PHE   A 117 ? 1.3968 1.3320 1.4501 0.2471  0.1926  0.1541  137 PHE   A C   
880  O  O   . PHE   A 117 ? 1.2834 1.2593 1.3845 0.2306  0.1795  0.1640  137 PHE   A O   
881  C  CB  . PHE   A 117 ? 1.2651 1.1868 1.2882 0.1977  0.1610  0.1423  137 PHE   A CB  
882  C  CG  . PHE   A 117 ? 1.2624 1.1475 1.2407 0.1826  0.1444  0.1282  137 PHE   A CG  
883  C  CD1 . PHE   A 117 ? 1.2418 1.0992 1.2074 0.1674  0.1182  0.1203  137 PHE   A CD1 
884  C  CD2 . PHE   A 117 ? 1.1664 1.0458 1.1175 0.1838  0.1548  0.1244  137 PHE   A CD2 
885  C  CE1 . PHE   A 117 ? 1.2266 1.0564 1.1593 0.1533  0.1013  0.1072  137 PHE   A CE1 
886  C  CE2 . PHE   A 117 ? 1.3331 1.1810 1.2447 0.1722  0.1366  0.1110  137 PHE   A CE2 
887  C  CZ  . PHE   A 117 ? 1.2248 1.0505 1.1303 0.1566  0.1090  0.1016  137 PHE   A CZ  
888  N  N   . THR   A 118 ? 1.3884 1.3173 1.4346 0.2801  0.2180  0.1555  138 THR   A N   
889  C  CA  . THR   A 118 ? 1.4596 1.4318 1.5612 0.2974  0.2291  0.1690  138 THR   A CA  
890  C  C   . THR   A 118 ? 1.5316 1.4729 1.6270 0.3069  0.2089  0.1663  138 THR   A C   
891  O  O   . THR   A 118 ? 1.5673 1.4460 1.6106 0.3065  0.1936  0.1533  138 THR   A O   
892  C  CB  . THR   A 118 ? 1.4937 1.4757 1.5950 0.3320  0.2669  0.1730  138 THR   A CB  
893  O  OG1 . THR   A 118 ? 1.4941 1.4067 1.5221 0.3577  0.2729  0.1569  138 THR   A OG1 
894  C  CG2 . THR   A 118 ? 1.5132 1.5333 1.6321 0.3211  0.2901  0.1820  138 THR   A CG2 
895  N  N   . SER   A 119 ? 1.5415 1.5268 1.6926 0.3151  0.2074  0.1797  139 SER   A N   
896  C  CA  . SER   A 119 ? 1.6799 1.6367 1.8265 0.3279  0.1901  0.1809  139 SER   A CA  
897  C  C   . SER   A 119 ? 1.6538 1.5497 1.7521 0.3635  0.2023  0.1699  139 SER   A C   
898  O  O   . SER   A 119 ? 1.6944 1.5343 1.7608 0.3678  0.1840  0.1643  139 SER   A O   
899  C  CB  . SER   A 119 ? 1.6696 1.6883 1.8845 0.3362  0.1876  0.1972  139 SER   A CB  
900  O  OG  . SER   A 119 ? 1.6457 1.7140 1.9023 0.3569  0.2165  0.2038  139 SER   A OG  
901  N  N   . GLY   A 120 ? 1.5836 1.4862 1.6736 0.3896  0.2336  0.1668  140 GLY   A N   
902  C  CA  . GLY   A 120 ? 1.6964 1.5387 1.7340 0.4277  0.2464  0.1540  140 GLY   A CA  
903  C  C   . GLY   A 120 ? 1.6641 1.4251 1.6244 0.4181  0.2296  0.1333  140 GLY   A C   
904  O  O   . GLY   A 120 ? 1.6985 1.3941 1.6202 0.4317  0.2149  0.1224  140 GLY   A O   
905  N  N   . LYS   A 121 ? 1.6646 1.4271 1.6027 0.3947  0.2298  0.1275  141 LYS   A N   
906  C  CA  . LYS   A 121 ? 1.7166 1.4080 1.5870 0.3831  0.2096  0.1072  141 LYS   A CA  
907  C  C   . LYS   A 121 ? 1.6207 1.2851 1.4962 0.3543  0.1734  0.1062  141 LYS   A C   
908  O  O   . LYS   A 121 ? 1.7004 1.2942 1.5282 0.3544  0.1543  0.0902  141 LYS   A O   
909  C  CB  . LYS   A 121 ? 1.6103 1.3172 1.4639 0.3627  0.2142  0.1040  141 LYS   A CB  
910  C  CG  . LYS   A 121 ? 1.5746 1.3149 1.4286 0.3856  0.2529  0.1108  141 LYS   A CG  
911  C  CD  . LYS   A 121 ? 1.6682 1.3540 1.4581 0.4293  0.2727  0.0964  141 LYS   A CD  
912  C  CE  . LYS   A 121 ? 1.7214 1.4459 1.5144 0.4523  0.3165  0.1076  141 LYS   A CE  
913  N  NZ  . LYS   A 121 ? 1.6262 1.3759 1.4187 0.4244  0.3191  0.1139  141 LYS   A NZ  
914  N  N   . LEU   A 122 ? 1.6697 1.3887 1.6024 0.3293  0.1637  0.1235  142 LEU   A N   
915  C  CA  . LEU   A 122 ? 1.6519 1.3512 1.5907 0.3022  0.1339  0.1268  142 LEU   A CA  
916  C  C   . LEU   A 122 ? 1.6816 1.3272 1.6047 0.3234  0.1253  0.1261  142 LEU   A C   
917  O  O   . LEU   A 122 ? 1.7258 1.3156 1.6226 0.3081  0.1027  0.1197  142 LEU   A O   
918  C  CB  . LEU   A 122 ? 1.5406 1.3100 1.5385 0.2788  0.1284  0.1458  142 LEU   A CB  
919  C  CG  . LEU   A 122 ? 1.5318 1.2924 1.5405 0.2540  0.1029  0.1548  142 LEU   A CG  
920  C  CD1 . LEU   A 122 ? 1.5039 1.2158 1.4758 0.2286  0.0847  0.1423  142 LEU   A CD1 
921  C  CD2 . LEU   A 122 ? 1.4683 1.2992 1.5258 0.2336  0.0990  0.1697  142 LEU   A CD2 
922  N  N   . LYS   A 123 ? 1.6647 1.3261 1.6066 0.3586  0.1429  0.1332  143 LYS   A N   
923  C  CA  . LYS   A 123 ? 1.8200 1.4268 1.7448 0.3842  0.1357  0.1325  143 LYS   A CA  
924  C  C   . LYS   A 123 ? 1.8876 1.4055 1.7436 0.3977  0.1305  0.1085  143 LYS   A C   
925  O  O   . LYS   A 123 ? 1.9834 1.4351 1.8148 0.3952  0.1096  0.1041  143 LYS   A O   
926  C  CB  . LYS   A 123 ? 1.8126 1.4593 1.7724 0.4240  0.1580  0.1430  143 LYS   A CB  
927  C  CG  . LYS   A 123 ? 1.9413 1.5523 1.9034 0.4476  0.1471  0.1504  143 LYS   A CG  
928  C  CD  . LYS   A 123 ? 2.0150 1.6901 2.0319 0.4798  0.1646  0.1653  143 LYS   A CD  
929  C  CE  . LYS   A 123 ? 2.0756 1.7734 2.0908 0.5130  0.1994  0.1566  143 LYS   A CE  
930  N  NZ  . LYS   A 123 ? 2.0988 1.8678 2.1784 0.5431  0.2174  0.1721  143 LYS   A NZ  
931  N  N   . GLU   A 124 ? 1.8637 1.3762 1.6858 0.4115  0.1479  0.0930  144 GLU   A N   
932  C  CA  . GLU   A 124 ? 1.8740 1.3011 1.6238 0.4254  0.1401  0.0669  144 GLU   A CA  
933  C  C   . GLU   A 124 ? 1.8973 1.2825 1.6249 0.3843  0.1070  0.0563  144 GLU   A C   
934  O  O   . GLU   A 124 ? 1.9055 1.2105 1.5798 0.3901  0.0897  0.0349  144 GLU   A O   
935  C  CB  . GLU   A 124 ? 1.8809 1.3171 1.5960 0.4506  0.1679  0.0551  144 GLU   A CB  
936  C  CG  . GLU   A 124 ? 1.9302 1.4100 1.6695 0.4929  0.2051  0.0657  144 GLU   A CG  
937  C  CD  . GLU   A 124 ? 2.0744 1.5484 1.7669 0.5228  0.2355  0.0539  144 GLU   A CD  
938  O  OE1 . GLU   A 124 ? 1.9358 1.4587 1.6406 0.5060  0.2494  0.0611  144 GLU   A OE1 
939  O  OE2 . GLU   A 124 ? 2.0306 1.4476 1.6701 0.5646  0.2459  0.0376  144 GLU   A OE2 
940  N  N   . MET   A 125 ? 1.8642 1.3019 1.6331 0.3439  0.0970  0.0699  145 MET   A N   
941  C  CA  . MET   A 125 ? 1.8911 1.3009 1.6504 0.3041  0.0675  0.0627  145 MET   A CA  
942  C  C   . MET   A 125 ? 1.9663 1.3475 1.7454 0.2846  0.0459  0.0742  145 MET   A C   
943  O  O   . MET   A 125 ? 2.0536 1.3974 1.8226 0.2548  0.0213  0.0671  145 MET   A O   
944  C  CB  . MET   A 125 ? 1.7293 1.2081 1.5210 0.2721  0.0686  0.0714  145 MET   A CB  
945  C  CG  . MET   A 125 ? 1.6628 1.1643 1.4323 0.2853  0.0876  0.0620  145 MET   A CG  
946  S  SD  . MET   A 125 ? 1.6844 1.2459 1.4811 0.2463  0.0814  0.0677  145 MET   A SD  
947  C  CE  . MET   A 125 ? 1.7752 1.3355 1.5264 0.2713  0.1041  0.0554  145 MET   A CE  
948  N  N   . VAL   A 126 ? 1.9264 1.3247 1.7344 0.3011  0.0545  0.0930  146 VAL   A N   
949  C  CA  . VAL   A 126 ? 2.0054 1.3821 1.8327 0.2822  0.0365  0.1096  146 VAL   A CA  
950  C  C   . VAL   A 126 ? 2.1649 1.4440 1.9519 0.2800  0.0150  0.0953  146 VAL   A C   
951  O  O   . VAL   A 126 ? 2.1620 1.4207 1.9586 0.2436  -0.0054 0.1016  146 VAL   A O   
952  C  CB  . VAL   A 126 ? 2.0283 1.4400 1.8890 0.3062  0.0486  0.1316  146 VAL   A CB  
953  C  CG1 . VAL   A 126 ? 1.9749 1.3544 1.8454 0.2914  0.0308  0.1504  146 VAL   A CG1 
954  C  CG2 . VAL   A 126 ? 1.8935 1.4016 1.8005 0.2996  0.0632  0.1455  146 VAL   A CG2 
955  N  N   . PRO   A 127 ? 2.2233 1.4389 1.9665 0.3169  0.0180  0.0766  147 PRO   A N   
956  C  CA  . PRO   A 127 ? 2.2501 1.3659 1.9561 0.3128  -0.0067 0.0623  147 PRO   A CA  
957  C  C   . PRO   A 127 ? 2.3026 1.3895 1.9931 0.2746  -0.0311 0.0449  147 PRO   A C   
958  O  O   . PRO   A 127 ? 2.3764 1.4051 2.0656 0.2493  -0.0557 0.0447  147 PRO   A O   
959  C  CB  . PRO   A 127 ? 2.2524 1.3149 1.9087 0.3651  0.0048  0.0408  147 PRO   A CB  
960  C  CG  . PRO   A 127 ? 2.1435 1.2810 1.8291 0.3970  0.0366  0.0560  147 PRO   A CG  
961  C  CD  . PRO   A 127 ? 2.1253 1.3542 1.8527 0.3654  0.0444  0.0689  147 PRO   A CD  
962  N  N   . ILE   A 128 ? 2.2352 1.3606 1.9161 0.2694  -0.0259 0.0311  148 ILE   A N   
963  C  CA  . ILE   A 128 ? 2.2831 1.3918 1.9566 0.2326  -0.0512 0.0160  148 ILE   A CA  
964  C  C   . ILE   A 128 ? 2.2993 1.4600 2.0305 0.1861  -0.0590 0.0404  148 ILE   A C   
965  O  O   . ILE   A 128 ? 2.3168 1.4474 2.0574 0.1511  -0.0840 0.0371  148 ILE   A O   
966  C  CB  . ILE   A 128 ? 2.3311 1.4659 1.9747 0.2436  -0.0433 -0.0036 148 ILE   A CB  
967  C  CG1 . ILE   A 128 ? 2.3934 1.4612 1.9678 0.2885  -0.0392 -0.0312 148 ILE   A CG1 
968  C  CG2 . ILE   A 128 ? 2.2845 1.4216 1.9329 0.2038  -0.0698 -0.0149 148 ILE   A CG2 
969  C  CD1 . ILE   A 128 ? 2.3033 1.4003 1.8726 0.3346  -0.0023 -0.0227 148 ILE   A CD1 
970  N  N   . ILE   A 129 ? 2.1898 1.4292 1.9614 0.1856  -0.0379 0.0651  149 ILE   A N   
971  C  CA  . ILE   A 129 ? 2.1537 1.4387 1.9742 0.1481  -0.0423 0.0902  149 ILE   A CA  
972  C  C   . ILE   A 129 ? 2.1930 1.4266 2.0213 0.1396  -0.0529 0.1068  149 ILE   A C   
973  O  O   . ILE   A 129 ? 2.1670 1.4049 2.0231 0.1027  -0.0642 0.1217  149 ILE   A O   
974  C  CB  . ILE   A 129 ? 2.0223 1.3966 1.8771 0.1544  -0.0195 0.1099  149 ILE   A CB  
975  C  CG1 . ILE   A 129 ? 2.0312 1.4523 1.8803 0.1579  -0.0096 0.0958  149 ILE   A CG1 
976  C  CG2 . ILE   A 129 ? 1.8859 1.3034 1.7830 0.1213  -0.0229 0.1355  149 ILE   A CG2 
977  C  CD1 . ILE   A 129 ? 1.8575 1.3624 1.7426 0.1611  0.0101  0.1130  149 ILE   A CD1 
978  N  N   . ALA   A 130 ? 2.2124 1.3953 2.0163 0.1744  -0.0485 0.1056  150 ALA   A N   
979  C  CA  . ALA   A 130 ? 2.2204 1.3499 2.0287 0.1703  -0.0576 0.1239  150 ALA   A CA  
980  C  C   . ALA   A 130 ? 2.3207 1.3719 2.1165 0.1408  -0.0847 0.1123  150 ALA   A C   
981  O  O   . ALA   A 130 ? 2.3958 1.4235 2.2130 0.1139  -0.0937 0.1340  150 ALA   A O   
982  C  CB  . ALA   A 130 ? 2.2526 1.3446 2.0363 0.2191  -0.0472 0.1229  150 ALA   A CB  
983  N  N   . GLN   A 131 ? 2.3161 1.3254 2.0774 0.1450  -0.0985 0.0788  151 GLN   A N   
984  C  CA  . GLN   A 131 ? 2.4196 1.3469 2.1678 0.1198  -0.1290 0.0632  151 GLN   A CA  
985  C  C   . GLN   A 131 ? 2.3737 1.3359 2.1699 0.0649  -0.1419 0.0767  151 GLN   A C   
986  O  O   . GLN   A 131 ? 2.3436 1.2554 2.1565 0.0351  -0.1595 0.0862  151 GLN   A O   
987  C  CB  . GLN   A 131 ? 2.4524 1.3323 2.1481 0.1401  -0.1426 0.0219  151 GLN   A CB  
988  C  CG  . GLN   A 131 ? 2.4792 1.3027 2.1709 0.1047  -0.1790 0.0006  151 GLN   A CG  
989  C  CD  . GLN   A 131 ? 2.5312 1.3606 2.1877 0.1129  -0.1897 -0.0336 151 GLN   A CD  
990  O  OE1 . GLN   A 131 ? 2.4925 1.3634 2.1241 0.1459  -0.1671 -0.0400 151 GLN   A OE1 
991  N  NE2 . GLN   A 131 ? 2.4984 1.2871 2.1542 0.0824  -0.2249 -0.0545 151 GLN   A NE2 
992  N  N   . TYR   A 132 ? 2.3813 1.4291 2.2019 0.0511  -0.1324 0.0787  152 TYR   A N   
993  C  CA  . TYR   A 132 ? 2.3053 1.3917 2.1717 0.0028  -0.1435 0.0886  152 TYR   A CA  
994  C  C   . TYR   A 132 ? 2.2769 1.4007 2.1877 -0.0202 -0.1298 0.1286  152 TYR   A C   
995  O  O   . TYR   A 132 ? 2.2526 1.4039 2.2042 -0.0607 -0.1364 0.1407  152 TYR   A O   
996  C  CB  . TYR   A 132 ? 2.2501 1.4112 2.1239 -0.0003 -0.1384 0.0762  152 TYR   A CB  
997  C  CG  . TYR   A 132 ? 2.3429 1.4649 2.1709 0.0168  -0.1552 0.0380  152 TYR   A CG  
998  C  CD1 . TYR   A 132 ? 2.3902 1.4762 2.2200 -0.0103 -0.1874 0.0169  152 TYR   A CD1 
999  C  CD2 . TYR   A 132 ? 2.3276 1.4483 2.1104 0.0608  -0.1391 0.0235  152 TYR   A CD2 
1000 C  CE1 . TYR   A 132 ? 2.4132 1.4600 2.1937 0.0080  -0.2054 -0.0190 152 TYR   A CE1 
1001 C  CE2 . TYR   A 132 ? 2.3967 1.4789 2.1295 0.0795  -0.1524 -0.0100 152 TYR   A CE2 
1002 C  CZ  . TYR   A 132 ? 2.4168 1.4602 2.1449 0.0540  -0.1867 -0.0319 152 TYR   A CZ  
1003 O  OH  . TYR   A 132 ? 2.4678 1.4702 2.1389 0.0753  -0.2022 -0.0663 152 TYR   A OH  
1004 N  N   . GLY   A 133 ? 2.2500 1.3775 2.1534 0.0061  -0.1110 0.1496  153 GLY   A N   
1005 C  CA  . GLY   A 133 ? 2.1409 1.2837 2.0744 -0.0126 -0.1016 0.1877  153 GLY   A CA  
1006 C  C   . GLY   A 133 ? 2.1943 1.2531 2.1309 -0.0358 -0.1187 0.1969  153 GLY   A C   
1007 O  O   . GLY   A 133 ? 2.1655 1.2368 2.1373 -0.0718 -0.1173 0.2238  153 GLY   A O   
1008 N  N   . ASP   A 134 ? 2.2347 1.2048 2.1338 -0.0152 -0.1342 0.1752  154 ASP   A N   
1009 C  CA  . ASP   A 134 ? 2.3104 1.1895 2.2111 -0.0392 -0.1554 0.1787  154 ASP   A CA  
1010 C  C   . ASP   A 134 ? 2.3571 1.2450 2.2961 -0.0899 -0.1747 0.1714  154 ASP   A C   
1011 O  O   . ASP   A 134 ? 2.3967 1.2589 2.3695 -0.1280 -0.1812 0.1943  154 ASP   A O   
1012 C  CB  . ASP   A 134 ? 2.4692 1.2519 2.3173 -0.0049 -0.1716 0.1480  154 ASP   A CB  
1013 C  CG  . ASP   A 134 ? 2.5623 1.3537 2.3755 0.0511  -0.1512 0.1474  154 ASP   A CG  
1014 O  OD1 . ASP   A 134 ? 2.5650 1.4092 2.3958 0.0603  -0.1297 0.1786  154 ASP   A OD1 
1015 O  OD2 . ASP   A 134 ? 2.6406 1.3874 2.4092 0.0868  -0.1569 0.1155  154 ASP   A OD2 
1016 N  N   . VAL   A 135 ? 2.2588 1.1841 2.1948 -0.0907 -0.1837 0.1409  155 VAL   A N   
1017 C  CA  . VAL   A 135 ? 2.2454 1.1990 2.2249 -0.1364 -0.2011 0.1346  155 VAL   A CA  
1018 C  C   . VAL   A 135 ? 2.1759 1.2104 2.2110 -0.1676 -0.1799 0.1733  155 VAL   A C   
1019 O  O   . VAL   A 135 ? 2.1359 1.1653 2.2170 -0.2107 -0.1878 0.1904  155 VAL   A O   
1020 C  CB  . VAL   A 135 ? 2.3435 1.3327 2.3045 -0.1239 -0.2111 0.0982  155 VAL   A CB  
1021 C  CG1 . VAL   A 135 ? 2.2667 1.2912 2.2766 -0.1688 -0.2310 0.0917  155 VAL   A CG1 
1022 C  CG2 . VAL   A 135 ? 2.3926 1.2984 2.2906 -0.0901 -0.2303 0.0600  155 VAL   A CG2 
1023 N  N   . LEU   A 136 ? 2.1275 1.2373 2.1592 -0.1455 -0.1523 0.1877  156 LEU   A N   
1024 C  CA  . LEU   A 136 ? 2.0128 1.1988 2.0869 -0.1681 -0.1306 0.2228  156 LEU   A CA  
1025 C  C   . LEU   A 136 ? 2.0280 1.1742 2.1165 -0.1857 -0.1230 0.2607  156 LEU   A C   
1026 O  O   . LEU   A 136 ? 2.0050 1.1851 2.1377 -0.2219 -0.1148 0.2872  156 LEU   A O   
1027 C  CB  . LEU   A 136 ? 1.8519 1.1101 1.9105 -0.1357 -0.1061 0.2286  156 LEU   A CB  
1028 C  CG  . LEU   A 136 ? 1.7552 1.0883 1.8438 -0.1492 -0.0826 0.2631  156 LEU   A CG  
1029 C  CD1 . LEU   A 136 ? 1.6820 1.0739 1.8151 -0.1843 -0.0850 0.2608  156 LEU   A CD1 
1030 C  CD2 . LEU   A 136 ? 1.7636 1.1513 1.8312 -0.1134 -0.0642 0.2653  156 LEU   A CD2 
1031 N  N   . VAL   A 137 ? 2.1105 1.1842 2.1615 -0.1590 -0.1242 0.2650  157 VAL   A N   
1032 C  CA  . VAL   A 137 ? 2.1278 1.1537 2.1854 -0.1721 -0.1176 0.3026  157 VAL   A CA  
1033 C  C   . VAL   A 137 ? 2.1724 1.1412 2.2639 -0.2185 -0.1378 0.3049  157 VAL   A C   
1034 O  O   . VAL   A 137 ? 2.1896 1.1727 2.3203 -0.2541 -0.1269 0.3402  157 VAL   A O   
1035 C  CB  . VAL   A 137 ? 2.1930 1.1507 2.2011 -0.1284 -0.1172 0.3035  157 VAL   A CB  
1036 C  CG1 . VAL   A 137 ? 2.1580 1.0275 2.1665 -0.1449 -0.1232 0.3307  157 VAL   A CG1 
1037 C  CG2 . VAL   A 137 ? 2.1584 1.1808 2.1512 -0.0934 -0.0928 0.3210  157 VAL   A CG2 
1038 N  N   . ARG   A 138 ? 2.1505 1.0538 2.2278 -0.2191 -0.1676 0.2674  158 ARG   A N   
1039 C  CA  . ARG   A 138 ? 2.2299 1.0702 2.3406 -0.2636 -0.1924 0.2664  158 ARG   A CA  
1040 C  C   . ARG   A 138 ? 2.2704 1.1863 2.4473 -0.3106 -0.1932 0.2720  158 ARG   A C   
1041 O  O   . ARG   A 138 ? 2.3791 1.2809 2.6060 -0.3552 -0.1954 0.2972  158 ARG   A O   
1042 C  CB  . ARG   A 138 ? 2.3123 1.0644 2.3858 -0.2493 -0.2275 0.2202  158 ARG   A CB  
1043 C  CG  . ARG   A 138 ? 2.4559 1.1182 2.4693 -0.2063 -0.2286 0.2162  158 ARG   A CG  
1044 C  CD  . ARG   A 138 ? 2.4860 1.0527 2.4615 -0.1950 -0.2647 0.1702  158 ARG   A CD  
1045 N  NE  . ARG   A 138 ? 2.3603 0.9703 2.3171 -0.1790 -0.2748 0.1293  158 ARG   A NE  
1046 C  CZ  . ARG   A 138 ? 2.3983 1.0256 2.3034 -0.1277 -0.2625 0.1088  158 ARG   A CZ  
1047 N  NH1 . ARG   A 138 ? 2.4677 1.0774 2.3386 -0.0863 -0.2413 0.1228  158 ARG   A NH1 
1048 N  NH2 . ARG   A 138 ? 2.4008 1.0649 2.2897 -0.1175 -0.2715 0.0748  158 ARG   A NH2 
1049 N  N   . ASN   A 139 ? 2.3332 1.3299 2.5139 -0.3009 -0.1908 0.2500  159 ASN   A N   
1050 C  CA  . ASN   A 139 ? 2.3237 1.4036 2.5681 -0.3395 -0.1875 0.2580  159 ASN   A CA  
1051 C  C   . ASN   A 139 ? 2.3452 1.4844 2.6227 -0.3556 -0.1519 0.3078  159 ASN   A C   
1052 O  O   . ASN   A 139 ? 2.4088 1.5881 2.7484 -0.3977 -0.1473 0.3275  159 ASN   A O   
1053 C  CB  . ASN   A 139 ? 2.3202 1.4723 2.5540 -0.3192 -0.1895 0.2271  159 ASN   A CB  
1054 C  CG  . ASN   A 139 ? 2.4734 1.5746 2.6809 -0.3108 -0.2266 0.1788  159 ASN   A CG  
1055 O  OD1 . ASN   A 139 ? 2.5006 1.5312 2.7207 -0.3350 -0.2565 0.1661  159 ASN   A OD1 
1056 N  ND2 . ASN   A 139 ? 2.3946 1.5295 2.5638 -0.2765 -0.2254 0.1518  159 ASN   A ND2 
1057 N  N   . LEU   A 140 ? 2.2493 1.3962 2.4863 -0.3214 -0.1265 0.3286  160 LEU   A N   
1058 C  CA  . LEU   A 140 ? 2.1696 1.3614 2.4255 -0.3321 -0.0939 0.3764  160 LEU   A CA  
1059 C  C   . LEU   A 140 ? 2.3078 1.4258 2.5788 -0.3597 -0.0929 0.4107  160 LEU   A C   
1060 O  O   . LEU   A 140 ? 2.3569 1.5086 2.6691 -0.3914 -0.0723 0.4490  160 LEU   A O   
1061 C  CB  . LEU   A 140 ? 2.0529 1.2737 2.2592 -0.2859 -0.0721 0.3858  160 LEU   A CB  
1062 C  CG  . LEU   A 140 ? 1.8559 1.1845 2.0724 -0.2779 -0.0506 0.3898  160 LEU   A CG  
1063 C  CD1 . LEU   A 140 ? 1.8168 1.1637 1.9891 -0.2378 -0.0314 0.4059  160 LEU   A CD1 
1064 C  CD2 . LEU   A 140 ? 1.8657 1.2489 2.1368 -0.3183 -0.0335 0.4195  160 LEU   A CD2 
1065 N  N   . ARG   A 141 ? 2.3275 1.3427 2.5643 -0.3470 -0.1136 0.3988  161 ARG   A N   
1066 C  CA  A ARG   A 141 ? 2.3892 1.3230 2.6376 -0.3726 -0.1147 0.4312  161 ARG   A CA  
1067 C  CA  B ARG   A 141 ? 2.3894 1.3229 2.6377 -0.3726 -0.1148 0.4311  161 ARG   A CA  
1068 C  C   . ARG   A 141 ? 2.5312 1.4577 2.8500 -0.4314 -0.1298 0.4339  161 ARG   A C   
1069 O  O   . ARG   A 141 ? 2.6098 1.5080 2.9614 -0.4656 -0.1186 0.4744  161 ARG   A O   
1070 C  CB  A ARG   A 141 ? 2.3477 1.1697 2.5410 -0.3417 -0.1359 0.4128  161 ARG   A CB  
1071 C  CB  B ARG   A 141 ? 2.3484 1.1695 2.5417 -0.3419 -0.1361 0.4128  161 ARG   A CB  
1072 C  CG  A ARG   A 141 ? 2.3743 1.1107 2.5580 -0.3499 -0.1298 0.4531  161 ARG   A CG  
1073 C  CG  B ARG   A 141 ? 2.3865 1.1060 2.5891 -0.3685 -0.1436 0.4411  161 ARG   A CG  
1074 C  CD  A ARG   A 141 ? 2.3762 1.0394 2.4906 -0.2964 -0.1359 0.4423  161 ARG   A CD  
1075 C  CD  B ARG   A 141 ? 2.3914 1.0200 2.5291 -0.3243 -0.1471 0.4434  161 ARG   A CD  
1076 N  NE  A ARG   A 141 ? 2.3575 0.9944 2.4426 -0.2696 -0.1624 0.3870  161 ARG   A NE  
1077 N  NE  B ARG   A 141 ? 2.3220 0.9965 2.4279 -0.2891 -0.1160 0.4752  161 ARG   A NE  
1078 C  CZ  A ARG   A 141 ? 2.3572 0.9583 2.3845 -0.2161 -0.1655 0.3669  161 ARG   A CZ  
1079 C  CZ  B ARG   A 141 ? 2.3126 1.0151 2.3730 -0.2366 -0.1115 0.4561  161 ARG   A CZ  
1080 N  NH1 A ARG   A 141 ? 2.3420 0.9298 2.3372 -0.1825 -0.1475 0.3954  161 ARG   A NH1 
1081 N  NH1 B ARG   A 141 ? 2.3152 1.0028 2.3515 -0.2104 -0.1315 0.4076  161 ARG   A NH1 
1082 N  NH2 A ARG   A 141 ? 2.3692 0.9496 2.3705 -0.1942 -0.1869 0.3174  161 ARG   A NH2 
1083 N  NH2 B ARG   A 141 ? 2.3294 1.0757 2.3677 -0.2094 -0.0864 0.4869  161 ARG   A NH2 
1084 N  N   . ARG   A 142 ? 2.6917 1.6448 3.0363 -0.4442 -0.1553 0.3930  162 ARG   A N   
1085 C  CA  . ARG   A 142 ? 2.7791 1.7385 3.2000 -0.5007 -0.1720 0.3944  162 ARG   A CA  
1086 C  C   . ARG   A 142 ? 2.8356 1.8973 3.3177 -0.5304 -0.1376 0.4344  162 ARG   A C   
1087 O  O   . ARG   A 142 ? 2.8367 1.9091 3.3681 -0.5679 -0.1277 0.4534  162 ARG   A O   
1088 C  CB  . ARG   A 142 ? 2.7262 1.6935 3.1559 -0.5026 -0.2100 0.3398  162 ARG   A CB  
1089 C  CG  . ARG   A 142 ? 2.7527 1.7412 3.2653 -0.5580 -0.2298 0.3360  162 ARG   A CG  
1090 C  CD  . ARG   A 142 ? 2.7968 1.7742 3.3127 -0.5596 -0.2760 0.2814  162 ARG   A CD  
1091 N  NE  . ARG   A 142 ? 2.7495 1.8113 3.2420 -0.5269 -0.2684 0.2585  162 ARG   A NE  
1092 C  CZ  . ARG   A 142 ? 2.6968 1.7335 3.1165 -0.4805 -0.2810 0.2204  162 ARG   A CZ  
1093 N  NH1 . ARG   A 142 ? 2.7691 1.7004 3.1302 -0.4582 -0.3025 0.1984  162 ARG   A NH1 
1094 N  NH2 . ARG   A 142 ? 2.6433 1.7612 3.0485 -0.4551 -0.2709 0.2048  162 ARG   A NH2 
1095 N  N   . GLU   A 143 ? 2.5782 1.7319 3.0424 -0.5020 -0.1119 0.4362  163 GLU   A N   
1096 C  CA  . GLU   A 143 ? 2.5706 1.8202 3.0814 -0.5221 -0.0760 0.4736  163 GLU   A CA  
1097 C  C   . GLU   A 143 ? 2.6430 1.8779 3.1307 -0.5165 -0.0397 0.5269  163 GLU   A C   
1098 O  O   . GLU   A 143 ? 2.6245 1.9209 3.1493 -0.5382 -0.0080 0.5616  163 GLU   A O   
1099 C  CB  . GLU   A 143 ? 2.6091 1.9580 3.1072 -0.4931 -0.0648 0.4529  163 GLU   A CB  
1100 C  CG  . GLU   A 143 ? 2.6702 2.0656 3.2131 -0.5095 -0.0910 0.4140  163 GLU   A CG  
1101 C  CD  . GLU   A 143 ? 2.7095 2.1749 3.3420 -0.5563 -0.0797 0.4364  163 GLU   A CD  
1102 O  OE1 . GLU   A 143 ? 2.6176 2.0816 3.2809 -0.5824 -0.0534 0.4824  163 GLU   A OE1 
1103 O  OE2 . GLU   A 143 ? 2.7983 2.3218 3.4709 -0.5658 -0.0961 0.4092  163 GLU   A OE2 
1104 N  N   . ALA   A 144 ? 2.5839 1.7441 3.0040 -0.4819 -0.0419 0.5300  164 ALA   A N   
1105 C  CA  . ALA   A 144 ? 2.5292 1.6665 2.9218 -0.4743 -0.0115 0.5810  164 ALA   A CA  
1106 C  C   . ALA   A 144 ? 2.6724 1.7525 3.0827 -0.5058 -0.0077 0.5971  164 ALA   A C   
1107 O  O   . ALA   A 144 ? 2.6587 1.7634 3.0728 -0.5172 0.0260  0.6364  164 ALA   A O   
1108 C  CB  . ALA   A 144 ? 2.4552 1.5423 2.7668 -0.4199 -0.0155 0.5722  164 ALA   A CB  
1109 N  N   . GLU   A 145 ? 2.7435 1.7452 3.1612 -0.5194 -0.0420 0.5664  165 GLU   A N   
1110 C  CA  . GLU   A 145 ? 2.7867 1.7297 3.2253 -0.5520 -0.0421 0.5779  165 GLU   A CA  
1111 C  C   . GLU   A 145 ? 2.7746 1.7877 3.2933 -0.6010 -0.0322 0.5840  165 GLU   A C   
1112 O  O   . GLU   A 145 ? 2.8868 1.8597 3.4331 -0.6334 -0.0314 0.5947  165 GLU   A O   
1113 C  CB  . GLU   A 145 ? 2.8694 1.7068 3.2877 -0.5478 -0.0838 0.5389  165 GLU   A CB  
1114 C  CG  . GLU   A 145 ? 2.9180 1.6689 3.2577 -0.5011 -0.0880 0.5407  165 GLU   A CG  
1115 C  CD  . GLU   A 145 ? 2.9144 1.5863 3.2245 -0.4811 -0.1304 0.4905  165 GLU   A CD  
1116 O  OE1 . GLU   A 145 ? 2.8613 1.5617 3.1984 -0.4919 -0.1563 0.4525  165 GLU   A OE1 
1117 O  OE2 . GLU   A 145 ? 2.9821 1.5631 3.2385 -0.4519 -0.1375 0.4883  165 GLU   A OE2 
1118 N  N   . THR   A 146 ? 2.7316 1.8479 3.2897 -0.6062 -0.0249 0.5774  166 THR   A N   
1119 C  CA  . THR   A 146 ? 2.7029 1.9029 3.3379 -0.6461 -0.0095 0.5869  166 THR   A CA  
1120 C  C   . THR   A 146 ? 2.6180 1.9173 3.2490 -0.6298 0.0314  0.6159  166 THR   A C   
1121 O  O   . THR   A 146 ? 2.5274 1.8949 3.1686 -0.6163 0.0267  0.5972  166 THR   A O   
1122 C  CB  . THR   A 146 ? 2.6325 1.8602 3.3230 -0.6667 -0.0476 0.5416  166 THR   A CB  
1123 O  OG1 . THR   A 146 ? 2.5525 1.8182 3.2211 -0.6369 -0.0607 0.5163  166 THR   A OG1 
1124 C  CG2 . THR   A 146 ? 2.6808 1.8050 3.3656 -0.6787 -0.0901 0.5100  166 THR   A CG2 
1125 N  N   . GLY   A 147 ? 2.6541 1.9579 3.2659 -0.6299 0.0708  0.6604  167 GLY   A N   
1126 C  CA  . GLY   A 147 ? 2.5938 1.9762 3.1828 -0.6075 0.1103  0.6893  167 GLY   A CA  
1127 C  C   . GLY   A 147 ? 2.5040 2.0025 3.1468 -0.6154 0.1213  0.6793  167 GLY   A C   
1128 O  O   . GLY   A 147 ? 2.4431 2.0084 3.1143 -0.6288 0.1563  0.7053  167 GLY   A O   
1129 N  N   . LYS   A 148 ? 2.5281 2.0497 3.1820 -0.6049 0.0922  0.6415  168 LYS   A N   
1130 C  CA  . LYS   A 148 ? 2.4318 2.0586 3.1335 -0.6083 0.0974  0.6270  168 LYS   A CA  
1131 C  C   . LYS   A 148 ? 2.3301 1.9891 2.9816 -0.5670 0.1016  0.6212  168 LYS   A C   
1132 O  O   . LYS   A 148 ? 2.4006 2.0078 3.0182 -0.5481 0.0715  0.5969  168 LYS   A O   
1133 C  CB  . LYS   A 148 ? 2.4583 2.0866 3.2207 -0.6344 0.0560  0.5854  168 LYS   A CB  
1134 C  CG  . LYS   A 148 ? 2.3832 2.1200 3.2039 -0.6411 0.0589  0.5699  168 LYS   A CG  
1135 C  CD  . LYS   A 148 ? 2.4195 2.1500 3.2980 -0.6675 0.0143  0.5295  168 LYS   A CD  
1136 C  CE  . LYS   A 148 ? 2.3264 2.1601 3.2557 -0.6672 0.0115  0.5099  168 LYS   A CE  
1137 N  NZ  . LYS   A 148 ? 2.2920 2.2165 3.2708 -0.6799 0.0529  0.5383  168 LYS   A NZ  
1138 N  N   . PRO   A 149 ? 2.1141 1.8542 2.7568 -0.5508 0.1378  0.6421  169 PRO   A N   
1139 C  CA  . PRO   A 149 ? 1.9702 1.7414 2.5627 -0.5109 0.1419  0.6363  169 PRO   A CA  
1140 C  C   . PRO   A 149 ? 1.9031 1.6926 2.4993 -0.4973 0.1065  0.5794  169 PRO   A C   
1141 O  O   . PRO   A 149 ? 1.9310 1.7480 2.5921 -0.5253 0.0886  0.5596  169 PRO   A O   
1142 C  CB  . PRO   A 149 ? 1.8335 1.6983 2.4312 -0.5029 0.1842  0.6600  169 PRO   A CB  
1143 C  CG  . PRO   A 149 ? 1.9389 1.7892 2.5531 -0.5271 0.2091  0.6909  169 PRO   A CG  
1144 C  CD  . PRO   A 149 ? 2.0729 1.8713 2.7412 -0.5650 0.1785  0.6735  169 PRO   A CD  
1145 N  N   . VAL   A 150 ? 1.8387 1.6132 2.3651 -0.4536 0.0962  0.5542  170 VAL   A N   
1146 C  CA  . VAL   A 150 ? 1.8441 1.6095 2.3571 -0.4365 0.0614  0.5026  170 VAL   A CA  
1147 C  C   . VAL   A 150 ? 1.7742 1.6216 2.2719 -0.4080 0.0704  0.4830  170 VAL   A C   
1148 O  O   . VAL   A 150 ? 1.7196 1.5932 2.1734 -0.3801 0.0934  0.4981  170 VAL   A O   
1149 C  CB  . VAL   A 150 ? 1.8226 1.5003 2.2712 -0.4088 0.0414  0.4877  170 VAL   A CB  
1150 C  CG1 . VAL   A 150 ? 1.6979 1.3690 2.1279 -0.3884 0.0104  0.4367  170 VAL   A CG1 
1151 C  CG2 . VAL   A 150 ? 1.9863 1.5750 2.4476 -0.4356 0.0305  0.5055  170 VAL   A CG2 
1152 N  N   . THR   A 151 ? 1.8079 1.6914 2.3392 -0.4141 0.0499  0.4485  171 THR   A N   
1153 C  CA  . THR   A 151 ? 1.7965 1.7397 2.3062 -0.3841 0.0503  0.4222  171 THR   A CA  
1154 C  C   . THR   A 151 ? 1.7526 1.6449 2.2011 -0.3512 0.0282  0.3912  171 THR   A C   
1155 O  O   . THR   A 151 ? 1.7497 1.5860 2.1971 -0.3570 -0.0008 0.3672  171 THR   A O   
1156 C  CB  . THR   A 151 ? 1.8921 1.8923 2.4617 -0.4022 0.0367  0.3999  171 THR   A CB  
1157 O  OG1 . THR   A 151 ? 1.9970 1.9469 2.5698 -0.4084 -0.0024 0.3651  171 THR   A OG1 
1158 C  CG2 . THR   A 151 ? 1.9131 1.9532 2.5579 -0.4417 0.0542  0.4306  171 THR   A CG2 
1159 N  N   . LEU   A 152 ? 1.7569 1.6689 2.1553 -0.3162 0.0416  0.3911  172 LEU   A N   
1160 C  CA  . LEU   A 152 ? 1.7550 1.6173 2.0976 -0.2851 0.0273  0.3714  172 LEU   A CA  
1161 C  C   . LEU   A 152 ? 1.8101 1.6785 2.1464 -0.2720 0.0041  0.3292  172 LEU   A C   
1162 O  O   . LEU   A 152 ? 1.7810 1.5929 2.0872 -0.2581 -0.0144 0.3090  172 LEU   A O   
1163 C  CB  . LEU   A 152 ? 1.6358 1.5188 1.9331 -0.2541 0.0472  0.3867  172 LEU   A CB  
1164 C  CG  . LEU   A 152 ? 1.5589 1.4106 1.8411 -0.2578 0.0651  0.4271  172 LEU   A CG  
1165 C  CD1 . LEU   A 152 ? 1.4220 1.3010 1.6591 -0.2260 0.0809  0.4393  172 LEU   A CD1 
1166 C  CD2 . LEU   A 152 ? 1.5415 1.3048 1.8075 -0.2590 0.0484  0.4274  172 LEU   A CD2 
1167 N  N   . LYS   A 153 ? 1.8048 1.7391 2.1659 -0.2740 0.0057  0.3162  173 LYS   A N   
1168 C  CA  . LYS   A 153 ? 1.8824 1.8221 2.2308 -0.2584 -0.0144 0.2790  173 LYS   A CA  
1169 C  C   . LYS   A 153 ? 1.9200 1.8085 2.2808 -0.2739 -0.0444 0.2564  173 LYS   A C   
1170 O  O   . LYS   A 153 ? 1.8784 1.7420 2.2087 -0.2554 -0.0624 0.2271  173 LYS   A O   
1171 C  CB  . LYS   A 153 ? 1.9057 1.9231 2.2799 -0.2576 -0.0076 0.2717  173 LYS   A CB  
1172 C  CG  . LYS   A 153 ? 1.8331 1.8883 2.2720 -0.2902 -0.0081 0.2800  173 LYS   A CG  
1173 C  CD  . LYS   A 153 ? 1.7317 1.8630 2.1926 -0.2831 -0.0018 0.2702  173 LYS   A CD  
1174 C  CE  . LYS   A 153 ? 1.7761 1.9525 2.3092 -0.3139 -0.0023 0.2781  173 LYS   A CE  
1175 N  NZ  . LYS   A 153 ? 1.7860 2.0370 2.3407 -0.3031 0.0041  0.2682  173 LYS   A NZ  
1176 N  N   . ASP   A 154 ? 1.8157 1.6862 2.2198 -0.3075 -0.0506 0.2696  174 ASP   A N   
1177 C  CA  . ASP   A 154 ? 1.7598 1.5744 2.1751 -0.3240 -0.0832 0.2472  174 ASP   A CA  
1178 C  C   . ASP   A 154 ? 1.7469 1.4747 2.1095 -0.3066 -0.0931 0.2400  174 ASP   A C   
1179 O  O   . ASP   A 154 ? 1.7176 1.4111 2.0417 -0.2852 -0.1120 0.2093  174 ASP   A O   
1180 C  CB  . ASP   A 154 ? 1.7638 1.5819 2.2463 -0.3678 -0.0874 0.2655  174 ASP   A CB  
1181 C  CG  . ASP   A 154 ? 1.7919 1.6981 2.3346 -0.3848 -0.0800 0.2696  174 ASP   A CG  
1182 O  OD1 . ASP   A 154 ? 1.7993 1.7494 2.3313 -0.3647 -0.0844 0.2476  174 ASP   A OD1 
1183 O  OD2 . ASP   A 154 ? 1.7826 1.7138 2.3847 -0.4177 -0.0688 0.2958  174 ASP   A OD2 
1184 N  N   . VAL   A 155 ? 1.8161 1.5077 2.1751 -0.3137 -0.0790 0.2696  175 VAL   A N   
1185 C  CA  . VAL   A 155 ? 1.8409 1.4472 2.1538 -0.2968 -0.0877 0.2659  175 VAL   A CA  
1186 C  C   . VAL   A 155 ? 1.8022 1.4081 2.0579 -0.2527 -0.0829 0.2485  175 VAL   A C   
1187 O  O   . VAL   A 155 ? 1.7817 1.3286 1.9992 -0.2330 -0.0989 0.2254  175 VAL   A O   
1188 C  CB  . VAL   A 155 ? 1.6799 1.2575 1.9975 -0.3085 -0.0689 0.3063  175 VAL   A CB  
1189 C  CG1 . VAL   A 155 ? 1.7098 1.3618 2.0377 -0.3060 -0.0362 0.3370  175 VAL   A CG1 
1190 C  CG2 . VAL   A 155 ? 1.7041 1.2077 1.9668 -0.2794 -0.0713 0.3059  175 VAL   A CG2 
1191 N  N   . PHE   A 156 ? 1.8143 1.4865 2.0646 -0.2364 -0.0607 0.2589  176 PHE   A N   
1192 C  CA  . PHE   A 156 ? 1.8460 1.5254 2.0518 -0.1981 -0.0559 0.2438  176 PHE   A CA  
1193 C  C   . PHE   A 156 ? 1.9261 1.6172 2.1234 -0.1890 -0.0721 0.2085  176 PHE   A C   
1194 O  O   . PHE   A 156 ? 1.9015 1.5562 2.0596 -0.1633 -0.0795 0.1880  176 PHE   A O   
1195 C  CB  . PHE   A 156 ? 1.7623 1.5056 1.9663 -0.1856 -0.0312 0.2640  176 PHE   A CB  
1196 C  CG  . PHE   A 156 ? 1.7522 1.4732 1.9382 -0.1760 -0.0167 0.2935  176 PHE   A CG  
1197 C  CD1 . PHE   A 156 ? 1.7519 1.3988 1.9147 -0.1671 -0.0249 0.2956  176 PHE   A CD1 
1198 C  CD2 . PHE   A 156 ? 1.7175 1.4888 1.9056 -0.1731 0.0039  0.3183  176 PHE   A CD2 
1199 C  CE1 . PHE   A 156 ? 1.6865 1.3109 1.8310 -0.1558 -0.0133 0.3236  176 PHE   A CE1 
1200 C  CE2 . PHE   A 156 ? 1.6757 1.4247 1.8421 -0.1619 0.0150  0.3458  176 PHE   A CE2 
1201 C  CZ  . PHE   A 156 ? 1.6334 1.3094 1.7793 -0.1533 0.0061  0.3493  176 PHE   A CZ  
1202 N  N   . GLY   A 157 ? 1.7695 1.5124 2.0020 -0.2076 -0.0765 0.2022  177 GLY   A N   
1203 C  CA  . GLY   A 157 ? 1.7294 1.4815 1.9521 -0.1988 -0.0937 0.1705  177 GLY   A CA  
1204 C  C   . GLY   A 157 ? 1.7334 1.4133 1.9336 -0.1979 -0.1209 0.1453  177 GLY   A C   
1205 O  O   . GLY   A 157 ? 1.7504 1.4149 1.9138 -0.1754 -0.1307 0.1198  177 GLY   A O   
1206 N  N   . ALA   A 158 ? 1.7563 1.3880 1.9754 -0.2217 -0.1333 0.1523  178 ALA   A N   
1207 C  CA  . ALA   A 158 ? 1.8507 1.4025 2.0418 -0.2187 -0.1609 0.1273  178 ALA   A CA  
1208 C  C   . ALA   A 158 ? 1.7952 1.2965 1.9258 -0.1809 -0.1525 0.1207  178 ALA   A C   
1209 O  O   . ALA   A 158 ? 1.8827 1.3466 1.9702 -0.1584 -0.1664 0.0922  178 ALA   A O   
1210 C  CB  . ALA   A 158 ? 2.0514 1.5591 2.2790 -0.2540 -0.1752 0.1391  178 ALA   A CB  
1211 N  N   . TYR   A 159 ? 1.8485 1.3493 1.9746 -0.1716 -0.1295 0.1475  179 TYR   A N   
1212 C  CA  . TYR   A 159 ? 1.7835 1.2474 1.8605 -0.1338 -0.1196 0.1436  179 TYR   A CA  
1213 C  C   . TYR   A 159 ? 1.7872 1.2937 1.8389 -0.1047 -0.1091 0.1283  179 TYR   A C   
1214 O  O   . TYR   A 159 ? 1.7774 1.2470 1.7862 -0.0759 -0.1119 0.1081  179 TYR   A O   
1215 C  CB  . TYR   A 159 ? 1.6965 1.1635 1.7783 -0.1290 -0.0983 0.1771  179 TYR   A CB  
1216 C  CG  . TYR   A 159 ? 1.7098 1.1688 1.7528 -0.0876 -0.0842 0.1756  179 TYR   A CG  
1217 C  CD1 . TYR   A 159 ? 1.7368 1.1219 1.7429 -0.0641 -0.0916 0.1634  179 TYR   A CD1 
1218 C  CD2 . TYR   A 159 ? 1.6450 1.1710 1.6908 -0.0714 -0.0643 0.1854  179 TYR   A CD2 
1219 C  CE1 . TYR   A 159 ? 1.7356 1.1199 1.7132 -0.0251 -0.0773 0.1628  179 TYR   A CE1 
1220 C  CE2 . TYR   A 159 ? 1.5500 1.0744 1.5698 -0.0356 -0.0525 0.1844  179 TYR   A CE2 
1221 C  CZ  . TYR   A 159 ? 1.5590 1.0156 1.5471 -0.0123 -0.0579 0.1740  179 TYR   A CZ  
1222 O  OH  . TYR   A 159 ? 1.6000 1.0613 1.5688 0.0245  -0.0446 0.1740  179 TYR   A OH  
1223 N  N   . SER   A 160 ? 1.6828 1.2659 1.7600 -0.1110 -0.0955 0.1388  180 SER   A N   
1224 C  CA  . SER   A 160 ? 1.6534 1.2770 1.7116 -0.0874 -0.0860 0.1262  180 SER   A CA  
1225 C  C   . SER   A 160 ? 1.6948 1.2904 1.7252 -0.0794 -0.1048 0.0947  180 SER   A C   
1226 O  O   . SER   A 160 ? 1.6552 1.2427 1.6485 -0.0504 -0.0978 0.0816  180 SER   A O   
1227 C  CB  . SER   A 160 ? 1.5719 1.2744 1.6638 -0.1002 -0.0744 0.1389  180 SER   A CB  
1228 O  OG  . SER   A 160 ? 1.5552 1.2912 1.6311 -0.0813 -0.0686 0.1255  180 SER   A OG  
1229 N  N   . MET   A 161 ? 1.7397 1.3205 1.7880 -0.1045 -0.1288 0.0831  181 MET   A N   
1230 C  CA  . MET   A 161 ? 1.7826 1.3297 1.7993 -0.0962 -0.1520 0.0518  181 MET   A CA  
1231 C  C   . MET   A 161 ? 1.8650 1.3307 1.8296 -0.0725 -0.1593 0.0356  181 MET   A C   
1232 O  O   . MET   A 161 ? 1.8875 1.3302 1.8037 -0.0456 -0.1624 0.0138  181 MET   A O   
1233 C  CB  . MET   A 161 ? 1.8102 1.3605 1.8646 -0.1300 -0.1803 0.0431  181 MET   A CB  
1234 C  CG  . MET   A 161 ? 1.8002 1.3154 1.8210 -0.1220 -0.2102 0.0094  181 MET   A CG  
1235 S  SD  . MET   A 161 ? 1.9741 1.5332 1.9600 -0.0927 -0.1994 -0.0023 181 MET   A SD  
1236 C  CE  . MET   A 161 ? 1.8549 1.5083 1.9094 -0.1186 -0.1905 0.0173  181 MET   A CE  
1237 N  N   . ASP   A 162 ? 2.0039 1.4234 1.9749 -0.0802 -0.1611 0.0468  182 ASP   A N   
1238 C  CA  . ASP   A 162 ? 2.1025 1.4397 2.0238 -0.0558 -0.1685 0.0309  182 ASP   A CA  
1239 C  C   . ASP   A 162 ? 2.0552 1.3987 1.9353 -0.0130 -0.1428 0.0297  182 ASP   A C   
1240 O  O   . ASP   A 162 ? 2.0862 1.3820 1.9133 0.0157  -0.1474 0.0064  182 ASP   A O   
1241 C  CB  . ASP   A 162 ? 2.1854 1.4761 2.1246 -0.0706 -0.1711 0.0487  182 ASP   A CB  
1242 C  CG  . ASP   A 162 ? 2.2450 1.5118 2.2219 -0.1124 -0.1995 0.0463  182 ASP   A CG  
1243 O  OD1 . ASP   A 162 ? 2.2751 1.5398 2.2512 -0.1232 -0.2247 0.0218  182 ASP   A OD1 
1244 O  OD2 . ASP   A 162 ? 2.2742 1.5240 2.2825 -0.1346 -0.1971 0.0699  182 ASP   A OD2 
1245 N  N   . VAL   A 163 ? 1.9137 1.3164 1.8177 -0.0078 -0.1156 0.0547  183 VAL   A N   
1246 C  CA  . VAL   A 163 ? 1.8246 1.2444 1.7023 0.0292  -0.0909 0.0558  183 VAL   A CA  
1247 C  C   . VAL   A 163 ? 1.8192 1.2626 1.6719 0.0424  -0.0889 0.0373  183 VAL   A C   
1248 O  O   . VAL   A 163 ? 1.9159 1.3334 1.7242 0.0750  -0.0798 0.0235  183 VAL   A O   
1249 C  CB  . VAL   A 163 ? 1.7317 1.2131 1.6458 0.0280  -0.0678 0.0853  183 VAL   A CB  
1250 C  CG1 . VAL   A 163 ? 1.6290 1.1293 1.5254 0.0644  -0.0442 0.0870  183 VAL   A CG1 
1251 C  CG2 . VAL   A 163 ? 1.7498 1.2050 1.6837 0.0148  -0.0705 0.1061  183 VAL   A CG2 
1252 N  N   . ILE   A 164 ? 1.7176 1.2099 1.5972 0.0188  -0.0962 0.0379  184 ILE   A N   
1253 C  CA  . ILE   A 164 ? 1.7486 1.2669 1.6068 0.0304  -0.0937 0.0245  184 ILE   A CA  
1254 C  C   . ILE   A 164 ? 1.8610 1.3152 1.6609 0.0495  -0.1104 -0.0043 184 ILE   A C   
1255 O  O   . ILE   A 164 ? 1.8886 1.3283 1.6444 0.0821  -0.0945 -0.0120 184 ILE   A O   
1256 C  CB  . ILE   A 164 ? 1.6183 1.1904 1.5154 0.0015  -0.1044 0.0278  184 ILE   A CB  
1257 C  CG1 . ILE   A 164 ? 1.6147 1.2539 1.5559 -0.0081 -0.0833 0.0536  184 ILE   A CG1 
1258 C  CG2 . ILE   A 164 ? 1.6596 1.2408 1.5267 0.0135  -0.1099 0.0104  184 ILE   A CG2 
1259 C  CD1 . ILE   A 164 ? 1.5707 1.2621 1.5487 -0.0326 -0.0914 0.0568  184 ILE   A CD1 
1260 N  N   . THR   A 165 ? 1.8426 1.2569 1.6414 0.0297  -0.1428 -0.0205 185 THR   A N   
1261 C  CA  . THR   A 165 ? 1.8745 1.2255 1.6139 0.0470  -0.1651 -0.0513 185 THR   A CA  
1262 C  C   . THR   A 165 ? 1.9876 1.2763 1.6732 0.0829  -0.1532 -0.0602 185 THR   A C   
1263 O  O   . THR   A 165 ? 2.0719 1.3241 1.6947 0.1130  -0.1539 -0.0809 185 THR   A O   
1264 C  CB  . THR   A 165 ? 1.9758 1.2927 1.7332 0.0161  -0.2056 -0.0664 185 THR   A CB  
1265 O  OG1 . THR   A 165 ? 2.1385 1.4201 1.9208 0.0009  -0.2092 -0.0561 185 THR   A OG1 
1266 C  CG2 . THR   A 165 ? 1.7252 1.1100 1.5401 -0.0168 -0.2154 -0.0574 185 THR   A CG2 
1267 N  N   . SER   A 166 ? 2.0061 1.2821 1.7127 0.0831  -0.1411 -0.0440 186 SER   A N   
1268 C  CA  . SER   A 166 ? 2.1031 1.3249 1.7635 0.1207  -0.1274 -0.0508 186 SER   A CA  
1269 C  C   . SER   A 166 ? 2.0590 1.3252 1.7065 0.1533  -0.0893 -0.0399 186 SER   A C   
1270 O  O   . SER   A 166 ? 2.1133 1.3474 1.7040 0.1894  -0.0785 -0.0555 186 SER   A O   
1271 C  CB  . SER   A 166 ? 2.1199 1.3139 1.8083 0.1117  -0.1277 -0.0352 186 SER   A CB  
1272 O  OG  . SER   A 166 ? 2.0139 1.2775 1.7601 0.0950  -0.1081 -0.0035 186 SER   A OG  
1273 N  N   . THR   A 167 ? 1.9476 1.2875 1.6477 0.1414  -0.0683 -0.0130 187 THR   A N   
1274 C  CA  . THR   A 167 ? 1.9598 1.3451 1.6603 0.1681  -0.0334 -0.0003 187 THR   A CA  
1275 C  C   . THR   A 167 ? 1.9527 1.3643 1.6277 0.1774  -0.0245 -0.0083 187 THR   A C   
1276 O  O   . THR   A 167 ? 1.9362 1.3798 1.6079 0.2004  0.0054  0.0011  187 THR   A O   
1277 C  CB  . THR   A 167 ? 1.7697 1.2229 1.5334 0.1513  -0.0187 0.0287  187 THR   A CB  
1278 O  OG1 . THR   A 167 ? 1.6515 1.1446 1.4509 0.1149  -0.0334 0.0345  187 THR   A OG1 
1279 C  CG2 . THR   A 167 ? 1.8644 1.2908 1.6453 0.1523  -0.0205 0.0408  187 THR   A CG2 
1280 N  N   . SER   A 168 ? 1.9066 1.3066 1.5660 0.1603  -0.0497 -0.0239 188 SER   A N   
1281 C  CA  . SER   A 168 ? 1.9632 1.3854 1.5959 0.1692  -0.0432 -0.0297 188 SER   A CA  
1282 C  C   . SER   A 168 ? 2.0702 1.4281 1.6281 0.1902  -0.0602 -0.0580 188 SER   A C   
1283 O  O   . SER   A 168 ? 2.0828 1.4463 1.6008 0.2120  -0.0448 -0.0608 188 SER   A O   
1284 C  CB  . SER   A 168 ? 1.9275 1.4041 1.6056 0.1351  -0.0566 -0.0218 188 SER   A CB  
1285 O  OG  . SER   A 168 ? 1.9179 1.3794 1.6226 0.1049  -0.0881 -0.0279 188 SER   A OG  
1286 N  N   . PHE   A 169 ? 2.0793 1.3737 1.6145 0.1850  -0.0919 -0.0790 189 PHE   A N   
1287 C  CA  . PHE   A 169 ? 2.1827 1.4131 1.6425 0.2053  -0.1137 -0.1092 189 PHE   A CA  
1288 C  C   . PHE   A 169 ? 2.2519 1.3975 1.6689 0.2214  -0.1308 -0.1310 189 PHE   A C   
1289 O  O   . PHE   A 169 ? 2.3704 1.4554 1.7240 0.2351  -0.1571 -0.1601 189 PHE   A O   
1290 C  CB  . PHE   A 169 ? 2.1764 1.4148 1.6468 0.1763  -0.1520 -0.1218 189 PHE   A CB  
1291 C  CG  . PHE   A 169 ? 2.1339 1.4532 1.6556 0.1557  -0.1407 -0.1009 189 PHE   A CG  
1292 C  CD1 . PHE   A 169 ? 2.1117 1.4565 1.6027 0.1761  -0.1193 -0.0956 189 PHE   A CD1 
1293 C  CD2 . PHE   A 169 ? 2.0283 1.3951 1.6266 0.1170  -0.1502 -0.0859 189 PHE   A CD2 
1294 C  CE1 . PHE   A 169 ? 2.0465 1.4592 1.5827 0.1582  -0.1105 -0.0776 189 PHE   A CE1 
1295 C  CE2 . PHE   A 169 ? 1.9743 1.4117 1.6153 0.1014  -0.1401 -0.0689 189 PHE   A CE2 
1296 C  CZ  . PHE   A 169 ? 1.9456 1.4041 1.5557 0.1219  -0.1216 -0.0657 189 PHE   A CZ  
1297 N  N   . GLY   A 170 ? 2.3047 1.4402 1.7510 0.2216  -0.1194 -0.1192 190 GLY   A N   
1298 C  CA  . GLY   A 170 ? 2.2867 1.3376 1.6986 0.2332  -0.1391 -0.1392 190 GLY   A CA  
1299 C  C   . GLY   A 170 ? 2.3909 1.3977 1.8142 0.1985  -0.1881 -0.1576 190 GLY   A C   
1300 O  O   . GLY   A 170 ? 2.5254 1.4546 1.9216 0.2047  -0.2090 -0.1757 190 GLY   A O   
1301 N  N   . VAL   A 171 ? 2.2867 1.3400 1.7520 0.1627  -0.2077 -0.1540 191 VAL   A N   
1302 C  CA  . VAL   A 171 ? 2.3787 1.4035 1.8731 0.1245  -0.2530 -0.1673 191 VAL   A CA  
1303 C  C   . VAL   A 171 ? 2.3587 1.3925 1.9221 0.0938  -0.2499 -0.1435 191 VAL   A C   
1304 O  O   . VAL   A 171 ? 2.2855 1.3854 1.8987 0.0851  -0.2196 -0.1123 191 VAL   A O   
1305 C  CB  . VAL   A 171 ? 2.4153 1.4960 1.9389 0.0987  -0.2717 -0.1685 191 VAL   A CB  
1306 C  CG1 . VAL   A 171 ? 2.4292 1.5040 2.0106 0.0516  -0.3136 -0.1740 191 VAL   A CG1 
1307 C  CG2 . VAL   A 171 ? 2.4887 1.5420 1.9342 0.1292  -0.2837 -0.1953 191 VAL   A CG2 
1308 N  N   . ASN   A 172 ? 2.4323 1.3969 1.9972 0.0768  -0.2825 -0.1579 192 ASN   A N   
1309 C  CA  . ASN   A 172 ? 2.4794 1.4310 2.0941 0.0542  -0.2787 -0.1359 192 ASN   A CA  
1310 C  C   . ASN   A 172 ? 2.4871 1.4247 2.1539 0.0046  -0.3180 -0.1395 192 ASN   A C   
1311 O  O   . ASN   A 172 ? 2.5100 1.3741 2.1475 0.0005  -0.3570 -0.1698 192 ASN   A O   
1312 C  CB  . ASN   A 172 ? 2.5011 1.3687 2.0630 0.0890  -0.2732 -0.1463 192 ASN   A CB  
1313 C  CG  . ASN   A 172 ? 2.4981 1.3857 2.0157 0.1388  -0.2323 -0.1418 192 ASN   A CG  
1314 O  OD1 . ASN   A 172 ? 2.4510 1.3898 2.0027 0.1443  -0.1985 -0.1121 192 ASN   A OD1 
1315 N  ND2 . ASN   A 172 ? 2.5360 1.3856 1.9781 0.1754  -0.2352 -0.1705 192 ASN   A ND2 
1316 N  N   . ILE   A 173 ? 2.4627 1.4716 2.2073 -0.0328 -0.3081 -0.1092 193 ILE   A N   
1317 C  CA  . ILE   A 173 ? 2.4140 1.4311 2.2214 -0.0825 -0.3393 -0.1075 193 ILE   A CA  
1318 C  C   . ILE   A 173 ? 2.3391 1.3818 2.2121 -0.1123 -0.3201 -0.0690 193 ILE   A C   
1319 O  O   . ILE   A 173 ? 2.3246 1.4133 2.2063 -0.0992 -0.2825 -0.0415 193 ILE   A O   
1320 C  CB  . ILE   A 173 ? 2.4654 1.5592 2.3034 -0.0988 -0.3486 -0.1113 193 ILE   A CB  
1321 C  CG1 . ILE   A 173 ? 2.5267 1.5980 2.2917 -0.0643 -0.3632 -0.1453 193 ILE   A CG1 
1322 C  CG2 . ILE   A 173 ? 2.3910 1.4945 2.2980 -0.1486 -0.3832 -0.1123 193 ILE   A CG2 
1323 C  CD1 . ILE   A 173 ? 2.5474 1.6878 2.3367 -0.0760 -0.3743 -0.1494 193 ILE   A CD1 
1324 N  N   . ASP   A 174 ? 2.3597 1.3700 2.2782 -0.1528 -0.3471 -0.0668 194 ASP   A N   
1325 C  CA  . ASP   A 174 ? 2.3512 1.4008 2.3431 -0.1904 -0.3312 -0.0278 194 ASP   A CA  
1326 C  C   . ASP   A 174 ? 2.3729 1.5121 2.4280 -0.2221 -0.3353 -0.0206 194 ASP   A C   
1327 O  O   . ASP   A 174 ? 2.3622 1.4969 2.4622 -0.2581 -0.3671 -0.0299 194 ASP   A O   
1328 C  CB  . ASP   A 174 ? 2.3831 1.3507 2.3944 -0.2184 -0.3551 -0.0259 194 ASP   A CB  
1329 C  CG  . ASP   A 174 ? 2.4532 1.4487 2.5249 -0.2488 -0.3306 0.0197  194 ASP   A CG  
1330 O  OD1 . ASP   A 174 ? 2.4513 1.5278 2.5436 -0.2442 -0.2954 0.0476  194 ASP   A OD1 
1331 O  OD2 . ASP   A 174 ? 2.4060 1.3392 2.5021 -0.2768 -0.3468 0.0278  194 ASP   A OD2 
1332 N  N   . SER   A 175 ? 2.3615 1.5836 2.4219 -0.2075 -0.3035 -0.0046 195 SER   A N   
1333 C  CA  A SER   A 175 ? 2.3217 1.6295 2.4324 -0.2284 -0.3056 -0.0012 195 SER   A CA  
1334 C  CA  B SER   A 175 ? 2.3217 1.6293 2.4323 -0.2284 -0.3058 -0.0012 195 SER   A CA  
1335 C  C   . SER   A 175 ? 2.3748 1.7165 2.5697 -0.2769 -0.3074 0.0247  195 SER   A C   
1336 O  O   . SER   A 175 ? 2.2872 1.6621 2.5311 -0.3046 -0.3312 0.0157  195 SER   A O   
1337 C  CB  A SER   A 175 ? 2.2117 1.5935 2.3110 -0.2032 -0.2691 0.0137  195 SER   A CB  
1338 C  CB  B SER   A 175 ? 2.2114 1.5930 2.3105 -0.2032 -0.2694 0.0133  195 SER   A CB  
1339 O  OG  A SER   A 175 ? 2.1790 1.5303 2.2056 -0.1596 -0.2617 -0.0047 195 SER   A OG  
1340 O  OG  B SER   A 175 ? 2.1651 1.5675 2.2803 -0.2034 -0.2356 0.0477  195 SER   A OG  
1341 N  N   . LEU   A 176 ? 2.7744 2.1102 2.9884 -0.2868 -0.2819 0.0582  196 LEU   A N   
1342 C  CA  . LEU   A 176 ? 2.8793 2.2452 3.1707 -0.3321 -0.2779 0.0877  196 LEU   A CA  
1343 C  C   . LEU   A 176 ? 2.9494 2.2597 3.2753 -0.3678 -0.3190 0.0716  196 LEU   A C   
1344 O  O   . LEU   A 176 ? 2.9835 2.3340 3.3863 -0.4097 -0.3233 0.0884  196 LEU   A O   
1345 C  CB  . LEU   A 176 ? 2.9755 2.3281 3.2659 -0.3313 -0.2448 0.1261  196 LEU   A CB  
1346 C  CG  . LEU   A 176 ? 3.0233 2.4248 3.3858 -0.3707 -0.2251 0.1665  196 LEU   A CG  
1347 C  CD1 . LEU   A 176 ? 2.9665 2.4755 3.3572 -0.3681 -0.1996 0.1797  196 LEU   A CD1 
1348 C  CD2 . LEU   A 176 ? 3.0711 2.4297 3.4184 -0.3681 -0.2014 0.2005  196 LEU   A CD2 
1349 N  N   . ASN   A 177 ? 2.5246 1.7439 2.7964 -0.3518 -0.3494 0.0392  197 ASN   A N   
1350 C  CA  . ASN   A 177 ? 2.4259 1.5806 2.7225 -0.3833 -0.3945 0.0183  197 ASN   A CA  
1351 C  C   . ASN   A 177 ? 2.3829 1.5253 2.6511 -0.3716 -0.4362 -0.0282 197 ASN   A C   
1352 O  O   . ASN   A 177 ? 2.4990 1.5700 2.7649 -0.3870 -0.4800 -0.0554 197 ASN   A O   
1353 C  CB  . ASN   A 177 ? 2.4932 1.5369 2.7484 -0.3764 -0.4017 0.0170  197 ASN   A CB  
1354 C  CG  . ASN   A 177 ? 2.5757 1.6210 2.8670 -0.3961 -0.3687 0.0646  197 ASN   A CG  
1355 O  OD1 . ASN   A 177 ? 2.6164 1.7164 2.9853 -0.4371 -0.3587 0.0941  197 ASN   A OD1 
1356 N  ND2 . ASN   A 177 ? 2.5465 1.5332 2.7808 -0.3648 -0.3504 0.0733  197 ASN   A ND2 
1357 N  N   . ASN   A 178 ? 2.3360 1.5423 2.5803 -0.3445 -0.4254 -0.0381 198 ASN   A N   
1358 C  CA  . ASN   A 178 ? 2.1607 1.3601 2.3739 -0.3307 -0.4634 -0.0792 198 ASN   A CA  
1359 C  C   . ASN   A 178 ? 2.1325 1.4366 2.3790 -0.3297 -0.4528 -0.0739 198 ASN   A C   
1360 O  O   . ASN   A 178 ? 1.9871 1.2982 2.1851 -0.3008 -0.4656 -0.0999 198 ASN   A O   
1361 C  CB  . ASN   A 178 ? 2.2010 1.3306 2.3069 -0.2790 -0.4649 -0.1076 198 ASN   A CB  
1362 C  CG  . ASN   A 178 ? 2.2101 1.2243 2.2761 -0.2773 -0.4922 -0.1279 198 ASN   A CG  
1363 O  OD1 . ASN   A 178 ? 2.2584 1.2158 2.2996 -0.2787 -0.5388 -0.1652 198 ASN   A OD1 
1364 N  ND2 . ASN   A 178 ? 2.2565 1.2326 2.3137 -0.2725 -0.4651 -0.1045 198 ASN   A ND2 
1365 N  N   . LEU   A 196 ? 1.7119 2.1670 1.9907 -0.0072 -0.0107 0.0760  216 LEU   A N   
1366 C  CA  . LEU   A 196 ? 1.7252 2.2297 2.0236 0.0055  0.0002  0.0747  216 LEU   A CA  
1367 C  C   . LEU   A 196 ? 1.8256 2.3693 2.1755 -0.0033 -0.0037 0.0765  216 LEU   A C   
1368 O  O   . LEU   A 196 ? 1.7670 2.3620 2.1468 0.0024  0.0101  0.0811  216 LEU   A O   
1369 C  CB  . LEU   A 196 ? 1.5808 2.1059 1.8703 0.0060  0.0229  0.0889  216 LEU   A CB  
1370 C  CG  . LEU   A 196 ? 1.4971 1.9896 1.7390 0.0167  0.0233  0.0850  216 LEU   A CG  
1371 C  CD1 . LEU   A 196 ? 1.4187 1.9327 1.6459 0.0215  0.0432  0.0976  216 LEU   A CD1 
1372 C  CD2 . LEU   A 196 ? 1.4225 1.9013 1.6435 0.0376  0.0116  0.0645  216 LEU   A CD2 
1373 N  N   . ASP   A 197 ? 2.0131 2.5333 2.3736 -0.0162 -0.0229 0.0726  217 ASP   A N   
1374 C  CA  . ASP   A 197 ? 2.0242 2.5769 2.4351 -0.0256 -0.0346 0.0709  217 ASP   A CA  
1375 C  C   . ASP   A 197 ? 1.9659 2.5315 2.3787 -0.0024 -0.0493 0.0535  217 ASP   A C   
1376 O  O   . ASP   A 197 ? 1.9107 2.4544 2.2843 0.0184  -0.0492 0.0441  217 ASP   A O   
1377 C  CB  . ASP   A 197 ? 1.9232 2.4387 2.3371 -0.0475 -0.0517 0.0720  217 ASP   A CB  
1378 C  CG  . ASP   A 197 ? 1.9268 2.4038 2.3161 -0.0380 -0.0788 0.0543  217 ASP   A CG  
1379 O  OD1 . ASP   A 197 ? 1.9253 2.3797 2.2757 -0.0176 -0.0808 0.0451  217 ASP   A OD1 
1380 O  OD2 . ASP   A 197 ? 1.9153 2.3815 2.3223 -0.0513 -0.0989 0.0499  217 ASP   A OD2 
1381 N  N   . PRO   A 198 ? 1.9116 2.5129 2.3721 -0.0048 -0.0636 0.0488  218 PRO   A N   
1382 C  CA  . PRO   A 198 ? 1.9137 2.5303 2.3771 0.0211  -0.0775 0.0332  218 PRO   A CA  
1383 C  C   . PRO   A 198 ? 1.7941 2.3499 2.2035 0.0354  -0.0980 0.0196  218 PRO   A C   
1384 O  O   . PRO   A 198 ? 1.7399 2.2896 2.1265 0.0606  -0.0994 0.0102  218 PRO   A O   
1385 C  CB  . PRO   A 198 ? 1.9005 2.5639 2.4297 0.0107  -0.0936 0.0320  218 PRO   A CB  
1386 C  CG  . PRO   A 198 ? 1.8954 2.5906 2.4666 -0.0167 -0.0746 0.0507  218 PRO   A CG  
1387 C  CD  . PRO   A 198 ? 1.8709 2.5091 2.3924 -0.0298 -0.0657 0.0587  218 PRO   A CD  
1388 N  N   . PHE   A 199 ? 1.7121 2.2205 2.0985 0.0213  -0.1126 0.0189  219 PHE   A N   
1389 C  CA  . PHE   A 199 ? 1.6198 2.0747 1.9580 0.0358  -0.1314 0.0079  219 PHE   A CA  
1390 C  C   . PHE   A 199 ? 1.5344 1.9493 1.8216 0.0462  -0.1168 0.0094  219 PHE   A C   
1391 O  O   . PHE   A 199 ? 1.5058 1.9040 1.7680 0.0674  -0.1216 0.0018  219 PHE   A O   
1392 C  CB  . PHE   A 199 ? 1.5889 2.0049 1.9137 0.0203  -0.1499 0.0061  219 PHE   A CB  
1393 C  CG  . PHE   A 199 ? 1.5186 1.8757 1.7858 0.0355  -0.1641 -0.0019 219 PHE   A CG  
1394 C  CD1 . PHE   A 199 ? 1.5486 1.9030 1.8072 0.0562  -0.1855 -0.0127 219 PHE   A CD1 
1395 C  CD2 . PHE   A 199 ? 1.4725 1.7780 1.6942 0.0305  -0.1547 0.0031  219 PHE   A CD2 
1396 C  CE1 . PHE   A 199 ? 1.5826 1.8801 1.7837 0.0708  -0.1961 -0.0168 219 PHE   A CE1 
1397 C  CE2 . PHE   A 199 ? 1.5548 1.8082 1.7240 0.0446  -0.1633 -0.0013 219 PHE   A CE2 
1398 C  CZ  . PHE   A 199 ? 1.6005 1.8482 1.7571 0.0644  -0.1834 -0.0105 219 PHE   A CZ  
1399 N  N   . PHE   A 200 ? 1.6171 2.0148 1.8904 0.0312  -0.1005 0.0196  220 PHE   A N   
1400 C  CA  . PHE   A 200 ? 1.5894 1.9500 1.8204 0.0382  -0.0898 0.0209  220 PHE   A CA  
1401 C  C   . PHE   A 200 ? 1.5608 1.9442 1.7916 0.0538  -0.0782 0.0179  220 PHE   A C   
1402 O  O   . PHE   A 200 ? 1.4737 1.8255 1.6722 0.0633  -0.0760 0.0146  220 PHE   A O   
1403 C  CB  . PHE   A 200 ? 1.3159 1.6572 1.5370 0.0201  -0.0776 0.0321  220 PHE   A CB  
1404 C  CG  . PHE   A 200 ? 1.4476 1.7600 1.6631 0.0074  -0.0889 0.0331  220 PHE   A CG  
1405 C  CD1 . PHE   A 200 ? 1.4071 1.6693 1.5824 0.0127  -0.0946 0.0302  220 PHE   A CD1 
1406 C  CD2 . PHE   A 200 ? 1.4066 1.7406 1.6564 -0.0095 -0.0933 0.0369  220 PHE   A CD2 
1407 C  CE1 . PHE   A 200 ? 1.3780 1.6105 1.5412 0.0048  -0.1048 0.0290  220 PHE   A CE1 
1408 C  CE2 . PHE   A 200 ? 1.3822 1.6838 1.6232 -0.0200 -0.1066 0.0348  220 PHE   A CE2 
1409 C  CZ  . PHE   A 200 ? 1.3745 1.6246 1.5691 -0.0111 -0.1125 0.0298  220 PHE   A CZ  
1410 N  N   . LEU   A 201 ? 1.8356 2.2724 2.1022 0.0569  -0.0704 0.0188  221 LEU   A N   
1411 C  CA  . LEU   A 201 ? 1.8565 2.3138 2.1192 0.0787  -0.0626 0.0116  221 LEU   A CA  
1412 C  C   . LEU   A 201 ? 1.7322 2.1738 1.9841 0.1008  -0.0801 -0.0019 221 LEU   A C   
1413 O  O   . LEU   A 201 ? 1.8181 2.2323 2.0394 0.1173  -0.0808 -0.0096 221 LEU   A O   
1414 C  CB  . LEU   A 201 ? 1.8716 2.3932 2.1760 0.0793  -0.0472 0.0171  221 LEU   A CB  
1415 C  CG  . LEU   A 201 ? 1.9229 2.4608 2.2193 0.0751  -0.0235 0.0272  221 LEU   A CG  
1416 C  CD1 . LEU   A 201 ? 1.8511 2.4552 2.1892 0.0788  -0.0059 0.0342  221 LEU   A CD1 
1417 C  CD2 . LEU   A 201 ? 1.6247 2.1330 1.8759 0.0934  -0.0215 0.0173  221 LEU   A CD2 
1418 N  N   . SER   A 202 ? 1.4511 1.9072 1.7277 0.1016  -0.0966 -0.0049 222 SER   A N   
1419 C  CA  . SER   A 202 ? 1.4692 1.9041 1.7306 0.1234  -0.1165 -0.0160 222 SER   A CA  
1420 C  C   . SER   A 202 ? 1.4807 1.8459 1.6893 0.1243  -0.1234 -0.0162 222 SER   A C   
1421 O  O   . SER   A 202 ? 1.5570 1.8935 1.7411 0.1445  -0.1340 -0.0231 222 SER   A O   
1422 C  CB  . SER   A 202 ? 1.5366 1.9972 1.8325 0.1217  -0.1370 -0.0188 222 SER   A CB  
1423 O  OG  . SER   A 202 ? 1.4798 2.0046 1.8252 0.1339  -0.1351 -0.0224 222 SER   A OG  
1424 N  N   . ILE   A 203 ? 1.4042 1.7418 1.5960 0.1036  -0.1165 -0.0074 223 ILE   A N   
1425 C  CA  . ILE   A 203 ? 1.4805 1.7575 1.6271 0.1038  -0.1181 -0.0051 223 ILE   A CA  
1426 C  C   . ILE   A 203 ? 1.5017 1.7596 1.6285 0.1144  -0.1095 -0.0078 223 ILE   A C   
1427 O  O   . ILE   A 203 ? 1.4776 1.6934 1.5751 0.1259  -0.1163 -0.0099 223 ILE   A O   
1428 C  CB  . ILE   A 203 ? 1.4609 1.7187 1.5987 0.0817  -0.1098 0.0048  223 ILE   A CB  
1429 C  CG1 . ILE   A 203 ? 1.4033 1.6555 1.5437 0.0750  -0.1247 0.0043  223 ILE   A CG1 
1430 C  CG2 . ILE   A 203 ? 1.3820 1.5893 1.4821 0.0813  -0.1026 0.0097  223 ILE   A CG2 
1431 C  CD1 . ILE   A 203 ? 1.4747 1.6938 1.5944 0.0596  -0.1182 0.0119  223 ILE   A CD1 
1432 N  N   . THR   A 204 ? 1.3884 1.6733 1.5284 0.1105  -0.0955 -0.0076 224 THR   A N   
1433 C  CA  . THR   A 204 ? 1.3483 1.6095 1.4669 0.1180  -0.0907 -0.0121 224 THR   A CA  
1434 C  C   . THR   A 204 ? 1.2697 1.5391 1.3870 0.1436  -0.0965 -0.0253 224 THR   A C   
1435 O  O   . THR   A 204 ? 1.1967 1.4340 1.2916 0.1522  -0.0982 -0.0318 224 THR   A O   
1436 C  CB  . THR   A 204 ? 1.2017 1.4807 1.3256 0.1052  -0.0761 -0.0074 224 THR   A CB  
1437 O  OG1 . THR   A 204 ? 1.2726 1.5705 1.4138 0.0862  -0.0698 0.0039  224 THR   A OG1 
1438 C  CG2 . THR   A 204 ? 1.2658 1.5022 1.3662 0.0987  -0.0753 -0.0060 224 THR   A CG2 
1439 N  N   . VAL   A 205 ? 1.2868 1.5978 1.4299 0.1562  -0.1003 -0.0298 225 VAL   A N   
1440 C  CA  . VAL   A 205 ? 1.4001 1.7142 1.5407 0.1850  -0.1081 -0.0426 225 VAL   A CA  
1441 C  C   . VAL   A 205 ? 1.4779 1.7542 1.6020 0.1967  -0.1273 -0.0441 225 VAL   A C   
1442 O  O   . VAL   A 205 ? 1.5303 1.7798 1.6359 0.2196  -0.1359 -0.0529 225 VAL   A O   
1443 C  CB  . VAL   A 205 ? 1.4291 1.8124 1.6099 0.1965  -0.1010 -0.0462 225 VAL   A CB  
1444 C  CG1 . VAL   A 205 ? 1.3531 1.7417 1.5324 0.2307  -0.1083 -0.0604 225 VAL   A CG1 
1445 C  CG2 . VAL   A 205 ? 1.2930 1.7079 1.4809 0.1871  -0.0798 -0.0423 225 VAL   A CG2 
1446 N  N   . PHE   A 206 ? 1.5044 1.7725 1.6296 0.1830  -0.1349 -0.0357 226 PHE   A N   
1447 C  CA  . PHE   A 206 ? 1.5863 1.8125 1.6858 0.1938  -0.1529 -0.0350 226 PHE   A CA  
1448 C  C   . PHE   A 206 ? 1.6452 1.8269 1.7159 0.1739  -0.1501 -0.0233 226 PHE   A C   
1449 O  O   . PHE   A 206 ? 1.6497 1.8305 1.7188 0.1678  -0.1594 -0.0197 226 PHE   A O   
1450 C  CB  . PHE   A 206 ? 1.6119 1.8767 1.7396 0.2049  -0.1701 -0.0395 226 PHE   A CB  
1451 C  CG  . PHE   A 206 ? 1.6287 1.9600 1.8026 0.2171  -0.1659 -0.0475 226 PHE   A CG  
1452 C  CD1 . PHE   A 206 ? 1.6281 1.9612 1.7984 0.2451  -0.1662 -0.0575 226 PHE   A CD1 
1453 C  CD2 . PHE   A 206 ? 1.5588 1.9498 1.7804 0.2013  -0.1607 -0.0443 226 PHE   A CD2 
1454 C  CE1 . PHE   A 206 ? 1.5953 1.9927 1.8075 0.2594  -0.1590 -0.0644 226 PHE   A CE1 
1455 C  CE2 . PHE   A 206 ? 1.5057 1.9621 1.7731 0.2124  -0.1528 -0.0487 226 PHE   A CE2 
1456 C  CZ  . PHE   A 206 ? 1.5365 1.9981 1.7987 0.2428  -0.1508 -0.0589 226 PHE   A CZ  
1457 N  N   . PRO   A 207 ? 1.5064 1.6511 1.5549 0.1642  -0.1378 -0.0178 227 PRO   A N   
1458 C  CA  . PRO   A 207 ? 1.4420 1.5459 1.4646 0.1485  -0.1323 -0.0056 227 PRO   A CA  
1459 C  C   . PRO   A 207 ? 1.4120 1.4626 1.3955 0.1622  -0.1421 -0.0007 227 PRO   A C   
1460 O  O   . PRO   A 207 ? 1.3534 1.3726 1.3116 0.1540  -0.1378 0.0099  227 PRO   A O   
1461 C  CB  . PRO   A 207 ? 1.3593 1.4514 1.3819 0.1345  -0.1165 -0.0018 227 PRO   A CB  
1462 C  CG  . PRO   A 207 ? 1.3584 1.4517 1.3836 0.1504  -0.1205 -0.0130 227 PRO   A CG  
1463 C  CD  . PRO   A 207 ? 1.4678 1.6067 1.5150 0.1675  -0.1294 -0.0233 227 PRO   A CD  
1464 N  N   . PHE   A 208 ? 1.2555 1.2938 1.2308 0.1849  -0.1541 -0.0074 228 PHE   A N   
1465 C  CA  . PHE   A 208 ? 1.3967 1.3882 1.3341 0.2026  -0.1671 -0.0024 228 PHE   A CA  
1466 C  C   . PHE   A 208 ? 1.4458 1.4533 1.3800 0.2094  -0.1838 -0.0041 228 PHE   A C   
1467 O  O   . PHE   A 208 ? 1.5422 1.5116 1.4395 0.2264  -0.1973 0.0000  228 PHE   A O   
1468 C  CB  . PHE   A 208 ? 1.4912 1.4685 1.4240 0.2278  -0.1779 -0.0107 228 PHE   A CB  
1469 C  CG  . PHE   A 208 ? 1.5198 1.5562 1.4911 0.2429  -0.1871 -0.0264 228 PHE   A CG  
1470 C  CD1 . PHE   A 208 ? 1.4479 1.5199 1.4480 0.2382  -0.1753 -0.0352 228 PHE   A CD1 
1471 C  CD2 . PHE   A 208 ? 1.5350 1.5925 1.5134 0.2635  -0.2073 -0.0320 228 PHE   A CD2 
1472 C  CE1 . PHE   A 208 ? 1.4268 1.5556 1.4618 0.2538  -0.1792 -0.0476 228 PHE   A CE1 
1473 C  CE2 . PHE   A 208 ? 1.5334 1.6516 1.5547 0.2777  -0.2132 -0.0448 228 PHE   A CE2 
1474 C  CZ  . PHE   A 208 ? 1.5833 1.7377 1.6326 0.2730  -0.1969 -0.0518 228 PHE   A CZ  
1475 N  N   . LEU   A 209 ? 1.3511 1.4116 1.3221 0.1967  -0.1847 -0.0099 229 LEU   A N   
1476 C  CA  . LEU   A 209 ? 1.4140 1.4907 1.3880 0.1985  -0.2033 -0.0135 229 LEU   A CA  
1477 C  C   . LEU   A 209 ? 1.4527 1.5112 1.4085 0.1786  -0.1959 -0.0062 229 LEU   A C   
1478 O  O   . LEU   A 209 ? 1.5430 1.6103 1.4990 0.1778  -0.2128 -0.0110 229 LEU   A O   
1479 C  CB  . LEU   A 209 ? 1.4104 1.5585 1.4434 0.1972  -0.2117 -0.0245 229 LEU   A CB  
1480 C  CG  . LEU   A 209 ? 1.4483 1.6252 1.5051 0.2216  -0.2205 -0.0339 229 LEU   A CG  
1481 C  CD1 . LEU   A 209 ? 1.3714 1.6221 1.4890 0.2202  -0.2296 -0.0422 229 LEU   A CD1 
1482 C  CD2 . LEU   A 209 ? 1.4639 1.5965 1.4807 0.2490  -0.2408 -0.0344 229 LEU   A CD2 
1483 N  N   . ILE   A 210 ? 1.3621 1.3963 1.3041 0.1634  -0.1726 0.0040  230 ILE   A N   
1484 C  CA  . ILE   A 210 ? 1.3583 1.3706 1.2784 0.1491  -0.1634 0.0114  230 ILE   A CA  
1485 C  C   . ILE   A 210 ? 1.4203 1.3799 1.2827 0.1650  -0.1730 0.0164  230 ILE   A C   
1486 O  O   . ILE   A 210 ? 1.3923 1.3466 1.2384 0.1652  -0.1853 0.0122  230 ILE   A O   
1487 C  CB  . ILE   A 210 ? 1.3497 1.3517 1.2727 0.1319  -0.1363 0.0218  230 ILE   A CB  
1488 C  CG1 . ILE   A 210 ? 1.3692 1.4195 1.3405 0.1198  -0.1286 0.0168  230 ILE   A CG1 
1489 C  CG2 . ILE   A 210 ? 1.3691 1.3539 1.2737 0.1202  -0.1261 0.0284  230 ILE   A CG2 
1490 C  CD1 . ILE   A 210 ? 1.3056 1.3466 1.2810 0.1063  -0.1073 0.0251  230 ILE   A CD1 
1491 N  N   . PRO   A 211 ? 1.4982 1.4144 1.3250 0.1792  -0.1686 0.0256  231 PRO   A N   
1492 C  CA  . PRO   A 211 ? 1.5572 1.4218 1.3224 0.1968  -0.1769 0.0326  231 PRO   A CA  
1493 C  C   . PRO   A 211 ? 1.5345 1.4096 1.2928 0.2165  -0.2110 0.0198  231 PRO   A C   
1494 O  O   . PRO   A 211 ? 1.5463 1.3874 1.2546 0.2297  -0.2238 0.0209  231 PRO   A O   
1495 C  CB  . PRO   A 211 ? 1.4831 1.3030 1.2215 0.2058  -0.1640 0.0470  231 PRO   A CB  
1496 C  CG  . PRO   A 211 ? 1.4433 1.2895 1.2293 0.1904  -0.1497 0.0454  231 PRO   A CG  
1497 C  CD  . PRO   A 211 ? 1.4345 1.3435 1.2720 0.1830  -0.1604 0.0289  231 PRO   A CD  
1498 N  N   . ILE   A 212 ? 1.5710 1.4935 1.3781 0.2206  -0.2262 0.0074  232 ILE   A N   
1499 C  CA  . ILE   A 212 ? 1.5084 1.4573 1.3278 0.2358  -0.2600 -0.0064 232 ILE   A CA  
1500 C  C   . ILE   A 212 ? 1.4871 1.4480 1.3086 0.2230  -0.2720 -0.0140 232 ILE   A C   
1501 O  O   . ILE   A 212 ? 1.7445 1.6904 1.5374 0.2374  -0.3001 -0.0211 232 ILE   A O   
1502 C  CB  . ILE   A 212 ? 1.4465 1.4574 1.3318 0.2376  -0.2663 -0.0172 232 ILE   A CB  
1503 C  CG1 . ILE   A 212 ? 1.5656 1.5556 1.4384 0.2602  -0.2657 -0.0143 232 ILE   A CG1 
1504 C  CG2 . ILE   A 212 ? 1.4607 1.5203 1.3840 0.2420  -0.2971 -0.0317 232 ILE   A CG2 
1505 C  CD1 . ILE   A 212 ? 1.7133 1.7338 1.6088 0.2863  -0.2946 -0.0260 232 ILE   A CD1 
1506 N  N   . LEU   A 213 ? 1.5459 1.5304 1.3988 0.1967  -0.2530 -0.0133 233 LEU   A N   
1507 C  CA  . LEU   A 213 ? 1.6143 1.6105 1.4766 0.1823  -0.2647 -0.0216 233 LEU   A CA  
1508 C  C   . LEU   A 213 ? 1.7052 1.6434 1.5024 0.1834  -0.2568 -0.0158 233 LEU   A C   
1509 O  O   . LEU   A 213 ? 1.8058 1.7345 1.5875 0.1824  -0.2768 -0.0259 233 LEU   A O   
1510 C  CB  . LEU   A 213 ? 1.4519 1.4980 1.3769 0.1552  -0.2484 -0.0224 233 LEU   A CB  
1511 C  CG  . LEU   A 213 ? 1.3302 1.4354 1.3165 0.1559  -0.2501 -0.0266 233 LEU   A CG  
1512 C  CD1 . LEU   A 213 ? 1.3460 1.4957 1.3850 0.1310  -0.2299 -0.0239 233 LEU   A CD1 
1513 C  CD2 . LEU   A 213 ? 1.3581 1.4952 1.3710 0.1683  -0.2848 -0.0395 233 LEU   A CD2 
1514 N  N   . GLU   A 214 ? 1.5683 1.4676 1.3282 0.1860  -0.2282 0.0000  234 GLU   A N   
1515 C  CA  . GLU   A 214 ? 1.6469 1.4930 1.3432 0.1910  -0.2166 0.0075  234 GLU   A CA  
1516 C  C   . GLU   A 214 ? 1.8373 1.6411 1.4686 0.2180  -0.2421 0.0037  234 GLU   A C   
1517 O  O   . GLU   A 214 ? 1.9910 1.7589 1.5708 0.2246  -0.2459 0.0010  234 GLU   A O   
1518 C  CB  . GLU   A 214 ? 1.5773 1.3971 1.2564 0.1875  -0.1793 0.0275  234 GLU   A CB  
1519 C  CG  . GLU   A 214 ? 1.5820 1.4408 1.3210 0.1636  -0.1566 0.0311  234 GLU   A CG  
1520 C  CD  . GLU   A 214 ? 1.5867 1.4577 1.3410 0.1458  -0.1455 0.0288  234 GLU   A CD  
1521 O  OE1 . GLU   A 214 ? 1.5166 1.3742 1.2471 0.1494  -0.1606 0.0195  234 GLU   A OE1 
1522 O  OE2 . GLU   A 214 ? 1.5211 1.4123 1.3097 0.1292  -0.1234 0.0357  234 GLU   A OE2 
1523 N  N   . VAL   A 215 ? 1.8945 1.6992 1.5231 0.2364  -0.2606 0.0030  235 VAL   A N   
1524 C  CA  . VAL   A 215 ? 1.8722 1.6402 1.4406 0.2644  -0.2906 -0.0016 235 VAL   A CA  
1525 C  C   . VAL   A 215 ? 1.9006 1.7047 1.5000 0.2648  -0.3331 -0.0246 235 VAL   A C   
1526 O  O   . VAL   A 215 ? 1.9782 1.7525 1.5265 0.2851  -0.3635 -0.0331 235 VAL   A O   
1527 C  CB  . VAL   A 215 ? 1.8269 1.5737 1.3743 0.2869  -0.2931 0.0094  235 VAL   A CB  
1528 C  CG1 . VAL   A 215 ? 1.7432 1.5464 1.3596 0.2878  -0.3135 -0.0024 235 VAL   A CG1 
1529 C  CG2 . VAL   A 215 ? 1.8611 1.5512 1.3237 0.3185  -0.3145 0.0124  235 VAL   A CG2 
1530 N  N   . LEU   A 216 ? 1.8124 1.6798 1.4944 0.2425  -0.3364 -0.0344 236 LEU   A N   
1531 C  CA  . LEU   A 216 ? 1.8113 1.7191 1.5364 0.2366  -0.3739 -0.0545 236 LEU   A CA  
1532 C  C   . LEU   A 216 ? 1.9882 1.8857 1.7081 0.2175  -0.3766 -0.0634 236 LEU   A C   
1533 O  O   . LEU   A 216 ? 1.9878 1.9164 1.7487 0.2070  -0.4074 -0.0800 236 LEU   A O   
1534 C  CB  . LEU   A 216 ? 1.6963 1.6795 1.5153 0.2222  -0.3736 -0.0584 236 LEU   A CB  
1535 C  CG  . LEU   A 216 ? 1.7746 1.7837 1.6166 0.2436  -0.3845 -0.0580 236 LEU   A CG  
1536 C  CD1 . LEU   A 216 ? 1.6856 1.7613 1.6000 0.2418  -0.4178 -0.0739 236 LEU   A CD1 
1537 C  CD2 . LEU   A 216 ? 1.8649 1.8141 1.6286 0.2765  -0.3967 -0.0522 236 LEU   A CD2 
1538 N  N   . ASN   A 217 ? 2.1787 2.0331 1.8520 0.2132  -0.3456 -0.0527 237 ASN   A N   
1539 C  CA  . ASN   A 217 ? 2.3110 2.1469 1.9713 0.1988  -0.3444 -0.0605 237 ASN   A CA  
1540 C  C   . ASN   A 217 ? 2.2575 2.1496 2.0031 0.1682  -0.3501 -0.0692 237 ASN   A C   
1541 O  O   . ASN   A 217 ? 2.2804 2.1687 2.0332 0.1575  -0.3732 -0.0841 237 ASN   A O   
1542 C  CB  . ASN   A 217 ? 2.4206 2.2086 2.0121 0.2186  -0.3791 -0.0757 237 ASN   A CB  
1543 C  CG  . ASN   A 217 ? 2.6215 2.3609 2.1593 0.2169  -0.3635 -0.0772 237 ASN   A CG  
1544 O  OD1 . ASN   A 217 ? 2.6582 2.3831 2.1822 0.2128  -0.3214 -0.0604 237 ASN   A OD1 
1545 N  ND2 . ASN   A 217 ? 2.7464 2.4609 2.2559 0.2206  -0.3983 -0.0982 237 ASN   A ND2 
1546 N  N   . ILE   A 218 ? 2.0796 2.0212 1.8883 0.1543  -0.3290 -0.0595 238 ILE   A N   
1547 C  CA  . ILE   A 218 ? 2.0076 2.0009 1.8929 0.1254  -0.3246 -0.0618 238 ILE   A CA  
1548 C  C   . ILE   A 218 ? 1.9994 1.9788 1.8793 0.1105  -0.2860 -0.0488 238 ILE   A C   
1549 O  O   . ILE   A 218 ? 2.0431 1.9875 1.8765 0.1214  -0.2608 -0.0370 238 ILE   A O   
1550 C  CB  . ILE   A 218 ? 1.8679 1.9273 1.8243 0.1218  -0.3250 -0.0597 238 ILE   A CB  
1551 C  CG1 . ILE   A 218 ? 1.8750 1.9391 1.8217 0.1469  -0.3567 -0.0683 238 ILE   A CG1 
1552 C  CG2 . ILE   A 218 ? 1.8248 1.9396 1.8601 0.0944  -0.3316 -0.0646 238 ILE   A CG2 
1553 C  CD1 . ILE   A 218 ? 1.7308 1.8597 1.7452 0.1487  -0.3575 -0.0677 238 ILE   A CD1 
1554 N  N   . CYS   A 219 ? 1.9428 1.9507 1.8735 0.0851  -0.2815 -0.0498 239 CYS   A N   
1555 C  CA  . CYS   A 219 ? 1.9501 1.9448 1.8769 0.0721  -0.2493 -0.0385 239 CYS   A CA  
1556 C  C   . CYS   A 219 ? 1.9081 1.9512 1.9061 0.0453  -0.2432 -0.0354 239 CYS   A C   
1557 O  O   . CYS   A 219 ? 1.9089 1.9737 1.9454 0.0322  -0.2675 -0.0450 239 CYS   A O   
1558 C  CB  . CYS   A 219 ? 2.0592 1.9960 1.9291 0.0767  -0.2526 -0.0445 239 CYS   A CB  
1559 S  SG  . CYS   A 219 ? 2.0225 1.9144 1.8340 0.0894  -0.2130 -0.0290 239 CYS   A SG  
1560 N  N   . VAL   A 220 ? 1.9305 1.9886 1.9449 0.0369  -0.2112 -0.0210 240 VAL   A N   
1561 C  CA  . VAL   A 220 ? 1.9083 2.0036 1.9784 0.0131  -0.2008 -0.0145 240 VAL   A CA  
1562 C  C   . VAL   A 220 ? 1.9471 2.0088 2.0055 0.0004  -0.2024 -0.0162 240 VAL   A C   
1563 O  O   . VAL   A 220 ? 1.8851 1.9672 1.9835 -0.0199 -0.1942 -0.0092 240 VAL   A O   
1564 C  CB  . VAL   A 220 ? 1.8044 1.9231 1.8887 0.0113  -0.1692 0.0003  240 VAL   A CB  
1565 C  CG1 . VAL   A 220 ? 1.6664 1.8227 1.7719 0.0215  -0.1699 -0.0002 240 VAL   A CG1 
1566 C  CG2 . VAL   A 220 ? 1.7781 1.8534 1.8120 0.0222  -0.1498 0.0069  240 VAL   A CG2 
1567 N  N   . PHE   A 221 ? 2.0413 2.0482 2.0415 0.0138  -0.2112 -0.0245 241 PHE   A N   
1568 C  CA  . PHE   A 221 ? 2.0189 1.9859 2.0011 0.0062  -0.2194 -0.0313 241 PHE   A CA  
1569 C  C   . PHE   A 221 ? 2.0345 1.9791 1.9971 0.0121  -0.2584 -0.0514 241 PHE   A C   
1570 O  O   . PHE   A 221 ? 2.0426 1.9481 1.9431 0.0356  -0.2664 -0.0590 241 PHE   A O   
1571 C  CB  . PHE   A 221 ? 2.0806 2.0009 2.0071 0.0204  -0.1953 -0.0254 241 PHE   A CB  
1572 C  CG  . PHE   A 221 ? 2.1534 2.0970 2.0911 0.0221  -0.1623 -0.0077 241 PHE   A CG  
1573 C  CD1 . PHE   A 221 ? 2.0683 2.0425 2.0509 0.0046  -0.1459 0.0040  241 PHE   A CD1 
1574 C  CD2 . PHE   A 221 ? 2.1067 2.0439 2.0136 0.0400  -0.1502 -0.0025 241 PHE   A CD2 
1575 C  CE1 . PHE   A 221 ? 2.0444 2.0417 2.0388 0.0060  -0.1204 0.0179  241 PHE   A CE1 
1576 C  CE2 . PHE   A 221 ? 2.0714 2.0312 1.9953 0.0388  -0.1239 0.0121  241 PHE   A CE2 
1577 C  CZ  . PHE   A 221 ? 2.0339 2.0245 2.0012 0.0222  -0.1106 0.0209  241 PHE   A CZ  
1578 N  N   . PRO   A 222 ? 2.0798 2.0478 2.0936 -0.0082 -0.2841 -0.0599 242 PRO   A N   
1579 C  CA  . PRO   A 222 ? 2.1038 2.0679 2.1147 -0.0030 -0.3264 -0.0794 242 PRO   A CA  
1580 C  C   . PRO   A 222 ? 2.3782 2.2722 2.3040 0.0201  -0.3440 -0.0951 242 PRO   A C   
1581 O  O   . PRO   A 222 ? 2.4251 2.2702 2.3102 0.0222  -0.3343 -0.0971 242 PRO   A O   
1582 C  CB  . PRO   A 222 ? 2.0660 2.0537 2.1446 -0.0341 -0.3471 -0.0845 242 PRO   A CB  
1583 C  CG  . PRO   A 222 ? 1.8740 1.8630 1.9743 -0.0524 -0.3140 -0.0672 242 PRO   A CG  
1584 C  CD  . PRO   A 222 ? 1.9267 1.9297 2.0078 -0.0376 -0.2760 -0.0503 242 PRO   A CD  
1585 N  N   . ARG   A 223 ? 2.6011 2.4895 2.4972 0.0403  -0.3701 -0.1064 243 ARG   A N   
1586 C  CA  . ARG   A 223 ? 2.7369 2.5593 2.5410 0.0685  -0.3844 -0.1191 243 ARG   A CA  
1587 C  C   . ARG   A 223 ? 2.7217 2.4964 2.5023 0.0623  -0.4146 -0.1403 243 ARG   A C   
1588 O  O   . ARG   A 223 ? 2.8184 2.5347 2.5190 0.0864  -0.4321 -0.1551 243 ARG   A O   
1589 C  CB  . ARG   A 223 ? 2.7465 2.5766 2.5292 0.0906  -0.4108 -0.1261 243 ARG   A CB  
1590 C  CG  . ARG   A 223 ? 2.8048 2.5701 2.4826 0.1258  -0.4121 -0.1300 243 ARG   A CG  
1591 C  CD  . ARG   A 223 ? 2.8704 2.6099 2.5055 0.1357  -0.3614 -0.1099 243 ARG   A CD  
1592 N  NE  . ARG   A 223 ? 2.7571 2.5358 2.4223 0.1360  -0.3322 -0.0890 243 ARG   A NE  
1593 C  CZ  . ARG   A 223 ? 2.6779 2.4457 2.3216 0.1417  -0.2898 -0.0697 243 ARG   A CZ  
1594 N  NH1 . ARG   A 223 ? 2.7013 2.4260 2.2966 0.1487  -0.2676 -0.0665 243 ARG   A NH1 
1595 N  NH2 . ARG   A 223 ? 2.6034 2.4047 2.2769 0.1408  -0.2699 -0.0539 243 ARG   A NH2 
1596 N  N   . GLU   A 224 ? 2.5137 2.3092 2.3604 0.0309  -0.4208 -0.1418 244 GLU   A N   
1597 C  CA  . GLU   A 224 ? 2.6264 2.3732 2.4584 0.0205  -0.4471 -0.1607 244 GLU   A CA  
1598 C  C   . GLU   A 224 ? 2.5837 2.2967 2.3987 0.0153  -0.4132 -0.1508 244 GLU   A C   
1599 O  O   . GLU   A 224 ? 2.6143 2.2605 2.3648 0.0289  -0.4214 -0.1654 244 GLU   A O   
1600 C  CB  . GLU   A 224 ? 2.6382 2.4266 2.5596 -0.0132 -0.4814 -0.1690 244 GLU   A CB  
1601 C  CG  . GLU   A 224 ? 2.5601 2.4256 2.5745 -0.0389 -0.4538 -0.1453 244 GLU   A CG  
1602 C  CD  . GLU   A 224 ? 2.6235 2.4980 2.7040 -0.0757 -0.4553 -0.1411 244 GLU   A CD  
1603 O  OE1 . GLU   A 224 ? 2.8276 2.6791 2.9237 -0.0908 -0.4961 -0.1605 244 GLU   A OE1 
1604 O  OE2 . GLU   A 224 ? 2.5648 2.4664 2.6801 -0.0894 -0.4168 -0.1182 244 GLU   A OE2 
1605 N  N   . VAL   A 225 ? 2.5393 2.2962 2.4085 -0.0017 -0.3762 -0.1270 245 VAL   A N   
1606 C  CA  . VAL   A 225 ? 2.4955 2.2244 2.3502 -0.0038 -0.3436 -0.1156 245 VAL   A CA  
1607 C  C   . VAL   A 225 ? 2.4644 2.1460 2.2322 0.0305  -0.3206 -0.1151 245 VAL   A C   
1608 O  O   . VAL   A 225 ? 2.4049 2.0284 2.1218 0.0422  -0.3189 -0.1242 245 VAL   A O   
1609 C  CB  . VAL   A 225 ? 2.3700 2.1580 2.2917 -0.0233 -0.3090 -0.0894 245 VAL   A CB  
1610 C  CG1 . VAL   A 225 ? 2.4006 2.1611 2.3012 -0.0195 -0.2749 -0.0765 245 VAL   A CG1 
1611 C  CG2 . VAL   A 225 ? 2.3138 2.1444 2.3195 -0.0577 -0.3264 -0.0872 245 VAL   A CG2 
1612 N  N   . THR   A 226 ? 2.6569 2.3621 2.4075 0.0476  -0.3016 -0.1036 246 THR   A N   
1613 C  CA  . THR   A 226 ? 2.5693 2.2343 2.2422 0.0790  -0.2771 -0.0996 246 THR   A CA  
1614 C  C   . THR   A 226 ? 2.5402 2.1409 2.1325 0.1029  -0.3056 -0.1230 246 THR   A C   
1615 O  O   . THR   A 226 ? 2.5603 2.1098 2.0875 0.1246  -0.2891 -0.1258 246 THR   A O   
1616 C  CB  . THR   A 226 ? 2.4879 2.1878 2.1619 0.0896  -0.2570 -0.0832 246 THR   A CB  
1617 O  OG1 . THR   A 226 ? 2.5850 2.2968 2.2581 0.0943  -0.2908 -0.0945 246 THR   A OG1 
1618 C  CG2 . THR   A 226 ? 2.3972 2.1569 2.1452 0.0680  -0.2314 -0.0630 246 THR   A CG2 
1619 N  N   . ASN   A 227 ? 2.5457 2.1487 2.1405 0.1012  -0.3493 -0.1408 247 ASN   A N   
1620 C  CA  . ASN   A 227 ? 2.6231 2.1626 2.1400 0.1233  -0.3837 -0.1666 247 ASN   A CA  
1621 C  C   . ASN   A 227 ? 2.6509 2.1405 2.1534 0.1166  -0.3952 -0.1832 247 ASN   A C   
1622 O  O   . ASN   A 227 ? 2.6746 2.0982 2.0913 0.1440  -0.3977 -0.1975 247 ASN   A O   
1623 C  CB  . ASN   A 227 ? 2.6612 2.2194 2.1979 0.1187  -0.4343 -0.1837 247 ASN   A CB  
1624 C  CG  . ASN   A 227 ? 2.7177 2.2839 2.2129 0.1451  -0.4330 -0.1769 247 ASN   A CG  
1625 O  OD1 . ASN   A 227 ? 2.7492 2.2854 2.1757 0.1720  -0.4015 -0.1650 247 ASN   A OD1 
1626 N  ND2 . ASN   A 227 ? 2.6987 2.3059 2.2380 0.1380  -0.4668 -0.1830 247 ASN   A ND2 
1627 N  N   . PHE   A 228 ? 2.5774 2.0948 2.1602 0.0817  -0.4015 -0.1810 248 PHE   A N   
1628 C  CA  . PHE   A 228 ? 2.5369 2.0036 2.1112 0.0731  -0.4126 -0.1950 248 PHE   A CA  
1629 C  C   . PHE   A 228 ? 2.5091 1.9345 2.0247 0.0974  -0.3707 -0.1863 248 PHE   A C   
1630 O  O   . PHE   A 228 ? 2.5346 1.8904 1.9760 0.1203  -0.3806 -0.2058 248 PHE   A O   
1631 C  CB  . PHE   A 228 ? 2.4489 1.9578 2.1239 0.0306  -0.4163 -0.1854 248 PHE   A CB  
1632 C  CG  . PHE   A 228 ? 2.3922 1.8509 2.0644 0.0207  -0.4160 -0.1914 248 PHE   A CG  
1633 C  CD1 . PHE   A 228 ? 2.4932 1.8861 2.1294 0.0219  -0.4585 -0.2215 248 PHE   A CD1 
1634 C  CD2 . PHE   A 228 ? 2.2392 1.7134 1.9430 0.0114  -0.3757 -0.1677 248 PHE   A CD2 
1635 C  CE1 . PHE   A 228 ? 2.4782 1.8187 2.1101 0.0140  -0.4592 -0.2275 248 PHE   A CE1 
1636 C  CE2 . PHE   A 228 ? 2.3083 1.7331 2.0081 0.0046  -0.3760 -0.1721 248 PHE   A CE2 
1637 C  CZ  . PHE   A 228 ? 2.4184 1.7748 2.0823 0.0058  -0.4171 -0.2018 248 PHE   A CZ  
1638 N  N   . LEU   A 229 ? 2.4821 1.9504 2.0297 0.0948  -0.3244 -0.1579 249 LEU   A N   
1639 C  CA  . LEU   A 229 ? 2.4234 1.8632 1.9323 0.1149  -0.2841 -0.1475 249 LEU   A CA  
1640 C  C   . LEU   A 229 ? 2.5331 1.9401 1.9527 0.1551  -0.2657 -0.1488 249 LEU   A C   
1641 O  O   . LEU   A 229 ? 2.5122 1.8702 1.8725 0.1804  -0.2477 -0.1535 249 LEU   A O   
1642 C  CB  . LEU   A 229 ? 2.1828 1.6814 1.7593 0.0978  -0.2450 -0.1177 249 LEU   A CB  
1643 C  CG  . LEU   A 229 ? 2.1390 1.6645 1.7957 0.0611  -0.2558 -0.1124 249 LEU   A CG  
1644 C  CD1 . LEU   A 229 ? 1.9198 1.5123 1.6405 0.0453  -0.2233 -0.0840 249 LEU   A CD1 
1645 C  CD2 . LEU   A 229 ? 2.0377 1.5074 1.6772 0.0622  -0.2580 -0.1211 249 LEU   A CD2 
1646 N  N   . ARG   A 230 ? 2.6034 2.0355 2.0109 0.1631  -0.2685 -0.1434 250 ARG   A N   
1647 C  CA  . ARG   A 230 ? 2.6292 2.0291 1.9502 0.2007  -0.2492 -0.1408 250 ARG   A CA  
1648 C  C   . ARG   A 230 ? 2.6940 2.0160 1.9226 0.2287  -0.2730 -0.1687 250 ARG   A C   
1649 O  O   . ARG   A 230 ? 2.7306 2.0127 1.8866 0.2612  -0.2439 -0.1662 250 ARG   A O   
1650 C  CB  . ARG   A 230 ? 2.5815 2.0125 1.9024 0.2036  -0.2576 -0.1331 250 ARG   A CB  
1651 C  CG  . ARG   A 230 ? 2.5104 1.9994 1.8828 0.1938  -0.2184 -0.1026 250 ARG   A CG  
1652 C  CD  . ARG   A 230 ? 2.4244 1.9449 1.8107 0.1917  -0.2356 -0.0984 250 ARG   A CD  
1653 N  NE  . ARG   A 230 ? 2.4969 1.9745 1.7938 0.2252  -0.2397 -0.1016 250 ARG   A NE  
1654 C  CZ  . ARG   A 230 ? 2.5730 2.0588 1.8583 0.2321  -0.2636 -0.1033 250 ARG   A CZ  
1655 N  NH1 . ARG   A 230 ? 2.5738 2.1115 1.9332 0.2091  -0.2860 -0.1041 250 ARG   A NH1 
1656 N  NH2 . ARG   A 230 ? 2.5391 1.9796 1.7343 0.2652  -0.2641 -0.1035 250 ARG   A NH2 
1657 N  N   . LYS   A 231 ? 2.7728 2.0723 2.0033 0.2173  -0.3260 -0.1958 251 LYS   A N   
1658 C  CA  . LYS   A 231 ? 2.8639 2.0841 2.0076 0.2423  -0.3546 -0.2266 251 LYS   A CA  
1659 C  C   . LYS   A 231 ? 2.8436 2.0278 1.9974 0.2350  -0.3516 -0.2367 251 LYS   A C   
1660 O  O   . LYS   A 231 ? 2.9041 2.0195 1.9747 0.2657  -0.3514 -0.2547 251 LYS   A O   
1661 C  CB  . LYS   A 231 ? 2.9922 2.2003 2.1314 0.2343  -0.4180 -0.2539 251 LYS   A CB  
1662 C  CG  . LYS   A 231 ? 2.9733 2.2259 2.2207 0.1878  -0.4498 -0.2577 251 LYS   A CG  
1663 C  CD  . LYS   A 231 ? 2.9909 2.2591 2.2529 0.1796  -0.5045 -0.2755 251 LYS   A CD  
1664 C  CE  . LYS   A 231 ? 2.9383 2.2649 2.3198 0.1322  -0.5279 -0.2732 251 LYS   A CE  
1665 N  NZ  . LYS   A 231 ? 2.9691 2.2624 2.3794 0.1093  -0.5394 -0.2850 251 LYS   A NZ  
1666 N  N   . SER   A 232 ? 2.7909 2.0175 2.0411 0.1973  -0.3483 -0.2248 252 SER   A N   
1667 C  CA  . SER   A 232 ? 2.8207 2.0123 2.0818 0.1912  -0.3419 -0.2299 252 SER   A CA  
1668 C  C   . SER   A 232 ? 2.8217 1.9977 2.0392 0.2224  -0.2887 -0.2147 252 SER   A C   
1669 O  O   . SER   A 232 ? 2.8534 1.9722 2.0308 0.2393  -0.2858 -0.2280 252 SER   A O   
1670 C  CB  . SER   A 232 ? 2.6358 1.8804 2.0075 0.1458  -0.3430 -0.2140 252 SER   A CB  
1671 O  OG  . SER   A 232 ? 2.6174 1.8765 2.0368 0.1156  -0.3916 -0.2284 252 SER   A OG  
1672 N  N   . VAL   A 233 ? 2.7637 1.9901 1.9919 0.2305  -0.2468 -0.1869 253 VAL   A N   
1673 C  CA  . VAL   A 233 ? 2.7389 1.9592 1.9343 0.2593  -0.1951 -0.1705 253 VAL   A CA  
1674 C  C   . VAL   A 233 ? 2.9538 2.1037 2.0352 0.3050  -0.1930 -0.1895 253 VAL   A C   
1675 O  O   . VAL   A 233 ? 3.0357 2.1420 2.0764 0.3294  -0.1750 -0.1965 253 VAL   A O   
1676 C  CB  . VAL   A 233 ? 2.4738 1.7633 1.7099 0.2546  -0.1550 -0.1373 253 VAL   A CB  
1677 C  CG1 . VAL   A 233 ? 2.4769 1.7576 1.6678 0.2890  -0.1039 -0.1218 253 VAL   A CG1 
1678 C  CG2 . VAL   A 233 ? 2.3523 1.7044 1.6923 0.2167  -0.1478 -0.1180 253 VAL   A CG2 
1679 N  N   . LYS   A 234 ? 2.9310 2.0669 1.9552 0.3198  -0.2118 -0.1985 254 LYS   A N   
1680 C  CA  . LYS   A 234 ? 3.1077 2.1771 2.0141 0.3667  -0.2070 -0.2143 254 LYS   A CA  
1681 C  C   . LYS   A 234 ? 3.2650 2.2550 2.1144 0.3793  -0.2476 -0.2530 254 LYS   A C   
1682 O  O   . LYS   A 234 ? 3.3582 2.2859 2.1053 0.4224  -0.2391 -0.2680 254 LYS   A O   
1683 C  CB  . LYS   A 234 ? 3.1463 2.2176 2.0022 0.3800  -0.2201 -0.2132 254 LYS   A CB  
1684 C  CG  . LYS   A 234 ? 3.2376 2.2897 2.0882 0.3657  -0.2869 -0.2419 254 LYS   A CG  
1685 C  CD  . LYS   A 234 ? 3.2932 2.3316 2.0688 0.3916  -0.2981 -0.2425 254 LYS   A CD  
1686 C  CE  . LYS   A 234 ? 3.3703 2.3413 2.0182 0.4443  -0.2741 -0.2489 254 LYS   A CE  
1687 N  NZ  . LYS   A 234 ? 3.2776 2.2314 1.8447 0.4720  -0.2819 -0.2459 254 LYS   A NZ  
1688 N  N   . ARG   A 235 ? 3.3018 2.2903 2.2128 0.3435  -0.2910 -0.2692 255 ARG   A N   
1689 C  CA  . ARG   A 235 ? 3.3614 2.2727 2.2314 0.3514  -0.3248 -0.3032 255 ARG   A CA  
1690 C  C   . ARG   A 235 ? 3.4119 2.3024 2.2772 0.3688  -0.2830 -0.2952 255 ARG   A C   
1691 O  O   . ARG   A 235 ? 3.4564 2.2784 2.2308 0.4101  -0.2758 -0.3142 255 ARG   A O   
1692 C  CB  . ARG   A 235 ? 3.3757 2.2956 2.3260 0.3038  -0.3777 -0.3175 255 ARG   A CB  
1693 C  CG  . ARG   A 235 ? 3.4277 2.3507 2.3738 0.2911  -0.4324 -0.3366 255 ARG   A CG  
1694 C  CD  . ARG   A 235 ? 3.4450 2.3556 2.4566 0.2500  -0.4870 -0.3576 255 ARG   A CD  
1695 N  NE  . ARG   A 235 ? 3.4752 2.4297 2.5361 0.2231  -0.5298 -0.3624 255 ARG   A NE  
1696 C  CZ  . ARG   A 235 ? 3.3477 2.3844 2.5169 0.1835  -0.5241 -0.3382 255 ARG   A CZ  
1697 N  NH1 . ARG   A 235 ? 3.2744 2.3571 2.5120 0.1645  -0.4800 -0.3078 255 ARG   A NH1 
1698 N  NH2 . ARG   A 235 ? 3.3840 2.4582 2.5923 0.1647  -0.5643 -0.3452 255 ARG   A NH2 
1699 N  N   . MET   A 236 ? 3.3910 2.3405 2.3522 0.3401  -0.2555 -0.2673 256 MET   A N   
1700 C  CA  . MET   A 236 ? 3.3623 2.3004 2.3290 0.3561  -0.2164 -0.2569 256 MET   A CA  
1701 C  C   . MET   A 236 ? 3.3457 2.2882 2.2520 0.4012  -0.1616 -0.2416 256 MET   A C   
1702 O  O   . MET   A 236 ? 3.2866 2.1914 2.1535 0.4334  -0.1359 -0.2459 256 MET   A O   
1703 C  CB  . MET   A 236 ? 3.2035 2.2097 2.2848 0.3162  -0.2004 -0.2280 256 MET   A CB  
1704 C  CG  . MET   A 236 ? 3.2092 2.2305 2.3625 0.2674  -0.2468 -0.2345 256 MET   A CG  
1705 S  SD  . MET   A 236 ? 3.1449 2.2425 2.4207 0.2252  -0.2245 -0.1991 256 MET   A SD  
1706 C  CE  . MET   A 236 ? 3.0942 2.2068 2.4368 0.1740  -0.2796 -0.2095 256 MET   A CE  
1707 N  N   . LYS   A 237 ? 3.3961 2.3839 2.2960 0.4047  -0.1422 -0.2227 257 LYS   A N   
1708 C  CA  . LYS   A 237 ? 3.3565 2.3504 2.2020 0.4450  -0.0883 -0.2050 257 LYS   A CA  
1709 C  C   . LYS   A 237 ? 3.4331 2.3418 2.1542 0.4952  -0.0918 -0.2330 257 LYS   A C   
1710 O  O   . LYS   A 237 ? 3.4335 2.3246 2.1144 0.5323  -0.0492 -0.2278 257 LYS   A O   
1711 C  CB  . LYS   A 237 ? 3.2614 2.3084 2.1171 0.4374  -0.0736 -0.1813 257 LYS   A CB  
1712 C  CG  . LYS   A 237 ? 3.0599 2.1936 2.0277 0.3992  -0.0532 -0.1487 257 LYS   A CG  
1713 C  CD  . LYS   A 237 ? 3.0380 2.2143 2.0019 0.4034  -0.0239 -0.1224 257 LYS   A CD  
1714 C  CE  . LYS   A 237 ? 3.0800 2.2443 1.9852 0.4451  0.0305  -0.1072 257 LYS   A CE  
1715 N  NZ  . LYS   A 237 ? 2.9778 2.1836 1.8873 0.4458  0.0628  -0.0772 257 LYS   A NZ  
1716 N  N   . GLU   A 238 ? 3.4475 2.3035 2.1058 0.4988  -0.1429 -0.2637 258 GLU   A N   
1717 C  CA  . GLU   A 238 ? 3.5780 2.3488 2.1068 0.5486  -0.1515 -0.2932 258 GLU   A CA  
1718 C  C   . GLU   A 238 ? 3.6097 2.3039 2.1102 0.5554  -0.1875 -0.3304 258 GLU   A C   
1719 O  O   . GLU   A 238 ? 3.5834 2.1987 1.9720 0.5993  -0.1965 -0.3592 258 GLU   A O   
1720 C  CB  . GLU   A 238 ? 3.5872 2.3362 2.0498 0.5550  -0.1895 -0.3078 258 GLU   A CB  
1721 C  CG  . GLU   A 238 ? 3.6316 2.3439 1.9717 0.6105  -0.1563 -0.3052 258 GLU   A CG  
1722 C  CD  . GLU   A 238 ? 3.6881 2.3809 1.9624 0.6180  -0.1938 -0.3161 258 GLU   A CD  
1723 O  OE1 . GLU   A 238 ? 3.7383 2.4620 2.0773 0.5778  -0.2395 -0.3202 258 GLU   A OE1 
1724 O  OE2 . GLU   A 238 ? 3.5924 2.2537 1.7728 0.6598  -0.1763 -0.3123 258 GLU   A OE2 
1725 N  N   . SER   A 239 ? 3.5851 2.2966 2.1800 0.5141  -0.2084 -0.3305 259 SER   A N   
1726 C  CA  . SER   A 239 ? 3.6095 2.2471 2.1836 0.5212  -0.2341 -0.3605 259 SER   A CA  
1727 C  C   . SER   A 239 ? 3.5660 2.2007 2.1356 0.5528  -0.1787 -0.3462 259 SER   A C   
1728 O  O   . SER   A 239 ? 3.6726 2.2299 2.1609 0.5937  -0.1789 -0.3722 259 SER   A O   
1729 C  CB  . SER   A 239 ? 3.5906 2.2432 2.2655 0.4641  -0.2787 -0.3644 259 SER   A CB  
1730 O  OG  . SER   A 239 ? 3.4984 2.2317 2.2816 0.4332  -0.2436 -0.3263 259 SER   A OG  
1731 N  N   . ARG   A 240 ? 3.5057 2.2240 2.1617 0.5363  -0.1324 -0.3062 260 ARG   A N   
1732 C  CA  . ARG   A 240 ? 3.4203 2.1508 2.0840 0.5658  -0.0777 -0.2885 260 ARG   A CA  
1733 C  C   . ARG   A 240 ? 3.2801 1.9973 1.8496 0.6219  -0.0319 -0.2851 260 ARG   A C   
1734 O  O   . ARG   A 240 ? 3.1541 1.8120 1.6504 0.6684  -0.0160 -0.3027 260 ARG   A O   
1735 C  CB  . ARG   A 240 ? 3.3174 2.1452 2.1005 0.5314  -0.0451 -0.2470 260 ARG   A CB  
1736 C  CG  . ARG   A 240 ? 3.2333 2.0842 2.1110 0.4756  -0.0839 -0.2444 260 ARG   A CG  
1737 C  CD  . ARG   A 240 ? 3.0346 1.9772 2.0177 0.4485  -0.0497 -0.2046 260 ARG   A CD  
1738 N  NE  . ARG   A 240 ? 2.9604 1.9301 2.0291 0.3960  -0.0832 -0.1990 260 ARG   A NE  
1739 C  CZ  . ARG   A 240 ? 2.7023 1.7394 1.8622 0.3688  -0.0645 -0.1695 260 ARG   A CZ  
1740 N  NH1 . ARG   A 240 ? 2.5030 1.5890 1.6878 0.3864  -0.0163 -0.1437 260 ARG   A NH1 
1741 N  NH2 . ARG   A 240 ? 2.5856 1.6422 1.8135 0.3234  -0.0952 -0.1655 260 ARG   A NH2 
1742 N  N   . ASP   A 250 ? 2.4672 1.7468 1.9391 0.3453  0.0597  -0.0449 270 ASP   A N   
1743 C  CA  . ASP   A 250 ? 2.3102 1.6433 1.8388 0.3004  0.0438  -0.0314 270 ASP   A CA  
1744 C  C   . ASP   A 250 ? 2.1829 1.5824 1.7284 0.2982  0.0685  -0.0159 270 ASP   A C   
1745 O  O   . ASP   A 250 ? 2.2178 1.6247 1.7359 0.3295  0.1000  -0.0127 270 ASP   A O   
1746 C  CB  . ASP   A 250 ? 2.3190 1.6088 1.8254 0.2744  0.0012  -0.0525 270 ASP   A CB  
1747 C  CG  . ASP   A 250 ? 2.3810 1.5996 1.8009 0.3021  -0.0107 -0.0824 270 ASP   A CG  
1748 O  OD1 . ASP   A 250 ? 2.3920 1.6218 1.7718 0.3233  0.0081  -0.0841 270 ASP   A OD1 
1749 O  OD2 . ASP   A 250 ? 2.4344 1.5829 1.8241 0.3029  -0.0396 -0.1041 270 ASP   A OD2 
1750 N  N   . PHE   A 251 ? 2.0394 1.4860 1.6309 0.2615  0.0551  -0.0056 271 PHE   A N   
1751 C  CA  . PHE   A 251 ? 1.9715 1.4769 1.5822 0.2560  0.0747  0.0090  271 PHE   A CA  
1752 C  C   . PHE   A 251 ? 1.9981 1.4740 1.5406 0.2758  0.0787  -0.0046 271 PHE   A C   
1753 O  O   . PHE   A 251 ? 1.8521 1.3518 1.3837 0.2950  0.1109  0.0068  271 PHE   A O   
1754 C  CB  . PHE   A 251 ? 1.8932 1.4444 1.5578 0.2153  0.0552  0.0182  271 PHE   A CB  
1755 C  CG  . PHE   A 251 ? 1.7720 1.3699 1.5039 0.1993  0.0613  0.0385  271 PHE   A CG  
1756 C  CD1 . PHE   A 251 ? 1.6240 1.2605 1.3846 0.2152  0.0911  0.0557  271 PHE   A CD1 
1757 C  CD2 . PHE   A 251 ? 1.6886 1.2928 1.4553 0.1689  0.0369  0.0409  271 PHE   A CD2 
1758 C  CE1 . PHE   A 251 ? 1.5422 1.2203 1.3607 0.2024  0.0927  0.0730  271 PHE   A CE1 
1759 C  CE2 . PHE   A 251 ? 1.5783 1.2223 1.3983 0.1570  0.0423  0.0601  271 PHE   A CE2 
1760 C  CZ  . PHE   A 251 ? 1.5136 1.1930 1.3572 0.1745  0.0683  0.0751  271 PHE   A CZ  
1761 N  N   . LEU   A 252 ? 2.0993 1.5228 1.5955 0.2711  0.0453  -0.0283 272 LEU   A N   
1762 C  CA  . LEU   A 252 ? 2.0450 1.4311 1.4650 0.2938  0.0441  -0.0438 272 LEU   A CA  
1763 C  C   . LEU   A 252 ? 2.1468 1.5041 1.5120 0.3391  0.0786  -0.0452 272 LEU   A C   
1764 O  O   . LEU   A 252 ? 2.1506 1.5132 1.4759 0.3601  0.1031  -0.0396 272 LEU   A O   
1765 C  CB  . LEU   A 252 ? 2.1454 1.4715 1.5245 0.2852  -0.0022 -0.0729 272 LEU   A CB  
1766 C  CG  . LEU   A 252 ? 2.1873 1.4529 1.4710 0.3152  -0.0124 -0.0966 272 LEU   A CG  
1767 C  CD1 . LEU   A 252 ? 2.1027 1.3987 1.3714 0.3131  -0.0078 -0.0885 272 LEU   A CD1 
1768 C  CD2 . LEU   A 252 ? 2.3943 1.5967 1.6490 0.3054  -0.0624 -0.1276 272 LEU   A CD2 
1769 N  N   . GLN   A 253 ? 2.0942 1.4205 1.4566 0.3560  0.0827  -0.0513 273 GLN   A N   
1770 C  CA  . GLN   A 253 ? 2.1145 1.4187 1.4315 0.4021  0.1187  -0.0519 273 GLN   A CA  
1771 C  C   . GLN   A 253 ? 2.0915 1.4682 1.4532 0.4090  0.1654  -0.0214 273 GLN   A C   
1772 O  O   . GLN   A 253 ? 2.1593 1.5385 1.4786 0.4336  0.1949  -0.0161 273 GLN   A O   
1773 C  CB  . GLN   A 253 ? 2.2920 1.5566 1.6121 0.4164  0.1132  -0.0614 273 GLN   A CB  
1774 C  CG  . GLN   A 253 ? 2.3753 1.6191 1.6539 0.4672  0.1511  -0.0626 273 GLN   A CG  
1775 C  CD  . GLN   A 253 ? 2.4877 1.6848 1.7664 0.4825  0.1411  -0.0739 273 GLN   A CD  
1776 O  OE1 . GLN   A 253 ? 2.5271 1.7057 1.8370 0.4527  0.1061  -0.0789 273 GLN   A OE1 
1777 N  NE2 . GLN   A 253 ? 2.5683 1.7451 1.8119 0.5301  0.1730  -0.0767 273 GLN   A NE2 
1778 N  N   . LEU   A 254 ? 2.1918 1.6283 1.6399 0.3858  0.1715  -0.0005 274 LEU   A N   
1779 C  CA  . LEU   A 254 ? 2.0837 1.5914 1.5850 0.3887  0.2113  0.0276  274 LEU   A CA  
1780 C  C   . LEU   A 254 ? 2.1095 1.6445 1.6018 0.3777  0.2217  0.0379  274 LEU   A C   
1781 O  O   . LEU   A 254 ? 2.0367 1.6045 1.5351 0.3936  0.2609  0.0560  274 LEU   A O   
1782 C  CB  . LEU   A 254 ? 1.8314 1.3951 1.4234 0.3606  0.2049  0.0449  274 LEU   A CB  
1783 C  CG  . LEU   A 254 ? 1.8492 1.3898 1.4568 0.3707  0.1957  0.0401  274 LEU   A CG  
1784 C  CD1 . LEU   A 254 ? 1.6923 1.2903 1.3839 0.3431  0.1885  0.0592  274 LEU   A CD1 
1785 C  CD2 . LEU   A 254 ? 1.7883 1.3158 1.3721 0.4173  0.2300  0.0404  274 LEU   A CD2 
1786 N  N   . MET   A 255 ? 2.0383 1.5601 1.5181 0.3509  0.1875  0.0276  275 MET   A N   
1787 C  CA  . MET   A 255 ? 2.0702 1.6090 1.5338 0.3432  0.1939  0.0360  275 MET   A CA  
1788 C  C   . MET   A 255 ? 2.1590 1.6462 1.5281 0.3796  0.2085  0.0257  275 MET   A C   
1789 O  O   . MET   A 255 ? 2.1921 1.6983 1.5469 0.3906  0.2400  0.0429  275 MET   A O   
1790 C  CB  . MET   A 255 ? 1.9499 1.4914 1.4292 0.3076  0.1522  0.0273  275 MET   A CB  
1791 C  CG  . MET   A 255 ? 1.8899 1.4874 1.4575 0.2724  0.1422  0.0406  275 MET   A CG  
1792 S  SD  . MET   A 255 ? 2.0151 1.6266 1.6011 0.2354  0.1034  0.0345  275 MET   A SD  
1793 C  CE  . MET   A 255 ? 1.7297 1.3458 1.2766 0.2469  0.1226  0.0438  275 MET   A CE  
1794 N  N   . ILE   A 256 ? 2.2031 1.6218 1.5042 0.3987  0.1854  -0.0019 276 ILE   A N   
1795 C  CA  . ILE   A 256 ? 2.3500 1.7135 1.5510 0.4389  0.1987  -0.0142 276 ILE   A CA  
1796 C  C   . ILE   A 256 ? 2.4345 1.8136 1.6288 0.4752  0.2536  0.0025  276 ILE   A C   
1797 O  O   . ILE   A 256 ? 2.5162 1.8893 1.6579 0.5011  0.2859  0.0123  276 ILE   A O   
1798 C  CB  . ILE   A 256 ? 2.3222 1.6060 1.4551 0.4516  0.1584  -0.0506 276 ILE   A CB  
1799 C  CG1 . ILE   A 256 ? 2.3388 1.6072 1.4654 0.4210  0.1074  -0.0665 276 ILE   A CG1 
1800 C  CG2 . ILE   A 256 ? 2.2467 1.4696 1.2730 0.5025  0.1779  -0.0648 276 ILE   A CG2 
1801 C  CD1 . ILE   A 256 ? 2.4075 1.5966 1.4673 0.4313  0.0636  -0.1034 276 ILE   A CD1 
1802 N  N   . ASP   A 257 ? 2.3719 1.7733 1.6208 0.4785  0.2661  0.0078  277 ASP   A N   
1803 C  CA  . ASP   A 257 ? 2.3655 1.7954 1.6259 0.5112  0.3191  0.0261  277 ASP   A CA  
1804 C  C   . ASP   A 257 ? 2.3997 1.9029 1.7182 0.4962  0.3547  0.0602  277 ASP   A C   
1805 O  O   . ASP   A 257 ? 2.4452 1.9670 1.7525 0.5245  0.4029  0.0775  277 ASP   A O   
1806 C  CB  . ASP   A 257 ? 2.3583 1.8029 1.6759 0.5151  0.3197  0.0260  277 ASP   A CB  
1807 C  CG  . ASP   A 257 ? 2.3781 1.7469 1.6465 0.5247  0.2816  -0.0063 277 ASP   A CG  
1808 O  OD1 . ASP   A 257 ? 2.3718 1.6765 1.5593 0.5318  0.2560  -0.0305 277 ASP   A OD1 
1809 O  OD2 . ASP   A 257 ? 2.2875 1.6591 1.5990 0.5246  0.2751  -0.0072 277 ASP   A OD2 
1810 N  N   . SER   A 258 ? 2.4343 1.9788 1.8155 0.4522  0.3325  0.0704  278 SER   A N   
1811 C  CA  . SER   A 258 ? 2.4380 2.0472 1.8776 0.4344  0.3612  0.1010  278 SER   A CA  
1812 C  C   . SER   A 258 ? 2.4781 2.0650 1.8491 0.4487  0.3816  0.1087  278 SER   A C   
1813 O  O   . SER   A 258 ? 2.4519 2.0702 1.8350 0.4616  0.4281  0.1339  278 SER   A O   
1814 C  CB  . SER   A 258 ? 2.1975 1.8475 1.7114 0.3868  0.3288  0.1059  278 SER   A CB  
1815 O  OG  . SER   A 258 ? 2.2411 1.8551 1.7114 0.3704  0.2913  0.0900  278 SER   A OG  
1816 N  N   . GLN   A 259 ? 2.4938 2.0270 1.7936 0.4468  0.3474  0.0886  279 GLN   A N   
1817 C  CA  . GLN   A 259 ? 2.4616 1.9664 1.6857 0.4638  0.3634  0.0954  279 GLN   A CA  
1818 C  C   . GLN   A 259 ? 2.6720 2.1365 1.8116 0.5148  0.4010  0.0932  279 GLN   A C   
1819 O  O   . GLN   A 259 ? 2.7736 2.2132 1.8428 0.5345  0.4214  0.1022  279 GLN   A O   
1820 C  CB  . GLN   A 259 ? 2.4633 1.9222 1.6336 0.4512  0.3126  0.0726  279 GLN   A CB  
1821 C  CG  . GLN   A 259 ? 2.5001 1.8951 1.6097 0.4663  0.2738  0.0359  279 GLN   A CG  
1822 C  CD  . GLN   A 259 ? 2.5527 1.9061 1.6096 0.4561  0.2252  0.0148  279 GLN   A CD  
1823 O  OE1 . GLN   A 259 ? 2.6748 1.9760 1.6863 0.4629  0.1868  -0.0162 279 GLN   A OE1 
1824 N  NE2 . GLN   A 259 ? 2.4364 1.8123 1.5016 0.4399  0.2251  0.0313  279 GLN   A NE2 
1825 N  N   . ASN   A 260 ? 2.5645 2.0197 1.7053 0.5388  0.4113  0.0819  280 ASN   A N   
1826 C  CA  . ASN   A 260 ? 2.6582 2.0863 1.7305 0.5902  0.4556  0.0831  280 ASN   A CA  
1827 C  C   . ASN   A 260 ? 2.5643 2.0622 1.7007 0.5951  0.5170  0.1217  280 ASN   A C   
1828 O  O   . ASN   A 260 ? 2.4669 2.0126 1.6815 0.5947  0.5348  0.1308  280 ASN   A O   
1829 C  CB  . ASN   A 260 ? 2.6425 2.0328 1.6944 0.6162  0.4435  0.0560  280 ASN   A CB  
1830 C  CG  . ASN   A 260 ? 2.6803 1.9787 1.6210 0.6371  0.4034  0.0177  280 ASN   A CG  
1831 O  OD1 . ASN   A 260 ? 2.6649 1.9261 1.5282 0.6442  0.3940  0.0125  280 ASN   A OD1 
1832 N  ND2 . ASN   A 260 ? 2.6514 1.9099 1.5826 0.6478  0.3778  -0.0094 280 ASN   A ND2 
1833 N  N   . SER   A 266 ? 2.1610 2.1207 1.9510 0.3751  0.6546  0.3374  286 SER   A N   
1834 C  CA  . SER   A 266 ? 2.2661 2.2068 2.0317 0.3573  0.6626  0.3567  286 SER   A CA  
1835 C  C   . SER   A 266 ? 2.3332 2.2223 2.0435 0.3407  0.6078  0.3322  286 SER   A C   
1836 O  O   . SER   A 266 ? 2.3218 2.1634 1.9592 0.3599  0.5795  0.3031  286 SER   A O   
1837 C  CB  . SER   A 266 ? 2.1338 2.1399 2.0142 0.3199  0.6783  0.3864  286 SER   A CB  
1838 O  OG  . SER   A 266 ? 1.9677 2.0069 1.9261 0.2861  0.6325  0.3713  286 SER   A OG  
1839 N  N   . HIS   A 267 ? 2.0643 1.9637 1.8132 0.3051  0.5927  0.3441  287 HIS   A N   
1840 C  CA  . HIS   A 267 ? 2.0646 1.9229 1.7717 0.2881  0.5439  0.3249  287 HIS   A CA  
1841 C  C   . HIS   A 267 ? 2.1648 1.9527 1.7471 0.3201  0.5469  0.3177  287 HIS   A C   
1842 O  O   . HIS   A 267 ? 2.3039 2.0759 1.8458 0.3361  0.5886  0.3433  287 HIS   A O   
1843 C  CB  . HIS   A 267 ? 1.9098 1.7814 1.6528 0.2728  0.4946  0.2948  287 HIS   A CB  
1844 C  CG  . HIS   A 267 ? 1.6998 1.6310 1.5532 0.2365  0.4816  0.3017  287 HIS   A CG  
1845 N  ND1 . HIS   A 267 ? 1.6036 1.5449 1.4946 0.2054  0.4712  0.3136  287 HIS   A ND1 
1846 C  CD2 . HIS   A 267 ? 1.5843 1.5645 1.5143 0.2281  0.4748  0.2972  287 HIS   A CD2 
1847 C  CE1 . HIS   A 267 ? 1.5762 1.5700 1.5611 0.1792  0.4579  0.3146  287 HIS   A CE1 
1848 N  NE2 . HIS   A 267 ? 1.5160 1.5355 1.5261 0.1925  0.4596  0.3054  287 HIS   A NE2 
1849 N  N   . LYS   A 268 ? 2.2115 1.9556 1.7301 0.3304  0.5044  0.2849  288 LYS   A N   
1850 C  CA  . LYS   A 268 ? 2.4162 2.0920 1.8152 0.3606  0.5000  0.2750  288 LYS   A CA  
1851 C  C   . LYS   A 268 ? 2.2722 1.9102 1.6153 0.3796  0.4635  0.2372  288 LYS   A C   
1852 O  O   . LYS   A 268 ? 2.4062 1.9901 1.6660 0.3920  0.4343  0.2189  288 LYS   A O   
1853 C  CB  . LYS   A 268 ? 2.3613 2.0104 1.7333 0.3436  0.4746  0.2788  288 LYS   A CB  
1854 C  CG  . LYS   A 268 ? 2.4344 2.0768 1.7896 0.3463  0.5171  0.3159  288 LYS   A CG  
1855 C  CD  . LYS   A 268 ? 2.4655 2.0948 1.8270 0.3209  0.4890  0.3213  288 LYS   A CD  
1856 C  CE  . LYS   A 268 ? 2.3752 1.9962 1.7279 0.3201  0.5321  0.3615  288 LYS   A CE  
1857 N  NZ  . LYS   A 268 ? 2.3282 1.9514 1.7231 0.2872  0.5085  0.3701  288 LYS   A NZ  
1858 N  N   . ALA   A 269 ? 2.0451 1.7095 1.4345 0.3816  0.4625  0.2252  289 ALA   A N   
1859 C  CA  . ALA   A 269 ? 2.1210 1.7504 1.4706 0.3954  0.4277  0.1905  289 ALA   A CA  
1860 C  C   . ALA   A 269 ? 2.0714 1.6905 1.4315 0.3666  0.3695  0.1683  289 ALA   A C   
1861 O  O   . ALA   A 269 ? 2.0529 1.7048 1.4711 0.3343  0.3572  0.1790  289 ALA   A O   
1862 C  CB  . ALA   A 269 ? 2.1241 1.6877 1.3548 0.4404  0.4387  0.1779  289 ALA   A CB  
1863 N  N   . LEU   A 270 ? 2.1105 1.6845 1.4172 0.3780  0.3337  0.1372  290 LEU   A N   
1864 C  CA  . LEU   A 270 ? 2.0049 1.5731 1.3277 0.3514  0.2798  0.1157  290 LEU   A CA  
1865 C  C   . LEU   A 270 ? 2.0782 1.5825 1.3041 0.3696  0.2491  0.0931  290 LEU   A C   
1866 O  O   . LEU   A 270 ? 2.2590 1.7150 1.4096 0.4024  0.2530  0.0780  290 LEU   A O   
1867 C  CB  . LEU   A 270 ? 1.9269 1.5105 1.3017 0.3391  0.2589  0.0995  290 LEU   A CB  
1868 C  CG  . LEU   A 270 ? 1.7193 1.3645 1.1970 0.3015  0.2500  0.1104  290 LEU   A CG  
1869 C  CD1 . LEU   A 270 ? 1.7027 1.3554 1.2195 0.2941  0.2315  0.0964  290 LEU   A CD1 
1870 C  CD2 . LEU   A 270 ? 1.7643 1.4161 1.2539 0.2747  0.2176  0.1073  290 LEU   A CD2 
1871 N  N   . SER   A 271 ? 2.0965 1.6005 1.3247 0.3497  0.2165  0.0893  291 SER   A N   
1872 C  CA  . SER   A 271 ? 2.0124 1.4622 1.1562 0.3649  0.1827  0.0690  291 SER   A CA  
1873 C  C   . SER   A 271 ? 2.2816 1.7067 1.4190 0.3599  0.1362  0.0349  291 SER   A C   
1874 O  O   . SER   A 271 ? 2.1960 1.6413 1.3884 0.3465  0.1332  0.0287  291 SER   A O   
1875 C  CB  . SER   A 271 ? 1.9879 1.4508 1.1442 0.3465  0.1645  0.0783  291 SER   A CB  
1876 O  OG  . SER   A 271 ? 1.9947 1.4194 1.0982 0.3517  0.1169  0.0532  291 SER   A OG  
1877 N  N   . ASP   A 272 ? 2.4315 1.8108 1.5014 0.3706  0.0981  0.0132  292 ASP   A N   
1878 C  CA  . ASP   A 272 ? 2.4166 1.7689 1.4803 0.3636  0.0493  -0.0198 292 ASP   A CA  
1879 C  C   . ASP   A 272 ? 2.2647 1.6561 1.4032 0.3249  0.0105  -0.0251 292 ASP   A C   
1880 O  O   . ASP   A 272 ? 2.2714 1.6730 1.4588 0.3040  -0.0133 -0.0393 292 ASP   A O   
1881 C  CB  . ASP   A 272 ? 2.6381 1.9203 1.5912 0.3960  0.0239  -0.0436 292 ASP   A CB  
1882 C  CG  . ASP   A 272 ? 2.7892 2.0273 1.6604 0.4383  0.0611  -0.0427 292 ASP   A CG  
1883 O  OD1 . ASP   A 272 ? 2.7810 2.0310 1.6835 0.4412  0.0889  -0.0385 292 ASP   A OD1 
1884 O  OD2 . ASP   A 272 ? 2.9039 2.0959 1.6779 0.4707  0.0632  -0.0456 292 ASP   A OD2 
1885 N  N   . LEU   A 273 ? 2.0445 1.4569 1.1919 0.3163  0.0049  -0.0130 293 LEU   A N   
1886 C  CA  . LEU   A 273 ? 1.9559 1.4127 1.1795 0.2820  -0.0253 -0.0152 293 LEU   A CA  
1887 C  C   . LEU   A 273 ? 1.8313 1.3457 1.1480 0.2551  -0.0014 0.0026  293 LEU   A C   
1888 O  O   . LEU   A 273 ? 1.7383 1.2832 1.1190 0.2282  -0.0240 -0.0049 293 LEU   A O   
1889 C  CB  . LEU   A 273 ? 1.8932 1.3550 1.0998 0.2841  -0.0352 -0.0064 293 LEU   A CB  
1890 C  CG  . LEU   A 273 ? 1.8562 1.3651 1.1380 0.2535  -0.0646 -0.0088 293 LEU   A CG  
1891 C  CD1 . LEU   A 273 ? 1.9470 1.4468 1.2367 0.2435  -0.1139 -0.0379 293 LEU   A CD1 
1892 C  CD2 . LEU   A 273 ? 1.8430 1.3559 1.1085 0.2594  -0.0673 0.0036  293 LEU   A CD2 
1893 N  N   . GLU   A 274 ? 1.8085 1.3393 1.1342 0.2623  0.0439  0.0268  294 GLU   A N   
1894 C  CA  . GLU   A 274 ? 1.6581 1.2423 1.0691 0.2392  0.0646  0.0429  294 GLU   A CA  
1895 C  C   . GLU   A 274 ? 1.5645 1.1486 1.0019 0.2342  0.0595  0.0312  294 GLU   A C   
1896 O  O   . GLU   A 274 ? 1.5744 1.1966 1.0813 0.2084  0.0500  0.0328  294 GLU   A O   
1897 C  CB  . GLU   A 274 ? 1.7023 1.3018 1.1174 0.2493  0.1127  0.0702  294 GLU   A CB  
1898 C  CG  . GLU   A 274 ? 1.8339 1.4318 1.2286 0.2514  0.1206  0.0860  294 GLU   A CG  
1899 C  CD  . GLU   A 274 ? 1.8372 1.4413 1.2275 0.2632  0.1701  0.1140  294 GLU   A CD  
1900 O  OE1 . GLU   A 274 ? 1.7709 1.3942 1.1911 0.2661  0.1980  0.1218  294 GLU   A OE1 
1901 O  OE2 . GLU   A 274 ? 1.8187 1.4091 1.1779 0.2699  0.1812  0.1292  294 GLU   A OE2 
1902 N  N   . LEU   A 275 ? 1.6997 1.2375 1.0778 0.2604  0.0656  0.0195  295 LEU   A N   
1903 C  CA  . LEU   A 275 ? 1.6897 1.2174 1.0858 0.2590  0.0599  0.0078  295 LEU   A CA  
1904 C  C   . LEU   A 275 ? 1.6617 1.1906 1.0907 0.2325  0.0150  -0.0103 295 LEU   A C   
1905 O  O   . LEU   A 275 ? 1.6339 1.1810 1.1158 0.2153  0.0112  -0.0097 295 LEU   A O   
1906 C  CB  . LEU   A 275 ? 1.8842 1.3515 1.1980 0.2955  0.0686  -0.0063 295 LEU   A CB  
1907 C  CG  . LEU   A 275 ? 1.9457 1.4018 1.2702 0.3067  0.0838  -0.0097 295 LEU   A CG  
1908 C  CD1 . LEU   A 275 ? 2.0448 1.5163 1.3625 0.3321  0.1363  0.0116  295 LEU   A CD1 
1909 C  CD2 . LEU   A 275 ? 2.1098 1.4959 1.3658 0.3258  0.0561  -0.0401 295 LEU   A CD2 
1910 N  N   . VAL   A 276 ? 1.6814 1.1922 1.0814 0.2292  -0.0189 -0.0252 296 VAL   A N   
1911 C  CA  . VAL   A 276 ? 1.6478 1.1670 1.0876 0.2022  -0.0605 -0.0406 296 VAL   A CA  
1912 C  C   . VAL   A 276 ? 1.5897 1.1745 1.1146 0.1713  -0.0571 -0.0238 296 VAL   A C   
1913 O  O   . VAL   A 276 ? 1.6127 1.2175 1.1915 0.1477  -0.0709 -0.0258 296 VAL   A O   
1914 C  CB  . VAL   A 276 ? 1.7777 1.2661 1.1690 0.2084  -0.0990 -0.0607 296 VAL   A CB  
1915 C  CG1 . VAL   A 276 ? 1.8399 1.3428 1.2825 0.1787  -0.1410 -0.0756 296 VAL   A CG1 
1916 C  CG2 . VAL   A 276 ? 2.0640 1.4827 1.3610 0.2423  -0.1035 -0.0791 296 VAL   A CG2 
1917 N  N   . ALA   A 277 ? 1.4706 1.0866 1.0059 0.1718  -0.0387 -0.0067 297 ALA   A N   
1918 C  CA  . ALA   A 277 ? 1.4071 1.0813 1.0155 0.1459  -0.0370 0.0067  297 ALA   A CA  
1919 C  C   . ALA   A 277 ? 1.3566 1.0595 1.0186 0.1334  -0.0175 0.0186  297 ALA   A C   
1920 O  O   . ALA   A 277 ? 1.4174 1.1542 1.1351 0.1099  -0.0291 0.0204  297 ALA   A O   
1921 C  CB  . ALA   A 277 ? 1.3718 1.0639 0.9750 0.1517  -0.0188 0.0225  297 ALA   A CB  
1922 N  N   . GLN   A 278 ? 1.3315 1.0225 0.9770 0.1507  0.0127  0.0276  298 GLN   A N   
1923 C  CA  . GLN   A 278 ? 1.3997 1.1173 1.0942 0.1427  0.0296  0.0389  298 GLN   A CA  
1924 C  C   . GLN   A 278 ? 1.3576 1.0581 1.0646 0.1323  0.0076  0.0268  298 GLN   A C   
1925 O  O   . GLN   A 278 ? 1.2926 1.0247 1.0531 0.1129  0.0051  0.0346  298 GLN   A O   
1926 C  CB  . GLN   A 278 ? 1.4345 1.1422 1.1084 0.1670  0.0652  0.0496  298 GLN   A CB  
1927 C  CG  . GLN   A 278 ? 1.3757 1.0849 1.0221 0.1811  0.0890  0.0614  298 GLN   A CG  
1928 C  CD  . GLN   A 278 ? 1.2644 1.0207 0.9605 0.1610  0.0928  0.0763  298 GLN   A CD  
1929 O  OE1 . GLN   A 278 ? 1.2497 1.0459 1.0060 0.1418  0.0910  0.0830  298 GLN   A OE1 
1930 N  NE2 . GLN   A 278 ? 1.2805 1.0281 0.9472 0.1667  0.0972  0.0814  298 GLN   A NE2 
1931 N  N   . SER   A 279 ? 1.4063 1.0531 1.0616 0.1454  -0.0092 0.0078  299 SER   A N   
1932 C  CA  . SER   A 279 ? 1.3705 0.9927 1.0365 0.1340  -0.0323 -0.0044 299 SER   A CA  
1933 C  C   . SER   A 279 ? 1.3691 1.0244 1.0877 0.1015  -0.0579 -0.0047 299 SER   A C   
1934 O  O   . SER   A 279 ? 1.3853 1.0504 1.1450 0.0834  -0.0635 0.0000  299 SER   A O   
1935 C  CB  . SER   A 279 ? 1.4714 1.0265 1.0689 0.1529  -0.0517 -0.0284 299 SER   A CB  
1936 O  OG  . SER   A 279 ? 1.6418 1.1687 1.1823 0.1870  -0.0250 -0.0279 299 SER   A OG  
1937 N  N   . ILE   A 280 ? 1.3880 1.0613 1.1057 0.0953  -0.0721 -0.0086 300 ILE   A N   
1938 C  CA  . ILE   A 280 ? 1.3321 1.0446 1.1029 0.0674  -0.0928 -0.0078 300 ILE   A CA  
1939 C  C   . ILE   A 280 ? 1.3025 1.0691 1.1303 0.0529  -0.0722 0.0131  300 ILE   A C   
1940 O  O   . ILE   A 280 ? 1.3159 1.1069 1.1899 0.0309  -0.0805 0.0179  300 ILE   A O   
1941 C  CB  . ILE   A 280 ? 1.3272 1.0477 1.0820 0.0699  -0.1109 -0.0163 300 ILE   A CB  
1942 C  CG1 . ILE   A 280 ? 1.4427 1.1096 1.1443 0.0813  -0.1403 -0.0398 300 ILE   A CG1 
1943 C  CG2 . ILE   A 280 ? 1.2348 1.0078 1.0507 0.0448  -0.1247 -0.0121 300 ILE   A CG2 
1944 C  CD1 . ILE   A 280 ? 1.5739 1.2328 1.2329 0.0976  -0.1516 -0.0470 300 ILE   A CD1 
1945 N  N   . ILE   A 281 ? 1.3090 1.0940 1.1337 0.0649  -0.0453 0.0262  301 ILE   A N   
1946 C  CA  . ILE   A 281 ? 1.2862 1.1196 1.1609 0.0529  -0.0292 0.0435  301 ILE   A CA  
1947 C  C   . ILE   A 281 ? 1.2030 1.0326 1.0967 0.0506  -0.0199 0.0514  301 ILE   A C   
1948 O  O   . ILE   A 281 ? 1.2663 1.1323 1.2019 0.0374  -0.0148 0.0637  301 ILE   A O   
1949 C  CB  . ILE   A 281 ? 1.2318 1.0841 1.1026 0.0643  -0.0062 0.0545  301 ILE   A CB  
1950 C  CG1 . ILE   A 281 ? 1.3303 1.2328 1.2470 0.0483  -0.0056 0.0637  301 ILE   A CG1 
1951 C  CG2 . ILE   A 281 ? 1.2386 1.0856 1.1071 0.0782  0.0199  0.0650  301 ILE   A CG2 
1952 C  CD1 . ILE   A 281 ? 1.3718 1.2821 1.2772 0.0524  -0.0060 0.0633  301 ILE   A CD1 
1953 N  N   . PHE   A 282 ? 1.2031 0.9869 1.0632 0.0655  -0.0182 0.0443  302 PHE   A N   
1954 C  CA  . PHE   A 282 ? 1.2559 1.0297 1.1314 0.0654  -0.0120 0.0513  302 PHE   A CA  
1955 C  C   . PHE   A 282 ? 1.2978 1.0615 1.1944 0.0433  -0.0349 0.0476  302 PHE   A C   
1956 O  O   . PHE   A 282 ? 1.3004 1.0791 1.2295 0.0326  -0.0309 0.0607  302 PHE   A O   
1957 C  CB  . PHE   A 282 ? 1.2702 0.9963 1.1010 0.0926  -0.0007 0.0444  302 PHE   A CB  
1958 C  CG  . PHE   A 282 ? 1.2462 0.9874 1.0653 0.1140  0.0283  0.0532  302 PHE   A CG  
1959 C  CD1 . PHE   A 282 ? 1.0737 0.8669 0.9290 0.1058  0.0415  0.0678  302 PHE   A CD1 
1960 C  CD2 . PHE   A 282 ? 1.4463 1.1486 1.2188 0.1426  0.0430  0.0470  302 PHE   A CD2 
1961 C  CE1 . PHE   A 282 ? 1.2429 1.0508 1.0950 0.1220  0.0681  0.0776  302 PHE   A CE1 
1962 C  CE2 . PHE   A 282 ? 1.4858 1.2060 1.2532 0.1612  0.0732  0.0580  302 PHE   A CE2 
1963 C  CZ  . PHE   A 282 ? 1.3557 1.1296 1.1662 0.1490  0.0855  0.0741  302 PHE   A CZ  
1964 N  N   . ILE   A 283 ? 1.2437 0.9822 1.1233 0.0360  -0.0595 0.0309  303 ILE   A N   
1965 C  CA  . ILE   A 283 ? 1.3082 1.0411 1.2163 0.0110  -0.0820 0.0283  303 ILE   A CA  
1966 C  C   . ILE   A 283 ? 1.2307 1.0242 1.1926 -0.0114 -0.0791 0.0435  303 ILE   A C   
1967 O  O   . ILE   A 283 ? 1.3004 1.1062 1.2948 -0.0264 -0.0755 0.0574  303 ILE   A O   
1968 C  CB  . ILE   A 283 ? 1.4333 1.1323 1.3167 0.0078  -0.1121 0.0056  303 ILE   A CB  
1969 C  CG1 . ILE   A 283 ? 1.4123 1.0460 1.2320 0.0341  -0.1150 -0.0114 303 ILE   A CG1 
1970 C  CG2 . ILE   A 283 ? 1.5516 1.2492 1.4753 -0.0219 -0.1356 0.0043  303 ILE   A CG2 
1971 C  CD1 . ILE   A 283 ? 1.4953 1.0915 1.2817 0.0347  -0.1480 -0.0363 303 ILE   A CD1 
1972 N  N   . PHE   A 284 ? 1.1446 0.9739 1.1126 -0.0120 -0.0804 0.0412  304 PHE   A N   
1973 C  CA  . PHE   A 284 ? 1.2440 1.1312 1.2566 -0.0274 -0.0752 0.0537  304 PHE   A CA  
1974 C  C   . PHE   A 284 ? 1.2913 1.2009 1.3223 -0.0266 -0.0534 0.0727  304 PHE   A C   
1975 O  O   . PHE   A 284 ? 1.4074 1.3436 1.4720 -0.0425 -0.0515 0.0851  304 PHE   A O   
1976 C  CB  . PHE   A 284 ? 1.3232 1.2363 1.3281 -0.0188 -0.0743 0.0488  304 PHE   A CB  
1977 C  CG  . PHE   A 284 ? 1.4222 1.3516 1.4422 -0.0297 -0.0967 0.0382  304 PHE   A CG  
1978 C  CD1 . PHE   A 284 ? 1.3574 1.3365 1.4238 -0.0460 -0.0975 0.0458  304 PHE   A CD1 
1979 C  CD2 . PHE   A 284 ? 1.4572 1.3545 1.4437 -0.0206 -0.1166 0.0204  304 PHE   A CD2 
1980 C  CE1 . PHE   A 284 ? 1.4577 1.4581 1.5445 -0.0541 -0.1173 0.0365  304 PHE   A CE1 
1981 C  CE2 . PHE   A 284 ? 1.4124 1.3286 1.4167 -0.0289 -0.1400 0.0103  304 PHE   A CE2 
1982 C  CZ  . PHE   A 284 ? 1.4596 1.4297 1.5178 -0.0460 -0.1400 0.0186  304 PHE   A CZ  
1983 N  N   . ALA   A 285 ? 1.2482 1.1489 1.2579 -0.0071 -0.0367 0.0758  305 ALA   A N   
1984 C  CA  . ALA   A 285 ? 1.1693 1.0911 1.1966 -0.0037 -0.0194 0.0922  305 ALA   A CA  
1985 C  C   . ALA   A 285 ? 1.1591 1.0633 1.1979 -0.0121 -0.0219 0.1014  305 ALA   A C   
1986 O  O   . ALA   A 285 ? 1.2147 1.1471 1.2810 -0.0254 -0.0202 0.1147  305 ALA   A O   
1987 C  CB  . ALA   A 285 ? 1.0818 0.9918 1.0880 0.0189  -0.0028 0.0929  305 ALA   A CB  
1988 N  N   . GLY   A 286 ? 1.1911 1.0450 1.2052 -0.0028 -0.0254 0.0949  306 GLY   A N   
1989 C  CA  . GLY   A 286 ? 1.2547 1.0817 1.2748 -0.0072 -0.0270 0.1042  306 GLY   A CA  
1990 C  C   . GLY   A 286 ? 1.4085 1.2265 1.4486 -0.0330 -0.0430 0.1061  306 GLY   A C   
1991 O  O   . GLY   A 286 ? 1.5083 1.2986 1.5532 -0.0386 -0.0443 0.1160  306 GLY   A O   
1992 N  N   . TYR   A 287 ? 1.3292 1.1697 1.3840 -0.0489 -0.0549 0.0982  307 TYR   A N   
1993 C  CA  . TYR   A 287 ? 1.3771 1.2135 1.4600 -0.0754 -0.0694 0.1013  307 TYR   A CA  
1994 C  C   . TYR   A 287 ? 1.3950 1.2813 1.5160 -0.0915 -0.0576 0.1233  307 TYR   A C   
1995 O  O   . TYR   A 287 ? 1.4078 1.2824 1.5384 -0.0987 -0.0511 0.1410  307 TYR   A O   
1996 C  CB  . TYR   A 287 ? 1.4568 1.2951 1.5439 -0.0855 -0.0907 0.0823  307 TYR   A CB  
1997 C  CG  . TYR   A 287 ? 1.5974 1.4341 1.7228 -0.1152 -0.1064 0.0859  307 TYR   A CG  
1998 C  CD1 . TYR   A 287 ? 1.6658 1.4457 1.7862 -0.1243 -0.1189 0.0839  307 TYR   A CD1 
1999 C  CD2 . TYR   A 287 ? 1.5287 1.4209 1.6983 -0.1342 -0.1077 0.0923  307 TYR   A CD2 
2000 C  CE1 . TYR   A 287 ? 1.6161 1.3940 1.7780 -0.1550 -0.1331 0.0891  307 TYR   A CE1 
2001 C  CE2 . TYR   A 287 ? 1.5225 1.4191 1.7356 -0.1632 -0.1196 0.0982  307 TYR   A CE2 
2002 C  CZ  . TYR   A 287 ? 1.6234 1.4626 1.8342 -0.1753 -0.1325 0.0972  307 TYR   A CZ  
2003 O  OH  . TYR   A 287 ? 1.7502 1.5932 2.0101 -0.2074 -0.1444 0.1046  307 TYR   A OH  
2004 N  N   . GLU   A 288 ? 1.4479 1.3867 1.5869 -0.0951 -0.0546 0.1225  308 GLU   A N   
2005 C  CA  . GLU   A 288 ? 1.4833 1.4703 1.6544 -0.1083 -0.0432 0.1413  308 GLU   A CA  
2006 C  C   . GLU   A 288 ? 1.4336 1.4384 1.5943 -0.0940 -0.0249 0.1563  308 GLU   A C   
2007 O  O   . GLU   A 288 ? 1.4336 1.4762 1.6113 -0.1004 -0.0145 0.1715  308 GLU   A O   
2008 C  CB  . GLU   A 288 ? 1.5031 1.5388 1.6954 -0.1136 -0.0469 0.1333  308 GLU   A CB  
2009 C  CG  . GLU   A 288 ? 1.6126 1.6921 1.8450 -0.1328 -0.0393 0.1497  308 GLU   A CG  
2010 C  CD  . GLU   A 288 ? 1.7657 1.9013 2.0085 -0.1257 -0.0311 0.1481  308 GLU   A CD  
2011 O  OE1 . GLU   A 288 ? 1.8530 2.0024 2.1013 -0.1229 -0.0430 0.1315  308 GLU   A OE1 
2012 O  OE2 . GLU   A 288 ? 1.7707 1.9335 2.0128 -0.1209 -0.0143 0.1628  308 GLU   A OE2 
2013 N  N   . THR   A 289 ? 1.3279 1.3084 1.4617 -0.0739 -0.0212 0.1523  309 THR   A N   
2014 C  CA  . THR   A 289 ? 1.3262 1.3218 1.4545 -0.0605 -0.0081 0.1660  309 THR   A CA  
2015 C  C   . THR   A 289 ? 1.2665 1.2267 1.3885 -0.0586 -0.0055 0.1812  309 THR   A C   
2016 O  O   . THR   A 289 ? 1.2145 1.1909 1.3426 -0.0606 0.0020  0.2004  309 THR   A O   
2017 C  CB  . THR   A 289 ? 1.1792 1.1777 1.2911 -0.0396 -0.0042 0.1550  309 THR   A CB  
2018 O  OG1 . THR   A 289 ? 1.2043 1.1563 1.2948 -0.0290 -0.0077 0.1443  309 THR   A OG1 
2019 C  CG2 . THR   A 289 ? 1.1529 1.1833 1.2691 -0.0408 -0.0063 0.1427  309 THR   A CG2 
2020 N  N   . THR   A 290 ? 1.2647 1.1735 1.3702 -0.0525 -0.0120 0.1727  310 THR   A N   
2021 C  CA  . THR   A 290 ? 1.2004 1.0667 1.2988 -0.0504 -0.0117 0.1859  310 THR   A CA  
2022 C  C   . THR   A 290 ? 1.2809 1.1465 1.3997 -0.0753 -0.0128 0.2039  310 THR   A C   
2023 O  O   . THR   A 290 ? 1.2929 1.1513 1.4110 -0.0744 -0.0058 0.2256  310 THR   A O   
2024 C  CB  . THR   A 290 ? 1.3087 1.1150 1.3840 -0.0410 -0.0211 0.1694  310 THR   A CB  
2025 O  OG1 . THR   A 290 ? 1.2600 1.0676 1.3156 -0.0147 -0.0142 0.1580  310 THR   A OG1 
2026 C  CG2 . THR   A 290 ? 1.3393 1.0935 1.4074 -0.0404 -0.0234 0.1820  310 THR   A CG2 
2027 N  N   . SER   A 291 ? 1.3226 1.1977 1.4614 -0.0975 -0.0212 0.1965  311 SER   A N   
2028 C  CA  . SER   A 291 ? 1.3201 1.1981 1.4864 -0.1242 -0.0203 0.2147  311 SER   A CA  
2029 C  C   . SER   A 291 ? 1.3027 1.2380 1.4833 -0.1278 -0.0035 0.2350  311 SER   A C   
2030 O  O   . SER   A 291 ? 1.3769 1.3085 1.5642 -0.1377 0.0061  0.2602  311 SER   A O   
2031 C  CB  . SER   A 291 ? 1.4141 1.2905 1.6047 -0.1465 -0.0362 0.1995  311 SER   A CB  
2032 O  OG  . SER   A 291 ? 1.4278 1.3570 1.6295 -0.1450 -0.0362 0.1871  311 SER   A OG  
2033 N  N   . SER   A 292 ? 1.2770 1.2617 1.4587 -0.1189 0.0003  0.2247  312 SER   A N   
2034 C  CA  . SER   A 292 ? 1.2699 1.3067 1.4600 -0.1197 0.0150  0.2404  312 SER   A CA  
2035 C  C   . SER   A 292 ? 1.3288 1.3606 1.4954 -0.1035 0.0247  0.2590  312 SER   A C   
2036 O  O   . SER   A 292 ? 1.3104 1.3582 1.4781 -0.1089 0.0368  0.2820  312 SER   A O   
2037 C  CB  . SER   A 292 ? 1.2437 1.3260 1.4355 -0.1105 0.0144  0.2226  312 SER   A CB  
2038 O  OG  . SER   A 292 ? 1.4405 1.5366 1.6570 -0.1250 0.0059  0.2092  312 SER   A OG  
2039 N  N   . VAL   A 293 ? 1.1383 1.1494 1.2833 -0.0823 0.0198  0.2502  313 VAL   A N   
2040 C  CA  . VAL   A 293 ? 1.2091 1.2183 1.3351 -0.0648 0.0249  0.2663  313 VAL   A CA  
2041 C  C   . VAL   A 293 ? 1.2916 1.2580 1.4119 -0.0710 0.0275  0.2895  313 VAL   A C   
2042 O  O   . VAL   A 293 ? 1.3863 1.3606 1.4958 -0.0676 0.0358  0.3127  313 VAL   A O   
2043 C  CB  . VAL   A 293 ? 1.0531 1.0551 1.1671 -0.0414 0.0193  0.2516  313 VAL   A CB  
2044 C  CG1 . VAL   A 293 ? 1.0644 1.0683 1.1643 -0.0226 0.0209  0.2676  313 VAL   A CG1 
2045 C  CG2 . VAL   A 293 ? 1.1436 1.1844 1.2638 -0.0375 0.0177  0.2317  313 VAL   A CG2 
2046 N  N   . LEU   A 294 ? 1.2525 1.1689 1.3763 -0.0792 0.0197  0.2836  314 LEU   A N   
2047 C  CA  . LEU   A 294 ? 1.2688 1.1357 1.3873 -0.0860 0.0205  0.3052  314 LEU   A CA  
2048 C  C   . LEU   A 294 ? 1.3459 1.2285 1.4814 -0.1108 0.0316  0.3300  314 LEU   A C   
2049 O  O   . LEU   A 294 ? 1.4007 1.2600 1.5253 -0.1114 0.0391  0.3575  314 LEU   A O   
2050 C  CB  . LEU   A 294 ? 1.2472 1.0544 1.3657 -0.0913 0.0074  0.2899  314 LEU   A CB  
2051 C  CG  . LEU   A 294 ? 1.2174 0.9912 1.3115 -0.0620 0.0015  0.2759  314 LEU   A CG  
2052 C  CD1 . LEU   A 294 ? 1.4012 1.1109 1.4885 -0.0659 -0.0116 0.2596  314 LEU   A CD1 
2053 C  CD2 . LEU   A 294 ? 1.2455 1.0064 1.3227 -0.0420 0.0071  0.2983  314 LEU   A CD2 
2054 N  N   . SER   A 295 ? 1.2631 1.1856 1.4257 -0.1300 0.0341  0.3224  315 SER   A N   
2055 C  CA  . SER   A 295 ? 1.2106 1.1618 1.3929 -0.1507 0.0497  0.3473  315 SER   A CA  
2056 C  C   . SER   A 295 ? 1.1948 1.1853 1.3533 -0.1332 0.0651  0.3645  315 SER   A C   
2057 O  O   . SER   A 295 ? 1.3086 1.2960 1.4596 -0.1385 0.0798  0.3953  315 SER   A O   
2058 C  CB  . SER   A 295 ? 1.3301 1.3217 1.5508 -0.1714 0.0482  0.3330  315 SER   A CB  
2059 O  OG  . SER   A 295 ? 1.5388 1.4920 1.7837 -0.1921 0.0324  0.3218  315 SER   A OG  
2060 N  N   . PHE   A 296 ? 1.1848 1.2094 1.3288 -0.1120 0.0611  0.3453  316 PHE   A N   
2061 C  CA  . PHE   A 296 ? 1.1607 1.2177 1.2775 -0.0928 0.0700  0.3567  316 PHE   A CA  
2062 C  C   . PHE   A 296 ? 1.2147 1.2351 1.3007 -0.0770 0.0695  0.3782  316 PHE   A C   
2063 O  O   . PHE   A 296 ? 1.1614 1.1966 1.2229 -0.0677 0.0797  0.3996  316 PHE   A O   
2064 C  CB  . PHE   A 296 ? 1.1454 1.2351 1.2553 -0.0743 0.0608  0.3293  316 PHE   A CB  
2065 C  CG  . PHE   A 296 ? 1.1563 1.2928 1.2854 -0.0826 0.0649  0.3144  316 PHE   A CG  
2066 C  CD1 . PHE   A 296 ? 1.1584 1.3295 1.2923 -0.0908 0.0816  0.3302  316 PHE   A CD1 
2067 C  CD2 . PHE   A 296 ? 1.0919 1.2372 1.2330 -0.0803 0.0534  0.2858  316 PHE   A CD2 
2068 C  CE1 . PHE   A 296 ? 1.2096 1.4248 1.3627 -0.0952 0.0856  0.3160  316 PHE   A CE1 
2069 C  CE2 . PHE   A 296 ? 1.1529 1.3381 1.3105 -0.0855 0.0557  0.2725  316 PHE   A CE2 
2070 C  CZ  . PHE   A 296 ? 1.1946 1.4157 1.3596 -0.0923 0.0712  0.2867  316 PHE   A CZ  
2071 N  N   . ILE   A 297 ? 1.1662 1.1377 1.2497 -0.0711 0.0575  0.3727  317 ILE   A N   
2072 C  CA  . ILE   A 297 ? 1.1700 1.1049 1.2259 -0.0530 0.0552  0.3925  317 ILE   A CA  
2073 C  C   . ILE   A 297 ? 1.2572 1.1563 1.3096 -0.0697 0.0667  0.4260  317 ILE   A C   
2074 O  O   . ILE   A 297 ? 1.3286 1.2207 1.3523 -0.0577 0.0735  0.4528  317 ILE   A O   
2075 C  CB  . ILE   A 297 ? 1.2271 1.1231 1.2821 -0.0375 0.0404  0.3748  317 ILE   A CB  
2076 C  CG1 . ILE   A 297 ? 1.2089 1.1437 1.2671 -0.0197 0.0325  0.3479  317 ILE   A CG1 
2077 C  CG2 . ILE   A 297 ? 1.2696 1.1232 1.3001 -0.0184 0.0374  0.3965  317 ILE   A CG2 
2078 C  CD1 . ILE   A 297 ? 1.1916 1.0970 1.2503 -0.0015 0.0226  0.3319  317 ILE   A CD1 
2079 N  N   . MET   A 298 ? 1.2447 1.1195 1.3260 -0.0978 0.0681  0.4259  318 MET   A N   
2080 C  CA  . MET   A 298 ? 1.3326 1.1703 1.4172 -0.1178 0.0792  0.4592  318 MET   A CA  
2081 C  C   . MET   A 298 ? 1.3523 1.2348 1.4340 -0.1264 0.1022  0.4863  318 MET   A C   
2082 O  O   . MET   A 298 ? 1.3100 1.1687 1.3716 -0.1273 0.1153  0.5218  318 MET   A O   
2083 C  CB  . MET   A 298 ? 1.3342 1.1388 1.4567 -0.1488 0.0723  0.4502  318 MET   A CB  
2084 C  CG  . MET   A 298 ? 1.3410 1.0927 1.4585 -0.1385 0.0508  0.4243  318 MET   A CG  
2085 S  SD  . MET   A 298 ? 1.5626 1.2793 1.6349 -0.0972 0.0444  0.4293  318 MET   A SD  
2086 C  CE  . MET   A 298 ? 1.5237 1.1719 1.5825 -0.1070 0.0511  0.4710  318 MET   A CE  
2087 N  N   . TYR   A 299 ? 1.3445 1.2897 1.4432 -0.1310 0.1087  0.4711  319 TYR   A N   
2088 C  CA  . TYR   A 299 ? 1.3049 1.2970 1.3938 -0.1317 0.1321  0.4938  319 TYR   A CA  
2089 C  C   . TYR   A 299 ? 1.3517 1.3428 1.3851 -0.1000 0.1342  0.5092  319 TYR   A C   
2090 O  O   . TYR   A 299 ? 1.3518 1.3394 1.3605 -0.0990 0.1530  0.5439  319 TYR   A O   
2091 C  CB  . TYR   A 299 ? 1.2395 1.2972 1.3509 -0.1341 0.1352  0.4692  319 TYR   A CB  
2092 C  CG  . TYR   A 299 ? 1.2873 1.3955 1.3780 -0.1247 0.1582  0.4865  319 TYR   A CG  
2093 C  CD1 . TYR   A 299 ? 1.2951 1.4266 1.3420 -0.0936 0.1537  0.4764  319 TYR   A CD1 
2094 C  CD2 . TYR   A 299 ? 1.3384 1.4709 1.4536 -0.1465 0.1844  0.5127  319 TYR   A CD2 
2095 C  CE1 . TYR   A 299 ? 1.3283 1.5009 1.3482 -0.0818 0.1734  0.4898  319 TYR   A CE1 
2096 C  CE2 . TYR   A 299 ? 1.3904 1.5687 1.4815 -0.1343 0.2085  0.5286  319 TYR   A CE2 
2097 C  CZ  . TYR   A 299 ? 1.4046 1.6003 1.4440 -0.1006 0.2023  0.5161  319 TYR   A CZ  
2098 O  OH  . TYR   A 299 ? 1.4155 1.6523 1.4233 -0.0853 0.2248  0.5293  319 TYR   A OH  
2099 N  N   . GLU   A 300 ? 1.2805 1.2748 1.2943 -0.0737 0.1145  0.4843  320 GLU   A N   
2100 C  CA  . GLU   A 300 ? 1.2621 1.2596 1.2272 -0.0427 0.1105  0.4947  320 GLU   A CA  
2101 C  C   . GLU   A 300 ? 1.3129 1.2516 1.2522 -0.0346 0.1088  0.5243  320 GLU   A C   
2102 O  O   . GLU   A 300 ? 1.3792 1.3150 1.2758 -0.0181 0.1158  0.5508  320 GLU   A O   
2103 C  CB  . GLU   A 300 ? 1.2928 1.3108 1.2549 -0.0202 0.0883  0.4604  320 GLU   A CB  
2104 C  CG  . GLU   A 300 ? 1.2256 1.3008 1.1987 -0.0211 0.0898  0.4353  320 GLU   A CG  
2105 C  CD  . GLU   A 300 ? 1.3459 1.4560 1.2875 -0.0136 0.1061  0.4516  320 GLU   A CD  
2106 O  OE1 . GLU   A 300 ? 1.3469 1.4444 1.2450 0.0053  0.1064  0.4731  320 GLU   A OE1 
2107 O  OE2 . GLU   A 300 ? 1.3810 1.5305 1.3387 -0.0243 0.1185  0.4429  320 GLU   A OE2 
2108 N  N   . LEU   A 301 ? 1.3947 1.2825 1.3550 -0.0437 0.0986  0.5200  321 LEU   A N   
2109 C  CA  . LEU   A 301 ? 1.4476 1.2726 1.3847 -0.0361 0.0968  0.5485  321 LEU   A CA  
2110 C  C   . LEU   A 301 ? 1.5456 1.3520 1.4773 -0.0580 0.1208  0.5895  321 LEU   A C   
2111 O  O   . LEU   A 301 ? 1.6494 1.4239 1.5420 -0.0444 0.1264  0.6227  321 LEU   A O   
2112 C  CB  . LEU   A 301 ? 1.4062 1.1776 1.3660 -0.0405 0.0810  0.5318  321 LEU   A CB  
2113 C  CG  . LEU   A 301 ? 1.3246 1.1041 1.2880 -0.0160 0.0604  0.4970  321 LEU   A CG  
2114 C  CD1 . LEU   A 301 ? 1.2627 0.9803 1.2394 -0.0177 0.0490  0.4859  321 LEU   A CD1 
2115 C  CD2 . LEU   A 301 ? 1.3672 1.1608 1.2966 0.0201  0.0510  0.5032  321 LEU   A CD2 
2116 N  N   . ALA   A 302 ? 1.5781 1.4050 1.5503 -0.0916 0.1355  0.5893  322 ALA   A N   
2117 C  CA  . ALA   A 302 ? 1.6278 1.4429 1.6052 -0.1163 0.1614  0.6301  322 ALA   A CA  
2118 C  C   . ALA   A 302 ? 1.6033 1.4602 1.5388 -0.1003 0.1834  0.6554  322 ALA   A C   
2119 O  O   . ALA   A 302 ? 1.6979 1.5265 1.6037 -0.1001 0.2012  0.6974  322 ALA   A O   
2120 C  CB  . ALA   A 302 ? 1.7107 1.5473 1.7506 -0.1559 0.1698  0.6213  322 ALA   A CB  
2121 N  N   . THR   A 303 ? 1.5193 1.4397 1.4479 -0.0854 0.1825  0.6307  323 THR   A N   
2122 C  CA  . THR   A 303 ? 1.4462 1.4048 1.3270 -0.0650 0.2002  0.6487  323 THR   A CA  
2123 C  C   . THR   A 303 ? 1.5951 1.5316 1.4125 -0.0261 0.1835  0.6543  323 THR   A C   
2124 O  O   . THR   A 303 ? 1.5951 1.5591 1.3631 -0.0038 0.1922  0.6650  323 THR   A O   
2125 C  CB  . THR   A 303 ? 1.4760 1.5055 1.3708 -0.0616 0.2028  0.6175  323 THR   A CB  
2126 O  OG1 . THR   A 303 ? 1.3405 1.3774 1.2375 -0.0439 0.1722  0.5761  323 THR   A OG1 
2127 C  CG2 . THR   A 303 ? 1.5279 1.5845 1.4878 -0.0977 0.2179  0.6126  323 THR   A CG2 
2128 N  N   . HIS   A 304 ? 1.5896 1.4786 1.4070 -0.0157 0.1587  0.6458  324 HIS   A N   
2129 C  CA  . HIS   A 304 ? 1.6104 1.4763 1.3752 0.0212  0.1401  0.6530  324 HIS   A CA  
2130 C  C   . HIS   A 304 ? 1.5811 1.3741 1.3494 0.0203  0.1304  0.6697  324 HIS   A C   
2131 O  O   . HIS   A 304 ? 1.5780 1.3524 1.3631 0.0318  0.1063  0.6448  324 HIS   A O   
2132 C  CB  . HIS   A 304 ? 1.5601 1.4633 1.3262 0.0452  0.1125  0.6112  324 HIS   A CB  
2133 C  CG  . HIS   A 304 ? 1.5192 1.4865 1.2769 0.0493  0.1184  0.5927  324 HIS   A CG  
2134 N  ND1 . HIS   A 304 ? 1.4779 1.4829 1.2787 0.0251  0.1298  0.5721  324 HIS   A ND1 
2135 C  CD2 . HIS   A 304 ? 1.5245 1.5220 1.2336 0.0767  0.1123  0.5904  324 HIS   A CD2 
2136 C  CE1 . HIS   A 304 ? 1.4515 1.5058 1.2307 0.0381  0.1322  0.5584  324 HIS   A CE1 
2137 N  NE2 . HIS   A 304 ? 1.5545 1.6040 1.2770 0.0689  0.1214  0.5682  324 HIS   A NE2 
2138 N  N   . PRO   A 305 ? 1.7742 1.5226 1.5267 0.0074  0.1504  0.7130  325 PRO   A N   
2139 C  CA  . PRO   A 305 ? 1.8296 1.5002 1.5876 0.0037  0.1414  0.7287  325 PRO   A CA  
2140 C  C   . PRO   A 305 ? 1.8098 1.4502 1.5296 0.0447  0.1153  0.7270  325 PRO   A C   
2141 O  O   . PRO   A 305 ? 1.6683 1.2534 1.4012 0.0485  0.1003  0.7230  325 PRO   A O   
2142 C  CB  . PRO   A 305 ? 1.7066 1.3422 1.4483 -0.0167 0.1711  0.7806  325 PRO   A CB  
2143 C  CG  . PRO   A 305 ? 1.6804 1.3834 1.4303 -0.0335 0.1987  0.7851  325 PRO   A CG  
2144 C  CD  . PRO   A 305 ? 1.7915 1.5565 1.5204 -0.0041 0.1836  0.7505  325 PRO   A CD  
2145 N  N   . ASP   A 306 ? 1.8404 1.5153 1.5135 0.0770  0.1079  0.7290  326 ASP   A N   
2146 C  CA  . ASP   A 306 ? 1.8000 1.4569 1.4437 0.1175  0.0793  0.7243  326 ASP   A CA  
2147 C  C   . ASP   A 306 ? 1.7189 1.3919 1.4090 0.1240  0.0550  0.6791  326 ASP   A C   
2148 O  O   . ASP   A 306 ? 1.7018 1.3324 1.3973 0.1414  0.0379  0.6765  326 ASP   A O   
2149 C  CB  . ASP   A 306 ? 1.8508 1.5497 1.4396 0.1480  0.0728  0.7296  326 ASP   A CB  
2150 C  CG  . ASP   A 306 ? 1.9168 1.6850 1.5138 0.1345  0.0856  0.7092  326 ASP   A CG  
2151 O  OD1 . ASP   A 306 ? 1.9619 1.7376 1.5806 0.1018  0.1142  0.7192  326 ASP   A OD1 
2152 O  OD2 . ASP   A 306 ? 1.9563 1.7712 1.5412 0.1566  0.0661  0.6826  326 ASP   A OD2 
2153 N  N   . VAL   A 307 ? 1.7337 1.4667 1.4564 0.1117  0.0547  0.6440  327 VAL   A N   
2154 C  CA  . VAL   A 307 ? 1.5027 1.2531 1.2691 0.1157  0.0360  0.6029  327 VAL   A CA  
2155 C  C   . VAL   A 307 ? 1.5795 1.2764 1.3803 0.0966  0.0389  0.5987  327 VAL   A C   
2156 O  O   . VAL   A 307 ? 1.5721 1.2505 1.3908 0.1124  0.0226  0.5794  327 VAL   A O   
2157 C  CB  . VAL   A 307 ? 1.4680 1.2868 1.2597 0.1028  0.0384  0.5705  327 VAL   A CB  
2158 C  CG1 . VAL   A 307 ? 1.5251 1.3642 1.3562 0.1107  0.0198  0.5314  327 VAL   A CG1 
2159 C  CG2 . VAL   A 307 ? 1.3766 1.2402 1.1276 0.1201  0.0367  0.5757  327 VAL   A CG2 
2160 N  N   . GLN   A 308 ? 1.5823 1.2537 1.3934 0.0631  0.0592  0.6164  328 GLN   A N   
2161 C  CA  . GLN   A 308 ? 1.6372 1.2513 1.4780 0.0430  0.0588  0.6120  328 GLN   A CA  
2162 C  C   . GLN   A 308 ? 1.6686 1.2095 1.4852 0.0655  0.0481  0.6320  328 GLN   A C   
2163 O  O   . GLN   A 308 ? 1.6578 1.1584 1.4923 0.0709  0.0358  0.6134  328 GLN   A O   
2164 C  CB  . GLN   A 308 ? 1.5149 1.1193 1.3750 0.0010  0.0811  0.6305  328 GLN   A CB  
2165 C  CG  . GLN   A 308 ? 1.5280 1.0785 1.4244 -0.0253 0.0772  0.6200  328 GLN   A CG  
2166 C  CD  . GLN   A 308 ? 1.6327 1.1885 1.5606 -0.0696 0.0967  0.6344  328 GLN   A CD  
2167 O  OE1 . GLN   A 308 ? 1.7179 1.2233 1.6735 -0.0956 0.0937  0.6339  328 GLN   A OE1 
2168 N  NE2 . GLN   A 308 ? 1.5126 1.1304 1.4383 -0.0777 0.1158  0.6462  328 GLN   A NE2 
2169 N  N   . GLN   A 309 ? 1.7452 1.2664 1.5171 0.0819  0.0523  0.6696  329 GLN   A N   
2170 C  CA  . GLN   A 309 ? 1.7147 1.1647 1.4600 0.1071  0.0409  0.6908  329 GLN   A CA  
2171 C  C   . GLN   A 309 ? 1.7620 1.2288 1.5075 0.1486  0.0157  0.6655  329 GLN   A C   
2172 O  O   . GLN   A 309 ? 1.7109 1.1289 1.4662 0.1635  0.0039  0.6564  329 GLN   A O   
2173 C  CB  . GLN   A 309 ? 1.9115 1.3368 1.6042 0.1156  0.0521  0.7397  329 GLN   A CB  
2174 C  CG  . GLN   A 309 ? 1.9355 1.2919 1.5936 0.1494  0.0371  0.7627  329 GLN   A CG  
2175 C  CD  . GLN   A 309 ? 1.9791 1.2887 1.5866 0.1489  0.0527  0.8170  329 GLN   A CD  
2176 O  OE1 . GLN   A 309 ? 1.9958 1.3074 1.6044 0.1146  0.0790  0.8401  329 GLN   A OE1 
2177 N  NE2 . GLN   A 309 ? 2.0490 1.3172 1.6126 0.1880  0.0374  0.8391  329 GLN   A NE2 
2178 N  N   . LYS   A 310 ? 1.8175 1.3535 1.5543 0.1682  0.0071  0.6534  330 LYS   A N   
2179 C  CA  . LYS   A 310 ? 1.7804 1.3421 1.5276 0.2050  -0.0169 0.6297  330 LYS   A CA  
2180 C  C   . LYS   A 310 ? 1.7518 1.3203 1.5484 0.1984  -0.0206 0.5908  330 LYS   A C   
2181 O  O   . LYS   A 310 ? 1.7689 1.3264 1.5781 0.2272  -0.0352 0.5779  330 LYS   A O   
2182 C  CB  . LYS   A 310 ? 1.7312 1.3684 1.4669 0.2201  -0.0268 0.6201  330 LYS   A CB  
2183 C  CG  . LYS   A 310 ? 1.7786 1.4459 1.5280 0.2582  -0.0537 0.6011  330 LYS   A CG  
2184 C  CD  . LYS   A 310 ? 1.7957 1.5282 1.5285 0.2731  -0.0681 0.5948  330 LYS   A CD  
2185 C  CE  . LYS   A 310 ? 1.7460 1.5086 1.4992 0.3099  -0.0973 0.5789  330 LYS   A CE  
2186 N  NZ  . LYS   A 310 ? 1.7151 1.5394 1.4549 0.3230  -0.1165 0.5694  330 LYS   A NZ  
2187 N  N   . LEU   A 311 ? 1.5921 1.1793 1.4159 0.1631  -0.0071 0.5726  331 LEU   A N   
2188 C  CA  . LEU   A 311 ? 1.6809 1.2653 1.5432 0.1563  -0.0094 0.5381  331 LEU   A CA  
2189 C  C   . LEU   A 311 ? 1.7715 1.2710 1.6315 0.1550  -0.0095 0.5447  331 LEU   A C   
2190 O  O   . LEU   A 311 ? 1.7797 1.2588 1.6524 0.1760  -0.0185 0.5245  331 LEU   A O   
2191 C  CB  . LEU   A 311 ? 1.4993 1.1245 1.3870 0.1206  0.0025  0.5182  331 LEU   A CB  
2192 C  CG  . LEU   A 311 ? 1.5759 1.2053 1.4981 0.1119  0.0008  0.4814  331 LEU   A CG  
2193 C  CD1 . LEU   A 311 ? 1.5568 1.2035 1.4905 0.1466  -0.0117 0.4609  331 LEU   A CD1 
2194 C  CD2 . LEU   A 311 ? 1.4685 1.1562 1.4113 0.0855  0.0087  0.4631  331 LEU   A CD2 
2195 N  N   . GLN   A 312 ? 1.7610 1.2087 1.6050 0.1308  0.0011  0.5732  332 GLN   A N   
2196 C  CA  . GLN   A 312 ? 1.7653 1.1232 1.6044 0.1283  -0.0015 0.5814  332 GLN   A CA  
2197 C  C   . GLN   A 312 ? 1.8154 1.1311 1.6298 0.1724  -0.0152 0.5936  332 GLN   A C   
2198 O  O   . GLN   A 312 ? 1.8638 1.1170 1.6796 0.1850  -0.0226 0.5839  332 GLN   A O   
2199 C  CB  . GLN   A 312 ? 1.7785 1.0922 1.6085 0.0923  0.0128  0.6151  332 GLN   A CB  
2200 C  CG  . GLN   A 312 ? 1.8116 1.1472 1.6764 0.0468  0.0236  0.6004  332 GLN   A CG  
2201 C  CD  . GLN   A 312 ? 1.9341 1.2350 1.7982 0.0103  0.0399  0.6372  332 GLN   A CD  
2202 O  OE1 . GLN   A 312 ? 1.9221 1.1948 1.7538 0.0186  0.0472  0.6768  332 GLN   A OE1 
2203 N  NE2 . GLN   A 312 ? 1.8683 1.1720 1.7697 -0.0304 0.0455  0.6255  332 GLN   A NE2 
2204 N  N   . GLU   A 313 ? 1.7886 1.1364 1.5784 0.1984  -0.0201 0.6139  333 GLU   A N   
2205 C  CA  . GLU   A 313 ? 1.8486 1.1660 1.6187 0.2442  -0.0360 0.6243  333 GLU   A CA  
2206 C  C   . GLU   A 313 ? 1.8130 1.1629 1.6148 0.2728  -0.0478 0.5870  333 GLU   A C   
2207 O  O   . GLU   A 313 ? 1.8265 1.1266 1.6274 0.3010  -0.0560 0.5830  333 GLU   A O   
2208 C  CB  . GLU   A 313 ? 1.9729 1.3240 1.7091 0.2656  -0.0420 0.6520  333 GLU   A CB  
2209 C  CG  . GLU   A 313 ? 1.9407 1.2463 1.6349 0.2481  -0.0289 0.6970  333 GLU   A CG  
2210 C  CD  . GLU   A 313 ? 1.9697 1.3180 1.6244 0.2681  -0.0335 0.7201  333 GLU   A CD  
2211 O  OE1 . GLU   A 313 ? 2.1416 1.5520 1.8047 0.2954  -0.0510 0.6997  333 GLU   A OE1 
2212 O  OE2 . GLU   A 313 ? 2.0046 1.3236 1.6194 0.2565  -0.0197 0.7589  333 GLU   A OE2 
2213 N  N   . GLU   A 314 ? 1.9004 1.3333 1.7308 0.2667  -0.0472 0.5603  334 GLU   A N   
2214 C  CA  . GLU   A 314 ? 1.8634 1.3340 1.7281 0.2911  -0.0544 0.5274  334 GLU   A CA  
2215 C  C   . GLU   A 314 ? 1.9129 1.3354 1.7919 0.2830  -0.0476 0.5038  334 GLU   A C   
2216 O  O   . GLU   A 314 ? 1.9602 1.3688 1.8507 0.3146  -0.0525 0.4885  334 GLU   A O   
2217 C  CB  . GLU   A 314 ? 1.9253 1.4890 1.8168 0.2804  -0.0540 0.5063  334 GLU   A CB  
2218 C  CG  . GLU   A 314 ? 1.9547 1.5599 1.8876 0.2941  -0.0550 0.4718  334 GLU   A CG  
2219 C  CD  . GLU   A 314 ? 1.7660 1.4609 1.7248 0.2914  -0.0597 0.4571  334 GLU   A CD  
2220 O  OE1 . GLU   A 314 ? 1.7905 1.5215 1.7501 0.3158  -0.0752 0.4664  334 GLU   A OE1 
2221 O  OE2 . GLU   A 314 ? 1.6569 1.3839 1.6345 0.2652  -0.0500 0.4361  334 GLU   A OE2 
2222 N  N   . ILE   A 315 ? 1.8750 1.2722 1.7533 0.2424  -0.0370 0.5000  335 ILE   A N   
2223 C  CA  . ILE   A 315 ? 1.9381 1.2857 1.8248 0.2333  -0.0341 0.4757  335 ILE   A CA  
2224 C  C   . ILE   A 315 ? 2.0038 1.2563 1.8666 0.2541  -0.0407 0.4879  335 ILE   A C   
2225 O  O   . ILE   A 315 ? 2.0288 1.2465 1.8940 0.2757  -0.0436 0.4651  335 ILE   A O   
2226 C  CB  . ILE   A 315 ? 1.8858 1.2310 1.7802 0.1840  -0.0253 0.4703  335 ILE   A CB  
2227 C  CG1 . ILE   A 315 ? 1.7554 1.1922 1.6729 0.1683  -0.0194 0.4544  335 ILE   A CG1 
2228 C  CG2 . ILE   A 315 ? 1.8852 1.1718 1.7828 0.1749  -0.0273 0.4448  335 ILE   A CG2 
2229 C  CD1 . ILE   A 315 ? 1.7083 1.1547 1.6348 0.1225  -0.0107 0.4551  335 ILE   A CD1 
2230 N  N   . ASP   A 316 ? 1.9663 1.1726 1.8026 0.2500  -0.0424 0.5246  336 ASP   A N   
2231 C  CA  . ASP   A 316 ? 2.0039 1.1127 1.8152 0.2699  -0.0497 0.5390  336 ASP   A CA  
2232 C  C   . ASP   A 316 ? 2.0692 1.1826 1.8771 0.3262  -0.0600 0.5361  336 ASP   A C   
2233 O  O   . ASP   A 316 ? 2.0795 1.1262 1.8780 0.3522  -0.0656 0.5269  336 ASP   A O   
2234 C  CB  . ASP   A 316 ? 2.0784 1.1381 1.8616 0.2508  -0.0468 0.5834  336 ASP   A CB  
2235 C  CG  . ASP   A 316 ? 2.0280 1.0756 1.8213 0.1950  -0.0354 0.5885  336 ASP   A CG  
2236 O  OD1 . ASP   A 316 ? 1.9121 0.9706 1.7302 0.1732  -0.0342 0.5559  336 ASP   A OD1 
2237 O  OD2 . ASP   A 316 ? 1.9629 0.9920 1.7400 0.1739  -0.0273 0.6260  336 ASP   A OD2 
2238 N  N   . ALA   A 317 ? 2.0401 1.2320 1.8570 0.3466  -0.0640 0.5428  337 ALA   A N   
2239 C  CA  . ALA   A 317 ? 1.8510 1.0557 1.6719 0.3999  -0.0759 0.5429  337 ALA   A CA  
2240 C  C   . ALA   A 317 ? 1.9940 1.2230 1.8468 0.4222  -0.0729 0.5047  337 ALA   A C   
2241 O  O   . ALA   A 317 ? 2.0725 1.2615 1.9228 0.4624  -0.0778 0.4999  337 ALA   A O   
2242 C  CB  . ALA   A 317 ? 1.8114 1.0977 1.6374 0.4127  -0.0845 0.5573  337 ALA   A CB  
2243 N  N   . VAL   A 318 ? 1.9517 1.2457 1.8332 0.3986  -0.0634 0.4784  338 VAL   A N   
2244 C  CA  . VAL   A 318 ? 1.9122 1.2333 1.8217 0.4188  -0.0569 0.4445  338 VAL   A CA  
2245 C  C   . VAL   A 318 ? 2.0357 1.2736 1.9261 0.4126  -0.0510 0.4256  338 VAL   A C   
2246 O  O   . VAL   A 318 ? 2.0778 1.2990 1.9727 0.4461  -0.0474 0.4051  338 VAL   A O   
2247 C  CB  . VAL   A 318 ? 1.9265 1.3428 1.8702 0.3967  -0.0492 0.4253  338 VAL   A CB  
2248 C  CG1 . VAL   A 318 ? 1.9120 1.3538 1.8819 0.4150  -0.0384 0.3932  338 VAL   A CG1 
2249 C  CG2 . VAL   A 318 ? 1.7971 1.2911 1.7591 0.4069  -0.0593 0.4404  338 VAL   A CG2 
2250 N  N   . LEU   A 319 ? 2.0042 1.1886 1.8735 0.3712  -0.0504 0.4318  339 LEU   A N   
2251 C  CA  . LEU   A 319 ? 2.1523 1.2513 2.0020 0.3604  -0.0502 0.4136  339 LEU   A CA  
2252 C  C   . LEU   A 319 ? 2.2520 1.2545 2.0705 0.3519  -0.0591 0.4417  339 LEU   A C   
2253 O  O   . LEU   A 319 ? 2.2702 1.2460 2.0833 0.3070  -0.0588 0.4540  339 LEU   A O   
2254 C  CB  . LEU   A 319 ? 2.1756 1.2975 2.0358 0.3152  -0.0440 0.3926  339 LEU   A CB  
2255 C  CG  . LEU   A 319 ? 2.0644 1.2808 1.9539 0.3173  -0.0343 0.3687  339 LEU   A CG  
2256 C  CD1 . LEU   A 319 ? 2.0487 1.2795 1.9442 0.2719  -0.0308 0.3527  339 LEU   A CD1 
2257 C  CD2 . LEU   A 319 ? 2.0324 1.2464 1.9240 0.3603  -0.0288 0.3429  339 LEU   A CD2 
2258 N  N   . PRO   A 320 ? 2.3403 1.2889 2.1404 0.3941  -0.0666 0.4536  340 PRO   A N   
2259 C  CA  . PRO   A 320 ? 2.4062 1.2579 2.1748 0.3874  -0.0751 0.4841  340 PRO   A CA  
2260 C  C   . PRO   A 320 ? 2.5657 1.3222 2.3183 0.3599  -0.0790 0.4685  340 PRO   A C   
2261 O  O   . PRO   A 320 ? 2.5921 1.3315 2.3444 0.3696  -0.0792 0.4316  340 PRO   A O   
2262 C  CB  . PRO   A 320 ? 2.3148 1.1363 2.0699 0.4473  -0.0831 0.4933  340 PRO   A CB  
2263 C  CG  . PRO   A 320 ? 2.3396 1.2134 2.1176 0.4825  -0.0774 0.4567  340 PRO   A CG  
2264 C  CD  . PRO   A 320 ? 2.2686 1.2442 2.0788 0.4508  -0.0670 0.4414  340 PRO   A CD  
2265 N  N   . ASN   A 321 ? 2.6781 1.3721 2.4167 0.3249  -0.0823 0.4980  341 ASN   A N   
2266 C  CA  . ASN   A 321 ? 2.7716 1.3709 2.5002 0.2913  -0.0897 0.4884  341 ASN   A CA  
2267 C  C   . ASN   A 321 ? 2.6686 1.3115 2.4215 0.2516  -0.0865 0.4562  341 ASN   A C   
2268 O  O   . ASN   A 321 ? 2.6748 1.2555 2.4203 0.2415  -0.0961 0.4272  341 ASN   A O   
2269 C  CB  . ASN   A 321 ? 2.8412 1.3394 2.5413 0.3308  -0.1020 0.4690  341 ASN   A CB  
2270 C  CG  . ASN   A 321 ? 2.8400 1.2912 2.5157 0.3747  -0.1069 0.4998  341 ASN   A CG  
2271 O  OD1 . ASN   A 321 ? 2.8158 1.2763 2.4874 0.4282  -0.1087 0.4846  341 ASN   A OD1 
2272 N  ND2 . ASN   A 321 ? 2.9698 1.3901 2.6406 0.3491  -0.1077 0.5414  341 ASN   A ND2 
2273 N  N   . LYS   A 322 ? 2.6554 1.4026 2.4346 0.2304  -0.0749 0.4607  342 LYS   A N   
2274 C  CA  . LYS   A 322 ? 2.5682 1.3695 2.3716 0.1976  -0.0714 0.4313  342 LYS   A CA  
2275 C  C   . LYS   A 322 ? 2.5231 1.3244 2.3201 0.2286  -0.0743 0.3867  342 LYS   A C   
2276 O  O   . LYS   A 322 ? 2.5415 1.3118 2.3366 0.2095  -0.0813 0.3574  342 LYS   A O   
2277 C  CB  . LYS   A 322 ? 2.6020 1.3515 2.4145 0.1431  -0.0775 0.4349  342 LYS   A CB  
2278 C  CG  . LYS   A 322 ? 2.6027 1.3344 2.4195 0.1114  -0.0719 0.4819  342 LYS   A CG  
2279 C  CD  . LYS   A 322 ? 2.6230 1.2912 2.4549 0.0602  -0.0804 0.4812  342 LYS   A CD  
2280 C  CE  . LYS   A 322 ? 2.6315 1.3009 2.4782 0.0200  -0.0688 0.5283  342 LYS   A CE  
2281 N  NZ  . LYS   A 322 ? 2.6478 1.2783 2.5248 -0.0353 -0.0761 0.5248  342 LYS   A NZ  
2282 N  N   . ALA   A 323 ? 2.4678 1.3041 2.2613 0.2783  -0.0689 0.3825  343 ALA   A N   
2283 C  CA  . ALA   A 323 ? 2.4277 1.2642 2.2135 0.3137  -0.0669 0.3445  343 ALA   A CA  
2284 C  C   . ALA   A 323 ? 2.3709 1.2764 2.1753 0.2896  -0.0599 0.3172  343 ALA   A C   
2285 O  O   . ALA   A 323 ? 2.2562 1.2384 2.0866 0.2603  -0.0535 0.3289  343 ALA   A O   
2286 C  CB  . ALA   A 323 ? 2.4004 1.2813 2.1918 0.3682  -0.0596 0.3494  343 ALA   A CB  
2287 N  N   . PRO   A 324 ? 2.3618 1.2380 2.1491 0.3031  -0.0611 0.2806  344 PRO   A N   
2288 C  CA  . PRO   A 324 ? 2.2581 1.1948 2.0575 0.2840  -0.0549 0.2551  344 PRO   A CA  
2289 C  C   . PRO   A 324 ? 2.2941 1.3395 2.1220 0.3019  -0.0376 0.2589  344 PRO   A C   
2290 O  O   . PRO   A 324 ? 2.2542 1.3169 2.0826 0.3472  -0.0285 0.2558  344 PRO   A O   
2291 C  CB  . PRO   A 324 ? 2.2587 1.1299 2.0223 0.3091  -0.0593 0.2173  344 PRO   A CB  
2292 C  CG  . PRO   A 324 ? 2.3747 1.1357 2.1090 0.3236  -0.0737 0.2225  344 PRO   A CG  
2293 C  CD  . PRO   A 324 ? 2.4492 1.2288 2.1994 0.3379  -0.0691 0.2606  344 PRO   A CD  
2294 N  N   . PRO   A 325 ? 2.2510 1.3717 2.1061 0.2676  -0.0332 0.2656  345 PRO   A N   
2295 C  CA  . PRO   A 325 ? 2.1248 1.3457 2.0086 0.2813  -0.0192 0.2671  345 PRO   A CA  
2296 C  C   . PRO   A 325 ? 1.9747 1.2147 1.8536 0.3081  -0.0076 0.2369  345 PRO   A C   
2297 O  O   . PRO   A 325 ? 1.9617 1.1654 1.8183 0.2987  -0.0102 0.2118  345 PRO   A O   
2298 C  CB  . PRO   A 325 ? 1.9598 1.2380 1.8653 0.2354  -0.0193 0.2751  345 PRO   A CB  
2299 C  CG  . PRO   A 325 ? 2.0299 1.2457 1.9203 0.2005  -0.0306 0.2659  345 PRO   A CG  
2300 C  CD  . PRO   A 325 ? 2.2761 1.3947 2.1402 0.2151  -0.0409 0.2722  345 PRO   A CD  
2301 N  N   . THR   A 326 ? 1.9594 1.2568 1.8595 0.3424  0.0049  0.2403  346 THR   A N   
2302 C  CA  . THR   A 326 ? 1.9218 1.2536 1.8253 0.3684  0.0217  0.2177  346 THR   A CA  
2303 C  C   . THR   A 326 ? 1.9043 1.3384 1.8485 0.3540  0.0319  0.2225  346 THR   A C   
2304 O  O   . THR   A 326 ? 1.8416 1.3186 1.8092 0.3310  0.0248  0.2420  346 THR   A O   
2305 C  CB  . THR   A 326 ? 1.9118 1.2291 1.8139 0.4226  0.0306  0.2171  346 THR   A CB  
2306 O  OG1 . THR   A 326 ? 1.9773 1.3670 1.9226 0.4368  0.0333  0.2392  346 THR   A OG1 
2307 C  CG2 . THR   A 326 ? 2.0931 1.3074 1.9582 0.4370  0.0167  0.2193  346 THR   A CG2 
2308 N  N   . TYR   A 327 ? 1.9067 1.3758 1.8559 0.3684  0.0490  0.2043  347 TYR   A N   
2309 C  CA  . TYR   A 327 ? 1.7526 1.3151 1.7427 0.3583  0.0598  0.2080  347 TYR   A CA  
2310 C  C   . TYR   A 327 ? 1.7524 1.3728 1.7856 0.3726  0.0575  0.2302  347 TYR   A C   
2311 O  O   . TYR   A 327 ? 1.7498 1.4211 1.8079 0.3477  0.0493  0.2432  347 TYR   A O   
2312 C  CB  . TYR   A 327 ? 1.7965 1.3797 1.7845 0.3803  0.0824  0.1890  347 TYR   A CB  
2313 C  CG  . TYR   A 327 ? 1.7394 1.4152 1.7732 0.3724  0.0958  0.1936  347 TYR   A CG  
2314 C  CD1 . TYR   A 327 ? 1.6767 1.4154 1.7595 0.3955  0.1041  0.2068  347 TYR   A CD1 
2315 C  CD2 . TYR   A 327 ? 1.6432 1.3419 1.6731 0.3423  0.0986  0.1844  347 TYR   A CD2 
2316 C  CE1 . TYR   A 327 ? 1.5545 1.3744 1.6831 0.3855  0.1143  0.2106  347 TYR   A CE1 
2317 C  CE2 . TYR   A 327 ? 1.5848 1.3609 1.6557 0.3342  0.1101  0.1888  347 TYR   A CE2 
2318 C  CZ  . TYR   A 327 ? 1.5099 1.3454 1.6309 0.3545  0.1178  0.2018  347 TYR   A CZ  
2319 O  OH  . TYR   A 327 ? 1.4609 1.3709 1.6269 0.3437  0.1272  0.2060  347 TYR   A OH  
2320 N  N   . ASP   A 328 ? 1.7721 1.3840 1.8128 0.4150  0.0631  0.2337  348 ASP   A N   
2321 C  CA  . ASP   A 328 ? 1.8330 1.5058 1.9192 0.4342  0.0596  0.2524  348 ASP   A CA  
2322 C  C   . ASP   A 328 ? 1.8910 1.5493 1.9717 0.4190  0.0369  0.2748  348 ASP   A C   
2323 O  O   . ASP   A 328 ? 1.8519 1.5730 1.9667 0.4152  0.0283  0.2891  348 ASP   A O   
2324 C  CB  . ASP   A 328 ? 1.8007 1.4634 1.8954 0.4862  0.0707  0.2504  348 ASP   A CB  
2325 C  CG  . ASP   A 328 ? 1.8385 1.5181 1.9360 0.5050  0.0977  0.2306  348 ASP   A CG  
2326 O  OD1 . ASP   A 328 ? 1.7762 1.5362 1.9188 0.5001  0.1110  0.2312  348 ASP   A OD1 
2327 O  OD2 . ASP   A 328 ? 1.9176 1.5272 1.9697 0.5242  0.1056  0.2146  348 ASP   A OD2 
2328 N  N   . THR   A 329 ? 1.9488 1.5238 1.9862 0.4102  0.0266  0.2785  349 THR   A N   
2329 C  CA  . THR   A 329 ? 1.9108 1.4682 1.9386 0.3944  0.0087  0.3031  349 THR   A CA  
2330 C  C   . THR   A 329 ? 1.7852 1.3866 1.8207 0.3501  0.0044  0.3084  349 THR   A C   
2331 O  O   . THR   A 329 ? 1.7566 1.3828 1.7976 0.3424  -0.0067 0.3293  349 THR   A O   
2332 C  CB  . THR   A 329 ? 2.0011 1.4552 1.9840 0.3926  0.0008  0.3071  349 THR   A CB  
2333 O  OG1 . THR   A 329 ? 2.0677 1.4781 2.0266 0.3749  0.0066  0.2832  349 THR   A OG1 
2334 C  CG2 . THR   A 329 ? 2.0823 1.4923 2.0568 0.4410  -0.0011 0.3118  349 THR   A CG2 
2335 N  N   . VAL   A 330 ? 1.6913 1.3011 1.7238 0.3234  0.0127  0.2896  350 VAL   A N   
2336 C  CA  . VAL   A 330 ? 1.5977 1.2505 1.6385 0.2841  0.0097  0.2926  350 VAL   A CA  
2337 C  C   . VAL   A 330 ? 1.5809 1.3199 1.6598 0.2893  0.0085  0.2986  350 VAL   A C   
2338 O  O   . VAL   A 330 ? 1.5764 1.3441 1.6581 0.2724  -0.0012 0.3131  350 VAL   A O   
2339 C  CB  . VAL   A 330 ? 1.6101 1.2564 1.6419 0.2601  0.0178  0.2696  350 VAL   A CB  
2340 C  CG1 . VAL   A 330 ? 1.5081 1.2144 1.5572 0.2276  0.0171  0.2699  350 VAL   A CG1 
2341 C  CG2 . VAL   A 330 ? 1.6864 1.2501 1.6829 0.2446  0.0117  0.2654  350 VAL   A CG2 
2342 N  N   . LEU   A 331 ? 1.4672 1.2483 1.5762 0.3129  0.0183  0.2875  351 LEU   A N   
2343 C  CA  . LEU   A 331 ? 1.4644 1.3265 1.6170 0.3179  0.0144  0.2923  351 LEU   A CA  
2344 C  C   . LEU   A 331 ? 1.5307 1.4018 1.6921 0.3412  -0.0019 0.3126  351 LEU   A C   
2345 O  O   . LEU   A 331 ? 1.5318 1.4634 1.7215 0.3396  -0.0134 0.3190  351 LEU   A O   
2346 C  CB  . LEU   A 331 ? 1.4254 1.3297 1.6137 0.3366  0.0313  0.2778  351 LEU   A CB  
2347 C  CG  . LEU   A 331 ? 1.4780 1.3677 1.6512 0.3215  0.0490  0.2581  351 LEU   A CG  
2348 C  CD1 . LEU   A 331 ? 1.5379 1.4755 1.7482 0.3413  0.0687  0.2492  351 LEU   A CD1 
2349 C  CD2 . LEU   A 331 ? 1.4017 1.3076 1.5670 0.2806  0.0435  0.2545  351 LEU   A CD2 
2350 N  N   . GLN   A 332 ? 1.5225 1.3316 1.6582 0.3638  -0.0053 0.3223  352 GLN   A N   
2351 C  CA  . GLN   A 332 ? 1.5418 1.3518 1.6798 0.3892  -0.0221 0.3434  352 GLN   A CA  
2352 C  C   . GLN   A 332 ? 1.5156 1.3206 1.6275 0.3654  -0.0371 0.3625  352 GLN   A C   
2353 O  O   . GLN   A 332 ? 1.5318 1.3618 1.6488 0.3812  -0.0539 0.3790  352 GLN   A O   
2354 C  CB  . GLN   A 332 ? 1.6728 1.4086 1.7860 0.4205  -0.0205 0.3483  352 GLN   A CB  
2355 C  CG  . GLN   A 332 ? 1.6985 1.4313 1.8152 0.4558  -0.0371 0.3694  352 GLN   A CG  
2356 C  CD  . GLN   A 332 ? 1.8178 1.4803 1.9155 0.4922  -0.0332 0.3697  352 GLN   A CD  
2357 O  OE1 . GLN   A 332 ? 1.8457 1.4811 1.9394 0.4995  -0.0165 0.3500  352 GLN   A OE1 
2358 N  NE2 . GLN   A 332 ? 1.9064 1.5351 1.9876 0.5173  -0.0491 0.3919  352 GLN   A NE2 
2359 N  N   . MET   A 333 ? 1.5205 1.2962 1.6044 0.3291  -0.0314 0.3607  353 MET   A N   
2360 C  CA  . MET   A 333 ? 1.5091 1.2738 1.5641 0.3065  -0.0399 0.3806  353 MET   A CA  
2361 C  C   . MET   A 333 ? 1.4874 1.3265 1.5610 0.2887  -0.0449 0.3757  353 MET   A C   
2362 O  O   . MET   A 333 ? 1.4646 1.3276 1.5488 0.2631  -0.0355 0.3586  353 MET   A O   
2363 C  CB  . MET   A 333 ? 1.4575 1.1600 1.4818 0.2759  -0.0307 0.3814  353 MET   A CB  
2364 C  CG  . MET   A 333 ? 1.5934 1.2169 1.5997 0.2915  -0.0276 0.3801  353 MET   A CG  
2365 S  SD  . MET   A 333 ? 1.6406 1.1880 1.6167 0.2531  -0.0224 0.3812  353 MET   A SD  
2366 C  CE  . MET   A 333 ? 1.8835 1.3433 1.8417 0.2833  -0.0235 0.3733  353 MET   A CE  
2367 N  N   . GLU   A 334 ? 1.4385 1.3107 1.5129 0.3037  -0.0616 0.3901  354 GLU   A N   
2368 C  CA  . GLU   A 334 ? 1.3228 1.2619 1.4121 0.2905  -0.0705 0.3837  354 GLU   A CA  
2369 C  C   . GLU   A 334 ? 1.3036 1.2317 1.3547 0.2618  -0.0682 0.3944  354 GLU   A C   
2370 O  O   . GLU   A 334 ? 1.3149 1.2800 1.3742 0.2386  -0.0645 0.3807  354 GLU   A O   
2371 C  CB  . GLU   A 334 ? 1.4167 1.3974 1.5232 0.3201  -0.0933 0.3914  354 GLU   A CB  
2372 C  CG  . GLU   A 334 ? 1.5910 1.6004 1.7483 0.3481  -0.0945 0.3803  354 GLU   A CG  
2373 C  CD  . GLU   A 334 ? 1.7937 1.8376 1.9693 0.3805  -0.1202 0.3910  354 GLU   A CD  
2374 O  OE1 . GLU   A 334 ? 1.8442 1.8875 1.9865 0.3817  -0.1386 0.4059  354 GLU   A OE1 
2375 O  OE2 . GLU   A 334 ? 1.8311 1.9042 2.0541 0.4062  -0.1220 0.3846  354 GLU   A OE2 
2376 N  N   . TYR   A 335 ? 1.4069 1.2841 1.4167 0.2640  -0.0688 0.4198  355 TYR   A N   
2377 C  CA  . TYR   A 335 ? 1.3535 1.2237 1.3287 0.2384  -0.0627 0.4335  355 TYR   A CA  
2378 C  C   . TYR   A 335 ? 1.3576 1.2138 1.3384 0.2036  -0.0438 0.4211  355 TYR   A C   
2379 O  O   . TYR   A 335 ? 1.2962 1.1767 1.2683 0.1803  -0.0377 0.4202  355 TYR   A O   
2380 C  CB  . TYR   A 335 ? 1.3508 1.1661 1.2819 0.2481  -0.0643 0.4673  355 TYR   A CB  
2381 C  CG  . TYR   A 335 ? 1.3865 1.2079 1.2800 0.2302  -0.0587 0.4862  355 TYR   A CG  
2382 C  CD1 . TYR   A 335 ? 1.3107 1.1777 1.1867 0.2432  -0.0731 0.4893  355 TYR   A CD1 
2383 C  CD2 . TYR   A 335 ? 1.4761 1.2588 1.3524 0.2010  -0.0392 0.5003  355 TYR   A CD2 
2384 C  CE1 . TYR   A 335 ? 1.4353 1.3075 1.2711 0.2308  -0.0656 0.5061  355 TYR   A CE1 
2385 C  CE2 . TYR   A 335 ? 1.4356 1.2285 1.2798 0.1863  -0.0298 0.5193  355 TYR   A CE2 
2386 C  CZ  . TYR   A 335 ? 1.4120 1.2489 1.2327 0.2028  -0.0417 0.5222  355 TYR   A CZ  
2387 O  OH  . TYR   A 335 ? 1.3621 1.2085 1.1450 0.1920  -0.0301 0.5407  355 TYR   A OH  
2388 N  N   . LEU   A 336 ? 1.2988 1.1160 1.2926 0.2016  -0.0357 0.4105  356 LEU   A N   
2389 C  CA  . LEU   A 336 ? 1.3249 1.1333 1.3273 0.1709  -0.0224 0.3943  356 LEU   A CA  
2390 C  C   . LEU   A 336 ? 1.3044 1.1760 1.3337 0.1615  -0.0214 0.3695  356 LEU   A C   
2391 O  O   . LEU   A 336 ? 1.2435 1.1310 1.2728 0.1347  -0.0142 0.3627  356 LEU   A O   
2392 C  CB  . LEU   A 336 ? 1.3171 1.0696 1.3232 0.1760  -0.0178 0.3842  356 LEU   A CB  
2393 C  CG  . LEU   A 336 ? 1.2702 1.0153 1.2865 0.1502  -0.0087 0.3616  356 LEU   A CG  
2394 C  CD1 . LEU   A 336 ? 1.2713 1.0050 1.2772 0.1149  -0.0032 0.3722  356 LEU   A CD1 
2395 C  CD2 . LEU   A 336 ? 1.3891 1.0758 1.4017 0.1622  -0.0073 0.3493  356 LEU   A CD2 
2396 N  N   . ASP   A 337 ? 1.2269 1.1353 1.2821 0.1833  -0.0283 0.3568  357 ASP   A N   
2397 C  CA  . ASP   A 337 ? 1.1995 1.1664 1.2818 0.1745  -0.0284 0.3361  357 ASP   A CA  
2398 C  C   . ASP   A 337 ? 1.1342 1.1396 1.2047 0.1638  -0.0362 0.3414  357 ASP   A C   
2399 O  O   . ASP   A 337 ? 1.0367 1.0723 1.1152 0.1447  -0.0324 0.3270  357 ASP   A O   
2400 C  CB  . ASP   A 337 ? 1.2328 1.2326 1.3508 0.1998  -0.0341 0.3260  357 ASP   A CB  
2401 C  CG  . ASP   A 337 ? 1.2044 1.2657 1.3531 0.1908  -0.0372 0.3088  357 ASP   A CG  
2402 O  OD1 . ASP   A 337 ? 1.1940 1.2920 1.3444 0.1925  -0.0524 0.3123  357 ASP   A OD1 
2403 O  OD2 . ASP   A 337 ? 1.2519 1.3212 1.4202 0.1826  -0.0253 0.2918  357 ASP   A OD2 
2404 N  N   . MET   A 338 ? 1.1853 1.1873 1.2323 0.1782  -0.0473 0.3619  358 MET   A N   
2405 C  CA  . MET   A 338 ? 1.0404 1.0742 1.0664 0.1725  -0.0549 0.3671  358 MET   A CA  
2406 C  C   . MET   A 338 ? 1.1031 1.1231 1.1059 0.1449  -0.0388 0.3727  358 MET   A C   
2407 O  O   . MET   A 338 ? 1.1227 1.1776 1.1209 0.1333  -0.0384 0.3639  358 MET   A O   
2408 C  CB  . MET   A 338 ? 1.0618 1.0877 1.0594 0.1973  -0.0703 0.3898  358 MET   A CB  
2409 C  CG  . MET   A 338 ? 1.1642 1.2173 1.1906 0.2258  -0.0906 0.3835  358 MET   A CG  
2410 S  SD  . MET   A 338 ? 1.2613 1.2878 1.2535 0.2595  -0.1087 0.4130  358 MET   A SD  
2411 C  CE  . MET   A 338 ? 1.1967 1.2310 1.1313 0.2518  -0.1129 0.4274  358 MET   A CE  
2412 N  N   . VAL   A 339 ? 1.1227 1.0922 1.1135 0.1343  -0.0259 0.3869  359 VAL   A N   
2413 C  CA  . VAL   A 339 ? 1.1677 1.1277 1.1473 0.1059  -0.0101 0.3932  359 VAL   A CA  
2414 C  C   . VAL   A 339 ? 1.1708 1.1566 1.1783 0.0864  -0.0042 0.3660  359 VAL   A C   
2415 O  O   . VAL   A 339 ? 1.1151 1.1292 1.1201 0.0702  0.0023  0.3619  359 VAL   A O   
2416 C  CB  . VAL   A 339 ? 1.2112 1.1085 1.1797 0.0968  -0.0006 0.4136  359 VAL   A CB  
2417 C  CG1 . VAL   A 339 ? 1.1992 1.0908 1.1747 0.0634  0.0148  0.4137  359 VAL   A CG1 
2418 C  CG2 . VAL   A 339 ? 1.1612 1.0326 1.0936 0.1121  -0.0030 0.4463  359 VAL   A CG2 
2419 N  N   . VAL   A 340 ? 1.0965 1.0722 1.1285 0.0901  -0.0058 0.3476  360 VAL   A N   
2420 C  CA  . VAL   A 340 ? 1.0751 1.0683 1.1286 0.0738  -0.0005 0.3232  360 VAL   A CA  
2421 C  C   . VAL   A 340 ? 1.0480 1.0969 1.1105 0.0737  -0.0056 0.3093  360 VAL   A C   
2422 O  O   . VAL   A 340 ? 0.9615 1.0303 1.0255 0.0561  -0.0001 0.3007  360 VAL   A O   
2423 C  CB  . VAL   A 340 ? 1.1142 1.0854 1.1848 0.0839  -0.0004 0.3079  360 VAL   A CB  
2424 C  CG1 . VAL   A 340 ? 0.9838 0.9782 1.0723 0.0722  0.0037  0.2834  360 VAL   A CG1 
2425 C  CG2 . VAL   A 340 ? 1.0509 0.9596 1.1095 0.0803  0.0036  0.3163  360 VAL   A CG2 
2426 N  N   . ASN   A 341 ? 0.9845 1.0591 1.0554 0.0938  -0.0178 0.3064  361 ASN   A N   
2427 C  CA  . ASN   A 341 ? 0.9644 1.0869 1.0468 0.0932  -0.0260 0.2909  361 ASN   A CA  
2428 C  C   . ASN   A 341 ? 0.9759 1.1155 1.0307 0.0858  -0.0264 0.2973  361 ASN   A C   
2429 O  O   . ASN   A 341 ? 0.9097 1.0762 0.9688 0.0754  -0.0258 0.2822  361 ASN   A O   
2430 C  CB  . ASN   A 341 ? 0.8996 1.0461 1.0003 0.1152  -0.0423 0.2886  361 ASN   A CB  
2431 C  CG  . ASN   A 341 ? 1.0405 1.1785 1.1726 0.1250  -0.0381 0.2817  361 ASN   A CG  
2432 O  OD1 . ASN   A 341 ? 1.1304 1.2478 1.2680 0.1150  -0.0244 0.2734  361 ASN   A OD1 
2433 N  ND2 . ASN   A 341 ? 1.0772 1.2325 1.2294 0.1465  -0.0503 0.2848  361 ASN   A ND2 
2434 N  N   . GLU   A 342 ? 1.0796 1.2022 1.1034 0.0929  -0.0263 0.3205  362 GLU   A N   
2435 C  CA  . GLU   A 342 ? 0.9936 1.1322 0.9853 0.0894  -0.0232 0.3290  362 GLU   A CA  
2436 C  C   . GLU   A 342 ? 1.0432 1.1805 1.0370 0.0653  -0.0040 0.3278  362 GLU   A C   
2437 O  O   . GLU   A 342 ? 1.1209 1.2867 1.1046 0.0605  -0.0005 0.3206  362 GLU   A O   
2438 C  CB  . GLU   A 342 ? 1.1637 1.2803 1.1178 0.1038  -0.0246 0.3579  362 GLU   A CB  
2439 C  CG  . GLU   A 342 ? 1.1619 1.2887 1.0756 0.1012  -0.0147 0.3725  362 GLU   A CG  
2440 C  CD  . GLU   A 342 ? 1.2014 1.3668 1.0957 0.1148  -0.0301 0.3573  362 GLU   A CD  
2441 O  OE1 . GLU   A 342 ? 1.1949 1.3836 1.1165 0.1184  -0.0469 0.3322  362 GLU   A OE1 
2442 O  OE2 . GLU   A 342 ? 1.2779 1.4485 1.1280 0.1221  -0.0250 0.3709  362 GLU   A OE2 
2443 N  N   . THR   A 343 ? 1.0404 1.1451 1.0484 0.0512  0.0070  0.3336  363 THR   A N   
2444 C  CA  . THR   A 343 ? 1.0096 1.1167 1.0293 0.0273  0.0214  0.3297  363 THR   A CA  
2445 C  C   . THR   A 343 ? 1.0164 1.1534 1.0581 0.0218  0.0176  0.3010  363 THR   A C   
2446 O  O   . THR   A 343 ? 0.9905 1.1529 1.0330 0.0117  0.0245  0.2947  363 THR   A O   
2447 C  CB  . THR   A 343 ? 1.0139 1.0761 1.0466 0.0135  0.0278  0.3376  363 THR   A CB  
2448 O  OG1 . THR   A 343 ? 1.1343 1.1627 1.1457 0.0190  0.0308  0.3659  363 THR   A OG1 
2449 C  CG2 . THR   A 343 ? 1.0281 1.0965 1.0775 -0.0124 0.0395  0.3347  363 THR   A CG2 
2450 N  N   . LEU   A 344 ? 1.0380 1.1721 1.0976 0.0299  0.0080  0.2847  364 LEU   A N   
2451 C  CA  . LEU   A 344 ? 1.0001 1.1576 1.0788 0.0255  0.0049  0.2601  364 LEU   A CA  
2452 C  C   . LEU   A 344 ? 0.9852 1.1804 1.0561 0.0327  -0.0032 0.2509  364 LEU   A C   
2453 O  O   . LEU   A 344 ? 0.9324 1.1462 1.0133 0.0262  -0.0035 0.2332  364 LEU   A O   
2454 C  CB  . LEU   A 344 ? 0.8238 0.9694 0.9224 0.0339  0.0000  0.2489  364 LEU   A CB  
2455 C  CG  . LEU   A 344 ? 0.8230 0.9288 0.9264 0.0274  0.0070  0.2492  364 LEU   A CG  
2456 C  CD1 . LEU   A 344 ? 0.8287 0.9250 0.9464 0.0412  0.0053  0.2396  364 LEU   A CD1 
2457 C  CD2 . LEU   A 344 ? 0.8679 0.9729 0.9761 0.0081  0.0127  0.2382  364 LEU   A CD2 
2458 N  N   . ARG   A 345 ? 1.0045 1.2077 1.0548 0.0472  -0.0116 0.2618  365 ARG   A N   
2459 C  CA  . ARG   A 345 ? 1.0169 1.2507 1.0522 0.0548  -0.0216 0.2517  365 ARG   A CA  
2460 C  C   . ARG   A 345 ? 0.9575 1.2030 0.9720 0.0469  -0.0081 0.2548  365 ARG   A C   
2461 O  O   . ARG   A 345 ? 0.9803 1.2478 0.9937 0.0462  -0.0108 0.2373  365 ARG   A O   
2462 C  CB  . ARG   A 345 ? 1.0260 1.2631 1.0399 0.0746  -0.0372 0.2618  365 ARG   A CB  
2463 C  CG  . ARG   A 345 ? 1.0278 1.2921 1.0230 0.0846  -0.0530 0.2478  365 ARG   A CG  
2464 C  CD  . ARG   A 345 ? 0.9965 1.2610 0.9600 0.1054  -0.0693 0.2602  365 ARG   A CD  
2465 N  NE  . ARG   A 345 ? 1.0944 1.3414 1.0180 0.1087  -0.0537 0.2868  365 ARG   A NE  
2466 C  CZ  . ARG   A 345 ? 1.1547 1.4101 1.0372 0.1124  -0.0448 0.2922  365 ARG   A CZ  
2467 N  NH1 . ARG   A 345 ? 1.1344 1.4128 1.0064 0.1153  -0.0518 0.2705  365 ARG   A NH1 
2468 N  NH2 . ARG   A 345 ? 1.2683 1.5068 1.1186 0.1140  -0.0271 0.3208  365 ARG   A NH2 
2469 N  N   . LEU   A 346 ? 0.9568 1.1876 0.9569 0.0411  0.0073  0.2776  366 LEU   A N   
2470 C  CA  . LEU   A 346 ? 1.0725 1.3197 1.0591 0.0334  0.0241  0.2838  366 LEU   A CA  
2471 C  C   . LEU   A 346 ? 1.0157 1.2690 1.0344 0.0144  0.0335  0.2714  366 LEU   A C   
2472 O  O   . LEU   A 346 ? 1.0248 1.3035 1.0417 0.0113  0.0427  0.2658  366 LEU   A O   
2473 C  CB  . LEU   A 346 ? 0.9761 1.2066 0.9410 0.0315  0.0394  0.3159  366 LEU   A CB  
2474 C  CG  . LEU   A 346 ? 1.1490 1.3801 1.0676 0.0533  0.0338  0.3310  366 LEU   A CG  
2475 C  CD1 . LEU   A 346 ? 1.0691 1.2737 0.9681 0.0504  0.0495  0.3664  366 LEU   A CD1 
2476 C  CD2 . LEU   A 346 ? 1.0833 1.3471 0.9728 0.0639  0.0365  0.3211  366 LEU   A CD2 
2477 N  N   . PHE   A 347 ? 0.9705 1.2009 1.0164 0.0040  0.0307  0.2663  367 PHE   A N   
2478 C  CA  . PHE   A 347 ? 0.9698 1.2013 1.0432 -0.0129 0.0361  0.2548  367 PHE   A CA  
2479 C  C   . PHE   A 347 ? 0.9059 1.1263 0.9964 -0.0112 0.0243  0.2340  367 PHE   A C   
2480 O  O   . PHE   A 347 ? 0.9789 1.1704 1.0812 -0.0170 0.0235  0.2342  367 PHE   A O   
2481 C  CB  . PHE   A 347 ? 1.0398 1.2480 1.1251 -0.0301 0.0469  0.2729  367 PHE   A CB  
2482 C  CG  . PHE   A 347 ? 1.1085 1.3237 1.1776 -0.0325 0.0619  0.2994  367 PHE   A CG  
2483 C  CD1 . PHE   A 347 ? 1.1106 1.3629 1.1777 -0.0345 0.0748  0.3014  367 PHE   A CD1 
2484 C  CD2 . PHE   A 347 ? 1.1118 1.2957 1.1659 -0.0307 0.0646  0.3235  367 PHE   A CD2 
2485 C  CE1 . PHE   A 347 ? 1.1647 1.4251 1.2148 -0.0354 0.0928  0.3283  367 PHE   A CE1 
2486 C  CE2 . PHE   A 347 ? 1.1240 1.3117 1.1597 -0.0326 0.0808  0.3513  367 PHE   A CE2 
2487 C  CZ  . PHE   A 347 ? 1.1780 1.4051 1.2114 -0.0353 0.0962  0.3543  367 PHE   A CZ  
2488 N  N   . PRO   A 348 ? 0.9280 1.1684 1.0183 -0.0026 0.0157  0.2159  368 PRO   A N   
2489 C  CA  . PRO   A 348 ? 0.8948 1.1265 1.0023 -0.0023 0.0084  0.1986  368 PRO   A CA  
2490 C  C   . PRO   A 348 ? 0.9995 1.2307 1.1199 -0.0139 0.0121  0.1866  368 PRO   A C   
2491 O  O   . PRO   A 348 ? 1.0737 1.3259 1.1948 -0.0134 0.0107  0.1743  368 PRO   A O   
2492 C  CB  . PRO   A 348 ? 0.8228 1.0754 0.9267 0.0090  -0.0028 0.1865  368 PRO   A CB  
2493 C  CG  . PRO   A 348 ? 0.8636 1.1384 0.9470 0.0123  -0.0005 0.1884  368 PRO   A CG  
2494 C  CD  . PRO   A 348 ? 0.8740 1.1423 0.9458 0.0080  0.0120  0.2108  368 PRO   A CD  
2495 N  N   . ILE   A 349 ? 0.9373 1.1423 1.0661 -0.0226 0.0148  0.1888  369 ILE   A N   
2496 C  CA  . ILE   A 349 ? 1.0195 1.2225 1.1594 -0.0344 0.0155  0.1798  369 ILE   A CA  
2497 C  C   . ILE   A 349 ? 0.8734 1.0864 1.0161 -0.0304 0.0102  0.1604  369 ILE   A C   
2498 O  O   . ILE   A 349 ? 1.0385 1.2560 1.1890 -0.0372 0.0086  0.1520  369 ILE   A O   
2499 C  CB  . ILE   A 349 ? 0.9648 1.1294 1.1078 -0.0414 0.0142  0.1819  369 ILE   A CB  
2500 C  CG1 . ILE   A 349 ? 1.0118 1.1536 1.1479 -0.0291 0.0113  0.1746  369 ILE   A CG1 
2501 C  CG2 . ILE   A 349 ? 1.1337 1.2834 1.2753 -0.0479 0.0192  0.2023  369 ILE   A CG2 
2502 C  CD1 . ILE   A 349 ? 1.1481 1.2479 1.2795 -0.0303 0.0103  0.1759  369 ILE   A CD1 
2503 N  N   . ALA   A 350 ? 0.7626 0.9790 0.9015 -0.0198 0.0064  0.1540  370 ALA   A N   
2504 C  CA  . ALA   A 350 ? 0.9242 1.1469 1.0651 -0.0167 0.0021  0.1382  370 ALA   A CA  
2505 C  C   . ALA   A 350 ? 0.9293 1.1802 1.0669 -0.0131 -0.0006 0.1320  370 ALA   A C   
2506 O  O   . ALA   A 350 ? 1.0464 1.3014 1.1850 -0.0117 -0.0039 0.1193  370 ALA   A O   
2507 C  CB  . ALA   A 350 ? 0.9167 1.1283 1.0608 -0.0095 0.0004  0.1349  370 ALA   A CB  
2508 N  N   . MET   A 351 ? 0.7945 1.0614 0.9237 -0.0090 0.0004  0.1404  371 MET   A N   
2509 C  CA  . MET   A 351 ? 0.8945 1.1856 1.0123 -0.0016 -0.0018 0.1342  371 MET   A CA  
2510 C  C   . MET   A 351 ? 0.7588 1.0491 0.8751 0.0058  -0.0137 0.1194  371 MET   A C   
2511 O  O   . MET   A 351 ? 0.7419 1.0417 0.8463 0.0140  -0.0214 0.1175  371 MET   A O   
2512 C  CB  . MET   A 351 ? 0.8769 1.1841 0.9990 -0.0045 0.0043  0.1291  371 MET   A CB  
2513 C  CG  . MET   A 351 ? 1.0160 1.3323 1.1451 -0.0137 0.0163  0.1452  371 MET   A CG  
2514 S  SD  . MET   A 351 ? 1.4716 1.8039 1.6240 -0.0220 0.0197  0.1386  371 MET   A SD  
2515 C  CE  . MET   A 351 ? 1.2698 1.5659 1.4310 -0.0298 0.0094  0.1308  371 MET   A CE  
2516 N  N   . ARG   A 352 ? 0.8071 1.0841 0.9344 0.0028  -0.0164 0.1093  372 ARG   A N   
2517 C  CA  . ARG   A 352 ? 0.7753 1.0479 0.9062 0.0064  -0.0267 0.0970  372 ARG   A CA  
2518 C  C   . ARG   A 352 ? 0.7411 0.9940 0.8878 0.0015  -0.0246 0.0988  372 ARG   A C   
2519 O  O   . ARG   A 352 ? 0.8067 1.0463 0.9549 -0.0023 -0.0161 0.1048  372 ARG   A O   
2520 C  CB  . ARG   A 352 ? 0.8110 1.0864 0.9347 0.0106  -0.0304 0.0822  372 ARG   A CB  
2521 C  CG  . ARG   A 352 ? 0.8348 1.1322 0.9428 0.0182  -0.0277 0.0799  372 ARG   A CG  
2522 C  CD  . ARG   A 352 ? 0.9188 1.2185 1.0270 0.0220  -0.0267 0.0687  372 ARG   A CD  
2523 N  NE  . ARG   A 352 ? 0.9316 1.2485 1.0232 0.0354  -0.0283 0.0585  372 ARG   A NE  
2524 C  CZ  . ARG   A 352 ? 0.9559 1.2738 1.0449 0.0442  -0.0308 0.0450  372 ARG   A CZ  
2525 N  NH1 . ARG   A 352 ? 0.9523 1.2541 1.0528 0.0407  -0.0336 0.0409  372 ARG   A NH1 
2526 N  NH2 . ARG   A 352 ? 0.9069 1.2402 0.9776 0.0596  -0.0307 0.0354  372 ARG   A NH2 
2527 N  N   . LEU   A 353 ? 0.6656 0.9162 0.8239 0.0018  -0.0323 0.0933  373 LEU   A N   
2528 C  CA  . LEU   A 353 ? 0.5998 0.8347 0.7747 -0.0022 -0.0275 0.0952  373 LEU   A CA  
2529 C  C   . LEU   A 353 ? 0.7638 0.9891 0.9399 -0.0037 -0.0337 0.0837  373 LEU   A C   
2530 O  O   . LEU   A 353 ? 0.7151 0.9475 0.8891 -0.0018 -0.0467 0.0737  373 LEU   A O   
2531 C  CB  . LEU   A 353 ? 0.6905 0.9335 0.8887 -0.0024 -0.0293 0.1029  373 LEU   A CB  
2532 C  CG  . LEU   A 353 ? 0.7071 0.9569 0.9033 0.0019  -0.0258 0.1147  373 LEU   A CG  
2533 C  CD1 . LEU   A 353 ? 0.7743 1.0373 0.9975 0.0046  -0.0314 0.1206  373 LEU   A CD1 
2534 C  CD2 . LEU   A 353 ? 0.5750 0.8058 0.7625 0.0017  -0.0113 0.1217  373 LEU   A CD2 
2535 N  N   . GLU   A 354 ? 0.7706 0.9757 0.9458 -0.0057 -0.0253 0.0850  374 GLU   A N   
2536 C  CA  . GLU   A 354 ? 0.6738 0.8631 0.8452 -0.0061 -0.0302 0.0762  374 GLU   A CA  
2537 C  C   . GLU   A 354 ? 0.7101 0.8801 0.8943 -0.0110 -0.0204 0.0842  374 GLU   A C   
2538 O  O   . GLU   A 354 ? 0.7885 0.9520 0.9714 -0.0101 -0.0064 0.0944  374 GLU   A O   
2539 C  CB  . GLU   A 354 ? 0.6600 0.8421 0.8082 -0.0001 -0.0303 0.0695  374 GLU   A CB  
2540 C  CG  . GLU   A 354 ? 0.7532 0.9577 0.8919 0.0054  -0.0368 0.0621  374 GLU   A CG  
2541 C  CD  . GLU   A 354 ? 0.9988 1.2021 1.1239 0.0120  -0.0375 0.0551  374 GLU   A CD  
2542 O  OE1 . GLU   A 354 ? 1.0117 1.1940 1.1312 0.0129  -0.0356 0.0555  374 GLU   A OE1 
2543 O  OE2 . GLU   A 354 ? 1.0584 1.2834 1.1785 0.0178  -0.0395 0.0500  374 GLU   A OE2 
2544 N  N   . ARG   A 355 ? 0.5851 0.7440 0.7801 -0.0156 -0.0270 0.0798  375 ARG   A N   
2545 C  CA  . ARG   A 355 ? 0.7183 0.8568 0.9256 -0.0214 -0.0159 0.0893  375 ARG   A CA  
2546 C  C   . ARG   A 355 ? 0.7172 0.8299 0.9138 -0.0219 -0.0245 0.0814  375 ARG   A C   
2547 O  O   . ARG   A 355 ? 0.7879 0.9031 0.9865 -0.0221 -0.0422 0.0679  375 ARG   A O   
2548 C  CB  . ARG   A 355 ? 0.7112 0.8657 0.9608 -0.0314 -0.0144 0.0974  375 ARG   A CB  
2549 C  CG  . ARG   A 355 ? 0.7199 0.8989 0.9831 -0.0285 -0.0065 0.1060  375 ARG   A CG  
2550 C  CD  . ARG   A 355 ? 0.6104 0.7764 0.8593 -0.0222 0.0165  0.1182  375 ARG   A CD  
2551 N  NE  . ARG   A 355 ? 0.7084 0.8942 0.9744 -0.0180 0.0247  0.1267  375 ARG   A NE  
2552 C  CZ  . ARG   A 355 ? 0.6305 0.8237 0.8811 -0.0112 0.0209  0.1246  375 ARG   A CZ  
2553 N  NH1 . ARG   A 355 ? 0.7691 0.9567 0.9909 -0.0092 0.0107  0.1153  375 ARG   A NH1 
2554 N  NH2 . ARG   A 355 ? 0.5822 0.7891 0.8491 -0.0058 0.0281  0.1332  375 ARG   A NH2 
2555 N  N   . VAL   A 356 ? 0.9087 0.9932 1.0897 -0.0199 -0.0127 0.0894  376 VAL   A N   
2556 C  CA  . VAL   A 356 ? 0.8103 0.8634 0.9807 -0.0196 -0.0195 0.0852  376 VAL   A CA  
2557 C  C   . VAL   A 356 ? 0.8760 0.9186 1.0808 -0.0347 -0.0166 0.0942  376 VAL   A C   
2558 O  O   . VAL   A 356 ? 0.9104 0.9544 1.1328 -0.0412 0.0027  0.1115  376 VAL   A O   
2559 C  CB  . VAL   A 356 ? 0.7900 0.8146 0.9240 -0.0089 -0.0098 0.0912  376 VAL   A CB  
2560 C  CG1 . VAL   A 356 ? 0.7564 0.7435 0.8795 -0.0079 -0.0158 0.0903  376 VAL   A CG1 
2561 C  CG2 . VAL   A 356 ? 0.7169 0.7546 0.8260 0.0036  -0.0173 0.0804  376 VAL   A CG2 
2562 N  N   . CYS   A 357 ? 0.8119 0.8441 1.0276 -0.0402 -0.0356 0.0820  377 CYS   A N   
2563 C  CA  . CYS   A 357 ? 0.8729 0.8933 1.1273 -0.0579 -0.0384 0.0880  377 CYS   A CA  
2564 C  C   . CYS   A 357 ? 1.0097 0.9871 1.2521 -0.0602 -0.0248 0.1023  377 CYS   A C   
2565 O  O   . CYS   A 357 ? 0.9976 0.9409 1.2129 -0.0530 -0.0358 0.0936  377 CYS   A O   
2566 C  CB  . CYS   A 357 ? 0.9024 0.9207 1.1654 -0.0609 -0.0676 0.0664  377 CYS   A CB  
2567 S  SG  . CYS   A 357 ? 0.9813 0.9720 1.2876 -0.0834 -0.0804 0.0674  377 CYS   A SG  
2568 N  N   . LYS   A 358 ? 0.9927 0.9706 1.2529 -0.0681 0.0004  0.1254  378 LYS   A N   
2569 C  CA  . LYS   A 358 ? 1.0382 0.9750 1.2764 -0.0667 0.0188  0.1433  378 LYS   A CA  
2570 C  C   . LYS   A 358 ? 1.1227 1.0285 1.3912 -0.0853 0.0152  0.1510  378 LYS   A C   
2571 O  O   . LYS   A 358 ? 1.1515 1.0145 1.3961 -0.0833 0.0271  0.1654  378 LYS   A O   
2572 C  CB  . LYS   A 358 ? 0.9892 0.9369 1.2254 -0.0638 0.0511  0.1658  378 LYS   A CB  
2573 C  CG  . LYS   A 358 ? 1.1748 1.1401 1.4688 -0.0830 0.0696  0.1856  378 LYS   A CG  
2574 C  CD  . LYS   A 358 ? 1.1193 1.0865 1.4004 -0.0750 0.1063  0.2094  378 LYS   A CD  
2575 C  CE  . LYS   A 358 ? 1.0833 1.0815 1.3475 -0.0592 0.1105  0.2022  378 LYS   A CE  
2576 N  NZ  . LYS   A 358 ? 1.0734 1.0728 1.3256 -0.0495 0.1460  0.2232  378 LYS   A NZ  
2577 N  N   . LYS   A 359 ? 1.0603 0.9837 1.3794 -0.1033 -0.0021 0.1423  379 LYS   A N   
2578 C  CA  . LYS   A 359 ? 1.1714 1.0626 1.5234 -0.1236 -0.0113 0.1462  379 LYS   A CA  
2579 C  C   . LYS   A 359 ? 1.1735 1.0729 1.5473 -0.1303 -0.0483 0.1184  379 LYS   A C   
2580 O  O   . LYS   A 359 ? 1.2606 1.2006 1.6384 -0.1239 -0.0608 0.1032  379 LYS   A O   
2581 C  CB  . LYS   A 359 ? 1.2520 1.1579 1.6638 -0.1467 0.0123  0.1733  379 LYS   A CB  
2582 C  CG  . LYS   A 359 ? 1.2348 1.1435 1.6301 -0.1391 0.0531  0.2020  379 LYS   A CG  
2583 C  CD  . LYS   A 359 ? 1.2915 1.2253 1.7571 -0.1622 0.0758  0.2270  379 LYS   A CD  
2584 C  CE  . LYS   A 359 ? 1.4968 1.4279 1.9433 -0.1534 0.1204  0.2578  379 LYS   A CE  
2585 N  NZ  . LYS   A 359 ? 1.4925 1.4478 2.0128 -0.1767 0.1460  0.2850  379 LYS   A NZ  
2586 N  N   . ASP   A 360 ? 1.2516 1.1085 1.6372 -0.1429 -0.0663 0.1123  380 ASP   A N   
2587 C  CA  . ASP   A 360 ? 1.1525 1.0130 1.5647 -0.1525 -0.1026 0.0865  380 ASP   A CA  
2588 C  C   . ASP   A 360 ? 1.0928 1.0038 1.5727 -0.1728 -0.1043 0.0924  380 ASP   A C   
2589 O  O   . ASP   A 360 ? 1.0354 0.9550 1.5652 -0.1930 -0.0832 0.1180  380 ASP   A O   
2590 C  CB  . ASP   A 360 ? 1.0709 0.8707 1.4903 -0.1659 -0.1206 0.0815  380 ASP   A CB  
2591 C  CG  . ASP   A 360 ? 1.3535 1.1060 1.7066 -0.1412 -0.1320 0.0648  380 ASP   A CG  
2592 O  OD1 . ASP   A 360 ? 1.3454 1.1159 1.6513 -0.1153 -0.1240 0.0592  380 ASP   A OD1 
2593 O  OD2 . ASP   A 360 ? 1.4620 1.1592 1.8131 -0.1475 -0.1498 0.0570  380 ASP   A OD2 
2594 N  N   . VAL   A 361 ? 1.1333 1.0793 1.6154 -0.1660 -0.1286 0.0699  381 VAL   A N   
2595 C  CA  . VAL   A 361 ? 1.1632 1.1609 1.7061 -0.1805 -0.1343 0.0734  381 VAL   A CA  
2596 C  C   . VAL   A 361 ? 1.1445 1.1511 1.6884 -0.1785 -0.1771 0.0419  381 VAL   A C   
2597 O  O   . VAL   A 361 ? 1.1526 1.1399 1.6395 -0.1584 -0.1943 0.0186  381 VAL   A O   
2598 C  CB  . VAL   A 361 ? 1.0653 1.1116 1.6030 -0.1670 -0.1070 0.0884  381 VAL   A CB  
2599 C  CG1 . VAL   A 361 ? 1.1434 1.1929 1.7067 -0.1760 -0.0672 0.1215  381 VAL   A CG1 
2600 C  CG2 . VAL   A 361 ? 0.9863 1.0274 1.4505 -0.1387 -0.1035 0.0771  381 VAL   A CG2 
2601 N  N   . GLU   A 362 ? 1.1280 1.1659 1.7379 -0.1982 -0.1940 0.0417  382 GLU   A N   
2602 C  CA  . GLU   A 362 ? 1.1822 1.2391 1.7970 -0.1952 -0.2349 0.0143  382 GLU   A CA  
2603 C  C   . GLU   A 362 ? 1.0972 1.2180 1.7408 -0.1904 -0.2278 0.0242  382 GLU   A C   
2604 O  O   . GLU   A 362 ? 1.1501 1.3031 1.8577 -0.2066 -0.2091 0.0475  382 GLU   A O   
2605 C  CB  . GLU   A 362 ? 1.3120 1.3488 1.9829 -0.2226 -0.2694 0.0023  382 GLU   A CB  
2606 C  CG  . GLU   A 362 ? 1.4292 1.4129 2.0533 -0.2149 -0.3071 -0.0318 382 GLU   A CG  
2607 C  CD  . GLU   A 362 ? 1.6305 1.5859 2.3129 -0.2452 -0.3413 -0.0426 382 GLU   A CD  
2608 O  OE1 . GLU   A 362 ? 1.6541 1.5896 2.3847 -0.2708 -0.3236 -0.0201 382 GLU   A OE1 
2609 O  OE2 . GLU   A 362 ? 1.6638 1.6159 2.3435 -0.2437 -0.3861 -0.0732 382 GLU   A OE2 
2610 N  N   . ILE   A 363 ? 1.1752 1.3140 1.7714 -0.1669 -0.2407 0.0082  383 ILE   A N   
2611 C  CA  . ILE   A 363 ? 1.1471 1.3406 1.7625 -0.1589 -0.2370 0.0165  383 ILE   A CA  
2612 C  C   . ILE   A 363 ? 1.1580 1.3629 1.7578 -0.1493 -0.2800 -0.0102 383 ILE   A C   
2613 O  O   . ILE   A 363 ? 1.0556 1.2389 1.5870 -0.1293 -0.2919 -0.0297 383 ILE   A O   
2614 C  CB  . ILE   A 363 ? 1.1216 1.3269 1.6893 -0.1373 -0.2020 0.0310  383 ILE   A CB  
2615 C  CG1 . ILE   A 363 ? 0.9621 1.1380 1.4495 -0.1157 -0.2056 0.0139  383 ILE   A CG1 
2616 C  CG2 . ILE   A 363 ? 1.1556 1.3536 1.7409 -0.1454 -0.1613 0.0579  383 ILE   A CG2 
2617 C  CD1 . ILE   A 363 ? 1.0353 1.2285 1.4818 -0.0961 -0.1793 0.0249  383 ILE   A CD1 
2618 N  N   . ASN   A 364 ? 1.1511 1.3906 1.8145 -0.1626 -0.3033 -0.0109 384 ASN   A N   
2619 C  CA  . ASN   A 364 ? 1.2061 1.4600 1.8577 -0.1527 -0.3471 -0.0347 384 ASN   A CA  
2620 C  C   . ASN   A 364 ? 1.2151 1.4194 1.8182 -0.1487 -0.3815 -0.0671 384 ASN   A C   
2621 O  O   . ASN   A 364 ? 1.1724 1.3699 1.7112 -0.1251 -0.4012 -0.0874 384 ASN   A O   
2622 C  CB  . ASN   A 364 ? 1.2163 1.4982 1.8186 -0.1247 -0.3370 -0.0301 384 ASN   A CB  
2623 C  CG  . ASN   A 364 ? 1.0639 1.3888 1.7089 -0.1254 -0.3040 -0.0003 384 ASN   A CG  
2624 O  OD1 . ASN   A 364 ? 1.1494 1.5157 1.8504 -0.1298 -0.3177 0.0054  384 ASN   A OD1 
2625 N  ND2 . ASN   A 364 ? 1.0175 1.3322 1.6360 -0.1194 -0.2618 0.0176  384 ASN   A ND2 
2626 N  N   . GLY   A 365 ? 1.2289 1.3954 1.8611 -0.1708 -0.3871 -0.0710 385 GLY   A N   
2627 C  CA  . GLY   A 365 ? 1.2767 1.3909 1.8728 -0.1695 -0.4229 -0.1029 385 GLY   A CA  
2628 C  C   . GLY   A 365 ? 1.3776 1.4452 1.8941 -0.1490 -0.4054 -0.1110 385 GLY   A C   
2629 O  O   . GLY   A 365 ? 1.4148 1.4345 1.8969 -0.1444 -0.4332 -0.1385 385 GLY   A O   
2630 N  N   . MET   A 366 ? 1.2804 1.3599 1.7681 -0.1359 -0.3622 -0.0895 386 MET   A N   
2631 C  CA  . MET   A 366 ? 1.2322 1.2773 1.6481 -0.1140 -0.3454 -0.0962 386 MET   A CA  
2632 C  C   . MET   A 366 ? 1.2113 1.2314 1.6437 -0.1264 -0.3126 -0.0741 386 MET   A C   
2633 O  O   . MET   A 366 ? 1.0507 1.0986 1.5151 -0.1350 -0.2808 -0.0457 386 MET   A O   
2634 C  CB  . MET   A 366 ? 1.2290 1.3066 1.5930 -0.0869 -0.3255 -0.0909 386 MET   A CB  
2635 C  CG  . MET   A 366 ? 1.1720 1.2238 1.4685 -0.0635 -0.3090 -0.0980 386 MET   A CG  
2636 S  SD  . MET   A 366 ? 1.2741 1.3639 1.5127 -0.0336 -0.2977 -0.0984 386 MET   A SD  
2637 C  CE  . MET   A 366 ? 1.3688 1.4708 1.6057 -0.0300 -0.3422 -0.1208 386 MET   A CE  
2638 N  N   . PHE   A 367 ? 1.2634 1.2285 1.6693 -0.1247 -0.3206 -0.0874 387 PHE   A N   
2639 C  CA  . PHE   A 367 ? 1.1819 1.1164 1.5896 -0.1312 -0.2910 -0.0671 387 PHE   A CA  
2640 C  C   . PHE   A 367 ? 1.1889 1.1315 1.5391 -0.1045 -0.2618 -0.0601 387 PHE   A C   
2641 O  O   . PHE   A 367 ? 1.1998 1.1411 1.4959 -0.0793 -0.2711 -0.0802 387 PHE   A O   
2642 C  CB  . PHE   A 367 ? 1.1285 0.9967 1.5288 -0.1379 -0.3122 -0.0833 387 PHE   A CB  
2643 C  CG  . PHE   A 367 ? 1.3396 1.1696 1.7261 -0.1378 -0.2838 -0.0640 387 PHE   A CG  
2644 C  CD1 . PHE   A 367 ? 1.3464 1.1805 1.7813 -0.1611 -0.2565 -0.0311 387 PHE   A CD1 
2645 C  CD2 . PHE   A 367 ? 1.4106 1.2020 1.7343 -0.1121 -0.2838 -0.0779 387 PHE   A CD2 
2646 C  CE1 . PHE   A 367 ? 1.3701 1.1663 1.7850 -0.1586 -0.2309 -0.0123 387 PHE   A CE1 
2647 C  CE2 . PHE   A 367 ? 1.4332 1.1888 1.7421 -0.1097 -0.2605 -0.0599 387 PHE   A CE2 
2648 C  CZ  . PHE   A 367 ? 1.3800 1.1359 1.7315 -0.1330 -0.2347 -0.0269 387 PHE   A CZ  
2649 N  N   . ILE   A 368 ? 1.1495 1.1011 1.5120 -0.1096 -0.2264 -0.0314 388 ILE   A N   
2650 C  CA  . ILE   A 368 ? 1.1326 1.0917 1.4483 -0.0878 -0.2000 -0.0231 388 ILE   A CA  
2651 C  C   . ILE   A 368 ? 1.1916 1.1107 1.5016 -0.0916 -0.1797 -0.0063 388 ILE   A C   
2652 O  O   . ILE   A 368 ? 1.2041 1.1223 1.5533 -0.1110 -0.1620 0.0173  388 ILE   A O   
2653 C  CB  . ILE   A 368 ? 1.1096 1.1214 1.4358 -0.0854 -0.1778 -0.0054 388 ILE   A CB  
2654 C  CG1 . ILE   A 368 ? 1.1023 1.1503 1.4286 -0.0793 -0.1984 -0.0200 388 ILE   A CG1 
2655 C  CG2 . ILE   A 368 ? 1.1194 1.1342 1.4013 -0.0661 -0.1534 0.0025  388 ILE   A CG2 
2656 C  CD1 . ILE   A 368 ? 0.9853 1.0795 1.3185 -0.0749 -0.1789 -0.0034 388 ILE   A CD1 
2657 N  N   . PRO   A 369 ? 1.2243 1.1106 1.4860 -0.0720 -0.1805 -0.0164 389 PRO   A N   
2658 C  CA  . PRO   A 369 ? 1.1136 0.9572 1.3647 -0.0729 -0.1642 -0.0003 389 PRO   A CA  
2659 C  C   . PRO   A 369 ? 1.1985 1.0644 1.4369 -0.0660 -0.1319 0.0232  389 PRO   A C   
2660 O  O   . PRO   A 369 ? 1.2098 1.1197 1.4409 -0.0572 -0.1233 0.0236  389 PRO   A O   
2661 C  CB  . PRO   A 369 ? 1.1797 0.9857 1.3823 -0.0492 -0.1807 -0.0231 389 PRO   A CB  
2662 C  CG  . PRO   A 369 ? 1.1977 1.0317 1.3836 -0.0349 -0.2018 -0.0507 389 PRO   A CG  
2663 C  CD  . PRO   A 369 ? 1.1301 1.0202 1.3437 -0.0452 -0.1943 -0.0415 389 PRO   A CD  
2664 N  N   . LYS   A 370 ? 1.2074 1.0375 1.4406 -0.0699 -0.1149 0.0430  390 LYS   A N   
2665 C  CA  . LYS   A 370 ? 1.1448 0.9856 1.3592 -0.0620 -0.0862 0.0645  390 LYS   A CA  
2666 C  C   . LYS   A 370 ? 1.1457 0.9968 1.3120 -0.0347 -0.0881 0.0520  390 LYS   A C   
2667 O  O   . LYS   A 370 ? 1.1954 1.0311 1.3378 -0.0195 -0.1068 0.0315  390 LYS   A O   
2668 C  CB  . LYS   A 370 ? 1.1476 0.9405 1.3583 -0.0692 -0.0698 0.0878  390 LYS   A CB  
2669 C  CG  . LYS   A 370 ? 1.1321 0.9297 1.3197 -0.0612 -0.0399 0.1114  390 LYS   A CG  
2670 C  CD  . LYS   A 370 ? 1.1542 0.8976 1.3287 -0.0652 -0.0251 0.1343  390 LYS   A CD  
2671 C  CE  . LYS   A 370 ? 1.2181 0.9576 1.3519 -0.0498 0.0004  0.1537  390 LYS   A CE  
2672 N  NZ  . LYS   A 370 ? 1.6323 1.3136 1.7416 -0.0492 0.0138  0.1765  390 LYS   A NZ  
2673 N  N   . GLY   A 371 ? 1.1722 1.0508 1.3270 -0.0281 -0.0689 0.0640  391 GLY   A N   
2674 C  CA  . GLY   A 371 ? 1.0675 0.9596 1.1853 -0.0059 -0.0697 0.0552  391 GLY   A CA  
2675 C  C   . GLY   A 371 ? 0.9718 0.9072 1.0912 0.0014  -0.0807 0.0370  391 GLY   A C   
2676 O  O   . GLY   A 371 ? 0.9990 0.9554 1.0977 0.0158  -0.0777 0.0333  391 GLY   A O   
2677 N  N   . VAL   A 372 ? 0.9259 0.8750 1.0689 -0.0082 -0.0939 0.0262  392 VAL   A N   
2678 C  CA  . VAL   A 372 ? 0.9291 0.9169 1.0680 0.0001  -0.1030 0.0110  392 VAL   A CA  
2679 C  C   . VAL   A 372 ? 0.9059 0.9328 1.0544 -0.0039 -0.0871 0.0240  392 VAL   A C   
2680 O  O   . VAL   A 372 ? 0.9181 0.9483 1.0899 -0.0175 -0.0745 0.0406  392 VAL   A O   
2681 C  CB  . VAL   A 372 ? 0.8292 0.8162 0.9857 -0.0079 -0.1239 -0.0040 392 VAL   A CB  
2682 C  CG1 . VAL   A 372 ? 0.7757 0.8048 0.9271 -0.0007 -0.1299 -0.0141 392 VAL   A CG1 
2683 C  CG2 . VAL   A 372 ? 0.9106 0.8565 1.0485 0.0013  -0.1426 -0.0224 392 VAL   A CG2 
2684 N  N   . VAL   A 373 ? 0.8405 0.8963 0.9720 0.0086  -0.0865 0.0174  393 VAL   A N   
2685 C  CA  . VAL   A 373 ? 0.8123 0.9024 0.9517 0.0053  -0.0750 0.0274  393 VAL   A CA  
2686 C  C   . VAL   A 373 ? 0.8241 0.9387 0.9771 0.0014  -0.0856 0.0209  393 VAL   A C   
2687 O  O   . VAL   A 373 ? 0.8489 0.9726 0.9859 0.0118  -0.0975 0.0058  393 VAL   A O   
2688 C  CB  . VAL   A 373 ? 0.7546 0.8622 0.8729 0.0180  -0.0689 0.0260  393 VAL   A CB  
2689 C  CG1 . VAL   A 373 ? 0.7254 0.8631 0.8519 0.0133  -0.0592 0.0357  393 VAL   A CG1 
2690 C  CG2 . VAL   A 373 ? 0.7989 0.8823 0.9024 0.0232  -0.0624 0.0317  393 VAL   A CG2 
2691 N  N   . VAL   A 374 ? 0.7359 0.8615 0.9166 -0.0113 -0.0813 0.0323  394 VAL   A N   
2692 C  CA  . VAL   A 374 ? 0.7357 0.8863 0.9300 -0.0139 -0.0929 0.0282  394 VAL   A CA  
2693 C  C   . VAL   A 374 ? 0.6662 0.8450 0.8516 -0.0082 -0.0819 0.0370  394 VAL   A C   
2694 O  O   . VAL   A 374 ? 0.6579 0.8387 0.8498 -0.0114 -0.0652 0.0514  394 VAL   A O   
2695 C  CB  . VAL   A 374 ? 0.7798 0.9312 1.0161 -0.0299 -0.0962 0.0361  394 VAL   A CB  
2696 C  CG1 . VAL   A 374 ? 0.7490 0.9313 1.0003 -0.0303 -0.1075 0.0350  394 VAL   A CG1 
2697 C  CG2 . VAL   A 374 ? 0.8425 0.9650 1.0904 -0.0380 -0.1121 0.0255  394 VAL   A CG2 
2698 N  N   . MET   A 375 ? 0.6444 0.8416 0.8117 0.0011  -0.0908 0.0285  395 MET   A N   
2699 C  CA  A MET   A 375 ? 0.7748 0.9950 0.9303 0.0065  -0.0802 0.0375  395 MET   A CA  
2700 C  CA  B MET   A 375 ? 0.7633 0.9835 0.9187 0.0065  -0.0803 0.0375  395 MET   A CA  
2701 C  C   . MET   A 375 ? 0.7416 0.9814 0.9016 0.0075  -0.0901 0.0396  395 MET   A C   
2702 O  O   . MET   A 375 ? 0.7519 0.9923 0.9053 0.0116  -0.1087 0.0265  395 MET   A O   
2703 C  CB  A MET   A 375 ? 0.7069 0.9337 0.8336 0.0187  -0.0770 0.0299  395 MET   A CB  
2704 C  CB  B MET   A 375 ? 0.6623 0.8893 0.7890 0.0187  -0.0772 0.0298  395 MET   A CB  
2705 C  CG  A MET   A 375 ? 0.7487 0.9979 0.8673 0.0212  -0.0641 0.0416  395 MET   A CG  
2706 C  CG  B MET   A 375 ? 0.7561 1.0065 0.8739 0.0217  -0.0655 0.0410  395 MET   A CG  
2707 S  SD  A MET   A 375 ? 0.7028 0.9752 0.8009 0.0310  -0.0704 0.0406  395 MET   A SD  
2708 S  SD  B MET   A 375 ? 0.9411 1.2095 1.0331 0.0362  -0.0609 0.0330  395 MET   A SD  
2709 C  CE  A MET   A 375 ? 0.8140 1.0864 0.8847 0.0472  -0.0774 0.0200  395 MET   A CE  
2710 C  CE  B MET   A 375 ? 0.8167 1.0906 0.8850 0.0485  -0.0768 0.0195  395 MET   A CE  
2711 N  N   . ILE   A 376 ? 0.6626 0.9151 0.8310 0.0054  -0.0795 0.0552  396 ILE   A N   
2712 C  CA  . ILE   A 376 ? 0.7541 1.0247 0.9238 0.0091  -0.0878 0.0604  396 ILE   A CA  
2713 C  C   . ILE   A 376 ? 0.7132 0.9946 0.8541 0.0173  -0.0777 0.0679  396 ILE   A C   
2714 O  O   . ILE   A 376 ? 0.6845 0.9643 0.8284 0.0139  -0.0616 0.0807  396 ILE   A O   
2715 C  CB  . ILE   A 376 ? 0.7063 0.9818 0.9095 0.0025  -0.0831 0.0741  396 ILE   A CB  
2716 C  CG1 . ILE   A 376 ? 0.5831 0.8537 0.8218 -0.0073 -0.0917 0.0693  396 ILE   A CG1 
2717 C  CG2 . ILE   A 376 ? 0.6255 0.9189 0.8269 0.0095  -0.0918 0.0813  396 ILE   A CG2 
2718 C  CD1 . ILE   A 376 ? 0.6908 0.9427 0.9412 -0.0151 -0.0747 0.0741  396 ILE   A CD1 
2719 N  N   . PRO   A 377 ? 0.7399 1.0308 0.8524 0.0280  -0.0857 0.0608  397 PRO   A N   
2720 C  CA  . PRO   A 377 ? 0.7552 1.0581 0.8427 0.0345  -0.0718 0.0711  397 PRO   A CA  
2721 C  C   . PRO   A 377 ? 0.7787 1.0881 0.8662 0.0349  -0.0681 0.0897  397 PRO   A C   
2722 O  O   . PRO   A 377 ? 0.8171 1.1346 0.8846 0.0447  -0.0784 0.0912  397 PRO   A O   
2723 C  CB  . PRO   A 377 ? 0.8095 1.1193 0.8634 0.0488  -0.0807 0.0571  397 PRO   A CB  
2724 C  CG  . PRO   A 377 ? 0.7202 1.0218 0.7786 0.0504  -0.1058 0.0425  397 PRO   A CG  
2725 C  CD  . PRO   A 377 ? 0.6987 0.9875 0.7981 0.0351  -0.1074 0.0424  397 PRO   A CD  
2726 N  N   . SER   A 378 ? 0.7307 1.0332 0.8367 0.0262  -0.0548 0.1034  398 SER   A N   
2727 C  CA  . SER   A 378 ? 0.6583 0.9609 0.7663 0.0277  -0.0523 0.1209  398 SER   A CA  
2728 C  C   . SER   A 378 ? 0.7956 1.1066 0.8720 0.0354  -0.0469 0.1325  398 SER   A C   
2729 O  O   . SER   A 378 ? 0.8334 1.1484 0.8957 0.0447  -0.0562 0.1397  398 SER   A O   
2730 C  CB  . SER   A 378 ? 0.7689 1.0566 0.8957 0.0190  -0.0382 0.1310  398 SER   A CB  
2731 O  OG  . SER   A 378 ? 0.8515 1.1320 1.0045 0.0150  -0.0407 0.1249  398 SER   A OG  
2732 N  N   . TYR   A 379 ? 0.7314 1.0464 0.7977 0.0321  -0.0316 0.1357  399 TYR   A N   
2733 C  CA  . TYR   A 379 ? 0.8798 1.2045 0.9196 0.0375  -0.0208 0.1507  399 TYR   A CA  
2734 C  C   . TYR   A 379 ? 0.9357 1.2715 0.9408 0.0542  -0.0321 0.1442  399 TYR   A C   
2735 O  O   . TYR   A 379 ? 0.9384 1.2757 0.9173 0.0632  -0.0312 0.1591  399 TYR   A O   
2736 C  CB  . TYR   A 379 ? 0.8153 1.1501 0.8594 0.0304  -0.0030 0.1526  399 TYR   A CB  
2737 C  CG  . TYR   A 379 ? 0.9439 1.2925 0.9670 0.0335  0.0136  0.1712  399 TYR   A CG  
2738 C  CD1 . TYR   A 379 ? 0.9437 1.3109 0.9346 0.0489  0.0164  0.1673  399 TYR   A CD1 
2739 C  CD2 . TYR   A 379 ? 0.9943 1.3351 1.0286 0.0214  0.0274  0.1933  399 TYR   A CD2 
2740 C  CE1 . TYR   A 379 ? 1.0873 1.4687 1.0576 0.0527  0.0358  0.1871  399 TYR   A CE1 
2741 C  CE2 . TYR   A 379 ? 0.9543 1.3073 0.9726 0.0220  0.0452  0.2138  399 TYR   A CE2 
2742 C  CZ  . TYR   A 379 ? 0.8994 1.2747 0.8858 0.0380  0.0511  0.2118  399 TYR   A CZ  
2743 O  OH  . TYR   A 379 ? 0.9983 1.3875 0.9671 0.0397  0.0730  0.2350  399 TYR   A OH  
2744 N  N   . ALA   A 380 ? 0.9137 1.2535 0.9145 0.0599  -0.0440 0.1216  400 ALA   A N   
2745 C  CA  . ALA   A 380 ? 0.8825 1.2285 0.8450 0.0775  -0.0572 0.1109  400 ALA   A CA  
2746 C  C   . ALA   A 380 ? 0.9771 1.3172 0.9363 0.0835  -0.0814 0.1095  400 ALA   A C   
2747 O  O   . ALA   A 380 ? 1.1120 1.4552 1.0316 0.0999  -0.0925 0.1082  400 ALA   A O   
2748 C  CB  . ALA   A 380 ? 0.7567 1.1023 0.7160 0.0822  -0.0653 0.0851  400 ALA   A CB  
2749 N  N   . LEU   A 381 ? 0.9117 1.2449 0.9114 0.0722  -0.0902 0.1098  401 LEU   A N   
2750 C  CA  . LEU   A 381 ? 0.9082 1.2421 0.9150 0.0777  -0.1128 0.1106  401 LEU   A CA  
2751 C  C   . LEU   A 381 ? 0.9286 1.2611 0.9257 0.0827  -0.1053 0.1358  401 LEU   A C   
2752 O  O   . LEU   A 381 ? 1.0276 1.3632 1.0062 0.0960  -0.1233 0.1395  401 LEU   A O   
2753 C  CB  . LEU   A 381 ? 0.8898 1.2213 0.9486 0.0647  -0.1222 0.1023  401 LEU   A CB  
2754 C  CG  . LEU   A 381 ? 0.8748 1.2016 0.9471 0.0580  -0.1316 0.0793  401 LEU   A CG  
2755 C  CD1 . LEU   A 381 ? 0.8108 1.1346 0.9358 0.0432  -0.1315 0.0789  401 LEU   A CD1 
2756 C  CD2 . LEU   A 381 ? 0.9499 1.2781 0.9996 0.0690  -0.1604 0.0600  401 LEU   A CD2 
2757 N  N   . HIS   A 382 ? 0.9054 1.2307 0.9136 0.0730  -0.0812 0.1528  402 HIS   A N   
2758 C  CA  . HIS   A 382 ? 0.9620 1.2788 0.9597 0.0770  -0.0729 0.1778  402 HIS   A CA  
2759 C  C   . HIS   A 382 ? 1.0654 1.3848 1.0113 0.0906  -0.0681 0.1907  402 HIS   A C   
2760 O  O   . HIS   A 382 ? 1.0988 1.4088 1.0277 0.0980  -0.0666 0.2120  402 HIS   A O   
2761 C  CB  . HIS   A 382 ? 0.9446 1.2481 0.9641 0.0619  -0.0499 0.1902  402 HIS   A CB  
2762 C  CG  . HIS   A 382 ? 0.9212 1.2166 0.9827 0.0534  -0.0521 0.1841  402 HIS   A CG  
2763 N  ND1 . HIS   A 382 ? 0.8506 1.1280 0.9286 0.0437  -0.0368 0.1937  402 HIS   A ND1 
2764 C  CD2 . HIS   A 382 ? 0.8538 1.1564 0.9434 0.0536  -0.0667 0.1698  402 HIS   A CD2 
2765 C  CE1 . HIS   A 382 ? 0.8576 1.1312 0.9665 0.0411  -0.0402 0.1855  402 HIS   A CE1 
2766 N  NE2 . HIS   A 382 ? 0.8017 1.0923 0.9213 0.0460  -0.0567 0.1726  402 HIS   A NE2 
2767 N  N   . ARG   A 383 ? 1.1638 1.4940 1.0819 0.0958  -0.0643 0.1793  403 ARG   A N   
2768 C  CA  . ARG   A 383 ? 1.1073 1.4418 0.9709 0.1117  -0.0565 0.1911  403 ARG   A CA  
2769 C  C   . ARG   A 383 ? 1.2144 1.5554 1.0407 0.1306  -0.0796 0.1690  403 ARG   A C   
2770 O  O   . ARG   A 383 ? 1.3818 1.7288 1.1596 0.1453  -0.0702 0.1702  403 ARG   A O   
2771 C  CB  . ARG   A 383 ? 0.9987 1.3420 0.8585 0.1037  -0.0249 0.2011  403 ARG   A CB  
2772 C  CG  . ARG   A 383 ? 0.9879 1.3210 0.8779 0.0853  -0.0044 0.2245  403 ARG   A CG  
2773 C  CD  . ARG   A 383 ? 1.0750 1.4221 0.9788 0.0730  0.0216  0.2284  403 ARG   A CD  
2774 N  NE  . ARG   A 383 ? 1.1034 1.4378 1.0363 0.0539  0.0376  0.2494  403 ARG   A NE  
2775 C  CZ  . ARG   A 383 ? 1.0422 1.3758 0.9639 0.0493  0.0591  0.2770  403 ARG   A CZ  
2776 N  NH1 . ARG   A 383 ? 1.0995 1.4469 0.9787 0.0639  0.0713  0.2895  403 ARG   A NH1 
2777 N  NH2 . ARG   A 383 ? 1.0081 1.3247 0.9605 0.0297  0.0690  0.2928  403 ARG   A NH2 
2778 N  N   . ASP   A 384 ? 1.2027 1.5424 1.0513 0.1307  -0.1094 0.1487  404 ASP   A N   
2779 C  CA  . ASP   A 384 ? 1.3363 1.6774 1.1527 0.1471  -0.1378 0.1249  404 ASP   A CA  
2780 C  C   . ASP   A 384 ? 1.4605 1.7982 1.2327 0.1677  -0.1557 0.1360  404 ASP   A C   
2781 O  O   . ASP   A 384 ? 1.4180 1.7545 1.2159 0.1661  -0.1703 0.1457  404 ASP   A O   
2782 C  CB  . ASP   A 384 ? 1.2853 1.6260 1.1501 0.1358  -0.1639 0.1006  404 ASP   A CB  
2783 C  CG  . ASP   A 384 ? 1.4674 1.8050 1.3040 0.1497  -0.1977 0.0727  404 ASP   A CG  
2784 O  OD1 . ASP   A 384 ? 1.5251 1.8597 1.2989 0.1701  -0.1982 0.0683  404 ASP   A OD1 
2785 O  OD2 . ASP   A 384 ? 1.4733 1.8105 1.3507 0.1403  -0.2237 0.0551  404 ASP   A OD2 
2786 N  N   . PRO   A 385 ? 1.5316 1.8679 1.2357 0.1896  -0.1548 0.1357  405 PRO   A N   
2787 C  CA  . PRO   A 385 ? 1.6352 1.9652 1.2892 0.2123  -0.1749 0.1460  405 PRO   A CA  
2788 C  C   . PRO   A 385 ? 1.6410 1.9712 1.3104 0.2179  -0.2225 0.1229  405 PRO   A C   
2789 O  O   . PRO   A 385 ? 1.5826 1.9107 1.2382 0.2309  -0.2433 0.1341  405 PRO   A O   
2790 C  CB  . PRO   A 385 ? 1.4902 1.8184 1.0649 0.2356  -0.1624 0.1448  405 PRO   A CB  
2791 C  CG  . PRO   A 385 ? 1.6406 1.9786 1.2335 0.2220  -0.1244 0.1470  405 PRO   A CG  
2792 C  CD  . PRO   A 385 ? 1.4526 1.7933 1.1195 0.1973  -0.1327 0.1284  405 PRO   A CD  
2793 N  N   . LYS   A 386 ? 1.6416 1.9742 1.3426 0.2080  -0.2413 0.0915  406 LYS   A N   
2794 C  CA  . LYS   A 386 ? 1.7423 2.0771 1.4686 0.2090  -0.2876 0.0688  406 LYS   A CA  
2795 C  C   . LYS   A 386 ? 1.6466 1.9933 1.4427 0.1947  -0.2950 0.0828  406 LYS   A C   
2796 O  O   . LYS   A 386 ? 1.6640 2.0191 1.4845 0.1979  -0.3332 0.0712  406 LYS   A O   
2797 C  CB  . LYS   A 386 ? 1.8168 2.1472 1.5670 0.1977  -0.3019 0.0351  406 LYS   A CB  
2798 C  CG  . LYS   A 386 ? 1.9183 2.2363 1.6017 0.2143  -0.2925 0.0192  406 LYS   A CG  
2799 C  CD  . LYS   A 386 ? 2.1391 2.4444 1.8328 0.2105  -0.3211 -0.0188 406 LYS   A CD  
2800 C  CE  . LYS   A 386 ? 2.2359 2.5265 1.8535 0.2343  -0.3152 -0.0366 406 LYS   A CE  
2801 N  NZ  . LYS   A 386 ? 2.3068 2.5768 1.9235 0.2352  -0.3507 -0.0765 406 LYS   A NZ  
2802 N  N   . TYR   A 387 ? 1.5857 1.9339 1.4154 0.1802  -0.2602 0.1064  407 TYR   A N   
2803 C  CA  . TYR   A 387 ? 1.4892 1.8457 1.3744 0.1723  -0.2615 0.1228  407 TYR   A CA  
2804 C  C   . TYR   A 387 ? 1.4394 1.7867 1.2961 0.1833  -0.2422 0.1560  407 TYR   A C   
2805 O  O   . TYR   A 387 ? 1.4792 1.8308 1.3582 0.1901  -0.2561 0.1682  407 TYR   A O   
2806 C  CB  . TYR   A 387 ? 1.3562 1.7163 1.3081 0.1465  -0.2399 0.1212  407 TYR   A CB  
2807 C  CG  . TYR   A 387 ? 1.4186 1.7887 1.4216 0.1328  -0.2622 0.0953  407 TYR   A CG  
2808 C  CD1 . TYR   A 387 ? 1.3028 1.6905 1.3619 0.1295  -0.2867 0.0927  407 TYR   A CD1 
2809 C  CD2 . TYR   A 387 ? 1.5163 1.8784 1.5149 0.1231  -0.2579 0.0750  407 TYR   A CD2 
2810 C  CE1 . TYR   A 387 ? 1.4473 1.8446 1.5587 0.1140  -0.3053 0.0718  407 TYR   A CE1 
2811 C  CE2 . TYR   A 387 ? 1.4653 1.8311 1.5106 0.1090  -0.2776 0.0535  407 TYR   A CE2 
2812 C  CZ  . TYR   A 387 ? 1.4812 1.8648 1.5840 0.1029  -0.3007 0.0528  407 TYR   A CZ  
2813 O  OH  . TYR   A 387 ? 1.4337 1.8217 1.5885 0.0861  -0.3187 0.0341  407 TYR   A OH  
2814 N  N   . TRP   A 388 ? 1.4497 1.7847 1.2607 0.1852  -0.2105 0.1716  408 TRP   A N   
2815 C  CA  . TRP   A 388 ? 1.4573 1.7786 1.2478 0.1897  -0.1866 0.2056  408 TRP   A CA  
2816 C  C   . TRP   A 388 ? 1.5401 1.8520 1.2487 0.2135  -0.1862 0.2189  408 TRP   A C   
2817 O  O   . TRP   A 388 ? 1.5854 1.8984 1.2525 0.2173  -0.1722 0.2123  408 TRP   A O   
2818 C  CB  . TRP   A 388 ? 1.3243 1.6392 1.1381 0.1683  -0.1469 0.2172  408 TRP   A CB  
2819 C  CG  . TRP   A 388 ? 1.2747 1.5954 1.1578 0.1473  -0.1448 0.2039  408 TRP   A CG  
2820 C  CD1 . TRP   A 388 ? 1.1969 1.5262 1.1056 0.1334  -0.1428 0.1808  408 TRP   A CD1 
2821 C  CD2 . TRP   A 388 ? 1.2743 1.5904 1.2057 0.1403  -0.1434 0.2139  408 TRP   A CD2 
2822 N  NE1 . TRP   A 388 ? 1.0939 1.4241 1.0616 0.1176  -0.1393 0.1774  408 TRP   A NE1 
2823 C  CE2 . TRP   A 388 ? 1.1774 1.5008 1.1599 0.1222  -0.1388 0.1967  408 TRP   A CE2 
2824 C  CE3 . TRP   A 388 ? 1.1803 1.4846 1.1139 0.1500  -0.1449 0.2361  408 TRP   A CE3 
2825 C  CZ2 . TRP   A 388 ? 1.0036 1.3248 1.0365 0.1142  -0.1338 0.2008  408 TRP   A CZ2 
2826 C  CZ3 . TRP   A 388 ? 1.1597 1.4619 1.1463 0.1427  -0.1412 0.2383  408 TRP   A CZ3 
2827 C  CH2 . TRP   A 388 ? 1.1347 1.4461 1.1691 0.1252  -0.1348 0.2207  408 TRP   A CH2 
2828 N  N   . THR   A 389 ? 1.4294 1.7318 1.1132 0.2316  -0.2002 0.2386  409 THR   A N   
2829 C  CA  . THR   A 389 ? 1.6008 1.8892 1.2017 0.2552  -0.1949 0.2587  409 THR   A CA  
2830 C  C   . THR   A 389 ? 1.6249 1.8991 1.2114 0.2446  -0.1480 0.2906  409 THR   A C   
2831 O  O   . THR   A 389 ? 1.6493 1.9121 1.2766 0.2298  -0.1322 0.3096  409 THR   A O   
2832 C  CB  . THR   A 389 ? 1.6053 1.8850 1.1850 0.2786  -0.2250 0.2724  409 THR   A CB  
2833 O  OG1 . THR   A 389 ? 1.6469 1.9130 1.2633 0.2704  -0.2095 0.2995  409 THR   A OG1 
2834 C  CG2 . THR   A 389 ? 1.4839 1.7833 1.0991 0.2840  -0.2732 0.2413  409 THR   A CG2 
2835 N  N   . GLU   A 390 ? 1.5997 1.8744 1.1293 0.2524  -0.1261 0.2961  410 GLU   A N   
2836 C  CA  . GLU   A 390 ? 1.6486 1.9163 1.1693 0.2401  -0.0801 0.3258  410 GLU   A CA  
2837 C  C   . GLU   A 390 ? 1.6315 1.9045 1.2300 0.2073  -0.0606 0.3220  410 GLU   A C   
2838 O  O   . GLU   A 390 ? 1.6068 1.8628 1.2320 0.1935  -0.0442 0.3464  410 GLU   A O   
2839 C  CB  . GLU   A 390 ? 1.6779 1.9193 1.1608 0.2513  -0.0700 0.3667  410 GLU   A CB  
2840 C  CG  . GLU   A 390 ? 1.7502 1.9831 1.1459 0.2866  -0.0876 0.3740  410 GLU   A CG  
2841 C  CD  . GLU   A 390 ? 1.9144 2.1167 1.2683 0.2986  -0.0755 0.4183  410 GLU   A CD  
2842 O  OE1 . GLU   A 390 ? 1.7407 1.9263 1.1250 0.2980  -0.0927 0.4282  410 GLU   A OE1 
2843 O  OE2 . GLU   A 390 ? 2.0769 2.2711 1.3669 0.3096  -0.0472 0.4443  410 GLU   A OE2 
2844 N  N   . PRO   A 391 ? 1.7981 2.0907 1.4303 0.1956  -0.0635 0.2910  411 PRO   A N   
2845 C  CA  . PRO   A 391 ? 1.6714 1.9667 1.3764 0.1679  -0.0544 0.2831  411 PRO   A CA  
2846 C  C   . PRO   A 391 ? 1.5941 1.8866 1.3160 0.1480  -0.0160 0.3047  411 PRO   A C   
2847 O  O   . PRO   A 391 ? 1.5624 1.8465 1.3361 0.1275  -0.0098 0.3066  411 PRO   A O   
2848 C  CB  . PRO   A 391 ? 1.6395 1.9535 1.3630 0.1651  -0.0691 0.2457  411 PRO   A CB  
2849 C  CG  . PRO   A 391 ? 1.7418 2.0637 1.4007 0.1864  -0.0687 0.2390  411 PRO   A CG  
2850 C  CD  . PRO   A 391 ? 1.8497 2.1581 1.4508 0.2090  -0.0766 0.2615  411 PRO   A CD  
2851 N  N   . GLU   A 392 ? 1.5791 1.8792 1.2608 0.1534  0.0098  0.3206  412 GLU   A N   
2852 C  CA  . GLU   A 392 ? 1.5131 1.8149 1.2197 0.1320  0.0455  0.3426  412 GLU   A CA  
2853 C  C   . GLU   A 392 ? 1.4590 1.7308 1.1687 0.1238  0.0560  0.3778  412 GLU   A C   
2854 O  O   . GLU   A 392 ? 1.2297 1.4975 0.9701 0.1016  0.0812  0.3956  412 GLU   A O   
2855 C  CB  . GLU   A 392 ? 1.5802 1.9043 1.2481 0.1407  0.0733  0.3514  412 GLU   A CB  
2856 C  CG  . GLU   A 392 ? 1.5921 1.9460 1.2853 0.1352  0.0794  0.3234  412 GLU   A CG  
2857 C  CD  . GLU   A 392 ? 1.8708 2.2506 1.5383 0.1416  0.1145  0.3374  412 GLU   A CD  
2858 O  OE1 . GLU   A 392 ? 1.8657 2.2397 1.4927 0.1497  0.1352  0.3701  412 GLU   A OE1 
2859 O  OE2 . GLU   A 392 ? 1.9625 2.3687 1.6505 0.1396  0.1225  0.3172  412 GLU   A OE2 
2860 N  N   . LYS   A 393 ? 1.3796 1.6292 1.0608 0.1412  0.0356  0.3877  413 LYS   A N   
2861 C  CA  . LYS   A 393 ? 1.4417 1.6573 1.1159 0.1384  0.0448  0.4231  413 LYS   A CA  
2862 C  C   . LYS   A 393 ? 1.3493 1.5434 1.0770 0.1257  0.0303  0.4167  413 LYS   A C   
2863 O  O   . LYS   A 393 ? 1.2582 1.4610 1.0094 0.1316  0.0040  0.3899  413 LYS   A O   
2864 C  CB  . LYS   A 393 ? 1.5047 1.7054 1.1115 0.1688  0.0311  0.4407  413 LYS   A CB  
2865 C  CG  . LYS   A 393 ? 1.6457 1.8630 1.1871 0.1865  0.0467  0.4486  413 LYS   A CG  
2866 C  CD  . LYS   A 393 ? 1.7074 1.9064 1.1748 0.2195  0.0295  0.4649  413 LYS   A CD  
2867 C  CE  . LYS   A 393 ? 1.7158 1.8829 1.1492 0.2198  0.0566  0.5140  413 LYS   A CE  
2868 N  NZ  . LYS   A 393 ? 1.8725 2.0193 1.2265 0.2552  0.0387  0.5311  413 LYS   A NZ  
2869 N  N   . PHE   A 394 ? 1.3876 1.5529 1.1347 0.1083  0.0486  0.4417  414 PHE   A N   
2870 C  CA  . PHE   A 394 ? 1.2584 1.3946 1.0464 0.0997  0.0379  0.4393  414 PHE   A CA  
2871 C  C   . PHE   A 394 ? 1.3496 1.4601 1.1078 0.1249  0.0180  0.4540  414 PHE   A C   
2872 O  O   . PHE   A 394 ? 1.4117 1.4914 1.1365 0.1305  0.0283  0.4876  414 PHE   A O   
2873 C  CB  . PHE   A 394 ? 1.2763 1.3863 1.0916 0.0725  0.0620  0.4591  414 PHE   A CB  
2874 C  CG  . PHE   A 394 ? 1.2447 1.3159 1.0923 0.0664  0.0522  0.4581  414 PHE   A CG  
2875 C  CD1 . PHE   A 394 ? 1.1793 1.2567 1.0725 0.0552  0.0438  0.4289  414 PHE   A CD1 
2876 C  CD2 . PHE   A 394 ? 1.2336 1.2587 1.0618 0.0737  0.0524  0.4871  414 PHE   A CD2 
2877 C  CE1 . PHE   A 394 ? 1.1757 1.2158 1.0927 0.0530  0.0364  0.4269  414 PHE   A CE1 
2878 C  CE2 . PHE   A 394 ? 1.1705 1.1565 1.0251 0.0712  0.0436  0.4845  414 PHE   A CE2 
2879 C  CZ  . PHE   A 394 ? 1.2393 1.2337 1.1374 0.0615  0.0361  0.4536  414 PHE   A CZ  
2880 N  N   . LEU   A 395 ? 1.1944 1.3185 0.9667 0.1405  -0.0108 0.4301  415 LEU   A N   
2881 C  CA  . LEU   A 395 ? 1.3215 1.4305 1.0721 0.1676  -0.0348 0.4397  415 LEU   A CA  
2882 C  C   . LEU   A 395 ? 1.2578 1.3650 1.0615 0.1688  -0.0520 0.4214  415 LEU   A C   
2883 O  O   . LEU   A 395 ? 1.2961 1.4354 1.1249 0.1748  -0.0725 0.3941  415 LEU   A O   
2884 C  CB  . LEU   A 395 ? 1.2943 1.4307 1.0021 0.1916  -0.0564 0.4300  415 LEU   A CB  
2885 C  CG  . LEU   A 395 ? 1.5097 1.6425 1.1499 0.2000  -0.0396 0.4531  415 LEU   A CG  
2886 C  CD1 . LEU   A 395 ? 1.5104 1.6670 1.1042 0.2265  -0.0659 0.4375  415 LEU   A CD1 
2887 C  CD2 . LEU   A 395 ? 1.3378 1.4266 0.9446 0.2071  -0.0271 0.4951  415 LEU   A CD2 
2888 N  N   . PRO   A 396 ? 1.2477 1.3165 1.0700 0.1634  -0.0433 0.4360  416 PRO   A N   
2889 C  CA  . PRO   A 396 ? 1.2312 1.2970 1.1010 0.1678  -0.0556 0.4195  416 PRO   A CA  
2890 C  C   . PRO   A 396 ? 1.1821 1.2686 1.0570 0.1963  -0.0854 0.4121  416 PRO   A C   
2891 O  O   . PRO   A 396 ? 1.2553 1.3590 1.1770 0.1995  -0.0956 0.3924  416 PRO   A O   
2892 C  CB  . PRO   A 396 ? 1.1483 1.1590 1.0177 0.1638  -0.0422 0.4424  416 PRO   A CB  
2893 C  CG  . PRO   A 396 ? 1.2060 1.2006 1.0530 0.1408  -0.0175 0.4607  416 PRO   A CG  
2894 C  CD  . PRO   A 396 ? 1.1882 1.2144 0.9937 0.1492  -0.0188 0.4660  416 PRO   A CD  
2895 N  N   . GLU   A 397 ? 1.2563 1.3432 1.0848 0.2177  -0.0998 0.4279  417 GLU   A N   
2896 C  CA  . GLU   A 397 ? 1.3782 1.4841 1.2124 0.2463  -0.1324 0.4225  417 GLU   A CA  
2897 C  C   . GLU   A 397 ? 1.3377 1.4963 1.2043 0.2449  -0.1533 0.3892  417 GLU   A C   
2898 O  O   . GLU   A 397 ? 1.3586 1.5403 1.2457 0.2649  -0.1824 0.3810  417 GLU   A O   
2899 C  CB  . GLU   A 397 ? 1.4986 1.5877 1.2669 0.2710  -0.1445 0.4483  417 GLU   A CB  
2900 C  CG  . GLU   A 397 ? 1.5699 1.6028 1.3105 0.2787  -0.1308 0.4843  417 GLU   A CG  
2901 C  CD  . GLU   A 397 ? 1.7114 1.7287 1.4920 0.2952  -0.1433 0.4849  417 GLU   A CD  
2902 O  OE1 . GLU   A 397 ? 1.6970 1.7506 1.5101 0.3133  -0.1708 0.4667  417 GLU   A OE1 
2903 O  OE2 . GLU   A 397 ? 1.8043 1.7730 1.5858 0.2903  -0.1257 0.5033  417 GLU   A OE2 
2904 N  N   . ARG   A 398 ? 1.2851 1.4629 1.1593 0.2220  -0.1406 0.3705  418 ARG   A N   
2905 C  CA  . ARG   A 398 ? 1.0477 1.2683 0.9609 0.2172  -0.1587 0.3387  418 ARG   A CA  
2906 C  C   . ARG   A 398 ? 1.1359 1.3681 1.1172 0.2149  -0.1616 0.3270  418 ARG   A C   
2907 O  O   . ARG   A 398 ? 1.0503 1.3181 1.0705 0.2199  -0.1843 0.3083  418 ARG   A O   
2908 C  CB  . ARG   A 398 ? 1.2556 1.4876 1.1665 0.1934  -0.1415 0.3221  418 ARG   A CB  
2909 C  CG  . ARG   A 398 ? 1.3203 1.5406 1.1697 0.1923  -0.1265 0.3355  418 ARG   A CG  
2910 C  CD  . ARG   A 398 ? 1.2650 1.4958 1.1261 0.1681  -0.1050 0.3204  418 ARG   A CD  
2911 N  NE  . ARG   A 398 ? 1.3381 1.5599 1.1502 0.1649  -0.0828 0.3366  418 ARG   A NE  
2912 C  CZ  . ARG   A 398 ? 1.3776 1.6135 1.1419 0.1771  -0.0885 0.3321  418 ARG   A CZ  
2913 N  NH1 . ARG   A 398 ? 1.3945 1.6498 1.1505 0.1926  -0.1199 0.3105  418 ARG   A NH1 
2914 N  NH2 . ARG   A 398 ? 1.4761 1.7066 1.2008 0.1740  -0.0622 0.3493  418 ARG   A NH2 
2915 N  N   . PHE   A 399 ? 1.1077 1.3100 1.1044 0.2075  -0.1386 0.3376  419 PHE   A N   
2916 C  CA  . PHE   A 399 ? 1.0850 1.2935 1.1388 0.2078  -0.1354 0.3280  419 PHE   A CA  
2917 C  C   . PHE   A 399 ? 1.1705 1.3636 1.2317 0.2343  -0.1454 0.3444  419 PHE   A C   
2918 O  O   . PHE   A 399 ? 1.2066 1.3909 1.3039 0.2379  -0.1353 0.3425  419 PHE   A O   
2919 C  CB  . PHE   A 399 ? 1.0270 1.2101 1.0907 0.1854  -0.1060 0.3247  419 PHE   A CB  
2920 C  CG  . PHE   A 399 ? 1.0634 1.2646 1.1287 0.1614  -0.0970 0.3067  419 PHE   A CG  
2921 C  CD1 . PHE   A 399 ? 0.9843 1.2165 1.0925 0.1530  -0.1001 0.2839  419 PHE   A CD1 
2922 C  CD2 . PHE   A 399 ? 1.1256 1.3135 1.1508 0.1483  -0.0846 0.3141  419 PHE   A CD2 
2923 C  CE1 . PHE   A 399 ? 0.9953 1.2399 1.1028 0.1332  -0.0930 0.2679  419 PHE   A CE1 
2924 C  CE2 . PHE   A 399 ? 1.0717 1.2775 1.0997 0.1296  -0.0769 0.2972  419 PHE   A CE2 
2925 C  CZ  . PHE   A 399 ? 0.9817 1.2136 1.0490 0.1227  -0.0823 0.2737  419 PHE   A CZ  
2926 N  N   . SER   A 400 ? 1.3298 1.5177 1.3540 0.2556  -0.1648 0.3607  420 SER   A N   
2927 C  CA  . SER   A 400 ? 1.4383 1.6176 1.4730 0.2851  -0.1797 0.3747  420 SER   A CA  
2928 C  C   . SER   A 400 ? 1.5357 1.7655 1.6390 0.2947  -0.1978 0.3554  420 SER   A C   
2929 O  O   . SER   A 400 ? 1.4733 1.7462 1.6029 0.2830  -0.2101 0.3346  420 SER   A O   
2930 C  CB  . SER   A 400 ? 1.5046 1.6727 1.4831 0.3077  -0.2012 0.3947  420 SER   A CB  
2931 O  OG  . SER   A 400 ? 1.6255 1.8387 1.6047 0.3134  -0.2307 0.3787  420 SER   A OG  
2932 N  N   . LYS   A 401 ? 1.6560 1.8799 1.7908 0.3163  -0.1986 0.3631  421 LYS   A N   
2933 C  CA  . LYS   A 401 ? 1.6355 1.9108 1.8431 0.3280  -0.2123 0.3488  421 LYS   A CA  
2934 C  C   . LYS   A 401 ? 1.6876 2.0136 1.9101 0.3358  -0.2502 0.3393  421 LYS   A C   
2935 O  O   . LYS   A 401 ? 1.6844 2.0628 1.9736 0.3325  -0.2615 0.3221  421 LYS   A O   
2936 C  CB  . LYS   A 401 ? 1.6943 1.9524 1.9211 0.3586  -0.2107 0.3630  421 LYS   A CB  
2937 C  CG  . LYS   A 401 ? 1.7523 2.0556 2.0598 0.3675  -0.2070 0.3499  421 LYS   A CG  
2938 C  CD  . LYS   A 401 ? 1.8544 2.1252 2.1682 0.3965  -0.1950 0.3633  421 LYS   A CD  
2939 C  CE  . LYS   A 401 ? 1.8877 2.1276 2.1575 0.4260  -0.2176 0.3861  421 LYS   A CE  
2940 N  NZ  . LYS   A 401 ? 1.9582 2.1431 2.2136 0.4503  -0.2023 0.4009  421 LYS   A NZ  
2941 N  N   . LYS   A 402 ? 1.7997 2.1098 1.9606 0.3458  -0.2702 0.3502  422 LYS   A N   
2942 C  CA  . LYS   A 402 ? 1.7621 2.1136 1.9247 0.3525  -0.3092 0.3379  422 LYS   A CA  
2943 C  C   . LYS   A 402 ? 1.7896 2.1594 1.9500 0.3222  -0.3065 0.3151  422 LYS   A C   
2944 O  O   . LYS   A 402 ? 1.7985 2.2150 2.0088 0.3151  -0.3288 0.2937  422 LYS   A O   
2945 C  CB  . LYS   A 402 ? 1.7777 2.1006 1.8642 0.3772  -0.3303 0.3581  422 LYS   A CB  
2946 C  CG  . LYS   A 402 ? 1.8791 2.2264 1.9334 0.3791  -0.3648 0.3443  422 LYS   A CG  
2947 C  CD  . LYS   A 402 ? 1.9627 2.2678 1.9196 0.3978  -0.3706 0.3672  422 LYS   A CD  
2948 C  CE  . LYS   A 402 ? 2.0221 2.3462 1.9355 0.4017  -0.4030 0.3511  422 LYS   A CE  
2949 N  NZ  . LYS   A 402 ? 2.1076 2.3889 1.9176 0.4195  -0.4016 0.3748  422 LYS   A NZ  
2950 N  N   . ASN   A 403 ? 1.7147 2.0479 1.8208 0.3039  -0.2798 0.3196  423 ASN   A N   
2951 C  CA  . ASN   A 403 ? 1.5532 1.8987 1.6456 0.2802  -0.2783 0.2995  423 ASN   A CA  
2952 C  C   . ASN   A 403 ? 1.5131 1.8696 1.6560 0.2520  -0.2528 0.2831  423 ASN   A C   
2953 O  O   . ASN   A 403 ? 1.4845 1.8571 1.6304 0.2337  -0.2559 0.2632  423 ASN   A O   
2954 C  CB  . ASN   A 403 ? 1.4367 1.7438 1.4461 0.2768  -0.2625 0.3130  423 ASN   A CB  
2955 C  CG  . ASN   A 403 ? 1.7451 2.0400 1.6922 0.3048  -0.2872 0.3292  423 ASN   A CG  
2956 O  OD1 . ASN   A 403 ? 1.6883 2.0112 1.6462 0.3229  -0.3256 0.3198  423 ASN   A OD1 
2957 N  ND2 . ASN   A 403 ? 1.6551 1.9077 1.5367 0.3083  -0.2659 0.3545  423 ASN   A ND2 
2958 N  N   . LYS   A 404 ? 1.4670 1.8118 1.6449 0.2503  -0.2284 0.2904  424 LYS   A N   
2959 C  CA  . LYS   A 404 ? 1.4759 1.8296 1.6977 0.2271  -0.2046 0.2760  424 LYS   A CA  
2960 C  C   . LYS   A 404 ? 1.4720 1.8763 1.7580 0.2196  -0.2226 0.2554  424 LYS   A C   
2961 O  O   . LYS   A 404 ? 1.3857 1.7982 1.7005 0.1980  -0.2058 0.2421  424 LYS   A O   
2962 C  CB  . LYS   A 404 ? 1.4994 1.8308 1.7435 0.2332  -0.1791 0.2869  424 LYS   A CB  
2963 C  CG  . LYS   A 404 ? 1.4894 1.8464 1.7834 0.2585  -0.1932 0.2920  424 LYS   A CG  
2964 C  CD  . LYS   A 404 ? 1.5420 1.8946 1.8781 0.2599  -0.1658 0.2913  424 LYS   A CD  
2965 C  CE  . LYS   A 404 ? 1.6055 1.8971 1.8965 0.2646  -0.1422 0.3058  424 LYS   A CE  
2966 N  NZ  . LYS   A 404 ? 1.6350 1.9197 1.9615 0.2739  -0.1195 0.3041  424 LYS   A NZ  
2967 N  N   . ASP   A 405 ? 1.4511 1.8886 1.7613 0.2363  -0.2574 0.2531  425 ASP   A N   
2968 C  CA  . ASP   A 405 ? 1.4656 1.9532 1.8449 0.2274  -0.2781 0.2346  425 ASP   A CA  
2969 C  C   . ASP   A 405 ? 1.4161 1.9101 1.7740 0.2098  -0.2969 0.2143  425 ASP   A C   
2970 O  O   . ASP   A 405 ? 1.2277 1.7517 1.6402 0.1922  -0.3045 0.1973  425 ASP   A O   
2971 C  CB  . ASP   A 405 ? 1.5063 2.0299 1.9260 0.2525  -0.3120 0.2390  425 ASP   A CB  
2972 C  CG  . ASP   A 405 ? 1.6112 2.1188 2.0317 0.2783  -0.2983 0.2610  425 ASP   A CG  
2973 O  OD1 . ASP   A 405 ? 1.7020 2.1849 2.1247 0.2730  -0.2611 0.2679  425 ASP   A OD1 
2974 O  OD2 . ASP   A 405 ? 1.5991 2.1159 2.0153 0.3054  -0.3265 0.2704  425 ASP   A OD2 
2975 N  N   . ASN   A 406 ? 1.5791 2.0440 1.8588 0.2147  -0.3034 0.2163  426 ASN   A N   
2976 C  CA  . ASN   A 406 ? 1.5298 1.9977 1.7811 0.2037  -0.3228 0.1958  426 ASN   A CA  
2977 C  C   . ASN   A 406 ? 1.5242 1.9732 1.7616 0.1788  -0.2926 0.1865  426 ASN   A C   
2978 O  O   . ASN   A 406 ? 1.5869 2.0380 1.8089 0.1685  -0.3062 0.1668  426 ASN   A O   
2979 C  CB  . ASN   A 406 ? 1.5697 2.0169 1.7384 0.2243  -0.3421 0.2022  426 ASN   A CB  
2980 C  CG  . ASN   A 406 ? 1.7363 2.1848 1.8978 0.2533  -0.3598 0.2218  426 ASN   A CG  
2981 O  OD1 . ASN   A 406 ? 1.8029 2.2183 1.9020 0.2683  -0.3477 0.2433  426 ASN   A OD1 
2982 N  ND2 . ASN   A 406 ? 1.7472 2.2347 1.9752 0.2614  -0.3885 0.2156  426 ASN   A ND2 
2983 N  N   . ILE   A 407 ? 1.3431 1.7720 1.5841 0.1705  -0.2546 0.1988  427 ILE   A N   
2984 C  CA  . ILE   A 407 ? 1.2194 1.6288 1.4426 0.1496  -0.2271 0.1918  427 ILE   A CA  
2985 C  C   . ILE   A 407 ? 1.1874 1.6172 1.4737 0.1301  -0.2225 0.1763  427 ILE   A C   
2986 O  O   . ILE   A 407 ? 1.1447 1.5916 1.4876 0.1303  -0.2155 0.1813  427 ILE   A O   
2987 C  CB  . ILE   A 407 ? 1.2479 1.6241 1.4449 0.1491  -0.1923 0.2109  427 ILE   A CB  
2988 C  CG1 . ILE   A 407 ? 1.1713 1.5239 1.3020 0.1644  -0.1941 0.2282  427 ILE   A CG1 
2989 C  CG2 . ILE   A 407 ? 1.0433 1.4053 1.2357 0.1273  -0.1661 0.2024  427 ILE   A CG2 
2990 C  CD1 . ILE   A 407 ? 1.1426 1.4600 1.2513 0.1627  -0.1638 0.2487  427 ILE   A CD1 
2991 N  N   . ASP   A 408 ? 1.1453 1.5722 1.4207 0.1146  -0.2249 0.1585  428 ASP   A N   
2992 C  CA  . ASP   A 408 ? 0.8917 1.3321 1.2210 0.0949  -0.2206 0.1451  428 ASP   A CA  
2993 C  C   . ASP   A 408 ? 0.9880 1.4078 1.3181 0.0835  -0.1820 0.1521  428 ASP   A C   
2994 O  O   . ASP   A 408 ? 0.9211 1.3157 1.2029 0.0803  -0.1664 0.1528  428 ASP   A O   
2995 C  CB  . ASP   A 408 ? 0.8560 1.2948 1.1689 0.0850  -0.2413 0.1226  428 ASP   A CB  
2996 C  CG  . ASP   A 408 ? 0.9130 1.3668 1.2881 0.0650  -0.2457 0.1095  428 ASP   A CG  
2997 O  OD1 . ASP   A 408 ? 0.8859 1.3356 1.2896 0.0533  -0.2168 0.1160  428 ASP   A OD1 
2998 O  OD2 . ASP   A 408 ? 0.9132 1.3802 1.3065 0.0611  -0.2788 0.0927  428 ASP   A OD2 
2999 N  N   . PRO   A 409 ? 0.9951 1.4262 1.3782 0.0784  -0.1659 0.1574  429 PRO   A N   
3000 C  CA  . PRO   A 409 ? 0.8488 1.2567 1.2255 0.0704  -0.1313 0.1629  429 PRO   A CA  
3001 C  C   . PRO   A 409 ? 0.8232 1.2184 1.1900 0.0522  -0.1234 0.1496  429 PRO   A C   
3002 O  O   . PRO   A 409 ? 0.8798 1.2549 1.2377 0.0461  -0.0979 0.1525  429 PRO   A O   
3003 C  CB  . PRO   A 409 ? 0.8522 1.2799 1.2883 0.0735  -0.1189 0.1709  429 PRO   A CB  
3004 C  CG  . PRO   A 409 ? 0.8737 1.3401 1.3625 0.0708  -0.1463 0.1637  429 PRO   A CG  
3005 C  CD  . PRO   A 409 ? 0.7971 1.2646 1.2495 0.0804  -0.1785 0.1584  429 PRO   A CD  
3006 N  N   . TYR   A 410 ? 0.7091 1.1125 1.0755 0.0451  -0.1464 0.1341  430 TYR   A N   
3007 C  CA  . TYR   A 410 ? 0.8608 1.2476 1.2100 0.0314  -0.1419 0.1207  430 TYR   A CA  
3008 C  C   . TYR   A 410 ? 0.8613 1.2335 1.1502 0.0373  -0.1503 0.1130  430 TYR   A C   
3009 O  O   . TYR   A 410 ? 0.8663 1.2252 1.1365 0.0299  -0.1483 0.1006  430 TYR   A O   
3010 C  CB  . TYR   A 410 ? 0.9121 1.3134 1.3078 0.0180  -0.1593 0.1078  430 TYR   A CB  
3011 C  CG  . TYR   A 410 ? 0.8177 1.2380 1.2771 0.0118  -0.1457 0.1185  430 TYR   A CG  
3012 C  CD1 . TYR   A 410 ? 0.7664 1.1720 1.2289 0.0073  -0.1127 0.1278  430 TYR   A CD1 
3013 C  CD2 . TYR   A 410 ? 0.7782 1.2326 1.2941 0.0121  -0.1655 0.1196  430 TYR   A CD2 
3014 C  CE1 . TYR   A 410 ? 0.9397 1.3630 1.4556 0.0045  -0.0960 0.1389  430 TYR   A CE1 
3015 C  CE2 . TYR   A 410 ? 0.7446 1.2219 1.3231 0.0077  -0.1490 0.1312  430 TYR   A CE2 
3016 C  CZ  . TYR   A 410 ? 0.8148 1.2757 1.3908 0.0046  -0.1124 0.1414  430 TYR   A CZ  
3017 O  OH  . TYR   A 410 ? 0.8952 1.3793 1.5292 0.0029  -0.0923 0.1540  430 TYR   A OH  
3018 N  N   . ILE   A 411 ? 0.9026 1.2768 1.1600 0.0523  -0.1581 0.1213  431 ILE   A N   
3019 C  CA  . ILE   A 411 ? 0.9096 1.2700 1.1069 0.0596  -0.1552 0.1212  431 ILE   A CA  
3020 C  C   . ILE   A 411 ? 0.8818 1.2263 1.0581 0.0613  -0.1278 0.1397  431 ILE   A C   
3021 O  O   . ILE   A 411 ? 0.8888 1.2210 1.0348 0.0576  -0.1127 0.1395  431 ILE   A O   
3022 C  CB  . ILE   A 411 ? 0.9749 1.3446 1.1430 0.0757  -0.1829 0.1188  431 ILE   A CB  
3023 C  CG1 . ILE   A 411 ? 1.0287 1.4105 1.2180 0.0724  -0.2147 0.0967  431 ILE   A CG1 
3024 C  CG2 . ILE   A 411 ? 0.8763 1.2331 0.9794 0.0852  -0.1747 0.1220  431 ILE   A CG2 
3025 C  CD1 . ILE   A 411 ? 1.0740 1.4432 1.2583 0.0603  -0.2119 0.0779  431 ILE   A CD1 
3026 N  N   . TYR   A 412 ? 0.8630 1.2077 1.0589 0.0670  -0.1221 0.1552  432 TYR   A N   
3027 C  CA  . TYR   A 412 ? 0.8062 1.1300 0.9879 0.0675  -0.0986 0.1717  432 TYR   A CA  
3028 C  C   . TYR   A 412 ? 0.7979 1.1140 1.0129 0.0577  -0.0807 0.1700  432 TYR   A C   
3029 O  O   . TYR   A 412 ? 0.7892 1.1158 1.0425 0.0612  -0.0817 0.1720  432 TYR   A O   
3030 C  CB  . TYR   A 412 ? 0.7921 1.1133 0.9670 0.0833  -0.1043 0.1893  432 TYR   A CB  
3031 C  CG  . TYR   A 412 ? 0.7952 1.0882 0.9532 0.0834  -0.0827 0.2063  432 TYR   A CG  
3032 C  CD1 . TYR   A 412 ? 0.8103 1.0869 0.9304 0.0773  -0.0703 0.2129  432 TYR   A CD1 
3033 C  CD2 . TYR   A 412 ? 0.7605 1.0428 0.9424 0.0897  -0.0749 0.2152  432 TYR   A CD2 
3034 C  CE1 . TYR   A 412 ? 0.8087 1.0575 0.9182 0.0742  -0.0532 0.2280  432 TYR   A CE1 
3035 C  CE2 . TYR   A 412 ? 0.7083 0.9581 0.8728 0.0895  -0.0582 0.2284  432 TYR   A CE2 
3036 C  CZ  . TYR   A 412 ? 0.7977 1.0300 0.9274 0.0801  -0.0487 0.2347  432 TYR   A CZ  
3037 O  OH  . TYR   A 412 ? 0.8207 1.0190 0.9378 0.0766  -0.0345 0.2476  432 TYR   A OH  
3038 N  N   . THR   A 413 ? 0.8588 1.1584 1.0588 0.0471  -0.0641 0.1664  433 THR   A N   
3039 C  CA  . THR   A 413 ? 0.8477 1.1359 1.0680 0.0392  -0.0480 0.1632  433 THR   A CA  
3040 C  C   . THR   A 413 ? 0.8563 1.1190 1.0515 0.0339  -0.0315 0.1676  433 THR   A C   
3041 O  O   . THR   A 413 ? 0.8705 1.1273 1.0579 0.0246  -0.0257 0.1586  433 THR   A O   
3042 C  CB  . THR   A 413 ? 0.9210 1.2179 1.1568 0.0294  -0.0521 0.1478  433 THR   A CB  
3043 O  OG1 . THR   A 413 ? 0.8651 1.1622 1.0723 0.0260  -0.0585 0.1386  433 THR   A OG1 
3044 C  CG2 . THR   A 413 ? 0.8258 1.1462 1.0991 0.0306  -0.0679 0.1436  433 THR   A CG2 
3045 N  N   . PRO   A 414 ? 0.8915 1.1373 1.0752 0.0396  -0.0255 0.1814  434 PRO   A N   
3046 C  CA  . PRO   A 414 ? 0.8530 1.0723 1.0189 0.0320  -0.0125 0.1847  434 PRO   A CA  
3047 C  C   . PRO   A 414 ? 0.7868 0.9892 0.9621 0.0283  -0.0019 0.1766  434 PRO   A C   
3048 O  O   . PRO   A 414 ? 0.7698 0.9560 0.9323 0.0193  0.0039  0.1724  434 PRO   A O   
3049 C  CB  . PRO   A 414 ? 0.8351 1.0357 0.9902 0.0399  -0.0110 0.2017  434 PRO   A CB  
3050 C  CG  . PRO   A 414 ? 0.7529 0.9670 0.9279 0.0549  -0.0192 0.2051  434 PRO   A CG  
3051 C  CD  . PRO   A 414 ? 0.8777 1.1250 1.0663 0.0536  -0.0320 0.1941  434 PRO   A CD  
3052 N  N   . PHE   A 415 ? 0.8303 1.0378 1.0280 0.0357  0.0007  0.1746  435 PHE   A N   
3053 C  CA  . PHE   A 415 ? 0.8374 1.0276 1.0383 0.0358  0.0134  0.1688  435 PHE   A CA  
3054 C  C   . PHE   A 415 ? 0.6575 0.8660 0.8786 0.0319  0.0145  0.1607  435 PHE   A C   
3055 O  O   . PHE   A 415 ? 0.7468 0.9465 0.9751 0.0356  0.0272  0.1597  435 PHE   A O   
3056 C  CB  . PHE   A 415 ? 0.7654 0.9399 0.9726 0.0503  0.0224  0.1762  435 PHE   A CB  
3057 C  CG  . PHE   A 415 ? 0.7766 0.9228 0.9626 0.0541  0.0216  0.1844  435 PHE   A CG  
3058 C  CD1 . PHE   A 415 ? 0.7843 0.9381 0.9728 0.0612  0.0130  0.1962  435 PHE   A CD1 
3059 C  CD2 . PHE   A 415 ? 0.8371 0.9463 0.9998 0.0503  0.0274  0.1804  435 PHE   A CD2 
3060 C  CE1 . PHE   A 415 ? 0.8382 0.9610 1.0067 0.0637  0.0130  0.2063  435 PHE   A CE1 
3061 C  CE2 . PHE   A 415 ? 0.9586 1.0375 1.1051 0.0511  0.0253  0.1882  435 PHE   A CE2 
3062 C  CZ  . PHE   A 415 ? 0.8667 0.9513 1.0163 0.0574  0.0194  0.2023  435 PHE   A CZ  
3063 N  N   . GLY   A 416 ? 0.7254 0.9562 0.9532 0.0251  0.0021  0.1552  436 GLY   A N   
3064 C  CA  . GLY   A 416 ? 0.6995 0.9452 0.9507 0.0200  0.0002  0.1485  436 GLY   A CA  
3065 C  C   . GLY   A 416 ? 0.8224 1.0880 1.1129 0.0264  0.0016  0.1551  436 GLY   A C   
3066 O  O   . GLY   A 416 ? 0.7730 1.0454 1.0720 0.0369  -0.0002 0.1636  436 GLY   A O   
3067 N  N   . SER   A 417 ? 0.7913 1.0666 1.1086 0.0198  0.0053  0.1523  437 SER   A N   
3068 C  CA  . SER   A 417 ? 0.8384 1.1396 1.2039 0.0232  0.0080  0.1593  437 SER   A CA  
3069 C  C   . SER   A 417 ? 0.8384 1.1375 1.2244 0.0153  0.0240  0.1606  437 SER   A C   
3070 O  O   . SER   A 417 ? 0.8271 1.1061 1.1903 0.0067  0.0262  0.1542  437 SER   A O   
3071 C  CB  . SER   A 417 ? 0.9394 1.2711 1.3328 0.0202  -0.0178 0.1557  437 SER   A CB  
3072 O  OG  . SER   A 417 ? 1.0773 1.4395 1.5243 0.0244  -0.0176 0.1633  437 SER   A OG  
3073 N  N   . GLY   A 418 ? 0.7545 1.0753 1.1845 0.0196  0.0365  0.1706  438 GLY   A N   
3074 C  CA  . GLY   A 418 ? 0.7415 1.0646 1.1974 0.0118  0.0548  0.1762  438 GLY   A CA  
3075 C  C   . GLY   A 418 ? 0.6888 0.9854 1.1155 0.0231  0.0851  0.1833  438 GLY   A C   
3076 O  O   . GLY   A 418 ? 0.6367 0.9148 1.0298 0.0378  0.0912  0.1830  438 GLY   A O   
3077 N  N   . PRO   A 419 ? 0.5869 0.8778 1.0233 0.0167  0.1043  0.1898  439 PRO   A N   
3078 C  CA  . PRO   A 419 ? 0.7043 0.9689 1.1079 0.0302  0.1346  0.1971  439 PRO   A CA  
3079 C  C   . PRO   A 419 ? 0.8210 1.0416 1.1551 0.0363  0.1308  0.1866  439 PRO   A C   
3080 O  O   . PRO   A 419 ? 0.8219 1.0168 1.1202 0.0516  0.1500  0.1889  439 PRO   A O   
3081 C  CB  . PRO   A 419 ? 0.8003 1.0663 1.2262 0.0185  0.1520  0.2073  439 PRO   A CB  
3082 C  CG  . PRO   A 419 ? 0.8794 1.1833 1.3705 0.0002  0.1337  0.2080  439 PRO   A CG  
3083 C  CD  . PRO   A 419 ? 0.7742 1.0805 1.2520 -0.0026 0.0992  0.1920  439 PRO   A CD  
3084 N  N   . ARG   A 420 ? 0.6759 1.0337 1.0718 0.0243  0.1188  0.1671  440 ARG   A N   
3085 C  CA  . ARG   A 420 ? 0.7185 1.0364 1.0488 0.0268  0.1146  0.1560  440 ARG   A CA  
3086 C  C   . ARG   A 420 ? 0.6797 0.9978 0.9946 0.0270  0.0919  0.1478  440 ARG   A C   
3087 O  O   . ARG   A 420 ? 0.7211 1.0274 1.0077 0.0187  0.0763  0.1378  440 ARG   A O   
3088 C  CB  . ARG   A 420 ? 0.6978 0.9994 1.0084 0.0137  0.1084  0.1498  440 ARG   A CB  
3089 C  CG  . ARG   A 420 ? 0.7589 1.0196 1.0073 0.0197  0.1107  0.1414  440 ARG   A CG  
3090 C  CD  . ARG   A 420 ? 0.7861 1.0288 1.0172 0.0122  0.1103  0.1396  440 ARG   A CD  
3091 N  NE  . ARG   A 420 ? 0.7422 0.9469 0.9153 0.0208  0.1103  0.1318  440 ARG   A NE  
3092 C  CZ  . ARG   A 420 ? 0.7685 0.9481 0.9128 0.0208  0.1116  0.1311  440 ARG   A CZ  
3093 N  NH1 . ARG   A 420 ? 0.5967 0.7807 0.7635 0.0116  0.1154  0.1390  440 ARG   A NH1 
3094 N  NH2 . ARG   A 420 ? 0.8483 0.9951 0.9405 0.0305  0.1065  0.1224  440 ARG   A NH2 
3095 N  N   . ASN   A 421 ? 0.7823 1.1148 1.1170 0.0377  0.0914  0.1538  441 ASN   A N   
3096 C  CA  . ASN   A 421 ? 0.7106 1.0376 1.0266 0.0396  0.0741  0.1508  441 ASN   A CA  
3097 C  C   . ASN   A 421 ? 0.7542 1.0400 1.0243 0.0482  0.0828  0.1475  441 ASN   A C   
3098 O  O   . ASN   A 421 ? 0.8353 1.0956 1.0804 0.0526  0.0977  0.1440  441 ASN   A O   
3099 C  CB  . ASN   A 421 ? 0.6615 1.0173 1.0161 0.0488  0.0663  0.1596  441 ASN   A CB  
3100 C  CG  . ASN   A 421 ? 0.7640 1.1253 1.1441 0.0667  0.0883  0.1691  441 ASN   A CG  
3101 O  OD1 . ASN   A 421 ? 0.8259 1.1608 1.1813 0.0754  0.1107  0.1686  441 ASN   A OD1 
3102 N  ND2 . ASN   A 421 ? 0.9941 1.3903 1.4226 0.0748  0.0815  0.1772  441 ASN   A ND2 
3103 N  N   . CYS   A 422 ? 0.7999 1.0749 1.0562 0.0508  0.0722  0.1488  442 CYS   A N   
3104 C  CA  . CYS   A 422 ? 0.7395 0.9719 0.9579 0.0565  0.0759  0.1451  442 CYS   A CA  
3105 C  C   . CYS   A 422 ? 0.7381 0.9529 0.9549 0.0779  0.0947  0.1481  442 CYS   A C   
3106 O  O   . CYS   A 422 ? 0.7765 1.0034 1.0170 0.0914  0.0971  0.1569  442 CYS   A O   
3107 C  CB  . CYS   A 422 ? 0.6878 0.9128 0.8984 0.0524  0.0616  0.1500  442 CYS   A CB  
3108 S  SG  . CYS   A 422 ? 0.7279 0.8964 0.9015 0.0559  0.0619  0.1463  442 CYS   A SG  
3109 N  N   . ILE   A 423 ? 0.8466 0.9130 0.9783 0.0783  0.0914  0.1500  443 ILE   A N   
3110 C  CA  . ILE   A 423 ? 0.9358 0.9826 1.0551 0.0998  0.1106  0.1521  443 ILE   A CA  
3111 C  C   . ILE   A 423 ? 0.9736 0.9884 1.0732 0.1105  0.1049  0.1495  443 ILE   A C   
3112 O  O   . ILE   A 423 ? 0.9900 0.9950 1.0887 0.1316  0.1188  0.1528  443 ILE   A O   
3113 C  CB  . ILE   A 423 ? 0.8254 0.8442 0.9063 0.1061  0.1229  0.1457  443 ILE   A CB  
3114 C  CG1 . ILE   A 423 ? 0.9230 0.9342 0.9978 0.1304  0.1499  0.1513  443 ILE   A CG1 
3115 C  CG2 . ILE   A 423 ? 0.8412 0.8154 0.8749 0.1042  0.1078  0.1319  443 ILE   A CG2 
3116 C  CD1 . ILE   A 423 ? 1.0495 1.0271 1.0752 0.1413  0.1638  0.1460  443 ILE   A CD1 
3117 N  N   . GLY   A 424 ? 0.8014 0.7993 0.8871 0.0969  0.0856  0.1445  444 GLY   A N   
3118 C  CA  . GLY   A 424 ? 0.9783 0.9396 1.0457 0.1036  0.0787  0.1431  444 GLY   A CA  
3119 C  C   . GLY   A 424 ? 0.9664 0.9449 1.0589 0.0978  0.0683  0.1544  444 GLY   A C   
3120 O  O   . GLY   A 424 ? 1.0067 0.9558 1.0853 0.0928  0.0574  0.1550  444 GLY   A O   
3121 N  N   . MET   A 425 ? 0.9269 0.9511 1.0558 0.0984  0.0706  0.1640  445 MET   A N   
3122 C  CA  . MET   A 425 ? 0.9080 0.9503 1.0560 0.0957  0.0592  0.1752  445 MET   A CA  
3123 C  C   . MET   A 425 ? 0.9739 0.9859 1.1138 0.1139  0.0603  0.1817  445 MET   A C   
3124 O  O   . MET   A 425 ? 1.0251 1.0124 1.1511 0.1080  0.0499  0.1869  445 MET   A O   
3125 C  CB  . MET   A 425 ? 0.8803 0.9749 1.0678 0.0963  0.0587  0.1815  445 MET   A CB  
3126 C  CG  . MET   A 425 ? 0.9312 1.0435 1.1356 0.1016  0.0467  0.1934  445 MET   A CG  
3127 S  SD  . MET   A 425 ? 1.0047 1.1776 1.2554 0.0999  0.0385  0.1968  445 MET   A SD  
3128 C  CE  . MET   A 425 ? 1.0535 1.2423 1.3360 0.1142  0.0594  0.1960  445 MET   A CE  
3129 N  N   . ARG   A 426 ? 1.0491 1.0622 1.1986 0.1370  0.0744  0.1825  446 ARG   A N   
3130 C  CA  . ARG   A 426 ? 1.1033 1.0892 1.2475 0.1592  0.0757  0.1884  446 ARG   A CA  
3131 C  C   . ARG   A 426 ? 1.1315 1.0525 1.2324 0.1582  0.0708  0.1808  446 ARG   A C   
3132 O  O   . ARG   A 426 ? 1.1592 1.0498 1.2512 0.1634  0.0624  0.1880  446 ARG   A O   
3133 C  CB  . ARG   A 426 ? 1.1619 1.1629 1.3244 0.1862  0.0954  0.1888  446 ARG   A CB  
3134 C  CG  . ARG   A 426 ? 1.4169 1.4720 1.6152 0.1802  0.1059  0.1898  446 ARG   A CG  
3135 C  CD  . ARG   A 426 ? 1.4317 1.5099 1.6584 0.2065  0.1279  0.1944  446 ARG   A CD  
3136 N  NE  . ARG   A 426 ? 1.4945 1.6130 1.7683 0.2179  0.1209  0.2063  446 ARG   A NE  
3137 C  CZ  . ARG   A 426 ? 1.6531 1.7550 1.9262 0.2427  0.1195  0.2114  446 ARG   A CZ  
3138 N  NH1 . ARG   A 426 ? 1.6981 1.7403 1.9254 0.2583  0.1251  0.2050  446 ARG   A NH1 
3139 N  NH2 . ARG   A 426 ? 1.5888 1.7324 1.9072 0.2530  0.1101  0.2225  446 ARG   A NH2 
3140 N  N   . PHE   A 427 ? 1.2236 1.1201 1.2969 0.1511  0.0740  0.1664  447 PHE   A N   
3141 C  CA  . PHE   A 427 ? 1.1974 1.0317 1.2317 0.1477  0.0648  0.1561  447 PHE   A CA  
3142 C  C   . PHE   A 427 ? 1.1805 1.0082 1.2178 0.1208  0.0467  0.1627  447 PHE   A C   
3143 O  O   . PHE   A 427 ? 1.2432 1.0261 1.2664 0.1197  0.0377  0.1655  447 PHE   A O   
3144 C  CB  . PHE   A 427 ? 1.2204 1.0350 1.2243 0.1465  0.0687  0.1385  447 PHE   A CB  
3145 C  CG  . PHE   A 427 ? 1.2855 1.0375 1.2509 0.1403  0.0539  0.1246  447 PHE   A CG  
3146 C  CD1 . PHE   A 427 ? 1.3785 1.0739 1.3136 0.1627  0.0549  0.1169  447 PHE   A CD1 
3147 C  CD2 . PHE   A 427 ? 1.1754 0.9250 1.1370 0.1129  0.0377  0.1181  447 PHE   A CD2 
3148 C  CE1 . PHE   A 427 ? 1.5464 1.1803 1.4470 0.1556  0.0374  0.1019  447 PHE   A CE1 
3149 C  CE2 . PHE   A 427 ? 1.2485 0.9431 1.1817 0.1051  0.0207  0.1045  447 PHE   A CE2 
3150 C  CZ  . PHE   A 427 ? 1.4403 1.0751 1.3424 0.1254  0.0194  0.0959  447 PHE   A CZ  
3151 N  N   . ALA   A 428 ? 1.1237 0.9949 1.1799 0.0994  0.0425  0.1660  448 ALA   A N   
3152 C  CA  . ALA   A 428 ? 1.1394 1.0112 1.1999 0.0747  0.0296  0.1733  448 ALA   A CA  
3153 C  C   . ALA   A 428 ? 1.1713 1.0410 1.2409 0.0788  0.0264  0.1924  448 ALA   A C   
3154 O  O   . ALA   A 428 ? 1.1912 1.0284 1.2523 0.0670  0.0188  0.2000  448 ALA   A O   
3155 C  CB  . ALA   A 428 ? 0.9463 0.8683 1.0240 0.0571  0.0281  0.1724  448 ALA   A CB  
3156 N  N   . LEU   A 429 ? 1.1147 1.0188 1.2031 0.0952  0.0313  0.2014  449 LEU   A N   
3157 C  CA  . LEU   A 429 ? 1.0776 0.9796 1.1710 0.1037  0.0264  0.2199  449 LEU   A CA  
3158 C  C   . LEU   A 429 ? 1.1712 1.0126 1.2449 0.1188  0.0258  0.2226  449 LEU   A C   
3159 O  O   . LEU   A 429 ? 1.2004 1.0113 1.2641 0.1125  0.0189  0.2365  449 LEU   A O   
3160 C  CB  . LEU   A 429 ? 1.0313 0.9824 1.1514 0.1210  0.0284  0.2257  449 LEU   A CB  
3161 C  CG  . LEU   A 429 ? 1.1301 1.1372 1.2700 0.1073  0.0258  0.2228  449 LEU   A CG  
3162 C  CD1 . LEU   A 429 ? 0.9706 1.0215 1.1426 0.1244  0.0267  0.2244  449 LEU   A CD1 
3163 C  CD2 . LEU   A 429 ? 1.0622 1.0798 1.1943 0.0915  0.0159  0.2344  449 LEU   A CD2 
3164 N  N   . MET   A 430 ? 1.2321 1.0529 1.2981 0.1401  0.0342  0.2099  450 MET   A N   
3165 C  CA  . MET   A 430 ? 1.2662 1.0229 1.3084 0.1577  0.0332  0.2081  450 MET   A CA  
3166 C  C   . MET   A 430 ? 1.3418 1.0437 1.3601 0.1345  0.0222  0.2033  450 MET   A C   
3167 O  O   . MET   A 430 ? 1.3813 1.0337 1.3873 0.1352  0.0148  0.2127  450 MET   A O   
3168 C  CB  . MET   A 430 ? 1.2843 1.0307 1.3173 0.1849  0.0467  0.1922  450 MET   A CB  
3169 C  CG  . MET   A 430 ? 1.4611 1.1361 1.4632 0.2074  0.0459  0.1857  450 MET   A CG  
3170 S  SD  . MET   A 430 ? 1.5688 1.2305 1.5818 0.2322  0.0422  0.2068  450 MET   A SD  
3171 C  CE  . MET   A 430 ? 1.4329 1.1805 1.4917 0.2531  0.0556  0.2141  450 MET   A CE  
3172 N  N   . ASN   A 431 ? 1.3542 1.0639 1.3683 0.1135  0.0198  0.1891  451 ASN   A N   
3173 C  CA  . ASN   A 431 ? 1.3852 1.0504 1.3851 0.0890  0.0068  0.1829  451 ASN   A CA  
3174 C  C   . ASN   A 431 ? 1.3620 1.0295 1.3767 0.0660  0.0004  0.2050  451 ASN   A C   
3175 O  O   . ASN   A 431 ? 1.3240 0.9373 1.3291 0.0570  -0.0082 0.2107  451 ASN   A O   
3176 C  CB  . ASN   A 431 ? 1.3240 1.0111 1.3232 0.0720  0.0042  0.1656  451 ASN   A CB  
3177 C  CG  . ASN   A 431 ? 1.4570 1.1010 1.4462 0.0481  -0.0122 0.1557  451 ASN   A CG  
3178 O  OD1 . ASN   A 431 ? 1.5315 1.1131 1.5032 0.0506  -0.0213 0.1525  451 ASN   A OD1 
3179 N  ND2 . ASN   A 431 ? 1.3681 1.0447 1.3707 0.0250  -0.0177 0.1501  451 ASN   A ND2 
3180 N  N   . MET   A 432 ? 1.2616 0.9892 1.2976 0.0569  0.0049  0.2182  452 MET   A N   
3181 C  CA  . MET   A 432 ? 1.2915 1.0259 1.3369 0.0364  0.0024  0.2404  452 MET   A CA  
3182 C  C   . MET   A 432 ? 1.2923 0.9952 1.3288 0.0523  0.0023  0.2615  452 MET   A C   
3183 O  O   . MET   A 432 ? 1.2840 0.9516 1.3164 0.0371  -0.0012 0.2783  452 MET   A O   
3184 C  CB  . MET   A 432 ? 1.1816 0.9857 1.2443 0.0278  0.0073  0.2465  452 MET   A CB  
3185 C  CG  . MET   A 432 ? 1.1725 1.0058 1.2443 0.0109  0.0066  0.2286  452 MET   A CG  
3186 S  SD  . MET   A 432 ? 1.2242 1.1310 1.3129 0.0018  0.0112  0.2350  452 MET   A SD  
3187 C  CE  . MET   A 432 ? 1.1280 1.0648 1.2197 0.0305  0.0143  0.2337  452 MET   A CE  
3188 N  N   . LYS   A 433 ? 1.3296 1.0454 1.3655 0.0828  0.0059  0.2625  453 LYS   A N   
3189 C  CA  . LYS   A 433 ? 1.3348 1.0228 1.3622 0.1022  0.0038  0.2826  453 LYS   A CA  
3190 C  C   . LYS   A 433 ? 1.4161 1.0227 1.4228 0.1068  -0.0013 0.2807  453 LYS   A C   
3191 O  O   . LYS   A 433 ? 1.5100 1.0762 1.5067 0.1052  -0.0052 0.3017  453 LYS   A O   
3192 C  CB  . LYS   A 433 ? 1.2382 0.9623 1.2766 0.1352  0.0070  0.2812  453 LYS   A CB  
3193 C  CG  . LYS   A 433 ? 1.1850 0.9815 1.2429 0.1318  0.0069  0.2876  453 LYS   A CG  
3194 C  CD  . LYS   A 433 ? 1.1545 0.9881 1.2321 0.1620  0.0074  0.2856  453 LYS   A CD  
3195 C  CE  . LYS   A 433 ? 1.1135 1.0138 1.2100 0.1571  0.0024  0.2901  453 LYS   A CE  
3196 N  NZ  . LYS   A 433 ? 1.1826 1.1243 1.3078 0.1831  0.0001  0.2878  453 LYS   A NZ  
3197 N  N   . LEU   A 434 ? 1.4126 0.9898 1.4091 0.1131  -0.0017 0.2556  454 LEU   A N   
3198 C  CA  . LEU   A 434 ? 1.4857 0.9794 1.4587 0.1164  -0.0097 0.2491  454 LEU   A CA  
3199 C  C   . LEU   A 434 ? 1.4959 0.9556 1.4707 0.0783  -0.0193 0.2576  454 LEU   A C   
3200 O  O   . LEU   A 434 ? 1.6029 0.9932 1.5643 0.0759  -0.0273 0.2655  454 LEU   A O   
3201 C  CB  . LEU   A 434 ? 1.5214 0.9933 1.4770 0.1317  -0.0088 0.2181  454 LEU   A CB  
3202 C  CG  . LEU   A 434 ? 1.5670 1.0497 1.5177 0.1747  0.0028  0.2116  454 LEU   A CG  
3203 C  CD1 . LEU   A 434 ? 1.7291 1.2085 1.6627 0.1869  0.0091  0.1834  454 LEU   A CD1 
3204 C  CD2 . LEU   A 434 ? 1.5871 1.0052 1.5197 0.2009  -0.0012 0.2197  454 LEU   A CD2 
3205 N  N   . ALA   A 435 ? 1.4553 0.9625 1.4495 0.0483  -0.0184 0.2567  455 ALA   A N   
3206 C  CA  . ALA   A 435 ? 1.5239 1.0109 1.5299 0.0107  -0.0251 0.2676  455 ALA   A CA  
3207 C  C   . ALA   A 435 ? 1.4854 0.9720 1.4960 0.0038  -0.0192 0.3034  455 ALA   A C   
3208 O  O   . ALA   A 435 ? 1.5996 1.0305 1.6086 -0.0129 -0.0243 0.3185  455 ALA   A O   
3209 C  CB  . ALA   A 435 ? 1.4369 0.9814 1.4652 -0.0151 -0.0243 0.2571  455 ALA   A CB  
3210 N  N   . LEU   A 436 ? 1.4250 0.9705 1.4394 0.0167  -0.0093 0.3177  456 LEU   A N   
3211 C  CA  . LEU   A 436 ? 1.4849 1.0336 1.4961 0.0130  -0.0035 0.3523  456 LEU   A CA  
3212 C  C   . LEU   A 436 ? 1.6017 1.0815 1.5911 0.0336  -0.0081 0.3682  456 LEU   A C   
3213 O  O   . LEU   A 436 ? 1.6602 1.1049 1.6435 0.0203  -0.0063 0.3966  456 LEU   A O   
3214 C  CB  . LEU   A 436 ? 1.3949 1.0167 1.4084 0.0280  0.0034  0.3592  456 LEU   A CB  
3215 C  CG  . LEU   A 436 ? 1.3836 1.0709 1.4149 0.0054  0.0099  0.3549  456 LEU   A CG  
3216 C  CD1 . LEU   A 436 ? 1.4147 1.1632 1.4428 0.0232  0.0131  0.3605  456 LEU   A CD1 
3217 C  CD2 . LEU   A 436 ? 1.3013 0.9776 1.3400 -0.0270 0.0161  0.3765  456 LEU   A CD2 
3218 N  N   . ILE   A 437 ? 1.6077 1.0673 1.5854 0.0673  -0.0125 0.3518  457 ILE   A N   
3219 C  CA  . ILE   A 437 ? 1.7159 1.1135 1.6725 0.0939  -0.0171 0.3657  457 ILE   A CA  
3220 C  C   . ILE   A 437 ? 1.8157 1.1260 1.7623 0.0737  -0.0248 0.3708  457 ILE   A C   
3221 O  O   . ILE   A 437 ? 1.8655 1.1342 1.8024 0.0676  -0.0249 0.4007  457 ILE   A O   
3222 C  CB  . ILE   A 437 ? 1.7246 1.1219 1.6754 0.1349  -0.0183 0.3437  457 ILE   A CB  
3223 C  CG1 . ILE   A 437 ? 1.6420 1.1200 1.6077 0.1563  -0.0129 0.3469  457 ILE   A CG1 
3224 C  CG2 . ILE   A 437 ? 1.8074 1.1263 1.7355 0.1620  -0.0246 0.3519  457 ILE   A CG2 
3225 C  CD1 . ILE   A 437 ? 1.5864 1.0796 1.5578 0.1925  -0.0102 0.3257  457 ILE   A CD1 
3226 N  N   . ARG   A 438 ? 1.9365 1.2152 1.8839 0.0628  -0.0324 0.3416  458 ARG   A N   
3227 C  CA  . ARG   A 438 ? 2.0511 1.2419 1.9906 0.0432  -0.0443 0.3413  458 ARG   A CA  
3228 C  C   . ARG   A 438 ? 2.0370 1.2312 1.9992 -0.0030 -0.0422 0.3661  458 ARG   A C   
3229 O  O   . ARG   A 438 ? 2.1709 1.2933 2.1307 -0.0207 -0.0492 0.3812  458 ARG   A O   
3230 C  CB  . ARG   A 438 ? 2.1334 1.2952 2.0660 0.0427  -0.0559 0.3013  458 ARG   A CB  
3231 C  CG  . ARG   A 438 ? 2.2639 1.3218 2.1683 0.0570  -0.0705 0.2890  458 ARG   A CG  
3232 C  CD  . ARG   A 438 ? 2.2561 1.3058 2.1338 0.1014  -0.0696 0.2581  458 ARG   A CD  
3233 N  NE  . ARG   A 438 ? 2.4512 1.3987 2.2961 0.1181  -0.0842 0.2406  458 ARG   A NE  
3234 C  CZ  . ARG   A 438 ? 2.5879 1.4739 2.4129 0.1454  -0.0858 0.2543  458 ARG   A CZ  
3235 N  NH1 . ARG   A 438 ? 2.6211 1.5365 2.4553 0.1586  -0.0750 0.2872  458 ARG   A NH1 
3236 N  NH2 . ARG   A 438 ? 2.6972 1.4870 2.4894 0.1617  -0.1003 0.2336  458 ARG   A NH2 
3237 N  N   . VAL   A 439 ? 1.7812 1.0570 1.7670 -0.0226 -0.0318 0.3712  459 VAL   A N   
3238 C  CA  . VAL   A 439 ? 1.7918 1.0809 1.8029 -0.0646 -0.0255 0.3957  459 VAL   A CA  
3239 C  C   . VAL   A 439 ? 1.8524 1.1404 1.8521 -0.0605 -0.0124 0.4390  459 VAL   A C   
3240 O  O   . VAL   A 439 ? 1.8952 1.1605 1.9075 -0.0913 -0.0064 0.4672  459 VAL   A O   
3241 C  CB  . VAL   A 439 ? 1.7187 1.0936 1.7575 -0.0840 -0.0191 0.3827  459 VAL   A CB  
3242 C  CG1 . VAL   A 439 ? 1.6558 1.0972 1.7000 -0.0875 -0.0004 0.4123  459 VAL   A CG1 
3243 C  CG2 . VAL   A 439 ? 1.7415 1.1019 1.8118 -0.1249 -0.0285 0.3721  459 VAL   A CG2 
3244 N  N   . LEU   A 440 ? 1.7600 1.0715 1.7363 -0.0228 -0.0081 0.4460  460 LEU   A N   
3245 C  CA  . LEU   A 440 ? 1.7939 1.0996 1.7506 -0.0127 0.0010  0.4860  460 LEU   A CA  
3246 C  C   . LEU   A 440 ? 1.9081 1.1245 1.8380 0.0088  -0.0076 0.5004  460 LEU   A C   
3247 O  O   . LEU   A 440 ? 1.9239 1.1158 1.8349 0.0121  -0.0013 0.5380  460 LEU   A O   
3248 C  CB  . LEU   A 440 ? 1.6994 1.0803 1.6458 0.0165  0.0062  0.4867  460 LEU   A CB  
3249 C  CG  . LEU   A 440 ? 1.6414 1.1066 1.6080 -0.0043 0.0167  0.4812  460 LEU   A CG  
3250 C  CD1 . LEU   A 440 ? 1.4473 0.9795 1.4047 0.0253  0.0166  0.4747  460 LEU   A CD1 
3251 C  CD2 . LEU   A 440 ? 1.6258 1.0946 1.5956 -0.0350 0.0319  0.5160  460 LEU   A CD2 
3252 N  N   . GLN   A 441 ? 1.9587 1.1239 1.8825 0.0261  -0.0213 0.4718  461 GLN   A N   
3253 C  CA  . GLN   A 441 ? 2.0489 1.1182 1.9479 0.0441  -0.0307 0.4831  461 GLN   A CA  
3254 C  C   . GLN   A 441 ? 2.2018 1.2002 2.1086 0.0033  -0.0327 0.5034  461 GLN   A C   
3255 O  O   . GLN   A 441 ? 2.3238 1.2469 2.2096 0.0105  -0.0355 0.5298  461 GLN   A O   
3256 C  CB  . GLN   A 441 ? 2.1133 1.1452 2.0017 0.0739  -0.0434 0.4444  461 GLN   A CB  
3257 C  CG  . GLN   A 441 ? 2.0426 1.1176 1.9204 0.1236  -0.0414 0.4345  461 GLN   A CG  
3258 C  CD  . GLN   A 441 ? 2.1984 1.2505 2.0691 0.1509  -0.0482 0.3950  461 GLN   A CD  
3259 O  OE1 . GLN   A 441 ? 2.1454 1.1747 2.0197 0.1308  -0.0539 0.3683  461 GLN   A OE1 
3260 N  NE2 . GLN   A 441 ? 2.2332 1.2927 2.0934 0.1986  -0.0474 0.3913  461 GLN   A NE2 
3261 N  N   . ASN   A 442 ? 2.1702 1.1913 2.1096 -0.0397 -0.0319 0.4927  462 ASN   A N   
3262 C  CA  . ASN   A 442 ? 2.2416 1.1997 2.2004 -0.0833 -0.0365 0.5068  462 ASN   A CA  
3263 C  C   . ASN   A 442 ? 2.2245 1.2282 2.2104 -0.1225 -0.0171 0.5439  462 ASN   A C   
3264 O  O   . ASN   A 442 ? 2.3365 1.2836 2.3293 -0.1490 -0.0134 0.5762  462 ASN   A O   
3265 C  CB  . ASN   A 442 ? 2.2312 1.1717 2.2117 -0.1044 -0.0547 0.4647  462 ASN   A CB  
3266 C  CG  . ASN   A 442 ? 2.4046 1.2586 2.3543 -0.0751 -0.0752 0.4352  462 ASN   A CG  
3267 O  OD1 . ASN   A 442 ? 2.4395 1.2010 2.3865 -0.0909 -0.0899 0.4370  462 ASN   A OD1 
3268 N  ND2 . ASN   A 442 ? 2.4360 1.3188 2.3628 -0.0318 -0.0757 0.4080  462 ASN   A ND2 
3269 N  N   . PHE   A 443 ? 2.0197 1.1226 2.0211 -0.1265 -0.0032 0.5410  463 PHE   A N   
3270 C  CA  . PHE   A 443 ? 2.0607 1.2129 2.0910 -0.1637 0.0168  0.5710  463 PHE   A CA  
3271 C  C   . PHE   A 443 ? 1.9711 1.1944 1.9786 -0.1412 0.0367  0.5939  463 PHE   A C   
3272 O  O   . PHE   A 443 ? 1.9149 1.1718 1.8975 -0.1028 0.0322  0.5769  463 PHE   A O   
3273 C  CB  . PHE   A 443 ? 2.0279 1.2344 2.1058 -0.1973 0.0138  0.5438  463 PHE   A CB  
3274 C  CG  . PHE   A 443 ? 2.0636 1.2075 2.1615 -0.2168 -0.0110 0.5135  463 PHE   A CG  
3275 C  CD1 . PHE   A 443 ? 2.1486 1.2328 2.2758 -0.2573 -0.0159 0.5317  463 PHE   A CD1 
3276 C  CD2 . PHE   A 443 ? 2.0331 1.1769 2.1196 -0.1948 -0.0299 0.4671  463 PHE   A CD2 
3277 C  CE1 . PHE   A 443 ? 2.1771 1.2003 2.3208 -0.2750 -0.0433 0.5007  463 PHE   A CE1 
3278 C  CE2 . PHE   A 443 ? 2.0942 1.1772 2.1908 -0.2096 -0.0548 0.4371  463 PHE   A CE2 
3279 C  CZ  . PHE   A 443 ? 2.1400 1.1617 2.2648 -0.2497 -0.0635 0.4524  463 PHE   A CZ  
3280 N  N   . SER   A 444 ? 1.9600 1.2051 1.9768 -0.1661 0.0588  0.6332  464 SER   A N   
3281 C  CA  . SER   A 444 ? 1.8676 1.1898 1.8673 -0.1534 0.0793  0.6524  464 SER   A CA  
3282 C  C   . SER   A 444 ? 1.8508 1.2422 1.8954 -0.1906 0.0959  0.6526  464 SER   A C   
3283 O  O   . SER   A 444 ? 1.8932 1.2648 1.9826 -0.2301 0.0950  0.6527  464 SER   A O   
3284 C  CB  . SER   A 444 ? 1.9690 1.2567 1.9283 -0.1419 0.0947  0.7032  464 SER   A CB  
3285 O  OG  . SER   A 444 ? 1.9577 1.1936 1.8746 -0.1007 0.0784  0.7019  464 SER   A OG  
3286 N  N   . PHE   A 445 ? 1.8208 1.2939 1.8551 -0.1768 0.1094  0.6514  465 PHE   A N   
3287 C  CA  . PHE   A 445 ? 1.7855 1.3331 1.8610 -0.2038 0.1237  0.6445  465 PHE   A CA  
3288 C  C   . PHE   A 445 ? 1.7998 1.3947 1.8560 -0.2023 0.1542  0.6828  465 PHE   A C   
3289 O  O   . PHE   A 445 ? 1.7729 1.3852 1.7789 -0.1672 0.1571  0.6902  465 PHE   A O   
3290 C  CB  . PHE   A 445 ? 1.5371 1.1419 1.6213 -0.1880 0.1092  0.5970  465 PHE   A CB  
3291 C  CG  . PHE   A 445 ? 1.6031 1.1684 1.7077 -0.1926 0.0830  0.5590  465 PHE   A CG  
3292 C  CD1 . PHE   A 445 ? 1.7105 1.2181 1.7840 -0.1641 0.0647  0.5459  465 PHE   A CD1 
3293 C  CD2 . PHE   A 445 ? 1.6222 1.2081 1.7751 -0.2230 0.0763  0.5364  465 PHE   A CD2 
3294 C  CE1 . PHE   A 445 ? 1.7383 1.2075 1.8235 -0.1650 0.0426  0.5108  465 PHE   A CE1 
3295 C  CE2 . PHE   A 445 ? 1.5961 1.1421 1.7594 -0.2246 0.0510  0.5008  465 PHE   A CE2 
3296 C  CZ  . PHE   A 445 ? 1.6468 1.1333 1.7736 -0.1951 0.0353  0.4880  465 PHE   A CZ  
3297 N  N   . LYS   A 446 ? 1.8163 1.4329 1.9129 -0.2396 0.1765  0.7064  466 LYS   A N   
3298 C  CA  . LYS   A 446 ? 1.9309 1.5911 2.0133 -0.2423 0.2111  0.7462  466 LYS   A CA  
3299 C  C   . LYS   A 446 ? 1.8171 1.5629 1.9481 -0.2629 0.2266  0.7333  466 LYS   A C   
3300 O  O   . LYS   A 446 ? 1.7440 1.4986 1.9345 -0.2913 0.2145  0.7092  466 LYS   A O   
3301 C  CB  . LYS   A 446 ? 1.8784 1.4817 1.9665 -0.2689 0.2312  0.7981  466 LYS   A CB  
3302 C  CG  . LYS   A 446 ? 2.0567 1.5661 2.0995 -0.2503 0.2158  0.8139  466 LYS   A CG  
3303 C  CD  . LYS   A 446 ? 2.2276 1.7390 2.1928 -0.2086 0.2258  0.8366  466 LYS   A CD  
3304 C  CE  . LYS   A 446 ? 2.4751 1.8938 2.3959 -0.1886 0.2092  0.8498  466 LYS   A CE  
3305 N  NZ  . LYS   A 446 ? 2.3848 1.8021 2.2300 -0.1518 0.2184  0.8749  466 LYS   A NZ  
3306 N  N   . PRO   A 447 ? 1.8539 1.6627 1.9588 -0.2468 0.2517  0.7475  467 PRO   A N   
3307 C  CA  . PRO   A 447 ? 1.7782 1.6683 1.9300 -0.2647 0.2704  0.7396  467 PRO   A CA  
3308 C  C   . PRO   A 447 ? 1.9307 1.8205 2.1458 -0.3111 0.2934  0.7726  467 PRO   A C   
3309 O  O   . PRO   A 447 ? 1.9059 1.7393 2.1078 -0.3224 0.3012  0.7986  467 PRO   A O   
3310 C  CB  . PRO   A 447 ? 1.7380 1.6790 1.8329 -0.2321 0.2941  0.7542  467 PRO   A CB  
3311 C  CG  . PRO   A 447 ? 1.6293 1.5253 1.6520 -0.1931 0.2745  0.7509  467 PRO   A CG  
3312 C  CD  . PRO   A 447 ? 1.7980 1.6076 1.8262 -0.2069 0.2603  0.7662  467 PRO   A CD  
3313 N  N   . CYS   A 448 ? 1.9141 1.8675 2.1940 -0.3340 0.2983  0.7551  468 CYS   A N   
3314 C  CA  . CYS   A 448 ? 1.9728 1.9471 2.3124 -0.3712 0.3178  0.7677  468 CYS   A CA  
3315 C  C   . CYS   A 448 ? 1.9360 2.0008 2.2805 -0.3616 0.3508  0.7721  468 CYS   A C   
3316 O  O   . CYS   A 448 ? 1.8461 1.9581 2.1597 -0.3312 0.3527  0.7587  468 CYS   A O   
3317 C  CB  . CYS   A 448 ? 1.9951 1.9641 2.4160 -0.4082 0.2911  0.7413  468 CYS   A CB  
3318 S  SG  . CYS   A 448 ? 2.0699 1.9231 2.4909 -0.4259 0.2554  0.7370  468 CYS   A SG  
3319 N  N   . LYS   A 449 ? 2.1304 2.2179 2.5134 -0.3868 0.3772  0.7909  469 LYS   A N   
3320 C  CA  . LYS   A 449 ? 2.1023 2.2744 2.4925 -0.3769 0.4109  0.7958  469 LYS   A CA  
3321 C  C   . LYS   A 449 ? 2.0073 2.2520 2.4450 -0.3741 0.3998  0.7611  469 LYS   A C   
3322 O  O   . LYS   A 449 ? 1.9246 2.2370 2.3491 -0.3518 0.4221  0.7578  469 LYS   A O   
3323 C  CB  . LYS   A 449 ? 1.9028 2.0874 2.3402 -0.4093 0.4393  0.8208  469 LYS   A CB  
3324 C  CG  . LYS   A 449 ? 1.9503 2.1943 2.4871 -0.4413 0.4359  0.8016  469 LYS   A CG  
3325 C  CD  . LYS   A 449 ? 1.8566 2.0972 2.4467 -0.4797 0.4567  0.8268  469 LYS   A CD  
3326 C  CE  . LYS   A 449 ? 1.8460 2.1482 2.5385 -0.5105 0.4491  0.8057  469 LYS   A CE  
3327 N  NZ  . LYS   A 449 ? 2.0278 2.3239 2.7799 -0.5519 0.4649  0.8289  469 LYS   A NZ  
3328 N  N   . GLU   A 450 ? 2.0216 2.2502 2.5100 -0.3943 0.3647  0.7344  470 GLU   A N   
3329 C  CA  . GLU   A 450 ? 1.9922 2.2818 2.5226 -0.3914 0.3491  0.7004  470 GLU   A CA  
3330 C  C   . GLU   A 450 ? 1.9129 2.1941 2.3827 -0.3544 0.3280  0.6747  470 GLU   A C   
3331 O  O   . GLU   A 450 ? 1.9014 2.2324 2.3822 -0.3397 0.3165  0.6388  470 GLU   A O   
3332 C  CB  . GLU   A 450 ? 2.0745 2.3493 2.6855 -0.4298 0.3175  0.6789  470 GLU   A CB  
3333 C  CG  . GLU   A 450 ? 2.1926 2.3703 2.7920 -0.4456 0.2878  0.6794  470 GLU   A CG  
3334 C  CD  . GLU   A 450 ? 2.3411 2.4694 2.9469 -0.4702 0.3021  0.7093  470 GLU   A CD  
3335 O  OE1 . GLU   A 450 ? 2.4095 2.5652 2.9980 -0.4650 0.3396  0.7376  470 GLU   A OE1 
3336 O  OE2 . GLU   A 450 ? 2.4017 2.4609 3.0272 -0.4943 0.2758  0.7039  470 GLU   A OE2 
3337 N  N   . THR   A 451 ? 1.9565 2.1707 2.3558 -0.3339 0.3176  0.6806  471 THR   A N   
3338 C  CA  . THR   A 451 ? 1.8175 2.0194 2.1528 -0.2940 0.2931  0.6453  471 THR   A CA  
3339 C  C   . THR   A 451 ? 1.8127 2.0809 2.1121 -0.2621 0.3133  0.6401  471 THR   A C   
3340 O  O   . THR   A 451 ? 1.7739 2.0570 2.0364 -0.2500 0.3455  0.6741  471 THR   A O   
3341 C  CB  . THR   A 451 ? 1.8141 1.9396 2.0844 -0.2768 0.2830  0.6596  471 THR   A CB  
3342 O  OG1 . THR   A 451 ? 1.8403 1.8984 2.1402 -0.3028 0.2611  0.6589  471 THR   A OG1 
3343 C  CG2 . THR   A 451 ? 1.6733 1.7946 1.8848 -0.2361 0.2594  0.6253  471 THR   A CG2 
3344 N  N   . GLN   A 452 ? 1.8210 2.1250 2.1274 -0.2472 0.2941  0.5975  472 GLN   A N   
3345 C  CA  . GLN   A 452 ? 1.7334 2.0967 2.0084 -0.2164 0.3082  0.5856  472 GLN   A CA  
3346 C  C   . GLN   A 452 ? 1.6600 1.9939 1.8476 -0.1793 0.3034  0.5865  472 GLN   A C   
3347 O  O   . GLN   A 452 ? 1.6906 1.9999 1.8505 -0.1611 0.2727  0.5550  472 GLN   A O   
3348 C  CB  . GLN   A 452 ? 1.7747 2.1725 2.0807 -0.2117 0.2847  0.5397  472 GLN   A CB  
3349 C  CG  . GLN   A 452 ? 1.7376 2.1925 2.0150 -0.1804 0.2964  0.5237  472 GLN   A CG  
3350 C  CD  . GLN   A 452 ? 1.7173 2.1882 2.0097 -0.1706 0.2674  0.4772  472 GLN   A CD  
3351 O  OE1 . GLN   A 452 ? 1.7267 2.1540 2.0075 -0.1687 0.2361  0.4538  472 GLN   A OE1 
3352 N  NE2 . GLN   A 452 ? 1.6844 2.2174 2.0020 -0.1630 0.2792  0.4650  472 GLN   A NE2 
3353 N  N   . ILE   A 453 ? 1.6672 2.0046 1.8116 -0.1679 0.3335  0.6234  473 ILE   A N   
3354 C  CA  . ILE   A 453 ? 1.7442 2.0578 1.8026 -0.1311 0.3294  0.6274  473 ILE   A CA  
3355 C  C   . ILE   A 453 ? 1.7517 2.1233 1.7733 -0.1035 0.3529  0.6260  473 ILE   A C   
3356 O  O   . ILE   A 453 ? 1.7747 2.1780 1.8012 -0.1092 0.3919  0.6591  473 ILE   A O   
3357 C  CB  . ILE   A 453 ? 1.8470 2.1061 1.8707 -0.1348 0.3418  0.6722  473 ILE   A CB  
3358 C  CG1 . ILE   A 453 ? 1.8606 2.0637 1.9317 -0.1672 0.3242  0.6767  473 ILE   A CG1 
3359 C  CG2 . ILE   A 453 ? 1.7856 2.0138 1.7242 -0.0958 0.3259  0.6697  473 ILE   A CG2 
3360 C  CD1 . ILE   A 453 ? 2.0007 2.1457 2.0453 -0.1748 0.3380  0.7235  473 ILE   A CD1 
3361 N  N   . PRO   A 454 ? 1.7312 2.1170 1.7155 -0.0731 0.3316  0.5890  474 PRO   A N   
3362 C  CA  . PRO   A 454 ? 1.5928 1.9488 1.5702 -0.0636 0.2892  0.5508  474 PRO   A CA  
3363 C  C   . PRO   A 454 ? 1.5313 1.9044 1.5768 -0.0840 0.2719  0.5178  474 PRO   A C   
3364 O  O   . PRO   A 454 ? 1.5038 1.9207 1.5983 -0.0997 0.2893  0.5182  474 PRO   A O   
3365 C  CB  . PRO   A 454 ? 1.5068 1.8808 1.4185 -0.0243 0.2814  0.5308  474 PRO   A CB  
3366 C  CG  . PRO   A 454 ? 1.5900 2.0218 1.5045 -0.0184 0.3146  0.5372  474 PRO   A CG  
3367 C  CD  . PRO   A 454 ? 1.6365 2.0719 1.5807 -0.0441 0.3511  0.5833  474 PRO   A CD  
3368 N  N   . LEU   A 455 ? 1.4592 1.7995 1.5086 -0.0825 0.2378  0.4896  475 LEU   A N   
3369 C  CA  . LEU   A 455 ? 1.4469 1.7981 1.5509 -0.0983 0.2198  0.4581  475 LEU   A CA  
3370 C  C   . LEU   A 455 ? 1.4392 1.8380 1.5390 -0.0795 0.2171  0.4280  475 LEU   A C   
3371 O  O   . LEU   A 455 ? 1.4072 1.8046 1.4595 -0.0522 0.2052  0.4116  475 LEU   A O   
3372 C  CB  . LEU   A 455 ? 1.4262 1.7268 1.5284 -0.0986 0.1878  0.4389  475 LEU   A CB  
3373 C  CG  . LEU   A 455 ? 1.3767 1.6763 1.5281 -0.1150 0.1683  0.4095  475 LEU   A CG  
3374 C  CD1 . LEU   A 455 ? 1.3838 1.6453 1.5732 -0.1447 0.1655  0.4233  475 LEU   A CD1 
3375 C  CD2 . LEU   A 455 ? 1.2120 1.4928 1.3420 -0.0963 0.1411  0.3781  475 LEU   A CD2 
3376 N  N   . LYS   A 456 ? 1.3967 1.8367 1.5480 -0.0938 0.2264  0.4204  476 LYS   A N   
3377 C  CA  . LYS   A 456 ? 1.4667 1.9480 1.6210 -0.0770 0.2219  0.3902  476 LYS   A CA  
3378 C  C   . LYS   A 456 ? 1.4566 1.9241 1.6453 -0.0867 0.1924  0.3582  476 LYS   A C   
3379 O  O   . LYS   A 456 ? 1.4418 1.8973 1.6778 -0.1130 0.1863  0.3612  476 LYS   A O   
3380 C  CB  . LYS   A 456 ? 1.4972 2.0381 1.6850 -0.0812 0.2522  0.4023  476 LYS   A CB  
3381 C  CG  . LYS   A 456 ? 1.5526 2.1106 1.7036 -0.0700 0.2871  0.4366  476 LYS   A CG  
3382 C  CD  . LYS   A 456 ? 1.5701 2.1948 1.7548 -0.0687 0.3192  0.4451  476 LYS   A CD  
3383 C  CE  . LYS   A 456 ? 1.5639 2.2045 1.7206 -0.0638 0.3601  0.4870  476 LYS   A CE  
3384 N  NZ  . LYS   A 456 ? 1.6125 2.2309 1.6765 -0.0282 0.3605  0.4875  476 LYS   A NZ  
3385 N  N   . LEU   A 457 ? 1.3826 1.8492 1.5457 -0.0655 0.1736  0.3280  477 LEU   A N   
3386 C  CA  . LEU   A 457 ? 1.3895 1.8383 1.5747 -0.0709 0.1470  0.2995  477 LEU   A CA  
3387 C  C   . LEU   A 457 ? 1.4429 1.9318 1.6727 -0.0766 0.1479  0.2840  477 LEU   A C   
3388 O  O   . LEU   A 457 ? 1.6080 2.1429 1.8469 -0.0696 0.1680  0.2896  477 LEU   A O   
3389 C  CB  . LEU   A 457 ? 1.3481 1.7780 1.4917 -0.0479 0.1273  0.2765  477 LEU   A CB  
3390 C  CG  . LEU   A 457 ? 1.3602 1.7496 1.4682 -0.0419 0.1187  0.2869  477 LEU   A CG  
3391 C  CD1 . LEU   A 457 ? 1.3756 1.7641 1.4421 -0.0165 0.1055  0.2696  477 LEU   A CD1 
3392 C  CD2 . LEU   A 457 ? 1.2474 1.5963 1.3763 -0.0566 0.1021  0.2822  477 LEU   A CD2 
3393 N  N   . SER   A 458 ? 1.5297 2.0005 1.7855 -0.0870 0.1260  0.2645  478 SER   A N   
3394 C  CA  . SER   A 458 ? 1.5757 2.0792 1.8740 -0.0918 0.1209  0.2485  478 SER   A CA  
3395 C  C   . SER   A 458 ? 1.6025 2.1276 1.8786 -0.0654 0.1170  0.2252  478 SER   A C   
3396 O  O   . SER   A 458 ? 1.4971 1.9931 1.7391 -0.0518 0.1009  0.2081  478 SER   A O   
3397 C  CB  . SER   A 458 ? 1.4465 1.9169 1.7683 -0.1078 0.0962  0.2341  478 SER   A CB  
3398 O  OG  . SER   A 458 ? 1.3950 1.8916 1.7464 -0.1058 0.0850  0.2139  478 SER   A OG  
3399 N  N   . LEU   A 459 ? 1.9371 2.5132 2.2357 -0.0582 0.1320  0.2250  479 LEU   A N   
3400 C  CA  . LEU   A 459 ? 1.8444 2.4400 2.1233 -0.0315 0.1287  0.2025  479 LEU   A CA  
3401 C  C   . LEU   A 459 ? 1.8099 2.3881 2.0993 -0.0293 0.1020  0.1755  479 LEU   A C   
3402 O  O   . LEU   A 459 ? 1.7389 2.3217 2.0084 -0.0074 0.0956  0.1557  479 LEU   A O   
3403 C  CB  . LEU   A 459 ? 1.7663 2.4230 2.0713 -0.0226 0.1530  0.2094  479 LEU   A CB  
3404 C  CG  . LEU   A 459 ? 1.9427 2.6225 2.2160 -0.0086 0.1832  0.2293  479 LEU   A CG  
3405 C  CD1 . LEU   A 459 ? 1.8245 2.4983 2.1088 -0.0319 0.2007  0.2634  479 LEU   A CD1 
3406 C  CD2 . LEU   A 459 ? 1.9015 2.6421 2.1961 0.0088  0.2050  0.2274  479 LEU   A CD2 
3407 N  N   . GLY   A 460 ? 1.6177 2.1725 1.9336 -0.0498 0.0861  0.1742  480 GLY   A N   
3408 C  CA  . GLY   A 460 ? 1.4963 2.0325 1.8174 -0.0468 0.0619  0.1511  480 GLY   A CA  
3409 C  C   . GLY   A 460 ? 1.5726 2.0605 1.8493 -0.0370 0.0473  0.1384  480 GLY   A C   
3410 O  O   . GLY   A 460 ? 1.5813 2.0594 1.8227 -0.0256 0.0533  0.1408  480 GLY   A O   
3411 N  N   . GLY   A 461 ? 1.4540 1.9125 1.7332 -0.0411 0.0276  0.1252  481 GLY   A N   
3412 C  CA  . GLY   A 461 ? 1.4981 1.9133 1.7427 -0.0337 0.0158  0.1148  481 GLY   A CA  
3413 C  C   . GLY   A 461 ? 1.5356 1.9123 1.7694 -0.0458 0.0134  0.1242  481 GLY   A C   
3414 O  O   . GLY   A 461 ? 1.4886 1.8325 1.6988 -0.0399 0.0057  0.1173  481 GLY   A O   
3415 N  N   . LEU   A 462 ? 1.5996 1.9788 1.8516 -0.0622 0.0207  0.1408  482 LEU   A N   
3416 C  CA  . LEU   A 462 ? 1.5787 1.9186 1.8205 -0.0722 0.0185  0.1503  482 LEU   A CA  
3417 C  C   . LEU   A 462 ? 1.5948 1.9385 1.8228 -0.0714 0.0337  0.1699  482 LEU   A C   
3418 O  O   . LEU   A 462 ? 1.6180 1.9956 1.8560 -0.0728 0.0484  0.1823  482 LEU   A O   
3419 C  CB  . LEU   A 462 ? 1.5666 1.8948 1.8371 -0.0923 0.0113  0.1537  482 LEU   A CB  
3420 C  CG  . LEU   A 462 ? 1.6568 1.9654 1.9300 -0.0922 -0.0088 0.1341  482 LEU   A CG  
3421 C  CD1 . LEU   A 462 ? 1.6383 1.9423 1.9447 -0.1131 -0.0190 0.1360  482 LEU   A CD1 
3422 C  CD2 . LEU   A 462 ? 1.7554 2.0172 1.9924 -0.0824 -0.0156 0.1263  482 LEU   A CD2 
3423 N  N   . LEU   A 463 ? 1.3499 1.6600 1.5543 -0.0674 0.0307  0.1737  483 LEU   A N   
3424 C  CA  . LEU   A 463 ? 1.3264 1.6340 1.5156 -0.0659 0.0418  0.1938  483 LEU   A CA  
3425 C  C   . LEU   A 463 ? 1.3668 1.6554 1.5734 -0.0849 0.0460  0.2114  483 LEU   A C   
3426 O  O   . LEU   A 463 ? 1.2975 1.5459 1.4983 -0.0885 0.0385  0.2129  483 LEU   A O   
3427 C  CB  . LEU   A 463 ? 1.2422 1.5262 1.4042 -0.0523 0.0352  0.1909  483 LEU   A CB  
3428 C  CG  . LEU   A 463 ? 1.2526 1.5416 1.3948 -0.0462 0.0445  0.2106  483 LEU   A CG  
3429 C  CD1 . LEU   A 463 ? 1.1743 1.5028 1.3082 -0.0384 0.0548  0.2121  483 LEU   A CD1 
3430 C  CD2 . LEU   A 463 ? 1.1667 1.4381 1.2879 -0.0323 0.0355  0.2086  483 LEU   A CD2 
3431 N  N   . GLN   A 464 ? 1.3483 1.6659 1.5782 -0.0968 0.0586  0.2249  484 GLN   A N   
3432 C  CA  . GLN   A 464 ? 1.2943 1.5981 1.5487 -0.1190 0.0637  0.2438  484 GLN   A CA  
3433 C  C   . GLN   A 464 ? 1.3081 1.6462 1.5685 -0.1228 0.0873  0.2689  484 GLN   A C   
3434 O  O   . GLN   A 464 ? 1.3581 1.7353 1.6081 -0.1081 0.0979  0.2665  484 GLN   A O   
3435 C  CB  . GLN   A 464 ? 1.2939 1.5999 1.5881 -0.1367 0.0514  0.2315  484 GLN   A CB  
3436 C  CG  . GLN   A 464 ? 1.4594 1.7209 1.7425 -0.1348 0.0294  0.2110  484 GLN   A CG  
3437 C  CD  . GLN   A 464 ? 1.5479 1.8114 1.8648 -0.1499 0.0135  0.1971  484 GLN   A CD  
3438 O  OE1 . GLN   A 464 ? 1.5404 1.8471 1.8831 -0.1505 0.0133  0.1901  484 GLN   A OE1 
3439 N  NE2 . GLN   A 464 ? 1.5859 1.8018 1.9021 -0.1603 -0.0018 0.1920  484 GLN   A NE2 
3440 N  N   . PRO   A 465 ? 1.4362 1.7576 1.7100 -0.1410 0.0969  0.2939  485 PRO   A N   
3441 C  CA  . PRO   A 465 ? 1.4227 1.7786 1.7055 -0.1467 0.1234  0.3215  485 PRO   A CA  
3442 C  C   . PRO   A 465 ? 1.4306 1.8378 1.7655 -0.1604 0.1315  0.3193  485 PRO   A C   
3443 O  O   . PRO   A 465 ? 1.3626 1.7684 1.7347 -0.1743 0.1142  0.3026  485 PRO   A O   
3444 C  CB  . PRO   A 465 ? 1.4021 1.7158 1.6879 -0.1651 0.1286  0.3490  485 PRO   A CB  
3445 C  CG  . PRO   A 465 ? 1.4012 1.6580 1.6628 -0.1585 0.1056  0.3345  485 PRO   A CG  
3446 C  CD  . PRO   A 465 ? 1.3579 1.6225 1.6299 -0.1531 0.0860  0.3003  485 PRO   A CD  
3447 N  N   . GLU   A 466 ? 1.5676 2.0218 1.9034 -0.1538 0.1579  0.3361  486 GLU   A N   
3448 C  CA  . GLU   A 466 ? 1.5833 2.0949 1.9738 -0.1655 0.1718  0.3399  486 GLU   A CA  
3449 C  C   . GLU   A 466 ? 1.5891 2.0906 2.0380 -0.2018 0.1692  0.3551  486 GLU   A C   
3450 O  O   . GLU   A 466 ? 1.5682 2.0771 2.0623 -0.2159 0.1493  0.3367  486 GLU   A O   
3451 C  CB  . GLU   A 466 ? 1.6670 2.2241 2.0423 -0.1518 0.2066  0.3623  486 GLU   A CB  
3452 C  CG  . GLU   A 466 ? 1.6900 2.3128 2.0924 -0.1393 0.2178  0.3500  486 GLU   A CG  
3453 C  CD  . GLU   A 466 ? 1.7808 2.4441 2.1579 -0.1212 0.2544  0.3718  486 GLU   A CD  
3454 O  OE1 . GLU   A 466 ? 1.7213 2.3681 2.0761 -0.1272 0.2745  0.4035  486 GLU   A OE1 
3455 O  OE2 . GLU   A 466 ? 1.8151 2.5237 2.1904 -0.0988 0.2633  0.3574  486 GLU   A OE2 
3456 N  N   . LYS   A 467 ? 1.5417 2.0229 1.9884 -0.2168 0.1872  0.3885  487 LYS   A N   
3457 C  CA  . LYS   A 467 ? 1.5387 1.9954 2.0339 -0.2529 0.1840  0.4064  487 LYS   A CA  
3458 C  C   . LYS   A 467 ? 1.5414 1.9185 2.0029 -0.2558 0.1607  0.4013  487 LYS   A C   
3459 O  O   . LYS   A 467 ? 1.5218 1.8683 1.9224 -0.2325 0.1609  0.4021  487 LYS   A O   
3460 C  CB  . LYS   A 467 ? 1.5783 2.0569 2.0909 -0.2679 0.2209  0.4502  487 LYS   A CB  
3461 C  CG  . LYS   A 467 ? 1.7376 2.2676 2.3370 -0.2991 0.2325  0.4630  487 LYS   A CG  
3462 C  CD  . LYS   A 467 ? 1.8248 2.4309 2.4507 -0.2827 0.2390  0.4442  487 LYS   A CD  
3463 C  CE  . LYS   A 467 ? 1.9463 2.6061 2.6692 -0.3139 0.2427  0.4512  487 LYS   A CE  
3464 N  NZ  . LYS   A 467 ? 1.9200 2.5441 2.6830 -0.3384 0.2008  0.4274  487 LYS   A NZ  
3465 N  N   . PRO   A 468 ? 1.5903 1.9330 2.0901 -0.2824 0.1389  0.3945  488 PRO   A N   
3466 C  CA  . PRO   A 468 ? 1.4527 1.7166 1.9194 -0.2830 0.1183  0.3895  488 PRO   A CA  
3467 C  C   . PRO   A 468 ? 1.3856 1.6141 1.8226 -0.2845 0.1383  0.4259  488 PRO   A C   
3468 O  O   . PRO   A 468 ? 1.3504 1.6072 1.8063 -0.2969 0.1668  0.4590  488 PRO   A O   
3469 C  CB  . PRO   A 468 ? 1.4603 1.7010 1.9810 -0.3146 0.0941  0.3783  488 PRO   A CB  
3470 C  CG  . PRO   A 468 ? 1.4550 1.7647 2.0280 -0.3209 0.0920  0.3637  488 PRO   A CG  
3471 C  CD  . PRO   A 468 ? 1.5119 1.8862 2.0862 -0.3100 0.1285  0.3867  488 PRO   A CD  
3472 N  N   . VAL   A 469 ? 1.3492 1.5153 1.7385 -0.2700 0.1241  0.4206  489 VAL   A N   
3473 C  CA  . VAL   A 469 ? 1.4608 1.5867 1.8138 -0.2655 0.1388  0.4531  489 VAL   A CA  
3474 C  C   . VAL   A 469 ? 1.5356 1.6108 1.9227 -0.2990 0.1352  0.4729  489 VAL   A C   
3475 O  O   . VAL   A 469 ? 1.6421 1.6674 2.0382 -0.3081 0.1081  0.4523  489 VAL   A O   
3476 C  CB  . VAL   A 469 ? 1.4183 1.5030 1.7103 -0.2333 0.1246  0.4395  489 VAL   A CB  
3477 C  CG1 . VAL   A 469 ? 1.3742 1.4237 1.6267 -0.2245 0.1394  0.4744  489 VAL   A CG1 
3478 C  CG2 . VAL   A 469 ? 1.2756 1.4077 1.5424 -0.2047 0.1234  0.4160  489 VAL   A CG2 
3479 N  N   . VAL   A 470 ? 1.4339 1.5194 1.8381 -0.3170 0.1627  0.5132  490 VAL   A N   
3480 C  CA  . VAL   A 470 ? 1.5416 1.5792 1.9819 -0.3523 0.1630  0.5383  490 VAL   A CA  
3481 C  C   . VAL   A 470 ? 1.6067 1.5952 1.9968 -0.3417 0.1799  0.5755  490 VAL   A C   
3482 O  O   . VAL   A 470 ? 1.6837 1.7066 2.0483 -0.3291 0.2101  0.6040  490 VAL   A O   
3483 C  CB  . VAL   A 470 ? 1.7039 1.7970 2.2197 -0.3881 0.1825  0.5581  490 VAL   A CB  
3484 C  CG1 . VAL   A 470 ? 1.6125 1.7225 2.1878 -0.4084 0.1534  0.5227  490 VAL   A CG1 
3485 C  CG2 . VAL   A 470 ? 1.7162 1.8905 2.2243 -0.3708 0.2163  0.5720  490 VAL   A CG2 
3486 N  N   . LEU   A 471 ? 1.7067 1.6127 2.0787 -0.3441 0.1600  0.5749  491 LEU   A N   
3487 C  CA  . LEU   A 471 ? 1.6979 1.5489 2.0173 -0.3291 0.1704  0.6070  491 LEU   A CA  
3488 C  C   . LEU   A 471 ? 1.8026 1.5745 2.1451 -0.3594 0.1621  0.6264  491 LEU   A C   
3489 O  O   . LEU   A 471 ? 1.8272 1.5780 2.2177 -0.3869 0.1405  0.6061  491 LEU   A O   
3490 C  CB  . LEU   A 471 ? 1.5593 1.3844 1.8148 -0.2860 0.1522  0.5835  491 LEU   A CB  
3491 C  CG  . LEU   A 471 ? 1.5125 1.4053 1.7380 -0.2541 0.1584  0.5665  491 LEU   A CG  
3492 C  CD1 . LEU   A 471 ? 1.4747 1.3394 1.6504 -0.2170 0.1375  0.5430  491 LEU   A CD1 
3493 C  CD2 . LEU   A 471 ? 1.5784 1.5100 1.7801 -0.2467 0.1915  0.6036  491 LEU   A CD2 
3494 N  N   . LYS   A 472 ? 1.7646 1.4893 2.0694 -0.3531 0.1777  0.6659  492 LYS   A N   
3495 C  CA  . LYS   A 472 ? 1.7792 1.4188 2.0966 -0.3785 0.1718  0.6899  492 LYS   A CA  
3496 C  C   . LYS   A 472 ? 1.8208 1.3798 2.0894 -0.3506 0.1426  0.6690  492 LYS   A C   
3497 O  O   . LYS   A 472 ? 1.7021 1.2623 1.9121 -0.3093 0.1422  0.6654  492 LYS   A O   
3498 C  CB  . LYS   A 472 ? 1.7965 1.4263 2.0975 -0.3862 0.2073  0.7475  492 LYS   A CB  
3499 C  CG  . LYS   A 472 ? 1.9876 1.5431 2.3057 -0.4164 0.2044  0.7609  492 LYS   A CG  
3500 C  CD  . LYS   A 472 ? 2.0706 1.6530 2.3901 -0.4319 0.2425  0.7965  492 LYS   A CD  
3501 C  CE  . LYS   A 472 ? 2.1005 1.7028 2.3456 -0.3930 0.2676  0.8231  492 LYS   A CE  
3502 N  NZ  . LYS   A 472 ? 1.9408 1.5663 2.1813 -0.4063 0.3056  0.8580  492 LYS   A NZ  
3503 N  N   . VAL   A 473 ? 1.9782 1.4679 2.2725 -0.3724 0.1174  0.6545  493 VAL   A N   
3504 C  CA  . VAL   A 473 ? 1.9868 1.3981 2.2401 -0.3462 0.0888  0.6298  493 VAL   A CA  
3505 C  C   . VAL   A 473 ? 2.0683 1.3834 2.3111 -0.3592 0.0887  0.6641  493 VAL   A C   
3506 O  O   . VAL   A 473 ? 2.1179 1.3955 2.4090 -0.4016 0.0835  0.6740  493 VAL   A O   
3507 C  CB  . VAL   A 473 ? 1.7946 1.1959 2.0742 -0.3536 0.0561  0.5784  493 VAL   A CB  
3508 C  CG1 . VAL   A 473 ? 1.8919 1.2152 2.1239 -0.3213 0.0307  0.5530  493 VAL   A CG1 
3509 C  CG2 . VAL   A 473 ? 1.6634 1.1584 1.9552 -0.3429 0.0577  0.5484  493 VAL   A CG2 
3510 N  N   . GLU   A 474 ? 2.2107 1.4851 2.3926 -0.3230 0.0927  0.6824  494 GLU   A N   
3511 C  CA  . GLU   A 474 ? 2.3364 1.5145 2.4974 -0.3274 0.0928  0.7170  494 GLU   A CA  
3512 C  C   . GLU   A 474 ? 2.3369 1.4376 2.4568 -0.2926 0.0633  0.6883  494 GLU   A C   
3513 O  O   . GLU   A 474 ? 2.3334 1.4636 2.4183 -0.2507 0.0555  0.6620  494 GLU   A O   
3514 C  CB  . GLU   A 474 ? 2.4502 1.6429 2.5660 -0.3094 0.1231  0.7628  494 GLU   A CB  
3515 C  CG  . GLU   A 474 ? 2.4637 1.7438 2.6040 -0.3319 0.1562  0.7822  494 GLU   A CG  
3516 C  CD  . GLU   A 474 ? 2.5480 1.8343 2.6313 -0.3116 0.1842  0.8215  494 GLU   A CD  
3517 O  OE1 . GLU   A 474 ? 2.5728 1.8080 2.5968 -0.2754 0.1756  0.8317  494 GLU   A OE1 
3518 O  OE2 . GLU   A 474 ? 2.5303 1.8725 2.6270 -0.3300 0.2140  0.8412  494 GLU   A OE2 
3519 N  N   . SER   A 475 ? 2.2896 1.2909 2.4154 -0.3098 0.0475  0.6940  495 SER   A N   
3520 C  CA  . SER   A 475 ? 2.2584 1.1783 2.3477 -0.2778 0.0193  0.6651  495 SER   A CA  
3521 C  C   . SER   A 475 ? 2.2733 1.1412 2.3044 -0.2394 0.0262  0.6974  495 SER   A C   
3522 O  O   . SER   A 475 ? 2.3093 1.1437 2.3250 -0.2518 0.0430  0.7317  495 SER   A O   
3523 C  CB  . SER   A 475 ? 2.2605 1.0939 2.3786 -0.3114 -0.0043 0.6488  495 SER   A CB  
3524 O  OG  . SER   A 475 ? 2.4502 1.1995 2.5301 -0.2780 -0.0313 0.6211  495 SER   A OG  
3525 N  N   . ARG   A 476 ? 2.3114 1.1859 2.3006 -0.1882 0.0154  0.6727  496 ARG   A N   
3526 C  CA  . ARG   A 476 ? 2.2868 1.1108 2.2224 -0.1460 0.0158  0.6973  496 ARG   A CA  
3527 C  C   . ARG   A 476 ? 2.2520 0.9528 2.1733 -0.1414 -0.0055 0.6931  496 ARG   A C   
3528 O  O   . ARG   A 476 ? 2.5002 1.1390 2.3929 -0.1416 0.0023  0.7216  496 ARG   A O   
3529 C  CB  . ARG   A 476 ? 2.2141 1.0962 2.1194 -0.0934 0.0110  0.6718  496 ARG   A CB  
3530 C  CG  . ARG   A 476 ? 2.0871 1.0801 1.9946 -0.0900 0.0301  0.6795  496 ARG   A CG  
3531 C  CD  . ARG   A 476 ? 1.9869 1.0336 1.8742 -0.0427 0.0209  0.6490  496 ARG   A CD  
3532 N  NE  . ARG   A 476 ? 1.9710 0.9940 1.8135 0.0011  0.0183  0.6720  496 ARG   A NE  
3533 C  CZ  . ARG   A 476 ? 2.0058 1.0465 1.8320 0.0466  0.0054  0.6491  496 ARG   A CZ  
3534 N  NH1 . ARG   A 476 ? 1.9117 0.9880 1.7588 0.0549  -0.0038 0.6041  496 ARG   A NH1 
3535 N  NH2 . ARG   A 476 ? 2.0219 1.0450 1.8111 0.0850  0.0018  0.6733  496 ARG   A NH2 
3536 C  CHA . HEM   B .   ? 0.7949 1.0123 0.9664 0.0229  0.0572  0.1213  601 HEM   A CHA 
3537 C  CHB . HEM   B .   ? 0.6980 0.9355 0.8813 0.0127  0.0329  0.1534  601 HEM   A CHB 
3538 C  CHC . HEM   B .   ? 0.9727 1.0548 1.1036 0.0245  0.0361  0.1450  601 HEM   A CHC 
3539 C  CHD . HEM   B .   ? 0.8641 0.9328 0.9399 0.0548  0.0614  0.1041  601 HEM   A CHD 
3540 C  C1A . HEM   B .   ? 0.8300 1.0661 1.0143 0.0172  0.0472  0.1273  601 HEM   A C1A 
3541 C  C2A . HEM   B .   ? 0.7579 1.0281 0.9590 0.0104  0.0378  0.1284  601 HEM   A C2A 
3542 C  C3A . HEM   B .   ? 0.7602 1.0367 0.9602 0.0095  0.0314  0.1363  601 HEM   A C3A 
3543 C  C4A . HEM   B .   ? 0.7482 0.9938 0.9362 0.0132  0.0361  0.1418  601 HEM   A C4A 
3544 C  CMA . HEM   B .   ? 0.6988 1.0045 0.9030 0.0070  0.0203  0.1390  601 HEM   A CMA 
3545 C  CAA . HEM   B .   ? 0.5219 0.8114 0.7354 0.0060  0.0349  0.1216  601 HEM   A CAA 
3546 C  CBA . HEM   B .   ? 0.5965 0.9068 0.8426 0.0110  0.0361  0.1279  601 HEM   A CBA 
3547 C  CGA . HEM   B .   ? 0.6638 0.9890 0.9260 0.0033  0.0299  0.1215  601 HEM   A CGA 
3548 O  O1A . HEM   B .   ? 0.7223 1.0683 1.0198 0.0031  0.0267  0.1254  601 HEM   A O1A 
3549 O  O2A . HEM   B .   ? 0.6797 0.9952 0.9228 -0.0026 0.0266  0.1124  601 HEM   A O2A 
3550 C  C1B . HEM   B .   ? 0.8068 1.0075 0.9787 0.0140  0.0350  0.1577  601 HEM   A C1B 
3551 C  C2B . HEM   B .   ? 0.9194 1.1059 1.0864 0.0110  0.0323  0.1728  601 HEM   A C2B 
3552 C  C3B . HEM   B .   ? 0.8648 1.0075 1.0220 0.0122  0.0330  0.1714  601 HEM   A C3B 
3553 C  C4B . HEM   B .   ? 0.7602 0.8892 0.9099 0.0186  0.0364  0.1542  601 HEM   A C4B 
3554 C  CMB . HEM   B .   ? 0.7274 0.9411 0.8947 0.0089  0.0289  0.1875  601 HEM   A CMB 
3555 C  CAB . HEM   B .   ? 0.9026 1.0070 1.0529 0.0084  0.0304  0.1853  601 HEM   A CAB 
3556 C  CBB . HEM   B .   ? 1.0011 1.1127 1.1524 0.0039  0.0301  0.2052  601 HEM   A CBB 
3557 C  C1C . HEM   B .   ? 0.9651 1.0304 1.0784 0.0346  0.0407  0.1297  601 HEM   A C1C 
3558 C  C2C . HEM   B .   ? 0.9866 0.9980 1.0706 0.0475  0.0403  0.1185  601 HEM   A C2C 
3559 C  C3C . HEM   B .   ? 1.0221 1.0301 1.0865 0.0579  0.0477  0.1063  601 HEM   A C3C 
3560 C  C4C . HEM   B .   ? 0.8957 0.9545 0.9815 0.0495  0.0526  0.1104  601 HEM   A C4C 
3561 C  CMC . HEM   B .   ? 1.0103 0.9704 1.0828 0.0502  0.0321  0.1205  601 HEM   A CMC 
3562 C  CAC . HEM   B .   ? 0.9359 0.8882 0.9561 0.0774  0.0497  0.0906  601 HEM   A CAC 
3563 C  CBC . HEM   B .   ? 1.0626 1.0099 1.0560 0.0910  0.0607  0.0817  601 HEM   A CBC 
3564 C  C1D . HEM   B .   ? 0.8497 0.9608 0.9481 0.0476  0.0656  0.1087  601 HEM   A C1D 
3565 C  C2D . HEM   B .   ? 0.9094 1.0245 0.9969 0.0516  0.0750  0.1049  601 HEM   A C2D 
3566 C  C3D . HEM   B .   ? 0.8491 1.0043 0.9672 0.0410  0.0739  0.1106  601 HEM   A C3D 
3567 C  C4D . HEM   B .   ? 0.7831 0.9625 0.9274 0.0322  0.0637  0.1170  601 HEM   A C4D 
3568 C  CMD . HEM   B .   ? 0.8850 0.9591 0.9266 0.0673  0.0839  0.0960  601 HEM   A CMD 
3569 C  CAD . HEM   B .   ? 0.7485 0.9165 0.8696 0.0392  0.0815  0.1110  601 HEM   A CAD 
3570 C  CBD . HEM   B .   ? 0.7354 0.9120 0.8728 0.0519  0.1047  0.1218  601 HEM   A CBD 
3571 C  CGD . HEM   B .   ? 0.7945 0.9768 0.9343 0.0486  0.1145  0.1254  601 HEM   A CGD 
3572 O  O1D . HEM   B .   ? 0.7049 0.8923 0.8570 0.0579  0.1380  0.1364  601 HEM   A O1D 
3573 O  O2D . HEM   B .   ? 0.7752 0.9566 0.9065 0.0372  0.1003  0.1187  601 HEM   A O2D 
3574 N  NA  . HEM   B .   ? 0.7910 1.0118 0.9690 0.0184  0.0443  0.1340  601 HEM   A NA  
3575 N  NB  . HEM   B .   ? 0.8624 1.0283 1.0220 0.0190  0.0392  0.1484  601 HEM   A NB  
3576 N  NC  . HEM   B .   ? 0.8261 0.9180 0.9408 0.0360  0.0468  0.1227  601 HEM   A NC  
3577 N  ND  . HEM   B .   ? 0.8300 0.9819 0.9617 0.0362  0.0603  0.1177  601 HEM   A ND  
3578 FE FE  . HEM   B .   ? 0.7294 0.8906 0.8791 0.0277  0.0487  0.1310  601 HEM   A FE  
3579 C  C13 . A1A07 C .   ? 1.5985 1.8470 1.7379 -0.0140 -0.0076 0.0627  602 A1A07 A C13 
3580 C  C15 . A1A07 C .   ? 1.5597 1.7478 1.6782 -0.0198 -0.0199 0.0590  602 A1A07 A C15 
3581 C  C17 . A1A07 C .   ? 1.5355 1.6580 1.6149 -0.0160 -0.0516 0.0370  602 A1A07 A C17 
3582 C  C20 . A1A07 C .   ? 1.6006 1.6212 1.5818 0.0118  -0.0747 0.0117  602 A1A07 A C20 
3583 C  C21 . A1A07 C .   ? 1.6120 1.6655 1.6044 0.0142  -0.0592 0.0212  602 A1A07 A C21 
3584 C  C22 . A1A07 C .   ? 1.5617 1.6639 1.6027 0.0005  -0.0498 0.0318  602 A1A07 A C22 
3585 C  C26 . A1A07 C .   ? 1.1724 1.3058 1.2746 -0.0154 -0.0038 0.0734  602 A1A07 A C26 
3586 C  C28 . A1A07 C .   ? 0.9496 1.0843 1.0680 -0.0094 0.0166  0.0974  602 A1A07 A C28 
3587 C  C02 . A1A07 C .   ? 1.9804 2.3459 2.1752 0.0090  -0.0328 0.0281  602 A1A07 A C02 
3588 C  C05 . A1A07 C .   ? 2.0063 2.3645 2.2020 -0.0055 -0.0235 0.0413  602 A1A07 A C05 
3589 C  C08 . A1A07 C .   ? 1.8533 2.2292 2.0694 -0.0256 -0.0058 0.0647  602 A1A07 A C08 
3590 C  C09 . A1A07 C .   ? 1.8414 2.1819 2.0331 -0.0239 -0.0046 0.0674  602 A1A07 A C09 
3591 C  C12 . A1A07 C .   ? 1.4760 1.7514 1.6378 -0.0227 -0.0027 0.0718  602 A1A07 A C12 
3592 C  C16 . A1A07 C .   ? 1.5467 1.7188 1.6673 -0.0267 -0.0398 0.0491  602 A1A07 A C16 
3593 C  C18 . A1A07 C .   ? 1.4900 1.5794 1.5625 -0.0207 -0.0654 0.0304  602 A1A07 A C18 
3594 C  C19 . A1A07 C .   ? 1.5414 1.5800 1.5666 -0.0073 -0.0784 0.0163  602 A1A07 A C19 
3595 C  C23 . A1A07 C .   ? 1.4311 1.5870 1.5204 -0.0071 -0.0066 0.0625  602 A1A07 A C23 
3596 C  C27 . A1A07 C .   ? 1.0463 1.1541 1.1395 -0.0066 0.0068  0.0811  602 A1A07 A C27 
3597 C  C29 . A1A07 C .   ? 0.9685 1.1069 1.0876 0.0043  0.0302  0.1052  602 A1A07 A C29 
3598 C  C31 . A1A07 C .   ? 1.0007 1.1792 1.1525 -0.0077 0.0288  0.1270  602 A1A07 A C31 
3599 C  C32 . A1A07 C .   ? 1.0415 1.2206 1.1962 -0.0227 0.0206  0.1225  602 A1A07 A C32 
3600 C  C33 . A1A07 C .   ? 0.9661 1.1254 1.1085 -0.0241 0.0130  0.1071  602 A1A07 A C33 
3601 C  C34 . A1A07 C .   ? 1.4161 1.7034 1.5810 -0.0198 0.0063  0.0802  602 A1A07 A C34 
3602 C  C35 . A1A07 C .   ? 1.1816 1.4494 1.3422 -0.0169 0.0139  0.0885  602 A1A07 A C35 
3603 C  C36 . A1A07 C .   ? 1.0637 1.3098 1.2135 -0.0098 0.0194  0.0873  602 A1A07 A C36 
3604 C  C37 . A1A07 C .   ? 0.9782 1.2113 1.1280 -0.0038 0.0294  0.0953  602 A1A07 A C37 
3605 C  C38 . A1A07 C .   ? 0.9926 1.2297 1.1513 -0.0044 0.0307  0.1040  602 A1A07 A C38 
3606 C  C39 . A1A07 C .   ? 0.8857 1.1392 1.0510 -0.0128 0.0241  0.1069  602 A1A07 A C39 
3607 C  C40 . A1A07 C .   ? 1.0375 1.3080 1.2046 -0.0192 0.0176  0.0997  602 A1A07 A C40 
3608 F  F01 . A1A07 C .   ? 1.9358 2.2738 2.1177 0.0132  -0.0455 0.0225  602 A1A07 A F01 
3609 F  F03 . A1A07 C .   ? 1.9507 2.3555 2.1728 0.0120  -0.0320 0.0256  602 A1A07 A F03 
3610 F  F04 . A1A07 C .   ? 1.8283 2.1875 2.0081 0.0173  -0.0305 0.0241  602 A1A07 A F04 
3611 N  N07 . A1A07 C .   ? 1.9416 2.3291 2.1580 -0.0141 -0.0131 0.0515  602 A1A07 A N07 
3612 N  N11 . A1A07 C .   ? 1.6515 1.9574 1.8329 -0.0273 -0.0081 0.0683  602 A1A07 A N11 
3613 N  N25 . A1A07 C .   ? 1.2701 1.4054 1.3543 -0.0044 0.0011  0.0683  602 A1A07 A N25 
3614 N  N30 . A1A07 C .   ? 0.8629 1.0240 1.0018 0.0048  0.0345  0.1187  602 A1A07 A N30 
3615 O  O06 . A1A07 C .   ? 2.0264 2.3512 2.2029 -0.0066 -0.0248 0.0429  602 A1A07 A O06 
3616 O  O10 . A1A07 C .   ? 1.8817 2.2261 2.0646 -0.0182 -0.0009 0.0680  602 A1A07 A O10 
3617 O  O24 . A1A07 C .   ? 1.3242 1.4729 1.3957 0.0024  -0.0012 0.0610  602 A1A07 A O24 
3618 S  S14 . A1A07 C .   ? 1.8277 2.0414 1.9483 -0.0134 -0.0213 0.0539  602 A1A07 A S14 
# 
