data_9COS
# 
_entry.id   9COS 
# 
_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   9COS         pdb_00009cos 10.2210/pdb9cos/pdb 
WWPDB D_1000285784 ?            ?                   
# 
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                        9COS 
_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 syn '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-[3-(pyridin-3-yl)propyl]propanamide' 
586.668   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-[3-(pyridin-3-yl)propyl]propanamide' 
A1A06 
# 
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 
A1A06 non-polymer         . 
'(2R)-3-phenyl-2-{[(2S)-3-phenyl-2-{[N-(trifluoroacetyl)glycyl]amino}propyl]sulfanyl}-N-[3-(pyridin-3-yl)propyl]propanamide' ?    
'C30 H33 F3 N4 O3 S' 586.668 
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  ?   ?   ?   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 ?   ?   ?   A . n 
A 1 178 ASN 178 198 ?   ?   ?   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 ?   ?   ?   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 ?   ?   ?   A . n 
A 1 238 GLU 238 258 ?   ?   ?   A . n 
A 1 239 SER 239 259 ?   ?   ?   A . n 
A 1 240 ARG 240 260 ?   ?   ?   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 ?   ?   ?   A . n 
A 1 259 GLN 259 279 ?   ?   ?   A . n 
A 1 260 ASN 260 280 ?   ?   ?   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 ?   ?   ?   A . n 
A 1 267 HIS 267 287 ?   ?   ?   A . n 
A 1 268 LYS 268 288 ?   ?   ?   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        A1A06 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1A06 
_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 A1A06 1 602 700 A1A06 103 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                     9COS 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     76.190 
_cell.length_a_esd                 ? 
_cell.length_b                     100.160 
_cell.length_b_esd                 ? 
_cell.length_c                     124.730 
_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                         9COS 
_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                   9COS 
_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             2.13 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          42.36 
_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    'PEG 3350, taximate, succinic acid' 
_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         2017-08-05 
_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                          100 
_reflns.entry_id                                       9COS 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.75 
_reflns.d_resolution_low                               78.10 
_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                                     12660 
_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                           99.4 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                3.7 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          6.9 
_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                                0.041 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.996 
_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                                    2.75 
_reflns_shell.d_res_low                                     2.90 
_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                             1819 
_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                               0.924 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.374 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          99.6 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  1.690 
_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                                 9COS 
_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                            2.75 
_refine.ls_d_res_low                             78.10 
_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                     12582 
_refine.ls_number_reflns_R_free                  645 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    98.55 
_refine.ls_percent_reflns_R_free                 5.13 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2471 
_refine.ls_R_factor_R_free                       0.2803 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2442 
_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                          1.33 
_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                 31.43 
_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                            0.43 
_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.details                          ? 
_refine_hist.d_res_high                       2.75 
_refine_hist.d_res_low                        78.10 
_refine_hist.number_atoms_solvent             0 
_refine_hist.number_atoms_total               3482 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        3398 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         84 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.005  ? 3704 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.003  ? 5024 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 14.488 ? 490  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.051  ? 549  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.009  ? 632  ? 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' 2.75 2.96  . . 124 2349 98.00  . . . . 0.3758 . . . . . . . . . . . 0.3869 
'X-RAY DIFFRACTION' 2.96 3.26  . . 123 2372 99.00  . . . . 0.3100 . . . . . . . . . . . 0.3208 
'X-RAY DIFFRACTION' 3.26 3.73  . . 129 2348 98.00  . . . . 0.3077 . . . . . . . . . . . 0.3394 
'X-RAY DIFFRACTION' 3.73 4.70  . . 124 2424 100.00 . . . . 0.2303 . . . . . . . . . . . 0.2831 
'X-RAY DIFFRACTION' 4.70 78.10 . . 145 2444 97.00  . . . . 0.2057 . . . . . . . . . . . 0.2403 
# 
_struct.entry_id                     9COS 
_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        9COS 
_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              9COS 
_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 9COS ?   A ?   ? UNP P08684 LEU 3  deletion         ?   1  
1 9COS ?   A ?   ? UNP P08684 ILE 4  deletion         ?   2  
1 9COS ?   A ?   ? UNP P08684 PRO 5  deletion         ?   3  
1 9COS ?   A ?   ? UNP P08684 ASP 6  deletion         ?   4  
1 9COS ?   A ?   ? UNP P08684 LEU 7  deletion         ?   5  
1 9COS ?   A ?   ? UNP P08684 ALA 8  deletion         ?   6  
1 9COS ?   A ?   ? UNP P08684 MET 9  deletion         ?   7  
1 9COS ?   A ?   ? UNP P08684 GLU 10 deletion         ?   8  
1 9COS ?   A ?   ? UNP P08684 THR 11 deletion         ?   9  
1 9COS ?   A ?   ? UNP P08684 TRP 12 deletion         ?   10 
1 9COS ?   A ?   ? UNP P08684 LEU 13 deletion         ?   11 
1 9COS ?   A ?   ? UNP P08684 LEU 14 deletion         ?   12 
1 9COS ?   A ?   ? UNP P08684 LEU 15 deletion         ?   13 
1 9COS ?   A ?   ? UNP P08684 ALA 16 deletion         ?   14 
1 9COS ?   A ?   ? UNP P08684 VAL 17 deletion         ?   15 
1 9COS ?   A ?   ? UNP P08684 SER 18 deletion         ?   16 
1 9COS ?   A ?   ? UNP P08684 LEU 19 deletion         ?   17 
1 9COS ?   A ?   ? UNP P08684 VAL 20 deletion         ?   18 
1 9COS ?   A ?   ? UNP P08684 LEU 21 deletion         ?   19 
1 9COS ?   A ?   ? UNP P08684 LEU 22 deletion         ?   20 
1 9COS HIS A 484 ? UNP P08684 ?   ?  'expression tag' 504 21 
1 9COS HIS A 485 ? UNP P08684 ?   ?  'expression tag' 505 22 
1 9COS HIS A 486 ? UNP P08684 ?   ?  'expression tag' 506 23 
1 9COS 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 
# 
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 -100.1600000000 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 GLY A 11  ? LEU A 16  ? GLY A 31  LEU A 36  1 ? 6  
HELX_P HELX_P2  AA2 ASN A 29  ? HIS A 34  ? ASN A 49  HIS A 54  5 ? 6  
HELX_P HELX_P3  AA3 LYS A 35  ? GLY A 49  ? LYS A 55  GLY A 69  1 ? 15 
HELX_P HELX_P4  AA4 ASP A 66  ? VAL A 75  ? ASP A 86  VAL A 95  1 ? 10 
HELX_P HELX_P5  AA5 VAL A 91  ? ALA A 97  ? VAL A 111 ALA A 117 5 ? 7  
HELX_P HELX_P6  AA6 GLU A 102 ? SER A 114 ? GLU A 122 SER A 134 1 ? 13 
HELX_P HELX_P7  AA7 PRO A 115 ? PHE A 117 ? PRO A 135 PHE A 137 5 ? 3  
HELX_P HELX_P8  AA8 THR A 118 ? GLU A 124 ? THR A 138 GLU A 144 1 ? 7  
HELX_P HELX_P9  AA9 MET A 125 ? THR A 146 ? MET A 145 THR A 166 1 ? 22 
HELX_P HELX_P10 AB1 LEU A 152 ? SER A 168 ? LEU A 172 SER A 188 1 ? 17 
HELX_P HELX_P11 AB2 PHE A 199 ? PHE A 206 ? PHE A 219 PHE A 226 1 ? 8  
HELX_P HELX_P12 AB3 LEU A 209 ? VAL A 215 ? LEU A 229 VAL A 235 1 ? 7  
HELX_P HELX_P13 AB4 PRO A 222 ? ARG A 230 ? PRO A 242 ARG A 250 1 ? 9  
HELX_P HELX_P14 AB5 PHE A 251 ? ASP A 257 ? PHE A 271 ASP A 277 1 ? 7  
HELX_P HELX_P15 AB6 ASP A 272 ? HIS A 304 ? ASP A 292 HIS A 324 1 ? 33 
HELX_P HELX_P16 AB7 HIS A 304 ? LEU A 319 ? HIS A 324 LEU A 339 1 ? 16 
HELX_P HELX_P17 AB8 THR A 326 ? LEU A 331 ? THR A 346 LEU A 351 1 ? 6  
HELX_P HELX_P18 AB9 MET A 333 ? PHE A 347 ? MET A 353 PHE A 367 1 ? 15 
HELX_P HELX_P19 AC1 PRO A 377 ? ARG A 383 ? PRO A 397 ARG A 403 1 ? 7  
HELX_P HELX_P20 AC2 LEU A 395 ? SER A 400 ? LEU A 415 SER A 420 5 ? 6  
HELX_P HELX_P21 AC3 GLY A 424 ? GLN A 441 ? GLY A 444 GLN A 461 1 ? 18 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1 metalc ? ? A CYS 422 SG ? ? ? 1_555 B HEM   . FE  ? ? A CYS 442 A HEM   601 1_555 ? ? ? ? ? ? ? 2.408 ? ? 
metalc2 metalc ? ? B HEM .   FE ? ? ? 1_555 C A1A06 . N33 ? ? A HEM 601 A A1A06 602 1_555 ? ? ? ? ? ? ? 2.192 ? ? 
# 
_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 98.2  ? 
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 87.1  ? 
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 87.5  ? 
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 89.0  ? 
5  NA ? B HEM .   ? A HEM 601 ? 1_555 FE ? B HEM . ? A HEM 601 ? 1_555 NC  ? B HEM   . ? A HEM   601 ? 1_555 172.7 ? 
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 92.1  ? 
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 98.7  ? 
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 91.9  ? 
9  NB ? B HEM .   ? A HEM 601 ? 1_555 FE ? B HEM . ? A HEM 601 ? 1_555 ND  ? B HEM   . ? A HEM   601 ? 1_555 174.2 ? 
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 87.8  ? 
11 SG ? A CYS 422 ? A CYS 442 ? 1_555 FE ? B HEM . ? A HEM 601 ? 1_555 N33 ? C A1A06 . ? A A1A06 602 ? 1_555 176.7 ? 
12 NA ? B HEM .   ? A HEM 601 ? 1_555 FE ? B HEM . ? A HEM 601 ? 1_555 N33 ? C A1A06 . ? A A1A06 602 ? 1_555 84.8  ? 
13 NB ? B HEM .   ? A HEM 601 ? 1_555 FE ? B HEM . ? A HEM 601 ? 1_555 N33 ? C A1A06 . ? A A1A06 602 ? 1_555 91.7  ? 
14 NC ? B HEM .   ? A HEM 601 ? 1_555 FE ? B HEM . ? A HEM 601 ? 1_555 N33 ? C A1A06 . ? A A1A06 602 ? 1_555 88.0  ? 
15 ND ? B HEM .   ? A HEM 601 ? 1_555 FE ? B HEM . ? A HEM 601 ? 1_555 N33 ? C A1A06 . ? A A1A06 602 ? 1_555 82.5  ? 
# 
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 4.20 
2 ILE 453 A . ? ILE 473 A PRO 454 A ? PRO 474 A 1 1.67 
# 
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 MET A 375 ? O MET A 395 
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                   9COS 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 PHE A 46  ? ? 74.30   -59.74  
2  1 PHE A 102 ? ? -111.17 66.94   
3  1 ASP A 123 ? ? 47.36   -123.33 
4  1 PHE A 189 ? ? -127.18 -56.81  
5  1 SER A 195 ? ? -80.17  48.25   
6  1 PHE A 226 ? ? -118.56 66.39   
7  1 LEU A 249 ? ? -58.00  -6.98   
8  1 ARG A 250 ? ? -81.25  49.44   
9  1 SER A 252 ? ? 36.46   52.07   
10 1 ARG A 255 ? ? -111.19 -166.49 
11 1 TYR A 307 ? ? -89.16  -70.05  
12 1 LEU A 339 ? ? -116.57 78.89   
13 1 LYS A 342 ? ? 35.90   50.29   
14 1 MET A 353 ? ? -66.10  99.82   
15 1 MET A 371 ? ? 73.97   -49.21  
16 1 GLU A 410 ? ? 49.94   74.48   
17 1 ASN A 426 ? ? -85.39  31.80   
18 1 PRO A 429 ? ? -69.69  6.45    
# 
_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         -19.3870 
_pdbx_refine_tls.origin_y         -26.5679 
_pdbx_refine_tls.origin_z         -13.1274 
_pdbx_refine_tls.T[1][1]          0.5175 
_pdbx_refine_tls.T[1][1]_esd      ? 
_pdbx_refine_tls.T[1][2]          -0.0839 
_pdbx_refine_tls.T[1][2]_esd      ? 
_pdbx_refine_tls.T[1][3]          0.0550 
_pdbx_refine_tls.T[1][3]_esd      ? 
_pdbx_refine_tls.T[2][2]          0.6359 
_pdbx_refine_tls.T[2][2]_esd      ? 
_pdbx_refine_tls.T[2][3]          0.0873 
_pdbx_refine_tls.T[2][3]_esd      ? 
_pdbx_refine_tls.T[3][3]          0.6527 
_pdbx_refine_tls.T[3][3]_esd      ? 
_pdbx_refine_tls.L[1][1]          2.7043 
_pdbx_refine_tls.L[1][1]_esd      ? 
_pdbx_refine_tls.L[1][2]          -1.1185 
_pdbx_refine_tls.L[1][2]_esd      ? 
_pdbx_refine_tls.L[1][3]          0.4144 
_pdbx_refine_tls.L[1][3]_esd      ? 
_pdbx_refine_tls.L[2][2]          4.7068 
_pdbx_refine_tls.L[2][2]_esd      ? 
_pdbx_refine_tls.L[2][3]          -0.7727 
_pdbx_refine_tls.L[2][3]_esd      ? 
_pdbx_refine_tls.L[3][3]          3.7036 
_pdbx_refine_tls.L[3][3]_esd      ? 
_pdbx_refine_tls.S[1][1]          -0.0122 
_pdbx_refine_tls.S[1][1]_esd      ? 
_pdbx_refine_tls.S[1][2]          0.2687 
_pdbx_refine_tls.S[1][2]_esd      ? 
_pdbx_refine_tls.S[1][3]          0.4482 
_pdbx_refine_tls.S[1][3]_esd      ? 
_pdbx_refine_tls.S[2][1]          0.3412 
_pdbx_refine_tls.S[2][1]_esd      ? 
_pdbx_refine_tls.S[2][2]          0.0480 
_pdbx_refine_tls.S[2][2]_esd      ? 
_pdbx_refine_tls.S[2][3]          0.1296 
_pdbx_refine_tls.S[2][3]_esd      ? 
_pdbx_refine_tls.S[3][1]          -0.6737 
_pdbx_refine_tls.S[3][1]_esd      ? 
_pdbx_refine_tls.S[3][2]          0.2337 
_pdbx_refine_tls.S[3][2]_esd      ? 
_pdbx_refine_tls.S[3][3]          -0.0309 
_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 HIS 28  ? A HIS 8   
9  1 Y 1 A ASN 197 ? A ASN 177 
10 1 Y 1 A ASN 198 ? A ASN 178 
11 1 Y 1 A PRO 199 ? A PRO 179 
12 1 Y 1 A GLN 200 ? A GLN 180 
13 1 Y 1 A ASP 201 ? A ASP 181 
14 1 Y 1 A PRO 202 ? A PRO 182 
15 1 Y 1 A PHE 203 ? A PHE 183 
16 1 Y 1 A VAL 204 ? A VAL 184 
17 1 Y 1 A GLU 205 ? A GLU 185 
18 1 Y 1 A ASN 206 ? A ASN 186 
19 1 Y 1 A THR 207 ? A THR 187 
20 1 Y 1 A LYS 208 ? A LYS 188 
21 1 Y 1 A LYS 209 ? A LYS 189 
22 1 Y 1 A LEU 210 ? A LEU 190 
23 1 Y 1 A LEU 211 ? A LEU 191 
24 1 Y 1 A ARG 212 ? A ARG 192 
25 1 Y 1 A PHE 213 ? A PHE 193 
26 1 Y 1 A ASP 214 ? A ASP 194 
27 1 Y 1 A PHE 215 ? A PHE 195 
28 1 Y 1 A LEU 216 ? A LEU 196 
29 1 Y 1 A LYS 257 ? A LYS 237 
30 1 Y 1 A GLU 258 ? A GLU 238 
31 1 Y 1 A SER 259 ? A SER 239 
32 1 Y 1 A ARG 260 ? A ARG 240 
33 1 Y 1 A LEU 261 ? A LEU 241 
34 1 Y 1 A GLU 262 ? A GLU 242 
35 1 Y 1 A ASP 263 ? A ASP 243 
36 1 Y 1 A THR 264 ? A THR 244 
37 1 Y 1 A GLN 265 ? A GLN 245 
38 1 Y 1 A LYS 266 ? A LYS 246 
39 1 Y 1 A HIS 267 ? A HIS 247 
40 1 Y 1 A ARG 268 ? A ARG 248 
41 1 Y 1 A VAL 269 ? A VAL 249 
42 1 Y 1 A SER 278 ? A SER 258 
43 1 Y 1 A GLN 279 ? A GLN 259 
44 1 Y 1 A ASN 280 ? A ASN 260 
45 1 Y 1 A SER 281 ? A SER 261 
46 1 Y 1 A LYS 282 ? A LYS 262 
47 1 Y 1 A GLU 283 ? A GLU 263 
48 1 Y 1 A THR 284 ? A THR 264 
49 1 Y 1 A GLU 285 ? A GLU 265 
50 1 Y 1 A SER 286 ? A SER 266 
51 1 Y 1 A HIS 287 ? A HIS 267 
52 1 Y 1 A LYS 288 ? A LYS 268 
53 1 Y 1 A ASP 497 ? A ASP 477 
54 1 Y 1 A GLY 498 ? A GLY 478 
55 1 Y 1 A THR 499 ? A THR 479 
56 1 Y 1 A VAL 500 ? A VAL 480 
57 1 Y 1 A SER 501 ? A SER 481 
58 1 Y 1 A GLY 502 ? A GLY 482 
59 1 Y 1 A ALA 503 ? A ALA 483 
60 1 Y 1 A HIS 504 ? A HIS 484 
61 1 Y 1 A HIS 505 ? A HIS 485 
62 1 Y 1 A HIS 506 ? A HIS 486 
63 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 
A1A06 C02  C  N N 1   
A1A06 C05  C  N N 2   
A1A06 C08  C  N N 3   
A1A06 C09  C  N N 4   
A1A06 C12  C  N S 5   
A1A06 C13  C  N N 6   
A1A06 C15  C  N R 7   
A1A06 C16  C  N N 8   
A1A06 C17  C  Y N 9   
A1A06 C18  C  Y N 10  
A1A06 C19  C  Y N 11  
A1A06 C20  C  Y N 12  
A1A06 C21  C  Y N 13  
A1A06 C22  C  Y N 14  
A1A06 C23  C  N N 15  
A1A06 C26  C  N N 16  
A1A06 C27  C  N N 17  
A1A06 C28  C  N N 18  
A1A06 C29  C  Y N 19  
A1A06 C30  C  Y N 20  
A1A06 C31  C  Y N 21  
A1A06 C32  C  Y N 22  
A1A06 C34  C  Y N 23  
A1A06 C35  C  N N 24  
A1A06 C36  C  Y N 25  
A1A06 C37  C  Y N 26  
A1A06 C38  C  Y N 27  
A1A06 C39  C  Y N 28  
A1A06 C40  C  Y N 29  
A1A06 C41  C  Y N 30  
A1A06 F01  F  N N 31  
A1A06 F03  F  N N 32  
A1A06 F04  F  N N 33  
A1A06 N07  N  N N 34  
A1A06 N11  N  N N 35  
A1A06 N25  N  N N 36  
A1A06 N33  N  Y N 37  
A1A06 O06  O  N N 38  
A1A06 O10  O  N N 39  
A1A06 O24  O  N N 40  
A1A06 S14  S  N N 41  
A1A06 H1   H  N N 42  
A1A06 H2   H  N N 43  
A1A06 H3   H  N N 44  
A1A06 H4   H  N N 45  
A1A06 H5   H  N N 46  
A1A06 H6   H  N N 47  
A1A06 H7   H  N N 48  
A1A06 H8   H  N N 49  
A1A06 H9   H  N N 50  
A1A06 H10  H  N N 51  
A1A06 H11  H  N N 52  
A1A06 H12  H  N N 53  
A1A06 H13  H  N N 54  
A1A06 H14  H  N N 55  
A1A06 H15  H  N N 56  
A1A06 H16  H  N N 57  
A1A06 H17  H  N N 58  
A1A06 H18  H  N N 59  
A1A06 H19  H  N N 60  
A1A06 H20  H  N N 61  
A1A06 H21  H  N N 62  
A1A06 H22  H  N N 63  
A1A06 H23  H  N N 64  
A1A06 H24  H  N N 65  
A1A06 H25  H  N N 66  
A1A06 H26  H  N N 67  
A1A06 H27  H  N N 68  
A1A06 H28  H  N N 69  
A1A06 H29  H  N N 70  
A1A06 H30  H  N N 71  
A1A06 H31  H  N N 72  
A1A06 H32  H  N N 73  
A1A06 H33  H  N N 74  
ALA   N    N  N N 75  
ALA   CA   C  N S 76  
ALA   C    C  N N 77  
ALA   O    O  N N 78  
ALA   CB   C  N N 79  
ALA   OXT  O  N N 80  
ALA   H    H  N N 81  
ALA   H2   H  N N 82  
ALA   HA   H  N N 83  
ALA   HB1  H  N N 84  
ALA   HB2  H  N N 85  
ALA   HB3  H  N N 86  
ALA   HXT  H  N N 87  
ARG   N    N  N N 88  
ARG   CA   C  N S 89  
ARG   C    C  N N 90  
ARG   O    O  N N 91  
ARG   CB   C  N N 92  
ARG   CG   C  N N 93  
ARG   CD   C  N N 94  
ARG   NE   N  N N 95  
ARG   CZ   C  N N 96  
ARG   NH1  N  N N 97  
ARG   NH2  N  N N 98  
ARG   OXT  O  N N 99  
ARG   H    H  N N 100 
ARG   H2   H  N N 101 
ARG   HA   H  N N 102 
ARG   HB2  H  N N 103 
ARG   HB3  H  N N 104 
ARG   HG2  H  N N 105 
ARG   HG3  H  N N 106 
ARG   HD2  H  N N 107 
ARG   HD3  H  N N 108 
ARG   HE   H  N N 109 
ARG   HH11 H  N N 110 
ARG   HH12 H  N N 111 
ARG   HH21 H  N N 112 
ARG   HH22 H  N N 113 
ARG   HXT  H  N N 114 
ASN   N    N  N N 115 
ASN   CA   C  N S 116 
ASN   C    C  N N 117 
ASN   O    O  N N 118 
ASN   CB   C  N N 119 
ASN   CG   C  N N 120 
ASN   OD1  O  N N 121 
ASN   ND2  N  N N 122 
ASN   OXT  O  N N 123 
ASN   H    H  N N 124 
ASN   H2   H  N N 125 
ASN   HA   H  N N 126 
ASN   HB2  H  N N 127 
ASN   HB3  H  N N 128 
ASN   HD21 H  N N 129 
ASN   HD22 H  N N 130 
ASN   HXT  H  N N 131 
ASP   N    N  N N 132 
ASP   CA   C  N S 133 
ASP   C    C  N N 134 
ASP   O    O  N N 135 
ASP   CB   C  N N 136 
ASP   CG   C  N N 137 
ASP   OD1  O  N N 138 
ASP   OD2  O  N N 139 
ASP   OXT  O  N N 140 
ASP   H    H  N N 141 
ASP   H2   H  N N 142 
ASP   HA   H  N N 143 
ASP   HB2  H  N N 144 
ASP   HB3  H  N N 145 
ASP   HD2  H  N N 146 
ASP   HXT  H  N N 147 
CYS   N    N  N N 148 
CYS   CA   C  N R 149 
CYS   C    C  N N 150 
CYS   O    O  N N 151 
CYS   CB   C  N N 152 
CYS   SG   S  N N 153 
CYS   OXT  O  N N 154 
CYS   H    H  N N 155 
CYS   H2   H  N N 156 
CYS   HA   H  N N 157 
CYS   HB2  H  N N 158 
CYS   HB3  H  N N 159 
CYS   HG   H  N N 160 
CYS   HXT  H  N N 161 
GLN   N    N  N N 162 
GLN   CA   C  N S 163 
GLN   C    C  N N 164 
GLN   O    O  N N 165 
GLN   CB   C  N N 166 
GLN   CG   C  N N 167 
GLN   CD   C  N N 168 
GLN   OE1  O  N N 169 
GLN   NE2  N  N N 170 
GLN   OXT  O  N N 171 
GLN   H    H  N N 172 
GLN   H2   H  N N 173 
GLN   HA   H  N N 174 
GLN   HB2  H  N N 175 
GLN   HB3  H  N N 176 
GLN   HG2  H  N N 177 
GLN   HG3  H  N N 178 
GLN   HE21 H  N N 179 
GLN   HE22 H  N N 180 
GLN   HXT  H  N N 181 
GLU   N    N  N N 182 
GLU   CA   C  N S 183 
GLU   C    C  N N 184 
GLU   O    O  N N 185 
GLU   CB   C  N N 186 
GLU   CG   C  N N 187 
GLU   CD   C  N N 188 
GLU   OE1  O  N N 189 
GLU   OE2  O  N N 190 
GLU   OXT  O  N N 191 
GLU   H    H  N N 192 
GLU   H2   H  N N 193 
GLU   HA   H  N N 194 
GLU   HB2  H  N N 195 
GLU   HB3  H  N N 196 
GLU   HG2  H  N N 197 
GLU   HG3  H  N N 198 
GLU   HE2  H  N N 199 
GLU   HXT  H  N N 200 
GLY   N    N  N N 201 
GLY   CA   C  N N 202 
GLY   C    C  N N 203 
GLY   O    O  N N 204 
GLY   OXT  O  N N 205 
GLY   H    H  N N 206 
GLY   H2   H  N N 207 
GLY   HA2  H  N N 208 
GLY   HA3  H  N N 209 
GLY   HXT  H  N N 210 
HEM   CHA  C  N N 211 
HEM   CHB  C  N N 212 
HEM   CHC  C  N N 213 
HEM   CHD  C  N N 214 
HEM   C1A  C  Y N 215 
HEM   C2A  C  Y N 216 
HEM   C3A  C  Y N 217 
HEM   C4A  C  Y N 218 
HEM   CMA  C  N N 219 
HEM   CAA  C  N N 220 
HEM   CBA  C  N N 221 
HEM   CGA  C  N N 222 
HEM   O1A  O  N N 223 
HEM   O2A  O  N N 224 
HEM   C1B  C  N N 225 
HEM   C2B  C  N N 226 
HEM   C3B  C  N N 227 
HEM   C4B  C  N N 228 
HEM   CMB  C  N N 229 
HEM   CAB  C  N N 230 
HEM   CBB  C  N N 231 
HEM   C1C  C  Y N 232 
HEM   C2C  C  Y N 233 
HEM   C3C  C  Y N 234 
HEM   C4C  C  Y N 235 
HEM   CMC  C  N N 236 
HEM   CAC  C  N N 237 
HEM   CBC  C  N N 238 
HEM   C1D  C  N N 239 
HEM   C2D  C  N N 240 
HEM   C3D  C  N N 241 
HEM   C4D  C  N N 242 
HEM   CMD  C  N N 243 
HEM   CAD  C  N N 244 
HEM   CBD  C  N N 245 
HEM   CGD  C  N N 246 
HEM   O1D  O  N N 247 
HEM   O2D  O  N N 248 
HEM   NA   N  Y N 249 
HEM   NB   N  N N 250 
HEM   NC   N  Y N 251 
HEM   ND   N  N N 252 
HEM   FE   FE N N 253 
HEM   HHB  H  N N 254 
HEM   HHC  H  N N 255 
HEM   HHD  H  N N 256 
HEM   HMA  H  N N 257 
HEM   HMAA H  N N 258 
HEM   HMAB H  N N 259 
HEM   HAA  H  N N 260 
HEM   HAAA H  N N 261 
HEM   HBA  H  N N 262 
HEM   HBAA H  N N 263 
HEM   HMB  H  N N 264 
HEM   HMBA H  N N 265 
HEM   HMBB H  N N 266 
HEM   HAB  H  N N 267 
HEM   HBB  H  N N 268 
HEM   HBBA H  N N 269 
HEM   HMC  H  N N 270 
HEM   HMCA H  N N 271 
HEM   HMCB H  N N 272 
HEM   HAC  H  N N 273 
HEM   HBC  H  N N 274 
HEM   HBCA H  N N 275 
HEM   HMD  H  N N 276 
HEM   HMDA H  N N 277 
HEM   HMDB H  N N 278 
HEM   HAD  H  N N 279 
HEM   HADA H  N N 280 
HEM   HBD  H  N N 281 
HEM   HBDA H  N N 282 
HEM   H2A  H  N N 283 
HEM   H2D  H  N N 284 
HEM   HHA  H  N N 285 
HIS   N    N  N N 286 
HIS   CA   C  N S 287 
HIS   C    C  N N 288 
HIS   O    O  N N 289 
HIS   CB   C  N N 290 
HIS   CG   C  Y N 291 
HIS   ND1  N  Y N 292 
HIS   CD2  C  Y N 293 
HIS   CE1  C  Y N 294 
HIS   NE2  N  Y N 295 
HIS   OXT  O  N N 296 
HIS   H    H  N N 297 
HIS   H2   H  N N 298 
HIS   HA   H  N N 299 
HIS   HB2  H  N N 300 
HIS   HB3  H  N N 301 
HIS   HD1  H  N N 302 
HIS   HD2  H  N N 303 
HIS   HE1  H  N N 304 
HIS   HE2  H  N N 305 
HIS   HXT  H  N N 306 
ILE   N    N  N N 307 
ILE   CA   C  N S 308 
ILE   C    C  N N 309 
ILE   O    O  N N 310 
ILE   CB   C  N S 311 
ILE   CG1  C  N N 312 
ILE   CG2  C  N N 313 
ILE   CD1  C  N N 314 
ILE   OXT  O  N N 315 
ILE   H    H  N N 316 
ILE   H2   H  N N 317 
ILE   HA   H  N N 318 
ILE   HB   H  N N 319 
ILE   HG12 H  N N 320 
ILE   HG13 H  N N 321 
ILE   HG21 H  N N 322 
ILE   HG22 H  N N 323 
ILE   HG23 H  N N 324 
ILE   HD11 H  N N 325 
ILE   HD12 H  N N 326 
ILE   HD13 H  N N 327 
ILE   HXT  H  N N 328 
LEU   N    N  N N 329 
LEU   CA   C  N S 330 
LEU   C    C  N N 331 
LEU   O    O  N N 332 
LEU   CB   C  N N 333 
LEU   CG   C  N N 334 
LEU   CD1  C  N N 335 
LEU   CD2  C  N N 336 
LEU   OXT  O  N N 337 
LEU   H    H  N N 338 
LEU   H2   H  N N 339 
LEU   HA   H  N N 340 
LEU   HB2  H  N N 341 
LEU   HB3  H  N N 342 
LEU   HG   H  N N 343 
LEU   HD11 H  N N 344 
LEU   HD12 H  N N 345 
LEU   HD13 H  N N 346 
LEU   HD21 H  N N 347 
LEU   HD22 H  N N 348 
LEU   HD23 H  N N 349 
LEU   HXT  H  N N 350 
LYS   N    N  N N 351 
LYS   CA   C  N S 352 
LYS   C    C  N N 353 
LYS   O    O  N N 354 
LYS   CB   C  N N 355 
LYS   CG   C  N N 356 
LYS   CD   C  N N 357 
LYS   CE   C  N N 358 
LYS   NZ   N  N N 359 
LYS   OXT  O  N N 360 
LYS   H    H  N N 361 
LYS   H2   H  N N 362 
LYS   HA   H  N N 363 
LYS   HB2  H  N N 364 
LYS   HB3  H  N N 365 
LYS   HG2  H  N N 366 
LYS   HG3  H  N N 367 
LYS   HD2  H  N N 368 
LYS   HD3  H  N N 369 
LYS   HE2  H  N N 370 
LYS   HE3  H  N N 371 
LYS   HZ1  H  N N 372 
LYS   HZ2  H  N N 373 
LYS   HZ3  H  N N 374 
LYS   HXT  H  N N 375 
MET   N    N  N N 376 
MET   CA   C  N S 377 
MET   C    C  N N 378 
MET   O    O  N N 379 
MET   CB   C  N N 380 
MET   CG   C  N N 381 
MET   SD   S  N N 382 
MET   CE   C  N N 383 
MET   OXT  O  N N 384 
MET   H    H  N N 385 
MET   H2   H  N N 386 
MET   HA   H  N N 387 
MET   HB2  H  N N 388 
MET   HB3  H  N N 389 
MET   HG2  H  N N 390 
MET   HG3  H  N N 391 
MET   HE1  H  N N 392 
MET   HE2  H  N N 393 
MET   HE3  H  N N 394 
MET   HXT  H  N N 395 
PHE   N    N  N N 396 
PHE   CA   C  N S 397 
PHE   C    C  N N 398 
PHE   O    O  N N 399 
PHE   CB   C  N N 400 
PHE   CG   C  Y N 401 
PHE   CD1  C  Y N 402 
PHE   CD2  C  Y N 403 
PHE   CE1  C  Y N 404 
PHE   CE2  C  Y N 405 
PHE   CZ   C  Y N 406 
PHE   OXT  O  N N 407 
PHE   H    H  N N 408 
PHE   H2   H  N N 409 
PHE   HA   H  N N 410 
PHE   HB2  H  N N 411 
PHE   HB3  H  N N 412 
PHE   HD1  H  N N 413 
PHE   HD2  H  N N 414 
PHE   HE1  H  N N 415 
PHE   HE2  H  N N 416 
PHE   HZ   H  N N 417 
PHE   HXT  H  N N 418 
PRO   N    N  N N 419 
PRO   CA   C  N S 420 
PRO   C    C  N N 421 
PRO   O    O  N N 422 
PRO   CB   C  N N 423 
PRO   CG   C  N N 424 
PRO   CD   C  N N 425 
PRO   OXT  O  N N 426 
PRO   H    H  N N 427 
PRO   HA   H  N N 428 
PRO   HB2  H  N N 429 
PRO   HB3  H  N N 430 
PRO   HG2  H  N N 431 
PRO   HG3  H  N N 432 
PRO   HD2  H  N N 433 
PRO   HD3  H  N N 434 
PRO   HXT  H  N N 435 
SER   N    N  N N 436 
SER   CA   C  N S 437 
SER   C    C  N N 438 
SER   O    O  N N 439 
SER   CB   C  N N 440 
SER   OG   O  N N 441 
SER   OXT  O  N N 442 
SER   H    H  N N 443 
SER   H2   H  N N 444 
SER   HA   H  N N 445 
SER   HB2  H  N N 446 
SER   HB3  H  N N 447 
SER   HG   H  N N 448 
SER   HXT  H  N N 449 
THR   N    N  N N 450 
THR   CA   C  N S 451 
THR   C    C  N N 452 
THR   O    O  N N 453 
THR   CB   C  N R 454 
THR   OG1  O  N N 455 
THR   CG2  C  N N 456 
THR   OXT  O  N N 457 
THR   H    H  N N 458 
THR   H2   H  N N 459 
THR   HA   H  N N 460 
THR   HB   H  N N 461 
THR   HG1  H  N N 462 
THR   HG21 H  N N 463 
THR   HG22 H  N N 464 
THR   HG23 H  N N 465 
THR   HXT  H  N N 466 
TRP   N    N  N N 467 
TRP   CA   C  N S 468 
TRP   C    C  N N 469 
TRP   O    O  N N 470 
TRP   CB   C  N N 471 
TRP   CG   C  Y N 472 
TRP   CD1  C  Y N 473 
TRP   CD2  C  Y N 474 
TRP   NE1  N  Y N 475 
TRP   CE2  C  Y N 476 
TRP   CE3  C  Y N 477 
TRP   CZ2  C  Y N 478 
TRP   CZ3  C  Y N 479 
TRP   CH2  C  Y N 480 
TRP   OXT  O  N N 481 
TRP   H    H  N N 482 
TRP   H2   H  N N 483 
TRP   HA   H  N N 484 
TRP   HB2  H  N N 485 
TRP   HB3  H  N N 486 
TRP   HD1  H  N N 487 
TRP   HE1  H  N N 488 
TRP   HE3  H  N N 489 
TRP   HZ2  H  N N 490 
TRP   HZ3  H  N N 491 
TRP   HH2  H  N N 492 
TRP   HXT  H  N N 493 
TYR   N    N  N N 494 
TYR   CA   C  N S 495 
TYR   C    C  N N 496 
TYR   O    O  N N 497 
TYR   CB   C  N N 498 
TYR   CG   C  Y N 499 
TYR   CD1  C  Y N 500 
TYR   CD2  C  Y N 501 
TYR   CE1  C  Y N 502 
TYR   CE2  C  Y N 503 
TYR   CZ   C  Y N 504 
TYR   OH   O  N N 505 
TYR   OXT  O  N N 506 
TYR   H    H  N N 507 
TYR   H2   H  N N 508 
TYR   HA   H  N N 509 
TYR   HB2  H  N N 510 
TYR   HB3  H  N N 511 
TYR   HD1  H  N N 512 
TYR   HD2  H  N N 513 
TYR   HE1  H  N N 514 
TYR   HE2  H  N N 515 
TYR   HH   H  N N 516 
TYR   HXT  H  N N 517 
VAL   N    N  N N 518 
VAL   CA   C  N S 519 
VAL   C    C  N N 520 
VAL   O    O  N N 521 
VAL   CB   C  N N 522 
VAL   CG1  C  N N 523 
VAL   CG2  C  N N 524 
VAL   OXT  O  N N 525 
VAL   H    H  N N 526 
VAL   H2   H  N N 527 
VAL   HA   H  N N 528 
VAL   HB   H  N N 529 
VAL   HG11 H  N N 530 
VAL   HG12 H  N N 531 
VAL   HG13 H  N N 532 
VAL   HG21 H  N N 533 
VAL   HG22 H  N N 534 
VAL   HG23 H  N N 535 
VAL   HXT  H  N N 536 
# 
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 
A1A06 F04 C02  sing N N 1   
A1A06 C40 C39  doub Y N 2   
A1A06 C40 C41  sing Y N 3   
A1A06 C39 C38  sing Y N 4   
A1A06 C08 N07  sing N N 5   
A1A06 C08 C09  sing N N 6   
A1A06 C02 F01  sing N N 7   
A1A06 C02 C05  sing N N 8   
A1A06 C02 F03  sing N N 9   
A1A06 C41 C36  doub Y N 10  
A1A06 N07 C05  sing N N 11  
A1A06 C05 O06  doub N N 12  
A1A06 C32 C31  doub Y N 13  
A1A06 C32 N33  sing Y N 14  
A1A06 C31 C30  sing Y N 15  
A1A06 C09 O10  doub N N 16  
A1A06 C09 N11  sing N N 17  
A1A06 C38 C37  doub Y N 18  
A1A06 C36 C37  sing Y N 19  
A1A06 C36 C35  sing N N 20  
A1A06 N33 C34  doub Y N 21  
A1A06 N11 C12  sing N N 22  
A1A06 C30 C29  doub Y N 23  
A1A06 C35 C12  sing N N 24  
A1A06 C12 C13  sing N N 25  
A1A06 C34 C29  sing Y N 26  
A1A06 C29 C28  sing N N 27  
A1A06 N25 C26  sing N N 28  
A1A06 N25 C23  sing N N 29  
A1A06 C13 S14  sing N N 30  
A1A06 C26 C27  sing N N 31  
A1A06 C28 C27  sing N N 32  
A1A06 C15 S14  sing N N 33  
A1A06 C15 C23  sing N N 34  
A1A06 C15 C16  sing N N 35  
A1A06 C23 O24  doub N N 36  
A1A06 C18 C19  doub Y N 37  
A1A06 C18 C17  sing Y N 38  
A1A06 C19 C20  sing Y N 39  
A1A06 C16 C17  sing N N 40  
A1A06 C17 C22  doub Y N 41  
A1A06 C20 C21  doub Y N 42  
A1A06 C22 C21  sing Y N 43  
A1A06 C08 H1   sing N N 44  
A1A06 C08 H2   sing N N 45  
A1A06 C12 H3   sing N N 46  
A1A06 C13 H4   sing N N 47  
A1A06 C13 H5   sing N N 48  
A1A06 C15 H6   sing N N 49  
A1A06 C16 H7   sing N N 50  
A1A06 C16 H8   sing N N 51  
A1A06 C18 H9   sing N N 52  
A1A06 C19 H10  sing N N 53  
A1A06 C20 H11  sing N N 54  
A1A06 C21 H12  sing N N 55  
A1A06 C22 H13  sing N N 56  
A1A06 C26 H14  sing N N 57  
A1A06 C26 H15  sing N N 58  
A1A06 C27 H16  sing N N 59  
A1A06 C27 H17  sing N N 60  
A1A06 C28 H18  sing N N 61  
A1A06 C28 H19  sing N N 62  
A1A06 C30 H20  sing N N 63  
A1A06 C31 H21  sing N N 64  
A1A06 C32 H22  sing N N 65  
A1A06 C34 H23  sing N N 66  
A1A06 C35 H24  sing N N 67  
A1A06 C35 H25  sing N N 68  
A1A06 C37 H26  sing N N 69  
A1A06 C38 H27  sing N N 70  
A1A06 C39 H28  sing N N 71  
A1A06 C40 H29  sing N N 72  
A1A06 C41 H30  sing N N 73  
A1A06 N07 H31  sing N N 74  
A1A06 N11 H32  sing N N 75  
A1A06 N25 H33  sing N N 76  
ALA   N   CA   sing N N 77  
ALA   N   H    sing N N 78  
ALA   N   H2   sing N N 79  
ALA   CA  C    sing N N 80  
ALA   CA  CB   sing N N 81  
ALA   CA  HA   sing N N 82  
ALA   C   O    doub N N 83  
ALA   C   OXT  sing N N 84  
ALA   CB  HB1  sing N N 85  
ALA   CB  HB2  sing N N 86  
ALA   CB  HB3  sing N N 87  
ALA   OXT HXT  sing N N 88  
ARG   N   CA   sing N N 89  
ARG   N   H    sing N N 90  
ARG   N   H2   sing N N 91  
ARG   CA  C    sing N N 92  
ARG   CA  CB   sing N N 93  
ARG   CA  HA   sing N N 94  
ARG   C   O    doub N N 95  
ARG   C   OXT  sing N N 96  
ARG   CB  CG   sing N N 97  
ARG   CB  HB2  sing N N 98  
ARG   CB  HB3  sing N N 99  
ARG   CG  CD   sing N N 100 
ARG   CG  HG2  sing N N 101 
ARG   CG  HG3  sing N N 102 
ARG   CD  NE   sing N N 103 
ARG   CD  HD2  sing N N 104 
ARG   CD  HD3  sing N N 105 
ARG   NE  CZ   sing N N 106 
ARG   NE  HE   sing N N 107 
ARG   CZ  NH1  sing N N 108 
ARG   CZ  NH2  doub N N 109 
ARG   NH1 HH11 sing N N 110 
ARG   NH1 HH12 sing N N 111 
ARG   NH2 HH21 sing N N 112 
ARG   NH2 HH22 sing N N 113 
ARG   OXT HXT  sing N N 114 
ASN   N   CA   sing N N 115 
ASN   N   H    sing N N 116 
ASN   N   H2   sing N N 117 
ASN   CA  C    sing N N 118 
ASN   CA  CB   sing N N 119 
ASN   CA  HA   sing N N 120 
ASN   C   O    doub N N 121 
ASN   C   OXT  sing N N 122 
ASN   CB  CG   sing N N 123 
ASN   CB  HB2  sing N N 124 
ASN   CB  HB3  sing N N 125 
ASN   CG  OD1  doub N N 126 
ASN   CG  ND2  sing N N 127 
ASN   ND2 HD21 sing N N 128 
ASN   ND2 HD22 sing N N 129 
ASN   OXT HXT  sing N N 130 
ASP   N   CA   sing N N 131 
ASP   N   H    sing N N 132 
ASP   N   H2   sing N N 133 
ASP   CA  C    sing N N 134 
ASP   CA  CB   sing N N 135 
ASP   CA  HA   sing N N 136 
ASP   C   O    doub N N 137 
ASP   C   OXT  sing N N 138 
ASP   CB  CG   sing N N 139 
ASP   CB  HB2  sing N N 140 
ASP   CB  HB3  sing N N 141 
ASP   CG  OD1  doub N N 142 
ASP   CG  OD2  sing N N 143 
ASP   OD2 HD2  sing N N 144 
ASP   OXT HXT  sing N N 145 
CYS   N   CA   sing N N 146 
CYS   N   H    sing N N 147 
CYS   N   H2   sing N N 148 
CYS   CA  C    sing N N 149 
CYS   CA  CB   sing N N 150 
CYS   CA  HA   sing N N 151 
CYS   C   O    doub N N 152 
CYS   C   OXT  sing N N 153 
CYS   CB  SG   sing N N 154 
CYS   CB  HB2  sing N N 155 
CYS   CB  HB3  sing N N 156 
CYS   SG  HG   sing N N 157 
CYS   OXT HXT  sing N N 158 
GLN   N   CA   sing N N 159 
GLN   N   H    sing N N 160 
GLN   N   H2   sing N N 161 
GLN   CA  C    sing N N 162 
GLN   CA  CB   sing N N 163 
GLN   CA  HA   sing N N 164 
GLN   C   O    doub N N 165 
GLN   C   OXT  sing N N 166 
GLN   CB  CG   sing N N 167 
GLN   CB  HB2  sing N N 168 
GLN   CB  HB3  sing N N 169 
GLN   CG  CD   sing N N 170 
GLN   CG  HG2  sing N N 171 
GLN   CG  HG3  sing N N 172 
GLN   CD  OE1  doub N N 173 
GLN   CD  NE2  sing N N 174 
GLN   NE2 HE21 sing N N 175 
GLN   NE2 HE22 sing N N 176 
GLN   OXT HXT  sing N N 177 
GLU   N   CA   sing N N 178 
GLU   N   H    sing N N 179 
GLU   N   H2   sing N N 180 
GLU   CA  C    sing N N 181 
GLU   CA  CB   sing N N 182 
GLU   CA  HA   sing N N 183 
GLU   C   O    doub N N 184 
GLU   C   OXT  sing N N 185 
GLU   CB  CG   sing N N 186 
GLU   CB  HB2  sing N N 187 
GLU   CB  HB3  sing N N 188 
GLU   CG  CD   sing N N 189 
GLU   CG  HG2  sing N N 190 
GLU   CG  HG3  sing N N 191 
GLU   CD  OE1  doub N N 192 
GLU   CD  OE2  sing N N 193 
GLU   OE2 HE2  sing N N 194 
GLU   OXT HXT  sing N N 195 
GLY   N   CA   sing N N 196 
GLY   N   H    sing N N 197 
GLY   N   H2   sing N N 198 
GLY   CA  C    sing N N 199 
GLY   CA  HA2  sing N N 200 
GLY   CA  HA3  sing N N 201 
GLY   C   O    doub N N 202 
GLY   C   OXT  sing N N 203 
GLY   OXT HXT  sing N N 204 
HEM   CHA C1A  sing N N 205 
HEM   CHA C4D  doub N N 206 
HEM   CHA HHA  sing N N 207 
HEM   CHB C4A  sing N N 208 
HEM   CHB C1B  doub N N 209 
HEM   CHB HHB  sing N N 210 
HEM   CHC C4B  sing N N 211 
HEM   CHC C1C  doub N N 212 
HEM   CHC HHC  sing N N 213 
HEM   CHD C4C  doub N N 214 
HEM   CHD C1D  sing N N 215 
HEM   CHD HHD  sing N N 216 
HEM   C1A C2A  doub Y N 217 
HEM   C1A NA   sing Y N 218 
HEM   C2A C3A  sing Y N 219 
HEM   C2A CAA  sing N N 220 
HEM   C3A C4A  doub Y N 221 
HEM   C3A CMA  sing N N 222 
HEM   C4A NA   sing Y N 223 
HEM   CMA HMA  sing N N 224 
HEM   CMA HMAA sing N N 225 
HEM   CMA HMAB sing N N 226 
HEM   CAA CBA  sing N N 227 
HEM   CAA HAA  sing N N 228 
HEM   CAA HAAA sing N N 229 
HEM   CBA CGA  sing N N 230 
HEM   CBA HBA  sing N N 231 
HEM   CBA HBAA sing N N 232 
HEM   CGA O1A  doub N N 233 
HEM   CGA O2A  sing N N 234 
HEM   C1B C2B  sing N N 235 
HEM   C1B NB   sing N N 236 
HEM   C2B C3B  doub N N 237 
HEM   C2B CMB  sing N N 238 
HEM   C3B C4B  sing N N 239 
HEM   C3B CAB  sing N N 240 
HEM   C4B NB   doub N N 241 
HEM   CMB HMB  sing N N 242 
HEM   CMB HMBA sing N N 243 
HEM   CMB HMBB sing N N 244 
HEM   CAB CBB  doub N N 245 
HEM   CAB HAB  sing N N 246 
HEM   CBB HBB  sing N N 247 
HEM   CBB HBBA sing N N 248 
HEM   C1C C2C  sing Y N 249 
HEM   C1C NC   sing Y N 250 
HEM   C2C C3C  doub Y N 251 
HEM   C2C CMC  sing N N 252 
HEM   C3C C4C  sing Y N 253 
HEM   C3C CAC  sing N N 254 
HEM   C4C NC   sing Y N 255 
HEM   CMC HMC  sing N N 256 
HEM   CMC HMCA sing N N 257 
HEM   CMC HMCB sing N N 258 
HEM   CAC CBC  doub N N 259 
HEM   CAC HAC  sing N N 260 
HEM   CBC HBC  sing N N 261 
HEM   CBC HBCA sing N N 262 
HEM   C1D C2D  sing N N 263 
HEM   C1D ND   doub N N 264 
HEM   C2D C3D  doub N N 265 
HEM   C2D CMD  sing N N 266 
HEM   C3D C4D  sing N N 267 
HEM   C3D CAD  sing N N 268 
HEM   C4D ND   sing N N 269 
HEM   CMD HMD  sing N N 270 
HEM   CMD HMDA sing N N 271 
HEM   CMD HMDB sing N N 272 
HEM   CAD CBD  sing N N 273 
HEM   CAD HAD  sing N N 274 
HEM   CAD HADA sing N N 275 
HEM   CBD CGD  sing N N 276 
HEM   CBD HBD  sing N N 277 
HEM   CBD HBDA sing N N 278 
HEM   CGD O1D  doub N N 279 
HEM   CGD O2D  sing N N 280 
HEM   O2A H2A  sing N N 281 
HEM   O2D H2D  sing N N 282 
HEM   FE  NA   sing N N 283 
HEM   FE  NB   sing N N 284 
HEM   FE  NC   sing N N 285 
HEM   FE  ND   sing N N 286 
HIS   N   CA   sing N N 287 
HIS   N   H    sing N N 288 
HIS   N   H2   sing N N 289 
HIS   CA  C    sing N N 290 
HIS   CA  CB   sing N N 291 
HIS   CA  HA   sing N N 292 
HIS   C   O    doub N N 293 
HIS   C   OXT  sing N N 294 
HIS   CB  CG   sing N N 295 
HIS   CB  HB2  sing N N 296 
HIS   CB  HB3  sing N N 297 
HIS   CG  ND1  sing Y N 298 
HIS   CG  CD2  doub Y N 299 
HIS   ND1 CE1  doub Y N 300 
HIS   ND1 HD1  sing N N 301 
HIS   CD2 NE2  sing Y N 302 
HIS   CD2 HD2  sing N N 303 
HIS   CE1 NE2  sing Y N 304 
HIS   CE1 HE1  sing N N 305 
HIS   NE2 HE2  sing N N 306 
HIS   OXT HXT  sing N N 307 
ILE   N   CA   sing N N 308 
ILE   N   H    sing N N 309 
ILE   N   H2   sing N N 310 
ILE   CA  C    sing N N 311 
ILE   CA  CB   sing N N 312 
ILE   CA  HA   sing N N 313 
ILE   C   O    doub N N 314 
ILE   C   OXT  sing N N 315 
ILE   CB  CG1  sing N N 316 
ILE   CB  CG2  sing N N 317 
ILE   CB  HB   sing N N 318 
ILE   CG1 CD1  sing N N 319 
ILE   CG1 HG12 sing N N 320 
ILE   CG1 HG13 sing N N 321 
ILE   CG2 HG21 sing N N 322 
ILE   CG2 HG22 sing N N 323 
ILE   CG2 HG23 sing N N 324 
ILE   CD1 HD11 sing N N 325 
ILE   CD1 HD12 sing N N 326 
ILE   CD1 HD13 sing N N 327 
ILE   OXT HXT  sing N N 328 
LEU   N   CA   sing N N 329 
LEU   N   H    sing N N 330 
LEU   N   H2   sing N N 331 
LEU   CA  C    sing N N 332 
LEU   CA  CB   sing N N 333 
LEU   CA  HA   sing N N 334 
LEU   C   O    doub N N 335 
LEU   C   OXT  sing N N 336 
LEU   CB  CG   sing N N 337 
LEU   CB  HB2  sing N N 338 
LEU   CB  HB3  sing N N 339 
LEU   CG  CD1  sing N N 340 
LEU   CG  CD2  sing N N 341 
LEU   CG  HG   sing N N 342 
LEU   CD1 HD11 sing N N 343 
LEU   CD1 HD12 sing N N 344 
LEU   CD1 HD13 sing N N 345 
LEU   CD2 HD21 sing N N 346 
LEU   CD2 HD22 sing N N 347 
LEU   CD2 HD23 sing N N 348 
LEU   OXT HXT  sing N N 349 
LYS   N   CA   sing N N 350 
LYS   N   H    sing N N 351 
LYS   N   H2   sing N N 352 
LYS   CA  C    sing N N 353 
LYS   CA  CB   sing N N 354 
LYS   CA  HA   sing N N 355 
LYS   C   O    doub N N 356 
LYS   C   OXT  sing N N 357 
LYS   CB  CG   sing N N 358 
LYS   CB  HB2  sing N N 359 
LYS   CB  HB3  sing N N 360 
LYS   CG  CD   sing N N 361 
LYS   CG  HG2  sing N N 362 
LYS   CG  HG3  sing N N 363 
LYS   CD  CE   sing N N 364 
LYS   CD  HD2  sing N N 365 
LYS   CD  HD3  sing N N 366 
LYS   CE  NZ   sing N N 367 
LYS   CE  HE2  sing N N 368 
LYS   CE  HE3  sing N N 369 
LYS   NZ  HZ1  sing N N 370 
LYS   NZ  HZ2  sing N N 371 
LYS   NZ  HZ3  sing N N 372 
LYS   OXT HXT  sing N N 373 
MET   N   CA   sing N N 374 
MET   N   H    sing N N 375 
MET   N   H2   sing N N 376 
MET   CA  C    sing N N 377 
MET   CA  CB   sing N N 378 
MET   CA  HA   sing N N 379 
MET   C   O    doub N N 380 
MET   C   OXT  sing N N 381 
MET   CB  CG   sing N N 382 
MET   CB  HB2  sing N N 383 
MET   CB  HB3  sing N N 384 
MET   CG  SD   sing N N 385 
MET   CG  HG2  sing N N 386 
MET   CG  HG3  sing N N 387 
MET   SD  CE   sing N N 388 
MET   CE  HE1  sing N N 389 
MET   CE  HE2  sing N N 390 
MET   CE  HE3  sing N N 391 
MET   OXT HXT  sing N N 392 
PHE   N   CA   sing N N 393 
PHE   N   H    sing N N 394 
PHE   N   H2   sing N N 395 
PHE   CA  C    sing N N 396 
PHE   CA  CB   sing N N 397 
PHE   CA  HA   sing N N 398 
PHE   C   O    doub N N 399 
PHE   C   OXT  sing N N 400 
PHE   CB  CG   sing N N 401 
PHE   CB  HB2  sing N N 402 
PHE   CB  HB3  sing N N 403 
PHE   CG  CD1  doub Y N 404 
PHE   CG  CD2  sing Y N 405 
PHE   CD1 CE1  sing Y N 406 
PHE   CD1 HD1  sing N N 407 
PHE   CD2 CE2  doub Y N 408 
PHE   CD2 HD2  sing N N 409 
PHE   CE1 CZ   doub Y N 410 
PHE   CE1 HE1  sing N N 411 
PHE   CE2 CZ   sing Y N 412 
PHE   CE2 HE2  sing N N 413 
PHE   CZ  HZ   sing N N 414 
PHE   OXT HXT  sing N N 415 
PRO   N   CA   sing N N 416 
PRO   N   CD   sing N N 417 
PRO   N   H    sing N N 418 
PRO   CA  C    sing N N 419 
PRO   CA  CB   sing N N 420 
PRO   CA  HA   sing N N 421 
PRO   C   O    doub N N 422 
PRO   C   OXT  sing N N 423 
PRO   CB  CG   sing N N 424 
PRO   CB  HB2  sing N N 425 
PRO   CB  HB3  sing N N 426 
PRO   CG  CD   sing N N 427 
PRO   CG  HG2  sing N N 428 
PRO   CG  HG3  sing N N 429 
PRO   CD  HD2  sing N N 430 
PRO   CD  HD3  sing N N 431 
PRO   OXT HXT  sing N N 432 
SER   N   CA   sing N N 433 
SER   N   H    sing N N 434 
SER   N   H2   sing N N 435 
SER   CA  C    sing N N 436 
SER   CA  CB   sing N N 437 
SER   CA  HA   sing N N 438 
SER   C   O    doub N N 439 
SER   C   OXT  sing N N 440 
SER   CB  OG   sing N N 441 
SER   CB  HB2  sing N N 442 
SER   CB  HB3  sing N N 443 
SER   OG  HG   sing N N 444 
SER   OXT HXT  sing N N 445 
THR   N   CA   sing N N 446 
THR   N   H    sing N N 447 
THR   N   H2   sing N N 448 
THR   CA  C    sing N N 449 
THR   CA  CB   sing N N 450 
THR   CA  HA   sing N N 451 
THR   C   O    doub N N 452 
THR   C   OXT  sing N N 453 
THR   CB  OG1  sing N N 454 
THR   CB  CG2  sing N N 455 
THR   CB  HB   sing N N 456 
THR   OG1 HG1  sing N N 457 
THR   CG2 HG21 sing N N 458 
THR   CG2 HG22 sing N N 459 
THR   CG2 HG23 sing N N 460 
THR   OXT HXT  sing N N 461 
TRP   N   CA   sing N N 462 
TRP   N   H    sing N N 463 
TRP   N   H2   sing N N 464 
TRP   CA  C    sing N N 465 
TRP   CA  CB   sing N N 466 
TRP   CA  HA   sing N N 467 
TRP   C   O    doub N N 468 
TRP   C   OXT  sing N N 469 
TRP   CB  CG   sing N N 470 
TRP   CB  HB2  sing N N 471 
TRP   CB  HB3  sing N N 472 
TRP   CG  CD1  doub Y N 473 
TRP   CG  CD2  sing Y N 474 
TRP   CD1 NE1  sing Y N 475 
TRP   CD1 HD1  sing N N 476 
TRP   CD2 CE2  doub Y N 477 
TRP   CD2 CE3  sing Y N 478 
TRP   NE1 CE2  sing Y N 479 
TRP   NE1 HE1  sing N N 480 
TRP   CE2 CZ2  sing Y N 481 
TRP   CE3 CZ3  doub Y N 482 
TRP   CE3 HE3  sing N N 483 
TRP   CZ2 CH2  doub Y N 484 
TRP   CZ2 HZ2  sing N N 485 
TRP   CZ3 CH2  sing Y N 486 
TRP   CZ3 HZ3  sing N N 487 
TRP   CH2 HH2  sing N N 488 
TRP   OXT HXT  sing N N 489 
TYR   N   CA   sing N N 490 
TYR   N   H    sing N N 491 
TYR   N   H2   sing N N 492 
TYR   CA  C    sing N N 493 
TYR   CA  CB   sing N N 494 
TYR   CA  HA   sing N N 495 
TYR   C   O    doub N N 496 
TYR   C   OXT  sing N N 497 
TYR   CB  CG   sing N N 498 
TYR   CB  HB2  sing N N 499 
TYR   CB  HB3  sing N N 500 
TYR   CG  CD1  doub Y N 501 
TYR   CG  CD2  sing Y N 502 
TYR   CD1 CE1  sing Y N 503 
TYR   CD1 HD1  sing N N 504 
TYR   CD2 CE2  doub Y N 505 
TYR   CD2 HD2  sing N N 506 
TYR   CE1 CZ   doub Y N 507 
TYR   CE1 HE1  sing N N 508 
TYR   CE2 CZ   sing Y N 509 
TYR   CE2 HE2  sing N N 510 
TYR   CZ  OH   sing N N 511 
TYR   OH  HH   sing N N 512 
TYR   OXT HXT  sing N N 513 
VAL   N   CA   sing N N 514 
VAL   N   H    sing N N 515 
VAL   N   H2   sing N N 516 
VAL   CA  C    sing N N 517 
VAL   CA  CB   sing N N 518 
VAL   CA  HA   sing N N 519 
VAL   C   O    doub N N 520 
VAL   C   OXT  sing N N 521 
VAL   CB  CG1  sing N N 522 
VAL   CB  CG2  sing N N 523 
VAL   CB  HB   sing N N 524 
VAL   CG1 HG11 sing N N 525 
VAL   CG1 HG12 sing N N 526 
VAL   CG1 HG13 sing N N 527 
VAL   CG2 HG21 sing N N 528 
VAL   CG2 HG22 sing N N 529 
VAL   CG2 HG23 sing N N 530 
VAL   OXT HXT  sing N N 531 
# 
_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                    9COS 
_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]   0.013125 
_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]   0.009984 
_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]   0.008017 
_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   . SER   A 1 9   ? -11.627 -59.150 -14.433 1.00 142.37 ? 29  SER   A N   1 
ATOM   2    C  CA  . SER   A 1 9   ? -12.494 -57.958 -14.440 1.00 134.12 ? 29  SER   A CA  1 
ATOM   3    C  C   . SER   A 1 9   ? -12.426 -57.087 -15.701 1.00 128.40 ? 29  SER   A C   1 
ATOM   4    O  O   . SER   A 1 9   ? -13.170 -56.113 -15.817 1.00 104.60 ? 29  SER   A O   1 
ATOM   5    C  CB  . SER   A 1 9   ? -12.206 -57.083 -13.212 1.00 125.56 ? 29  SER   A CB  1 
ATOM   6    O  OG  . SER   A 1 9   ? -12.852 -55.827 -13.321 1.00 129.15 ? 29  SER   A OG  1 
ATOM   7    N  N   . HIS   A 1 10  ? -11.559 -57.439 -16.648 1.00 123.76 ? 30  HIS   A N   1 
ATOM   8    C  CA  . HIS   A 1 10  ? -11.391 -56.660 -17.868 1.00 121.01 ? 30  HIS   A CA  1 
ATOM   9    C  C   . HIS   A 1 10  ? -12.240 -57.168 -19.026 1.00 124.69 ? 30  HIS   A C   1 
ATOM   10   O  O   . HIS   A 1 10  ? -12.195 -56.581 -20.111 1.00 128.38 ? 30  HIS   A O   1 
ATOM   11   C  CB  . HIS   A 1 10  ? -9.913  -56.635 -18.285 1.00 123.88 ? 30  HIS   A CB  1 
ATOM   12   C  CG  . HIS   A 1 10  ? -9.140  -55.484 -17.717 1.00 119.14 ? 30  HIS   A CG  1 
ATOM   13   N  ND1 . HIS   A 1 10  ? -9.405  -54.949 -16.474 1.00 122.54 ? 30  HIS   A ND1 1 
ATOM   14   C  CD2 . HIS   A 1 10  ? -8.115  -54.761 -18.228 1.00 117.88 ? 30  HIS   A CD2 1 
ATOM   15   C  CE1 . HIS   A 1 10  ? -8.572  -53.950 -16.243 1.00 116.94 ? 30  HIS   A CE1 1 
ATOM   16   N  NE2 . HIS   A 1 10  ? -7.780  -53.814 -17.291 1.00 113.97 ? 30  HIS   A NE2 1 
ATOM   17   N  N   . GLY   A 1 11  ? -13.012 -58.235 -18.826 1.00 118.09 ? 31  GLY   A N   1 
ATOM   18   C  CA  . GLY   A 1 11  ? -13.874 -58.767 -19.861 1.00 121.60 ? 31  GLY   A CA  1 
ATOM   19   C  C   . GLY   A 1 11  ? -15.354 -58.502 -19.694 1.00 123.12 ? 31  GLY   A C   1 
ATOM   20   O  O   . GLY   A 1 11  ? -16.156 -59.092 -20.430 1.00 126.01 ? 31  GLY   A O   1 
ATOM   21   N  N   . LEU   A 1 12  ? -15.752 -57.634 -18.759 1.00 114.83 ? 32  LEU   A N   1 
ATOM   22   C  CA  . LEU   A 1 12  ? -17.170 -57.376 -18.523 1.00 117.61 ? 32  LEU   A CA  1 
ATOM   23   C  C   . LEU   A 1 12  ? -17.862 -56.891 -19.793 1.00 116.69 ? 32  LEU   A C   1 
ATOM   24   O  O   . LEU   A 1 12  ? -18.860 -57.473 -20.238 1.00 116.18 ? 32  LEU   A O   1 
ATOM   25   C  CB  . LEU   A 1 12  ? -17.334 -56.352 -17.398 1.00 107.01 ? 32  LEU   A CB  1 
ATOM   26   C  CG  . LEU   A 1 12  ? -18.696 -55.671 -17.231 1.00 109.89 ? 32  LEU   A CG  1 
ATOM   27   C  CD1 . LEU   A 1 12  ? -19.813 -56.691 -17.033 1.00 117.86 ? 32  LEU   A CD1 1 
ATOM   28   C  CD2 . LEU   A 1 12  ? -18.652 -54.685 -16.076 1.00 109.63 ? 32  LEU   A CD2 1 
ATOM   29   N  N   . PHE   A 1 13  ? -17.344 -55.816 -20.392 1.00 108.30 ? 33  PHE   A N   1 
ATOM   30   C  CA  . PHE   A 1 13  ? -17.978 -55.256 -21.580 1.00 103.78 ? 33  PHE   A CA  1 
ATOM   31   C  C   . PHE   A 1 13  ? -17.891 -56.207 -22.766 1.00 110.10 ? 33  PHE   A C   1 
ATOM   32   O  O   . PHE   A 1 13  ? -18.750 -56.166 -23.655 1.00 108.79 ? 33  PHE   A O   1 
ATOM   33   C  CB  . PHE   A 1 13  ? -17.351 -53.903 -21.913 1.00 97.90  ? 33  PHE   A CB  1 
ATOM   34   C  CG  . PHE   A 1 13  ? -17.611 -52.852 -20.873 1.00 100.31 ? 33  PHE   A CG  1 
ATOM   35   C  CD1 . PHE   A 1 13  ? -18.905 -52.563 -20.473 1.00 100.25 ? 33  PHE   A CD1 1 
ATOM   36   C  CD2 . PHE   A 1 13  ? -16.564 -52.165 -20.282 1.00 91.23  ? 33  PHE   A CD2 1 
ATOM   37   C  CE1 . PHE   A 1 13  ? -19.152 -51.602 -19.512 1.00 90.70  ? 33  PHE   A CE1 1 
ATOM   38   C  CE2 . PHE   A 1 13  ? -16.805 -51.203 -19.319 1.00 90.43  ? 33  PHE   A CE2 1 
ATOM   39   C  CZ  . PHE   A 1 13  ? -18.100 -50.921 -18.934 1.00 87.52  ? 33  PHE   A CZ  1 
ATOM   40   N  N   . LYS   A 1 14  ? -16.871 -57.068 -22.799 1.00 116.83 ? 34  LYS   A N   1 
ATOM   41   C  CA  . LYS   A 1 14  ? -16.859 -58.156 -23.770 1.00 119.40 ? 34  LYS   A CA  1 
ATOM   42   C  C   . LYS   A 1 14  ? -18.018 -59.111 -23.513 1.00 118.80 ? 34  LYS   A C   1 
ATOM   43   O  O   . LYS   A 1 14  ? -18.723 -59.521 -24.442 1.00 121.47 ? 34  LYS   A O   1 
ATOM   44   C  CB  . LYS   A 1 14  ? -15.526 -58.906 -23.705 1.00 125.96 ? 34  LYS   A CB  1 
ATOM   45   C  CG  . LYS   A 1 14  ? -15.645 -60.410 -23.948 1.00 136.76 ? 34  LYS   A CG  1 
ATOM   46   C  CD  . LYS   A 1 14  ? -14.565 -61.197 -23.219 1.00 139.54 ? 34  LYS   A CD  1 
ATOM   47   C  CE  . LYS   A 1 14  ? -15.053 -61.666 -21.856 1.00 141.34 ? 34  LYS   A CE  1 
ATOM   48   N  NZ  . LYS   A 1 14  ? -14.081 -62.570 -21.183 1.00 142.75 ? 34  LYS   A NZ  1 
ATOM   49   N  N   . LYS   A 1 15  ? -18.235 -59.462 -22.244 1.00 112.20 ? 35  LYS   A N   1 
ATOM   50   C  CA  . LYS   A 1 15  ? -19.284 -60.413 -21.893 1.00 113.02 ? 35  LYS   A CA  1 
ATOM   51   C  C   . LYS   A 1 15  ? -20.668 -59.845 -22.176 1.00 110.31 ? 35  LYS   A C   1 
ATOM   52   O  O   . LYS   A 1 15  ? -21.535 -60.542 -22.716 1.00 129.48 ? 35  LYS   A O   1 
ATOM   53   C  CB  . LYS   A 1 15  ? -19.153 -60.799 -20.420 1.00 114.83 ? 35  LYS   A CB  1 
ATOM   54   C  CG  . LYS   A 1 15  ? -20.383 -61.473 -19.830 1.00 121.05 ? 35  LYS   A CG  1 
ATOM   55   C  CD  . LYS   A 1 15  ? -20.380 -61.450 -18.298 1.00 128.93 ? 35  LYS   A CD  1 
ATOM   56   C  CE  . LYS   A 1 15  ? -18.985 -61.557 -17.677 1.00 143.91 ? 35  LYS   A CE  1 
ATOM   57   N  NZ  . LYS   A 1 15  ? -18.177 -62.708 -18.184 1.00 154.32 ? 35  LYS   A NZ  1 
ATOM   58   N  N   . LEU   A 1 16  ? -20.895 -58.581 -21.824 1.00 115.93 ? 36  LEU   A N   1 
ATOM   59   C  CA  . LEU   A 1 16  ? -22.204 -57.964 -21.990 1.00 108.00 ? 36  LEU   A CA  1 
ATOM   60   C  C   . LEU   A 1 16  ? -22.491 -57.538 -23.423 1.00 106.30 ? 36  LEU   A C   1 
ATOM   61   O  O   . LEU   A 1 16  ? -23.566 -56.983 -23.680 1.00 112.24 ? 36  LEU   A O   1 
ATOM   62   C  CB  . LEU   A 1 16  ? -22.334 -56.755 -21.062 1.00 107.20 ? 36  LEU   A CB  1 
ATOM   63   C  CG  . LEU   A 1 16  ? -22.862 -57.093 -19.669 1.00 111.92 ? 36  LEU   A CG  1 
ATOM   64   C  CD1 . LEU   A 1 16  ? -22.954 -55.846 -18.802 1.00 105.80 ? 36  LEU   A CD1 1 
ATOM   65   C  CD2 . LEU   A 1 16  ? -24.206 -57.790 -19.779 1.00 116.42 ? 36  LEU   A CD2 1 
ATOM   66   N  N   . GLY   A 1 17  ? -21.573 -57.781 -24.355 1.00 105.46 ? 37  GLY   A N   1 
ATOM   67   C  CA  . GLY   A 1 17  ? -21.783 -57.361 -25.727 1.00 108.48 ? 37  GLY   A CA  1 
ATOM   68   C  C   . GLY   A 1 17  ? -21.843 -55.862 -25.912 1.00 102.62 ? 37  GLY   A C   1 
ATOM   69   O  O   . GLY   A 1 17  ? -22.578 -55.379 -26.780 1.00 105.76 ? 37  GLY   A O   1 
ATOM   70   N  N   . ILE   A 1 18  ? -21.095 -55.113 -25.115 1.00 106.57 ? 38  ILE   A N   1 
ATOM   71   C  CA  . ILE   A 1 18  ? -21.073 -53.654 -25.163 1.00 108.89 ? 38  ILE   A CA  1 
ATOM   72   C  C   . ILE   A 1 18  ? -19.772 -53.231 -25.831 1.00 101.69 ? 38  ILE   A C   1 
ATOM   73   O  O   . ILE   A 1 18  ? -18.689 -53.544 -25.318 1.00 89.64  ? 38  ILE   A O   1 
ATOM   74   C  CB  . ILE   A 1 18  ? -21.200 -53.044 -23.758 1.00 109.03 ? 38  ILE   A CB  1 
ATOM   75   C  CG1 . ILE   A 1 18  ? -22.398 -53.654 -23.027 1.00 99.61  ? 38  ILE   A CG1 1 
ATOM   76   C  CG2 . ILE   A 1 18  ? -21.321 -51.529 -23.848 1.00 98.34  ? 38  ILE   A CG2 1 
ATOM   77   C  CD1 . ILE   A 1 18  ? -22.946 -52.804 -21.901 1.00 104.69 ? 38  ILE   A CD1 1 
ATOM   78   N  N   . PRO   A 1 19  ? -19.819 -52.532 -26.963 1.00 98.86  ? 39  PRO   A N   1 
ATOM   79   C  CA  . PRO   A 1 19  ? -18.582 -52.172 -27.663 1.00 101.60 ? 39  PRO   A CA  1 
ATOM   80   C  C   . PRO   A 1 19  ? -17.744 -51.198 -26.851 1.00 111.51 ? 39  PRO   A C   1 
ATOM   81   O  O   . PRO   A 1 19  ? -18.239 -50.472 -25.987 1.00 109.02 ? 39  PRO   A O   1 
ATOM   82   C  CB  . PRO   A 1 19  ? -19.073 -51.527 -28.964 1.00 100.23 ? 39  PRO   A CB  1 
ATOM   83   C  CG  . PRO   A 1 19  ? -20.470 -51.095 -28.688 1.00 98.69  ? 39  PRO   A CG  1 
ATOM   84   C  CD  . PRO   A 1 19  ? -21.022 -51.987 -27.616 1.00 96.87  ? 39  PRO   A CD  1 
ATOM   85   N  N   . GLY   A 1 20  ? -16.448 -51.194 -27.143 1.00 112.62 ? 40  GLY   A N   1 
ATOM   86   C  CA  . GLY   A 1 20  ? -15.531 -50.309 -26.470 1.00 114.69 ? 40  GLY   A CA  1 
ATOM   87   C  C   . GLY   A 1 20  ? -14.093 -50.510 -26.897 1.00 115.29 ? 40  GLY   A C   1 
ATOM   88   O  O   . GLY   A 1 20  ? -13.743 -51.500 -27.547 1.00 119.70 ? 40  GLY   A O   1 
ATOM   89   N  N   . PRO   A 1 21  ? -13.230 -49.563 -26.540 1.00 122.92 ? 41  PRO   A N   1 
ATOM   90   C  CA  . PRO   A 1 21  ? -11.803 -49.723 -26.833 1.00 108.94 ? 41  PRO   A CA  1 
ATOM   91   C  C   . PRO   A 1 21  ? -11.195 -50.829 -25.987 1.00 109.14 ? 41  PRO   A C   1 
ATOM   92   O  O   . PRO   A 1 21  ? -11.573 -51.043 -24.833 1.00 106.00 ? 41  PRO   A O   1 
ATOM   93   C  CB  . PRO   A 1 21  ? -11.209 -48.356 -26.480 1.00 110.30 ? 41  PRO   A CB  1 
ATOM   94   C  CG  . PRO   A 1 21  ? -12.155 -47.772 -25.485 1.00 97.59  ? 41  PRO   A CG  1 
ATOM   95   C  CD  . PRO   A 1 21  ? -13.517 -48.345 -25.762 1.00 98.47  ? 41  PRO   A CD  1 
ATOM   96   N  N   . THR   A 1 22  ? -10.248 -51.540 -26.580 1.00 112.72 ? 42  THR   A N   1 
ATOM   97   C  CA  . THR   A 1 22  ? -9.648  -52.693 -25.917 1.00 108.56 ? 42  THR   A CA  1 
ATOM   98   C  C   . THR   A 1 22  ? -8.753  -52.232 -24.774 1.00 102.70 ? 42  THR   A C   1 
ATOM   99   O  O   . THR   A 1 22  ? -7.782  -51.504 -25.014 1.00 101.98 ? 42  THR   A O   1 
ATOM   100  C  CB  . THR   A 1 22  ? -8.853  -53.525 -26.916 1.00 108.40 ? 42  THR   A CB  1 
ATOM   101  O  OG1 . THR   A 1 22  ? -9.598  -53.646 -28.134 1.00 118.10 ? 42  THR   A OG1 1 
ATOM   102  C  CG2 . THR   A 1 22  ? -8.593  -54.913 -26.354 1.00 97.93  ? 42  THR   A CG2 1 
ATOM   103  N  N   . PRO   A 1 23  ? -9.032  -52.624 -23.535 1.00 93.79  ? 43  PRO   A N   1 
ATOM   104  C  CA  . PRO   A 1 23  ? -8.239  -52.132 -22.407 1.00 101.46 ? 43  PRO   A CA  1 
ATOM   105  C  C   . PRO   A 1 23  ? -6.899  -52.838 -22.288 1.00 106.39 ? 43  PRO   A C   1 
ATOM   106  O  O   . PRO   A 1 23  ? -6.755  -54.022 -22.601 1.00 111.04 ? 43  PRO   A O   1 
ATOM   107  C  CB  . PRO   A 1 23  ? -9.130  -52.445 -21.200 1.00 96.21  ? 43  PRO   A CB  1 
ATOM   108  C  CG  . PRO   A 1 23  ? -9.855  -53.681 -21.619 1.00 94.78  ? 43  PRO   A CG  1 
ATOM   109  C  CD  . PRO   A 1 23  ? -10.142 -53.485 -23.090 1.00 95.21  ? 43  PRO   A CD  1 
ATOM   110  N  N   . LEU   A 1 24  ? -5.911  -52.083 -21.831 1.00 97.97  ? 44  LEU   A N   1 
ATOM   111  C  CA  . LEU   A 1 24  ? -4.618  -52.651 -21.495 1.00 91.33  ? 44  LEU   A CA  1 
ATOM   112  C  C   . LEU   A 1 24  ? -4.625  -53.140 -20.054 1.00 96.08  ? 44  LEU   A C   1 
ATOM   113  O  O   . LEU   A 1 24  ? -5.419  -52.671 -19.233 1.00 97.60  ? 44  LEU   A O   1 
ATOM   114  C  CB  . LEU   A 1 24  ? -3.517  -51.610 -21.693 1.00 85.89  ? 44  LEU   A CB  1 
ATOM   115  C  CG  . LEU   A 1 24  ? -3.171  -51.265 -23.143 1.00 86.92  ? 44  LEU   A CG  1 
ATOM   116  C  CD1 . LEU   A 1 24  ? -2.391  -49.959 -23.216 1.00 88.08  ? 44  LEU   A CD1 1 
ATOM   117  C  CD2 . LEU   A 1 24  ? -2.399  -52.398 -23.800 1.00 94.31  ? 44  LEU   A CD2 1 
ATOM   118  N  N   . PRO   A 1 25  ? -3.768  -54.106 -19.719 1.00 102.20 ? 45  PRO   A N   1 
ATOM   119  C  CA  . PRO   A 1 25  ? -3.706  -54.580 -18.331 1.00 94.06  ? 45  PRO   A CA  1 
ATOM   120  C  C   . PRO   A 1 25  ? -3.243  -53.582 -17.279 1.00 84.25  ? 45  PRO   A C   1 
ATOM   121  O  O   . PRO   A 1 25  ? -2.242  -52.883 -17.457 1.00 93.01  ? 45  PRO   A O   1 
ATOM   122  C  CB  . PRO   A 1 25  ? -2.585  -55.625 -18.359 1.00 98.31  ? 45  PRO   A CB  1 
ATOM   123  C  CG  . PRO   A 1 25  ? -2.495  -56.066 -19.774 1.00 87.78  ? 45  PRO   A CG  1 
ATOM   124  C  CD  . PRO   A 1 25  ? -2.963  -54.932 -20.636 1.00 92.06  ? 45  PRO   A CD  1 
ATOM   125  N  N   . PHE   A 1 26  ? -4.003  -53.510 -16.184 1.00 92.71  ? 46  PHE   A N   1 
ATOM   126  C  CA  . PHE   A 1 26  ? -3.797  -52.545 -15.107 1.00 101.60 ? 46  PHE   A CA  1 
ATOM   127  C  C   . PHE   A 1 26  ? -4.244  -51.144 -15.511 1.00 95.10  ? 46  PHE   A C   1 
ATOM   128  O  O   . PHE   A 1 26  ? -5.113  -50.556 -14.859 1.00 88.57  ? 46  PHE   A O   1 
ATOM   129  C  CB  . PHE   A 1 26  ? -2.332  -52.546 -14.658 1.00 99.29  ? 46  PHE   A CB  1 
ATOM   130  C  CG  . PHE   A 1 26  ? -1.878  -53.856 -14.087 1.00 116.18 ? 46  PHE   A CG  1 
ATOM   131  C  CD1 . PHE   A 1 26  ? -2.292  -54.255 -12.828 1.00 121.64 ? 46  PHE   A CD1 1 
ATOM   132  C  CD2 . PHE   A 1 26  ? -1.041  -54.691 -14.809 1.00 116.79 ? 46  PHE   A CD2 1 
ATOM   133  C  CE1 . PHE   A 1 26  ? -1.879  -55.461 -12.297 1.00 121.41 ? 46  PHE   A CE1 1 
ATOM   134  C  CE2 . PHE   A 1 26  ? -0.624  -55.898 -14.283 1.00 122.89 ? 46  PHE   A CE2 1 
ATOM   135  C  CZ  . PHE   A 1 26  ? -1.044  -56.284 -13.025 1.00 135.85 ? 46  PHE   A CZ  1 
ATOM   136  N  N   . LEU   A 1 27  ? -3.642  -50.593 -16.568 1.00 95.98  ? 47  LEU   A N   1 
ATOM   137  C  CA  . LEU   A 1 27  ? -3.945  -49.225 -16.968 1.00 102.14 ? 47  LEU   A CA  1 
ATOM   138  C  C   . LEU   A 1 27  ? -5.385  -49.034 -17.421 1.00 88.89  ? 47  LEU   A C   1 
ATOM   139  O  O   . LEU   A 1 27  ? -5.885  -47.907 -17.381 1.00 101.92 ? 47  LEU   A O   1 
ATOM   140  C  CB  . LEU   A 1 27  ? -2.994  -48.787 -18.084 1.00 96.19  ? 47  LEU   A CB  1 
ATOM   141  C  CG  . LEU   A 1 27  ? -1.500  -48.837 -17.763 1.00 89.21  ? 47  LEU   A CG  1 
ATOM   142  C  CD1 . LEU   A 1 27  ? -0.700  -48.104 -18.828 1.00 88.45  ? 47  LEU   A CD1 1 
ATOM   143  C  CD2 . LEU   A 1 27  ? -1.232  -48.247 -16.388 1.00 96.01  ? 47  LEU   A CD2 1 
ATOM   144  N  N   . GLY   A 1 28  ? -6.065  -50.098 -17.835 1.00 83.64  ? 48  GLY   A N   1 
ATOM   145  C  CA  . GLY   A 1 28  ? -7.364  -49.905 -18.451 1.00 92.54  ? 48  GLY   A CA  1 
ATOM   146  C  C   . GLY   A 1 28  ? -7.218  -49.133 -19.745 1.00 93.23  ? 48  GLY   A C   1 
ATOM   147  O  O   . GLY   A 1 28  ? -6.279  -49.342 -20.521 1.00 95.54  ? 48  GLY   A O   1 
ATOM   148  N  N   . ASN   A 1 29  ? -8.151  -48.213 -19.983 1.00 77.54  ? 49  ASN   A N   1 
ATOM   149  C  CA  . ASN   A 1 29  ? -8.129  -47.371 -21.171 1.00 87.65  ? 49  ASN   A CA  1 
ATOM   150  C  C   . ASN   A 1 29  ? -7.600  -45.968 -20.887 1.00 80.19  ? 49  ASN   A C   1 
ATOM   151  O  O   . ASN   A 1 29  ? -7.852  -45.051 -21.676 1.00 87.69  ? 49  ASN   A O   1 
ATOM   152  C  CB  . ASN   A 1 29  ? -9.527  -47.283 -21.786 1.00 86.20  ? 49  ASN   A CB  1 
ATOM   153  C  CG  . ASN   A 1 29  ? -10.198 -48.636 -21.911 1.00 93.04  ? 49  ASN   A CG  1 
ATOM   154  O  OD1 . ASN   A 1 29  ? -10.993 -49.028 -21.059 1.00 93.38  ? 49  ASN   A OD1 1 
ATOM   155  N  ND2 . ASN   A 1 29  ? -9.893  -49.350 -22.988 1.00 99.81  ? 49  ASN   A ND2 1 
ATOM   156  N  N   . ILE   A 1 30  ? -6.863  -45.782 -19.788 1.00 75.66  ? 50  ILE   A N   1 
ATOM   157  C  CA  . ILE   A 1 30  ? -6.494  -44.431 -19.371 1.00 98.28  ? 50  ILE   A CA  1 
ATOM   158  C  C   . ILE   A 1 30  ? -5.462  -43.787 -20.287 1.00 107.42 ? 50  ILE   A C   1 
ATOM   159  O  O   . ILE   A 1 30  ? -5.356  -42.555 -20.312 1.00 111.89 ? 50  ILE   A O   1 
ATOM   160  C  CB  . ILE   A 1 30  ? -5.976  -44.417 -17.919 1.00 97.84  ? 50  ILE   A CB  1 
ATOM   161  C  CG1 . ILE   A 1 30  ? -4.596  -45.078 -17.834 1.00 100.61 ? 50  ILE   A CG1 1 
ATOM   162  C  CG2 . ILE   A 1 30  ? -6.992  -45.053 -16.977 1.00 98.92  ? 50  ILE   A CG2 1 
ATOM   163  C  CD1 . ILE   A 1 30  ? -3.757  -44.596 -16.675 1.00 113.88 ? 50  ILE   A CD1 1 
ATOM   164  N  N   . LEU   A 1 31  ? -4.686  -44.573 -21.038 1.00 100.09 ? 51  LEU   A N   1 
ATOM   165  C  CA  . LEU   A 1 31  ? -3.720  -43.971 -21.950 1.00 96.97  ? 51  LEU   A CA  1 
ATOM   166  C  C   . LEU   A 1 31  ? -4.395  -43.202 -23.076 1.00 104.97 ? 51  LEU   A C   1 
ATOM   167  O  O   . LEU   A 1 31  ? -3.763  -42.328 -23.680 1.00 116.50 ? 51  LEU   A O   1 
ATOM   168  C  CB  . LEU   A 1 31  ? -2.789  -45.036 -22.532 1.00 104.93 ? 51  LEU   A CB  1 
ATOM   169  C  CG  . LEU   A 1 31  ? -1.723  -45.603 -21.593 1.00 92.21  ? 51  LEU   A CG  1 
ATOM   170  C  CD1 . LEU   A 1 31  ? -0.549  -46.141 -22.394 1.00 103.93 ? 51  LEU   A CD1 1 
ATOM   171  C  CD2 . LEU   A 1 31  ? -1.257  -44.553 -20.593 1.00 82.46  ? 51  LEU   A CD2 1 
ATOM   172  N  N   . SER   A 1 32  ? -5.662  -43.498 -23.364 1.00 107.96 ? 52  SER   A N   1 
ATOM   173  C  CA  . SER   A 1 32  ? -6.406  -42.746 -24.365 1.00 112.64 ? 52  SER   A CA  1 
ATOM   174  C  C   . SER   A 1 32  ? -6.721  -41.324 -23.918 1.00 115.60 ? 52  SER   A C   1 
ATOM   175  O  O   . SER   A 1 32  ? -7.168  -40.521 -24.744 1.00 119.88 ? 52  SER   A O   1 
ATOM   176  C  CB  . SER   A 1 32  ? -7.702  -43.481 -24.705 1.00 109.30 ? 52  SER   A CB  1 
ATOM   177  O  OG  . SER   A 1 32  ? -7.484  -44.877 -24.808 1.00 100.42 ? 52  SER   A OG  1 
ATOM   178  N  N   . TYR   A 1 33  ? -6.499  -40.995 -22.643 1.00 110.95 ? 53  TYR   A N   1 
ATOM   179  C  CA  . TYR   A 1 33  ? -6.772  -39.660 -22.121 1.00 117.10 ? 53  TYR   A CA  1 
ATOM   180  C  C   . TYR   A 1 33  ? -5.746  -38.627 -22.571 1.00 130.32 ? 53  TYR   A C   1 
ATOM   181  O  O   . TYR   A 1 33  ? -5.803  -37.470 -22.140 1.00 134.10 ? 53  TYR   A O   1 
ATOM   182  C  CB  . TYR   A 1 33  ? -6.914  -39.689 -20.595 1.00 111.76 ? 53  TYR   A CB  1 
ATOM   183  C  CG  . TYR   A 1 33  ? -8.146  -40.381 -20.055 1.00 105.70 ? 53  TYR   A CG  1 
ATOM   184  C  CD1 . TYR   A 1 33  ? -9.316  -40.454 -20.798 1.00 111.13 ? 53  TYR   A CD1 1 
ATOM   185  C  CD2 . TYR   A 1 33  ? -8.141  -40.946 -18.786 1.00 99.27  ? 53  TYR   A CD2 1 
ATOM   186  C  CE1 . TYR   A 1 33  ? -10.444 -41.078 -20.293 1.00 111.49 ? 53  TYR   A CE1 1 
ATOM   187  C  CE2 . TYR   A 1 33  ? -9.262  -41.573 -18.276 1.00 104.19 ? 53  TYR   A CE2 1 
ATOM   188  C  CZ  . TYR   A 1 33  ? -10.410 -41.637 -19.033 1.00 108.49 ? 53  TYR   A CZ  1 
ATOM   189  O  OH  . TYR   A 1 33  ? -11.529 -42.260 -18.529 1.00 107.21 ? 53  TYR   A OH  1 
ATOM   190  N  N   . HIS   A 1 34  ? -4.803  -39.019 -23.425 1.00 143.29 ? 54  HIS   A N   1 
ATOM   191  C  CA  . HIS   A 1 34  ? -3.761  -38.087 -23.835 1.00 146.90 ? 54  HIS   A CA  1 
ATOM   192  C  C   . HIS   A 1 34  ? -4.213  -36.902 -24.679 1.00 149.13 ? 54  HIS   A C   1 
ATOM   193  O  O   . HIS   A 1 34  ? -3.380  -36.062 -25.034 1.00 155.67 ? 54  HIS   A O   1 
ATOM   194  C  CB  . HIS   A 1 34  ? -2.649  -38.857 -24.555 1.00 153.43 ? 54  HIS   A CB  1 
ATOM   195  C  CG  . HIS   A 1 34  ? -2.987  -39.255 -25.958 1.00 158.42 ? 54  HIS   A CG  1 
ATOM   196  N  ND1 . HIS   A 1 34  ? -3.851  -40.287 -26.256 1.00 155.28 ? 54  HIS   A ND1 1 
ATOM   197  C  CD2 . HIS   A 1 34  ? -2.565  -38.762 -27.146 1.00 161.45 ? 54  HIS   A CD2 1 
ATOM   198  C  CE1 . HIS   A 1 34  ? -3.949  -40.410 -27.568 1.00 157.53 ? 54  HIS   A CE1 1 
ATOM   199  N  NE2 . HIS   A 1 34  ? -3.179  -39.496 -28.131 1.00 160.91 ? 54  HIS   A NE2 1 
ATOM   200  N  N   . LYS   A 1 35  ? -5.502  -36.809 -25.004 1.00 146.68 ? 55  LYS   A N   1 
ATOM   201  C  CA  . LYS   A 1 35  ? -6.062  -35.618 -25.627 1.00 152.98 ? 55  LYS   A CA  1 
ATOM   202  C  C   . LYS   A 1 35  ? -7.171  -35.014 -24.775 1.00 151.07 ? 55  LYS   A C   1 
ATOM   203  O  O   . LYS   A 1 35  ? -7.914  -34.149 -25.256 1.00 153.20 ? 55  LYS   A O   1 
ATOM   204  C  CB  . LYS   A 1 35  ? -6.579  -35.940 -27.032 1.00 155.48 ? 55  LYS   A CB  1 
ATOM   205  C  CG  . LYS   A 1 35  ? -5.470  -36.125 -28.059 1.00 154.65 ? 55  LYS   A CG  1 
ATOM   206  C  CD  . LYS   A 1 35  ? -6.021  -36.320 -29.461 1.00 164.28 ? 55  LYS   A CD  1 
ATOM   207  C  CE  . LYS   A 1 35  ? -5.612  -35.160 -30.354 1.00 158.82 ? 55  LYS   A CE  1 
ATOM   208  N  NZ  . LYS   A 1 35  ? -6.688  -34.150 -30.489 1.00 165.54 ? 55  LYS   A NZ  1 
ATOM   209  N  N   . GLY   A 1 36  ? -7.307  -35.457 -23.530 1.00 155.71 ? 56  GLY   A N   1 
ATOM   210  C  CA  . GLY   A 1 36  ? -8.292  -34.939 -22.607 1.00 158.71 ? 56  GLY   A CA  1 
ATOM   211  C  C   . GLY   A 1 36  ? -9.504  -35.850 -22.477 1.00 145.12 ? 56  GLY   A C   1 
ATOM   212  O  O   . GLY   A 1 36  ? -9.770  -36.715 -23.316 1.00 135.91 ? 56  GLY   A O   1 
ATOM   213  N  N   . PHE   A 1 37  ? -10.244 -35.646 -21.382 1.00 126.23 ? 57  PHE   A N   1 
ATOM   214  C  CA  . PHE   A 1 37  ? -11.539 -36.280 -21.148 1.00 126.53 ? 57  PHE   A CA  1 
ATOM   215  C  C   . PHE   A 1 37  ? -12.419 -36.229 -22.390 1.00 122.13 ? 57  PHE   A C   1 
ATOM   216  O  O   . PHE   A 1 37  ? -13.123 -37.192 -22.710 1.00 111.95 ? 57  PHE   A O   1 
ATOM   217  C  CB  . PHE   A 1 37  ? -12.278 -35.578 -20.003 1.00 128.70 ? 57  PHE   A CB  1 
ATOM   218  C  CG  . PHE   A 1 37  ? -12.014 -36.152 -18.638 1.00 131.54 ? 57  PHE   A CG  1 
ATOM   219  C  CD1 . PHE   A 1 37  ? -11.261 -37.301 -18.470 1.00 121.86 ? 57  PHE   A CD1 1 
ATOM   220  C  CD2 . PHE   A 1 37  ? -12.536 -35.528 -17.515 1.00 136.54 ? 57  PHE   A CD2 1 
ATOM   221  C  CE1 . PHE   A 1 37  ? -11.033 -37.814 -17.202 1.00 121.40 ? 57  PHE   A CE1 1 
ATOM   222  C  CE2 . PHE   A 1 37  ? -12.312 -36.033 -16.251 1.00 133.60 ? 57  PHE   A CE2 1 
ATOM   223  C  CZ  . PHE   A 1 37  ? -11.560 -37.177 -16.092 1.00 133.10 ? 57  PHE   A CZ  1 
ATOM   224  N  N   . CYS   A 1 38  ? -12.365 -35.100 -23.095 1.00 139.98 ? 58  CYS   A N   1 
ATOM   225  C  CA  . CYS   A 1 38  ? -13.361 -34.701 -24.081 1.00 138.31 ? 58  CYS   A CA  1 
ATOM   226  C  C   . CYS   A 1 38  ? -13.083 -35.251 -25.473 1.00 141.02 ? 58  CYS   A C   1 
ATOM   227  O  O   . CYS   A 1 38  ? -13.985 -35.795 -26.118 1.00 136.46 ? 58  CYS   A O   1 
ATOM   228  C  CB  . CYS   A 1 38  ? -13.429 -33.179 -24.131 1.00 134.59 ? 58  CYS   A CB  1 
ATOM   229  S  SG  . CYS   A 1 38  ? -14.103 -32.473 -22.640 1.00 141.04 ? 58  CYS   A SG  1 
ATOM   230  N  N   . MET   A 1 39  ? -11.852 -35.095 -25.964 1.00 130.02 ? 59  MET   A N   1 
ATOM   231  C  CA  . MET   A 1 39  ? -11.526 -35.667 -27.262 1.00 130.86 ? 59  MET   A CA  1 
ATOM   232  C  C   . MET   A 1 39  ? -11.663 -37.182 -27.228 1.00 121.69 ? 59  MET   A C   1 
ATOM   233  O  O   . MET   A 1 39  ? -11.903 -37.811 -28.265 1.00 124.47 ? 59  MET   A O   1 
ATOM   234  C  CB  . MET   A 1 39  ? -10.117 -35.252 -27.690 1.00 142.62 ? 59  MET   A CB  1 
ATOM   235  C  CG  . MET   A 1 39  ? -10.102 -33.936 -28.459 1.00 150.92 ? 59  MET   A CG  1 
ATOM   236  S  SD  . MET   A 1 39  ? -10.914 -34.060 -30.068 1.00 170.13 ? 59  MET   A SD  1 
ATOM   237  C  CE  . MET   A 1 39  ? -9.737  -33.255 -31.152 1.00 143.05 ? 59  MET   A CE  1 
ATOM   238  N  N   . PHE   A 1 40  ? -11.547 -37.775 -26.039 1.00 119.94 ? 60  PHE   A N   1 
ATOM   239  C  CA  . PHE   A 1 40  ? -11.773 -39.207 -25.880 1.00 112.01 ? 60  PHE   A CA  1 
ATOM   240  C  C   . PHE   A 1 40  ? -13.253 -39.548 -26.022 1.00 117.23 ? 60  PHE   A C   1 
ATOM   241  O  O   . PHE   A 1 40  ? -13.617 -40.491 -26.733 1.00 118.06 ? 60  PHE   A O   1 
ATOM   242  C  CB  . PHE   A 1 40  ? -11.240 -39.657 -24.522 1.00 114.56 ? 60  PHE   A CB  1 
ATOM   243  C  CG  . PHE   A 1 40  ? -11.435 -41.117 -24.243 1.00 108.69 ? 60  PHE   A CG  1 
ATOM   244  C  CD1 . PHE   A 1 40  ? -10.961 -42.075 -25.122 1.00 118.10 ? 60  PHE   A CD1 1 
ATOM   245  C  CD2 . PHE   A 1 40  ? -12.100 -41.530 -23.104 1.00 105.65 ? 60  PHE   A CD2 1 
ATOM   246  C  CE1 . PHE   A 1 40  ? -11.138 -43.421 -24.860 1.00 115.38 ? 60  PHE   A CE1 1 
ATOM   247  C  CE2 . PHE   A 1 40  ? -12.282 -42.872 -22.837 1.00 108.48 ? 60  PHE   A CE2 1 
ATOM   248  C  CZ  . PHE   A 1 40  ? -11.802 -43.819 -23.716 1.00 109.50 ? 60  PHE   A CZ  1 
ATOM   249  N  N   . ASP   A 1 41  ? -14.123 -38.792 -25.344 1.00 123.34 ? 61  ASP   A N   1 
ATOM   250  C  CA  . ASP   A 1 41  ? -15.559 -39.037 -25.447 1.00 109.18 ? 61  ASP   A CA  1 
ATOM   251  C  C   . ASP   A 1 41  ? -16.068 -38.740 -26.852 1.00 113.74 ? 61  ASP   A C   1 
ATOM   252  O  O   . ASP   A 1 41  ? -16.826 -39.530 -27.428 1.00 113.83 ? 61  ASP   A O   1 
ATOM   253  C  CB  . ASP   A 1 41  ? -16.315 -38.199 -24.414 1.00 105.29 ? 61  ASP   A CB  1 
ATOM   254  C  CG  . ASP   A 1 41  ? -15.965 -38.575 -22.989 1.00 108.24 ? 61  ASP   A CG  1 
ATOM   255  O  OD1 . ASP   A 1 41  ? -15.174 -39.522 -22.799 1.00 107.83 ? 61  ASP   A OD1 1 
ATOM   256  O  OD2 . ASP   A 1 41  ? -16.486 -37.925 -22.058 1.00 101.26 ? 61  ASP   A OD2 1 
ATOM   257  N  N   . MET   A 1 42  ? -15.673 -37.592 -27.412 1.00 110.26 ? 62  MET   A N   1 
ATOM   258  C  CA  A MET   A 1 42  ? -16.059 -37.255 -28.779 0.44 111.60 ? 62  MET   A CA  1 
ATOM   259  C  CA  B MET   A 1 42  ? -16.064 -37.258 -28.778 0.56 121.46 ? 62  MET   A CA  1 
ATOM   260  C  C   . MET   A 1 42  ? -15.652 -38.355 -29.752 1.00 115.76 ? 62  MET   A C   1 
ATOM   261  O  O   . MET   A 1 42  ? -16.394 -38.677 -30.687 1.00 119.45 ? 62  MET   A O   1 
ATOM   262  C  CB  A MET   A 1 42  ? -15.426 -35.923 -29.187 0.44 116.24 ? 62  MET   A CB  1 
ATOM   263  C  CB  B MET   A 1 42  ? -15.446 -35.920 -29.187 0.56 110.25 ? 62  MET   A CB  1 
ATOM   264  C  CG  A MET   A 1 42  ? -16.013 -34.705 -28.491 0.44 113.26 ? 62  MET   A CG  1 
ATOM   265  C  CG  B MET   A 1 42  ? -16.207 -34.699 -28.694 0.56 113.00 ? 62  MET   A CG  1 
ATOM   266  S  SD  A MET   A 1 42  ? -17.519 -34.104 -29.278 0.44 107.03 ? 62  MET   A SD  1 
ATOM   267  S  SD  B MET   A 1 42  ? -15.685 -33.186 -29.526 0.56 122.65 ? 62  MET   A SD  1 
ATOM   268  C  CE  A MET   A 1 42  ? -16.868 -33.485 -30.827 0.44 111.93 ? 62  MET   A CE  1 
ATOM   269  C  CE  B MET   A 1 42  ? -16.753 -33.200 -30.964 0.56 111.84 ? 62  MET   A CE  1 
ATOM   270  N  N   . GLU   A 1 43  ? -14.473 -38.944 -29.542 1.00 122.83 ? 63  GLU   A N   1 
ATOM   271  C  CA  . GLU   A 1 43  ? -14.004 -40.023 -30.405 1.00 126.74 ? 63  GLU   A CA  1 
ATOM   272  C  C   . GLU   A 1 43  ? -14.841 -41.282 -30.218 1.00 121.94 ? 63  GLU   A C   1 
ATOM   273  O  O   . GLU   A 1 43  ? -15.359 -41.846 -31.189 1.00 120.92 ? 63  GLU   A O   1 
ATOM   274  C  CB  . GLU   A 1 43  ? -12.534 -40.318 -30.114 1.00 133.56 ? 63  GLU   A CB  1 
ATOM   275  C  CG  . GLU   A 1 43  ? -11.544 -39.514 -30.933 1.00 146.36 ? 63  GLU   A CG  1 
ATOM   276  C  CD  . GLU   A 1 43  ? -10.121 -39.993 -30.735 1.00 163.07 ? 63  GLU   A CD  1 
ATOM   277  O  OE1 . GLU   A 1 43  ? -9.939  -41.092 -30.170 1.00 165.98 ? 63  GLU   A OE1 1 
ATOM   278  O  OE2 . GLU   A 1 43  ? -9.185  -39.270 -31.135 1.00 174.98 ? 63  GLU   A OE2 1 
ATOM   279  N  N   . CYS   A 1 44  ? -14.976 -41.740 -28.970 1.00 118.44 ? 64  CYS   A N   1 
ATOM   280  C  CA  . CYS   A 1 44  ? -15.689 -42.985 -28.702 1.00 110.00 ? 64  CYS   A CA  1 
ATOM   281  C  C   . CYS   A 1 44  ? -17.148 -42.905 -29.128 1.00 112.49 ? 64  CYS   A C   1 
ATOM   282  O  O   . CYS   A 1 44  ? -17.723 -43.911 -29.561 1.00 111.30 ? 64  CYS   A O   1 
ATOM   283  C  CB  . CYS   A 1 44  ? -15.589 -43.336 -27.218 1.00 102.27 ? 64  CYS   A CB  1 
ATOM   284  S  SG  . CYS   A 1 44  ? -13.936 -43.813 -26.686 1.00 104.76 ? 64  CYS   A SG  1 
ATOM   285  N  N   . HIS   A 1 45  ? -17.765 -41.727 -29.002 1.00 117.57 ? 65  HIS   A N   1 
ATOM   286  C  CA  . HIS   A 1 45  ? -19.103 -41.527 -29.546 1.00 109.90 ? 65  HIS   A CA  1 
ATOM   287  C  C   . HIS   A 1 45  ? -19.139 -41.843 -31.035 1.00 115.44 ? 65  HIS   A C   1 
ATOM   288  O  O   . HIS   A 1 45  ? -20.079 -42.481 -31.523 1.00 114.50 ? 65  HIS   A O   1 
ATOM   289  C  CB  . HIS   A 1 45  ? -19.556 -40.088 -29.295 1.00 112.44 ? 65  HIS   A CB  1 
ATOM   290  C  CG  . HIS   A 1 45  ? -21.026 -39.873 -29.477 1.00 123.29 ? 65  HIS   A CG  1 
ATOM   291  N  ND1 . HIS   A 1 45  ? -21.942 -40.903 -29.448 1.00 116.06 ? 65  HIS   A ND1 1 
ATOM   292  C  CD2 . HIS   A 1 45  ? -21.738 -38.743 -29.701 1.00 119.02 ? 65  HIS   A CD2 1 
ATOM   293  C  CE1 . HIS   A 1 45  ? -23.155 -40.416 -29.640 1.00 114.64 ? 65  HIS   A CE1 1 
ATOM   294  N  NE2 . HIS   A 1 45  ? -23.059 -39.108 -29.796 1.00 122.54 ? 65  HIS   A NE2 1 
ATOM   295  N  N   . LYS   A 1 46  ? -18.108 -41.420 -31.768 1.00 118.97 ? 66  LYS   A N   1 
ATOM   296  C  CA  . LYS   A 1 46  ? -18.080 -41.639 -33.209 1.00 120.42 ? 66  LYS   A CA  1 
ATOM   297  C  C   . LYS   A 1 46  ? -17.774 -43.093 -33.545 1.00 120.20 ? 66  LYS   A C   1 
ATOM   298  O  O   . LYS   A 1 46  ? -18.352 -43.651 -34.485 1.00 126.54 ? 66  LYS   A O   1 
ATOM   299  C  CB  . LYS   A 1 46  ? -17.052 -40.709 -33.853 1.00 120.65 ? 66  LYS   A CB  1 
ATOM   300  C  CG  . LYS   A 1 46  ? -17.413 -40.261 -35.257 1.00 127.23 ? 66  LYS   A CG  1 
ATOM   301  C  CD  . LYS   A 1 46  ? -17.203 -38.765 -35.418 1.00 136.05 ? 66  LYS   A CD  1 
ATOM   302  C  CE  . LYS   A 1 46  ? -17.981 -38.226 -36.605 1.00 144.92 ? 66  LYS   A CE  1 
ATOM   303  N  NZ  . LYS   A 1 46  ? -18.340 -36.792 -36.427 1.00 143.92 ? 66  LYS   A NZ  1 
ATOM   304  N  N   . LYS   A 1 47  ? -16.872 -43.723 -32.790 1.00 121.60 ? 67  LYS   A N   1 
ATOM   305  C  CA  . LYS   A 1 47  ? -16.477 -45.092 -33.109 1.00 120.55 ? 67  LYS   A CA  1 
ATOM   306  C  C   . LYS   A 1 47  ? -17.594 -46.087 -32.811 1.00 120.46 ? 67  LYS   A C   1 
ATOM   307  O  O   . LYS   A 1 47  ? -17.782 -47.054 -33.558 1.00 128.40 ? 67  LYS   A O   1 
ATOM   308  C  CB  . LYS   A 1 47  ? -15.214 -45.481 -32.337 1.00 117.14 ? 67  LYS   A CB  1 
ATOM   309  C  CG  . LYS   A 1 47  ? -13.903 -45.092 -33.004 1.00 117.82 ? 67  LYS   A CG  1 
ATOM   310  C  CD  . LYS   A 1 47  ? -12.707 -45.511 -32.154 1.00 122.24 ? 67  LYS   A CD  1 
ATOM   311  C  CE  . LYS   A 1 47  ? -12.235 -44.393 -31.239 1.00 133.23 ? 67  LYS   A CE  1 
ATOM   312  N  NZ  . LYS   A 1 47  ? -11.090 -44.824 -30.386 1.00 124.04 ? 67  LYS   A NZ  1 
ATOM   313  N  N   . TYR   A 1 48  ? -18.346 -45.870 -31.731 1.00 117.35 ? 68  TYR   A N   1 
ATOM   314  C  CA  . TYR   A 1 48  ? -19.205 -46.910 -31.184 1.00 117.00 ? 68  TYR   A CA  1 
ATOM   315  C  C   . TYR   A 1 48  ? -20.684 -46.561 -31.121 1.00 123.15 ? 68  TYR   A C   1 
ATOM   316  O  O   . TYR   A 1 48  ? -21.508 -47.481 -31.077 1.00 114.02 ? 68  TYR   A O   1 
ATOM   317  C  CB  . TYR   A 1 48  ? -18.728 -47.299 -29.777 1.00 106.19 ? 68  TYR   A CB  1 
ATOM   318  C  CG  . TYR   A 1 48  ? -17.248 -47.600 -29.723 1.00 114.99 ? 68  TYR   A CG  1 
ATOM   319  C  CD1 . TYR   A 1 48  ? -16.739 -48.771 -30.269 1.00 110.66 ? 68  TYR   A CD1 1 
ATOM   320  C  CD2 . TYR   A 1 48  ? -16.357 -46.710 -29.136 1.00 111.94 ? 68  TYR   A CD2 1 
ATOM   321  C  CE1 . TYR   A 1 48  ? -15.387 -49.050 -30.228 1.00 110.68 ? 68  TYR   A CE1 1 
ATOM   322  C  CE2 . TYR   A 1 48  ? -15.003 -46.981 -29.090 1.00 105.59 ? 68  TYR   A CE2 1 
ATOM   323  C  CZ  . TYR   A 1 48  ? -14.523 -48.152 -29.638 1.00 114.53 ? 68  TYR   A CZ  1 
ATOM   324  O  OH  . TYR   A 1 48  ? -13.176 -48.426 -29.594 1.00 107.24 ? 68  TYR   A OH  1 
ATOM   325  N  N   . GLY   A 1 49  ? -21.050 -45.283 -31.103 1.00 114.21 ? 69  GLY   A N   1 
ATOM   326  C  CA  . GLY   A 1 49  ? -22.453 -44.927 -31.165 1.00 109.11 ? 69  GLY   A CA  1 
ATOM   327  C  C   . GLY   A 1 49  ? -23.119 -44.677 -29.827 1.00 106.06 ? 69  GLY   A C   1 
ATOM   328  O  O   . GLY   A 1 49  ? -22.513 -44.101 -28.918 1.00 108.16 ? 69  GLY   A O   1 
ATOM   329  N  N   . LYS   A 1 50  ? -24.370 -45.129 -29.696 1.00 107.66 ? 70  LYS   A N   1 
ATOM   330  C  CA  . LYS   A 1 50  ? -25.215 -44.696 -28.587 1.00 109.52 ? 70  LYS   A CA  1 
ATOM   331  C  C   . LYS   A 1 50  ? -24.682 -45.148 -27.233 1.00 110.57 ? 70  LYS   A C   1 
ATOM   332  O  O   . LYS   A 1 50  ? -24.943 -44.491 -26.219 1.00 102.08 ? 70  LYS   A O   1 
ATOM   333  C  CB  . LYS   A 1 50  ? -26.644 -45.205 -28.793 1.00 104.94 ? 70  LYS   A CB  1 
ATOM   334  C  CG  . LYS   A 1 50  ? -26.813 -46.706 -28.602 1.00 107.59 ? 70  LYS   A CG  1 
ATOM   335  C  CD  . LYS   A 1 50  ? -28.105 -47.206 -29.226 1.00 133.89 ? 70  LYS   A CD  1 
ATOM   336  C  CE  . LYS   A 1 50  ? -28.053 -48.705 -29.476 1.00 130.85 ? 70  LYS   A CE  1 
ATOM   337  N  NZ  . LYS   A 1 50  ? -26.658 -49.190 -29.678 1.00 125.12 ? 70  LYS   A NZ  1 
ATOM   338  N  N   . VAL   A 1 51  ? -23.935 -46.249 -27.190 1.00 106.71 ? 71  VAL   A N   1 
ATOM   339  C  CA  . VAL   A 1 51  ? -23.503 -46.844 -25.928 1.00 103.66 ? 71  VAL   A CA  1 
ATOM   340  C  C   . VAL   A 1 51  ? -22.144 -47.499 -26.130 1.00 111.34 ? 71  VAL   A C   1 
ATOM   341  O  O   . VAL   A 1 51  ? -21.931 -48.217 -27.112 1.00 106.12 ? 71  VAL   A O   1 
ATOM   342  C  CB  . VAL   A 1 51  ? -24.536 -47.866 -25.409 1.00 94.40  ? 71  VAL   A CB  1 
ATOM   343  C  CG1 . VAL   A 1 51  ? -23.888 -48.854 -24.452 1.00 98.65  ? 71  VAL   A CG1 1 
ATOM   344  C  CG2 . VAL   A 1 51  ? -25.687 -47.148 -24.734 1.00 100.73 ? 71  VAL   A CG2 1 
ATOM   345  N  N   . TRP   A 1 52  ? -21.224 -47.252 -25.198 1.00 105.30 ? 72  TRP   A N   1 
ATOM   346  C  CA  . TRP   A 1 52  ? -19.921 -47.902 -25.217 1.00 96.52  ? 72  TRP   A CA  1 
ATOM   347  C  C   . TRP   A 1 52  ? -19.383 -47.981 -23.795 1.00 93.87  ? 72  TRP   A C   1 
ATOM   348  O  O   . TRP   A 1 52  ? -19.889 -47.328 -22.879 1.00 94.93  ? 72  TRP   A O   1 
ATOM   349  C  CB  . TRP   A 1 52  ? -18.937 -47.170 -26.138 1.00 97.51  ? 72  TRP   A CB  1 
ATOM   350  C  CG  . TRP   A 1 52  ? -18.491 -45.832 -25.633 1.00 99.09  ? 72  TRP   A CG  1 
ATOM   351  C  CD1 . TRP   A 1 52  ? -17.409 -45.573 -24.842 1.00 107.24 ? 72  TRP   A CD1 1 
ATOM   352  C  CD2 . TRP   A 1 52  ? -19.107 -44.566 -25.897 1.00 93.69  ? 72  TRP   A CD2 1 
ATOM   353  N  NE1 . TRP   A 1 52  ? -17.319 -44.225 -24.591 1.00 102.59 ? 72  TRP   A NE1 1 
ATOM   354  C  CE2 . TRP   A 1 52  ? -18.348 -43.585 -25.229 1.00 98.88  ? 72  TRP   A CE2 1 
ATOM   355  C  CE3 . TRP   A 1 52  ? -20.228 -44.168 -26.630 1.00 103.74 ? 72  TRP   A CE3 1 
ATOM   356  C  CZ2 . TRP   A 1 52  ? -18.675 -42.231 -25.272 1.00 100.52 ? 72  TRP   A CZ2 1 
ATOM   357  C  CZ3 . TRP   A 1 52  ? -20.551 -42.825 -26.671 1.00 104.32 ? 72  TRP   A CZ3 1 
ATOM   358  C  CH2 . TRP   A 1 52  ? -19.777 -41.872 -25.998 1.00 98.85  ? 72  TRP   A CH2 1 
ATOM   359  N  N   . GLY   A 1 53  ? -18.348 -48.791 -23.622 1.00 101.84 ? 73  GLY   A N   1 
ATOM   360  C  CA  . GLY   A 1 53  ? -17.768 -49.007 -22.309 1.00 81.37  ? 73  GLY   A CA  1 
ATOM   361  C  C   . GLY   A 1 53  ? -16.256 -48.979 -22.360 1.00 80.25  ? 73  GLY   A C   1 
ATOM   362  O  O   . GLY   A 1 53  ? -15.637 -49.327 -23.367 1.00 107.30 ? 73  GLY   A O   1 
ATOM   363  N  N   . PHE   A 1 54  ? -15.664 -48.557 -21.245 1.00 90.06  ? 74  PHE   A N   1 
ATOM   364  C  CA  . PHE   A 1 54  ? -14.216 -48.515 -21.096 1.00 78.74  ? 74  PHE   A CA  1 
ATOM   365  C  C   . PHE   A 1 54  ? -13.881 -48.722 -19.624 1.00 76.71  ? 74  PHE   A C   1 
ATOM   366  O  O   . PHE   A 1 54  ? -14.764 -48.943 -18.791 1.00 75.87  ? 74  PHE   A O   1 
ATOM   367  C  CB  . PHE   A 1 54  ? -13.642 -47.201 -21.638 1.00 83.88  ? 74  PHE   A CB  1 
ATOM   368  C  CG  . PHE   A 1 54  ? -14.139 -45.977 -20.924 1.00 83.13  ? 74  PHE   A CG  1 
ATOM   369  C  CD1 . PHE   A 1 54  ? -15.287 -45.330 -21.348 1.00 85.80  ? 74  PHE   A CD1 1 
ATOM   370  C  CD2 . PHE   A 1 54  ? -13.455 -45.469 -19.831 1.00 85.79  ? 74  PHE   A CD2 1 
ATOM   371  C  CE1 . PHE   A 1 54  ? -15.747 -44.203 -20.696 1.00 92.19  ? 74  PHE   A CE1 1 
ATOM   372  C  CE2 . PHE   A 1 54  ? -13.910 -44.342 -19.174 1.00 84.27  ? 74  PHE   A CE2 1 
ATOM   373  C  CZ  . PHE   A 1 54  ? -15.056 -43.708 -19.608 1.00 83.61  ? 74  PHE   A CZ  1 
ATOM   374  N  N   . TYR   A 1 55  ? -12.591 -48.649 -19.303 1.00 93.19  ? 75  TYR   A N   1 
ATOM   375  C  CA  . TYR   A 1 55  ? -12.114 -48.916 -17.952 1.00 85.90  ? 75  TYR   A CA  1 
ATOM   376  C  C   . TYR   A 1 55  ? -11.186 -47.802 -17.492 1.00 80.88  ? 75  TYR   A C   1 
ATOM   377  O  O   . TYR   A 1 55  ? -10.244 -47.438 -18.203 1.00 89.74  ? 75  TYR   A O   1 
ATOM   378  C  CB  . TYR   A 1 55  ? -11.382 -50.264 -17.866 1.00 76.83  ? 75  TYR   A CB  1 
ATOM   379  C  CG  . TYR   A 1 55  ? -12.193 -51.463 -18.311 1.00 86.18  ? 75  TYR   A CG  1 
ATOM   380  C  CD1 . TYR   A 1 55  ? -12.420 -51.718 -19.659 1.00 82.69  ? 75  TYR   A CD1 1 
ATOM   381  C  CD2 . TYR   A 1 55  ? -12.734 -52.341 -17.380 1.00 82.97  ? 75  TYR   A CD2 1 
ATOM   382  C  CE1 . TYR   A 1 55  ? -13.159 -52.813 -20.065 1.00 90.92  ? 75  TYR   A CE1 1 
ATOM   383  C  CE2 . TYR   A 1 55  ? -13.475 -53.438 -17.777 1.00 89.08  ? 75  TYR   A CE2 1 
ATOM   384  C  CZ  . TYR   A 1 55  ? -13.684 -53.669 -19.120 1.00 99.54  ? 75  TYR   A CZ  1 
ATOM   385  O  OH  . TYR   A 1 55  ? -14.421 -54.760 -19.519 1.00 108.78 ? 75  TYR   A OH  1 
ATOM   386  N  N   . ASP   A 1 56  ? -11.456 -47.267 -16.301 1.00 79.43  ? 76  ASP   A N   1 
ATOM   387  C  CA  . ASP   A 1 56  ? -10.525 -46.376 -15.608 1.00 93.17  ? 76  ASP   A CA  1 
ATOM   388  C  C   . ASP   A 1 56  ? -9.692  -47.248 -14.679 1.00 92.43  ? 76  ASP   A C   1 
ATOM   389  O  O   . ASP   A 1 56  ? -10.025 -47.447 -13.510 1.00 97.03  ? 76  ASP   A O   1 
ATOM   390  C  CB  . ASP   A 1 56  ? -11.270 -45.286 -14.848 1.00 92.98  ? 76  ASP   A CB  1 
ATOM   391  C  CG  . ASP   A 1 56  ? -11.677 -44.128 -15.736 1.00 96.48  ? 76  ASP   A CG  1 
ATOM   392  O  OD1 . ASP   A 1 56  ? -11.255 -44.101 -16.911 1.00 90.30  ? 76  ASP   A OD1 1 
ATOM   393  O  OD2 . ASP   A 1 56  ? -12.417 -43.243 -15.258 1.00 103.63 ? 76  ASP   A OD2 1 
ATOM   394  N  N   . GLY   A 1 57  ? -8.596  -47.782 -15.210 1.00 94.44  ? 77  GLY   A N   1 
ATOM   395  C  CA  . GLY   A 1 57  ? -7.833  -48.781 -14.491 1.00 97.46  ? 77  GLY   A CA  1 
ATOM   396  C  C   . GLY   A 1 57  ? -8.592  -50.089 -14.416 1.00 94.62  ? 77  GLY   A C   1 
ATOM   397  O  O   . GLY   A 1 57  ? -8.844  -50.725 -15.444 1.00 93.50  ? 77  GLY   A O   1 
ATOM   398  N  N   . GLN   A 1 58  ? -8.970  -50.498 -13.208 1.00 98.80  ? 78  GLN   A N   1 
ATOM   399  C  CA  . GLN   A 1 58  ? -9.793  -51.683 -13.010 1.00 106.08 ? 78  GLN   A CA  1 
ATOM   400  C  C   . GLN   A 1 58  ? -11.283 -51.368 -12.978 1.00 97.66  ? 78  GLN   A C   1 
ATOM   401  O  O   . GLN   A 1 58  ? -12.092 -52.292 -12.844 1.00 98.92  ? 78  GLN   A O   1 
ATOM   402  C  CB  . GLN   A 1 58  ? -9.399  -52.390 -11.708 1.00 106.54 ? 78  GLN   A CB  1 
ATOM   403  C  CG  . GLN   A 1 58  ? -8.078  -53.143 -11.758 1.00 114.93 ? 78  GLN   A CG  1 
ATOM   404  C  CD  . GLN   A 1 58  ? -8.064  -54.241 -12.803 1.00 118.47 ? 78  GLN   A CD  1 
ATOM   405  O  OE1 . GLN   A 1 58  ? -9.026  -54.998 -12.940 1.00 124.10 ? 78  GLN   A OE1 1 
ATOM   406  N  NE2 . GLN   A 1 58  ? -6.963  -54.343 -13.538 1.00 119.88 ? 78  GLN   A NE2 1 
ATOM   407  N  N   . GLN   A 1 59  ? -11.665 -50.097 -13.103 1.00 86.43  ? 79  GLN   A N   1 
ATOM   408  C  CA  . GLN   A 1 59  ? -13.044 -49.690 -12.882 1.00 88.66  ? 79  GLN   A CA  1 
ATOM   409  C  C   . GLN   A 1 59  ? -13.798 -49.638 -14.201 1.00 75.82  ? 79  GLN   A C   1 
ATOM   410  O  O   . GLN   A 1 59  ? -13.473 -48.799 -15.056 1.00 76.54  ? 79  GLN   A O   1 
ATOM   411  C  CB  . GLN   A 1 59  ? -13.094 -48.330 -12.188 1.00 85.47  ? 79  GLN   A CB  1 
ATOM   412  C  CG  . GLN   A 1 59  ? -14.469 -47.693 -12.200 1.00 85.00  ? 79  GLN   A CG  1 
ATOM   413  C  CD  . GLN   A 1 59  ? -15.473 -48.485 -11.388 1.00 90.95  ? 79  GLN   A CD  1 
ATOM   414  O  OE1 . GLN   A 1 59  ? -15.201 -48.870 -10.251 1.00 94.76  ? 79  GLN   A OE1 1 
ATOM   415  N  NE2 . GLN   A 1 59  ? -16.637 -48.743 -11.973 1.00 70.36  ? 79  GLN   A NE2 1 
ATOM   416  N  N   . PRO   A 1 60  ? -14.801 -50.488 -14.414 1.00 70.07  ? 80  PRO   A N   1 
ATOM   417  C  CA  . PRO   A 1 60  ? -15.592 -50.396 -15.647 1.00 84.30  ? 80  PRO   A CA  1 
ATOM   418  C  C   . PRO   A 1 60  ? -16.476 -49.159 -15.638 1.00 88.51  ? 80  PRO   A C   1 
ATOM   419  O  O   . PRO   A 1 60  ? -17.112 -48.833 -14.633 1.00 73.10  ? 80  PRO   A O   1 
ATOM   420  C  CB  . PRO   A 1 60  ? -16.432 -51.679 -15.639 1.00 76.87  ? 80  PRO   A CB  1 
ATOM   421  C  CG  . PRO   A 1 60  ? -16.427 -52.154 -14.231 1.00 78.96  ? 80  PRO   A CG  1 
ATOM   422  C  CD  . PRO   A 1 60  ? -15.206 -51.615 -13.556 1.00 73.27  ? 80  PRO   A CD  1 
ATOM   423  N  N   . VAL   A 1 61  ? -16.510 -48.469 -16.774 1.00 77.43  ? 81  VAL   A N   1 
ATOM   424  C  CA  . VAL   A 1 61  ? -17.342 -47.285 -16.951 1.00 74.93  ? 81  VAL   A CA  1 
ATOM   425  C  C   . VAL   A 1 61  ? -18.165 -47.476 -18.215 1.00 77.44  ? 81  VAL   A C   1 
ATOM   426  O  O   . VAL   A 1 61  ? -17.605 -47.700 -19.295 1.00 73.03  ? 81  VAL   A O   1 
ATOM   427  C  CB  . VAL   A 1 61  ? -16.512 -45.994 -17.042 1.00 90.99  ? 81  VAL   A CB  1 
ATOM   428  C  CG1 . VAL   A 1 61  ? -17.423 -44.804 -17.311 1.00 63.62  ? 81  VAL   A CG1 1 
ATOM   429  C  CG2 . VAL   A 1 61  ? -15.710 -45.783 -15.768 1.00 88.09  ? 81  VAL   A CG2 1 
ATOM   430  N  N   . LEU   A 1 62  ? -19.484 -47.389 -18.085 1.00 81.49  ? 82  LEU   A N   1 
ATOM   431  C  CA  . LEU   A 1 62  ? -20.384 -47.473 -19.226 1.00 87.01  ? 82  LEU   A CA  1 
ATOM   432  C  C   . LEU   A 1 62  ? -20.854 -46.070 -19.587 1.00 82.31  ? 82  LEU   A C   1 
ATOM   433  O  O   . LEU   A 1 62  ? -21.410 -45.361 -18.742 1.00 79.27  ? 82  LEU   A O   1 
ATOM   434  C  CB  . LEU   A 1 62  ? -21.581 -48.373 -18.928 1.00 69.49  ? 82  LEU   A CB  1 
ATOM   435  C  CG  . LEU   A 1 62  ? -22.657 -48.286 -20.010 1.00 78.52  ? 82  LEU   A CG  1 
ATOM   436  C  CD1 . LEU   A 1 62  ? -22.200 -49.030 -21.253 1.00 85.37  ? 82  LEU   A CD1 1 
ATOM   437  C  CD2 . LEU   A 1 62  ? -23.980 -48.825 -19.511 1.00 73.22  ? 82  LEU   A CD2 1 
ATOM   438  N  N   . ALA   A 1 63  ? -20.630 -45.675 -20.835 1.00 77.37  ? 83  ALA   A N   1 
ATOM   439  C  CA  . ALA   A 1 63  ? -21.050 -44.374 -21.333 1.00 84.85  ? 83  ALA   A CA  1 
ATOM   440  C  C   . ALA   A 1 63  ? -22.334 -44.531 -22.135 1.00 94.15  ? 83  ALA   A C   1 
ATOM   441  O  O   . ALA   A 1 63  ? -22.413 -45.383 -23.026 1.00 94.94  ? 83  ALA   A O   1 
ATOM   442  C  CB  . ALA   A 1 63  ? -19.957 -43.741 -22.195 1.00 84.22  ? 83  ALA   A CB  1 
ATOM   443  N  N   . ILE   A 1 64  ? -23.336 -43.715 -21.814 1.00 85.86  ? 84  ILE   A N   1 
ATOM   444  C  CA  . ILE   A 1 64  ? -24.630 -43.759 -22.482 1.00 96.48  ? 84  ILE   A CA  1 
ATOM   445  C  C   . ILE   A 1 64  ? -24.921 -42.393 -23.088 1.00 82.30  ? 84  ILE   A C   1 
ATOM   446  O  O   . ILE   A 1 64  ? -24.580 -41.356 -22.508 1.00 80.76  ? 84  ILE   A O   1 
ATOM   447  C  CB  . ILE   A 1 64  ? -25.761 -44.193 -21.522 1.00 104.18 ? 84  ILE   A CB  1 
ATOM   448  C  CG1 . ILE   A 1 64  ? -26.095 -43.082 -20.522 1.00 97.77  ? 84  ILE   A CG1 1 
ATOM   449  C  CG2 . ILE   A 1 64  ? -25.379 -45.480 -20.798 1.00 93.44  ? 84  ILE   A CG2 1 
ATOM   450  C  CD1 . ILE   A 1 64  ? -26.879 -43.551 -19.316 1.00 82.50  ? 84  ILE   A CD1 1 
ATOM   451  N  N   . THR   A 1 65  ? -25.529 -42.399 -24.277 1.00 87.85  ? 85  THR   A N   1 
ATOM   452  C  CA  . THR   A 1 65  ? -25.931 -41.175 -24.960 1.00 91.42  ? 85  THR   A CA  1 
ATOM   453  C  C   . THR   A 1 65  ? -27.405 -41.189 -25.352 1.00 115.50 ? 85  THR   A C   1 
ATOM   454  O  O   . THR   A 1 65  ? -27.831 -40.336 -26.140 1.00 116.38 ? 85  THR   A O   1 
ATOM   455  C  CB  . THR   A 1 65  ? -25.072 -40.932 -26.209 1.00 106.92 ? 85  THR   A CB  1 
ATOM   456  O  OG1 . THR   A 1 65  ? -25.571 -41.719 -27.298 1.00 108.35 ? 85  THR   A OG1 1 
ATOM   457  C  CG2 . THR   A 1 65  ? -23.615 -41.288 -25.950 1.00 102.21 ? 85  THR   A CG2 1 
ATOM   458  N  N   . ASP   A 1 66  ? -28.186 -42.126 -24.827 1.00 109.22 ? 86  ASP   A N   1 
ATOM   459  C  CA  . ASP   A 1 66  ? -29.606 -42.220 -25.152 1.00 106.10 ? 86  ASP   A CA  1 
ATOM   460  C  C   . ASP   A 1 66  ? -30.425 -41.332 -24.225 1.00 106.97 ? 86  ASP   A C   1 
ATOM   461  O  O   . ASP   A 1 66  ? -30.487 -41.608 -23.023 1.00 104.69 ? 86  ASP   A O   1 
ATOM   462  C  CB  . ASP   A 1 66  ? -30.078 -43.661 -25.032 1.00 109.57 ? 86  ASP   A CB  1 
ATOM   463  C  CG  . ASP   A 1 66  ? -31.519 -43.844 -25.463 1.00 116.90 ? 86  ASP   A CG  1 
ATOM   464  O  OD1 . ASP   A 1 66  ? -32.421 -43.446 -24.693 1.00 115.03 ? 86  ASP   A OD1 1 
ATOM   465  O  OD2 . ASP   A 1 66  ? -31.755 -44.397 -26.555 1.00 130.95 ? 86  ASP   A OD2 1 
ATOM   466  N  N   . PRO   A 1 67  ? -31.093 -40.292 -24.742 1.00 115.05 ? 87  PRO   A N   1 
ATOM   467  C  CA  . PRO   A 1 67  ? -31.856 -39.383 -23.866 1.00 107.96 ? 87  PRO   A CA  1 
ATOM   468  C  C   . PRO   A 1 67  ? -32.785 -40.080 -22.882 1.00 101.32 ? 87  PRO   A C   1 
ATOM   469  O  O   . PRO   A 1 67  ? -32.846 -39.677 -21.713 1.00 81.28  ? 87  PRO   A O   1 
ATOM   470  C  CB  . PRO   A 1 67  ? -32.642 -38.532 -24.871 1.00 108.75 ? 87  PRO   A CB  1 
ATOM   471  C  CG  . PRO   A 1 67  ? -31.769 -38.497 -26.077 1.00 106.27 ? 87  PRO   A CG  1 
ATOM   472  C  CD  . PRO   A 1 67  ? -31.101 -39.847 -26.147 1.00 113.95 ? 87  PRO   A CD  1 
ATOM   473  N  N   . ASP   A 1 68  ? -33.510 -41.114 -23.318 1.00 105.48 ? 88  ASP   A N   1 
ATOM   474  C  CA  . ASP   A 1 68  ? -34.387 -41.840 -22.402 1.00 100.31 ? 88  ASP   A CA  1 
ATOM   475  C  C   . ASP   A 1 68  ? -33.585 -42.500 -21.290 1.00 98.87  ? 88  ASP   A C   1 
ATOM   476  O  O   . ASP   A 1 68  ? -33.902 -42.350 -20.104 1.00 85.72  ? 88  ASP   A O   1 
ATOM   477  C  CB  . ASP   A 1 68  ? -35.198 -42.888 -23.162 1.00 107.73 ? 88  ASP   A CB  1 
ATOM   478  C  CG  . ASP   A 1 68  ? -36.212 -42.274 -24.097 1.00 128.76 ? 88  ASP   A CG  1 
ATOM   479  O  OD1 . ASP   A 1 68  ? -36.229 -41.032 -24.224 1.00 118.58 ? 88  ASP   A OD1 1 
ATOM   480  O  OD2 . ASP   A 1 68  ? -36.995 -43.034 -24.704 1.00 135.88 ? 88  ASP   A OD2 1 
ATOM   481  N  N   . MET   A 1 69  ? -32.543 -43.247 -21.661 1.00 103.75 ? 89  MET   A N   1 
ATOM   482  C  CA  . MET   A 1 69  ? -31.696 -43.891 -20.665 1.00 94.92  ? 89  MET   A CA  1 
ATOM   483  C  C   . MET   A 1 69  ? -31.020 -42.867 -19.770 1.00 92.86  ? 89  MET   A C   1 
ATOM   484  O  O   . MET   A 1 69  ? -30.865 -43.089 -18.563 1.00 90.03  ? 89  MET   A O   1 
ATOM   485  C  CB  . MET   A 1 69  ? -30.645 -44.751 -21.348 1.00 99.89  ? 89  MET   A CB  1 
ATOM   486  C  CG  . MET   A 1 69  ? -30.482 -46.076 -20.686 1.00 104.48 ? 89  MET   A CG  1 
ATOM   487  S  SD  . MET   A 1 69  ? -29.246 -47.097 -21.485 1.00 109.88 ? 89  MET   A SD  1 
ATOM   488  C  CE  . MET   A 1 69  ? -29.303 -46.448 -23.146 1.00 112.18 ? 89  MET   A CE  1 
ATOM   489  N  N   . ILE   A 1 70  ? -30.577 -41.758 -20.357 1.00 92.33  ? 90  ILE   A N   1 
ATOM   490  C  CA  . ILE   A 1 70  ? -30.076 -40.638 -19.569 1.00 88.39  ? 90  ILE   A CA  1 
ATOM   491  C  C   . ILE   A 1 70  ? -31.117 -40.224 -18.531 1.00 89.71  ? 90  ILE   A C   1 
ATOM   492  O  O   . ILE   A 1 70  ? -30.897 -40.363 -17.322 1.00 84.05  ? 90  ILE   A O   1 
ATOM   493  C  CB  . ILE   A 1 70  ? -29.661 -39.485 -20.504 1.00 99.26  ? 90  ILE   A CB  1 
ATOM   494  C  CG1 . ILE   A 1 70  ? -28.570 -39.973 -21.461 1.00 85.90  ? 90  ILE   A CG1 1 
ATOM   495  C  CG2 . ILE   A 1 70  ? -29.125 -38.308 -19.760 1.00 84.71  ? 90  ILE   A CG2 1 
ATOM   496  C  CD1 . ILE   A 1 70  ? -27.946 -38.887 -22.300 1.00 84.20  ? 90  ILE   A CD1 1 
ATOM   497  N  N   . LYS   A 1 71  ? -32.296 -39.786 -18.993 1.00 87.83  ? 91  LYS   A N   1 
ATOM   498  C  CA  . LYS   A 1 71  ? -33.381 -39.409 -18.083 1.00 91.25  ? 91  LYS   A CA  1 
ATOM   499  C  C   . LYS   A 1 71  ? -33.673 -40.490 -17.048 1.00 92.71  ? 91  LYS   A C   1 
ATOM   500  O  O   . LYS   A 1 71  ? -33.998 -40.185 -15.894 1.00 80.19  ? 91  LYS   A O   1 
ATOM   501  C  CB  . LYS   A 1 71  ? -34.643 -39.091 -18.887 1.00 98.10  ? 91  LYS   A CB  1 
ATOM   502  C  CG  . LYS   A 1 71  ? -35.779 -38.467 -18.087 1.00 94.18  ? 91  LYS   A CG  1 
ATOM   503  C  CD  . LYS   A 1 71  ? -37.144 -38.883 -18.605 1.00 106.66 ? 91  LYS   A CD  1 
ATOM   504  C  CE  . LYS   A 1 71  ? -38.232 -38.036 -17.967 1.00 121.95 ? 91  LYS   A CE  1 
ATOM   505  N  NZ  . LYS   A 1 71  ? -38.718 -36.987 -18.906 1.00 117.89 ? 91  LYS   A NZ  1 
ATOM   506  N  N   . THR   A 1 72  ? -33.562 -41.759 -17.441 1.00 87.57  ? 92  THR   A N   1 
ATOM   507  C  CA  . THR   A 1 72  ? -33.782 -42.849 -16.497 1.00 89.62  ? 92  THR   A CA  1 
ATOM   508  C  C   . THR   A 1 72  ? -32.728 -42.843 -15.396 1.00 102.99 ? 92  THR   A C   1 
ATOM   509  O  O   . THR   A 1 72  ? -33.049 -42.981 -14.209 1.00 105.57 ? 92  THR   A O   1 
ATOM   510  C  CB  . THR   A 1 72  ? -33.779 -44.188 -17.235 1.00 100.17 ? 92  THR   A CB  1 
ATOM   511  O  OG1 . THR   A 1 72  ? -34.849 -44.212 -18.189 1.00 93.67  ? 92  THR   A OG1 1 
ATOM   512  C  CG2 . THR   A 1 72  ? -33.942 -45.340 -16.259 1.00 93.11  ? 92  THR   A CG2 1 
ATOM   513  N  N   . VAL   A 1 73  ? -31.461 -42.665 -15.772 1.00 83.29  ? 93  VAL   A N   1 
ATOM   514  C  CA  . VAL   A 1 73  ? -30.375 -42.753 -14.801 1.00 89.87  ? 93  VAL   A CA  1 
ATOM   515  C  C   . VAL   A 1 73  ? -30.418 -41.579 -13.828 1.00 85.84  ? 93  VAL   A C   1 
ATOM   516  O  O   . VAL   A 1 73  ? -30.289 -41.760 -12.611 1.00 89.84  ? 93  VAL   A O   1 
ATOM   517  C  CB  . VAL   A 1 73  ? -29.017 -42.846 -15.520 1.00 95.42  ? 93  VAL   A CB  1 
ATOM   518  C  CG1 . VAL   A 1 73  ? -27.883 -42.518 -14.562 1.00 81.96  ? 93  VAL   A CG1 1 
ATOM   519  C  CG2 . VAL   A 1 73  ? -28.826 -44.234 -16.102 1.00 83.24  ? 93  VAL   A CG2 1 
ATOM   520  N  N   . LEU   A 1 74  ? -30.602 -40.358 -14.337 1.00 81.33  ? 94  LEU   A N   1 
ATOM   521  C  CA  . LEU   A 1 74  ? -30.487 -39.203 -13.451 1.00 89.62  ? 94  LEU   A CA  1 
ATOM   522  C  C   . LEU   A 1 74  ? -31.778 -38.900 -12.700 1.00 87.59  ? 94  LEU   A C   1 
ATOM   523  O  O   . LEU   A 1 74  ? -31.729 -38.282 -11.631 1.00 80.33  ? 94  LEU   A O   1 
ATOM   524  C  CB  . LEU   A 1 74  ? -30.066 -37.952 -14.225 1.00 81.23  ? 94  LEU   A CB  1 
ATOM   525  C  CG  . LEU   A 1 74  ? -28.842 -37.942 -15.134 1.00 92.56  ? 94  LEU   A CG  1 
ATOM   526  C  CD1 . LEU   A 1 74  ? -29.349 -37.865 -16.530 1.00 90.32  ? 94  LEU   A CD1 1 
ATOM   527  C  CD2 . LEU   A 1 74  ? -27.918 -36.765 -14.826 1.00 92.58  ? 94  LEU   A CD2 1 
ATOM   528  N  N   . VAL   A 1 75  ? -32.934 -39.296 -13.233 1.00 82.81  ? 95  VAL   A N   1 
ATOM   529  C  CA  . VAL   A 1 75  ? -34.199 -38.893 -12.623 1.00 100.92 ? 95  VAL   A CA  1 
ATOM   530  C  C   . VAL   A 1 75  ? -34.999 -40.106 -12.167 1.00 101.42 ? 95  VAL   A C   1 
ATOM   531  O  O   . VAL   A 1 75  ? -35.255 -40.275 -10.969 1.00 90.16  ? 95  VAL   A O   1 
ATOM   532  C  CB  . VAL   A 1 75  ? -35.033 -38.031 -13.588 1.00 86.68  ? 95  VAL   A CB  1 
ATOM   533  C  CG1 . VAL   A 1 75  ? -36.303 -37.547 -12.898 1.00 77.76  ? 95  VAL   A CG1 1 
ATOM   534  C  CG2 . VAL   A 1 75  ? -34.216 -36.856 -14.100 1.00 90.55  ? 95  VAL   A CG2 1 
ATOM   535  N  N   . LYS   A 1 76  ? -35.405 -40.950 -13.120 1.00 94.31  ? 96  LYS   A N   1 
ATOM   536  C  CA  . LYS   A 1 76  ? -36.330 -42.038 -12.812 1.00 100.81 ? 96  LYS   A CA  1 
ATOM   537  C  C   . LYS   A 1 76  ? -35.765 -42.980 -11.755 1.00 99.36  ? 96  LYS   A C   1 
ATOM   538  O  O   . LYS   A 1 76  ? -36.486 -43.407 -10.845 1.00 96.91  ? 96  LYS   A O   1 
ATOM   539  C  CB  . LYS   A 1 76  ? -36.667 -42.813 -14.088 1.00 115.25 ? 96  LYS   A CB  1 
ATOM   540  C  CG  . LYS   A 1 76  ? -37.596 -42.082 -15.051 1.00 113.70 ? 96  LYS   A CG  1 
ATOM   541  C  CD  . LYS   A 1 76  ? -38.777 -41.446 -14.334 1.00 125.90 ? 96  LYS   A CD  1 
ATOM   542  C  CE  . LYS   A 1 76  ? -40.036 -42.286 -14.494 1.00 138.16 ? 96  LYS   A CE  1 
ATOM   543  N  NZ  . LYS   A 1 76  ? -40.932 -42.183 -13.309 1.00 135.89 ? 96  LYS   A NZ  1 
ATOM   544  N  N   . GLU   A 1 77  ? -34.475 -43.309 -11.849 1.00 106.94 ? 97  GLU   A N   1 
ATOM   545  C  CA  . GLU   A 1 77  ? -33.871 -44.336 -11.008 1.00 107.93 ? 97  GLU   A CA  1 
ATOM   546  C  C   . GLU   A 1 77  ? -32.800 -43.783 -10.073 1.00 95.18  ? 97  GLU   A C   1 
ATOM   547  O  O   . GLU   A 1 77  ? -31.920 -44.533 -9.640  1.00 85.37  ? 97  GLU   A O   1 
ATOM   548  C  CB  . GLU   A 1 77  ? -33.278 -45.444 -11.881 1.00 98.92  ? 97  GLU   A CB  1 
ATOM   549  C  CG  . GLU   A 1 77  ? -34.287 -46.171 -12.757 1.00 95.37  ? 97  GLU   A CG  1 
ATOM   550  C  CD  . GLU   A 1 77  ? -35.522 -46.615 -12.000 1.00 104.32 ? 97  GLU   A CD  1 
ATOM   551  O  OE1 . GLU   A 1 77  ? -35.381 -47.117 -10.865 1.00 100.90 ? 97  GLU   A OE1 1 
ATOM   552  O  OE2 . GLU   A 1 77  ? -36.637 -46.462 -12.542 1.00 114.61 ? 97  GLU   A OE2 1 
ATOM   553  N  N   . CYS   A 1 78  ? -32.856 -42.491 -9.744  1.00 91.73  ? 98  CYS   A N   1 
ATOM   554  C  CA  . CYS   A 1 78  ? -31.799 -41.890 -8.935  1.00 81.72  ? 98  CYS   A CA  1 
ATOM   555  C  C   . CYS   A 1 78  ? -31.788 -42.463 -7.522  1.00 84.66  ? 98  CYS   A C   1 
ATOM   556  O  O   . CYS   A 1 78  ? -30.774 -42.997 -7.061  1.00 81.50  ? 98  CYS   A O   1 
ATOM   557  C  CB  . CYS   A 1 78  ? -31.960 -40.371 -8.897  1.00 88.34  ? 98  CYS   A CB  1 
ATOM   558  S  SG  . CYS   A 1 78  ? -30.773 -39.555 -7.800  1.00 94.59  ? 98  CYS   A SG  1 
ATOM   559  N  N   . TYR   A 1 79  ? -32.918 -42.364 -6.819  1.00 102.21 ? 99  TYR   A N   1 
ATOM   560  C  CA  . TYR   A 1 79  ? -32.963 -42.747 -5.413  1.00 91.02  ? 99  TYR   A CA  1 
ATOM   561  C  C   . TYR   A 1 79  ? -32.739 -44.238 -5.196  1.00 92.58  ? 99  TYR   A C   1 
ATOM   562  O  O   . TYR   A 1 79  ? -32.335 -44.637 -4.098  1.00 90.72  ? 99  TYR   A O   1 
ATOM   563  C  CB  . TYR   A 1 79  ? -34.299 -42.327 -4.798  1.00 95.99  ? 99  TYR   A CB  1 
ATOM   564  C  CG  . TYR   A 1 79  ? -34.336 -40.872 -4.396  1.00 121.42 ? 99  TYR   A CG  1 
ATOM   565  C  CD1 . TYR   A 1 79  ? -33.667 -40.431 -3.262  1.00 134.72 ? 99  TYR   A CD1 1 
ATOM   566  C  CD2 . TYR   A 1 79  ? -35.026 -39.936 -5.156  1.00 115.96 ? 99  TYR   A CD2 1 
ATOM   567  C  CE1 . TYR   A 1 79  ? -33.691 -39.099 -2.891  1.00 122.76 ? 99  TYR   A CE1 1 
ATOM   568  C  CE2 . TYR   A 1 79  ? -35.057 -38.605 -4.793  1.00 114.89 ? 99  TYR   A CE2 1 
ATOM   569  C  CZ  . TYR   A 1 79  ? -34.388 -38.190 -3.660  1.00 117.50 ? 99  TYR   A CZ  1 
ATOM   570  O  OH  . TYR   A 1 79  ? -34.416 -36.864 -3.296  1.00 107.01 ? 99  TYR   A OH  1 
ATOM   571  N  N   . SER   A 1 80  ? -32.984 -45.069 -6.209  1.00 97.77  ? 100 SER   A N   1 
ATOM   572  C  CA  . SER   A 1 80  ? -32.835 -46.512 -6.055  1.00 97.62  ? 100 SER   A CA  1 
ATOM   573  C  C   . SER   A 1 80  ? -31.441 -46.986 -6.460  1.00 100.90 ? 100 SER   A C   1 
ATOM   574  O  O   . SER   A 1 80  ? -30.715 -47.567 -5.648  1.00 102.52 ? 100 SER   A O   1 
ATOM   575  C  CB  . SER   A 1 80  ? -33.907 -47.241 -6.874  1.00 102.57 ? 100 SER   A CB  1 
ATOM   576  O  OG  . SER   A 1 80  ? -33.949 -46.761 -8.206  1.00 105.36 ? 100 SER   A OG  1 
ATOM   577  N  N   . VAL   A 1 81  ? -31.054 -46.738 -7.707  1.00 100.41 ? 101 VAL   A N   1 
ATOM   578  C  CA  . VAL   A 1 81  ? -29.849 -47.322 -8.285  1.00 104.28 ? 101 VAL   A CA  1 
ATOM   579  C  C   . VAL   A 1 81  ? -28.710 -46.315 -8.366  1.00 79.41  ? 101 VAL   A C   1 
ATOM   580  O  O   . VAL   A 1 81  ? -27.583 -46.608 -7.970  1.00 77.86  ? 101 VAL   A O   1 
ATOM   581  C  CB  . VAL   A 1 81  ? -30.164 -47.914 -9.677  1.00 104.85 ? 101 VAL   A CB  1 
ATOM   582  C  CG1 . VAL   A 1 81  ? -29.134 -48.967 -10.048 1.00 90.95  ? 101 VAL   A CG1 1 
ATOM   583  C  CG2 . VAL   A 1 81  ? -31.573 -48.482 -9.702  1.00 90.15  ? 101 VAL   A CG2 1 
ATOM   584  N  N   . PHE   A 1 82  ? -28.984 -45.124 -8.888  1.00 83.71  ? 102 PHE   A N   1 
ATOM   585  C  CA  . PHE   A 1 82  ? -27.945 -44.158 -9.227  1.00 77.86  ? 102 PHE   A CA  1 
ATOM   586  C  C   . PHE   A 1 82  ? -28.026 -42.966 -8.279  1.00 68.62  ? 102 PHE   A C   1 
ATOM   587  O  O   . PHE   A 1 82  ? -28.344 -41.842 -8.673  1.00 78.32  ? 102 PHE   A O   1 
ATOM   588  C  CB  . PHE   A 1 82  ? -28.092 -43.731 -10.689 1.00 86.79  ? 102 PHE   A CB  1 
ATOM   589  C  CG  . PHE   A 1 82  ? -28.313 -44.878 -11.634 1.00 83.21  ? 102 PHE   A CG  1 
ATOM   590  C  CD1 . PHE   A 1 82  ? -27.249 -45.647 -12.076 1.00 90.52  ? 102 PHE   A CD1 1 
ATOM   591  C  CD2 . PHE   A 1 82  ? -29.588 -45.193 -12.073 1.00 90.15  ? 102 PHE   A CD2 1 
ATOM   592  C  CE1 . PHE   A 1 82  ? -27.454 -46.703 -12.945 1.00 98.40  ? 102 PHE   A CE1 1 
ATOM   593  C  CE2 . PHE   A 1 82  ? -29.799 -46.249 -12.940 1.00 98.78  ? 102 PHE   A CE2 1 
ATOM   594  C  CZ  . PHE   A 1 82  ? -28.730 -47.005 -13.376 1.00 90.15  ? 102 PHE   A CZ  1 
ATOM   595  N  N   . THR   A 1 83  ? -27.725 -43.222 -7.007  1.00 75.20  ? 103 THR   A N   1 
ATOM   596  C  CA  . THR   A 1 83  ? -27.772 -42.178 -5.991  1.00 85.97  ? 103 THR   A CA  1 
ATOM   597  C  C   . THR   A 1 83  ? -26.452 -41.426 -5.867  1.00 76.13  ? 103 THR   A C   1 
ATOM   598  O  O   . THR   A 1 83  ? -26.451 -40.219 -5.603  1.00 76.09  ? 103 THR   A O   1 
ATOM   599  C  CB  . THR   A 1 83  ? -28.151 -42.782 -4.633  1.00 78.37  ? 103 THR   A CB  1 
ATOM   600  O  OG1 . THR   A 1 83  ? -29.344 -43.563 -4.769  1.00 82.63  ? 103 THR   A OG1 1 
ATOM   601  C  CG2 . THR   A 1 83  ? -28.384 -41.689 -3.596  1.00 73.79  ? 103 THR   A CG2 1 
ATOM   602  N  N   . ASN   A 1 84  ? -25.330 -42.107 -6.076  1.00 80.18  ? 104 ASN   A N   1 
ATOM   603  C  CA  . ASN   A 1 84  ? -24.024 -41.577 -5.725  1.00 74.92  ? 104 ASN   A CA  1 
ATOM   604  C  C   . ASN   A 1 84  ? -23.115 -41.526 -6.945  1.00 80.84  ? 104 ASN   A C   1 
ATOM   605  O  O   . ASN   A 1 84  ? -23.331 -42.228 -7.937  1.00 74.95  ? 104 ASN   A O   1 
ATOM   606  C  CB  . ASN   A 1 84  ? -23.383 -42.432 -4.631  1.00 78.51  ? 104 ASN   A CB  1 
ATOM   607  C  CG  . ASN   A 1 84  ? -24.360 -42.782 -3.526  1.00 89.18  ? 104 ASN   A CG  1 
ATOM   608  O  OD1 . ASN   A 1 84  ? -25.053 -41.914 -2.995  1.00 94.48  ? 104 ASN   A OD1 1 
ATOM   609  N  ND2 . ASN   A 1 84  ? -24.417 -44.061 -3.170  1.00 89.99  ? 104 ASN   A ND2 1 
ATOM   610  N  N   . ARG   A 1 85  ? -22.086 -40.684 -6.858  1.00 88.85  ? 105 ARG   A N   1 
ATOM   611  C  CA  . ARG   A 1 85  ? -21.083 -40.577 -7.905  1.00 68.63  ? 105 ARG   A CA  1 
ATOM   612  C  C   . ARG   A 1 85  ? -19.904 -41.493 -7.584  1.00 78.25  ? 105 ARG   A C   1 
ATOM   613  O  O   . ARG   A 1 85  ? -19.933 -42.273 -6.628  1.00 90.39  ? 105 ARG   A O   1 
ATOM   614  C  CB  . ARG   A 1 85  ? -20.607 -39.135 -8.067  1.00 77.07  ? 105 ARG   A CB  1 
ATOM   615  C  CG  . ARG   A 1 85  ? -21.654 -38.063 -7.858  1.00 72.72  ? 105 ARG   A CG  1 
ATOM   616  C  CD  . ARG   A 1 85  ? -21.083 -36.712 -8.262  1.00 76.83  ? 105 ARG   A CD  1 
ATOM   617  N  NE  . ARG   A 1 85  ? -22.086 -35.821 -8.832  1.00 85.00  ? 105 ARG   A NE  1 
ATOM   618  C  CZ  . ARG   A 1 85  ? -22.751 -34.906 -8.141  1.00 84.29  ? 105 ARG   A CZ  1 
ATOM   619  N  NH1 . ARG   A 1 85  ? -22.531 -34.720 -6.849  1.00 90.40  ? 105 ARG   A NH1 1 
ATOM   620  N  NH2 . ARG   A 1 85  ? -23.654 -34.153 -8.761  1.00 76.09  ? 105 ARG   A NH2 1 
ATOM   621  N  N   . ARG   A 1 86  ? -18.878 -41.418 -8.427  1.00 88.11  ? 106 ARG   A N   1 
ATOM   622  C  CA  . ARG   A 1 86  ? -17.700 -42.300 -8.252  1.00 90.98  ? 106 ARG   A CA  1 
ATOM   623  C  C   . ARG   A 1 86  ? -16.973 -41.900 -6.975  1.00 106.63 ? 106 ARG   A C   1 
ATOM   624  O  O   . ARG   A 1 86  ? -16.781 -40.697 -6.753  1.00 108.43 ? 106 ARG   A O   1 
ATOM   625  C  CB  . ARG   A 1 86  ? -16.780 -42.169 -9.465  1.00 97.48  ? 106 ARG   A CB  1 
ATOM   626  C  CG  . ARG   A 1 86  ? -15.825 -43.335 -9.661  1.00 103.37 ? 106 ARG   A CG  1 
ATOM   627  C  CD  . ARG   A 1 86  ? -14.743 -42.970 -10.656 1.00 99.75  ? 106 ARG   A CD  1 
ATOM   628  N  NE  . ARG   A 1 86  ? -15.281 -42.535 -11.934 1.00 73.01  ? 106 ARG   A NE  1 
ATOM   629  C  CZ  . ARG   A 1 86  ? -14.821 -42.945 -13.107 1.00 85.27  ? 106 ARG   A CZ  1 
ATOM   630  N  NH1 . ARG   A 1 86  ? -13.817 -43.802 -13.153 1.00 86.75  ? 106 ARG   A NH1 1 
ATOM   631  N  NH2 . ARG   A 1 86  ? -15.361 -42.503 -14.227 1.00 69.71  ? 106 ARG   A NH2 1 
ATOM   632  N  N   . PRO   A 1 87  ? -16.570 -42.864 -6.129  1.00 109.17 ? 107 PRO   A N   1 
ATOM   633  C  CA  . PRO   A 1 87  ? -15.901 -42.545 -4.878  1.00 121.41 ? 107 PRO   A CA  1 
ATOM   634  C  C   . PRO   A 1 87  ? -14.675 -41.666 -5.154  1.00 128.54 ? 107 PRO   A C   1 
ATOM   635  O  O   . PRO   A 1 87  ? -13.962 -41.948 -6.092  1.00 134.62 ? 107 PRO   A O   1 
ATOM   636  C  CB  . PRO   A 1 87  ? -15.493 -43.919 -4.328  1.00 119.25 ? 107 PRO   A CB  1 
ATOM   637  C  CG  . PRO   A 1 87  ? -15.600 -44.858 -5.509  1.00 112.01 ? 107 PRO   A CG  1 
ATOM   638  C  CD  . PRO   A 1 87  ? -16.733 -44.298 -6.339  1.00 104.01 ? 107 PRO   A CD  1 
ATOM   639  N  N   . PHE   A 1 88  ? -14.469 -40.629 -4.340  1.00 116.70 ? 108 PHE   A N   1 
ATOM   640  C  CA  . PHE   A 1 88  ? -13.321 -39.708 -4.532  1.00 127.67 ? 108 PHE   A CA  1 
ATOM   641  C  C   . PHE   A 1 88  ? -12.475 -39.699 -3.260  1.00 134.58 ? 108 PHE   A C   1 
ATOM   642  O  O   . PHE   A 1 88  ? -13.022 -39.387 -2.192  1.00 140.03 ? 108 PHE   A O   1 
ATOM   643  C  CB  . PHE   A 1 88  ? -13.820 -38.298 -4.848  1.00 124.93 ? 108 PHE   A CB  1 
ATOM   644  C  CG  . PHE   A 1 88  ? -12.743 -37.255 -4.987  1.00 133.05 ? 108 PHE   A CG  1 
ATOM   645  C  CD1 . PHE   A 1 88  ? -11.823 -37.320 -6.019  1.00 147.81 ? 108 PHE   A CD1 1 
ATOM   646  C  CD2 . PHE   A 1 88  ? -12.656 -36.202 -4.092  1.00 135.24 ? 108 PHE   A CD2 1 
ATOM   647  C  CE1 . PHE   A 1 88  ? -10.835 -36.358 -6.150  1.00 145.77 ? 108 PHE   A CE1 1 
ATOM   648  C  CE2 . PHE   A 1 88  ? -11.667 -35.241 -4.223  1.00 143.44 ? 108 PHE   A CE2 1 
ATOM   649  C  CZ  . PHE   A 1 88  ? -10.759 -35.320 -5.252  1.00 141.98 ? 108 PHE   A CZ  1 
ATOM   650  N  N   . GLY   A 1 89  ? -11.189 -40.035 -3.375  1.00 139.62 ? 109 GLY   A N   1 
ATOM   651  C  CA  . GLY   A 1 89  ? -10.309 -40.091 -2.191  1.00 145.15 ? 109 GLY   A CA  1 
ATOM   652  C  C   . GLY   A 1 89  ? -8.845  -39.979 -2.567  1.00 141.91 ? 109 GLY   A C   1 
ATOM   653  O  O   . GLY   A 1 89  ? -8.531  -40.175 -3.753  1.00 142.41 ? 109 GLY   A O   1 
ATOM   654  N  N   . PRO   A 1 90  ? -7.928  -39.673 -1.624  1.00 139.30 ? 110 PRO   A N   1 
ATOM   655  C  CA  . PRO   A 1 90  ? -8.279  -39.528 -0.210  1.00 150.12 ? 110 PRO   A CA  1 
ATOM   656  C  C   . PRO   A 1 90  ? -8.982  -38.193 0.062   1.00 155.66 ? 110 PRO   A C   1 
ATOM   657  O  O   . PRO   A 1 90  ? -8.617  -37.214 -0.554  1.00 155.30 ? 110 PRO   A O   1 
ATOM   658  C  CB  . PRO   A 1 90  ? -6.914  -39.553 0.481   1.00 145.51 ? 110 PRO   A CB  1 
ATOM   659  C  CG  . PRO   A 1 90  ? -5.979  -38.955 -0.541  1.00 147.74 ? 110 PRO   A CG  1 
ATOM   660  C  CD  . PRO   A 1 90  ? -6.501  -39.462 -1.869  1.00 139.47 ? 110 PRO   A CD  1 
ATOM   661  N  N   . VAL   A 1 91  ? -9.954  -38.183 0.978   1.00 161.85 ? 111 VAL   A N   1 
ATOM   662  C  CA  . VAL   A 1 91  ? -10.751 -36.942 1.208   1.00 160.15 ? 111 VAL   A CA  1 
ATOM   663  C  C   . VAL   A 1 91  ? -10.637 -36.491 2.669   1.00 161.81 ? 111 VAL   A C   1 
ATOM   664  O  O   . VAL   A 1 91  ? -10.516 -35.272 2.883   1.00 158.87 ? 111 VAL   A O   1 
ATOM   665  C  CB  . VAL   A 1 91  ? -12.221 -37.151 0.803   1.00 159.15 ? 111 VAL   A CB  1 
ATOM   666  C  CG1 . VAL   A 1 91  ? -12.489 -36.643 -0.604  1.00 156.32 ? 111 VAL   A CG1 1 
ATOM   667  C  CG2 . VAL   A 1 91  ? -12.644 -38.604 0.943   1.00 163.55 ? 111 VAL   A CG2 1 
ATOM   668  N  N   . GLY   A 1 92  ? -10.701 -37.416 3.633   1.00 150.62 ? 112 GLY   A N   1 
ATOM   669  C  CA  . GLY   A 1 92  ? -10.638 -37.019 5.030   1.00 150.26 ? 112 GLY   A CA  1 
ATOM   670  C  C   . GLY   A 1 92  ? -12.012 -36.640 5.528   1.00 141.22 ? 112 GLY   A C   1 
ATOM   671  O  O   . GLY   A 1 92  ? -12.979 -37.384 5.344   1.00 141.22 ? 112 GLY   A O   1 
ATOM   672  N  N   . PHE   A 1 93  ? -12.112 -35.469 6.157   1.00 130.12 ? 113 PHE   A N   1 
ATOM   673  C  CA  . PHE   A 1 93  ? -13.402 -34.996 6.638   1.00 131.04 ? 113 PHE   A CA  1 
ATOM   674  C  C   . PHE   A 1 93  ? -14.313 -34.531 5.511   1.00 126.69 ? 113 PHE   A C   1 
ATOM   675  O  O   . PHE   A 1 93  ? -15.502 -34.296 5.755   1.00 120.55 ? 113 PHE   A O   1 
ATOM   676  C  CB  . PHE   A 1 93  ? -13.204 -33.865 7.643   1.00 130.36 ? 113 PHE   A CB  1 
ATOM   677  C  CG  . PHE   A 1 93  ? -12.944 -32.525 7.016   1.00 130.06 ? 113 PHE   A CG  1 
ATOM   678  C  CD1 . PHE   A 1 93  ? -11.736 -32.256 6.397   1.00 138.77 ? 113 PHE   A CD1 1 
ATOM   679  C  CD2 . PHE   A 1 93  ? -13.904 -31.525 7.064   1.00 130.00 ? 113 PHE   A CD2 1 
ATOM   680  C  CE1 . PHE   A 1 93  ? -11.493 -31.022 5.826   1.00 144.30 ? 113 PHE   A CE1 1 
ATOM   681  C  CE2 . PHE   A 1 93  ? -13.667 -30.288 6.493   1.00 134.30 ? 113 PHE   A CE2 1 
ATOM   682  C  CZ  . PHE   A 1 93  ? -12.460 -30.037 5.874   1.00 135.90 ? 113 PHE   A CZ  1 
ATOM   683  N  N   . MET   A 1 94  ? -13.789 -34.397 4.295   1.00 131.08 ? 114 MET   A N   1 
ATOM   684  C  CA  . MET   A 1 94  ? -14.577 -33.967 3.149   1.00 129.03 ? 114 MET   A CA  1 
ATOM   685  C  C   . MET   A 1 94  ? -15.445 -35.077 2.572   1.00 131.62 ? 114 MET   A C   1 
ATOM   686  O  O   . MET   A 1 94  ? -16.146 -34.839 1.583   1.00 116.80 ? 114 MET   A O   1 
ATOM   687  C  CB  . MET   A 1 94  ? -13.655 -33.412 2.062   1.00 131.45 ? 114 MET   A CB  1 
ATOM   688  C  CG  . MET   A 1 94  ? -12.899 -32.162 2.480   1.00 140.35 ? 114 MET   A CG  1 
ATOM   689  S  SD  . MET   A 1 94  ? -13.957 -30.702 2.512   1.00 120.75 ? 114 MET   A SD  1 
ATOM   690  C  CE  . MET   A 1 94  ? -14.558 -30.689 0.825   1.00 108.80 ? 114 MET   A CE  1 
ATOM   691  N  N   . LYS   A 1 95  ? -15.414 -36.280 3.153   1.00 127.10 ? 115 LYS   A N   1 
ATOM   692  C  CA  . LYS   A 1 95  ? -16.358 -37.314 2.742   1.00 126.30 ? 115 LYS   A CA  1 
ATOM   693  C  C   . LYS   A 1 95  ? -17.792 -36.868 2.982   1.00 118.88 ? 115 LYS   A C   1 
ATOM   694  O  O   . LYS   A 1 95  ? -18.707 -37.298 2.270   1.00 115.43 ? 115 LYS   A O   1 
ATOM   695  C  CB  . LYS   A 1 95  ? -16.056 -38.624 3.479   1.00 127.74 ? 115 LYS   A CB  1 
ATOM   696  C  CG  . LYS   A 1 95  ? -16.010 -38.541 5.011   1.00 129.28 ? 115 LYS   A CG  1 
ATOM   697  C  CD  . LYS   A 1 95  ? -17.388 -38.610 5.666   1.00 134.52 ? 115 LYS   A CD  1 
ATOM   698  C  CE  . LYS   A 1 95  ? -17.316 -38.284 7.149   1.00 130.42 ? 115 LYS   A CE  1 
ATOM   699  N  NZ  . LYS   A 1 95  ? -18.602 -37.744 7.669   1.00 139.95 ? 115 LYS   A NZ  1 
ATOM   700  N  N   . SER   A 1 96  ? -17.999 -35.999 3.969   1.00 125.27 ? 116 SER   A N   1 
ATOM   701  C  CA  . SER   A 1 96  ? -19.313 -35.485 4.312   1.00 123.12 ? 116 SER   A CA  1 
ATOM   702  C  C   . SER   A 1 96  ? -19.707 -34.264 3.497   1.00 106.61 ? 116 SER   A C   1 
ATOM   703  O  O   . SER   A 1 96  ? -20.832 -33.779 3.648   1.00 101.81 ? 116 SER   A O   1 
ATOM   704  C  CB  . SER   A 1 96  ? -19.364 -35.135 5.799   1.00 124.53 ? 116 SER   A CB  1 
ATOM   705  O  OG  . SER   A 1 96  ? -18.183 -34.466 6.205   1.00 126.52 ? 116 SER   A OG  1 
ATOM   706  N  N   . ALA   A 1 97  ? -18.809 -33.741 2.666   1.00 107.88 ? 117 ALA   A N   1 
ATOM   707  C  CA  . ALA   A 1 97  ? -19.199 -32.706 1.721   1.00 103.45 ? 117 ALA   A CA  1 
ATOM   708  C  C   . ALA   A 1 97  ? -20.326 -33.224 0.839   1.00 98.52  ? 117 ALA   A C   1 
ATOM   709  O  O   . ALA   A 1 97  ? -20.306 -34.376 0.397   1.00 104.98 ? 117 ALA   A O   1 
ATOM   710  C  CB  . ALA   A 1 97  ? -18.002 -32.280 0.873   1.00 106.67 ? 117 ALA   A CB  1 
ATOM   711  N  N   . ILE   A 1 98  ? -21.321 -32.367 0.597   1.00 92.81  ? 118 ILE   A N   1 
ATOM   712  C  CA  . ILE   A 1 98  ? -22.556 -32.816 -0.045  1.00 88.18  ? 118 ILE   A CA  1 
ATOM   713  C  C   . ILE   A 1 98  ? -22.270 -33.416 -1.417  1.00 87.79  ? 118 ILE   A C   1 
ATOM   714  O  O   . ILE   A 1 98  ? -22.844 -34.446 -1.790  1.00 91.26  ? 118 ILE   A O   1 
ATOM   715  C  CB  . ILE   A 1 98  ? -23.566 -31.657 -0.134  1.00 94.18  ? 118 ILE   A CB  1 
ATOM   716  C  CG1 . ILE   A 1 98  ? -24.724 -32.037 -1.056  1.00 78.62  ? 118 ILE   A CG1 1 
ATOM   717  C  CG2 . ILE   A 1 98  ? -22.888 -30.389 -0.628  1.00 83.49  ? 118 ILE   A CG2 1 
ATOM   718  C  CD1 . ILE   A 1 98  ? -26.016 -31.341 -0.727  1.00 91.06  ? 118 ILE   A CD1 1 
ATOM   719  N  N   . SER   A 1 99  ? -21.375 -32.790 -2.185  1.00 96.61  ? 119 SER   A N   1 
ATOM   720  C  CA  . SER   A 1 99  ? -21.028 -33.316 -3.500  1.00 96.94  ? 119 SER   A CA  1 
ATOM   721  C  C   . SER   A 1 99  ? -20.418 -34.709 -3.422  1.00 93.80  ? 119 SER   A C   1 
ATOM   722  O  O   . SER   A 1 99  ? -20.468 -35.453 -4.408  1.00 86.20  ? 119 SER   A O   1 
ATOM   723  C  CB  . SER   A 1 99  ? -20.056 -32.372 -4.209  1.00 100.08 ? 119 SER   A CB  1 
ATOM   724  O  OG  . SER   A 1 99  ? -18.825 -32.296 -3.511  1.00 105.20 ? 119 SER   A OG  1 
ATOM   725  N  N   . ILE   A 1 100 ? -19.855 -35.081 -2.274  1.00 103.06 ? 120 ILE   A N   1 
ATOM   726  C  CA  . ILE   A 1 100 ? -19.154 -36.345 -2.132  1.00 95.07  ? 120 ILE   A CA  1 
ATOM   727  C  C   . ILE   A 1 100 ? -19.947 -37.366 -1.317  1.00 94.91  ? 120 ILE   A C   1 
ATOM   728  O  O   . ILE   A 1 100 ? -19.807 -38.572 -1.555  1.00 100.01 ? 120 ILE   A O   1 
ATOM   729  C  CB  . ILE   A 1 100 ? -17.760 -36.099 -1.511  1.00 104.55 ? 120 ILE   A CB  1 
ATOM   730  C  CG1 . ILE   A 1 100 ? -16.851 -35.397 -2.523  1.00 110.56 ? 120 ILE   A CG1 1 
ATOM   731  C  CG2 . ILE   A 1 100 ? -17.107 -37.398 -1.047  1.00 101.03 ? 120 ILE   A CG2 1 
ATOM   732  C  CD1 . ILE   A 1 100 ? -15.633 -34.741 -1.904  1.00 123.99 ? 120 ILE   A CD1 1 
ATOM   733  N  N   . ALA   A 1 101 ? -20.807 -36.918 -0.402  1.00 97.25  ? 121 ALA   A N   1 
ATOM   734  C  CA  . ALA   A 1 101 ? -21.512 -37.824 0.497   1.00 101.71 ? 121 ALA   A CA  1 
ATOM   735  C  C   . ALA   A 1 101 ? -22.414 -38.783 -0.273  1.00 94.97  ? 121 ALA   A C   1 
ATOM   736  O  O   . ALA   A 1 101 ? -22.920 -38.470 -1.354  1.00 67.36  ? 121 ALA   A O   1 
ATOM   737  C  CB  . ALA   A 1 101 ? -22.339 -37.029 1.507   1.00 98.37  ? 121 ALA   A CB  1 
ATOM   738  N  N   . GLU   A 1 102 ? -22.627 -39.958 0.312   1.00 89.92  ? 122 GLU   A N   1 
ATOM   739  C  CA  . GLU   A 1 102 ? -23.311 -41.059 -0.347  1.00 92.68  ? 122 GLU   A CA  1 
ATOM   740  C  C   . GLU   A 1 102 ? -24.678 -41.314 0.279   1.00 99.67  ? 122 GLU   A C   1 
ATOM   741  O  O   . GLU   A 1 102 ? -24.903 -41.029 1.459   1.00 108.27 ? 122 GLU   A O   1 
ATOM   742  C  CB  . GLU   A 1 102 ? -22.486 -42.348 -0.269  1.00 101.37 ? 122 GLU   A CB  1 
ATOM   743  C  CG  . GLU   A 1 102 ? -21.768 -42.711 -1.553  1.00 101.88 ? 122 GLU   A CG  1 
ATOM   744  C  CD  . GLU   A 1 102 ? -20.755 -43.826 -1.383  1.00 125.45 ? 122 GLU   A CD  1 
ATOM   745  O  OE1 . GLU   A 1 102 ? -20.366 -44.127 -0.234  1.00 127.16 ? 122 GLU   A OE1 1 
ATOM   746  O  OE2 . GLU   A 1 102 ? -20.371 -44.423 -2.409  1.00 122.19 ? 122 GLU   A OE2 1 
ATOM   747  N  N   . ASP   A 1 103 ? -25.585 -41.859 -0.536  1.00 93.39  ? 123 ASP   A N   1 
ATOM   748  C  CA  . ASP   A 1 103 ? -26.847 -42.451 -0.093  1.00 111.47 ? 123 ASP   A CA  1 
ATOM   749  C  C   . ASP   A 1 103 ? -27.638 -41.599 0.895   1.00 119.19 ? 123 ASP   A C   1 
ATOM   750  O  O   . ASP   A 1 103 ? -27.983 -40.449 0.603   1.00 109.91 ? 123 ASP   A O   1 
ATOM   751  C  CB  . ASP   A 1 103 ? -26.582 -43.828 0.522   1.00 114.53 ? 123 ASP   A CB  1 
ATOM   752  C  CG  . ASP   A 1 103 ? -26.344 -44.898 -0.525  1.00 111.17 ? 123 ASP   A CG  1 
ATOM   753  O  OD1 . ASP   A 1 103 ? -27.294 -45.229 -1.264  1.00 101.85 ? 123 ASP   A OD1 1 
ATOM   754  O  OD2 . ASP   A 1 103 ? -25.207 -45.408 -0.609  1.00 108.19 ? 123 ASP   A OD2 1 
ATOM   755  N  N   . GLU   A 1 104 ? -27.939 -42.172 2.065   1.00 131.69 ? 124 GLU   A N   1 
ATOM   756  C  CA  . GLU   A 1 104 ? -28.804 -41.502 3.031   1.00 136.42 ? 124 GLU   A CA  1 
ATOM   757  C  C   . GLU   A 1 104 ? -28.124 -40.290 3.653   1.00 126.73 ? 124 GLU   A C   1 
ATOM   758  O  O   . GLU   A 1 104 ? -28.795 -39.306 3.985   1.00 126.71 ? 124 GLU   A O   1 
ATOM   759  C  CB  . GLU   A 1 104 ? -29.232 -42.485 4.122   1.00 144.66 ? 124 GLU   A CB  1 
ATOM   760  C  CG  . GLU   A 1 104 ? -29.518 -43.891 3.612   1.00 147.46 ? 124 GLU   A CG  1 
ATOM   761  C  CD  . GLU   A 1 104 ? -30.557 -43.921 2.507   1.00 153.99 ? 124 GLU   A CD  1 
ATOM   762  O  OE1 . GLU   A 1 104 ? -31.510 -43.115 2.555   1.00 152.65 ? 124 GLU   A OE1 1 
ATOM   763  O  OE2 . GLU   A 1 104 ? -30.414 -44.750 1.583   1.00 160.00 ? 124 GLU   A OE2 1 
ATOM   764  N  N   . GLU   A 1 105 ? -26.801 -40.346 3.828   1.00 123.16 ? 125 GLU   A N   1 
ATOM   765  C  CA  . GLU   A 1 105 ? -26.071 -39.193 4.342   1.00 125.48 ? 125 GLU   A CA  1 
ATOM   766  C  C   . GLU   A 1 105 ? -26.198 -37.995 3.409   1.00 120.15 ? 125 GLU   A C   1 
ATOM   767  O  O   . GLU   A 1 105 ? -26.204 -36.848 3.869   1.00 117.53 ? 125 GLU   A O   1 
ATOM   768  C  CB  . GLU   A 1 105 ? -24.603 -39.567 4.556   1.00 139.06 ? 125 GLU   A CB  1 
ATOM   769  C  CG  . GLU   A 1 105 ? -23.680 -38.407 4.894   1.00 149.06 ? 125 GLU   A CG  1 
ATOM   770  C  CD  . GLU   A 1 105 ? -22.215 -38.780 4.762   1.00 152.29 ? 125 GLU   A CD  1 
ATOM   771  O  OE1 . GLU   A 1 105 ? -21.871 -39.508 3.807   1.00 149.83 ? 125 GLU   A OE1 1 
ATOM   772  O  OE2 . GLU   A 1 105 ? -21.409 -38.350 5.613   1.00 153.03 ? 125 GLU   A OE2 1 
ATOM   773  N  N   . TRP   A 1 106 ? -26.319 -38.241 2.103   1.00 108.43 ? 126 TRP   A N   1 
ATOM   774  C  CA  . TRP   A 1 106 ? -26.502 -37.156 1.145   1.00 105.56 ? 126 TRP   A CA  1 
ATOM   775  C  C   . TRP   A 1 106 ? -27.921 -36.600 1.196   1.00 99.57  ? 126 TRP   A C   1 
ATOM   776  O  O   . TRP   A 1 106 ? -28.119 -35.381 1.150   1.00 85.70  ? 126 TRP   A O   1 
ATOM   777  C  CB  . TRP   A 1 106 ? -26.179 -37.642 -0.268  1.00 88.88  ? 126 TRP   A CB  1 
ATOM   778  C  CG  . TRP   A 1 106 ? -26.769 -36.769 -1.329  1.00 86.34  ? 126 TRP   A CG  1 
ATOM   779  C  CD1 . TRP   A 1 106 ? -26.287 -35.570 -1.763  1.00 76.53  ? 126 TRP   A CD1 1 
ATOM   780  C  CD2 . TRP   A 1 106 ? -27.970 -37.012 -2.072  1.00 89.76  ? 126 TRP   A CD2 1 
ATOM   781  N  NE1 . TRP   A 1 106 ? -27.104 -35.057 -2.740  1.00 82.02  ? 126 TRP   A NE1 1 
ATOM   782  C  CE2 . TRP   A 1 106 ? -28.146 -35.923 -2.947  1.00 87.27  ? 126 TRP   A CE2 1 
ATOM   783  C  CE3 . TRP   A 1 106 ? -28.910 -38.047 -2.085  1.00 101.11 ? 126 TRP   A CE3 1 
ATOM   784  C  CZ2 . TRP   A 1 106 ? -29.225 -35.838 -3.825  1.00 100.97 ? 126 TRP   A CZ2 1 
ATOM   785  C  CZ3 . TRP   A 1 106 ? -29.979 -37.961 -2.961  1.00 92.99  ? 126 TRP   A CZ3 1 
ATOM   786  C  CH2 . TRP   A 1 106 ? -30.126 -36.866 -3.819  1.00 97.41  ? 126 TRP   A CH2 1 
ATOM   787  N  N   . LYS   A 1 107 ? -28.917 -37.487 1.273   1.00 108.31 ? 127 LYS   A N   1 
ATOM   788  C  CA  . LYS   A 1 107 ? -30.316 -37.067 1.322   1.00 103.47 ? 127 LYS   A CA  1 
ATOM   789  C  C   . LYS   A 1 107 ? -30.568 -36.063 2.439   1.00 108.59 ? 127 LYS   A C   1 
ATOM   790  O  O   . LYS   A 1 107 ? -31.376 -35.139 2.287   1.00 86.82  ? 127 LYS   A O   1 
ATOM   791  C  CB  . LYS   A 1 107 ? -31.208 -38.296 1.496   1.00 89.82  ? 127 LYS   A CB  1 
ATOM   792  C  CG  . LYS   A 1 107 ? -32.451 -38.332 0.626   1.00 92.96  ? 127 LYS   A CG  1 
ATOM   793  C  CD  . LYS   A 1 107 ? -33.341 -39.486 1.060   1.00 127.00 ? 127 LYS   A CD  1 
ATOM   794  C  CE  . LYS   A 1 107 ? -34.323 -39.059 2.140   1.00 116.14 ? 127 LYS   A CE  1 
ATOM   795  N  NZ  . LYS   A 1 107 ? -35.138 -40.207 2.632   1.00 111.08 ? 127 LYS   A NZ  1 
ATOM   796  N  N   . ARG   A 1 108 ? -29.880 -36.227 3.568   1.00 106.25 ? 128 ARG   A N   1 
ATOM   797  C  CA  . ARG   A 1 108 ? -30.066 -35.334 4.705   1.00 107.04 ? 128 ARG   A CA  1 
ATOM   798  C  C   . ARG   A 1 108 ? -29.400 -33.981 4.475   1.00 110.93 ? 128 ARG   A C   1 
ATOM   799  O  O   . ARG   A 1 108 ? -29.957 -32.941 4.848   1.00 105.06 ? 128 ARG   A O   1 
ATOM   800  C  CB  . ARG   A 1 108 ? -29.525 -36.002 5.968   1.00 101.52 ? 128 ARG   A CB  1 
ATOM   801  C  CG  . ARG   A 1 108 ? -29.915 -35.330 7.265   1.00 131.17 ? 128 ARG   A CG  1 
ATOM   802  C  CD  . ARG   A 1 108 ? -28.954 -35.739 8.364   1.00 146.04 ? 128 ARG   A CD  1 
ATOM   803  N  NE  . ARG   A 1 108 ? -28.079 -34.644 8.761   1.00 154.14 ? 128 ARG   A NE  1 
ATOM   804  C  CZ  . ARG   A 1 108 ? -26.758 -34.737 8.840   1.00 151.96 ? 128 ARG   A CZ  1 
ATOM   805  N  NH1 . ARG   A 1 108 ? -26.126 -35.860 8.543   1.00 144.74 ? 128 ARG   A NH1 1 
ATOM   806  N  NH2 . ARG   A 1 108 ? -26.056 -33.677 9.230   1.00 156.43 ? 128 ARG   A NH2 1 
ATOM   807  N  N   . LEU   A 1 109 ? -28.212 -33.975 3.867   1.00 109.71 ? 129 LEU   A N   1 
ATOM   808  C  CA  . LEU   A 1 109 ? -27.534 -32.717 3.566   1.00 104.38 ? 129 LEU   A CA  1 
ATOM   809  C  C   . LEU   A 1 109 ? -28.291 -31.926 2.507   1.00 105.78 ? 129 LEU   A C   1 
ATOM   810  O  O   . LEU   A 1 109 ? -28.457 -30.707 2.628   1.00 103.72 ? 129 LEU   A O   1 
ATOM   811  C  CB  . LEU   A 1 109 ? -26.107 -32.995 3.100   1.00 102.81 ? 129 LEU   A CB  1 
ATOM   812  C  CG  . LEU   A 1 109 ? -25.225 -33.823 4.032   1.00 100.25 ? 129 LEU   A CG  1 
ATOM   813  C  CD1 . LEU   A 1 109 ? -23.897 -34.096 3.363   1.00 92.29  ? 129 LEU   A CD1 1 
ATOM   814  C  CD2 . LEU   A 1 109 ? -25.019 -33.110 5.358   1.00 109.68 ? 129 LEU   A CD2 1 
ATOM   815  N  N   . ARG   A 1 110 ? -28.755 -32.611 1.457   1.00 100.62 ? 130 ARG   A N   1 
ATOM   816  C  CA  . ARG   A 1 110 ? -29.432 -31.931 0.357   1.00 97.41  ? 130 ARG   A CA  1 
ATOM   817  C  C   . ARG   A 1 110 ? -30.693 -31.222 0.832   1.00 101.20 ? 130 ARG   A C   1 
ATOM   818  O  O   . ARG   A 1 110 ? -31.004 -30.117 0.372   1.00 112.49 ? 130 ARG   A O   1 
ATOM   819  C  CB  . ARG   A 1 110 ? -29.759 -32.935 -0.748  1.00 84.69  ? 130 ARG   A CB  1 
ATOM   820  C  CG  . ARG   A 1 110 ? -30.425 -32.328 -1.968  1.00 79.93  ? 130 ARG   A CG  1 
ATOM   821  C  CD  . ARG   A 1 110 ? -29.484 -32.321 -3.160  1.00 80.38  ? 130 ARG   A CD  1 
ATOM   822  N  NE  . ARG   A 1 110 ? -29.875 -31.330 -4.154  1.00 83.15  ? 130 ARG   A NE  1 
ATOM   823  C  CZ  . ARG   A 1 110 ? -29.249 -31.139 -5.308  1.00 85.70  ? 130 ARG   A CZ  1 
ATOM   824  N  NH1 . ARG   A 1 110 ? -28.185 -31.850 -5.642  1.00 103.00 ? 130 ARG   A NH1 1 
ATOM   825  N  NH2 . ARG   A 1 110 ? -29.703 -30.212 -6.147  1.00 71.50  ? 130 ARG   A NH2 1 
ATOM   826  N  N   . SER   A 1 111 ? -31.432 -31.840 1.755   1.00 107.54 ? 131 SER   A N   1 
ATOM   827  C  CA  . SER   A 1 111 ? -32.619 -31.196 2.307   1.00 108.10 ? 131 SER   A CA  1 
ATOM   828  C  C   . SER   A 1 111 ? -32.240 -29.983 3.148   1.00 106.08 ? 131 SER   A C   1 
ATOM   829  O  O   . SER   A 1 111 ? -32.851 -28.915 3.029   1.00 114.72 ? 131 SER   A O   1 
ATOM   830  C  CB  . SER   A 1 111 ? -33.417 -32.198 3.141   1.00 111.81 ? 131 SER   A CB  1 
ATOM   831  O  OG  . SER   A 1 111 ? -34.436 -32.813 2.374   1.00 135.33 ? 131 SER   A OG  1 
ATOM   832  N  N   . LEU   A 1 112 ? -31.226 -30.132 4.003   1.00 103.98 ? 132 LEU   A N   1 
ATOM   833  C  CA  . LEU   A 1 112 ? -30.846 -29.054 4.910   1.00 117.30 ? 132 LEU   A CA  1 
ATOM   834  C  C   . LEU   A 1 112 ? -30.264 -27.864 4.157   1.00 114.53 ? 132 LEU   A C   1 
ATOM   835  O  O   . LEU   A 1 112 ? -30.357 -26.727 4.633   1.00 118.43 ? 132 LEU   A O   1 
ATOM   836  C  CB  . LEU   A 1 112 ? -29.863 -29.596 5.955   1.00 119.66 ? 132 LEU   A CB  1 
ATOM   837  C  CG  . LEU   A 1 112 ? -29.047 -28.751 6.940   1.00 137.75 ? 132 LEU   A CG  1 
ATOM   838  C  CD1 . LEU   A 1 112 ? -28.616 -29.676 8.053   1.00 156.22 ? 132 LEU   A CD1 1 
ATOM   839  C  CD2 . LEU   A 1 112 ? -27.817 -28.099 6.327   1.00 139.12 ? 132 LEU   A CD2 1 
ATOM   840  N  N   . LEU   A 1 113 ? -29.673 -28.099 2.987   1.00 112.30 ? 133 LEU   A N   1 
ATOM   841  C  CA  . LEU   A 1 113 ? -29.078 -27.036 2.187   1.00 117.09 ? 133 LEU   A CA  1 
ATOM   842  C  C   . LEU   A 1 113 ? -29.966 -26.550 1.051   1.00 121.20 ? 133 LEU   A C   1 
ATOM   843  O  O   . LEU   A 1 113 ? -29.628 -25.546 0.415   1.00 128.84 ? 133 LEU   A O   1 
ATOM   844  C  CB  . LEU   A 1 113 ? -27.730 -27.500 1.621   1.00 119.12 ? 133 LEU   A CB  1 
ATOM   845  C  CG  . LEU   A 1 113 ? -26.676 -27.722 2.696   1.00 104.86 ? 133 LEU   A CG  1 
ATOM   846  C  CD1 . LEU   A 1 113 ? -25.325 -28.031 2.082   1.00 103.03 ? 133 LEU   A CD1 1 
ATOM   847  C  CD2 . LEU   A 1 113 ? -26.610 -26.447 3.494   1.00 112.17 ? 133 LEU   A CD2 1 
ATOM   848  N  N   . SER   A 1 114 ? -31.081 -27.224 0.785   1.00 115.51 ? 134 SER   A N   1 
ATOM   849  C  CA  . SER   A 1 114 ? -31.991 -26.799 -0.278  1.00 120.46 ? 134 SER   A CA  1 
ATOM   850  C  C   . SER   A 1 114 ? -32.532 -25.381 -0.120  1.00 120.20 ? 134 SER   A C   1 
ATOM   851  O  O   . SER   A 1 114 ? -32.474 -24.614 -1.096  1.00 120.17 ? 134 SER   A O   1 
ATOM   852  C  CB  . SER   A 1 114 ? -33.159 -27.790 -0.372  1.00 114.89 ? 134 SER   A CB  1 
ATOM   853  O  OG  . SER   A 1 114 ? -32.830 -28.889 -1.203  1.00 132.10 ? 134 SER   A OG  1 
ATOM   854  N  N   . PRO   A 1 115 ? -33.048 -24.952 1.054   1.00 124.61 ? 135 PRO   A N   1 
ATOM   855  C  CA  . PRO   A 1 115 ? -33.713 -23.640 1.119   1.00 132.01 ? 135 PRO   A CA  1 
ATOM   856  C  C   . PRO   A 1 115 ? -32.779 -22.446 0.983   1.00 132.50 ? 135 PRO   A C   1 
ATOM   857  O  O   . PRO   A 1 115 ? -33.213 -21.300 1.143   1.00 136.22 ? 135 PRO   A O   1 
ATOM   858  C  CB  . PRO   A 1 115 ? -34.429 -23.679 2.478   1.00 140.49 ? 135 PRO   A CB  1 
ATOM   859  C  CG  . PRO   A 1 115 ? -34.418 -25.124 2.892   1.00 128.81 ? 135 PRO   A CG  1 
ATOM   860  C  CD  . PRO   A 1 115 ? -33.134 -25.642 2.351   1.00 124.49 ? 135 PRO   A CD  1 
ATOM   861  N  N   . THR   A 1 116 ? -31.500 -22.691 0.695   1.00 141.71 ? 136 THR   A N   1 
ATOM   862  C  CA  . THR   A 1 116 ? -30.557 -21.593 0.520   1.00 136.33 ? 136 THR   A CA  1 
ATOM   863  C  C   . THR   A 1 116 ? -30.728 -20.847 -0.796  1.00 142.83 ? 136 THR   A C   1 
ATOM   864  O  O   . THR   A 1 116 ? -30.476 -19.638 -0.859  1.00 145.94 ? 136 THR   A O   1 
ATOM   865  C  CB  . THR   A 1 116 ? -29.129 -22.129 0.655   1.00 126.40 ? 136 THR   A CB  1 
ATOM   866  O  OG1 . THR   A 1 116 ? -28.950 -22.671 1.970   1.00 140.34 ? 136 THR   A OG1 1 
ATOM   867  C  CG2 . THR   A 1 116 ? -28.103 -21.022 0.443   1.00 127.20 ? 136 THR   A CG2 1 
ATOM   868  N  N   . PHE   A 1 117 ? -31.178 -21.531 -1.842  1.00 133.74 ? 137 PHE   A N   1 
ATOM   869  C  CA  . PHE   A 1 117 ? -31.360 -20.919 -3.150  1.00 133.36 ? 137 PHE   A CA  1 
ATOM   870  C  C   . PHE   A 1 117 ? -32.819 -20.950 -3.593  1.00 132.34 ? 137 PHE   A C   1 
ATOM   871  O  O   . PHE   A 1 117 ? -33.134 -21.259 -4.744  1.00 135.18 ? 137 PHE   A O   1 
ATOM   872  C  CB  . PHE   A 1 117 ? -30.453 -21.573 -4.189  1.00 133.07 ? 137 PHE   A CB  1 
ATOM   873  C  CG  . PHE   A 1 117 ? -29.025 -21.692 -3.746  1.00 132.08 ? 137 PHE   A CG  1 
ATOM   874  C  CD1 . PHE   A 1 117 ? -28.229 -20.564 -3.639  1.00 138.02 ? 137 PHE   A CD1 1 
ATOM   875  C  CD2 . PHE   A 1 117 ? -28.481 -22.924 -3.429  1.00 128.22 ? 137 PHE   A CD2 1 
ATOM   876  C  CE1 . PHE   A 1 117 ? -26.915 -20.661 -3.228  1.00 135.63 ? 137 PHE   A CE1 1 
ATOM   877  C  CE2 . PHE   A 1 117 ? -27.165 -23.029 -3.018  1.00 128.72 ? 137 PHE   A CE2 1 
ATOM   878  C  CZ  . PHE   A 1 117 ? -26.382 -21.895 -2.918  1.00 133.58 ? 137 PHE   A CZ  1 
ATOM   879  N  N   . THR   A 1 118 ? -33.725 -20.605 -2.682  1.00 139.63 ? 138 THR   A N   1 
ATOM   880  C  CA  . THR   A 1 118 ? -35.093 -20.302 -3.072  1.00 142.84 ? 138 THR   A CA  1 
ATOM   881  C  C   . THR   A 1 118 ? -35.140 -18.926 -3.724  1.00 143.26 ? 138 THR   A C   1 
ATOM   882  O  O   . THR   A 1 118 ? -34.341 -18.041 -3.407  1.00 140.08 ? 138 THR   A O   1 
ATOM   883  C  CB  . THR   A 1 118 ? -36.026 -20.323 -1.862  1.00 143.54 ? 138 THR   A CB  1 
ATOM   884  O  OG1 . THR   A 1 118 ? -35.621 -19.311 -0.934  1.00 140.70 ? 138 THR   A OG1 1 
ATOM   885  C  CG2 . THR   A 1 118 ? -35.973 -21.674 -1.170  1.00 136.03 ? 138 THR   A CG2 1 
ATOM   886  N  N   . SER   A 1 119 ? -36.105 -18.744 -4.632  1.00 148.48 ? 139 SER   A N   1 
ATOM   887  C  CA  . SER   A 1 119 ? -36.221 -17.489 -5.372  1.00 148.13 ? 139 SER   A CA  1 
ATOM   888  C  C   . SER   A 1 119 ? -36.243 -16.266 -4.462  1.00 148.49 ? 139 SER   A C   1 
ATOM   889  O  O   . SER   A 1 119 ? -35.872 -15.172 -4.901  1.00 150.70 ? 139 SER   A O   1 
ATOM   890  C  CB  . SER   A 1 119 ? -37.481 -17.508 -6.241  1.00 157.11 ? 139 SER   A CB  1 
ATOM   891  O  OG  . SER   A 1 119 ? -37.259 -18.218 -7.447  1.00 159.72 ? 139 SER   A OG  1 
ATOM   892  N  N   . GLY   A 1 120 ? -36.661 -16.426 -3.208  1.00 150.80 ? 140 GLY   A N   1 
ATOM   893  C  CA  . GLY   A 1 120 ? -36.646 -15.336 -2.254  1.00 146.40 ? 140 GLY   A CA  1 
ATOM   894  C  C   . GLY   A 1 120 ? -35.293 -15.147 -1.600  1.00 140.36 ? 140 GLY   A C   1 
ATOM   895  O  O   . GLY   A 1 120 ? -34.866 -14.012 -1.365  1.00 132.77 ? 140 GLY   A O   1 
ATOM   896  N  N   . LYS   A 1 121 ? -34.608 -16.253 -1.296  1.00 140.62 ? 141 LYS   A N   1 
ATOM   897  C  CA  . LYS   A 1 121 ? -33.268 -16.145 -0.731  1.00 137.46 ? 141 LYS   A CA  1 
ATOM   898  C  C   . LYS   A 1 121 ? -32.306 -15.496 -1.720  1.00 137.58 ? 141 LYS   A C   1 
ATOM   899  O  O   . LYS   A 1 121 ? -31.501 -14.645 -1.328  1.00 141.31 ? 141 LYS   A O   1 
ATOM   900  C  CB  . LYS   A 1 121 ? -32.757 -17.518 -0.289  1.00 135.28 ? 141 LYS   A CB  1 
ATOM   901  C  CG  . LYS   A 1 121 ? -33.471 -18.103 0.930   1.00 132.28 ? 141 LYS   A CG  1 
ATOM   902  C  CD  . LYS   A 1 121 ? -32.994 -17.494 2.241   1.00 137.76 ? 141 LYS   A CD  1 
ATOM   903  C  CE  . LYS   A 1 121 ? -33.841 -17.982 3.411   1.00 137.85 ? 141 LYS   A CE  1 
ATOM   904  N  NZ  . LYS   A 1 121 ? -34.149 -19.438 3.313   1.00 131.98 ? 141 LYS   A NZ  1 
ATOM   905  N  N   . LEU   A 1 122 ? -32.382 -15.869 -3.006  1.00 143.27 ? 142 LEU   A N   1 
ATOM   906  C  CA  . LEU   A 1 122 ? -31.596 -15.175 -4.029  1.00 139.39 ? 142 LEU   A CA  1 
ATOM   907  C  C   . LEU   A 1 122 ? -31.996 -13.711 -4.129  1.00 143.37 ? 142 LEU   A C   1 
ATOM   908  O  O   . LEU   A 1 122 ? -31.140 -12.825 -4.233  1.00 141.52 ? 142 LEU   A O   1 
ATOM   909  C  CB  . LEU   A 1 122 ? -31.751 -15.828 -5.404  1.00 135.71 ? 142 LEU   A CB  1 
ATOM   910  C  CG  . LEU   A 1 122 ? -31.074 -17.132 -5.811  1.00 129.19 ? 142 LEU   A CG  1 
ATOM   911  C  CD1 . LEU   A 1 122 ? -31.805 -18.262 -5.201  1.00 143.83 ? 142 LEU   A CD1 1 
ATOM   912  C  CD2 . LEU   A 1 122 ? -31.051 -17.273 -7.329  1.00 115.73 ? 142 LEU   A CD2 1 
ATOM   913  N  N   . LYS   A 1 123 ? -33.302 -13.442 -4.144  1.00 133.47 ? 143 LYS   A N   1 
ATOM   914  C  CA  . LYS   A 1 123 ? -33.761 -12.063 -4.224  1.00 137.56 ? 143 LYS   A CA  1 
ATOM   915  C  C   . LYS   A 1 123 ? -33.206 -11.228 -3.081  1.00 144.27 ? 143 LYS   A C   1 
ATOM   916  O  O   . LYS   A 1 123 ? -32.930 -10.035 -3.258  1.00 147.78 ? 143 LYS   A O   1 
ATOM   917  C  CB  . LYS   A 1 123 ? -35.286 -12.013 -4.226  1.00 139.05 ? 143 LYS   A CB  1 
ATOM   918  C  CG  . LYS   A 1 123 ? -35.843 -10.645 -4.557  1.00 146.21 ? 143 LYS   A CG  1 
ATOM   919  C  CD  . LYS   A 1 123 ? -37.266 -10.746 -5.062  1.00 139.06 ? 143 LYS   A CD  1 
ATOM   920  C  CE  . LYS   A 1 123 ? -37.888 -9.374  -5.217  1.00 154.04 ? 143 LYS   A CE  1 
ATOM   921  N  NZ  . LYS   A 1 123 ? -38.770 -9.318  -6.415  1.00 156.67 ? 143 LYS   A NZ  1 
ATOM   922  N  N   . GLU   A 1 124 ? -33.023 -11.835 -1.907  1.00 136.29 ? 144 GLU   A N   1 
ATOM   923  C  CA  . GLU   A 1 124 ? -32.373 -11.114 -0.823  1.00 137.66 ? 144 GLU   A CA  1 
ATOM   924  C  C   . GLU   A 1 124 ? -30.929 -10.765 -1.143  1.00 146.76 ? 144 GLU   A C   1 
ATOM   925  O  O   . GLU   A 1 124 ? -30.386 -9.857  -0.515  1.00 141.28 ? 144 GLU   A O   1 
ATOM   926  C  CB  . GLU   A 1 124 ? -32.429 -11.908 0.487   1.00 144.81 ? 144 GLU   A CB  1 
ATOM   927  C  CG  . GLU   A 1 124 ? -33.560 -11.482 1.414   1.00 160.32 ? 144 GLU   A CG  1 
ATOM   928  C  CD  . GLU   A 1 124 ? -33.957 -12.556 2.407   1.00 167.42 ? 144 GLU   A CD  1 
ATOM   929  O  OE1 . GLU   A 1 124 ? -33.283 -12.670 3.453   1.00 172.13 ? 144 GLU   A OE1 1 
ATOM   930  O  OE2 . GLU   A 1 124 ? -34.949 -13.271 2.156   1.00 161.80 ? 144 GLU   A OE2 1 
ATOM   931  N  N   . MET   A 1 125 ? -30.303 -11.435 -2.116  1.00 151.01 ? 145 MET   A N   1 
ATOM   932  C  CA  . MET   A 1 125 ? -28.884 -11.225 -2.388  1.00 151.55 ? 145 MET   A CA  1 
ATOM   933  C  C   . MET   A 1 125 ? -28.624 -10.191 -3.469  1.00 160.02 ? 145 MET   A C   1 
ATOM   934  O  O   . MET   A 1 125 ? -27.485 -9.723  -3.591  1.00 157.47 ? 145 MET   A O   1 
ATOM   935  C  CB  . MET   A 1 125 ? -28.206 -12.531 -2.814  1.00 144.89 ? 145 MET   A CB  1 
ATOM   936  C  CG  . MET   A 1 125 ? -28.943 -13.750 -2.378  1.00 142.88 ? 145 MET   A CG  1 
ATOM   937  S  SD  . MET   A 1 125 ? -28.028 -15.281 -2.366  1.00 140.30 ? 145 MET   A SD  1 
ATOM   938  C  CE  . MET   A 1 125 ? -26.870 -14.861 -1.078  1.00 148.31 ? 145 MET   A CE  1 
ATOM   939  N  N   . VAL   A 1 126 ? -29.635 -9.848  -4.271  1.00 172.63 ? 146 VAL   A N   1 
ATOM   940  C  CA  . VAL   A 1 126 ? -29.457 -8.838  -5.315  1.00 172.81 ? 146 VAL   A CA  1 
ATOM   941  C  C   . VAL   A 1 126 ? -28.966 -7.516  -4.730  1.00 174.77 ? 146 VAL   A C   1 
ATOM   942  O  O   . VAL   A 1 126 ? -28.108 -6.872  -5.349  1.00 175.81 ? 146 VAL   A O   1 
ATOM   943  C  CB  . VAL   A 1 126 ? -30.724 -8.699  -6.150  1.00 170.22 ? 146 VAL   A CB  1 
ATOM   944  C  CG1 . VAL   A 1 126 ? -30.581 -7.585  -7.179  1.00 167.65 ? 146 VAL   A CG1 1 
ATOM   945  C  CG2 . VAL   A 1 126 ? -31.058 -10.018 -6.837  1.00 170.10 ? 146 VAL   A CG2 1 
ATOM   946  N  N   . PRO   A 1 127 ? -29.454 -7.046  -3.573  1.00 176.54 ? 147 PRO   A N   1 
ATOM   947  C  CA  . PRO   A 1 127 ? -28.857 -5.826  -3.002  1.00 180.37 ? 147 PRO   A CA  1 
ATOM   948  C  C   . PRO   A 1 127 ? -27.413 -5.990  -2.544  1.00 179.43 ? 147 PRO   A C   1 
ATOM   949  O  O   . PRO   A 1 127 ? -26.621 -5.057  -2.723  1.00 184.23 ? 147 PRO   A O   1 
ATOM   950  C  CB  . PRO   A 1 127 ? -29.798 -5.494  -1.834  1.00 180.32 ? 147 PRO   A CB  1 
ATOM   951  C  CG  . PRO   A 1 127 ? -31.095 -6.106  -2.215  1.00 178.80 ? 147 PRO   A CG  1 
ATOM   952  C  CD  . PRO   A 1 127 ? -30.724 -7.384  -2.902  1.00 176.17 ? 147 PRO   A CD  1 
ATOM   953  N  N   . ILE   A 1 128 ? -27.037 -7.129  -1.950  1.00 168.82 ? 148 ILE   A N   1 
ATOM   954  C  CA  . ILE   A 1 128 ? -25.665 -7.264  -1.454  1.00 162.80 ? 148 ILE   A CA  1 
ATOM   955  C  C   . ILE   A 1 128 ? -24.684 -7.524  -2.592  1.00 165.92 ? 148 ILE   A C   1 
ATOM   956  O  O   . ILE   A 1 128 ? -23.560 -7.010  -2.575  1.00 164.91 ? 148 ILE   A O   1 
ATOM   957  C  CB  . ILE   A 1 128 ? -25.531 -8.337  -0.349  1.00 164.60 ? 148 ILE   A CB  1 
ATOM   958  C  CG1 . ILE   A 1 128 ? -26.608 -8.223  0.733   1.00 168.25 ? 148 ILE   A CG1 1 
ATOM   959  C  CG2 . ILE   A 1 128 ? -24.152 -8.280  0.291   1.00 169.27 ? 148 ILE   A CG2 1 
ATOM   960  C  CD1 . ILE   A 1 128 ? -27.888 -8.861  0.422   1.00 161.17 ? 148 ILE   A CD1 1 
ATOM   961  N  N   . ILE   A 1 129 ? -25.070 -8.327  -3.587  1.00 165.67 ? 149 ILE   A N   1 
ATOM   962  C  CA  . ILE   A 1 129 ? -24.196 -8.502  -4.745  1.00 165.38 ? 149 ILE   A CA  1 
ATOM   963  C  C   . ILE   A 1 129 ? -23.953 -7.164  -5.430  1.00 170.96 ? 149 ILE   A C   1 
ATOM   964  O  O   . ILE   A 1 129 ? -22.866 -6.916  -5.967  1.00 168.58 ? 149 ILE   A O   1 
ATOM   965  C  CB  . ILE   A 1 129 ? -24.787 -9.535  -5.726  1.00 157.39 ? 149 ILE   A CB  1 
ATOM   966  C  CG1 . ILE   A 1 129 ? -24.831 -10.923 -5.088  1.00 156.19 ? 149 ILE   A CG1 1 
ATOM   967  C  CG2 . ILE   A 1 129 ? -23.971 -9.587  -7.011  1.00 146.28 ? 149 ILE   A CG2 1 
ATOM   968  C  CD1 . ILE   A 1 129 ? -25.213 -12.025 -6.056  1.00 136.16 ? 149 ILE   A CD1 1 
ATOM   969  N  N   . ALA   A 1 130 ? -24.941 -6.266  -5.382  1.00 168.06 ? 150 ALA   A N   1 
ATOM   970  C  CA  . ALA   A 1 130 ? -24.870 -5.006  -6.113  1.00 171.61 ? 150 ALA   A CA  1 
ATOM   971  C  C   . ALA   A 1 130 ? -23.679 -4.143  -5.709  1.00 178.28 ? 150 ALA   A C   1 
ATOM   972  O  O   . ALA   A 1 130 ? -23.361 -3.181  -6.417  1.00 179.00 ? 150 ALA   A O   1 
ATOM   973  C  CB  . ALA   A 1 130 ? -26.167 -4.218  -5.925  1.00 171.36 ? 150 ALA   A CB  1 
ATOM   974  N  N   . GLN   A 1 131 ? -23.009 -4.455  -4.598  1.00 173.94 ? 151 GLN   A N   1 
ATOM   975  C  CA  . GLN   A 1 131 ? -21.833 -3.681  -4.212  1.00 174.03 ? 151 GLN   A CA  1 
ATOM   976  C  C   . GLN   A 1 131 ? -20.626 -4.034  -5.073  1.00 172.76 ? 151 GLN   A C   1 
ATOM   977  O  O   . GLN   A 1 131 ? -20.097 -3.187  -5.800  1.00 176.15 ? 151 GLN   A O   1 
ATOM   978  C  CB  . GLN   A 1 131 ? -21.495 -3.905  -2.736  1.00 175.26 ? 151 GLN   A CB  1 
ATOM   979  C  CG  . GLN   A 1 131 ? -20.140 -3.314  -2.350  1.00 181.91 ? 151 GLN   A CG  1 
ATOM   980  C  CD  . GLN   A 1 131 ? -19.709 -3.679  -0.945  1.00 184.34 ? 151 GLN   A CD  1 
ATOM   981  O  OE1 . GLN   A 1 131 ? -20.539 -3.925  -0.071  1.00 191.58 ? 151 GLN   A OE1 1 
ATOM   982  N  NE2 . GLN   A 1 131 ? -18.399 -3.723  -0.722  1.00 180.64 ? 151 GLN   A NE2 1 
ATOM   983  N  N   . TYR   A 1 132 ? -20.181 -5.292  -5.002  1.00 172.79 ? 152 TYR   A N   1 
ATOM   984  C  CA  . TYR   A 1 132 ? -18.892 -5.672  -5.567  1.00 174.56 ? 152 TYR   A CA  1 
ATOM   985  C  C   . TYR   A 1 132 ? -18.856 -5.559  -7.083  1.00 170.42 ? 152 TYR   A C   1 
ATOM   986  O  O   . TYR   A 1 132 ? -17.764 -5.548  -7.661  1.00 169.74 ? 152 TYR   A O   1 
ATOM   987  C  CB  . TYR   A 1 132 ? -18.533 -7.090  -5.131  1.00 170.13 ? 152 TYR   A CB  1 
ATOM   988  C  CG  . TYR   A 1 132 ? -18.414 -7.216  -3.632  1.00 172.60 ? 152 TYR   A CG  1 
ATOM   989  C  CD1 . TYR   A 1 132 ? -17.221 -6.929  -2.984  1.00 170.80 ? 152 TYR   A CD1 1 
ATOM   990  C  CD2 . TYR   A 1 132 ? -19.500 -7.610  -2.864  1.00 170.16 ? 152 TYR   A CD2 1 
ATOM   991  C  CE1 . TYR   A 1 132 ? -17.111 -7.037  -1.613  1.00 170.05 ? 152 TYR   A CE1 1 
ATOM   992  C  CE2 . TYR   A 1 132 ? -19.401 -7.720  -1.494  1.00 168.30 ? 152 TYR   A CE2 1 
ATOM   993  C  CZ  . TYR   A 1 132 ? -18.206 -7.433  -0.875  1.00 172.58 ? 152 TYR   A CZ  1 
ATOM   994  O  OH  . TYR   A 1 132 ? -18.109 -7.544  0.490   1.00 183.05 ? 152 TYR   A OH  1 
ATOM   995  N  N   . GLY   A 1 133 ? -20.014 -5.480  -7.740  1.00 168.42 ? 153 GLY   A N   1 
ATOM   996  C  CA  . GLY   A 1 133 ? -20.021 -5.110  -9.144  1.00 167.45 ? 153 GLY   A CA  1 
ATOM   997  C  C   . GLY   A 1 133 ? -19.397 -3.746  -9.369  1.00 171.95 ? 153 GLY   A C   1 
ATOM   998  O  O   . GLY   A 1 133 ? -18.642 -3.547  -10.322 1.00 174.38 ? 153 GLY   A O   1 
ATOM   999  N  N   . ASP   A 1 134 ? -19.694 -2.792  -8.482  1.00 167.79 ? 154 ASP   A N   1 
ATOM   1000 C  CA  . ASP   A 1 134 ? -19.034 -1.493  -8.541  1.00 167.65 ? 154 ASP   A CA  1 
ATOM   1001 C  C   . ASP   A 1 134 ? -17.581 -1.589  -8.102  1.00 171.80 ? 154 ASP   A C   1 
ATOM   1002 O  O   . ASP   A 1 134 ? -16.734 -0.838  -8.598  1.00 173.31 ? 154 ASP   A O   1 
ATOM   1003 C  CB  . ASP   A 1 134 ? -19.784 -0.483  -7.678  1.00 169.10 ? 154 ASP   A CB  1 
ATOM   1004 C  CG  . ASP   A 1 134 ? -21.225 -0.325  -8.100  1.00 174.19 ? 154 ASP   A CG  1 
ATOM   1005 O  OD1 . ASP   A 1 134 ? -21.523 -0.563  -9.289  1.00 177.82 ? 154 ASP   A OD1 1 
ATOM   1006 O  OD2 . ASP   A 1 134 ? -22.060 0.032   -7.244  1.00 170.13 ? 154 ASP   A OD2 1 
ATOM   1007 N  N   . VAL   A 1 135 ? -17.275 -2.486  -7.165  1.00 180.12 ? 155 VAL   A N   1 
ATOM   1008 C  CA  . VAL   A 1 135 ? -15.879 -2.821  -6.921  1.00 181.85 ? 155 VAL   A CA  1 
ATOM   1009 C  C   . VAL   A 1 135 ? -15.276 -3.450  -8.169  1.00 184.49 ? 155 VAL   A C   1 
ATOM   1010 O  O   . VAL   A 1 135 ? -14.147 -3.131  -8.559  1.00 185.98 ? 155 VAL   A O   1 
ATOM   1011 C  CB  . VAL   A 1 135 ? -15.756 -3.739  -5.690  1.00 185.80 ? 155 VAL   A CB  1 
ATOM   1012 C  CG1 . VAL   A 1 135 ? -14.351 -4.310  -5.581  1.00 187.19 ? 155 VAL   A CG1 1 
ATOM   1013 C  CG2 . VAL   A 1 135 ? -16.125 -2.975  -4.425  1.00 184.58 ? 155 VAL   A CG2 1 
ATOM   1014 N  N   . LEU   A 1 136 ? -16.038 -4.320  -8.841  1.00 176.78 ? 156 LEU   A N   1 
ATOM   1015 C  CA  . LEU   A 1 136 ? -15.569 -4.913  -10.088 1.00 169.09 ? 156 LEU   A CA  1 
ATOM   1016 C  C   . LEU   A 1 136 ? -15.339 -3.836  -11.145 1.00 167.20 ? 156 LEU   A C   1 
ATOM   1017 O  O   . LEU   A 1 136 ? -14.242 -3.731  -11.705 1.00 170.03 ? 156 LEU   A O   1 
ATOM   1018 C  CB  . LEU   A 1 136 ? -16.580 -5.957  -10.571 1.00 156.08 ? 156 LEU   A CB  1 
ATOM   1019 C  CG  . LEU   A 1 136 ? -16.388 -6.703  -11.894 1.00 151.96 ? 156 LEU   A CG  1 
ATOM   1020 C  CD1 . LEU   A 1 136 ? -15.078 -7.465  -11.891 1.00 143.85 ? 156 LEU   A CD1 1 
ATOM   1021 C  CD2 . LEU   A 1 136 ? -17.551 -7.646  -12.144 1.00 151.12 ? 156 LEU   A CD2 1 
ATOM   1022 N  N   . VAL   A 1 137 ? -16.353 -2.997  -11.396 1.00 169.48 ? 157 VAL   A N   1 
ATOM   1023 C  CA  . VAL   A 1 137 ? -16.258 -1.949  -12.418 1.00 165.77 ? 157 VAL   A CA  1 
ATOM   1024 C  C   . VAL   A 1 137 ? -15.044 -1.061  -12.170 1.00 168.01 ? 157 VAL   A C   1 
ATOM   1025 O  O   . VAL   A 1 137 ? -14.210 -0.854  -13.059 1.00 167.10 ? 157 VAL   A O   1 
ATOM   1026 C  CB  . VAL   A 1 137 ? -17.551 -1.115  -12.464 1.00 158.44 ? 157 VAL   A CB  1 
ATOM   1027 C  CG1 . VAL   A 1 137 ? -17.347 0.133   -13.314 1.00 167.77 ? 157 VAL   A CG1 1 
ATOM   1028 C  CG2 . VAL   A 1 137 ? -18.694 -1.937  -13.027 1.00 160.34 ? 157 VAL   A CG2 1 
ATOM   1029 N  N   . ARG   A 1 138 ? -14.937 -0.517  -10.955 1.00 171.38 ? 158 ARG   A N   1 
ATOM   1030 C  CA  . ARG   A 1 138 ? -13.832 0.384   -10.642 1.00 170.44 ? 158 ARG   A CA  1 
ATOM   1031 C  C   . ARG   A 1 138 ? -12.479 -0.294  -10.821 1.00 176.46 ? 158 ARG   A C   1 
ATOM   1032 O  O   . ARG   A 1 138 ? -11.507 0.363   -11.211 1.00 179.64 ? 158 ARG   A O   1 
ATOM   1033 C  CB  . ARG   A 1 138 ? -13.972 0.916   -9.216  1.00 175.95 ? 158 ARG   A CB  1 
ATOM   1034 C  CG  . ARG   A 1 138 ? -14.873 2.135   -9.089  1.00 168.94 ? 158 ARG   A CG  1 
ATOM   1035 C  CD  . ARG   A 1 138 ? -14.573 2.941   -7.827  1.00 174.91 ? 158 ARG   A CD  1 
ATOM   1036 N  NE  . ARG   A 1 138 ? -13.719 2.229   -6.882  1.00 176.93 ? 158 ARG   A NE  1 
ATOM   1037 C  CZ  . ARG   A 1 138 ? -14.158 1.370   -5.971  1.00 183.84 ? 158 ARG   A CZ  1 
ATOM   1038 N  NH1 . ARG   A 1 138 ? -15.445 1.089   -5.849  1.00 179.84 ? 158 ARG   A NH1 1 
ATOM   1039 N  NH2 . ARG   A 1 138 ? -13.283 0.778   -5.163  1.00 183.17 ? 158 ARG   A NH2 1 
ATOM   1040 N  N   . ASN   A 1 139 ? -12.388 -1.599  -10.543 1.00 180.09 ? 159 ASN   A N   1 
ATOM   1041 C  CA  . ASN   A 1 139 ? -11.133 -2.301  -10.802 1.00 184.63 ? 159 ASN   A CA  1 
ATOM   1042 C  C   . ASN   A 1 139 ? -10.881 -2.457  -12.297 1.00 184.16 ? 159 ASN   A C   1 
ATOM   1043 O  O   . ASN   A 1 139 ? -9.735  -2.351  -12.747 1.00 187.74 ? 159 ASN   A O   1 
ATOM   1044 C  CB  . ASN   A 1 139 ? -11.110 -3.668  -10.112 1.00 184.14 ? 159 ASN   A CB  1 
ATOM   1045 C  CG  . ASN   A 1 139 ? -11.312 -3.575  -8.611  1.00 185.55 ? 159 ASN   A CG  1 
ATOM   1046 O  OD1 . ASN   A 1 139 ? -10.649 -2.795  -7.926  1.00 186.58 ? 159 ASN   A OD1 1 
ATOM   1047 N  ND2 . ASN   A 1 139 ? -12.205 -4.404  -8.087  1.00 187.34 ? 159 ASN   A ND2 1 
ATOM   1048 N  N   . LEU   A 1 140 ? -11.929 -2.712  -13.088 1.00 178.05 ? 160 LEU   A N   1 
ATOM   1049 C  CA  . LEU   A 1 140 ? -11.723 -2.729  -14.533 1.00 173.38 ? 160 LEU   A CA  1 
ATOM   1050 C  C   . LEU   A 1 140 ? -11.529 -1.331  -15.101 1.00 178.87 ? 160 LEU   A C   1 
ATOM   1051 O  O   . LEU   A 1 140 ? -10.933 -1.191  -16.174 1.00 180.47 ? 160 LEU   A O   1 
ATOM   1052 C  CB  . LEU   A 1 140 ? -12.883 -3.400  -15.280 1.00 159.34 ? 160 LEU   A CB  1 
ATOM   1053 C  CG  . LEU   A 1 140 ? -13.301 -4.857  -15.073 1.00 159.09 ? 160 LEU   A CG  1 
ATOM   1054 C  CD1 . LEU   A 1 140 ? -14.687 -4.933  -14.470 1.00 160.24 ? 160 LEU   A CD1 1 
ATOM   1055 C  CD2 . LEU   A 1 140 ? -13.236 -5.628  -16.388 1.00 146.19 ? 160 LEU   A CD2 1 
ATOM   1056 N  N   . ARG   A 1 141 ? -12.023 -0.297  -14.417 1.00 173.64 ? 161 ARG   A N   1 
ATOM   1057 C  CA  . ARG   A 1 141 ? -11.837 1.064   -14.903 1.00 175.09 ? 161 ARG   A CA  1 
ATOM   1058 C  C   . ARG   A 1 141 ? -10.384 1.511   -14.823 1.00 184.51 ? 161 ARG   A C   1 
ATOM   1059 O  O   . ARG   A 1 141 ? -9.980  2.398   -15.582 1.00 199.24 ? 161 ARG   A O   1 
ATOM   1060 C  CB  . ARG   A 1 141 ? -12.721 2.034   -14.116 1.00 171.68 ? 161 ARG   A CB  1 
ATOM   1061 C  CG  . ARG   A 1 141 ? -13.432 3.063   -14.982 1.00 174.51 ? 161 ARG   A CG  1 
ATOM   1062 C  CD  . ARG   A 1 141 ? -14.663 3.619   -14.286 1.00 172.26 ? 161 ARG   A CD  1 
ATOM   1063 N  NE  . ARG   A 1 141 ? -15.703 3.999   -15.234 1.00 178.15 ? 161 ARG   A NE  1 
ATOM   1064 C  CZ  . ARG   A 1 141 ? -16.892 4.475   -14.891 1.00 183.98 ? 161 ARG   A CZ  1 
ATOM   1065 N  NH1 . ARG   A 1 141 ? -17.225 4.653   -13.623 1.00 190.48 ? 161 ARG   A NH1 1 
ATOM   1066 N  NH2 . ARG   A 1 141 ? -17.766 4.784   -15.844 1.00 189.29 ? 161 ARG   A NH2 1 
ATOM   1067 N  N   . ARG   A 1 142 ? -9.592  0.914   -13.930 1.00 183.71 ? 162 ARG   A N   1 
ATOM   1068 C  CA  . ARG   A 1 142 ? -8.201  1.323   -13.774 1.00 189.25 ? 162 ARG   A CA  1 
ATOM   1069 C  C   . ARG   A 1 142 ? -7.305  0.684   -14.829 1.00 197.19 ? 162 ARG   A C   1 
ATOM   1070 O  O   . ARG   A 1 142 ? -6.362  1.321   -15.313 1.00 208.85 ? 162 ARG   A O   1 
ATOM   1071 C  CB  . ARG   A 1 142 ? -7.709  0.971   -12.371 1.00 192.31 ? 162 ARG   A CB  1 
ATOM   1072 C  CG  . ARG   A 1 142 ? -8.350  1.798   -11.269 1.00 186.80 ? 162 ARG   A CG  1 
ATOM   1073 C  CD  . ARG   A 1 142 ? -8.176  1.140   -9.910  1.00 186.98 ? 162 ARG   A CD  1 
ATOM   1074 N  NE  . ARG   A 1 142 ? -8.451  2.065   -8.818  1.00 189.35 ? 162 ARG   A NE  1 
ATOM   1075 C  CZ  . ARG   A 1 142 ? -8.733  1.695   -7.576  1.00 195.91 ? 162 ARG   A CZ  1 
ATOM   1076 N  NH1 . ARG   A 1 142 ? -8.787  0.419   -7.230  1.00 188.71 ? 162 ARG   A NH1 1 
ATOM   1077 N  NH2 . ARG   A 1 142 ? -8.968  2.629   -6.658  1.00 191.18 ? 162 ARG   A NH2 1 
ATOM   1078 N  N   . GLU   A 1 143 ? -7.579  -0.565  -15.194 1.00 207.89 ? 163 GLU   A N   1 
ATOM   1079 C  CA  . GLU   A 1 143 ? -6.789  -1.273  -16.192 1.00 203.18 ? 163 GLU   A CA  1 
ATOM   1080 C  C   . GLU   A 1 143 ? -7.335  -1.097  -17.603 1.00 203.73 ? 163 GLU   A C   1 
ATOM   1081 O  O   . GLU   A 1 143 ? -6.877  -1.788  -18.519 1.00 200.54 ? 163 GLU   A O   1 
ATOM   1082 C  CB  . GLU   A 1 143 ? -6.788  -2.777  -15.892 1.00 204.01 ? 163 GLU   A CB  1 
ATOM   1083 C  CG  . GLU   A 1 143 ? -5.652  -3.246  -14.985 1.00 208.77 ? 163 GLU   A CG  1 
ATOM   1084 C  CD  . GLU   A 1 143 ? -5.790  -2.760  -13.550 1.00 211.30 ? 163 GLU   A CD  1 
ATOM   1085 O  OE1 . GLU   A 1 143 ? -5.626  -1.547  -13.301 1.00 212.54 ? 163 GLU   A OE1 1 
ATOM   1086 O  OE2 . GLU   A 1 143 ? -6.064  -3.599  -12.666 1.00 210.49 ? 163 GLU   A OE2 1 
ATOM   1087 N  N   . ALA   A 1 144 ? -8.299  -0.199  -17.799 1.00 204.57 ? 164 ALA   A N   1 
ATOM   1088 C  CA  . ALA   A 1 144 ? -8.806  0.159   -19.119 1.00 204.99 ? 164 ALA   A CA  1 
ATOM   1089 C  C   . ALA   A 1 144 ? -8.419  1.565   -19.546 1.00 214.60 ? 164 ALA   A C   1 
ATOM   1090 O  O   . ALA   A 1 144 ? -8.139  1.789   -20.726 1.00 210.59 ? 164 ALA   A O   1 
ATOM   1091 C  CB  . ALA   A 1 144 ? -10.331 0.021   -19.159 1.00 195.84 ? 164 ALA   A CB  1 
ATOM   1092 N  N   . GLU   A 1 145 ? -8.460  2.512   -18.601 1.00 233.19 ? 165 GLU   A N   1 
ATOM   1093 C  CA  . GLU   A 1 145 ? -7.951  3.865   -18.932 1.00 240.27 ? 165 GLU   A CA  1 
ATOM   1094 C  C   . GLU   A 1 145 ? -6.557  3.618   -19.497 1.00 240.16 ? 165 GLU   A C   1 
ATOM   1095 O  O   . GLU   A 1 145 ? -6.155  4.339   -20.430 1.00 250.40 ? 165 GLU   A O   1 
ATOM   1096 C  CB  . GLU   A 1 145 ? -7.910  4.750   -17.687 1.00 241.37 ? 165 GLU   A CB  1 
ATOM   1097 C  CG  . GLU   A 1 145 ? -9.284  5.172   -17.202 1.00 248.59 ? 165 GLU   A CG  1 
ATOM   1098 C  CD  . GLU   A 1 145 ? -9.444  5.177   -15.692 1.00 256.95 ? 165 GLU   A CD  1 
ATOM   1099 O  OE1 . GLU   A 1 145 ? -8.439  4.943   -14.992 1.00 261.74 ? 165 GLU   A OE1 1 
ATOM   1100 O  OE2 . GLU   A 1 145 ? -10.576 5.402   -15.219 1.00 261.67 ? 165 GLU   A OE2 1 
ATOM   1101 N  N   . THR   A 1 146 ? -5.862  2.620   -18.946 1.00 218.97 ? 166 THR   A N   1 
ATOM   1102 C  CA  . THR   A 1 146 ? -4.544  2.222   -19.499 1.00 209.70 ? 166 THR   A CA  1 
ATOM   1103 C  C   . THR   A 1 146 ? -4.906  1.144   -20.521 1.00 213.01 ? 166 THR   A C   1 
ATOM   1104 O  O   . THR   A 1 146 ? -5.746  0.286   -20.186 1.00 211.00 ? 166 THR   A O   1 
ATOM   1105 C  CB  . THR   A 1 146 ? -3.582  1.802   -18.382 1.00 200.55 ? 166 THR   A CB  1 
ATOM   1106 O  OG1 . THR   A 1 146 ? -3.671  0.386   -18.218 1.00 199.73 ? 166 THR   A OG1 1 
ATOM   1107 C  CG2 . THR   A 1 146 ? -3.881  2.485   -17.066 1.00 204.91 ? 166 THR   A CG2 1 
ATOM   1108 N  N   . GLY   A 1 147 ? -4.332  1.210   -21.723 1.00 208.69 ? 167 GLY   A N   1 
ATOM   1109 C  CA  . GLY   A 1 147 ? -4.615  0.184   -22.744 1.00 207.35 ? 167 GLY   A CA  1 
ATOM   1110 C  C   . GLY   A 1 147 ? -3.816  -1.064  -22.416 1.00 202.73 ? 167 GLY   A C   1 
ATOM   1111 O  O   . GLY   A 1 147 ? -3.114  -1.560  -23.318 1.00 198.22 ? 167 GLY   A O   1 
ATOM   1112 N  N   . LYS   A 1 148 ? -3.908  -1.557  -21.176 1.00 192.72 ? 168 LYS   A N   1 
ATOM   1113 C  CA  . LYS   A 1 148 ? -3.145  -2.740  -20.818 1.00 185.47 ? 168 LYS   A CA  1 
ATOM   1114 C  C   . LYS   A 1 148 ? -4.082  -3.929  -20.931 1.00 174.90 ? 168 LYS   A C   1 
ATOM   1115 O  O   . LYS   A 1 148 ? -5.130  -3.939  -20.264 1.00 178.94 ? 168 LYS   A O   1 
ATOM   1116 C  CB  . LYS   A 1 148 ? -2.587  -2.637  -19.402 1.00 187.08 ? 168 LYS   A CB  1 
ATOM   1117 C  CG  . LYS   A 1 148 ? -1.725  -3.809  -18.965 1.00 192.65 ? 168 LYS   A CG  1 
ATOM   1118 C  CD  . LYS   A 1 148 ? -1.234  -3.612  -17.539 1.00 198.75 ? 168 LYS   A CD  1 
ATOM   1119 C  CE  . LYS   A 1 148 ? -0.401  -4.790  -17.063 1.00 205.07 ? 168 LYS   A CE  1 
ATOM   1120 N  NZ  . LYS   A 1 148 ? 0.999   -4.715  -17.564 1.00 195.13 ? 168 LYS   A NZ  1 
ATOM   1121 N  N   . PRO   A 1 149 ? -3.775  -4.919  -21.769 1.00 168.92 ? 169 PRO   A N   1 
ATOM   1122 C  CA  . PRO   A 1 149 ? -4.619  -6.117  -21.850 1.00 171.36 ? 169 PRO   A CA  1 
ATOM   1123 C  C   . PRO   A 1 149 ? -4.862  -6.726  -20.475 1.00 165.20 ? 169 PRO   A C   1 
ATOM   1124 O  O   . PRO   A 1 149 ? -3.979  -6.742  -19.615 1.00 170.07 ? 169 PRO   A O   1 
ATOM   1125 C  CB  . PRO   A 1 149 ? -3.808  -7.057  -22.746 1.00 166.55 ? 169 PRO   A CB  1 
ATOM   1126 C  CG  . PRO   A 1 149 ? -2.965  -6.155  -23.580 1.00 168.80 ? 169 PRO   A CG  1 
ATOM   1127 C  CD  . PRO   A 1 149 ? -2.768  -4.864  -22.842 1.00 172.68 ? 169 PRO   A CD  1 
ATOM   1128 N  N   . VAL   A 1 150 ? -6.075  -7.233  -20.275 1.00 158.06 ? 170 VAL   A N   1 
ATOM   1129 C  CA  . VAL   A 1 150 ? -6.554  -7.660  -18.965 1.00 163.23 ? 170 VAL   A CA  1 
ATOM   1130 C  C   . VAL   A 1 150 ? -6.642  -9.178  -18.923 1.00 151.55 ? 170 VAL   A C   1 
ATOM   1131 O  O   . VAL   A 1 150 ? -7.054  -9.813  -19.900 1.00 145.74 ? 170 VAL   A O   1 
ATOM   1132 C  CB  . VAL   A 1 150 ? -7.922  -7.024  -18.647 1.00 155.82 ? 170 VAL   A CB  1 
ATOM   1133 C  CG1 . VAL   A 1 150 ? -8.410  -7.448  -17.271 1.00 137.81 ? 170 VAL   A CG1 1 
ATOM   1134 C  CG2 . VAL   A 1 150 ? -7.829  -5.511  -18.736 1.00 157.47 ? 170 VAL   A CG2 1 
ATOM   1135 N  N   . THR   A 1 151 ? -6.252  -9.757  -17.789 1.00 160.61 ? 171 THR   A N   1 
ATOM   1136 C  CA  . THR   A 1 151 ? -6.519  -11.161 -17.494 1.00 158.12 ? 171 THR   A CA  1 
ATOM   1137 C  C   . THR   A 1 151 ? -7.890  -11.238 -16.827 1.00 154.60 ? 171 THR   A C   1 
ATOM   1138 O  O   . THR   A 1 151 ? -8.055  -10.797 -15.686 1.00 154.05 ? 171 THR   A O   1 
ATOM   1139 C  CB  . THR   A 1 151 ? -5.431  -11.745 -16.595 1.00 163.12 ? 171 THR   A CB  1 
ATOM   1140 O  OG1 . THR   A 1 151 ? -5.426  -11.055 -15.339 1.00 173.20 ? 171 THR   A OG1 1 
ATOM   1141 C  CG2 . THR   A 1 151 ? -4.063  -11.590 -17.240 1.00 165.48 ? 171 THR   A CG2 1 
ATOM   1142 N  N   . LEU   A 1 152 ? -8.876  -11.798 -17.533 1.00 146.28 ? 172 LEU   A N   1 
ATOM   1143 C  CA  . LEU   A 1 152 ? -10.262 -11.664 -17.089 1.00 136.03 ? 172 LEU   A CA  1 
ATOM   1144 C  C   . LEU   A 1 152 ? -10.592 -12.599 -15.928 1.00 141.17 ? 172 LEU   A C   1 
ATOM   1145 O  O   . LEU   A 1 152 ? -11.355 -12.219 -15.032 1.00 136.72 ? 172 LEU   A O   1 
ATOM   1146 C  CB  . LEU   A 1 152 ? -11.228 -11.894 -18.258 1.00 132.56 ? 172 LEU   A CB  1 
ATOM   1147 C  CG  . LEU   A 1 152 ? -11.255 -10.924 -19.453 1.00 131.44 ? 172 LEU   A CG  1 
ATOM   1148 C  CD1 . LEU   A 1 152 ? -11.608 -9.494  -19.023 1.00 133.23 ? 172 LEU   A CD1 1 
ATOM   1149 C  CD2 . LEU   A 1 152 ? -9.976  -10.955 -20.283 1.00 140.20 ? 172 LEU   A CD2 1 
ATOM   1150 N  N   . LYS   A 1 153 ? -10.042 -13.820 -15.922 1.00 128.82 ? 173 LYS   A N   1 
ATOM   1151 C  CA  . LYS   A 1 153 ? -10.284 -14.734 -14.804 1.00 134.87 ? 173 LYS   A CA  1 
ATOM   1152 C  C   . LYS   A 1 153 ? -9.869  -14.130 -13.473 1.00 133.87 ? 173 LYS   A C   1 
ATOM   1153 O  O   . LYS   A 1 153 ? -10.486 -14.418 -12.441 1.00 136.64 ? 173 LYS   A O   1 
ATOM   1154 C  CB  . LYS   A 1 153 ? -9.547  -16.063 -15.004 1.00 140.54 ? 173 LYS   A CB  1 
ATOM   1155 C  CG  . LYS   A 1 153 ? -10.461 -17.184 -15.485 1.00 130.85 ? 173 LYS   A CG  1 
ATOM   1156 C  CD  . LYS   A 1 153 ? -9.881  -18.585 -15.355 1.00 134.59 ? 173 LYS   A CD  1 
ATOM   1157 C  CE  . LYS   A 1 153 ? -10.854 -19.495 -14.609 1.00 122.89 ? 173 LYS   A CE  1 
ATOM   1158 N  NZ  . LYS   A 1 153 ? -10.455 -20.938 -14.643 1.00 136.93 ? 173 LYS   A NZ  1 
ATOM   1159 N  N   . ASP   A 1 154 ? -8.823  -13.307 -13.472 1.00 145.60 ? 174 ASP   A N   1 
ATOM   1160 C  CA  . ASP   A 1 154 ? -8.314  -12.767 -12.219 1.00 146.48 ? 174 ASP   A CA  1 
ATOM   1161 C  C   . ASP   A 1 154 ? -9.234  -11.684 -11.673 1.00 143.73 ? 174 ASP   A C   1 
ATOM   1162 O  O   . ASP   A 1 154 ? -9.505  -11.642 -10.467 1.00 144.06 ? 174 ASP   A O   1 
ATOM   1163 C  CB  . ASP   A 1 154 ? -6.901  -12.230 -12.429 1.00 148.46 ? 174 ASP   A CB  1 
ATOM   1164 C  CG  . ASP   A 1 154 ? -5.842  -13.292 -12.218 1.00 158.67 ? 174 ASP   A CG  1 
ATOM   1165 O  OD1 . ASP   A 1 154 ? -6.178  -14.371 -11.686 1.00 156.26 ? 174 ASP   A OD1 1 
ATOM   1166 O  OD2 . ASP   A 1 154 ? -4.674  -13.048 -12.585 1.00 168.30 ? 174 ASP   A OD2 1 
ATOM   1167 N  N   . VAL   A 1 155 ? -9.730  -10.803 -12.542 1.00 146.26 ? 175 VAL   A N   1 
ATOM   1168 C  CA  . VAL   A 1 155 ? -10.638 -9.763  -12.081 1.00 141.17 ? 175 VAL   A CA  1 
ATOM   1169 C  C   . VAL   A 1 155 ? -12.028 -10.346 -11.827 1.00 135.44 ? 175 VAL   A C   1 
ATOM   1170 O  O   . VAL   A 1 155 ? -12.747 -9.882  -10.934 1.00 137.20 ? 175 VAL   A O   1 
ATOM   1171 C  CB  . VAL   A 1 155 ? -10.669 -8.599  -13.090 1.00 128.77 ? 175 VAL   A CB  1 
ATOM   1172 C  CG1 . VAL   A 1 155 ? -10.894 -9.110  -14.508 1.00 139.84 ? 175 VAL   A CG1 1 
ATOM   1173 C  CG2 . VAL   A 1 155 ? -11.696 -7.552  -12.698 1.00 139.27 ? 175 VAL   A CG2 1 
ATOM   1174 N  N   . PHE   A 1 156 ? -12.420 -11.377 -12.582 1.00 132.17 ? 176 PHE   A N   1 
ATOM   1175 C  CA  . PHE   A 1 156 ? -13.669 -12.076 -12.293 1.00 135.50 ? 176 PHE   A CA  1 
ATOM   1176 C  C   . PHE   A 1 156 ? -13.553 -12.896 -11.016 1.00 130.20 ? 176 PHE   A C   1 
ATOM   1177 O  O   . PHE   A 1 156 ? -14.448 -12.866 -10.163 1.00 119.38 ? 176 PHE   A O   1 
ATOM   1178 C  CB  . PHE   A 1 156 ? -14.059 -12.979 -13.464 1.00 122.71 ? 176 PHE   A CB  1 
ATOM   1179 C  CG  . PHE   A 1 156 ? -14.431 -12.237 -14.711 1.00 121.91 ? 176 PHE   A CG  1 
ATOM   1180 C  CD1 . PHE   A 1 156 ? -14.999 -10.976 -14.643 1.00 128.49 ? 176 PHE   A CD1 1 
ATOM   1181 C  CD2 . PHE   A 1 156 ? -14.214 -12.803 -15.956 1.00 115.21 ? 176 PHE   A CD2 1 
ATOM   1182 C  CE1 . PHE   A 1 156 ? -15.342 -10.295 -15.794 1.00 130.27 ? 176 PHE   A CE1 1 
ATOM   1183 C  CE2 . PHE   A 1 156 ? -14.555 -12.128 -17.108 1.00 106.40 ? 176 PHE   A CE2 1 
ATOM   1184 C  CZ  . PHE   A 1 156 ? -15.118 -10.872 -17.027 1.00 112.71 ? 176 PHE   A CZ  1 
ATOM   1185 N  N   . GLY   A 1 157 ? -12.460 -13.651 -10.875 1.00 133.53 ? 177 GLY   A N   1 
ATOM   1186 C  CA  . GLY   A 1 157 ? -12.282 -14.464 -9.683  1.00 135.18 ? 177 GLY   A CA  1 
ATOM   1187 C  C   . GLY   A 1 157 ? -12.212 -13.632 -8.418  1.00 137.41 ? 177 GLY   A C   1 
ATOM   1188 O  O   . GLY   A 1 157 ? -12.767 -14.010 -7.383  1.00 133.96 ? 177 GLY   A O   1 
ATOM   1189 N  N   . ALA   A 1 158 ? -11.525 -12.489 -8.484  1.00 141.17 ? 178 ALA   A N   1 
ATOM   1190 C  CA  . ALA   A 1 158 ? -11.552 -11.546 -7.372  1.00 134.13 ? 178 ALA   A CA  1 
ATOM   1191 C  C   . ALA   A 1 158 ? -12.979 -11.117 -7.061  1.00 134.00 ? 178 ALA   A C   1 
ATOM   1192 O  O   . ALA   A 1 158 ? -13.376 -11.045 -5.892  1.00 140.28 ? 178 ALA   A O   1 
ATOM   1193 C  CB  . ALA   A 1 158 ? -10.683 -10.333 -7.696  1.00 140.90 ? 178 ALA   A CB  1 
ATOM   1194 N  N   . TYR   A 1 159 ? -13.767 -10.834 -8.099  1.00 130.54 ? 179 TYR   A N   1 
ATOM   1195 C  CA  . TYR   A 1 159 ? -15.187 -10.570 -7.898  1.00 136.53 ? 179 TYR   A CA  1 
ATOM   1196 C  C   . TYR   A 1 159 ? -15.892 -11.818 -7.372  1.00 128.19 ? 179 TYR   A C   1 
ATOM   1197 O  O   . TYR   A 1 159 ? -16.610 -11.762 -6.367  1.00 127.36 ? 179 TYR   A O   1 
ATOM   1198 C  CB  . TYR   A 1 159 ? -15.817 -10.110 -9.214  1.00 136.08 ? 179 TYR   A CB  1 
ATOM   1199 C  CG  . TYR   A 1 159 ? -17.327 -10.199 -9.262  1.00 142.74 ? 179 TYR   A CG  1 
ATOM   1200 C  CD1 . TYR   A 1 159 ? -18.112 -9.827  -8.174  1.00 145.59 ? 179 TYR   A CD1 1 
ATOM   1201 C  CD2 . TYR   A 1 159 ? -17.962 -10.737 -10.366 1.00 148.89 ? 179 TYR   A CD2 1 
ATOM   1202 C  CE1 . TYR   A 1 159 ? -19.490 -9.938  -8.215  1.00 152.68 ? 179 TYR   A CE1 1 
ATOM   1203 C  CE2 . TYR   A 1 159 ? -19.329 -10.858 -10.409 1.00 148.74 ? 179 TYR   A CE2 1 
ATOM   1204 C  CZ  . TYR   A 1 159 ? -20.091 -10.455 -9.338  1.00 145.56 ? 179 TYR   A CZ  1 
ATOM   1205 O  OH  . TYR   A 1 159 ? -21.461 -10.579 -9.396  1.00 129.43 ? 179 TYR   A OH  1 
ATOM   1206 N  N   . SER   A 1 160 ? -15.698 -12.956 -8.049  1.00 143.37 ? 180 SER   A N   1 
ATOM   1207 C  CA  . SER   A 1 160 ? -16.394 -14.186 -7.676  1.00 139.45 ? 180 SER   A CA  1 
ATOM   1208 C  C   . SER   A 1 160 ? -16.148 -14.547 -6.218  1.00 136.12 ? 180 SER   A C   1 
ATOM   1209 O  O   . SER   A 1 160 ? -17.065 -14.973 -5.508  1.00 127.02 ? 180 SER   A O   1 
ATOM   1210 C  CB  . SER   A 1 160 ? -15.960 -15.334 -8.589  1.00 127.35 ? 180 SER   A CB  1 
ATOM   1211 O  OG  . SER   A 1 160 ? -15.714 -14.882 -9.907  1.00 136.93 ? 180 SER   A OG  1 
ATOM   1212 N  N   . MET   A 1 161 ? -14.907 -14.387 -5.753  1.00 133.64 ? 181 MET   A N   1 
ATOM   1213 C  CA  . MET   A 1 161 ? -14.621 -14.658 -4.349  1.00 132.63 ? 181 MET   A CA  1 
ATOM   1214 C  C   . MET   A 1 161 ? -15.329 -13.656 -3.450  1.00 138.22 ? 181 MET   A C   1 
ATOM   1215 O  O   . MET   A 1 161 ? -15.883 -14.025 -2.407  1.00 132.21 ? 181 MET   A O   1 
ATOM   1216 C  CB  . MET   A 1 161 ? -13.116 -14.632 -4.099  1.00 133.55 ? 181 MET   A CB  1 
ATOM   1217 C  CG  . MET   A 1 161 ? -12.726 -15.103 -2.710  1.00 134.71 ? 181 MET   A CG  1 
ATOM   1218 S  SD  . MET   A 1 161 ? -13.324 -16.768 -2.368  1.00 138.49 ? 181 MET   A SD  1 
ATOM   1219 C  CE  . MET   A 1 161 ? -12.006 -17.377 -1.323  1.00 139.99 ? 181 MET   A CE  1 
ATOM   1220 N  N   . ASP   A 1 162 ? -15.334 -12.382 -3.850  1.00 143.62 ? 182 ASP   A N   1 
ATOM   1221 C  CA  . ASP   A 1 162 ? -16.007 -11.356 -3.064  1.00 144.42 ? 182 ASP   A CA  1 
ATOM   1222 C  C   . ASP   A 1 162 ? -17.483 -11.665 -2.876  1.00 143.25 ? 182 ASP   A C   1 
ATOM   1223 O  O   . ASP   A 1 162 ? -18.059 -11.322 -1.839  1.00 142.96 ? 182 ASP   A O   1 
ATOM   1224 C  CB  . ASP   A 1 162 ? -15.833 -9.993  -3.728  1.00 145.96 ? 182 ASP   A CB  1 
ATOM   1225 C  CG  . ASP   A 1 162 ? -14.484 -9.381  -3.441  1.00 151.25 ? 182 ASP   A CG  1 
ATOM   1226 O  OD1 . ASP   A 1 162 ? -13.757 -9.938  -2.594  1.00 155.25 ? 182 ASP   A OD1 1 
ATOM   1227 O  OD2 . ASP   A 1 162 ? -14.149 -8.352  -4.063  1.00 159.39 ? 182 ASP   A OD2 1 
ATOM   1228 N  N   . VAL   A 1 163 ? -18.117 -12.314 -3.850  1.00 142.01 ? 183 VAL   A N   1 
ATOM   1229 C  CA  . VAL   A 1 163 ? -19.531 -12.621 -3.686  1.00 144.39 ? 183 VAL   A CA  1 
ATOM   1230 C  C   . VAL   A 1 163 ? -19.708 -13.833 -2.775  1.00 148.95 ? 183 VAL   A C   1 
ATOM   1231 O  O   . VAL   A 1 163 ? -20.522 -13.805 -1.847  1.00 158.11 ? 183 VAL   A O   1 
ATOM   1232 C  CB  . VAL   A 1 163 ? -20.219 -12.790 -5.056  1.00 137.81 ? 183 VAL   A CB  1 
ATOM   1233 C  CG1 . VAL   A 1 163 ? -20.065 -14.195 -5.619  1.00 144.73 ? 183 VAL   A CG1 1 
ATOM   1234 C  CG2 . VAL   A 1 163 ? -21.677 -12.381 -4.958  1.00 133.12 ? 183 VAL   A CG2 1 
ATOM   1235 N  N   . ILE   A 1 164 ? -18.890 -14.875 -2.959  1.00 144.84 ? 184 ILE   A N   1 
ATOM   1236 C  CA  . ILE   A 1 164 ? -19.132 -16.125 -2.243  1.00 139.25 ? 184 ILE   A CA  1 
ATOM   1237 C  C   . ILE   A 1 164 ? -18.827 -15.972 -0.754  1.00 146.05 ? 184 ILE   A C   1 
ATOM   1238 O  O   . ILE   A 1 164 ? -19.482 -16.593 0.092   1.00 152.98 ? 184 ILE   A O   1 
ATOM   1239 C  CB  . ILE   A 1 164 ? -18.336 -17.277 -2.889  1.00 128.63 ? 184 ILE   A CB  1 
ATOM   1240 C  CG1 . ILE   A 1 164 ? -19.075 -18.605 -2.698  1.00 126.60 ? 184 ILE   A CG1 1 
ATOM   1241 C  CG2 . ILE   A 1 164 ? -16.915 -17.348 -2.348  1.00 128.72 ? 184 ILE   A CG2 1 
ATOM   1242 C  CD1 . ILE   A 1 164 ? -20.535 -18.558 -3.113  1.00 136.11 ? 184 ILE   A CD1 1 
ATOM   1243 N  N   . THR   A 1 165 ? -17.857 -15.123 -0.404  1.00 151.03 ? 185 THR   A N   1 
ATOM   1244 C  CA  . THR   A 1 165 ? -17.504 -14.945 1.001   1.00 150.34 ? 185 THR   A CA  1 
ATOM   1245 C  C   . THR   A 1 165 ? -18.562 -14.147 1.751   1.00 154.80 ? 185 THR   A C   1 
ATOM   1246 O  O   . THR   A 1 165 ? -18.703 -14.298 2.970   1.00 157.28 ? 185 THR   A O   1 
ATOM   1247 C  CB  . THR   A 1 165 ? -16.142 -14.260 1.108   1.00 149.63 ? 185 THR   A CB  1 
ATOM   1248 O  OG1 . THR   A 1 165 ? -15.304 -14.712 0.037   1.00 148.94 ? 185 THR   A OG1 1 
ATOM   1249 C  CG2 . THR   A 1 165 ? -15.471 -14.594 2.429   1.00 151.90 ? 185 THR   A CG2 1 
ATOM   1250 N  N   . SER   A 1 166 ? -19.311 -13.302 1.046   1.00 169.66 ? 186 SER   A N   1 
ATOM   1251 C  CA  . SER   A 1 166 ? -20.363 -12.499 1.651   1.00 177.57 ? 186 SER   A CA  1 
ATOM   1252 C  C   . SER   A 1 166 ? -21.752 -13.077 1.436   1.00 174.40 ? 186 SER   A C   1 
ATOM   1253 O  O   . SER   A 1 166 ? -22.609 -12.946 2.317   1.00 174.91 ? 186 SER   A O   1 
ATOM   1254 C  CB  . SER   A 1 166 ? -20.331 -11.073 1.091   1.00 190.24 ? 186 SER   A CB  1 
ATOM   1255 O  OG  . SER   A 1 166 ? -20.207 -11.090 -0.322  1.00 195.28 ? 186 SER   A OG  1 
ATOM   1256 N  N   . THR   A 1 167 ? -21.993 -13.707 0.284   1.00 169.42 ? 187 THR   A N   1 
ATOM   1257 C  CA  . THR   A 1 167 ? -23.295 -14.306 0.018   1.00 169.79 ? 187 THR   A CA  1 
ATOM   1258 C  C   . THR   A 1 167 ? -23.608 -15.448 0.970   1.00 174.62 ? 187 THR   A C   1 
ATOM   1259 O  O   . THR   A 1 167 ? -24.773 -15.842 1.092   1.00 177.53 ? 187 THR   A O   1 
ATOM   1260 C  CB  . THR   A 1 167 ? -23.350 -14.824 -1.416  1.00 165.44 ? 187 THR   A CB  1 
ATOM   1261 O  OG1 . THR   A 1 167 ? -22.107 -15.466 -1.736  1.00 164.82 ? 187 THR   A OG1 1 
ATOM   1262 C  CG2 . THR   A 1 167 ? -23.572 -13.674 -2.363  1.00 164.90 ? 187 THR   A CG2 1 
ATOM   1263 N  N   . SER   A 1 168 ? -22.596 -15.983 1.644   1.00 165.02 ? 188 SER   A N   1 
ATOM   1264 C  CA  . SER   A 1 168 ? -22.750 -17.159 2.479   1.00 162.92 ? 188 SER   A CA  1 
ATOM   1265 C  C   . SER   A 1 168 ? -22.315 -16.958 3.921   1.00 158.99 ? 188 SER   A C   1 
ATOM   1266 O  O   . SER   A 1 168 ? -22.804 -17.679 4.796   1.00 158.37 ? 188 SER   A O   1 
ATOM   1267 C  CB  . SER   A 1 168 ? -21.958 -18.331 1.879   1.00 156.08 ? 188 SER   A CB  1 
ATOM   1268 O  OG  . SER   A 1 168 ? -22.368 -18.592 0.549   1.00 150.21 ? 188 SER   A OG  1 
ATOM   1269 N  N   . PHE   A 1 169 ? -21.417 -16.012 4.192   1.00 162.38 ? 189 PHE   A N   1 
ATOM   1270 C  CA  . PHE   A 1 169 ? -20.908 -15.789 5.539   1.00 152.52 ? 189 PHE   A CA  1 
ATOM   1271 C  C   . PHE   A 1 169 ? -21.071 -14.321 5.919   1.00 157.33 ? 189 PHE   A C   1 
ATOM   1272 O  O   . PHE   A 1 169 ? -21.707 -14.003 6.928   1.00 163.20 ? 189 PHE   A O   1 
ATOM   1273 C  CB  . PHE   A 1 169 ? -19.436 -16.226 5.655   1.00 147.77 ? 189 PHE   A CB  1 
ATOM   1274 C  CG  . PHE   A 1 169 ? -19.146 -17.607 5.096   1.00 140.87 ? 189 PHE   A CG  1 
ATOM   1275 C  CD1 . PHE   A 1 169 ? -19.171 -17.857 3.731   1.00 138.73 ? 189 PHE   A CD1 1 
ATOM   1276 C  CD2 . PHE   A 1 169 ? -18.847 -18.656 5.950   1.00 141.79 ? 189 PHE   A CD2 1 
ATOM   1277 C  CE1 . PHE   A 1 169 ? -18.910 -19.126 3.234   1.00 138.07 ? 189 PHE   A CE1 1 
ATOM   1278 C  CE2 . PHE   A 1 169 ? -18.588 -19.926 5.456   1.00 140.94 ? 189 PHE   A CE2 1 
ATOM   1279 C  CZ  . PHE   A 1 169 ? -18.619 -20.158 4.099   1.00 134.11 ? 189 PHE   A CZ  1 
ATOM   1280 N  N   . GLY   A 1 170 ? -20.503 -13.420 5.118   1.00 158.30 ? 190 GLY   A N   1 
ATOM   1281 C  CA  . GLY   A 1 170 ? -20.730 -12.000 5.303   1.00 157.95 ? 190 GLY   A CA  1 
ATOM   1282 C  C   . GLY   A 1 170 ? -19.490 -11.170 5.568   1.00 165.44 ? 190 GLY   A C   1 
ATOM   1283 O  O   . GLY   A 1 170 ? -19.570 -10.125 6.221   1.00 177.58 ? 190 GLY   A O   1 
ATOM   1284 N  N   . VAL   A 1 171 ? -18.341 -11.610 5.063   1.00 163.83 ? 191 VAL   A N   1 
ATOM   1285 C  CA  . VAL   A 1 171 ? -17.073 -10.917 5.269   1.00 178.67 ? 191 VAL   A CA  1 
ATOM   1286 C  C   . VAL   A 1 171 ? -16.774 -10.081 4.032   1.00 183.29 ? 191 VAL   A C   1 
ATOM   1287 O  O   . VAL   A 1 171 ? -16.660 -10.616 2.922   1.00 175.74 ? 191 VAL   A O   1 
ATOM   1288 C  CB  . VAL   A 1 171 ? -15.934 -11.905 5.561   1.00 167.86 ? 191 VAL   A CB  1 
ATOM   1289 C  CG1 . VAL   A 1 171 ? -14.605 -11.171 5.645   1.00 171.50 ? 191 VAL   A CG1 1 
ATOM   1290 C  CG2 . VAL   A 1 171 ? -16.211 -12.665 6.850   1.00 165.02 ? 191 VAL   A CG2 1 
ATOM   1291 N  N   . ASN   A 1 172 ? -16.639 -8.770  4.222   1.00 204.99 ? 192 ASN   A N   1 
ATOM   1292 C  CA  . ASN   A 1 172 ? -16.410 -7.841  3.122   1.00 210.29 ? 192 ASN   A CA  1 
ATOM   1293 C  C   . ASN   A 1 172 ? -14.918 -7.589  2.944   1.00 209.66 ? 192 ASN   A C   1 
ATOM   1294 O  O   . ASN   A 1 172 ? -14.228 -7.207  3.895   1.00 211.52 ? 192 ASN   A O   1 
ATOM   1295 C  CB  . ASN   A 1 172 ? -17.143 -6.521  3.371   1.00 218.50 ? 192 ASN   A CB  1 
ATOM   1296 C  CG  . ASN   A 1 172 ? -16.845 -5.936  4.737   1.00 225.06 ? 192 ASN   A CG  1 
ATOM   1297 O  OD1 . ASN   A 1 172 ? -17.459 -6.314  5.735   1.00 228.44 ? 192 ASN   A OD1 1 
ATOM   1298 N  ND2 . ASN   A 1 172 ? -15.898 -5.007  4.789   1.00 227.15 ? 192 ASN   A ND2 1 
ATOM   1299 N  N   . ILE   A 1 173 ? -14.429 -7.795  1.723   1.00 193.40 ? 193 ILE   A N   1 
ATOM   1300 C  CA  . ILE   A 1 173 ? -13.009 -7.657  1.408   1.00 185.86 ? 193 ILE   A CA  1 
ATOM   1301 C  C   . ILE   A 1 173 ? -12.875 -7.206  -0.040  1.00 183.78 ? 193 ILE   A C   1 
ATOM   1302 O  O   . ILE   A 1 173 ? -13.505 -7.775  -0.936  1.00 173.64 ? 193 ILE   A O   1 
ATOM   1303 C  CB  . ILE   A 1 173 ? -12.241 -8.977  1.638   1.00 179.05 ? 193 ILE   A CB  1 
ATOM   1304 C  CG1 . ILE   A 1 173 ? -11.922 -9.173  3.121   1.00 174.88 ? 193 ILE   A CG1 1 
ATOM   1305 C  CG2 . ILE   A 1 173 ? -10.961 -9.014  0.812   1.00 179.08 ? 193 ILE   A CG2 1 
ATOM   1306 C  CD1 . ILE   A 1 173 ? -11.394 -10.551 3.453   1.00 171.57 ? 193 ILE   A CD1 1 
ATOM   1307 N  N   . ASP   A 1 174 ? -12.061 -6.177  -0.270  1.00 187.44 ? 194 ASP   A N   1 
ATOM   1308 C  CA  . ASP   A 1 174 ? -11.679 -5.784  -1.626  1.00 189.68 ? 194 ASP   A CA  1 
ATOM   1309 C  C   . ASP   A 1 174 ? -10.676 -6.843  -2.065  1.00 186.14 ? 194 ASP   A C   1 
ATOM   1310 O  O   . ASP   A 1 174 ? -9.555  -6.902  -1.557  1.00 190.52 ? 194 ASP   A O   1 
ATOM   1311 C  CB  . ASP   A 1 174 ? -11.121 -4.365  -1.635  1.00 188.86 ? 194 ASP   A CB  1 
ATOM   1312 C  CG  . ASP   A 1 174 ? -10.641 -3.927  -3.013  1.00 185.72 ? 194 ASP   A CG  1 
ATOM   1313 O  OD1 . ASP   A 1 174 ? -10.979 -4.592  -4.015  1.00 185.06 ? 194 ASP   A OD1 1 
ATOM   1314 O  OD2 . ASP   A 1 174 ? -9.914  -2.914  -3.092  1.00 187.80 ? 194 ASP   A OD2 1 
ATOM   1315 N  N   . SER   A 1 175 ? -11.068 -7.684  -3.021  1.00 180.73 ? 195 SER   A N   1 
ATOM   1316 C  CA  . SER   A 1 175 ? -10.185 -8.755  -3.472  1.00 173.87 ? 195 SER   A CA  1 
ATOM   1317 C  C   . SER   A 1 175 ? -9.131  -8.265  -4.458  1.00 182.83 ? 195 SER   A C   1 
ATOM   1318 O  O   . SER   A 1 175 ? -8.935  -8.864  -5.519  1.00 175.15 ? 195 SER   A O   1 
ATOM   1319 C  CB  . SER   A 1 175 ? -10.994 -9.894  -4.092  1.00 166.53 ? 195 SER   A CB  1 
ATOM   1320 O  OG  . SER   A 1 175 ? -11.663 -10.640 -3.090  1.00 162.42 ? 195 SER   A OG  1 
ATOM   1321 N  N   . LEU   A 1 176 ? -8.457  -7.168  -4.120  1.00 188.96 ? 196 LEU   A N   1 
ATOM   1322 C  CA  . LEU   A 1 176 ? -7.180  -6.832  -4.723  1.00 190.14 ? 196 LEU   A CA  1 
ATOM   1323 C  C   . LEU   A 1 176 ? -6.062  -6.774  -3.695  1.00 199.57 ? 196 LEU   A C   1 
ATOM   1324 O  O   . LEU   A 1 176 ? -4.891  -6.676  -4.080  1.00 197.42 ? 196 LEU   A O   1 
ATOM   1325 C  CB  . LEU   A 1 176 ? -7.259  -5.499  -5.483  1.00 189.83 ? 196 LEU   A CB  1 
ATOM   1326 C  CG  . LEU   A 1 176 ? -6.262  -5.377  -6.641  1.00 183.13 ? 196 LEU   A CG  1 
ATOM   1327 C  CD1 . LEU   A 1 176 ? -6.681  -6.256  -7.812  1.00 172.65 ? 196 LEU   A CD1 1 
ATOM   1328 C  CD2 . LEU   A 1 176 ? -6.109  -3.930  -7.083  1.00 168.95 ? 196 LEU   A CD2 1 
ATOM   1329 N  N   . ASP   A 1 197 ? -2.832  -33.361 -13.878 1.00 185.89 ? 217 ASP   A N   1 
ATOM   1330 C  CA  . ASP   A 1 197 ? -2.981  -34.821 -13.643 1.00 191.20 ? 217 ASP   A CA  1 
ATOM   1331 C  C   . ASP   A 1 197 ? -1.708  -35.363 -12.989 1.00 201.25 ? 217 ASP   A C   1 
ATOM   1332 O  O   . ASP   A 1 197 ? -1.083  -36.265 -13.574 1.00 206.12 ? 217 ASP   A O   1 
ATOM   1333 C  CB  . ASP   A 1 197 ? -3.297  -35.560 -14.943 1.00 187.05 ? 217 ASP   A CB  1 
ATOM   1334 C  CG  . ASP   A 1 197 ? -4.149  -36.798 -14.730 1.00 184.13 ? 217 ASP   A CG  1 
ATOM   1335 O  OD1 . ASP   A 1 197 ? -4.820  -37.219 -15.693 1.00 187.50 ? 217 ASP   A OD1 1 
ATOM   1336 O  OD2 . ASP   A 1 197 ? -4.132  -37.331 -13.604 1.00 184.46 ? 217 ASP   A OD2 1 
ATOM   1337 N  N   . PRO   A 1 198 ? -1.303  -34.868 -11.801 1.00 208.48 ? 218 PRO   A N   1 
ATOM   1338 C  CA  . PRO   A 1 198 ? -0.058  -35.302 -11.173 1.00 213.33 ? 218 PRO   A CA  1 
ATOM   1339 C  C   . PRO   A 1 198 ? -0.200  -36.670 -10.495 1.00 217.82 ? 218 PRO   A C   1 
ATOM   1340 O  O   . PRO   A 1 198 ? 0.431   -37.605 -10.950 1.00 218.23 ? 218 PRO   A O   1 
ATOM   1341 C  CB  . PRO   A 1 198 ? 0.185   -34.227 -10.106 1.00 213.45 ? 218 PRO   A CB  1 
ATOM   1342 C  CG  . PRO   A 1 198 ? -1.200  -33.746 -9.733  1.00 209.29 ? 218 PRO   A CG  1 
ATOM   1343 C  CD  . PRO   A 1 198 ? -2.022  -33.877 -10.998 1.00 204.55 ? 218 PRO   A CD  1 
ATOM   1344 N  N   . PHE   A 1 199 ? -1.019  -36.760 -9.443  1.00 240.38 ? 219 PHE   A N   1 
ATOM   1345 C  CA  . PHE   A 1 199 ? -1.131  -38.033 -8.683  1.00 239.87 ? 219 PHE   A CA  1 
ATOM   1346 C  C   . PHE   A 1 199 ? -2.518  -38.648 -8.880  1.00 238.06 ? 219 PHE   A C   1 
ATOM   1347 O  O   . PHE   A 1 199 ? -2.627  -39.885 -8.908  1.00 236.95 ? 219 PHE   A O   1 
ATOM   1348 C  CB  . PHE   A 1 199 ? -0.845  -37.789 -7.200  1.00 242.62 ? 219 PHE   A CB  1 
ATOM   1349 C  CG  . PHE   A 1 199 ? -2.069  -37.727 -6.324  1.00 243.98 ? 219 PHE   A CG  1 
ATOM   1350 C  CD1 . PHE   A 1 199 ? -2.417  -38.799 -5.521  1.00 244.39 ? 219 PHE   A CD1 1 
ATOM   1351 C  CD2 . PHE   A 1 199 ? -2.870  -36.597 -6.304  1.00 235.58 ? 219 PHE   A CD2 1 
ATOM   1352 C  CE1 . PHE   A 1 199 ? -3.540  -38.745 -4.714  1.00 242.65 ? 219 PHE   A CE1 1 
ATOM   1353 C  CE2 . PHE   A 1 199 ? -3.995  -36.545 -5.499  1.00 232.62 ? 219 PHE   A CE2 1 
ATOM   1354 C  CZ  . PHE   A 1 199 ? -4.325  -37.617 -4.705  1.00 232.22 ? 219 PHE   A CZ  1 
ATOM   1355 N  N   . PHE   A 1 200 ? -3.545  -37.807 -9.002  1.00 216.21 ? 220 PHE   A N   1 
ATOM   1356 C  CA  . PHE   A 1 200 ? -4.912  -38.327 -9.255  1.00 209.02 ? 220 PHE   A CA  1 
ATOM   1357 C  C   . PHE   A 1 200 ? -4.796  -39.471 -10.261 1.00 202.51 ? 220 PHE   A C   1 
ATOM   1358 O  O   . PHE   A 1 200 ? -5.471  -40.496 -10.092 1.00 186.91 ? 220 PHE   A O   1 
ATOM   1359 C  CB  . PHE   A 1 200 ? -5.823  -37.192 -9.723  1.00 199.84 ? 220 PHE   A CB  1 
ATOM   1360 C  CG  . PHE   A 1 200 ? -5.661  -35.931 -8.914  1.00 205.36 ? 220 PHE   A CG  1 
ATOM   1361 C  CD1 . PHE   A 1 200 ? -4.708  -34.986 -9.255  1.00 204.90 ? 220 PHE   A CD1 1 
ATOM   1362 C  CD2 . PHE   A 1 200 ? -6.444  -35.702 -7.796  1.00 199.38 ? 220 PHE   A CD2 1 
ATOM   1363 C  CE1 . PHE   A 1 200 ? -4.552  -33.832 -8.504  1.00 199.73 ? 220 PHE   A CE1 1 
ATOM   1364 C  CE2 . PHE   A 1 200 ? -6.290  -34.546 -7.046  1.00 194.70 ? 220 PHE   A CE2 1 
ATOM   1365 C  CZ  . PHE   A 1 200 ? -5.343  -33.614 -7.401  1.00 196.99 ? 220 PHE   A CZ  1 
ATOM   1366 N  N   . LEU   A 1 201 ? -3.943  -39.296 -11.270 1.00 203.53 ? 221 LEU   A N   1 
ATOM   1367 C  CA  . LEU   A 1 201 ? -3.711  -40.382 -12.252 1.00 196.98 ? 221 LEU   A CA  1 
ATOM   1368 C  C   . LEU   A 1 201 ? -3.508  -41.683 -11.482 1.00 188.01 ? 221 LEU   A C   1 
ATOM   1369 O  O   . LEU   A 1 201 ? -4.336  -42.601 -11.628 1.00 178.86 ? 221 LEU   A O   1 
ATOM   1370 C  CB  . LEU   A 1 201 ? -2.463  -40.044 -13.068 1.00 201.23 ? 221 LEU   A CB  1 
ATOM   1371 C  CG  . LEU   A 1 201 ? -2.566  -40.348 -14.561 1.00 203.03 ? 221 LEU   A CG  1 
ATOM   1372 C  CD1 . LEU   A 1 201 ? -4.020  -40.503 -14.979 1.00 205.57 ? 221 LEU   A CD1 1 
ATOM   1373 C  CD2 . LEU   A 1 201 ? -1.887  -39.264 -15.384 1.00 204.06 ? 221 LEU   A CD2 1 
ATOM   1374 N  N   . SER   A 1 202 ? -2.439  -41.746 -10.692 1.00 189.66 ? 222 SER   A N   1 
ATOM   1375 C  CA  . SER   A 1 202 ? -2.163  -42.961 -9.891  1.00 187.36 ? 222 SER   A CA  1 
ATOM   1376 C  C   . SER   A 1 202 ? -3.479  -43.513 -9.343  1.00 188.22 ? 222 SER   A C   1 
ATOM   1377 O  O   . SER   A 1 202 ? -3.732  -44.715 -9.519  1.00 187.14 ? 222 SER   A O   1 
ATOM   1378 C  CB  . SER   A 1 202 ? -1.206  -42.647 -8.785  1.00 197.95 ? 222 SER   A CB  1 
ATOM   1379 O  OG  . SER   A 1 202 ? -0.445  -41.488 -9.090  1.00 196.22 ? 222 SER   A OG  1 
ATOM   1380 N  N   . ILE   A 1 203 ? -4.288  -42.654 -8.720  1.00 174.28 ? 223 ILE   A N   1 
ATOM   1381 C  CA  . ILE   A 1 203 ? -5.554  -43.129 -8.090  1.00 165.83 ? 223 ILE   A CA  1 
ATOM   1382 C  C   . ILE   A 1 203 ? -6.284  -44.046 -9.075  1.00 166.06 ? 223 ILE   A C   1 
ATOM   1383 O  O   . ILE   A 1 203 ? -6.565  -45.196 -8.716  1.00 166.53 ? 223 ILE   A O   1 
ATOM   1384 C  CB  . ILE   A 1 203 ? -6.426  -41.935 -7.664  1.00 167.24 ? 223 ILE   A CB  1 
ATOM   1385 C  CG1 . ILE   A 1 203 ? -5.628  -40.902 -6.866  1.00 175.84 ? 223 ILE   A CG1 1 
ATOM   1386 C  CG2 . ILE   A 1 203 ? -7.650  -42.414 -6.901  1.00 165.67 ? 223 ILE   A CG2 1 
ATOM   1387 C  CD1 . ILE   A 1 203 ? -6.446  -39.707 -6.440  1.00 187.27 ? 223 ILE   A CD1 1 
ATOM   1388 N  N   . THR   A 1 204 ? -6.587  -43.546 -10.273 1.00 166.33 ? 224 THR   A N   1 
ATOM   1389 C  CA  . THR   A 1 204 ? -7.339  -44.355 -11.263 1.00 158.11 ? 224 THR   A CA  1 
ATOM   1390 C  C   . THR   A 1 204 ? -6.787  -45.782 -11.286 1.00 157.28 ? 224 THR   A C   1 
ATOM   1391 O  O   . THR   A 1 204 ? -7.598  -46.719 -11.213 1.00 147.68 ? 224 THR   A O   1 
ATOM   1392 C  CB  . THR   A 1 204 ? -7.247  -43.718 -12.649 1.00 140.96 ? 224 THR   A CB  1 
ATOM   1393 O  OG1 . THR   A 1 204 ? -5.978  -44.072 -13.199 1.00 142.61 ? 224 THR   A OG1 1 
ATOM   1394 C  CG2 . THR   A 1 204 ? -7.379  -42.213 -12.608 1.00 147.48 ? 224 THR   A CG2 1 
ATOM   1395 N  N   . VAL   A 1 205 ? -5.465  -45.936 -11.377 1.00 155.80 ? 225 VAL   A N   1 
ATOM   1396 C  CA  . VAL   A 1 205 ? -4.850  -47.292 -11.499 1.00 162.24 ? 225 VAL   A CA  1 
ATOM   1397 C  C   . VAL   A 1 205 ? -4.706  -47.895 -10.107 1.00 170.70 ? 225 VAL   A C   1 
ATOM   1398 O  O   . VAL   A 1 205 ? -4.656  -49.132 -10.005 1.00 170.95 ? 225 VAL   A O   1 
ATOM   1399 C  CB  . VAL   A 1 205 ? -3.490  -47.216 -12.212 1.00 161.80 ? 225 VAL   A CB  1 
ATOM   1400 C  CG1 . VAL   A 1 205 ? -3.486  -48.029 -13.496 1.00 150.74 ? 225 VAL   A CG1 1 
ATOM   1401 C  CG2 . VAL   A 1 205 ? -3.083  -45.776 -12.487 1.00 143.58 ? 225 VAL   A CG2 1 
ATOM   1402 N  N   . PHE   A 1 206 ? -4.611  -47.050 -9.088  1.00 195.38 ? 226 PHE   A N   1 
ATOM   1403 C  CA  . PHE   A 1 206 ? -4.528  -47.509 -7.702  1.00 192.95 ? 226 PHE   A CA  1 
ATOM   1404 C  C   . PHE   A 1 206 ? -5.723  -46.984 -6.909  1.00 193.80 ? 226 PHE   A C   1 
ATOM   1405 O  O   . PHE   A 1 206 ? -5.563  -46.178 -5.988  1.00 193.93 ? 226 PHE   A O   1 
ATOM   1406 C  CB  . PHE   A 1 206 ? -3.207  -47.082 -7.056  1.00 205.98 ? 226 PHE   A CB  1 
ATOM   1407 C  CG  . PHE   A 1 206 ? -2.042  -47.060 -8.005  1.00 215.07 ? 226 PHE   A CG  1 
ATOM   1408 C  CD1 . PHE   A 1 206 ? -1.628  -48.217 -8.640  1.00 218.69 ? 226 PHE   A CD1 1 
ATOM   1409 C  CD2 . PHE   A 1 206 ? -1.349  -45.888 -8.247  1.00 217.10 ? 226 PHE   A CD2 1 
ATOM   1410 C  CE1 . PHE   A 1 206 ? -0.558  -48.199 -9.513  1.00 219.11 ? 226 PHE   A CE1 1 
ATOM   1411 C  CE2 . PHE   A 1 206 ? -0.276  -45.863 -9.120  1.00 217.38 ? 226 PHE   A CE2 1 
ATOM   1412 C  CZ  . PHE   A 1 206 ? 0.119   -47.021 -9.752  1.00 217.99 ? 226 PHE   A CZ  1 
ATOM   1413 N  N   . PRO   A 1 207 ? -6.945  -47.436 -7.227  1.00 177.43 ? 227 PRO   A N   1 
ATOM   1414 C  CA  . PRO   A 1 207 ? -8.066  -47.114 -6.337  1.00 167.40 ? 227 PRO   A CA  1 
ATOM   1415 C  C   . PRO   A 1 207 ? -8.034  -47.910 -5.052  1.00 166.69 ? 227 PRO   A C   1 
ATOM   1416 O  O   . PRO   A 1 207 ? -8.545  -47.439 -4.030  1.00 164.35 ? 227 PRO   A O   1 
ATOM   1417 C  CB  . PRO   A 1 207 ? -9.294  -47.439 -7.197  1.00 161.31 ? 227 PRO   A CB  1 
ATOM   1418 C  CG  . PRO   A 1 207 ? -8.794  -48.454 -8.229  1.00 165.50 ? 227 PRO   A CG  1 
ATOM   1419 C  CD  . PRO   A 1 207 ? -7.288  -48.612 -8.042  1.00 172.69 ? 227 PRO   A CD  1 
ATOM   1420 N  N   . PHE   A 1 208 ? -7.446  -49.101 -5.083  1.00 162.02 ? 228 PHE   A N   1 
ATOM   1421 C  CA  . PHE   A 1 208 ? -7.155  -49.852 -3.877  1.00 159.48 ? 228 PHE   A CA  1 
ATOM   1422 C  C   . PHE   A 1 208 ? -6.289  -49.073 -2.898  1.00 160.83 ? 228 PHE   A C   1 
ATOM   1423 O  O   . PHE   A 1 208 ? -6.257  -49.402 -1.704  1.00 159.94 ? 228 PHE   A O   1 
ATOM   1424 C  CB  . PHE   A 1 208 ? -6.480  -51.166 -4.270  1.00 160.96 ? 228 PHE   A CB  1 
ATOM   1425 C  CG  . PHE   A 1 208 ? -5.230  -50.998 -5.090  1.00 170.86 ? 228 PHE   A CG  1 
ATOM   1426 C  CD1 . PHE   A 1 208 ? -4.009  -50.820 -4.480  1.00 174.30 ? 228 PHE   A CD1 1 
ATOM   1427 C  CD2 . PHE   A 1 208 ? -5.281  -51.006 -6.477  1.00 166.69 ? 228 PHE   A CD2 1 
ATOM   1428 C  CE1 . PHE   A 1 208 ? -2.854  -50.663 -5.221  1.00 173.32 ? 228 PHE   A CE1 1 
ATOM   1429 C  CE2 . PHE   A 1 208 ? -4.123  -50.857 -7.229  1.00 172.27 ? 228 PHE   A CE2 1 
ATOM   1430 C  CZ  . PHE   A 1 208 ? -2.911  -50.680 -6.596  1.00 178.74 ? 228 PHE   A CZ  1 
ATOM   1431 N  N   . LEU   A 1 209 ? -5.583  -48.053 -3.373  1.00 163.96 ? 229 LEU   A N   1 
ATOM   1432 C  CA  . LEU   A 1 209 ? -4.737  -47.252 -2.510  1.00 159.33 ? 229 LEU   A CA  1 
ATOM   1433 C  C   . LEU   A 1 209 ? -5.514  -46.221 -1.705  1.00 152.91 ? 229 LEU   A C   1 
ATOM   1434 O  O   . LEU   A 1 209 ? -4.958  -45.678 -0.755  1.00 160.89 ? 229 LEU   A O   1 
ATOM   1435 C  CB  . LEU   A 1 209 ? -3.663  -46.546 -3.344  1.00 164.05 ? 229 LEU   A CB  1 
ATOM   1436 C  CG  . LEU   A 1 209 ? -2.283  -47.204 -3.437  1.00 171.77 ? 229 LEU   A CG  1 
ATOM   1437 C  CD1 . LEU   A 1 209 ? -1.286  -46.282 -4.120  1.00 175.94 ? 229 LEU   A CD1 1 
ATOM   1438 C  CD2 . LEU   A 1 209 ? -1.771  -47.595 -2.066  1.00 168.28 ? 229 LEU   A CD2 1 
ATOM   1439 N  N   . ILE   A 1 210 ? -6.773  -45.944 -2.028  1.00 144.67 ? 230 ILE   A N   1 
ATOM   1440 C  CA  . ILE   A 1 210 ? -7.437  -44.773 -1.452  1.00 143.48 ? 230 ILE   A CA  1 
ATOM   1441 C  C   . ILE   A 1 210 ? -7.592  -44.938 0.059   1.00 153.27 ? 230 ILE   A C   1 
ATOM   1442 O  O   . ILE   A 1 210 ? -7.221  -44.022 0.809   1.00 150.12 ? 230 ILE   A O   1 
ATOM   1443 C  CB  . ILE   A 1 210 ? -8.783  -44.500 -2.140  1.00 143.84 ? 230 ILE   A CB  1 
ATOM   1444 C  CG1 . ILE   A 1 210 ? -8.547  -43.650 -3.386  1.00 138.31 ? 230 ILE   A CG1 1 
ATOM   1445 C  CG2 . ILE   A 1 210 ? -9.743  -43.775 -1.192  1.00 140.94 ? 230 ILE   A CG2 1 
ATOM   1446 C  CD1 . ILE   A 1 210 ? -9.810  -43.171 -4.051  1.00 140.57 ? 230 ILE   A CD1 1 
ATOM   1447 N  N   . PRO   A 1 211 ? -8.101  -46.065 0.569   1.00 160.45 ? 231 PRO   A N   1 
ATOM   1448 C  CA  . PRO   A 1 211 ? -8.108  -46.236 2.031   1.00 156.57 ? 231 PRO   A CA  1 
ATOM   1449 C  C   . PRO   A 1 211 ? -6.714  -46.238 2.643   1.00 153.84 ? 231 PRO   A C   1 
ATOM   1450 O  O   . PRO   A 1 211 ? -6.583  -45.924 3.833   1.00 152.77 ? 231 PRO   A O   1 
ATOM   1451 C  CB  . PRO   A 1 211 ? -8.831  -47.586 2.198   1.00 152.52 ? 231 PRO   A CB  1 
ATOM   1452 C  CG  . PRO   A 1 211 ? -8.635  -48.217 0.833   1.00 147.66 ? 231 PRO   A CG  1 
ATOM   1453 C  CD  . PRO   A 1 211 ? -9.013  -47.066 -0.001  1.00 154.87 ? 231 PRO   A CD  1 
ATOM   1454 N  N   . ILE   A 1 212 ? -5.677  -46.612 1.876   1.00 163.86 ? 232 ILE   A N   1 
ATOM   1455 C  CA  . ILE   A 1 212 ? -4.292  -46.463 2.338   1.00 169.25 ? 232 ILE   A CA  1 
ATOM   1456 C  C   . ILE   A 1 212 ? -4.041  -45.026 2.779   1.00 171.25 ? 232 ILE   A C   1 
ATOM   1457 O  O   . ILE   A 1 212 ? -3.658  -44.764 3.924   1.00 169.62 ? 232 ILE   A O   1 
ATOM   1458 C  CB  . ILE   A 1 212 ? -3.293  -46.876 1.240   1.00 177.31 ? 232 ILE   A CB  1 
ATOM   1459 C  CG1 . ILE   A 1 212 ? -3.138  -48.394 1.099   1.00 185.59 ? 232 ILE   A CG1 1 
ATOM   1460 C  CG2 . ILE   A 1 212 ? -1.926  -46.250 1.505   1.00 178.36 ? 232 ILE   A CG2 1 
ATOM   1461 C  CD1 . ILE   A 1 212 ? -2.033  -48.993 1.959   1.00 193.25 ? 232 ILE   A CD1 1 
ATOM   1462 N  N   . LEU   A 1 213 ? -4.261  -44.067 1.873   1.00 171.90 ? 233 LEU   A N   1 
ATOM   1463 C  CA  . LEU   A 1 213 ? -4.011  -42.675 2.231   1.00 173.93 ? 233 LEU   A CA  1 
ATOM   1464 C  C   . LEU   A 1 213 ? -5.071  -42.130 3.179   1.00 179.15 ? 233 LEU   A C   1 
ATOM   1465 O  O   . LEU   A 1 213 ? -4.810  -41.144 3.878   1.00 185.59 ? 233 LEU   A O   1 
ATOM   1466 C  CB  . LEU   A 1 213 ? -3.932  -41.781 0.989   1.00 165.30 ? 233 LEU   A CB  1 
ATOM   1467 C  CG  . LEU   A 1 213 ? -3.212  -42.252 -0.279  1.00 157.04 ? 233 LEU   A CG  1 
ATOM   1468 C  CD1 . LEU   A 1 213 ? -4.160  -42.948 -1.217  1.00 152.21 ? 233 LEU   A CD1 1 
ATOM   1469 C  CD2 . LEU   A 1 213 ? -2.555  -41.102 -0.988  1.00 165.14 ? 233 LEU   A CD2 1 
ATOM   1470 N  N   . GLU   A 1 214 ? -6.253  -42.749 3.225   1.00 161.19 ? 234 GLU   A N   1 
ATOM   1471 C  CA  . GLU   A 1 214 ? -7.280  -42.308 4.161   1.00 152.20 ? 234 GLU   A CA  1 
ATOM   1472 C  C   . GLU   A 1 214 ? -6.862  -42.507 5.612   1.00 155.00 ? 234 GLU   A C   1 
ATOM   1473 O  O   . GLU   A 1 214 ? -7.406  -41.836 6.496   1.00 161.46 ? 234 GLU   A O   1 
ATOM   1474 C  CB  . GLU   A 1 214 ? -8.598  -43.040 3.896   1.00 150.56 ? 234 GLU   A CB  1 
ATOM   1475 C  CG  . GLU   A 1 214 ? -9.803  -42.119 3.750   1.00 151.86 ? 234 GLU   A CG  1 
ATOM   1476 C  CD  . GLU   A 1 214 ? -10.916 -42.734 2.922   1.00 162.53 ? 234 GLU   A CD  1 
ATOM   1477 O  OE1 . GLU   A 1 214 ? -11.528 -42.007 2.111   1.00 164.18 ? 234 GLU   A OE1 1 
ATOM   1478 O  OE2 . GLU   A 1 214 ? -11.180 -43.944 3.083   1.00 161.35 ? 234 GLU   A OE2 1 
ATOM   1479 N  N   . VAL   A 1 215 ? -5.912  -43.408 5.884   1.00 169.50 ? 235 VAL   A N   1 
ATOM   1480 C  CA  . VAL   A 1 215 ? -5.400  -43.585 7.238   1.00 174.02 ? 235 VAL   A CA  1 
ATOM   1481 C  C   . VAL   A 1 215 ? -4.115  -42.807 7.472   1.00 177.41 ? 235 VAL   A C   1 
ATOM   1482 O  O   . VAL   A 1 215 ? -3.578  -42.832 8.587   1.00 184.01 ? 235 VAL   A O   1 
ATOM   1483 C  CB  . VAL   A 1 215 ? -5.182  -45.077 7.573   1.00 166.16 ? 235 VAL   A CB  1 
ATOM   1484 C  CG1 . VAL   A 1 215 ? -6.447  -45.885 7.291   1.00 158.08 ? 235 VAL   A CG1 1 
ATOM   1485 C  CG2 . VAL   A 1 215 ? -3.966  -45.639 6.850   1.00 176.13 ? 235 VAL   A CG2 1 
ATOM   1486 N  N   . LEU   A 1 216 ? -3.605  -42.113 6.454   1.00 181.32 ? 236 LEU   A N   1 
ATOM   1487 C  CA  . LEU   A 1 216 ? -2.406  -41.296 6.573   1.00 190.43 ? 236 LEU   A CA  1 
ATOM   1488 C  C   . LEU   A 1 216 ? -2.719  -39.818 6.761   1.00 196.69 ? 236 LEU   A C   1 
ATOM   1489 O  O   . LEU   A 1 216 ? -1.794  -39.000 6.772   1.00 204.18 ? 236 LEU   A O   1 
ATOM   1490 C  CB  . LEU   A 1 216 ? -1.517  -41.468 5.337   1.00 191.10 ? 236 LEU   A CB  1 
ATOM   1491 C  CG  . LEU   A 1 216 ? -1.271  -42.862 4.759   1.00 189.79 ? 236 LEU   A CG  1 
ATOM   1492 C  CD1 . LEU   A 1 216 ? -0.206  -42.805 3.674   1.00 188.01 ? 236 LEU   A CD1 1 
ATOM   1493 C  CD2 . LEU   A 1 216 ? -0.865  -43.836 5.851   1.00 192.96 ? 236 LEU   A CD2 1 
ATOM   1494 N  N   . ASN   A 1 217 ? -3.997  -39.461 6.904   1.00 209.45 ? 237 ASN   A N   1 
ATOM   1495 C  CA  . ASN   A 1 217 ? -4.455  -38.069 6.852   1.00 219.71 ? 237 ASN   A CA  1 
ATOM   1496 C  C   . ASN   A 1 217 ? -4.016  -37.377 5.567   1.00 212.82 ? 237 ASN   A C   1 
ATOM   1497 O  O   . ASN   A 1 217 ? -3.938  -36.145 5.509   1.00 206.58 ? 237 ASN   A O   1 
ATOM   1498 C  CB  . ASN   A 1 217 ? -3.990  -37.268 8.074   1.00 219.61 ? 237 ASN   A CB  1 
ATOM   1499 C  CG  . ASN   A 1 217 ? -3.954  -38.101 9.336   1.00 230.30 ? 237 ASN   A CG  1 
ATOM   1500 O  OD1 . ASN   A 1 217 ? -4.758  -39.015 9.511   1.00 231.52 ? 237 ASN   A OD1 1 
ATOM   1501 N  ND2 . ASN   A 1 217 ? -3.024  -37.783 10.229  1.00 228.64 ? 237 ASN   A ND2 1 
ATOM   1502 N  N   . ILE   A 1 218 ? -3.722  -38.155 4.532   1.00 191.57 ? 238 ILE   A N   1 
ATOM   1503 C  CA  . ILE   A 1 218 ? -3.390  -37.597 3.230   1.00 180.22 ? 238 ILE   A CA  1 
ATOM   1504 C  C   . ILE   A 1 218 ? -4.676  -37.135 2.565   1.00 178.88 ? 238 ILE   A C   1 
ATOM   1505 O  O   . ILE   A 1 218 ? -5.650  -37.891 2.477   1.00 171.21 ? 238 ILE   A O   1 
ATOM   1506 C  CB  . ILE   A 1 218 ? -2.665  -38.631 2.358   1.00 172.24 ? 238 ILE   A CB  1 
ATOM   1507 C  CG1 . ILE   A 1 218 ? -1.226  -38.814 2.827   1.00 173.01 ? 238 ILE   A CG1 1 
ATOM   1508 C  CG2 . ILE   A 1 218 ? -2.686  -38.186 0.904   1.00 166.80 ? 238 ILE   A CG2 1 
ATOM   1509 C  CD1 . ILE   A 1 218 ? -0.380  -39.549 1.837   1.00 163.44 ? 238 ILE   A CD1 1 
ATOM   1510 N  N   . CYS   A 1 219 ? -4.686  -35.894 2.102   1.00 174.31 ? 239 CYS   A N   1 
ATOM   1511 C  CA  . CYS   A 1 219 ? -5.820  -35.348 1.378   1.00 167.92 ? 239 CYS   A CA  1 
ATOM   1512 C  C   . CYS   A 1 219 ? -5.357  -34.881 0.008   1.00 166.06 ? 239 CYS   A C   1 
ATOM   1513 O  O   . CYS   A 1 219 ? -4.234  -34.390 -0.143  1.00 169.52 ? 239 CYS   A O   1 
ATOM   1514 C  CB  . CYS   A 1 219 ? -6.456  -34.182 2.141   1.00 167.75 ? 239 CYS   A CB  1 
ATOM   1515 S  SG  . CYS   A 1 219 ? -7.132  -34.612 3.760   1.00 164.46 ? 239 CYS   A SG  1 
ATOM   1516 N  N   . VAL   A 1 220 ? -6.221  -35.053 -0.995  1.00 180.31 ? 240 VAL   A N   1 
ATOM   1517 C  CA  . VAL   A 1 220 ? -6.002  -34.380 -2.266  1.00 175.60 ? 240 VAL   A CA  1 
ATOM   1518 C  C   . VAL   A 1 220 ? -6.059  -32.875 -2.072  1.00 179.81 ? 240 VAL   A C   1 
ATOM   1519 O  O   . VAL   A 1 220 ? -5.487  -32.119 -2.866  1.00 172.88 ? 240 VAL   A O   1 
ATOM   1520 C  CB  . VAL   A 1 220 ? -7.030  -34.849 -3.316  1.00 168.60 ? 240 VAL   A CB  1 
ATOM   1521 C  CG1 . VAL   A 1 220 ? -7.128  -36.363 -3.320  1.00 159.25 ? 240 VAL   A CG1 1 
ATOM   1522 C  CG2 . VAL   A 1 220 ? -8.392  -34.230 -3.043  1.00 163.61 ? 240 VAL   A CG2 1 
ATOM   1523 N  N   . PHE   A 1 221 ? -6.739  -32.422 -1.019  1.00 172.22 ? 241 PHE   A N   1 
ATOM   1524 C  CA  . PHE   A 1 221 ? -6.766  -31.018 -0.648  1.00 174.21 ? 241 PHE   A CA  1 
ATOM   1525 C  C   . PHE   A 1 221 ? -5.638  -30.782 0.344   1.00 183.66 ? 241 PHE   A C   1 
ATOM   1526 O  O   . PHE   A 1 221 ? -5.739  -31.235 1.495   1.00 181.52 ? 241 PHE   A O   1 
ATOM   1527 C  CB  . PHE   A 1 221 ? -8.108  -30.661 -0.030  1.00 169.90 ? 241 PHE   A CB  1 
ATOM   1528 C  CG  . PHE   A 1 221 ? -9.270  -31.371 -0.668  1.00 162.21 ? 241 PHE   A CG  1 
ATOM   1529 C  CD1 . PHE   A 1 221 ? -9.753  -30.969 -1.902  1.00 158.98 ? 241 PHE   A CD1 1 
ATOM   1530 C  CD2 . PHE   A 1 221 ? -9.864  -32.456 -0.042  1.00 158.12 ? 241 PHE   A CD2 1 
ATOM   1531 C  CE1 . PHE   A 1 221 ? -10.816 -31.625 -2.492  1.00 157.46 ? 241 PHE   A CE1 1 
ATOM   1532 C  CE2 . PHE   A 1 221 ? -10.927 -33.117 -0.628  1.00 157.17 ? 241 PHE   A CE2 1 
ATOM   1533 C  CZ  . PHE   A 1 221 ? -11.403 -32.699 -1.855  1.00 158.11 ? 241 PHE   A CZ  1 
ATOM   1534 N  N   . PRO   A 1 222 ? -4.557  -30.106 -0.043  1.00 194.56 ? 242 PRO   A N   1 
ATOM   1535 C  CA  . PRO   A 1 222 ? -3.391  -29.984 0.844   1.00 200.34 ? 242 PRO   A CA  1 
ATOM   1536 C  C   . PRO   A 1 222 ? -3.776  -29.496 2.232   1.00 203.99 ? 242 PRO   A C   1 
ATOM   1537 O  O   . PRO   A 1 222 ? -4.427  -28.462 2.390   1.00 201.84 ? 242 PRO   A O   1 
ATOM   1538 C  CB  . PRO   A 1 222 ? -2.493  -28.976 0.113   1.00 206.27 ? 242 PRO   A CB  1 
ATOM   1539 C  CG  . PRO   A 1 222 ? -3.349  -28.378 -0.973  1.00 203.77 ? 242 PRO   A CG  1 
ATOM   1540 C  CD  . PRO   A 1 222 ? -4.355  -29.414 -1.324  1.00 197.06 ? 242 PRO   A CD  1 
ATOM   1541 N  N   . ARG   A 1 223 ? -3.359  -30.255 3.247   1.00 210.08 ? 243 ARG   A N   1 
ATOM   1542 C  CA  . ARG   A 1 223 ? -3.837  -30.085 4.616   1.00 205.94 ? 243 ARG   A CA  1 
ATOM   1543 C  C   . ARG   A 1 223 ? -3.534  -28.704 5.186   1.00 200.67 ? 243 ARG   A C   1 
ATOM   1544 O  O   . ARG   A 1 223 ? -3.947  -28.389 6.307   1.00 203.89 ? 243 ARG   A O   1 
ATOM   1545 C  CB  . ARG   A 1 223 ? -3.240  -31.168 5.518   1.00 210.65 ? 243 ARG   A CB  1 
ATOM   1546 C  CG  . ARG   A 1 223 ? -1.817  -30.898 5.975   1.00 213.73 ? 243 ARG   A CG  1 
ATOM   1547 C  CD  . ARG   A 1 223 ? -1.411  -31.876 7.064   1.00 213.24 ? 243 ARG   A CD  1 
ATOM   1548 N  NE  . ARG   A 1 223 ? -2.543  -32.225 7.914   1.00 211.15 ? 243 ARG   A NE  1 
ATOM   1549 C  CZ  . ARG   A 1 223 ? -2.829  -31.633 9.065   1.00 210.79 ? 243 ARG   A CZ  1 
ATOM   1550 N  NH1 . ARG   A 1 223 ? -2.075  -30.659 9.548   1.00 207.37 ? 243 ARG   A NH1 1 
ATOM   1551 N  NH2 . ARG   A 1 223 ? -3.896  -32.031 9.752   1.00 211.44 ? 243 ARG   A NH2 1 
ATOM   1552 N  N   . GLU   A 1 224 ? -2.815  -27.875 4.432   1.00 212.46 ? 244 GLU   A N   1 
ATOM   1553 C  CA  . GLU   A 1 224 ? -2.599  -26.490 4.822   1.00 212.60 ? 244 GLU   A CA  1 
ATOM   1554 C  C   . GLU   A 1 224 ? -3.671  -25.549 4.288   1.00 207.63 ? 244 GLU   A C   1 
ATOM   1555 O  O   . GLU   A 1 224 ? -3.881  -24.481 4.875   1.00 211.71 ? 244 GLU   A O   1 
ATOM   1556 C  CB  . GLU   A 1 224 ? -1.219  -26.017 4.355   1.00 215.09 ? 244 GLU   A CB  1 
ATOM   1557 C  CG  . GLU   A 1 224 ? -0.838  -26.484 2.963   1.00 212.67 ? 244 GLU   A CG  1 
ATOM   1558 C  CD  . GLU   A 1 224 ? 0.644   -26.333 2.690   1.00 218.22 ? 244 GLU   A CD  1 
ATOM   1559 O  OE1 . GLU   A 1 224 ? 1.430   -26.331 3.660   1.00 216.71 ? 244 GLU   A OE1 1 
ATOM   1560 O  OE2 . GLU   A 1 224 ? 1.022   -26.217 1.505   1.00 216.86 ? 244 GLU   A OE2 1 
ATOM   1561 N  N   . VAL   A 1 225 ? -4.343  -25.895 3.152   1.00 204.20 ? 245 VAL   A N   1 
ATOM   1562 C  CA  . VAL   A 1 225 ? -5.472  -25.092 2.694   1.00 183.62 ? 245 VAL   A CA  1 
ATOM   1563 C  C   . VAL   A 1 225 ? -6.687  -25.318 3.591   1.00 181.49 ? 245 VAL   A C   1 
ATOM   1564 O  O   . VAL   A 1 225 ? -7.449  -24.386 3.869   1.00 182.60 ? 245 VAL   A O   1 
ATOM   1565 C  CB  . VAL   A 1 225 ? -5.786  -25.400 1.220   1.00 166.82 ? 245 VAL   A CB  1 
ATOM   1566 C  CG1 . VAL   A 1 225 ? -6.928  -24.527 0.731   1.00 164.88 ? 245 VAL   A CG1 1 
ATOM   1567 C  CG2 . VAL   A 1 225 ? -4.560  -25.192 0.367   1.00 162.23 ? 245 VAL   A CG2 1 
ATOM   1568 N  N   . THR   A 1 226 ? -6.882  -26.551 4.076   1.00 173.84 ? 246 THR   A N   1 
ATOM   1569 C  CA  . THR   A 1 226 ? -8.031  -26.833 4.936   1.00 161.04 ? 246 THR   A CA  1 
ATOM   1570 C  C   . THR   A 1 226 ? -7.803  -26.340 6.363   1.00 170.33 ? 246 THR   A C   1 
ATOM   1571 O  O   . THR   A 1 226 ? -8.716  -25.773 6.975   1.00 170.04 ? 246 THR   A O   1 
ATOM   1572 C  CB  . THR   A 1 226 ? -8.361  -28.334 4.928   1.00 144.43 ? 246 THR   A CB  1 
ATOM   1573 O  OG1 . THR   A 1 226 ? -7.234  -29.096 5.390   1.00 157.18 ? 246 THR   A OG1 1 
ATOM   1574 C  CG2 . THR   A 1 226 ? -8.759  -28.799 3.530   1.00 119.62 ? 246 THR   A CG2 1 
ATOM   1575 N  N   . ASN   A 1 227 ? -6.604  -26.554 6.918   1.00 182.61 ? 247 ASN   A N   1 
ATOM   1576 C  CA  . ASN   A 1 227 ? -6.311  -26.017 8.244   1.00 196.66 ? 247 ASN   A CA  1 
ATOM   1577 C  C   . ASN   A 1 227 ? -6.570  -24.519 8.264   1.00 197.36 ? 247 ASN   A C   1 
ATOM   1578 O  O   . ASN   A 1 227 ? -6.994  -23.980 9.291   1.00 210.13 ? 247 ASN   A O   1 
ATOM   1579 C  CB  . ASN   A 1 227 ? -4.899  -26.400 8.690   1.00 207.01 ? 247 ASN   A CB  1 
ATOM   1580 C  CG  . ASN   A 1 227 ? -4.878  -27.657 9.531   1.00 209.76 ? 247 ASN   A CG  1 
ATOM   1581 O  OD1 . ASN   A 1 227 ? -5.888  -28.035 10.119  1.00 209.36 ? 247 ASN   A OD1 1 
ATOM   1582 N  ND2 . ASN   A 1 227 ? -3.722  -28.307 9.601   1.00 211.83 ? 247 ASN   A ND2 1 
ATOM   1583 N  N   . PHE   A 1 228 ? -6.450  -23.904 7.086   1.00 183.75 ? 248 PHE   A N   1 
ATOM   1584 C  CA  . PHE   A 1 228 ? -6.722  -22.452 6.992   1.00 173.46 ? 248 PHE   A CA  1 
ATOM   1585 C  C   . PHE   A 1 228 ? -8.203  -22.112 7.138   1.00 168.59 ? 248 PHE   A C   1 
ATOM   1586 O  O   . PHE   A 1 228 ? -8.591  -21.510 8.156   1.00 173.17 ? 248 PHE   A O   1 
ATOM   1587 C  CB  . PHE   A 1 228 ? -6.299  -21.930 5.620   1.00 163.25 ? 248 PHE   A CB  1 
ATOM   1588 C  CG  . PHE   A 1 228 ? -6.981  -20.650 5.211   1.00 164.85 ? 248 PHE   A CG  1 
ATOM   1589 C  CD1 . PHE   A 1 228 ? -6.859  -19.506 5.982   1.00 176.50 ? 248 PHE   A CD1 1 
ATOM   1590 C  CD2 . PHE   A 1 228 ? -7.755  -20.592 4.065   1.00 155.18 ? 248 PHE   A CD2 1 
ATOM   1591 C  CE1 . PHE   A 1 228 ? -7.490  -18.330 5.610   1.00 174.34 ? 248 PHE   A CE1 1 
ATOM   1592 C  CE2 . PHE   A 1 228 ? -8.388  -19.417 3.696   1.00 155.66 ? 248 PHE   A CE2 1 
ATOM   1593 C  CZ  . PHE   A 1 228 ? -8.257  -18.290 4.471   1.00 163.07 ? 248 PHE   A CZ  1 
ATOM   1594 N  N   . LEU   A 1 229 ? -8.990  -22.516 6.131   1.00 157.40 ? 249 LEU   A N   1 
ATOM   1595 C  CA  . LEU   A 1 229 ? -10.455 -22.282 6.147   1.00 140.56 ? 249 LEU   A CA  1 
ATOM   1596 C  C   . LEU   A 1 229 ? -11.029 -22.938 7.394   1.00 153.68 ? 249 LEU   A C   1 
ATOM   1597 O  O   . LEU   A 1 229 ? -12.229 -22.755 7.653   1.00 157.34 ? 249 LEU   A O   1 
ATOM   1598 C  CB  . LEU   A 1 229 ? -11.078 -22.923 4.906   1.00 108.66 ? 249 LEU   A CB  1 
ATOM   1599 C  CG  . LEU   A 1 229 ? -10.357 -22.671 3.585   1.00 106.22 ? 249 LEU   A CG  1 
ATOM   1600 C  CD1 . LEU   A 1 229 ? -10.304 -23.940 2.750   1.00 86.08  ? 249 LEU   A CD1 1 
ATOM   1601 C  CD2 . LEU   A 1 229 ? -11.040 -21.559 2.805   1.00 124.16 ? 249 LEU   A CD2 1 
ATOM   1602 N  N   . ARG   A 1 230 ? -10.207 -23.687 8.129   1.00 166.39 ? 250 ARG   A N   1 
ATOM   1603 C  CA  . ARG   A 1 230 ? -10.689 -24.228 9.422   1.00 181.18 ? 250 ARG   A CA  1 
ATOM   1604 C  C   . ARG   A 1 230 ? -10.474 -22.985 10.287  1.00 202.69 ? 250 ARG   A C   1 
ATOM   1605 O  O   . ARG   A 1 230 ? -9.881  -23.118 11.372  1.00 195.03 ? 250 ARG   A O   1 
ATOM   1606 C  CB  . ARG   A 1 230 ? -9.723  -25.296 9.936   1.00 178.83 ? 250 ARG   A CB  1 
ATOM   1607 C  CG  . ARG   A 1 230 ? -10.372 -26.647 10.197  1.00 174.38 ? 250 ARG   A CG  1 
ATOM   1608 C  CD  . ARG   A 1 230 ? -10.198 -27.592 9.025   1.00 179.47 ? 250 ARG   A CD  1 
ATOM   1609 N  NE  . ARG   A 1 230 ? -8.805  -27.948 8.807   1.00 191.80 ? 250 ARG   A NE  1 
ATOM   1610 C  CZ  . ARG   A 1 230 ? -8.396  -29.121 8.341   1.00 197.72 ? 250 ARG   A CZ  1 
ATOM   1611 N  NH1 . ARG   A 1 230 ? -9.281  -30.058 8.046   1.00 197.18 ? 250 ARG   A NH1 1 
ATOM   1612 N  NH2 . ARG   A 1 230 ? -7.109  -29.357 8.169   1.00 198.71 ? 250 ARG   A NH2 1 
ATOM   1613 N  N   . LYS   A 1 231 ? -10.952 -21.826 9.826   1.00 223.13 ? 251 LYS   A N   1 
ATOM   1614 C  CA  . LYS   A 1 231 ? -10.896 -20.568 10.611  1.00 227.50 ? 251 LYS   A CA  1 
ATOM   1615 C  C   . LYS   A 1 231 ? -12.201 -20.442 11.402  1.00 215.76 ? 251 LYS   A C   1 
ATOM   1616 O  O   . LYS   A 1 231 ? -12.350 -19.428 12.109  1.00 223.30 ? 251 LYS   A O   1 
ATOM   1617 C  CB  . LYS   A 1 231 ? -10.734 -19.378 9.663   1.00 236.85 ? 251 LYS   A CB  1 
ATOM   1618 C  CG  . LYS   A 1 231 ? -10.756 -18.006 10.323  1.00 236.79 ? 251 LYS   A CG  1 
ATOM   1619 C  CD  . LYS   A 1 231 ? -9.634  -17.791 11.311  1.00 238.73 ? 251 LYS   A CD  1 
ATOM   1620 C  CE  . LYS   A 1 231 ? -9.569  -16.371 11.830  1.00 232.87 ? 251 LYS   A CE  1 
ATOM   1621 N  NZ  . LYS   A 1 231 ? -8.606  -16.239 12.948  1.00 225.23 ? 251 LYS   A NZ  1 
ATOM   1622 N  N   . SER   A 1 232 ? -13.102 -21.422 11.293  1.00 201.87 ? 252 SER   A N   1 
ATOM   1623 C  CA  . SER   A 1 232 ? -14.350 -21.381 12.095  1.00 191.12 ? 252 SER   A CA  1 
ATOM   1624 C  C   . SER   A 1 232 ? -14.805 -19.926 12.196  1.00 193.95 ? 252 SER   A C   1 
ATOM   1625 O  O   . SER   A 1 232 ? -15.040 -19.455 13.323  1.00 199.28 ? 252 SER   A O   1 
ATOM   1626 C  CB  . SER   A 1 232 ? -14.122 -21.974 13.455  1.00 177.05 ? 252 SER   A CB  1 
ATOM   1627 O  OG  . SER   A 1 232 ? -13.186 -21.202 14.191  1.00 176.34 ? 252 SER   A OG  1 
ATOM   1628 N  N   . VAL   A 1 233 ? -14.918 -19.241 11.057  1.00 190.18 ? 253 VAL   A N   1 
ATOM   1629 C  CA  . VAL   A 1 233 ? -15.260 -17.786 11.068  1.00 185.10 ? 253 VAL   A CA  1 
ATOM   1630 C  C   . VAL   A 1 233 ? -16.637 -17.574 11.706  1.00 192.18 ? 253 VAL   A C   1 
ATOM   1631 O  O   . VAL   A 1 233 ? -17.016 -16.406 11.900  1.00 194.08 ? 253 VAL   A O   1 
ATOM   1632 C  CB  . VAL   A 1 233 ? -15.138 -17.187 9.655   1.00 173.00 ? 253 VAL   A CB  1 
ATOM   1633 C  CG1 . VAL   A 1 233 ? -13.847 -17.623 8.980   1.00 174.90 ? 253 VAL   A CG1 1 
ATOM   1634 C  CG2 . VAL   A 1 233 ? -16.337 -17.539 8.788   1.00 155.90 ? 253 VAL   A CG2 1 
ATOM   1635 N  N   . LYS   A 1 234 ? -17.353 -18.653 12.022  1.00 193.50 ? 254 LYS   A N   1 
ATOM   1636 C  CA  . LYS   A 1 234 ? -18.655 -18.515 12.721  1.00 194.01 ? 254 LYS   A CA  1 
ATOM   1637 C  C   . LYS   A 1 234 ? -18.515 -17.516 13.871  1.00 205.46 ? 254 LYS   A C   1 
ATOM   1638 O  O   . LYS   A 1 234 ? -17.466 -17.538 14.540  1.00 209.36 ? 254 LYS   A O   1 
ATOM   1639 C  CB  . LYS   A 1 234 ? -19.147 -19.876 13.222  1.00 183.69 ? 254 LYS   A CB  1 
ATOM   1640 C  CG  . LYS   A 1 234 ? -19.501 -20.880 12.132  1.00 176.59 ? 254 LYS   A CG  1 
ATOM   1641 C  CD  . LYS   A 1 234 ? -20.181 -22.122 12.664  1.00 172.70 ? 254 LYS   A CD  1 
ATOM   1642 C  CE  . LYS   A 1 234 ? -19.263 -22.983 13.505  1.00 163.51 ? 254 LYS   A CE  1 
ATOM   1643 N  NZ  . LYS   A 1 234 ? -19.916 -24.249 13.913  1.00 162.18 ? 254 LYS   A NZ  1 
ATOM   1644 N  N   . ARG   A 1 235 ? -19.529 -16.679 14.095  1.00 215.91 ? 255 ARG   A N   1 
ATOM   1645 C  CA  . ARG   A 1 235 ? -19.404 -15.627 15.135  1.00 233.84 ? 255 ARG   A CA  1 
ATOM   1646 C  C   . ARG   A 1 235 ? -20.333 -15.927 16.314  1.00 238.33 ? 255 ARG   A C   1 
ATOM   1647 O  O   . ARG   A 1 235 ? -20.838 -17.063 16.395  1.00 246.22 ? 255 ARG   A O   1 
ATOM   1648 C  CB  . ARG   A 1 235 ? -19.717 -14.255 14.533  1.00 240.53 ? 255 ARG   A CB  1 
ATOM   1649 C  CG  . ARG   A 1 235 ? -18.692 -13.793 13.509  1.00 247.73 ? 255 ARG   A CG  1 
ATOM   1650 C  CD  . ARG   A 1 235 ? -19.019 -12.410 12.979  1.00 248.22 ? 255 ARG   A CD  1 
ATOM   1651 N  NE  . ARG   A 1 235 ? -18.098 -11.963 11.944  1.00 246.87 ? 255 ARG   A NE  1 
ATOM   1652 C  CZ  . ARG   A 1 235 ? -18.238 -10.843 11.246  1.00 242.90 ? 255 ARG   A CZ  1 
ATOM   1653 N  NH1 . ARG   A 1 235 ? -19.272 -10.049 11.465  1.00 239.97 ? 255 ARG   A NH1 1 
ATOM   1654 N  NH2 . ARG   A 1 235 ? -17.346 -10.521 10.327  1.00 241.41 ? 255 ARG   A NH2 1 
ATOM   1655 N  N   . MET   A 1 236 ? -20.537 -14.939 17.191  1.00 231.05 ? 256 MET   A N   1 
ATOM   1656 C  CA  . MET   A 1 236 ? -21.410 -15.116 18.381  1.00 224.60 ? 256 MET   A CA  1 
ATOM   1657 C  C   . MET   A 1 236 ? -22.850 -15.344 17.920  1.00 213.65 ? 256 MET   A C   1 
ATOM   1658 O  O   . MET   A 1 236 ? -23.172 -14.964 16.779  1.00 209.30 ? 256 MET   A O   1 
ATOM   1659 C  CB  . MET   A 1 236 ? -21.355 -13.872 19.271  1.00 227.60 ? 256 MET   A CB  1 
ATOM   1660 C  CG  . MET   A 1 236 ? -20.622 -14.097 20.578  1.00 234.02 ? 256 MET   A CG  1 
ATOM   1661 S  SD  . MET   A 1 236 ? -18.823 -13.988 20.406  1.00 234.50 ? 256 MET   A SD  1 
ATOM   1662 C  CE  . MET   A 1 236 ? -18.386 -15.725 20.383  1.00 236.58 ? 256 MET   A CE  1 
ATOM   1663 N  N   . ASP   A 1 250 ? -27.959 -15.995 5.792   1.00 192.17 ? 270 ASP   A N   1 
ATOM   1664 C  CA  . ASP   A 1 250 ? -26.850 -16.519 5.007   1.00 184.11 ? 270 ASP   A CA  1 
ATOM   1665 C  C   . ASP   A 1 250 ? -26.778 -18.046 5.026   1.00 179.59 ? 270 ASP   A C   1 
ATOM   1666 O  O   . ASP   A 1 250 ? -27.428 -18.715 5.830   1.00 182.11 ? 270 ASP   A O   1 
ATOM   1667 C  CB  . ASP   A 1 250 ? -25.518 -15.940 5.504   1.00 179.59 ? 270 ASP   A CB  1 
ATOM   1668 C  CG  . ASP   A 1 250 ? -25.210 -14.574 4.911   1.00 184.44 ? 270 ASP   A CG  1 
ATOM   1669 O  OD1 . ASP   A 1 250 ? -25.812 -14.218 3.876   1.00 184.91 ? 270 ASP   A OD1 1 
ATOM   1670 O  OD2 . ASP   A 1 250 ? -24.355 -13.858 5.477   1.00 187.28 ? 270 ASP   A OD2 1 
ATOM   1671 N  N   . PHE   A 1 251 ? -25.988 -18.560 4.080   1.00 175.37 ? 271 PHE   A N   1 
ATOM   1672 C  CA  . PHE   A 1 251 ? -25.573 -19.960 4.054   1.00 169.74 ? 271 PHE   A CA  1 
ATOM   1673 C  C   . PHE   A 1 251 ? -25.014 -20.392 5.409   1.00 172.21 ? 271 PHE   A C   1 
ATOM   1674 O  O   . PHE   A 1 251 ? -25.434 -21.412 5.965   1.00 173.24 ? 271 PHE   A O   1 
ATOM   1675 C  CB  . PHE   A 1 251 ? -24.564 -20.105 2.909   1.00 170.10 ? 271 PHE   A CB  1 
ATOM   1676 C  CG  . PHE   A 1 251 ? -23.776 -21.378 2.880   1.00 156.96 ? 271 PHE   A CG  1 
ATOM   1677 C  CD1 . PHE   A 1 251 ? -24.284 -22.508 2.269   1.00 153.94 ? 271 PHE   A CD1 1 
ATOM   1678 C  CD2 . PHE   A 1 251 ? -22.477 -21.414 3.388   1.00 156.77 ? 271 PHE   A CD2 1 
ATOM   1679 C  CE1 . PHE   A 1 251 ? -23.537 -23.665 2.212   1.00 147.73 ? 271 PHE   A CE1 1 
ATOM   1680 C  CE2 . PHE   A 1 251 ? -21.727 -22.576 3.340   1.00 150.34 ? 271 PHE   A CE2 1 
ATOM   1681 C  CZ  . PHE   A 1 251 ? -22.254 -23.696 2.732   1.00 146.57 ? 271 PHE   A CZ  1 
ATOM   1682 N  N   . LEU   A 1 252 ? -24.100 -19.592 5.980   1.00 189.03 ? 272 LEU   A N   1 
ATOM   1683 C  CA  . LEU   A 1 252 ? -23.656 -19.801 7.362   1.00 175.40 ? 272 LEU   A CA  1 
ATOM   1684 C  C   . LEU   A 1 252 ? -24.829 -19.822 8.335   1.00 177.43 ? 272 LEU   A C   1 
ATOM   1685 O  O   . LEU   A 1 252 ? -24.877 -20.649 9.255   1.00 176.92 ? 272 LEU   A O   1 
ATOM   1686 C  CB  . LEU   A 1 252 ? -22.686 -18.695 7.785   1.00 160.13 ? 272 LEU   A CB  1 
ATOM   1687 C  CG  . LEU   A 1 252 ? -22.180 -18.726 9.232   1.00 149.71 ? 272 LEU   A CG  1 
ATOM   1688 C  CD1 . LEU   A 1 252 ? -21.359 -19.989 9.539   1.00 156.22 ? 272 LEU   A CD1 1 
ATOM   1689 C  CD2 . LEU   A 1 252 ? -21.462 -17.444 9.633   1.00 168.62 ? 272 LEU   A CD2 1 
ATOM   1690 N  N   . GLN   A 1 253 ? -25.772 -18.897 8.161   1.00 187.72 ? 273 GLN   A N   1 
ATOM   1691 C  CA  . GLN   A 1 253 ? -26.937 -18.796 9.030   1.00 195.70 ? 273 GLN   A CA  1 
ATOM   1692 C  C   . GLN   A 1 253 ? -27.765 -20.072 8.967   1.00 196.11 ? 273 GLN   A C   1 
ATOM   1693 O  O   . GLN   A 1 253 ? -27.813 -20.830 9.941   1.00 194.44 ? 273 GLN   A O   1 
ATOM   1694 C  CB  . GLN   A 1 253 ? -27.786 -17.584 8.637   1.00 197.03 ? 273 GLN   A CB  1 
ATOM   1695 C  CG  . GLN   A 1 253 ? -28.808 -17.151 9.669   1.00 205.39 ? 273 GLN   A CG  1 
ATOM   1696 C  CD  . GLN   A 1 253 ? -28.319 -16.016 10.543  1.00 219.05 ? 273 GLN   A CD  1 
ATOM   1697 O  OE1 . GLN   A 1 253 ? -28.594 -14.848 10.269  1.00 225.44 ? 273 GLN   A OE1 1 
ATOM   1698 N  NE2 . GLN   A 1 253 ? -27.599 -16.353 11.606  1.00 217.82 ? 273 GLN   A NE2 1 
ATOM   1699 N  N   . LEU   A 1 254 ? -28.375 -20.342 7.810   1.00 188.65 ? 274 LEU   A N   1 
ATOM   1700 C  CA  . LEU   A 1 254 ? -29.343 -21.424 7.642   1.00 189.66 ? 274 LEU   A CA  1 
ATOM   1701 C  C   . LEU   A 1 254 ? -28.821 -22.796 8.061   1.00 187.36 ? 274 LEU   A C   1 
ATOM   1702 O  O   . LEU   A 1 254 ? -29.600 -23.749 8.154   1.00 183.08 ? 274 LEU   A O   1 
ATOM   1703 C  CB  . LEU   A 1 254 ? -29.864 -21.442 6.202   1.00 180.75 ? 274 LEU   A CB  1 
ATOM   1704 C  CG  . LEU   A 1 254 ? -30.220 -20.080 5.604   1.00 185.09 ? 274 LEU   A CG  1 
ATOM   1705 C  CD1 . LEU   A 1 254 ? -30.498 -20.196 4.112   1.00 156.96 ? 274 LEU   A CD1 1 
ATOM   1706 C  CD2 . LEU   A 1 254 ? -31.399 -19.461 6.335   1.00 184.73 ? 274 LEU   A CD2 1 
ATOM   1707 N  N   . MET   A 1 255 ? -27.518 -22.917 8.308   1.00 182.72 ? 275 MET   A N   1 
ATOM   1708 C  CA  . MET   A 1 255 ? -26.940 -24.127 8.891   1.00 179.44 ? 275 MET   A CA  1 
ATOM   1709 C  C   . MET   A 1 255 ? -27.125 -24.317 10.388  1.00 189.67 ? 275 MET   A C   1 
ATOM   1710 O  O   . MET   A 1 255 ? -27.646 -25.345 10.831  1.00 195.76 ? 275 MET   A O   1 
ATOM   1711 C  CB  . MET   A 1 255 ? -25.455 -24.191 8.566   1.00 170.24 ? 275 MET   A CB  1 
ATOM   1712 C  CG  . MET   A 1 255 ? -25.263 -24.826 7.252   1.00 167.80 ? 275 MET   A CG  1 
ATOM   1713 S  SD  . MET   A 1 255 ? -23.558 -24.881 6.771   1.00 164.02 ? 275 MET   A SD  1 
ATOM   1714 C  CE  . MET   A 1 255 ? -23.782 -25.306 5.041   1.00 135.99 ? 275 MET   A CE  1 
ATOM   1715 N  N   . ILE   A 1 256 ? -26.613 -23.379 11.179  1.00 192.04 ? 276 ILE   A N   1 
ATOM   1716 C  CA  . ILE   A 1 256 ? -26.749 -23.500 12.614  1.00 193.87 ? 276 ILE   A CA  1 
ATOM   1717 C  C   . ILE   A 1 256 ? -28.206 -23.365 13.026  1.00 205.77 ? 276 ILE   A C   1 
ATOM   1718 O  O   . ILE   A 1 256 ? -28.599 -23.872 14.083  1.00 206.27 ? 276 ILE   A O   1 
ATOM   1719 C  CB  . ILE   A 1 256 ? -25.855 -22.460 13.309  1.00 184.72 ? 276 ILE   A CB  1 
ATOM   1720 C  CG1 . ILE   A 1 256 ? -24.635 -22.150 12.433  1.00 173.04 ? 276 ILE   A CG1 1 
ATOM   1721 C  CG2 . ILE   A 1 256 ? -25.404 -22.978 14.654  1.00 169.41 ? 276 ILE   A CG2 1 
ATOM   1722 C  CD1 . ILE   A 1 256 ? -23.806 -20.986 12.935  1.00 150.43 ? 276 ILE   A CD1 1 
ATOM   1723 N  N   . ASP   A 1 257 ? -29.028 -22.707 12.202  1.00 219.38 ? 277 ASP   A N   1 
ATOM   1724 C  CA  . ASP   A 1 257 ? -30.449 -22.581 12.511  1.00 227.27 ? 277 ASP   A CA  1 
ATOM   1725 C  C   . ASP   A 1 257 ? -31.148 -23.931 12.431  1.00 225.47 ? 277 ASP   A C   1 
ATOM   1726 O  O   . ASP   A 1 257 ? -31.917 -24.296 13.327  1.00 223.24 ? 277 ASP   A O   1 
ATOM   1727 C  CB  . ASP   A 1 257 ? -31.108 -21.581 11.563  1.00 234.57 ? 277 ASP   A CB  1 
ATOM   1728 C  CG  . ASP   A 1 257 ? -30.287 -20.329 11.376  1.00 239.68 ? 277 ASP   A CG  1 
ATOM   1729 O  OD1 . ASP   A 1 257 ? -29.333 -20.118 12.153  1.00 242.24 ? 277 ASP   A OD1 1 
ATOM   1730 O  OD2 . ASP   A 1 257 ? -30.589 -19.561 10.439  1.00 240.24 ? 277 ASP   A OD2 1 
ATOM   1731 N  N   . ALA   A 1 269 ? -29.561 -33.993 12.738  1.00 189.55 ? 289 ALA   A N   1 
ATOM   1732 C  CA  . ALA   A 1 269 ? -29.404 -32.610 12.306  1.00 188.26 ? 289 ALA   A CA  1 
ATOM   1733 C  C   . ALA   A 1 269 ? -27.977 -32.394 11.815  1.00 184.33 ? 289 ALA   A C   1 
ATOM   1734 O  O   . ALA   A 1 269 ? -27.335 -33.339 11.349  1.00 179.15 ? 289 ALA   A O   1 
ATOM   1735 C  CB  . ALA   A 1 269 ? -29.748 -31.640 13.437  1.00 190.36 ? 289 ALA   A CB  1 
ATOM   1736 N  N   . LEU   A 1 270 ? -27.461 -31.174 11.928  1.00 200.34 ? 290 LEU   A N   1 
ATOM   1737 C  CA  . LEU   A 1 270 ? -26.171 -30.827 11.352  1.00 198.15 ? 290 LEU   A CA  1 
ATOM   1738 C  C   . LEU   A 1 270 ? -25.097 -30.730 12.430  1.00 198.10 ? 290 LEU   A C   1 
ATOM   1739 O  O   . LEU   A 1 270 ? -25.366 -30.338 13.569  1.00 207.30 ? 290 LEU   A O   1 
ATOM   1740 C  CB  . LEU   A 1 270 ? -26.255 -29.506 10.585  1.00 196.52 ? 290 LEU   A CB  1 
ATOM   1741 C  CG  . LEU   A 1 270 ? -24.964 -28.967 9.972   1.00 197.87 ? 290 LEU   A CG  1 
ATOM   1742 C  CD1 . LEU   A 1 270 ? -24.478 -29.887 8.867   1.00 190.17 ? 290 LEU   A CD1 1 
ATOM   1743 C  CD2 . LEU   A 1 270 ? -25.187 -27.578 9.440   1.00 206.12 ? 290 LEU   A CD2 1 
ATOM   1744 N  N   . SER   A 1 271 ? -23.873 -31.087 12.050  1.00 172.31 ? 291 SER   A N   1 
ATOM   1745 C  CA  . SER   A 1 271 ? -22.704 -31.041 12.911  1.00 163.80 ? 291 SER   A CA  1 
ATOM   1746 C  C   . SER   A 1 271 ? -21.932 -29.738 12.669  1.00 158.64 ? 291 SER   A C   1 
ATOM   1747 O  O   . SER   A 1 271 ? -22.459 -28.788 12.080  1.00 159.31 ? 291 SER   A O   1 
ATOM   1748 C  CB  . SER   A 1 271 ? -21.852 -32.292 12.663  1.00 158.59 ? 291 SER   A CB  1 
ATOM   1749 O  OG  . SER   A 1 271 ? -20.499 -32.071 13.018  1.00 153.73 ? 291 SER   A OG  1 
ATOM   1750 N  N   . ASP   A 1 272 ? -20.676 -29.690 13.117  1.00 145.72 ? 292 ASP   A N   1 
ATOM   1751 C  CA  . ASP   A 1 272 ? -19.842 -28.497 13.016  1.00 142.78 ? 292 ASP   A CA  1 
ATOM   1752 C  C   . ASP   A 1 272 ? -18.668 -28.691 12.066  1.00 133.31 ? 292 ASP   A C   1 
ATOM   1753 O  O   . ASP   A 1 272 ? -18.461 -27.883 11.157  1.00 127.68 ? 292 ASP   A O   1 
ATOM   1754 C  CB  . ASP   A 1 272 ? -19.326 -28.096 14.404  1.00 145.59 ? 292 ASP   A CB  1 
ATOM   1755 C  CG  . ASP   A 1 272 ? -20.322 -27.265 15.179  1.00 163.89 ? 292 ASP   A CG  1 
ATOM   1756 O  OD1 . ASP   A 1 272 ? -21.432 -27.024 14.661  1.00 161.87 ? 292 ASP   A OD1 1 
ATOM   1757 O  OD2 . ASP   A 1 272 ? -19.991 -26.850 16.310  1.00 171.50 ? 292 ASP   A OD2 1 
ATOM   1758 N  N   . LEU   A 1 273 ? -17.864 -29.733 12.278  1.00 133.61 ? 293 LEU   A N   1 
ATOM   1759 C  CA  . LEU   A 1 273 ? -16.756 -30.012 11.371  1.00 136.58 ? 293 LEU   A CA  1 
ATOM   1760 C  C   . LEU   A 1 273 ? -17.254 -30.289 9.959   1.00 133.18 ? 293 LEU   A C   1 
ATOM   1761 O  O   . LEU   A 1 273 ? -16.584 -29.943 8.978   1.00 130.28 ? 293 LEU   A O   1 
ATOM   1762 C  CB  . LEU   A 1 273 ? -15.925 -31.168 11.936  1.00 139.81 ? 293 LEU   A CB  1 
ATOM   1763 C  CG  . LEU   A 1 273 ? -14.748 -31.847 11.230  1.00 132.09 ? 293 LEU   A CG  1 
ATOM   1764 C  CD1 . LEU   A 1 273 ? -15.224 -32.722 10.091  1.00 131.41 ? 293 LEU   A CD1 1 
ATOM   1765 C  CD2 . LEU   A 1 273 ? -13.753 -30.810 10.726  1.00 138.64 ? 293 LEU   A CD2 1 
ATOM   1766 N  N   . GLU   A 1 274 ? -18.431 -30.902 9.838   1.00 131.57 ? 294 GLU   A N   1 
ATOM   1767 C  CA  . GLU   A 1 274 ? -19.048 -31.080 8.532   1.00 125.34 ? 294 GLU   A CA  1 
ATOM   1768 C  C   . GLU   A 1 274 ? -19.595 -29.766 7.985   1.00 125.90 ? 294 GLU   A C   1 
ATOM   1769 O  O   . GLU   A 1 274 ? -19.745 -29.629 6.765   1.00 114.48 ? 294 GLU   A O   1 
ATOM   1770 C  CB  . GLU   A 1 274 ? -20.158 -32.131 8.626   1.00 133.03 ? 294 GLU   A CB  1 
ATOM   1771 C  CG  . GLU   A 1 274 ? -19.670 -33.485 9.140   1.00 144.13 ? 294 GLU   A CG  1 
ATOM   1772 C  CD  . GLU   A 1 274 ? -20.757 -34.545 9.142   1.00 148.94 ? 294 GLU   A CD  1 
ATOM   1773 O  OE1 . GLU   A 1 274 ? -21.799 -34.319 9.791   1.00 128.69 ? 294 GLU   A OE1 1 
ATOM   1774 O  OE2 . GLU   A 1 274 ? -20.563 -35.615 8.531   1.00 144.41 ? 294 GLU   A OE2 1 
ATOM   1775 N  N   . LEU   A 1 275 ? -19.893 -28.798 8.860   1.00 131.11 ? 295 LEU   A N   1 
ATOM   1776 C  CA  . LEU   A 1 275 ? -20.224 -27.451 8.402   1.00 134.50 ? 295 LEU   A CA  1 
ATOM   1777 C  C   . LEU   A 1 275 ? -19.043 -26.810 7.689   1.00 127.34 ? 295 LEU   A C   1 
ATOM   1778 O  O   . LEU   A 1 275 ? -19.219 -26.112 6.683   1.00 116.71 ? 295 LEU   A O   1 
ATOM   1779 C  CB  . LEU   A 1 275 ? -20.669 -26.583 9.581   1.00 132.75 ? 295 LEU   A CB  1 
ATOM   1780 C  CG  . LEU   A 1 275 ? -21.375 -25.258 9.292   1.00 131.07 ? 295 LEU   A CG  1 
ATOM   1781 C  CD1 . LEU   A 1 275 ? -22.383 -24.938 10.382  1.00 142.54 ? 295 LEU   A CD1 1 
ATOM   1782 C  CD2 . LEU   A 1 275 ? -20.381 -24.113 9.134   1.00 128.29 ? 295 LEU   A CD2 1 
ATOM   1783 N  N   . VAL   A 1 276 ? -17.832 -27.016 8.212   1.00 123.16 ? 296 VAL   A N   1 
ATOM   1784 C  CA  . VAL   A 1 276 ? -16.633 -26.590 7.498   1.00 126.30 ? 296 VAL   A CA  1 
ATOM   1785 C  C   . VAL   A 1 276 ? -16.626 -27.182 6.094   1.00 129.13 ? 296 VAL   A C   1 
ATOM   1786 O  O   . VAL   A 1 276 ? -16.529 -26.458 5.095   1.00 123.28 ? 296 VAL   A O   1 
ATOM   1787 C  CB  . VAL   A 1 276 ? -15.371 -26.990 8.284   1.00 126.29 ? 296 VAL   A CB  1 
ATOM   1788 C  CG1 . VAL   A 1 276 ? -14.124 -26.801 7.430   1.00 132.37 ? 296 VAL   A CG1 1 
ATOM   1789 C  CG2 . VAL   A 1 276 ? -15.275 -26.212 9.592   1.00 147.06 ? 296 VAL   A CG2 1 
ATOM   1790 N  N   . ALA   A 1 277 ? -16.783 -28.508 6.005   1.00 119.71 ? 297 ALA   A N   1 
ATOM   1791 C  CA  . ALA   A 1 277 ? -16.709 -29.205 4.724   1.00 112.51 ? 297 ALA   A CA  1 
ATOM   1792 C  C   . ALA   A 1 277 ? -17.643 -28.587 3.688   1.00 107.39 ? 297 ALA   A C   1 
ATOM   1793 O  O   . ALA   A 1 277 ? -17.236 -28.326 2.549   1.00 110.73 ? 297 ALA   A O   1 
ATOM   1794 C  CB  . ALA   A 1 277 ? -17.029 -30.686 4.922   1.00 116.37 ? 297 ALA   A CB  1 
ATOM   1795 N  N   . GLN   A 1 278 ? -18.902 -28.344 4.066   1.00 106.67 ? 298 GLN   A N   1 
ATOM   1796 C  CA  . GLN   A 1 278 ? -19.846 -27.740 3.128   1.00 104.99 ? 298 GLN   A CA  1 
ATOM   1797 C  C   . GLN   A 1 278 ? -19.371 -26.369 2.670   1.00 114.98 ? 298 GLN   A C   1 
ATOM   1798 O  O   . GLN   A 1 278 ? -19.501 -26.021 1.491   1.00 113.22 ? 298 GLN   A O   1 
ATOM   1799 C  CB  . GLN   A 1 278 ? -21.234 -27.628 3.761   1.00 99.14  ? 298 GLN   A CB  1 
ATOM   1800 C  CG  . GLN   A 1 278 ? -21.749 -28.893 4.417   1.00 109.25 ? 298 GLN   A CG  1 
ATOM   1801 C  CD  . GLN   A 1 278 ? -21.517 -30.129 3.576   1.00 104.80 ? 298 GLN   A CD  1 
ATOM   1802 O  OE1 . GLN   A 1 278 ? -21.862 -30.165 2.395   1.00 106.07 ? 298 GLN   A OE1 1 
ATOM   1803 N  NE2 . GLN   A 1 278 ? -20.931 -31.153 4.182   1.00 110.10 ? 298 GLN   A NE2 1 
ATOM   1804 N  N   . SER   A 1 279 ? -18.816 -25.577 3.592   1.00 111.48 ? 299 SER   A N   1 
ATOM   1805 C  CA  . SER   A 1 279 ? -18.356 -24.235 3.249   1.00 110.55 ? 299 SER   A CA  1 
ATOM   1806 C  C   . SER   A 1 279 ? -17.295 -24.268 2.153   1.00 112.88 ? 299 SER   A C   1 
ATOM   1807 O  O   . SER   A 1 279 ? -17.321 -23.440 1.234   1.00 104.95 ? 299 SER   A O   1 
ATOM   1808 C  CB  . SER   A 1 279 ? -17.815 -23.536 4.497   1.00 115.86 ? 299 SER   A CB  1 
ATOM   1809 O  OG  . SER   A 1 279 ? -18.800 -23.465 5.514   1.00 115.37 ? 299 SER   A OG  1 
ATOM   1810 N  N   . ILE   A 1 280 ? -16.355 -25.216 2.232   1.00 105.65 ? 300 ILE   A N   1 
ATOM   1811 C  CA  . ILE   A 1 280 ? -15.319 -25.331 1.203   1.00 105.24 ? 300 ILE   A CA  1 
ATOM   1812 C  C   . ILE   A 1 280 ? -15.941 -25.571 -0.172  1.00 104.27 ? 300 ILE   A C   1 
ATOM   1813 O  O   . ILE   A 1 280 ? -15.550 -24.943 -1.163  1.00 101.93 ? 300 ILE   A O   1 
ATOM   1814 C  CB  . ILE   A 1 280 ? -14.297 -26.431 1.561   1.00 99.23  ? 300 ILE   A CB  1 
ATOM   1815 C  CG1 . ILE   A 1 280 ? -13.456 -26.110 2.818   1.00 124.96 ? 300 ILE   A CG1 1 
ATOM   1816 C  CG2 . ILE   A 1 280 ? -13.364 -26.691 0.389   1.00 102.28 ? 300 ILE   A CG2 1 
ATOM   1817 C  CD1 . ILE   A 1 280 ? -12.607 -27.201 3.417   1.00 124.94 ? 300 ILE   A CD1 1 
ATOM   1818 N  N   . ILE   A 1 281 ? -16.923 -26.475 -0.251  1.00 92.57  ? 301 ILE   A N   1 
ATOM   1819 C  CA  . ILE   A 1 281 ? -17.572 -26.765 -1.531  1.00 105.01 ? 301 ILE   A CA  1 
ATOM   1820 C  C   . ILE   A 1 281 ? -18.181 -25.499 -2.122  1.00 104.16 ? 301 ILE   A C   1 
ATOM   1821 O  O   . ILE   A 1 281 ? -18.014 -25.203 -3.312  1.00 95.30  ? 301 ILE   A O   1 
ATOM   1822 C  CB  . ILE   A 1 281 ? -18.632 -27.867 -1.356  1.00 109.17 ? 301 ILE   A CB  1 
ATOM   1823 C  CG1 . ILE   A 1 281 ? -17.983 -29.145 -0.829  1.00 113.08 ? 301 ILE   A CG1 1 
ATOM   1824 C  CG2 . ILE   A 1 281 ? -19.375 -28.123 -2.663  1.00 97.48  ? 301 ILE   A CG2 1 
ATOM   1825 C  CD1 . ILE   A 1 281 ? -17.268 -29.950 -1.886  1.00 106.89 ? 301 ILE   A CD1 1 
ATOM   1826 N  N   . PHE   A 1 282 ? -18.893 -24.729 -1.296  1.00 101.90 ? 302 PHE   A N   1 
ATOM   1827 C  CA  . PHE   A 1 282 ? -19.561 -23.532 -1.795  1.00 102.23 ? 302 PHE   A CA  1 
ATOM   1828 C  C   . PHE   A 1 282 ? -18.554 -22.456 -2.184  1.00 104.12 ? 302 PHE   A C   1 
ATOM   1829 O  O   . PHE   A 1 282 ? -18.663 -21.854 -3.259  1.00 99.92  ? 302 PHE   A O   1 
ATOM   1830 C  CB  . PHE   A 1 282 ? -20.546 -22.998 -0.754  1.00 109.65 ? 302 PHE   A CB  1 
ATOM   1831 C  CG  . PHE   A 1 282 ? -21.855 -23.733 -0.728  1.00 120.59 ? 302 PHE   A CG  1 
ATOM   1832 C  CD1 . PHE   A 1 282 ? -21.899 -25.101 -0.515  1.00 115.09 ? 302 PHE   A CD1 1 
ATOM   1833 C  CD2 . PHE   A 1 282 ? -23.043 -23.057 -0.962  1.00 127.47 ? 302 PHE   A CD2 1 
ATOM   1834 C  CE1 . PHE   A 1 282 ? -23.103 -25.778 -0.503  1.00 114.57 ? 302 PHE   A CE1 1 
ATOM   1835 C  CE2 . PHE   A 1 282 ? -24.251 -23.732 -0.964  1.00 131.32 ? 302 PHE   A CE2 1 
ATOM   1836 C  CZ  . PHE   A 1 282 ? -24.281 -25.093 -0.731  1.00 123.13 ? 302 PHE   A CZ  1 
ATOM   1837 N  N   . ILE   A 1 283 ? -17.570 -22.195 -1.317  1.00 105.07 ? 303 ILE   A N   1 
ATOM   1838 C  CA  . ILE   A 1 283 ? -16.564 -21.177 -1.616  1.00 107.84 ? 303 ILE   A CA  1 
ATOM   1839 C  C   . ILE   A 1 283 ? -15.863 -21.489 -2.929  1.00 106.94 ? 303 ILE   A C   1 
ATOM   1840 O  O   . ILE   A 1 283 ? -15.651 -20.604 -3.765  1.00 115.72 ? 303 ILE   A O   1 
ATOM   1841 C  CB  . ILE   A 1 283 ? -15.558 -21.050 -0.455  1.00 101.23 ? 303 ILE   A CB  1 
ATOM   1842 C  CG1 . ILE   A 1 283 ? -16.235 -20.471 0.789   1.00 99.71  ? 303 ILE   A CG1 1 
ATOM   1843 C  CG2 . ILE   A 1 283 ? -14.376 -20.186 -0.860  1.00 103.25 ? 303 ILE   A CG2 1 
ATOM   1844 C  CD1 . ILE   A 1 283 ? -15.602 -20.916 2.093   1.00 103.02 ? 303 ILE   A CD1 1 
ATOM   1845 N  N   . PHE   A 1 284 ? -15.506 -22.756 -3.140  1.00 100.25 ? 304 PHE   A N   1 
ATOM   1846 C  CA  . PHE   A 1 284 ? -14.867 -23.154 -4.389  1.00 102.57 ? 304 PHE   A CA  1 
ATOM   1847 C  C   . PHE   A 1 284 ? -15.799 -22.942 -5.576  1.00 99.77  ? 304 PHE   A C   1 
ATOM   1848 O  O   . PHE   A 1 284 ? -15.472 -22.208 -6.516  1.00 104.95 ? 304 PHE   A O   1 
ATOM   1849 C  CB  . PHE   A 1 284 ? -14.426 -24.615 -4.314  1.00 102.38 ? 304 PHE   A CB  1 
ATOM   1850 C  CG  . PHE   A 1 284 ? -13.812 -25.124 -5.585  1.00 104.11 ? 304 PHE   A CG  1 
ATOM   1851 C  CD1 . PHE   A 1 284 ? -12.556 -24.700 -5.986  1.00 101.74 ? 304 PHE   A CD1 1 
ATOM   1852 C  CD2 . PHE   A 1 284 ? -14.508 -26.006 -6.394  1.00 99.87  ? 304 PHE   A CD2 1 
ATOM   1853 C  CE1 . PHE   A 1 284 ? -11.996 -25.167 -7.160  1.00 98.02  ? 304 PHE   A CE1 1 
ATOM   1854 C  CE2 . PHE   A 1 284 ? -13.954 -26.474 -7.568  1.00 118.92 ? 304 PHE   A CE2 1 
ATOM   1855 C  CZ  . PHE   A 1 284 ? -12.697 -26.054 -7.952  1.00 102.97 ? 304 PHE   A CZ  1 
ATOM   1856 N  N   . ALA   A 1 285 ? -16.967 -23.589 -5.550  1.00 103.62 ? 305 ALA   A N   1 
ATOM   1857 C  CA  . ALA   A 1 285 ? -17.910 -23.505 -6.661  1.00 103.54 ? 305 ALA   A CA  1 
ATOM   1858 C  C   . ALA   A 1 285 ? -18.254 -22.058 -6.986  1.00 110.60 ? 305 ALA   A C   1 
ATOM   1859 O  O   . ALA   A 1 285 ? -18.048 -21.593 -8.112  1.00 113.43 ? 305 ALA   A O   1 
ATOM   1860 C  CB  . ALA   A 1 285 ? -19.179 -24.291 -6.332  1.00 96.51  ? 305 ALA   A CB  1 
ATOM   1861 N  N   . GLY   A 1 286 ? -18.765 -21.327 -5.998  1.00 102.49 ? 306 GLY   A N   1 
ATOM   1862 C  CA  . GLY   A 1 286 ? -19.129 -19.936 -6.181  1.00 106.64 ? 306 GLY   A CA  1 
ATOM   1863 C  C   . GLY   A 1 286 ? -17.997 -19.066 -6.683  1.00 115.26 ? 306 GLY   A C   1 
ATOM   1864 O  O   . GLY   A 1 286 ? -18.233 -17.995 -7.252  1.00 112.71 ? 306 GLY   A O   1 
ATOM   1865 N  N   . TYR   A 1 287 ? -16.759 -19.516 -6.481  1.00 114.01 ? 307 TYR   A N   1 
ATOM   1866 C  CA  . TYR   A 1 287 ? -15.586 -18.803 -7.000  1.00 117.40 ? 307 TYR   A CA  1 
ATOM   1867 C  C   . TYR   A 1 287 ? -15.241 -19.278 -8.409  1.00 112.90 ? 307 TYR   A C   1 
ATOM   1868 O  O   . TYR   A 1 287 ? -15.434 -18.546 -9.384  1.00 118.46 ? 307 TYR   A O   1 
ATOM   1869 C  CB  . TYR   A 1 287 ? -14.394 -18.973 -6.052  1.00 121.84 ? 307 TYR   A CB  1 
ATOM   1870 C  CG  . TYR   A 1 287 ? -13.070 -18.516 -6.634  1.00 127.27 ? 307 TYR   A CG  1 
ATOM   1871 C  CD1 . TYR   A 1 287 ? -12.673 -17.191 -6.543  1.00 133.02 ? 307 TYR   A CD1 1 
ATOM   1872 C  CD2 . TYR   A 1 287 ? -12.204 -19.417 -7.246  1.00 127.99 ? 307 TYR   A CD2 1 
ATOM   1873 C  CE1 . TYR   A 1 287 ? -11.467 -16.769 -7.070  1.00 137.86 ? 307 TYR   A CE1 1 
ATOM   1874 C  CE2 . TYR   A 1 287 ? -10.998 -19.003 -7.778  1.00 135.60 ? 307 TYR   A CE2 1 
ATOM   1875 C  CZ  . TYR   A 1 287 ? -10.633 -17.678 -7.684  1.00 138.07 ? 307 TYR   A CZ  1 
ATOM   1876 O  OH  . TYR   A 1 287 ? -9.430  -17.260 -8.207  1.00 140.42 ? 307 TYR   A OH  1 
ATOM   1877 N  N   . GLU   A 1 288 ? -14.748 -20.513 -8.528  1.00 116.83 ? 308 GLU   A N   1 
ATOM   1878 C  CA  . GLU   A 1 288 ? -14.046 -20.911 -9.744  1.00 121.04 ? 308 GLU   A CA  1 
ATOM   1879 C  C   . GLU   A 1 288 ? -15.000 -21.082 -10.919 1.00 119.51 ? 308 GLU   A C   1 
ATOM   1880 O  O   . GLU   A 1 288 ? -14.688 -20.660 -12.038 1.00 121.75 ? 308 GLU   A O   1 
ATOM   1881 C  CB  . GLU   A 1 288 ? -13.256 -22.197 -9.500  1.00 120.84 ? 308 GLU   A CB  1 
ATOM   1882 C  CG  . GLU   A 1 288 ? -11.922 -22.234 -10.232 1.00 125.18 ? 308 GLU   A CG  1 
ATOM   1883 C  CD  . GLU   A 1 288 ? -12.067 -22.515 -11.715 1.00 132.82 ? 308 GLU   A CD  1 
ATOM   1884 O  OE1 . GLU   A 1 288 ? -13.107 -23.073 -12.122 1.00 134.82 ? 308 GLU   A OE1 1 
ATOM   1885 O  OE2 . GLU   A 1 288 ? -11.144 -22.159 -12.477 1.00 138.68 ? 308 GLU   A OE2 1 
ATOM   1886 N  N   . THR   A 1 289 ? -16.158 -21.707 -10.692 1.00 108.89 ? 309 THR   A N   1 
ATOM   1887 C  CA  . THR   A 1 289 ? -17.123 -21.880 -11.774 1.00 111.95 ? 309 THR   A CA  1 
ATOM   1888 C  C   . THR   A 1 289 ? -17.532 -20.536 -12.358 1.00 110.33 ? 309 THR   A C   1 
ATOM   1889 O  O   . THR   A 1 289 ? -17.486 -20.336 -13.577 1.00 99.98  ? 309 THR   A O   1 
ATOM   1890 C  CB  . THR   A 1 289 ? -18.353 -22.640 -11.276 1.00 102.26 ? 309 THR   A CB  1 
ATOM   1891 O  OG1 . THR   A 1 289 ? -19.197 -21.754 -10.530 1.00 99.38  ? 309 THR   A OG1 1 
ATOM   1892 C  CG2 . THR   A 1 289 ? -17.941 -23.815 -10.404 1.00 98.94  ? 309 THR   A CG2 1 
ATOM   1893 N  N   . THR   A 1 290 ? -17.926 -19.595 -11.497 1.00 99.63  ? 310 THR   A N   1 
ATOM   1894 C  CA  . THR   A 1 290 ? -18.315 -18.270 -11.966 1.00 107.56 ? 310 THR   A CA  1 
ATOM   1895 C  C   . THR   A 1 290 ? -17.191 -17.611 -12.752 1.00 113.49 ? 310 THR   A C   1 
ATOM   1896 O  O   . THR   A 1 290 ? -17.388 -17.173 -13.889 1.00 109.07 ? 310 THR   A O   1 
ATOM   1897 C  CB  . THR   A 1 290 ? -18.719 -17.389 -10.787 1.00 110.79 ? 310 THR   A CB  1 
ATOM   1898 O  OG1 . THR   A 1 290 ? -19.603 -18.112 -9.921  1.00 104.54 ? 310 THR   A OG1 1 
ATOM   1899 C  CG2 . THR   A 1 290 ? -19.400 -16.138 -11.290 1.00 115.35 ? 310 THR   A CG2 1 
ATOM   1900 N  N   . SER   A 1 291 ? -16.000 -17.533 -12.157 1.00 109.10 ? 311 SER   A N   1 
ATOM   1901 C  CA  . SER   A 1 291 ? -14.862 -16.930 -12.842 1.00 106.57 ? 311 SER   A CA  1 
ATOM   1902 C  C   . SER   A 1 291 ? -14.609 -17.598 -14.189 1.00 110.34 ? 311 SER   A C   1 
ATOM   1903 O  O   . SER   A 1 291 ? -14.461 -16.922 -15.213 1.00 114.59 ? 311 SER   A O   1 
ATOM   1904 C  CB  . SER   A 1 291 ? -13.619 -17.020 -11.956 1.00 118.37 ? 311 SER   A CB  1 
ATOM   1905 O  OG  . SER   A 1 291 ? -12.843 -18.155 -12.296 1.00 124.27 ? 311 SER   A OG  1 
ATOM   1906 N  N   . SER   A 1 292 ? -14.575 -18.932 -14.205 1.00 108.91 ? 312 SER   A N   1 
ATOM   1907 C  CA  . SER   A 1 292 ? -14.240 -19.657 -15.428 1.00 110.44 ? 312 SER   A CA  1 
ATOM   1908 C  C   . SER   A 1 292 ? -15.256 -19.386 -16.530 1.00 99.14  ? 312 SER   A C   1 
ATOM   1909 O  O   . SER   A 1 292 ? -14.886 -19.099 -17.675 1.00 103.00 ? 312 SER   A O   1 
ATOM   1910 C  CB  . SER   A 1 292 ? -14.145 -21.155 -15.140 1.00 116.70 ? 312 SER   A CB  1 
ATOM   1911 O  OG  . SER   A 1 292 ? -13.957 -21.890 -16.336 1.00 113.41 ? 312 SER   A OG  1 
ATOM   1912 N  N   . VAL   A 1 293 ? -16.547 -19.472 -16.204 1.00 94.53  ? 313 VAL   A N   1 
ATOM   1913 C  CA  . VAL   A 1 293 ? -17.578 -19.256 -17.214 1.00 100.94 ? 313 VAL   A CA  1 
ATOM   1914 C  C   . VAL   A 1 293 ? -17.590 -17.801 -17.667 1.00 95.67  ? 313 VAL   A C   1 
ATOM   1915 O  O   . VAL   A 1 293 ? -17.748 -17.512 -18.859 1.00 94.95  ? 313 VAL   A O   1 
ATOM   1916 C  CB  . VAL   A 1 293 ? -18.951 -19.695 -16.676 1.00 97.26  ? 313 VAL   A CB  1 
ATOM   1917 C  CG1 . VAL   A 1 293 ? -20.024 -19.488 -17.732 1.00 90.42  ? 313 VAL   A CG1 1 
ATOM   1918 C  CG2 . VAL   A 1 293 ? -18.906 -21.149 -16.246 1.00 88.44  ? 313 VAL   A CG2 1 
ATOM   1919 N  N   . LEU   A 1 294 ? -17.430 -16.866 -16.725 1.00 95.45  ? 314 LEU   A N   1 
ATOM   1920 C  CA  . LEU   A 1 294 ? -17.332 -15.453 -17.080 1.00 115.65 ? 314 LEU   A CA  1 
ATOM   1921 C  C   . LEU   A 1 294 ? -16.218 -15.204 -18.082 1.00 108.47 ? 314 LEU   A C   1 
ATOM   1922 O  O   . LEU   A 1 294 ? -16.342 -14.341 -18.959 1.00 99.17  ? 314 LEU   A O   1 
ATOM   1923 C  CB  . LEU   A 1 294 ? -17.119 -14.610 -15.825 1.00 111.76 ? 314 LEU   A CB  1 
ATOM   1924 C  CG  . LEU   A 1 294 ? -18.373 -13.980 -15.230 1.00 96.83  ? 314 LEU   A CG  1 
ATOM   1925 C  CD1 . LEU   A 1 294 ? -19.078 -13.184 -16.296 1.00 109.48 ? 314 LEU   A CD1 1 
ATOM   1926 C  CD2 . LEU   A 1 294 ? -19.305 -15.020 -14.659 1.00 116.95 ? 314 LEU   A CD2 1 
ATOM   1927 N  N   . SER   A 1 295 ? -15.127 -15.959 -17.971 1.00 92.12  ? 315 SER   A N   1 
ATOM   1928 C  CA  . SER   A 1 295 ? -14.021 -15.802 -18.905 1.00 103.37 ? 315 SER   A CA  1 
ATOM   1929 C  C   . SER   A 1 295 ? -14.379 -16.395 -20.262 1.00 101.40 ? 315 SER   A C   1 
ATOM   1930 O  O   . SER   A 1 295 ? -14.148 -15.775 -21.306 1.00 104.55 ? 315 SER   A O   1 
ATOM   1931 C  CB  . SER   A 1 295 ? -12.767 -16.452 -18.321 1.00 114.12 ? 315 SER   A CB  1 
ATOM   1932 O  OG  . SER   A 1 295 ? -12.458 -15.851 -17.076 1.00 126.02 ? 315 SER   A OG  1 
ATOM   1933 N  N   . PHE   A 1 296 ? -14.981 -17.588 -20.263 1.00 100.80 ? 316 PHE   A N   1 
ATOM   1934 C  CA  . PHE   A 1 296 ? -15.451 -18.179 -21.513 1.00 98.36  ? 316 PHE   A CA  1 
ATOM   1935 C  C   . PHE   A 1 296 ? -16.424 -17.249 -22.228 1.00 94.29  ? 316 PHE   A C   1 
ATOM   1936 O  O   . PHE   A 1 296 ? -16.426 -17.169 -23.462 1.00 99.19  ? 316 PHE   A O   1 
ATOM   1937 C  CB  . PHE   A 1 296 ? -16.106 -19.532 -21.238 1.00 106.13 ? 316 PHE   A CB  1 
ATOM   1938 C  CG  . PHE   A 1 296 ? -15.125 -20.653 -21.055 1.00 102.08 ? 316 PHE   A CG  1 
ATOM   1939 C  CD1 . PHE   A 1 296 ? -14.013 -20.760 -21.873 1.00 97.97  ? 316 PHE   A CD1 1 
ATOM   1940 C  CD2 . PHE   A 1 296 ? -15.316 -21.600 -20.063 1.00 98.46  ? 316 PHE   A CD2 1 
ATOM   1941 C  CE1 . PHE   A 1 296 ? -13.110 -21.793 -21.706 1.00 104.16 ? 316 PHE   A CE1 1 
ATOM   1942 C  CE2 . PHE   A 1 296 ? -14.418 -22.635 -19.892 1.00 102.38 ? 316 PHE   A CE2 1 
ATOM   1943 C  CZ  . PHE   A 1 296 ? -13.313 -22.731 -20.714 1.00 104.06 ? 316 PHE   A CZ  1 
ATOM   1944 N  N   . ILE   A 1 297 ? -17.240 -16.518 -21.468 1.00 97.91  ? 317 ILE   A N   1 
ATOM   1945 C  CA  . ILE   A 1 297 ? -18.247 -15.653 -22.073 1.00 96.58  ? 317 ILE   A CA  1 
ATOM   1946 C  C   . ILE   A 1 297 ? -17.591 -14.447 -22.737 1.00 100.19 ? 317 ILE   A C   1 
ATOM   1947 O  O   . ILE   A 1 297 ? -17.914 -14.097 -23.879 1.00 103.90 ? 317 ILE   A O   1 
ATOM   1948 C  CB  . ILE   A 1 297 ? -19.288 -15.228 -21.023 1.00 97.84  ? 317 ILE   A CB  1 
ATOM   1949 C  CG1 . ILE   A 1 297 ? -20.317 -16.341 -20.821 1.00 96.34  ? 317 ILE   A CG1 1 
ATOM   1950 C  CG2 . ILE   A 1 297 ? -19.979 -13.944 -21.446 1.00 99.92  ? 317 ILE   A CG2 1 
ATOM   1951 C  CD1 . ILE   A 1 297 ? -21.362 -16.030 -19.776 1.00 108.84 ? 317 ILE   A CD1 1 
ATOM   1952 N  N   . MET   A 1 298 ? -16.658 -13.795 -22.037 1.00 98.66  ? 318 MET   A N   1 
ATOM   1953 C  CA  . MET   A 1 298 ? -16.036 -12.595 -22.591 1.00 103.51 ? 318 MET   A CA  1 
ATOM   1954 C  C   . MET   A 1 298 ? -15.196 -12.911 -23.821 1.00 110.88 ? 318 MET   A C   1 
ATOM   1955 O  O   . MET   A 1 298 ? -15.114 -12.088 -24.740 1.00 106.33 ? 318 MET   A O   1 
ATOM   1956 C  CB  . MET   A 1 298 ? -15.182 -11.901 -21.530 1.00 108.99 ? 318 MET   A CB  1 
ATOM   1957 C  CG  . MET   A 1 298 ? -15.962 -11.408 -20.319 1.00 115.03 ? 318 MET   A CG  1 
ATOM   1958 S  SD  . MET   A 1 298 ? -17.663 -10.891 -20.643 1.00 127.00 ? 318 MET   A SD  1 
ATOM   1959 C  CE  . MET   A 1 298 ? -17.419 -9.482  -21.722 1.00 116.83 ? 318 MET   A CE  1 
ATOM   1960 N  N   . TYR   A 1 299 ? -14.561 -14.085 -23.856 1.00 112.03 ? 319 TYR   A N   1 
ATOM   1961 C  CA  . TYR   A 1 299 ? -13.848 -14.500 -25.060 1.00 110.83 ? 319 TYR   A CA  1 
ATOM   1962 C  C   . TYR   A 1 299 ? -14.798 -14.601 -26.245 1.00 114.17 ? 319 TYR   A C   1 
ATOM   1963 O  O   . TYR   A 1 299 ? -14.501 -14.107 -27.340 1.00 108.69 ? 319 TYR   A O   1 
ATOM   1964 C  CB  . TYR   A 1 299 ? -13.140 -15.836 -24.826 1.00 115.10 ? 319 TYR   A CB  1 
ATOM   1965 C  CG  . TYR   A 1 299 ? -12.672 -16.499 -26.106 1.00 119.69 ? 319 TYR   A CG  1 
ATOM   1966 C  CD1 . TYR   A 1 299 ? -11.449 -16.171 -26.675 1.00 107.21 ? 319 TYR   A CD1 1 
ATOM   1967 C  CD2 . TYR   A 1 299 ? -13.455 -17.456 -26.744 1.00 109.79 ? 319 TYR   A CD2 1 
ATOM   1968 C  CE1 . TYR   A 1 299 ? -11.020 -16.771 -27.845 1.00 109.51 ? 319 TYR   A CE1 1 
ATOM   1969 C  CE2 . TYR   A 1 299 ? -13.035 -18.059 -27.915 1.00 109.64 ? 319 TYR   A CE2 1 
ATOM   1970 C  CZ  . TYR   A 1 299 ? -11.816 -17.714 -28.460 1.00 118.88 ? 319 TYR   A CZ  1 
ATOM   1971 O  OH  . TYR   A 1 299 ? -11.392 -18.314 -29.623 1.00 126.12 ? 319 TYR   A OH  1 
ATOM   1972 N  N   . GLU   A 1 300 ? -15.951 -15.241 -26.043 1.00 104.15 ? 320 GLU   A N   1 
ATOM   1973 C  CA  . GLU   A 1 300 ? -16.891 -15.430 -27.140 1.00 105.87 ? 320 GLU   A CA  1 
ATOM   1974 C  C   . GLU   A 1 300 ? -17.535 -14.116 -27.562 1.00 111.75 ? 320 GLU   A C   1 
ATOM   1975 O  O   . GLU   A 1 300 ? -17.832 -13.926 -28.747 1.00 107.35 ? 320 GLU   A O   1 
ATOM   1976 C  CB  . GLU   A 1 300 ? -17.964 -16.446 -26.744 1.00 95.80  ? 320 GLU   A CB  1 
ATOM   1977 C  CG  . GLU   A 1 300 ? -17.468 -17.884 -26.697 1.00 105.95 ? 320 GLU   A CG  1 
ATOM   1978 C  CD  . GLU   A 1 300 ? -16.955 -18.376 -28.037 1.00 111.12 ? 320 GLU   A CD  1 
ATOM   1979 O  OE1 . GLU   A 1 300 ? -17.422 -17.875 -29.080 1.00 113.88 ? 320 GLU   A OE1 1 
ATOM   1980 O  OE2 . GLU   A 1 300 ? -16.080 -19.267 -28.046 1.00 111.15 ? 320 GLU   A OE2 1 
ATOM   1981 N  N   . LEU   A 1 301 ? -17.755 -13.199 -26.617 1.00 119.31 ? 321 LEU   A N   1 
ATOM   1982 C  CA  . LEU   A 1 301 ? -18.341 -11.910 -26.970 1.00 125.01 ? 321 LEU   A CA  1 
ATOM   1983 C  C   . LEU   A 1 301 ? -17.390 -11.062 -27.805 1.00 130.70 ? 321 LEU   A C   1 
ATOM   1984 O  O   . LEU   A 1 301 ? -17.843 -10.250 -28.618 1.00 135.50 ? 321 LEU   A O   1 
ATOM   1985 C  CB  . LEU   A 1 301 ? -18.760 -11.156 -25.707 1.00 124.35 ? 321 LEU   A CB  1 
ATOM   1986 C  CG  . LEU   A 1 301 ? -19.962 -11.714 -24.944 1.00 107.71 ? 321 LEU   A CG  1 
ATOM   1987 C  CD1 . LEU   A 1 301 ? -20.443 -10.721 -23.898 1.00 119.74 ? 321 LEU   A CD1 1 
ATOM   1988 C  CD2 . LEU   A 1 301 ? -21.088 -12.061 -25.907 1.00 104.73 ? 321 LEU   A CD2 1 
ATOM   1989 N  N   . ALA   A 1 302 ? -16.080 -11.238 -27.632 1.00 160.45 ? 322 ALA   A N   1 
ATOM   1990 C  CA  . ALA   A 1 302 ? -15.127 -10.432 -28.388 1.00 167.59 ? 322 ALA   A CA  1 
ATOM   1991 C  C   . ALA   A 1 302 ? -14.943 -10.958 -29.807 1.00 166.50 ? 322 ALA   A C   1 
ATOM   1992 O  O   . ALA   A 1 302 ? -14.982 -10.186 -30.771 1.00 168.93 ? 322 ALA   A O   1 
ATOM   1993 C  CB  . ALA   A 1 302 ? -13.784 -10.380 -27.665 1.00 165.63 ? 322 ALA   A CB  1 
ATOM   1994 N  N   . THR   A 1 303 ? -14.723 -12.267 -29.952 1.00 137.19 ? 323 THR   A N   1 
ATOM   1995 C  CA  . THR   A 1 303 ? -14.560 -12.852 -31.277 1.00 138.27 ? 323 THR   A CA  1 
ATOM   1996 C  C   . THR   A 1 303 ? -15.834 -12.749 -32.104 1.00 121.53 ? 323 THR   A C   1 
ATOM   1997 O  O   . THR   A 1 303 ? -15.769 -12.818 -33.335 1.00 133.70 ? 323 THR   A O   1 
ATOM   1998 C  CB  . THR   A 1 303 ? -14.107 -14.313 -31.134 1.00 128.31 ? 323 THR   A CB  1 
ATOM   1999 O  OG1 . THR   A 1 303 ? -12.877 -14.364 -30.398 1.00 130.24 ? 323 THR   A OG1 1 
ATOM   2000 C  CG2 . THR   A 1 303 ? -13.881 -14.971 -32.488 1.00 136.37 ? 323 THR   A CG2 1 
ATOM   2001 N  N   . HIS   A 1 304 ? -16.979 -12.555 -31.452 1.00 133.06 ? 324 HIS   A N   1 
ATOM   2002 C  CA  . HIS   A 1 304 ? -18.277 -12.377 -32.097 1.00 130.23 ? 324 HIS   A CA  1 
ATOM   2003 C  C   . HIS   A 1 304 ? -18.844 -11.033 -31.622 1.00 131.47 ? 324 HIS   A C   1 
ATOM   2004 O  O   . HIS   A 1 304 ? -19.749 -10.989 -30.769 1.00 124.82 ? 324 HIS   A O   1 
ATOM   2005 C  CB  . HIS   A 1 304 ? -19.238 -13.514 -31.754 1.00 107.28 ? 324 HIS   A CB  1 
ATOM   2006 C  CG  . HIS   A 1 304 ? -18.690 -14.872 -32.036 1.00 115.09 ? 324 HIS   A CG  1 
ATOM   2007 N  ND1 . HIS   A 1 304 ? -18.516 -15.373 -33.308 1.00 122.56 ? 324 HIS   A ND1 1 
ATOM   2008 C  CD2 . HIS   A 1 304 ? -18.254 -15.832 -31.192 1.00 108.21 ? 324 HIS   A CD2 1 
ATOM   2009 C  CE1 . HIS   A 1 304 ? -18.010 -16.592 -33.234 1.00 115.18 ? 324 HIS   A CE1 1 
ATOM   2010 N  NE2 . HIS   A 1 304 ? -17.839 -16.893 -31.960 1.00 110.69 ? 324 HIS   A NE2 1 
ATOM   2011 N  N   . PRO   A 1 305 ? -18.357 -9.921  -32.196 1.00 133.68 ? 325 PRO   A N   1 
ATOM   2012 C  CA  . PRO   A 1 305 ? -18.794 -8.588  -31.734 1.00 127.16 ? 325 PRO   A CA  1 
ATOM   2013 C  C   . PRO   A 1 305 ? -20.251 -8.248  -32.037 1.00 125.37 ? 325 PRO   A C   1 
ATOM   2014 O  O   . PRO   A 1 305 ? -20.845 -7.494  -31.263 1.00 119.78 ? 325 PRO   A O   1 
ATOM   2015 C  CB  . PRO   A 1 305 ? -17.786 -7.691  -32.459 1.00 120.70 ? 325 PRO   A CB  1 
ATOM   2016 C  CG  . PRO   A 1 305 ? -16.957 -8.709  -33.414 1.00 126.42 ? 325 PRO   A CG  1 
ATOM   2017 C  CD  . PRO   A 1 305 ? -17.910 -9.828  -33.609 1.00 127.49 ? 325 PRO   A CD  1 
ATOM   2018 N  N   . ASP   A 1 306 ? -20.852 -8.784  -33.107 1.00 130.88 ? 326 ASP   A N   1 
ATOM   2019 C  CA  . ASP   A 1 306 ? -22.283 -8.583  -33.338 1.00 131.68 ? 326 ASP   A CA  1 
ATOM   2020 C  C   . ASP   A 1 306 ? -23.120 -9.097  -32.171 1.00 129.07 ? 326 ASP   A C   1 
ATOM   2021 O  O   . ASP   A 1 306 ? -24.146 -8.502  -31.819 1.00 127.45 ? 326 ASP   A O   1 
ATOM   2022 C  CB  . ASP   A 1 306 ? -22.673 -9.276  -34.631 1.00 134.46 ? 326 ASP   A CB  1 
ATOM   2023 C  CG  . ASP   A 1 306 ? -22.211 -10.720 -34.671 1.00 138.35 ? 326 ASP   A CG  1 
ATOM   2024 O  OD1 . ASP   A 1 306 ? -20.984 -10.953 -34.567 1.00 138.70 ? 326 ASP   A OD1 1 
ATOM   2025 O  OD2 . ASP   A 1 306 ? -23.060 -11.615 -34.819 1.00 137.65 ? 326 ASP   A OD2 1 
ATOM   2026 N  N   . VAL   A 1 307 ? -22.707 -10.214 -31.571 1.00 124.05 ? 327 VAL   A N   1 
ATOM   2027 C  CA  . VAL   A 1 307 ? -23.395 -10.714 -30.386 1.00 121.76 ? 327 VAL   A CA  1 
ATOM   2028 C  C   . VAL   A 1 307 ? -23.142 -9.795  -29.197 1.00 119.37 ? 327 VAL   A C   1 
ATOM   2029 O  O   . VAL   A 1 307 ? -24.057 -9.497  -28.419 1.00 118.68 ? 327 VAL   A O   1 
ATOM   2030 C  CB  . VAL   A 1 307 ? -22.962 -12.162 -30.091 1.00 120.54 ? 327 VAL   A CB  1 
ATOM   2031 C  CG1 . VAL   A 1 307 ? -23.538 -12.632 -28.769 1.00 97.27  ? 327 VAL   A CG1 1 
ATOM   2032 C  CG2 . VAL   A 1 307 ? -23.388 -13.085 -31.222 1.00 102.24 ? 327 VAL   A CG2 1 
ATOM   2033 N  N   . GLN   A 1 308 ? -21.901 -9.324  -29.043 1.00 115.94 ? 328 GLN   A N   1 
ATOM   2034 C  CA  . GLN   A 1 308 ? -21.572 -8.446  -27.923 1.00 116.93 ? 328 GLN   A CA  1 
ATOM   2035 C  C   . GLN   A 1 308 ? -22.394 -7.163  -27.960 1.00 128.07 ? 328 GLN   A C   1 
ATOM   2036 O  O   . GLN   A 1 308 ? -22.882 -6.700  -26.922 1.00 119.04 ? 328 GLN   A O   1 
ATOM   2037 C  CB  . GLN   A 1 308 ? -20.079 -8.119  -27.926 1.00 125.75 ? 328 GLN   A CB  1 
ATOM   2038 C  CG  . GLN   A 1 308 ? -19.623 -7.282  -26.737 1.00 121.78 ? 328 GLN   A CG  1 
ATOM   2039 C  CD  . GLN   A 1 308 ? -18.115 -7.121  -26.676 1.00 122.05 ? 328 GLN   A CD  1 
ATOM   2040 O  OE1 . GLN   A 1 308 ? -17.585 -6.471  -25.775 1.00 118.08 ? 328 GLN   A OE1 1 
ATOM   2041 N  NE2 . GLN   A 1 308 ? -17.417 -7.712  -27.639 1.00 124.30 ? 328 GLN   A NE2 1 
ATOM   2042 N  N   . GLN   A 1 309 ? -22.560 -6.574  -29.147 1.00 115.35 ? 329 GLN   A N   1 
ATOM   2043 C  CA  . GLN   A 1 309 ? -23.313 -5.329  -29.250 1.00 115.12 ? 329 GLN   A CA  1 
ATOM   2044 C  C   . GLN   A 1 309 ? -24.808 -5.574  -29.094 1.00 121.57 ? 329 GLN   A C   1 
ATOM   2045 O  O   . GLN   A 1 309 ? -25.485 -4.869  -28.335 1.00 115.58 ? 329 GLN   A O   1 
ATOM   2046 C  CB  . GLN   A 1 309 ? -23.028 -4.641  -30.583 1.00 125.52 ? 329 GLN   A CB  1 
ATOM   2047 C  CG  . GLN   A 1 309 ? -23.754 -3.316  -30.726 1.00 126.78 ? 329 GLN   A CG  1 
ATOM   2048 C  CD  . GLN   A 1 309 ? -23.553 -2.681  -32.082 1.00 121.05 ? 329 GLN   A CD  1 
ATOM   2049 O  OE1 . GLN   A 1 309 ? -22.425 -2.499  -32.536 1.00 131.29 ? 329 GLN   A OE1 1 
ATOM   2050 N  NE2 . GLN   A 1 309 ? -24.654 -2.339  -32.740 1.00 122.87 ? 329 GLN   A NE2 1 
ATOM   2051 N  N   . LYS   A 1 310 ? -25.346 -6.561  -29.819 1.00 123.02 ? 330 LYS   A N   1 
ATOM   2052 C  CA  . LYS   A 1 310 ? -26.762 -6.892  -29.684 1.00 125.91 ? 330 LYS   A CA  1 
ATOM   2053 C  C   . LYS   A 1 310 ? -27.117 -7.211  -28.241 1.00 123.75 ? 330 LYS   A C   1 
ATOM   2054 O  O   . LYS   A 1 310 ? -28.228 -6.907  -27.790 1.00 129.31 ? 330 LYS   A O   1 
ATOM   2055 C  CB  . LYS   A 1 310 ? -27.124 -8.064  -30.599 1.00 132.31 ? 330 LYS   A CB  1 
ATOM   2056 C  CG  . LYS   A 1 310 ? -28.485 -8.684  -30.310 1.00 124.66 ? 330 LYS   A CG  1 
ATOM   2057 C  CD  . LYS   A 1 310 ? -29.069 -9.351  -31.542 1.00 130.03 ? 330 LYS   A CD  1 
ATOM   2058 C  CE  . LYS   A 1 310 ? -30.400 -10.021 -31.231 1.00 130.36 ? 330 LYS   A CE  1 
ATOM   2059 N  NZ  . LYS   A 1 310 ? -31.364 -9.892  -32.358 1.00 150.76 ? 330 LYS   A NZ  1 
ATOM   2060 N  N   . LEU   A 1 311 ? -26.189 -7.810  -27.495 1.00 123.51 ? 331 LEU   A N   1 
ATOM   2061 C  CA  . LEU   A 1 311 ? -26.396 -7.923  -26.058 1.00 124.57 ? 331 LEU   A CA  1 
ATOM   2062 C  C   . LEU   A 1 311 ? -26.446 -6.540  -25.419 1.00 129.06 ? 331 LEU   A C   1 
ATOM   2063 O  O   . LEU   A 1 311 ? -27.464 -6.165  -24.824 1.00 128.74 ? 331 LEU   A O   1 
ATOM   2064 C  CB  . LEU   A 1 311 ? -25.311 -8.803  -25.431 1.00 121.50 ? 331 LEU   A CB  1 
ATOM   2065 C  CG  . LEU   A 1 311 ? -25.696 -9.443  -24.094 1.00 122.22 ? 331 LEU   A CG  1 
ATOM   2066 C  CD1 . LEU   A 1 311 ? -26.634 -10.593 -24.338 1.00 117.27 ? 331 LEU   A CD1 1 
ATOM   2067 C  CD2 . LEU   A 1 311 ? -24.470 -9.963  -23.382 1.00 110.89 ? 331 LEU   A CD2 1 
ATOM   2068 N  N   . GLN   A 1 312 ? -25.382 -5.742  -25.598 1.00 136.29 ? 332 GLN   A N   1 
ATOM   2069 C  CA  . GLN   A 1 312 ? -25.337 -4.384  -25.050 1.00 127.30 ? 332 GLN   A CA  1 
ATOM   2070 C  C   . GLN   A 1 312 ? -26.610 -3.602  -25.354 1.00 130.36 ? 332 GLN   A C   1 
ATOM   2071 O  O   . GLN   A 1 312 ? -27.064 -2.796  -24.533 1.00 126.05 ? 332 GLN   A O   1 
ATOM   2072 C  CB  . GLN   A 1 312 ? -24.126 -3.624  -25.599 1.00 123.33 ? 332 GLN   A CB  1 
ATOM   2073 C  CG  . GLN   A 1 312 ? -22.777 -4.065  -25.058 1.00 135.90 ? 332 GLN   A CG  1 
ATOM   2074 C  CD  . GLN   A 1 312 ? -21.621 -3.582  -25.917 1.00 130.56 ? 332 GLN   A CD  1 
ATOM   2075 O  OE1 . GLN   A 1 312 ? -21.760 -3.412  -27.128 1.00 125.05 ? 332 GLN   A OE1 1 
ATOM   2076 N  NE2 . GLN   A 1 312 ? -20.471 -3.360  -25.291 1.00 131.42 ? 332 GLN   A NE2 1 
ATOM   2077 N  N   . GLU   A 1 313 ? -27.194 -3.821  -26.534 1.00 136.98 ? 333 GLU   A N   1 
ATOM   2078 C  CA  . GLU   A 1 313 ? -28.450 -3.159  -26.875 1.00 144.27 ? 333 GLU   A CA  1 
ATOM   2079 C  C   . GLU   A 1 313 ? -29.569 -3.591  -25.934 1.00 140.23 ? 333 GLU   A C   1 
ATOM   2080 O  O   . GLU   A 1 313 ? -30.352 -2.760  -25.459 1.00 143.06 ? 333 GLU   A O   1 
ATOM   2081 C  CB  . GLU   A 1 313 ? -28.818 -3.463  -28.328 1.00 150.18 ? 333 GLU   A CB  1 
ATOM   2082 C  CG  . GLU   A 1 313 ? -28.039 -2.657  -29.355 1.00 153.76 ? 333 GLU   A CG  1 
ATOM   2083 C  CD  . GLU   A 1 313 ? -27.960 -3.356  -30.699 1.00 151.80 ? 333 GLU   A CD  1 
ATOM   2084 O  OE1 . GLU   A 1 313 ? -26.897 -3.279  -31.349 1.00 151.52 ? 333 GLU   A OE1 1 
ATOM   2085 O  OE2 . GLU   A 1 313 ? -28.959 -3.989  -31.103 1.00 149.76 ? 333 GLU   A OE2 1 
ATOM   2086 N  N   . GLU   A 1 314 ? -29.655 -4.893  -25.650 1.00 145.53 ? 334 GLU   A N   1 
ATOM   2087 C  CA  . GLU   A 1 314 ? -30.710 -5.393  -24.773 1.00 145.83 ? 334 GLU   A CA  1 
ATOM   2088 C  C   . GLU   A 1 314 ? -30.520 -4.905  -23.344 1.00 147.45 ? 334 GLU   A C   1 
ATOM   2089 O  O   . GLU   A 1 314 ? -31.497 -4.594  -22.652 1.00 149.89 ? 334 GLU   A O   1 
ATOM   2090 C  CB  . GLU   A 1 314 ? -30.751 -6.921  -24.812 1.00 133.52 ? 334 GLU   A CB  1 
ATOM   2091 C  CG  . GLU   A 1 314 ? -31.974 -7.516  -24.136 1.00 134.94 ? 334 GLU   A CG  1 
ATOM   2092 C  CD  . GLU   A 1 314 ? -31.827 -8.998  -23.858 1.00 125.65 ? 334 GLU   A CD  1 
ATOM   2093 O  OE1 . GLU   A 1 314 ? -30.930 -9.366  -23.070 1.00 131.66 ? 334 GLU   A OE1 1 
ATOM   2094 O  OE2 . GLU   A 1 314 ? -32.616 -9.791  -24.410 1.00 121.51 ? 334 GLU   A OE2 1 
ATOM   2095 N  N   . ILE   A 1 315 ? -29.270 -4.829  -22.885 1.00 158.92 ? 335 ILE   A N   1 
ATOM   2096 C  CA  . ILE   A 1 315 ? -29.016 -4.413  -21.509 1.00 159.44 ? 335 ILE   A CA  1 
ATOM   2097 C  C   . ILE   A 1 315 ? -29.430 -2.961  -21.303 1.00 159.90 ? 335 ILE   A C   1 
ATOM   2098 O  O   . ILE   A 1 315 ? -30.124 -2.630  -20.335 1.00 164.65 ? 335 ILE   A O   1 
ATOM   2099 C  CB  . ILE   A 1 315 ? -27.540 -4.638  -21.129 1.00 153.94 ? 335 ILE   A CB  1 
ATOM   2100 C  CG1 . ILE   A 1 315 ? -26.937 -5.819  -21.894 1.00 151.00 ? 335 ILE   A CG1 1 
ATOM   2101 C  CG2 . ILE   A 1 315 ? -27.399 -4.857  -19.640 1.00 151.38 ? 335 ILE   A CG2 1 
ATOM   2102 C  CD1 . ILE   A 1 315 ? -25.476 -6.055  -21.586 1.00 146.82 ? 335 ILE   A CD1 1 
ATOM   2103 N  N   . ASP   A 1 316 ? -29.018 -2.071  -22.209 1.00 145.31 ? 336 ASP   A N   1 
ATOM   2104 C  CA  . ASP   A 1 316 ? -29.362 -0.662  -22.053 1.00 142.01 ? 336 ASP   A CA  1 
ATOM   2105 C  C   . ASP   A 1 316 ? -30.831 -0.387  -22.347 1.00 140.54 ? 336 ASP   A C   1 
ATOM   2106 O  O   . ASP   A 1 316 ? -31.339 0.674   -21.967 1.00 147.89 ? 336 ASP   A O   1 
ATOM   2107 C  CB  . ASP   A 1 316 ? -28.472 0.204   -22.946 1.00 143.01 ? 336 ASP   A CB  1 
ATOM   2108 C  CG  . ASP   A 1 316 ? -27.001 0.060   -22.611 1.00 148.23 ? 336 ASP   A CG  1 
ATOM   2109 O  OD1 . ASP   A 1 316 ? -26.668 0.006   -21.407 1.00 145.14 ? 336 ASP   A OD1 1 
ATOM   2110 O  OD2 . ASP   A 1 316 ? -26.179 -0.005  -23.548 1.00 140.30 ? 336 ASP   A OD2 1 
ATOM   2111 N  N   . ALA   A 1 317 ? -31.524 -1.313  -23.010 1.00 146.03 ? 337 ALA   A N   1 
ATOM   2112 C  CA  . ALA   A 1 317 ? -32.961 -1.167  -23.210 1.00 144.33 ? 337 ALA   A CA  1 
ATOM   2113 C  C   . ALA   A 1 317 ? -33.731 -1.525  -21.944 1.00 143.65 ? 337 ALA   A C   1 
ATOM   2114 O  O   . ALA   A 1 317 ? -34.554 -0.737  -21.464 1.00 139.11 ? 337 ALA   A O   1 
ATOM   2115 C  CB  . ALA   A 1 317 ? -33.418 -2.034  -24.384 1.00 128.44 ? 337 ALA   A CB  1 
ATOM   2116 N  N   . VAL   A 1 318 ? -33.472 -2.711  -21.388 1.00 144.90 ? 338 VAL   A N   1 
ATOM   2117 C  CA  . VAL   A 1 318 ? -34.157 -3.135  -20.171 1.00 146.21 ? 338 VAL   A CA  1 
ATOM   2118 C  C   . VAL   A 1 318 ? -33.753 -2.254  -18.996 1.00 142.50 ? 338 VAL   A C   1 
ATOM   2119 O  O   . VAL   A 1 318 ? -34.574 -1.937  -18.125 1.00 146.72 ? 338 VAL   A O   1 
ATOM   2120 C  CB  . VAL   A 1 318 ? -33.873 -4.625  -19.897 1.00 140.07 ? 338 VAL   A CB  1 
ATOM   2121 C  CG1 . VAL   A 1 318 ? -33.968 -4.936  -18.411 1.00 141.61 ? 338 VAL   A CG1 1 
ATOM   2122 C  CG2 . VAL   A 1 318 ? -34.836 -5.500  -20.685 1.00 140.06 ? 338 VAL   A CG2 1 
ATOM   2123 N  N   . LEU   A 1 319 ? -32.489 -1.827  -18.962 1.00 153.52 ? 339 LEU   A N   1 
ATOM   2124 C  CA  . LEU   A 1 319 ? -31.953 -0.980  -17.899 1.00 164.02 ? 339 LEU   A CA  1 
ATOM   2125 C  C   . LEU   A 1 319 ? -31.536 0.355   -18.508 1.00 166.42 ? 339 LEU   A C   1 
ATOM   2126 O  O   . LEU   A 1 319 ? -30.342 0.596   -18.745 1.00 162.90 ? 339 LEU   A O   1 
ATOM   2127 C  CB  . LEU   A 1 319 ? -30.784 -1.660  -17.191 1.00 139.20 ? 339 LEU   A CB  1 
ATOM   2128 C  CG  . LEU   A 1 319 ? -31.162 -2.890  -16.362 1.00 148.66 ? 339 LEU   A CG  1 
ATOM   2129 C  CD1 . LEU   A 1 319 ? -29.933 -3.530  -15.738 1.00 156.23 ? 339 LEU   A CD1 1 
ATOM   2130 C  CD2 . LEU   A 1 319 ? -32.187 -2.529  -15.298 1.00 136.25 ? 339 LEU   A CD2 1 
ATOM   2131 N  N   . PRO   A 1 320 ? -32.489 1.248   -18.763 1.00 150.73 ? 340 PRO   A N   1 
ATOM   2132 C  CA  . PRO   A 1 320 ? -32.153 2.544   -19.361 1.00 154.91 ? 340 PRO   A CA  1 
ATOM   2133 C  C   . PRO   A 1 320 ? -31.424 3.431   -18.365 1.00 162.09 ? 340 PRO   A C   1 
ATOM   2134 O  O   . PRO   A 1 320 ? -31.548 3.280   -17.149 1.00 168.93 ? 340 PRO   A O   1 
ATOM   2135 C  CB  . PRO   A 1 320 ? -33.522 3.125   -19.727 1.00 148.28 ? 340 PRO   A CB  1 
ATOM   2136 C  CG  . PRO   A 1 320 ? -34.440 2.534   -18.694 1.00 148.11 ? 340 PRO   A CG  1 
ATOM   2137 C  CD  . PRO   A 1 320 ? -33.921 1.145   -18.430 1.00 151.20 ? 340 PRO   A CD  1 
ATOM   2138 N  N   . ASN   A 1 321 ? -30.653 4.377   -18.905 1.00 167.49 ? 341 ASN   A N   1 
ATOM   2139 C  CA  . ASN   A 1 321 ? -29.808 5.249   -18.088 1.00 170.68 ? 341 ASN   A CA  1 
ATOM   2140 C  C   . ASN   A 1 321 ? -28.911 4.421   -17.168 1.00 164.74 ? 341 ASN   A C   1 
ATOM   2141 O  O   . ASN   A 1 321 ? -28.867 4.640   -15.952 1.00 165.65 ? 341 ASN   A O   1 
ATOM   2142 C  CB  . ASN   A 1 321 ? -30.645 6.245   -17.275 1.00 171.40 ? 341 ASN   A CB  1 
ATOM   2143 C  CG  . ASN   A 1 321 ? -31.326 7.298   -18.140 1.00 162.97 ? 341 ASN   A CG  1 
ATOM   2144 O  OD1 . ASN   A 1 321 ? -31.263 7.250   -19.368 1.00 163.94 ? 341 ASN   A OD1 1 
ATOM   2145 N  ND2 . ASN   A 1 321 ? -31.974 8.263   -17.493 1.00 164.28 ? 341 ASN   A ND2 1 
ATOM   2146 N  N   . LYS   A 1 322 ? -28.197 3.454   -17.762 1.00 165.08 ? 342 LYS   A N   1 
ATOM   2147 C  CA  . LYS   A 1 322 ? -27.337 2.496   -17.048 1.00 154.52 ? 342 LYS   A CA  1 
ATOM   2148 C  C   . LYS   A 1 322 ? -27.934 2.096   -15.692 1.00 155.03 ? 342 LYS   A C   1 
ATOM   2149 O  O   . LYS   A 1 322 ? -27.267 2.123   -14.657 1.00 155.08 ? 342 LYS   A O   1 
ATOM   2150 C  CB  . LYS   A 1 322 ? -25.903 3.045   -16.928 1.00 150.61 ? 342 LYS   A CB  1 
ATOM   2151 C  CG  . LYS   A 1 322 ? -25.820 4.492   -16.452 1.00 149.46 ? 342 LYS   A CG  1 
ATOM   2152 C  CD  . LYS   A 1 322 ? -25.095 5.360   -17.474 1.00 163.73 ? 342 LYS   A CD  1 
ATOM   2153 C  CE  . LYS   A 1 322 ? -24.997 6.791   -16.972 1.00 159.83 ? 342 LYS   A CE  1 
ATOM   2154 N  NZ  . LYS   A 1 322 ? -24.358 7.708   -17.957 1.00 140.21 ? 342 LYS   A NZ  1 
ATOM   2155 N  N   . ALA   A 1 323 ? -29.212 1.701   -15.719 1.00 151.42 ? 343 ALA   A N   1 
ATOM   2156 C  CA  . ALA   A 1 323 ? -29.994 1.399   -14.526 1.00 158.07 ? 343 ALA   A CA  1 
ATOM   2157 C  C   . ALA   A 1 323 ? -29.379 0.253   -13.722 1.00 150.26 ? 343 ALA   A C   1 
ATOM   2158 O  O   . ALA   A 1 323 ? -28.605 -0.535  -14.258 1.00 145.94 ? 343 ALA   A O   1 
ATOM   2159 C  CB  . ALA   A 1 323 ? -31.427 1.047   -14.930 1.00 154.53 ? 343 ALA   A CB  1 
ATOM   2160 N  N   . PRO   A 1 324 ? -29.716 0.121   -12.435 1.00 156.31 ? 344 PRO   A N   1 
ATOM   2161 C  CA  . PRO   A 1 324 ? -29.103 -0.954  -11.636 1.00 158.72 ? 344 PRO   A CA  1 
ATOM   2162 C  C   . PRO   A 1 324 ? -29.870 -2.254  -11.796 1.00 155.65 ? 344 PRO   A C   1 
ATOM   2163 O  O   . PRO   A 1 324 ? -31.112 -2.272  -11.735 1.00 153.44 ? 344 PRO   A O   1 
ATOM   2164 C  CB  . PRO   A 1 324 ? -29.189 -0.412  -10.201 1.00 161.24 ? 344 PRO   A CB  1 
ATOM   2165 C  CG  . PRO   A 1 324 ? -30.349 0.593   -10.220 1.00 160.83 ? 344 PRO   A CG  1 
ATOM   2166 C  CD  . PRO   A 1 324 ? -30.826 0.732   -11.662 1.00 162.88 ? 344 PRO   A CD  1 
ATOM   2167 N  N   . PRO   A 1 325 ? -29.158 -3.356  -12.016 1.00 154.07 ? 345 PRO   A N   1 
ATOM   2168 C  CA  . PRO   A 1 325 ? -29.837 -4.640  -12.195 1.00 153.45 ? 345 PRO   A CA  1 
ATOM   2169 C  C   . PRO   A 1 325 ? -30.544 -5.066  -10.920 1.00 149.86 ? 345 PRO   A C   1 
ATOM   2170 O  O   . PRO   A 1 325 ? -30.008 -4.947  -9.817  1.00 153.39 ? 345 PRO   A O   1 
ATOM   2171 C  CB  . PRO   A 1 325 ? -28.698 -5.596  -12.564 1.00 149.47 ? 345 PRO   A CB  1 
ATOM   2172 C  CG  . PRO   A 1 325 ? -27.469 -4.952  -12.015 1.00 146.64 ? 345 PRO   A CG  1 
ATOM   2173 C  CD  . PRO   A 1 325 ? -27.692 -3.474  -12.102 1.00 152.93 ? 345 PRO   A CD  1 
ATOM   2174 N  N   . THR   A 1 326 ? -31.778 -5.535  -11.082 1.00 158.47 ? 346 THR   A N   1 
ATOM   2175 C  CA  . THR   A 1 326 ? -32.565 -6.094  -9.994  1.00 157.30 ? 346 THR   A CA  1 
ATOM   2176 C  C   . THR   A 1 326 ? -32.958 -7.515  -10.373 1.00 155.09 ? 346 THR   A C   1 
ATOM   2177 O  O   . THR   A 1 326 ? -32.669 -7.985  -11.476 1.00 144.33 ? 346 THR   A O   1 
ATOM   2178 C  CB  . THR   A 1 326 ? -33.801 -5.234  -9.689  1.00 141.33 ? 346 THR   A CB  1 
ATOM   2179 O  OG1 . THR   A 1 326 ? -34.329 -4.693  -10.908 1.00 148.23 ? 346 THR   A OG1 1 
ATOM   2180 C  CG2 . THR   A 1 326 ? -33.432 -4.093  -8.755  1.00 154.81 ? 346 THR   A CG2 1 
ATOM   2181 N  N   . TYR   A 1 327 ? -33.622 -8.203  -9.443  1.00 146.65 ? 347 TYR   A N   1 
ATOM   2182 C  CA  . TYR   A 1 327 ? -33.983 -9.599  -9.669  1.00 142.49 ? 347 TYR   A CA  1 
ATOM   2183 C  C   . TYR   A 1 327 ? -34.881 -9.751  -10.891 1.00 141.67 ? 347 TYR   A C   1 
ATOM   2184 O  O   . TYR   A 1 327 ? -34.615 -10.577 -11.772 1.00 146.01 ? 347 TYR   A O   1 
ATOM   2185 C  CB  . TYR   A 1 327 ? -34.662 -10.171 -8.421  1.00 152.16 ? 347 TYR   A CB  1 
ATOM   2186 C  CG  . TYR   A 1 327 ? -34.940 -11.657 -8.494  1.00 149.82 ? 347 TYR   A CG  1 
ATOM   2187 C  CD1 . TYR   A 1 327 ? -33.954 -12.582 -8.180  1.00 140.43 ? 347 TYR   A CD1 1 
ATOM   2188 C  CD2 . TYR   A 1 327 ? -36.195 -12.135 -8.852  1.00 150.27 ? 347 TYR   A CD2 1 
ATOM   2189 C  CE1 . TYR   A 1 327 ? -34.199 -13.942 -8.242  1.00 139.20 ? 347 TYR   A CE1 1 
ATOM   2190 C  CE2 . TYR   A 1 327 ? -36.453 -13.495 -8.907  1.00 150.80 ? 347 TYR   A CE2 1 
ATOM   2191 C  CZ  . TYR   A 1 327 ? -35.450 -14.393 -8.607  1.00 148.38 ? 347 TYR   A CZ  1 
ATOM   2192 O  OH  . TYR   A 1 327 ? -35.699 -15.745 -8.665  1.00 159.09 ? 347 TYR   A OH  1 
ATOM   2193 N  N   . ASP   A 1 328 ? -35.937 -8.942  -10.973 1.00 149.28 ? 348 ASP   A N   1 
ATOM   2194 C  CA  . ASP   A 1 328 ? -36.938 -9.124  -12.017 1.00 151.38 ? 348 ASP   A CA  1 
ATOM   2195 C  C   . ASP   A 1 328 ? -36.463 -8.633  -13.380 1.00 150.32 ? 348 ASP   A C   1 
ATOM   2196 O  O   . ASP   A 1 328 ? -36.915 -9.151  -14.408 1.00 150.14 ? 348 ASP   A O   1 
ATOM   2197 C  CB  . ASP   A 1 328 ? -38.233 -8.419  -11.617 1.00 141.69 ? 348 ASP   A CB  1 
ATOM   2198 C  CG  . ASP   A 1 328 ? -38.690 -8.801  -10.223 1.00 147.52 ? 348 ASP   A CG  1 
ATOM   2199 O  OD1 . ASP   A 1 328 ? -39.356 -9.847  -10.080 1.00 147.50 ? 348 ASP   A OD1 1 
ATOM   2200 O  OD2 . ASP   A 1 328 ? -38.376 -8.058  -9.268  1.00 137.37 ? 348 ASP   A OD2 1 
ATOM   2201 N  N   . THR   A 1 329 ? -35.568 -7.643  -13.418 1.00 149.09 ? 349 THR   A N   1 
ATOM   2202 C  CA  . THR   A 1 329 ? -35.019 -7.208  -14.699 1.00 148.11 ? 349 THR   A CA  1 
ATOM   2203 C  C   . THR   A 1 329 ? -34.135 -8.286  -15.313 1.00 151.30 ? 349 THR   A C   1 
ATOM   2204 O  O   . THR   A 1 329 ? -34.140 -8.481  -16.534 1.00 150.39 ? 349 THR   A O   1 
ATOM   2205 C  CB  . THR   A 1 329 ? -34.226 -5.911  -14.528 1.00 146.48 ? 349 THR   A CB  1 
ATOM   2206 O  OG1 . THR   A 1 329 ? -33.547 -5.927  -13.266 1.00 147.62 ? 349 THR   A OG1 1 
ATOM   2207 C  CG2 . THR   A 1 329 ? -35.152 -4.705  -14.590 1.00 148.30 ? 349 THR   A CG2 1 
ATOM   2208 N  N   . VAL   A 1 330 ? -33.376 -8.999  -14.478 1.00 151.43 ? 350 VAL   A N   1 
ATOM   2209 C  CA  . VAL   A 1 330 ? -32.455 -10.016 -14.978 1.00 146.50 ? 350 VAL   A CA  1 
ATOM   2210 C  C   . VAL   A 1 330 ? -33.220 -11.165 -15.620 1.00 143.87 ? 350 VAL   A C   1 
ATOM   2211 O  O   . VAL   A 1 330 ? -32.772 -11.750 -16.615 1.00 146.59 ? 350 VAL   A O   1 
ATOM   2212 C  CB  . VAL   A 1 330 ? -31.540 -10.503 -13.839 1.00 140.99 ? 350 VAL   A CB  1 
ATOM   2213 C  CG1 . VAL   A 1 330 ? -30.710 -11.693 -14.282 1.00 133.33 ? 350 VAL   A CG1 1 
ATOM   2214 C  CG2 . VAL   A 1 330 ? -30.641 -9.379  -13.384 1.00 145.46 ? 350 VAL   A CG2 1 
ATOM   2215 N  N   . LEU   A 1 331 ? -34.386 -11.502 -15.074 1.00 135.08 ? 351 LEU   A N   1 
ATOM   2216 C  CA  . LEU   A 1 331 ? -35.203 -12.575 -15.622 1.00 148.93 ? 351 LEU   A CA  1 
ATOM   2217 C  C   . LEU   A 1 331 ? -36.047 -12.134 -16.812 1.00 148.82 ? 351 LEU   A C   1 
ATOM   2218 O  O   . LEU   A 1 331 ? -36.867 -12.921 -17.297 1.00 148.20 ? 351 LEU   A O   1 
ATOM   2219 C  CB  . LEU   A 1 331 ? -36.097 -13.164 -14.529 1.00 142.23 ? 351 LEU   A CB  1 
ATOM   2220 C  CG  . LEU   A 1 331 ? -35.342 -14.051 -13.537 1.00 135.78 ? 351 LEU   A CG  1 
ATOM   2221 C  CD1 . LEU   A 1 331 ? -35.570 -13.586 -12.118 1.00 145.12 ? 351 LEU   A CD1 1 
ATOM   2222 C  CD2 . LEU   A 1 331 ? -35.750 -15.507 -13.695 1.00 130.71 ? 351 LEU   A CD2 1 
ATOM   2223 N  N   . GLN   A 1 332 ? -35.869 -10.904 -17.290 1.00 145.25 ? 352 GLN   A N   1 
ATOM   2224 C  CA  . GLN   A 1 332 ? -36.507 -10.456 -18.520 1.00 145.19 ? 352 GLN   A CA  1 
ATOM   2225 C  C   . GLN   A 1 332 ? -35.549 -10.426 -19.701 1.00 147.25 ? 352 GLN   A C   1 
ATOM   2226 O  O   . GLN   A 1 332 ? -35.979 -10.631 -20.842 1.00 150.98 ? 352 GLN   A O   1 
ATOM   2227 C  CB  . GLN   A 1 332 ? -37.119 -9.062  -18.330 1.00 154.53 ? 352 GLN   A CB  1 
ATOM   2228 C  CG  . GLN   A 1 332 ? -37.947 -8.583  -19.514 1.00 152.81 ? 352 GLN   A CG  1 
ATOM   2229 C  CD  . GLN   A 1 332 ? -38.351 -7.127  -19.400 1.00 155.06 ? 352 GLN   A CD  1 
ATOM   2230 O  OE1 . GLN   A 1 332 ? -38.485 -6.591  -18.300 1.00 163.37 ? 352 GLN   A OE1 1 
ATOM   2231 N  NE2 . GLN   A 1 332 ? -38.548 -6.478  -20.542 1.00 156.59 ? 352 GLN   A NE2 1 
ATOM   2232 N  N   . MET   A 1 333 ? -34.263 -10.186 -19.453 1.00 159.18 ? 353 MET   A N   1 
ATOM   2233 C  CA  . MET   A 1 333 ? -33.251 -10.175 -20.507 1.00 150.93 ? 353 MET   A CA  1 
ATOM   2234 C  C   . MET   A 1 333 ? -33.113 -11.578 -21.077 1.00 151.02 ? 353 MET   A C   1 
ATOM   2235 O  O   . MET   A 1 333 ? -32.443 -12.437 -20.499 1.00 143.52 ? 353 MET   A O   1 
ATOM   2236 C  CB  . MET   A 1 333 ? -31.918 -9.674  -19.964 1.00 143.90 ? 353 MET   A CB  1 
ATOM   2237 C  CG  . MET   A 1 333 ? -31.945 -8.236  -19.497 1.00 150.61 ? 353 MET   A CG  1 
ATOM   2238 S  SD  . MET   A 1 333 ? -30.360 -7.708  -18.829 1.00 156.67 ? 353 MET   A SD  1 
ATOM   2239 C  CE  . MET   A 1 333 ? -30.907 -6.639  -17.504 1.00 155.61 ? 353 MET   A CE  1 
ATOM   2240 N  N   . GLU   A 1 334 ? -33.748 -11.815 -22.223 1.00 138.33 ? 354 GLU   A N   1 
ATOM   2241 C  CA  . GLU   A 1 334 ? -33.670 -13.130 -22.842 1.00 129.92 ? 354 GLU   A CA  1 
ATOM   2242 C  C   . GLU   A 1 334 ? -32.332 -13.334 -23.542 1.00 122.34 ? 354 GLU   A C   1 
ATOM   2243 O  O   . GLU   A 1 334 ? -31.631 -14.312 -23.265 1.00 120.65 ? 354 GLU   A O   1 
ATOM   2244 C  CB  . GLU   A 1 334 ? -34.835 -13.325 -23.813 1.00 134.34 ? 354 GLU   A CB  1 
ATOM   2245 C  CG  . GLU   A 1 334 ? -36.188 -13.458 -23.128 1.00 146.95 ? 354 GLU   A CG  1 
ATOM   2246 C  CD  . GLU   A 1 334 ? -37.212 -14.163 -23.995 1.00 163.42 ? 354 GLU   A CD  1 
ATOM   2247 O  OE1 . GLU   A 1 334 ? -36.838 -15.138 -24.680 1.00 160.07 ? 354 GLU   A OE1 1 
ATOM   2248 O  OE2 . GLU   A 1 334 ? -38.389 -13.745 -23.990 1.00 164.14 ? 354 GLU   A OE2 1 
ATOM   2249 N  N   . TYR   A 1 335 ? -31.949 -12.408 -24.431 1.00 124.37 ? 355 TYR   A N   1 
ATOM   2250 C  CA  . TYR   A 1 335 ? -30.707 -12.566 -25.187 1.00 112.31 ? 355 TYR   A CA  1 
ATOM   2251 C  C   . TYR   A 1 335 ? -29.505 -12.767 -24.276 1.00 109.23 ? 355 TYR   A C   1 
ATOM   2252 O  O   . TYR   A 1 335 ? -28.546 -13.447 -24.657 1.00 112.48 ? 355 TYR   A O   1 
ATOM   2253 C  CB  . TYR   A 1 335 ? -30.474 -11.364 -26.105 1.00 111.70 ? 355 TYR   A CB  1 
ATOM   2254 C  CG  . TYR   A 1 335 ? -29.490 -11.632 -27.226 1.00 112.42 ? 355 TYR   A CG  1 
ATOM   2255 C  CD1 . TYR   A 1 335 ? -29.796 -12.514 -28.255 1.00 114.71 ? 355 TYR   A CD1 1 
ATOM   2256 C  CD2 . TYR   A 1 335 ? -28.255 -10.999 -27.257 1.00 115.86 ? 355 TYR   A CD2 1 
ATOM   2257 C  CE1 . TYR   A 1 335 ? -28.896 -12.759 -29.279 1.00 120.34 ? 355 TYR   A CE1 1 
ATOM   2258 C  CE2 . TYR   A 1 335 ? -27.350 -11.239 -28.272 1.00 111.73 ? 355 TYR   A CE2 1 
ATOM   2259 C  CZ  . TYR   A 1 335 ? -27.675 -12.116 -29.282 1.00 110.93 ? 355 TYR   A CZ  1 
ATOM   2260 O  OH  . TYR   A 1 335 ? -26.773 -12.350 -30.294 1.00 114.34 ? 355 TYR   A OH  1 
ATOM   2261 N  N   . LEU   A 1 336 ? -29.533 -12.193 -23.072 1.00 108.87 ? 356 LEU   A N   1 
ATOM   2262 C  CA  . LEU   A 1 336 ? -28.507 -12.528 -22.093 1.00 114.29 ? 356 LEU   A CA  1 
ATOM   2263 C  C   . LEU   A 1 336 ? -28.560 -14.013 -21.757 1.00 114.23 ? 356 LEU   A C   1 
ATOM   2264 O  O   . LEU   A 1 336 ? -27.560 -14.726 -21.893 1.00 97.43  ? 356 LEU   A O   1 
ATOM   2265 C  CB  . LEU   A 1 336 ? -28.664 -11.666 -20.840 1.00 109.30 ? 356 LEU   A CB  1 
ATOM   2266 C  CG  . LEU   A 1 336 ? -27.667 -11.941 -19.715 1.00 109.60 ? 356 LEU   A CG  1 
ATOM   2267 C  CD1 . LEU   A 1 336 ? -26.259 -11.626 -20.183 1.00 96.39  ? 356 LEU   A CD1 1 
ATOM   2268 C  CD2 . LEU   A 1 336 ? -28.011 -11.107 -18.494 1.00 120.37 ? 356 LEU   A CD2 1 
ATOM   2269 N  N   . ASP   A 1 337 ? -29.741 -14.505 -21.366 1.00 104.36 ? 357 ASP   A N   1 
ATOM   2270 C  CA  . ASP   A 1 337 ? -29.913 -15.927 -21.073 1.00 105.13 ? 357 ASP   A CA  1 
ATOM   2271 C  C   . ASP   A 1 337 ? -29.452 -16.809 -22.230 1.00 107.36 ? 357 ASP   A C   1 
ATOM   2272 O  O   . ASP   A 1 337 ? -28.840 -17.861 -22.011 1.00 89.72  ? 357 ASP   A O   1 
ATOM   2273 C  CB  . ASP   A 1 337 ? -31.379 -16.215 -20.740 1.00 106.00 ? 357 ASP   A CB  1 
ATOM   2274 C  CG  . ASP   A 1 337 ? -31.653 -17.692 -20.527 1.00 102.82 ? 357 ASP   A CG  1 
ATOM   2275 O  OD1 . ASP   A 1 337 ? -31.146 -18.257 -19.537 1.00 113.21 ? 357 ASP   A OD1 1 
ATOM   2276 O  OD2 . ASP   A 1 337 ? -32.374 -18.288 -21.356 1.00 105.32 ? 357 ASP   A OD2 1 
ATOM   2277 N  N   . MET   A 1 338 ? -29.737 -16.397 -23.470 1.00 104.15 ? 358 MET   A N   1 
ATOM   2278 C  CA  . MET   A 1 338 ? -29.310 -17.178 -24.629 1.00 101.21 ? 358 MET   A CA  1 
ATOM   2279 C  C   . MET   A 1 338 ? -27.792 -17.236 -24.737 1.00 101.38 ? 358 MET   A C   1 
ATOM   2280 O  O   . MET   A 1 338 ? -27.225 -18.291 -25.048 1.00 98.95  ? 358 MET   A O   1 
ATOM   2281 C  CB  . MET   A 1 338 ? -29.908 -16.595 -25.910 1.00 97.74  ? 358 MET   A CB  1 
ATOM   2282 C  CG  . MET   A 1 338 ? -31.263 -15.956 -25.725 1.00 102.97 ? 358 MET   A CG  1 
ATOM   2283 S  SD  . MET   A 1 338 ? -32.291 -16.024 -27.196 1.00 113.94 ? 358 MET   A SD  1 
ATOM   2284 C  CE  . MET   A 1 338 ? -33.839 -15.384 -26.565 1.00 130.90 ? 358 MET   A CE  1 
ATOM   2285 N  N   . VAL   A 1 339 ? -27.117 -16.111 -24.491 1.00 93.15  ? 359 VAL   A N   1 
ATOM   2286 C  CA  . VAL   A 1 339 ? -25.659 -16.085 -24.582 1.00 106.54 ? 359 VAL   A CA  1 
ATOM   2287 C  C   . VAL   A 1 339 ? -25.043 -16.979 -23.511 1.00 96.41  ? 359 VAL   A C   1 
ATOM   2288 O  O   . VAL   A 1 339 ? -24.124 -17.760 -23.785 1.00 97.03  ? 359 VAL   A O   1 
ATOM   2289 C  CB  . VAL   A 1 339 ? -25.140 -14.638 -24.484 1.00 103.41 ? 359 VAL   A CB  1 
ATOM   2290 C  CG1 . VAL   A 1 339 ? -23.725 -14.609 -23.924 1.00 93.97  ? 359 VAL   A CG1 1 
ATOM   2291 C  CG2 . VAL   A 1 339 ? -25.196 -13.961 -25.845 1.00 95.14  ? 359 VAL   A CG2 1 
ATOM   2292 N  N   . VAL   A 1 340 ? -25.545 -16.884 -22.275 1.00 93.03  ? 360 VAL   A N   1 
ATOM   2293 C  CA  . VAL   A 1 340 ? -25.036 -17.737 -21.200 1.00 99.47  ? 360 VAL   A CA  1 
ATOM   2294 C  C   . VAL   A 1 340 ? -25.203 -19.208 -21.555 1.00 96.87  ? 360 VAL   A C   1 
ATOM   2295 O  O   . VAL   A 1 340 ? -24.256 -19.997 -21.458 1.00 89.01  ? 360 VAL   A O   1 
ATOM   2296 C  CB  . VAL   A 1 340 ? -25.717 -17.405 -19.860 1.00 100.92 ? 360 VAL   A CB  1 
ATOM   2297 C  CG1 . VAL   A 1 340 ? -24.886 -17.946 -18.718 1.00 108.52 ? 360 VAL   A CG1 1 
ATOM   2298 C  CG2 . VAL   A 1 340 ? -25.865 -15.905 -19.694 1.00 106.93 ? 360 VAL   A CG2 1 
ATOM   2299 N  N   . ASN   A 1 341 ? -26.412 -19.601 -21.965 1.00 101.41 ? 361 ASN   A N   1 
ATOM   2300 C  CA  . ASN   A 1 341 ? -26.663 -21.004 -22.282 1.00 91.80  ? 361 ASN   A CA  1 
ATOM   2301 C  C   . ASN   A 1 341 ? -25.762 -21.492 -23.410 1.00 89.14  ? 361 ASN   A C   1 
ATOM   2302 O  O   . ASN   A 1 341 ? -25.209 -22.597 -23.338 1.00 85.60  ? 361 ASN   A O   1 
ATOM   2303 C  CB  . ASN   A 1 341 ? -28.131 -21.209 -22.652 1.00 93.07  ? 361 ASN   A CB  1 
ATOM   2304 C  CG  . ASN   A 1 341 ? -29.066 -20.987 -21.482 1.00 91.98  ? 361 ASN   A CG  1 
ATOM   2305 O  OD1 . ASN   A 1 341 ? -28.701 -21.212 -20.328 1.00 94.17  ? 361 ASN   A OD1 1 
ATOM   2306 N  ND2 . ASN   A 1 341 ? -30.286 -20.554 -21.776 1.00 86.11  ? 361 ASN   A ND2 1 
ATOM   2307 N  N   . GLU   A 1 342 ? -25.601 -20.684 -24.461 1.00 94.49  ? 362 GLU   A N   1 
ATOM   2308 C  CA  . GLU   A 1 342 ? -24.794 -21.111 -25.599 1.00 91.99  ? 362 GLU   A CA  1 
ATOM   2309 C  C   . GLU   A 1 342 ? -23.328 -21.263 -25.213 1.00 93.10  ? 362 GLU   A C   1 
ATOM   2310 O  O   . GLU   A 1 342 ? -22.641 -22.166 -25.707 1.00 99.57  ? 362 GLU   A O   1 
ATOM   2311 C  CB  . GLU   A 1 342 ? -24.952 -20.127 -26.759 1.00 90.92  ? 362 GLU   A CB  1 
ATOM   2312 C  CG  . GLU   A 1 342 ? -23.987 -20.349 -27.925 1.00 100.64 ? 362 GLU   A CG  1 
ATOM   2313 C  CD  . GLU   A 1 342 ? -24.284 -21.601 -28.746 1.00 97.81  ? 362 GLU   A CD  1 
ATOM   2314 O  OE1 . GLU   A 1 342 ? -24.993 -22.509 -28.262 1.00 98.79  ? 362 GLU   A OE1 1 
ATOM   2315 O  OE2 . GLU   A 1 342 ? -23.795 -21.678 -29.892 1.00 98.16  ? 362 GLU   A OE2 1 
ATOM   2316 N  N   . THR   A 1 343 ? -22.828 -20.392 -24.334 1.00 89.95  ? 363 THR   A N   1 
ATOM   2317 C  CA  . THR   A 1 343 ? -21.489 -20.590 -23.789 1.00 90.55  ? 363 THR   A CA  1 
ATOM   2318 C  C   . THR   A 1 343 ? -21.410 -21.902 -23.020 1.00 83.35  ? 363 THR   A C   1 
ATOM   2319 O  O   . THR   A 1 343 ? -20.482 -22.695 -23.213 1.00 70.17  ? 363 THR   A O   1 
ATOM   2320 C  CB  . THR   A 1 343 ? -21.101 -19.419 -22.885 1.00 88.55  ? 363 THR   A CB  1 
ATOM   2321 O  OG1 . THR   A 1 343 ? -21.634 -18.199 -23.415 1.00 98.57  ? 363 THR   A OG1 1 
ATOM   2322 C  CG2 . THR   A 1 343 ? -19.586 -19.311 -22.778 1.00 93.53  ? 363 THR   A CG2 1 
ATOM   2323 N  N   . LEU   A 1 344 ? -22.391 -22.152 -22.150 1.00 93.66  ? 364 LEU   A N   1 
ATOM   2324 C  CA  . LEU   A 1 344 ? -22.413 -23.386 -21.378 1.00 92.41  ? 364 LEU   A CA  1 
ATOM   2325 C  C   . LEU   A 1 344 ? -22.617 -24.615 -22.254 1.00 89.35  ? 364 LEU   A C   1 
ATOM   2326 O  O   . LEU   A 1 344 ? -22.256 -25.721 -21.837 1.00 85.38  ? 364 LEU   A O   1 
ATOM   2327 C  CB  . LEU   A 1 344 ? -23.500 -23.311 -20.305 1.00 86.40  ? 364 LEU   A CB  1 
ATOM   2328 C  CG  . LEU   A 1 344 ? -23.165 -22.372 -19.145 1.00 80.62  ? 364 LEU   A CG  1 
ATOM   2329 C  CD1 . LEU   A 1 344 ? -24.330 -22.262 -18.177 1.00 75.37  ? 364 LEU   A CD1 1 
ATOM   2330 C  CD2 . LEU   A 1 344 ? -21.906 -22.840 -18.429 1.00 65.51  ? 364 LEU   A CD2 1 
ATOM   2331 N  N   . ARG   A 1 345 ? -23.186 -24.452 -23.450 1.00 76.65  ? 365 ARG   A N   1 
ATOM   2332 C  CA  . ARG   A 1 345 ? -23.189 -25.551 -24.408 1.00 88.74  ? 365 ARG   A CA  1 
ATOM   2333 C  C   . ARG   A 1 345 ? -21.773 -25.857 -24.875 1.00 90.26  ? 365 ARG   A C   1 
ATOM   2334 O  O   . ARG   A 1 345 ? -21.337 -27.013 -24.860 1.00 82.81  ? 365 ARG   A O   1 
ATOM   2335 C  CB  . ARG   A 1 345 ? -24.083 -25.219 -25.605 1.00 85.75  ? 365 ARG   A CB  1 
ATOM   2336 C  CG  . ARG   A 1 345 ? -24.415 -26.431 -26.466 1.00 81.05  ? 365 ARG   A CG  1 
ATOM   2337 C  CD  . ARG   A 1 345 ? -24.884 -26.038 -27.859 1.00 84.39  ? 365 ARG   A CD  1 
ATOM   2338 N  NE  . ARG   A 1 345 ? -23.972 -25.106 -28.513 1.00 102.13 ? 365 ARG   A NE  1 
ATOM   2339 C  CZ  . ARG   A 1 345 ? -23.117 -25.443 -29.469 1.00 96.87  ? 365 ARG   A CZ  1 
ATOM   2340 N  NH1 . ARG   A 1 345 ? -23.011 -26.692 -29.893 1.00 99.16  ? 365 ARG   A NH1 1 
ATOM   2341 N  NH2 . ARG   A 1 345 ? -22.349 -24.504 -30.013 1.00 104.84 ? 365 ARG   A NH2 1 
ATOM   2342 N  N   . LEU   A 1 346 ? -21.034 -24.824 -25.279 1.00 92.05  ? 366 LEU   A N   1 
ATOM   2343 C  CA  . LEU   A 1 346 ? -19.674 -25.032 -25.761 1.00 93.22  ? 366 LEU   A CA  1 
ATOM   2344 C  C   . LEU   A 1 346 ? -18.719 -25.389 -24.631 1.00 89.58  ? 366 LEU   A C   1 
ATOM   2345 O  O   . LEU   A 1 346 ? -17.768 -26.149 -24.846 1.00 86.13  ? 366 LEU   A O   1 
ATOM   2346 C  CB  . LEU   A 1 346 ? -19.181 -23.785 -26.492 1.00 96.94  ? 366 LEU   A CB  1 
ATOM   2347 C  CG  . LEU   A 1 346 ? -19.692 -23.591 -27.918 1.00 100.82 ? 366 LEU   A CG  1 
ATOM   2348 C  CD1 . LEU   A 1 346 ? -19.202 -22.269 -28.485 1.00 113.79 ? 366 LEU   A CD1 1 
ATOM   2349 C  CD2 . LEU   A 1 346 ? -19.253 -24.750 -28.798 1.00 95.69  ? 366 LEU   A CD2 1 
ATOM   2350 N  N   . PHE   A 1 347 ? -18.950 -24.865 -23.430 1.00 92.67  ? 367 PHE   A N   1 
ATOM   2351 C  CA  . PHE   A 1 347 ? -18.017 -25.009 -22.314 1.00 90.74  ? 367 PHE   A CA  1 
ATOM   2352 C  C   . PHE   A 1 347 ? -18.748 -25.479 -21.062 1.00 89.34  ? 367 PHE   A C   1 
ATOM   2353 O  O   . PHE   A 1 347 ? -18.902 -24.724 -20.095 1.00 86.89  ? 367 PHE   A O   1 
ATOM   2354 C  CB  . PHE   A 1 347 ? -17.286 -23.691 -22.060 1.00 87.19  ? 367 PHE   A CB  1 
ATOM   2355 C  CG  . PHE   A 1 347 ? -16.622 -23.128 -23.282 1.00 89.60  ? 367 PHE   A CG  1 
ATOM   2356 C  CD1 . PHE   A 1 347 ? -15.678 -23.868 -23.975 1.00 98.88  ? 367 PHE   A CD1 1 
ATOM   2357 C  CD2 . PHE   A 1 347 ? -16.953 -21.867 -23.751 1.00 88.48  ? 367 PHE   A CD2 1 
ATOM   2358 C  CE1 . PHE   A 1 347 ? -15.068 -23.357 -25.104 1.00 88.89  ? 367 PHE   A CE1 1 
ATOM   2359 C  CE2 . PHE   A 1 347 ? -16.347 -21.350 -24.880 1.00 110.77 ? 367 PHE   A CE2 1 
ATOM   2360 C  CZ  . PHE   A 1 347 ? -15.403 -22.097 -25.558 1.00 98.17  ? 367 PHE   A CZ  1 
ATOM   2361 N  N   . PRO   A 1 348 ? -19.207 -26.737 -21.042 1.00 87.30  ? 368 PRO   A N   1 
ATOM   2362 C  CA  . PRO   A 1 348 ? -19.734 -27.297 -19.792 1.00 88.06  ? 368 PRO   A CA  1 
ATOM   2363 C  C   . PRO   A 1 348 ? -18.600 -27.688 -18.858 1.00 86.11  ? 368 PRO   A C   1 
ATOM   2364 O  O   . PRO   A 1 348 ? -17.950 -28.720 -19.053 1.00 94.79  ? 368 PRO   A O   1 
ATOM   2365 C  CB  . PRO   A 1 348 ? -20.542 -28.511 -20.264 1.00 93.05  ? 368 PRO   A CB  1 
ATOM   2366 C  CG  . PRO   A 1 348 ? -19.860 -28.943 -21.519 1.00 89.80  ? 368 PRO   A CG  1 
ATOM   2367 C  CD  . PRO   A 1 348 ? -19.238 -27.717 -22.144 1.00 89.56  ? 368 PRO   A CD  1 
ATOM   2368 N  N   . ILE   A 1 349 ? -18.361 -26.862 -17.835 1.00 91.01  ? 369 ILE   A N   1 
ATOM   2369 C  CA  . ILE   A 1 349 ? -17.171 -26.994 -17.000 1.00 92.60  ? 369 ILE   A CA  1 
ATOM   2370 C  C   . ILE   A 1 349 ? -17.079 -28.352 -16.317 1.00 81.02  ? 369 ILE   A C   1 
ATOM   2371 O  O   . ILE   A 1 349 ? -15.990 -28.756 -15.895 1.00 102.31 ? 369 ILE   A O   1 
ATOM   2372 C  CB  . ILE   A 1 349 ? -17.136 -25.861 -15.956 1.00 87.74  ? 369 ILE   A CB  1 
ATOM   2373 C  CG1 . ILE   A 1 349 ? -18.544 -25.585 -15.429 1.00 79.73  ? 369 ILE   A CG1 1 
ATOM   2374 C  CG2 . ILE   A 1 349 ? -16.540 -24.599 -16.560 1.00 90.59  ? 369 ILE   A CG2 1 
ATOM   2375 C  CD1 . ILE   A 1 349 ? -18.568 -24.738 -14.184 1.00 87.67  ? 369 ILE   A CD1 1 
ATOM   2376 N  N   . ALA   A 1 350 ? -18.204 -29.059 -16.166 1.00 84.98  ? 370 ALA   A N   1 
ATOM   2377 C  CA  . ALA   A 1 350 ? -18.186 -30.405 -15.536 1.00 85.44  ? 370 ALA   A CA  1 
ATOM   2378 C  C   . ALA   A 1 350 ? -17.774 -31.527 -16.489 1.00 82.21  ? 370 ALA   A C   1 
ATOM   2379 O  O   . ALA   A 1 350 ? -17.292 -32.561 -15.984 1.00 79.00  ? 370 ALA   A O   1 
ATOM   2380 C  CB  . ALA   A 1 350 ? -19.579 -30.795 -15.111 1.00 77.71  ? 370 ALA   A CB  1 
ATOM   2381 N  N   . MET   A 1 351 ? -17.997 -31.347 -17.792 1.00 73.44  ? 371 MET   A N   1 
ATOM   2382 C  CA  . MET   A 1 351 ? -17.494 -32.193 -18.870 1.00 89.67  ? 371 MET   A CA  1 
ATOM   2383 C  C   . MET   A 1 351 ? -18.308 -33.484 -18.843 1.00 86.26  ? 371 MET   A C   1 
ATOM   2384 O  O   . MET   A 1 351 ? -18.812 -33.925 -19.882 1.00 75.45  ? 371 MET   A O   1 
ATOM   2385 C  CB  . MET   A 1 351 ? -15.973 -32.342 -18.772 1.00 99.03  ? 371 MET   A CB  1 
ATOM   2386 C  CG  . MET   A 1 351 ? -15.199 -31.407 -19.669 1.00 106.38 ? 371 MET   A CG  1 
ATOM   2387 S  SD  . MET   A 1 351 ? -13.422 -31.530 -19.390 1.00 143.93 ? 371 MET   A SD  1 
ATOM   2388 C  CE  . MET   A 1 351 ? -13.349 -31.436 -17.606 1.00 125.77 ? 371 MET   A CE  1 
ATOM   2389 N  N   . ARG   A 1 352 ? -18.442 -34.094 -17.665 1.00 82.31  ? 372 ARG   A N   1 
ATOM   2390 C  CA  . ARG   A 1 352 ? -19.110 -35.381 -17.523 1.00 74.27  ? 372 ARG   A CA  1 
ATOM   2391 C  C   . ARG   A 1 352 ? -20.101 -35.394 -16.368 1.00 69.88  ? 372 ARG   A C   1 
ATOM   2392 O  O   . ARG   A 1 352 ? -20.063 -34.538 -15.481 1.00 76.75  ? 372 ARG   A O   1 
ATOM   2393 C  CB  . ARG   A 1 352 ? -18.014 -36.425 -17.261 1.00 80.90  ? 372 ARG   A CB  1 
ATOM   2394 C  CG  . ARG   A 1 352 ? -17.002 -36.622 -18.378 1.00 90.28  ? 372 ARG   A CG  1 
ATOM   2395 C  CD  . ARG   A 1 352 ? -16.188 -37.873 -18.120 1.00 98.32  ? 372 ARG   A CD  1 
ATOM   2396 N  NE  . ARG   A 1 352 ? -15.504 -38.362 -19.311 1.00 93.26  ? 372 ARG   A NE  1 
ATOM   2397 C  CZ  . ARG   A 1 352 ? -14.615 -39.346 -19.307 1.00 93.83  ? 372 ARG   A CZ  1 
ATOM   2398 N  NH1 . ARG   A 1 352 ? -14.285 -39.974 -18.190 1.00 100.79 ? 372 ARG   A NH1 1 
ATOM   2399 N  NH2 . ARG   A 1 352 ? -14.048 -39.714 -20.452 1.00 105.49 ? 372 ARG   A NH2 1 
ATOM   2400 N  N   . LEU   A 1 353 ? -20.987 -36.387 -16.389 1.00 70.40  ? 373 LEU   A N   1 
ATOM   2401 C  CA  . LEU   A 1 353 ? -21.853 -36.708 -15.263 1.00 73.22  ? 373 LEU   A CA  1 
ATOM   2402 C  C   . LEU   A 1 353 ? -21.719 -38.192 -14.960 1.00 71.49  ? 373 LEU   A C   1 
ATOM   2403 O  O   . LEU   A 1 353 ? -21.716 -39.019 -15.875 1.00 70.98  ? 373 LEU   A O   1 
ATOM   2404 C  CB  . LEU   A 1 353 ? -23.319 -36.352 -15.545 1.00 77.88  ? 373 LEU   A CB  1 
ATOM   2405 C  CG  . LEU   A 1 353 ? -23.589 -34.928 -16.032 1.00 80.56  ? 373 LEU   A CG  1 
ATOM   2406 C  CD1 . LEU   A 1 353 ? -24.994 -34.807 -16.603 1.00 76.39  ? 373 LEU   A CD1 1 
ATOM   2407 C  CD2 . LEU   A 1 353 ? -23.379 -33.937 -14.900 1.00 59.31  ? 373 LEU   A CD2 1 
ATOM   2408 N  N   . GLU   A 1 354 ? -21.604 -38.526 -13.676 1.00 63.83  ? 374 GLU   A N   1 
ATOM   2409 C  CA  . GLU   A 1 354 ? -21.296 -39.886 -13.258 1.00 70.02  ? 374 GLU   A CA  1 
ATOM   2410 C  C   . GLU   A 1 354 ? -22.213 -40.325 -12.127 1.00 71.37  ? 374 GLU   A C   1 
ATOM   2411 O  O   . GLU   A 1 354 ? -22.528 -39.541 -11.227 1.00 73.08  ? 374 GLU   A O   1 
ATOM   2412 C  CB  . GLU   A 1 354 ? -19.836 -40.007 -12.806 1.00 77.96  ? 374 GLU   A CB  1 
ATOM   2413 C  CG  . GLU   A 1 354 ? -18.828 -40.053 -13.940 1.00 81.77  ? 374 GLU   A CG  1 
ATOM   2414 C  CD  . GLU   A 1 354 ? -17.398 -40.064 -13.440 1.00 93.11  ? 374 GLU   A CD  1 
ATOM   2415 O  OE1 . GLU   A 1 354 ? -17.199 -40.068 -12.207 1.00 100.07 ? 374 GLU   A OE1 1 
ATOM   2416 O  OE2 . GLU   A 1 354 ? -16.472 -40.069 -14.278 1.00 92.44  ? 374 GLU   A OE2 1 
ATOM   2417 N  N   . ARG   A 1 355 ? -22.633 -41.588 -12.184 1.00 67.17  ? 375 ARG   A N   1 
ATOM   2418 C  CA  . ARG   A 1 355 ? -23.367 -42.232 -11.105 1.00 85.29  ? 375 ARG   A CA  1 
ATOM   2419 C  C   . ARG   A 1 355 ? -22.859 -43.656 -10.943 1.00 78.01  ? 375 ARG   A C   1 
ATOM   2420 O  O   . ARG   A 1 355 ? -22.658 -44.365 -11.932 1.00 69.54  ? 375 ARG   A O   1 
ATOM   2421 C  CB  . ARG   A 1 355 ? -24.880 -42.268 -11.367 1.00 77.57  ? 375 ARG   A CB  1 
ATOM   2422 C  CG  . ARG   A 1 355 ? -25.543 -40.922 -11.586 1.00 75.18  ? 375 ARG   A CG  1 
ATOM   2423 C  CD  . ARG   A 1 355 ? -25.746 -40.181 -10.275 1.00 73.04  ? 375 ARG   A CD  1 
ATOM   2424 N  NE  . ARG   A 1 355 ? -26.460 -38.927 -10.477 1.00 84.85  ? 375 ARG   A NE  1 
ATOM   2425 C  CZ  . ARG   A 1 355 ? -25.921 -37.829 -10.989 1.00 83.57  ? 375 ARG   A CZ  1 
ATOM   2426 N  NH1 . ARG   A 1 355 ? -24.650 -37.788 -11.352 1.00 89.63  ? 375 ARG   A NH1 1 
ATOM   2427 N  NH2 . ARG   A 1 355 ? -26.678 -36.747 -11.143 1.00 63.60  ? 375 ARG   A NH2 1 
ATOM   2428 N  N   . VAL   A 1 356 ? -22.653 -44.070 -9.697  1.00 79.35  ? 376 VAL   A N   1 
ATOM   2429 C  CA  . VAL   A 1 356 ? -22.338 -45.465 -9.407  1.00 86.65  ? 376 VAL   A CA  1 
ATOM   2430 C  C   . VAL   A 1 356 ? -23.640 -46.250 -9.327  1.00 85.04  ? 376 VAL   A C   1 
ATOM   2431 O  O   . VAL   A 1 356 ? -24.489 -45.982 -8.471  1.00 77.43  ? 376 VAL   A O   1 
ATOM   2432 C  CB  . VAL   A 1 356 ? -21.528 -45.603 -8.111  1.00 83.74  ? 376 VAL   A CB  1 
ATOM   2433 C  CG1 . VAL   A 1 356 ? -21.322 -47.071 -7.781  1.00 71.14  ? 376 VAL   A CG1 1 
ATOM   2434 C  CG2 . VAL   A 1 356 ? -20.184 -44.926 -8.265  1.00 74.52  ? 376 VAL   A CG2 1 
ATOM   2435 N  N   . CYS   A 1 357 ? -23.801 -47.215 -10.228 1.00 88.69  ? 377 CYS   A N   1 
ATOM   2436 C  CA  . CYS   A 1 357 ? -24.966 -48.091 -10.215 1.00 93.76  ? 377 CYS   A CA  1 
ATOM   2437 C  C   . CYS   A 1 357 ? -24.828 -49.080 -9.065  1.00 88.05  ? 377 CYS   A C   1 
ATOM   2438 O  O   . CYS   A 1 357 ? -23.985 -49.982 -9.111  1.00 84.02  ? 377 CYS   A O   1 
ATOM   2439 C  CB  . CYS   A 1 357 ? -25.090 -48.811 -11.552 1.00 90.28  ? 377 CYS   A CB  1 
ATOM   2440 S  SG  . CYS   A 1 357 ? -26.075 -50.306 -11.478 1.00 93.48  ? 377 CYS   A SG  1 
ATOM   2441 N  N   . LYS   A 1 358 ? -25.658 -48.925 -8.036  1.00 83.80  ? 378 LYS   A N   1 
ATOM   2442 C  CA  . LYS   A 1 358 ? -25.446 -49.615 -6.771  1.00 98.49  ? 378 LYS   A CA  1 
ATOM   2443 C  C   . LYS   A 1 358 ? -26.164 -50.961 -6.672  1.00 104.60 ? 378 LYS   A C   1 
ATOM   2444 O  O   . LYS   A 1 358 ? -26.149 -51.570 -5.597  1.00 95.12  ? 378 LYS   A O   1 
ATOM   2445 C  CB  . LYS   A 1 358 ? -25.856 -48.709 -5.604  1.00 85.59  ? 378 LYS   A CB  1 
ATOM   2446 C  CG  . LYS   A 1 358 ? -27.350 -48.511 -5.430  1.00 100.43 ? 378 LYS   A CG  1 
ATOM   2447 C  CD  . LYS   A 1 358 ? -27.643 -47.867 -4.084  1.00 96.19  ? 378 LYS   A CD  1 
ATOM   2448 C  CE  . LYS   A 1 358 ? -27.849 -46.369 -4.227  1.00 99.21  ? 378 LYS   A CE  1 
ATOM   2449 N  NZ  . LYS   A 1 358 ? -29.002 -45.877 -3.422  1.00 97.52  ? 378 LYS   A NZ  1 
ATOM   2450 N  N   . LYS   A 1 359 ? -26.779 -51.442 -7.754  1.00 97.12  ? 379 LYS   A N   1 
ATOM   2451 C  CA  . LYS   A 1 359 ? -27.288 -52.810 -7.800  1.00 96.69  ? 379 LYS   A CA  1 
ATOM   2452 C  C   . LYS   A 1 359 ? -27.634 -53.169 -9.239  1.00 105.94 ? 379 LYS   A C   1 
ATOM   2453 O  O   . LYS   A 1 359 ? -27.792 -52.295 -10.093 1.00 105.50 ? 379 LYS   A O   1 
ATOM   2454 C  CB  . LYS   A 1 359 ? -28.514 -53.012 -6.897  1.00 98.90  ? 379 LYS   A CB  1 
ATOM   2455 C  CG  . LYS   A 1 359 ? -29.743 -52.196 -7.267  1.00 103.82 ? 379 LYS   A CG  1 
ATOM   2456 C  CD  . LYS   A 1 359 ? -30.780 -52.269 -6.151  1.00 105.52 ? 379 LYS   A CD  1 
ATOM   2457 C  CE  . LYS   A 1 359 ? -32.115 -51.674 -6.572  1.00 107.90 ? 379 LYS   A CE  1 
ATOM   2458 N  NZ  . LYS   A 1 359 ? -33.029 -51.492 -5.409  1.00 115.22 ? 379 LYS   A NZ  1 
ATOM   2459 N  N   . ASP   A 1 360 ? -27.757 -54.474 -9.489  1.00 111.72 ? 380 ASP   A N   1 
ATOM   2460 C  CA  . ASP   A 1 360 ? -28.115 -54.966 -10.816 1.00 102.45 ? 380 ASP   A CA  1 
ATOM   2461 C  C   . ASP   A 1 360 ? -29.428 -54.351 -11.288 1.00 103.50 ? 380 ASP   A C   1 
ATOM   2462 O  O   . ASP   A 1 360 ? -30.375 -54.186 -10.517 1.00 108.64 ? 380 ASP   A O   1 
ATOM   2463 C  CB  . ASP   A 1 360 ? -28.235 -56.492 -10.813 1.00 99.93  ? 380 ASP   A CB  1 
ATOM   2464 C  CG  . ASP   A 1 360 ? -26.890 -57.189 -10.860 1.00 113.44 ? 380 ASP   A CG  1 
ATOM   2465 O  OD1 . ASP   A 1 360 ? -25.870 -56.560 -10.514 1.00 114.18 ? 380 ASP   A OD1 1 
ATOM   2466 O  OD2 . ASP   A 1 360 ? -26.856 -58.372 -11.260 1.00 124.46 ? 380 ASP   A OD2 1 
ATOM   2467 N  N   . VAL   A 1 361 ? -29.481 -54.036 -12.584 1.00 108.16 ? 381 VAL   A N   1 
ATOM   2468 C  CA  . VAL   A 1 361 ? -30.574 -53.273 -13.181 1.00 117.30 ? 381 VAL   A CA  1 
ATOM   2469 C  C   . VAL   A 1 361 ? -30.630 -53.474 -14.692 1.00 121.70 ? 381 VAL   A C   1 
ATOM   2470 O  O   . VAL   A 1 361 ? -29.598 -53.662 -15.346 1.00 114.17 ? 381 VAL   A O   1 
ATOM   2471 C  CB  . VAL   A 1 361 ? -30.439 -51.779 -12.819 1.00 120.74 ? 381 VAL   A CB  1 
ATOM   2472 C  CG1 . VAL   A 1 361 ? -31.019 -50.926 -13.880 1.00 122.22 ? 381 VAL   A CG1 1 
ATOM   2473 C  CG2 . VAL   A 1 361 ? -31.192 -51.482 -11.543 1.00 116.79 ? 381 VAL   A CG2 1 
ATOM   2474 N  N   . GLU   A 1 362 ? -31.843 -53.448 -15.249 1.00 143.56 ? 382 GLU   A N   1 
ATOM   2475 C  CA  . GLU   A 1 362 ? -32.085 -53.421 -16.691 1.00 144.43 ? 382 GLU   A CA  1 
ATOM   2476 C  C   . GLU   A 1 362 ? -32.877 -52.152 -17.010 1.00 142.22 ? 382 GLU   A C   1 
ATOM   2477 O  O   . GLU   A 1 362 ? -34.093 -52.109 -16.800 1.00 148.31 ? 382 GLU   A O   1 
ATOM   2478 C  CB  . GLU   A 1 362 ? -32.848 -54.670 -17.133 1.00 149.92 ? 382 GLU   A CB  1 
ATOM   2479 C  CG  . GLU   A 1 362 ? -32.916 -54.915 -18.642 1.00 150.16 ? 382 GLU   A CG  1 
ATOM   2480 C  CD  . GLU   A 1 362 ? -32.749 -56.387 -19.008 1.00 163.80 ? 382 GLU   A CD  1 
ATOM   2481 O  OE1 . GLU   A 1 362 ? -33.057 -57.249 -18.158 1.00 171.93 ? 382 GLU   A OE1 1 
ATOM   2482 O  OE2 . GLU   A 1 362 ? -32.331 -56.687 -20.147 1.00 167.02 ? 382 GLU   A OE2 1 
ATOM   2483 N  N   . ILE   A 1 363 ? -32.204 -51.120 -17.517 1.00 135.42 ? 383 ILE   A N   1 
ATOM   2484 C  CA  . ILE   A 1 363 ? -32.855 -49.892 -17.970 1.00 129.46 ? 383 ILE   A CA  1 
ATOM   2485 C  C   . ILE   A 1 363 ? -32.912 -49.868 -19.491 1.00 130.72 ? 383 ILE   A C   1 
ATOM   2486 O  O   . ILE   A 1 363 ? -31.940 -50.227 -20.168 1.00 128.48 ? 383 ILE   A O   1 
ATOM   2487 C  CB  . ILE   A 1 363 ? -32.167 -48.628 -17.413 1.00 132.66 ? 383 ILE   A CB  1 
ATOM   2488 C  CG1 . ILE   A 1 363 ? -30.851 -48.323 -18.133 1.00 116.02 ? 383 ILE   A CG1 1 
ATOM   2489 C  CG2 . ILE   A 1 363 ? -32.074 -48.643 -15.915 1.00 130.02 ? 383 ILE   A CG2 1 
ATOM   2490 C  CD1 . ILE   A 1 363 ? -29.984 -47.342 -17.391 1.00 92.21  ? 383 ILE   A CD1 1 
ATOM   2491 N  N   . ASN   A 1 364 ? -34.077 -49.476 -20.016 1.00 124.13 ? 384 ASN   A N   1 
ATOM   2492 C  CA  . ASN   A 1 364 ? -34.290 -49.208 -21.438 1.00 124.85 ? 384 ASN   A CA  1 
ATOM   2493 C  C   . ASN   A 1 364 ? -33.686 -50.296 -22.322 1.00 133.59 ? 384 ASN   A C   1 
ATOM   2494 O  O   . ASN   A 1 364 ? -33.056 -50.020 -23.345 1.00 135.36 ? 384 ASN   A O   1 
ATOM   2495 C  CB  . ASN   A 1 364 ? -33.749 -47.829 -21.813 1.00 124.29 ? 384 ASN   A CB  1 
ATOM   2496 C  CG  . ASN   A 1 364 ? -34.601 -46.701 -21.259 1.00 117.81 ? 384 ASN   A CG  1 
ATOM   2497 O  OD1 . ASN   A 1 364 ? -34.319 -46.162 -20.188 1.00 116.91 ? 384 ASN   A OD1 1 
ATOM   2498 N  ND2 . ASN   A 1 364 ? -35.659 -46.349 -21.981 1.00 122.55 ? 384 ASN   A ND2 1 
ATOM   2499 N  N   . GLY   A 1 365 ? -33.873 -51.548 -21.914 1.00 135.21 ? 385 GLY   A N   1 
ATOM   2500 C  CA  . GLY   A 1 365 ? -33.438 -52.676 -22.709 1.00 132.26 ? 385 GLY   A CA  1 
ATOM   2501 C  C   . GLY   A 1 365 ? -31.978 -53.047 -22.585 1.00 133.24 ? 385 GLY   A C   1 
ATOM   2502 O  O   . GLY   A 1 365 ? -31.517 -53.913 -23.336 1.00 132.14 ? 385 GLY   A O   1 
ATOM   2503 N  N   . MET   A 1 366 ? -31.232 -52.429 -21.673 1.00 139.08 ? 386 MET   A N   1 
ATOM   2504 C  CA  . MET   A 1 366 ? -29.830 -52.768 -21.456 1.00 133.50 ? 386 MET   A CA  1 
ATOM   2505 C  C   . MET   A 1 366 ? -29.596 -53.136 -20.001 1.00 129.34 ? 386 MET   A C   1 
ATOM   2506 O  O   . MET   A 1 366 ? -29.891 -52.346 -19.098 1.00 126.97 ? 386 MET   A O   1 
ATOM   2507 C  CB  . MET   A 1 366 ? -28.899 -51.627 -21.867 1.00 131.14 ? 386 MET   A CB  1 
ATOM   2508 C  CG  . MET   A 1 366 ? -27.435 -52.048 -21.869 1.00 126.74 ? 386 MET   A CG  1 
ATOM   2509 S  SD  . MET   A 1 366 ? -26.328 -50.942 -22.754 1.00 136.85 ? 386 MET   A SD  1 
ATOM   2510 C  CE  . MET   A 1 366 ? -27.388 -49.520 -22.948 1.00 133.96 ? 386 MET   A CE  1 
ATOM   2511 N  N   . PHE   A 1 367 ? -29.054 -54.330 -19.784 1.00 117.50 ? 387 PHE   A N   1 
ATOM   2512 C  CA  . PHE   A 1 367 ? -28.669 -54.751 -18.447 1.00 113.07 ? 387 PHE   A CA  1 
ATOM   2513 C  C   . PHE   A 1 367 ? -27.404 -54.023 -18.012 1.00 112.46 ? 387 PHE   A C   1 
ATOM   2514 O  O   . PHE   A 1 367 ? -26.518 -53.741 -18.823 1.00 118.15 ? 387 PHE   A O   1 
ATOM   2515 C  CB  . PHE   A 1 367 ? -28.452 -56.263 -18.412 1.00 107.84 ? 387 PHE   A CB  1 
ATOM   2516 C  CG  . PHE   A 1 367 ? -27.752 -56.745 -17.176 1.00 108.23 ? 387 PHE   A CG  1 
ATOM   2517 C  CD1 . PHE   A 1 367 ? -28.445 -56.901 -15.988 1.00 110.41 ? 387 PHE   A CD1 1 
ATOM   2518 C  CD2 . PHE   A 1 367 ? -26.401 -57.047 -17.202 1.00 100.16 ? 387 PHE   A CD2 1 
ATOM   2519 C  CE1 . PHE   A 1 367 ? -27.801 -57.343 -14.848 1.00 114.64 ? 387 PHE   A CE1 1 
ATOM   2520 C  CE2 . PHE   A 1 367 ? -25.752 -57.490 -16.068 1.00 108.02 ? 387 PHE   A CE2 1 
ATOM   2521 C  CZ  . PHE   A 1 367 ? -26.453 -57.639 -14.888 1.00 109.34 ? 387 PHE   A CZ  1 
ATOM   2522 N  N   . ILE   A 1 368 ? -27.326 -53.716 -16.722 1.00 114.06 ? 388 ILE   A N   1 
ATOM   2523 C  CA  . ILE   A 1 368 ? -26.184 -52.995 -16.170 1.00 105.87 ? 388 ILE   A CA  1 
ATOM   2524 C  C   . ILE   A 1 368 ? -25.849 -53.636 -14.828 1.00 97.93  ? 388 ILE   A C   1 
ATOM   2525 O  O   . ILE   A 1 368 ? -26.725 -53.733 -13.955 1.00 104.71 ? 388 ILE   A O   1 
ATOM   2526 C  CB  . ILE   A 1 368 ? -26.492 -51.496 -16.027 1.00 114.75 ? 388 ILE   A CB  1 
ATOM   2527 C  CG1 . ILE   A 1 368 ? -26.151 -50.755 -17.314 1.00 111.65 ? 388 ILE   A CG1 1 
ATOM   2528 C  CG2 . ILE   A 1 368 ? -25.677 -50.881 -14.907 1.00 107.87 ? 388 ILE   A CG2 1 
ATOM   2529 C  CD1 . ILE   A 1 368 ? -26.729 -49.360 -17.358 1.00 102.89 ? 388 ILE   A CD1 1 
ATOM   2530 N  N   . PRO   A 1 369 ? -24.621 -54.099 -14.620 1.00 101.15 ? 389 PRO   A N   1 
ATOM   2531 C  CA  . PRO   A 1 369 ? -24.299 -54.803 -13.378 1.00 104.40 ? 389 PRO   A CA  1 
ATOM   2532 C  C   . PRO   A 1 369 ? -23.922 -53.855 -12.250 1.00 100.80 ? 389 PRO   A C   1 
ATOM   2533 O  O   . PRO   A 1 369 ? -23.510 -52.713 -12.467 1.00 99.92  ? 389 PRO   A O   1 
ATOM   2534 C  CB  . PRO   A 1 369 ? -23.110 -55.692 -13.771 1.00 91.74  ? 389 PRO   A CB  1 
ATOM   2535 C  CG  . PRO   A 1 369 ? -22.625 -55.179 -15.121 1.00 101.12 ? 389 PRO   A CG  1 
ATOM   2536 C  CD  . PRO   A 1 369 ? -23.457 -53.993 -15.512 1.00 103.01 ? 389 PRO   A CD  1 
ATOM   2537 N  N   . LYS   A 1 370 ? -24.082 -54.360 -11.026 1.00 98.64  ? 390 LYS   A N   1 
ATOM   2538 C  CA  . LYS   A 1 370 ? -23.713 -53.614 -9.829  1.00 91.09  ? 390 LYS   A CA  1 
ATOM   2539 C  C   . LYS   A 1 370 ? -22.267 -53.141 -9.898  1.00 98.10  ? 390 LYS   A C   1 
ATOM   2540 O  O   . LYS   A 1 370 ? -21.379 -53.868 -10.351 1.00 89.97  ? 390 LYS   A O   1 
ATOM   2541 C  CB  . LYS   A 1 370 ? -23.916 -54.493 -8.591  1.00 92.64  ? 390 LYS   A CB  1 
ATOM   2542 C  CG  . LYS   A 1 370 ? -23.214 -53.986 -7.339  1.00 92.03  ? 390 LYS   A CG  1 
ATOM   2543 C  CD  . LYS   A 1 370 ? -23.697 -54.694 -6.087  1.00 109.98 ? 390 LYS   A CD  1 
ATOM   2544 C  CE  . LYS   A 1 370 ? -23.244 -53.956 -4.837  1.00 117.46 ? 390 LYS   A CE  1 
ATOM   2545 N  NZ  . LYS   A 1 370 ? -23.434 -54.773 -3.607  1.00 114.79 ? 390 LYS   A NZ  1 
ATOM   2546 N  N   . GLY   A 1 371 ? -22.037 -51.906 -9.452  1.00 97.80  ? 391 GLY   A N   1 
ATOM   2547 C  CA  . GLY   A 1 371 ? -20.705 -51.364 -9.320  1.00 95.48  ? 391 GLY   A CA  1 
ATOM   2548 C  C   . GLY   A 1 371 ? -20.189 -50.608 -10.526 1.00 91.54  ? 391 GLY   A C   1 
ATOM   2549 O  O   . GLY   A 1 371 ? -19.216 -49.857 -10.396 1.00 91.56  ? 391 GLY   A O   1 
ATOM   2550 N  N   . VAL   A 1 372 ? -20.806 -50.785 -11.694 1.00 87.46  ? 392 VAL   A N   1 
ATOM   2551 C  CA  . VAL   A 1 372 ? -20.363 -50.081 -12.891 1.00 86.63  ? 392 VAL   A CA  1 
ATOM   2552 C  C   . VAL   A 1 372 ? -20.642 -48.592 -12.741 1.00 84.54  ? 392 VAL   A C   1 
ATOM   2553 O  O   . VAL   A 1 372 ? -21.677 -48.184 -12.197 1.00 84.75  ? 392 VAL   A O   1 
ATOM   2554 C  CB  . VAL   A 1 372 ? -21.057 -50.661 -14.136 1.00 86.63  ? 392 VAL   A CB  1 
ATOM   2555 C  CG1 . VAL   A 1 372 ? -20.791 -49.796 -15.363 1.00 69.15  ? 392 VAL   A CG1 1 
ATOM   2556 C  CG2 . VAL   A 1 372 ? -20.593 -52.085 -14.380 1.00 99.65  ? 392 VAL   A CG2 1 
ATOM   2557 N  N   . VAL   A 1 373 ? -19.706 -47.770 -13.207 1.00 82.32  ? 393 VAL   A N   1 
ATOM   2558 C  CA  . VAL   A 1 373 ? -19.879 -46.323 -13.222 1.00 74.73  ? 393 VAL   A CA  1 
ATOM   2559 C  C   . VAL   A 1 373 ? -20.562 -45.948 -14.532 1.00 66.88  ? 393 VAL   A C   1 
ATOM   2560 O  O   . VAL   A 1 373 ? -19.969 -46.055 -15.608 1.00 69.71  ? 393 VAL   A O   1 
ATOM   2561 C  CB  . VAL   A 1 373 ? -18.542 -45.591 -13.062 1.00 85.00  ? 393 VAL   A CB  1 
ATOM   2562 C  CG1 . VAL   A 1 373 ? -18.703 -44.114 -13.390 1.00 72.96  ? 393 VAL   A CG1 1 
ATOM   2563 C  CG2 . VAL   A 1 373 ? -18.011 -45.764 -11.649 1.00 71.74  ? 393 VAL   A CG2 1 
ATOM   2564 N  N   . VAL   A 1 374 ? -21.817 -45.526 -14.444 1.00 70.45  ? 394 VAL   A N   1 
ATOM   2565 C  CA  . VAL   A 1 374 ? -22.525 -45.003 -15.606 1.00 75.86  ? 394 VAL   A CA  1 
ATOM   2566 C  C   . VAL   A 1 374 ? -22.113 -43.553 -15.806 1.00 75.81  ? 394 VAL   A C   1 
ATOM   2567 O  O   . VAL   A 1 374 ? -21.994 -42.785 -14.843 1.00 79.02  ? 394 VAL   A O   1 
ATOM   2568 C  CB  . VAL   A 1 374 ? -24.045 -45.151 -15.426 1.00 79.00  ? 394 VAL   A CB  1 
ATOM   2569 C  CG1 . VAL   A 1 374 ? -24.774 -44.673 -16.666 1.00 77.04  ? 394 VAL   A CG1 1 
ATOM   2570 C  CG2 . VAL   A 1 374 ? -24.396 -46.600 -15.128 1.00 75.93  ? 394 VAL   A CG2 1 
ATOM   2571 N  N   . MET   A 1 375 ? -21.888 -43.169 -17.059 1.00 71.98  ? 395 MET   A N   1 
ATOM   2572 C  CA  A MET   A 1 375 ? -21.324 -41.865 -17.378 0.56 90.01  ? 395 MET   A CA  1 
ATOM   2573 C  CA  B MET   A 1 375 ? -21.334 -41.862 -17.367 0.44 100.01 ? 395 MET   A CA  1 
ATOM   2574 C  C   . MET   A 1 375 ? -22.102 -41.230 -18.519 1.00 80.92  ? 395 MET   A C   1 
ATOM   2575 O  O   . MET   A 1 375 ? -22.532 -41.922 -19.446 1.00 87.18  ? 395 MET   A O   1 
ATOM   2576 C  CB  A MET   A 1 375 ? -19.837 -41.985 -17.753 0.56 86.43  ? 395 MET   A CB  1 
ATOM   2577 C  CB  B MET   A 1 375 ? -19.850 -41.984 -17.716 0.44 85.78  ? 395 MET   A CB  1 
ATOM   2578 C  CG  A MET   A 1 375 ? -19.131 -40.660 -18.013 0.56 78.84  ? 395 MET   A CG  1 
ATOM   2579 C  CG  B MET   A 1 375 ? -19.094 -40.681 -17.763 0.44 79.27  ? 395 MET   A CG  1 
ATOM   2580 S  SD  A MET   A 1 375 ? -19.172 -40.160 -19.746 0.56 71.75  ? 395 MET   A SD  1 
ATOM   2581 S  SD  B MET   A 1 375 ? -17.501 -40.959 -18.547 0.44 82.26  ? 395 MET   A SD  1 
ATOM   2582 C  CE  A MET   A 1 375 ? -17.864 -41.174 -20.429 0.56 84.23  ? 395 MET   A CE  1 
ATOM   2583 C  CE  B MET   A 1 375 ? -17.983 -40.963 -20.271 0.44 83.67  ? 395 MET   A CE  1 
ATOM   2584 N  N   . ILE   A 1 376 ? -22.274 -39.913 -18.445 1.00 74.03  ? 396 ILE   A N   1 
ATOM   2585 C  CA  . ILE   A 1 376 ? -22.950 -39.140 -19.486 1.00 83.52  ? 396 ILE   A CA  1 
ATOM   2586 C  C   . ILE   A 1 376 ? -21.954 -38.135 -20.057 1.00 77.69  ? 396 ILE   A C   1 
ATOM   2587 O  O   . ILE   A 1 376 ? -21.589 -37.168 -19.371 1.00 74.25  ? 396 ILE   A O   1 
ATOM   2588 C  CB  . ILE   A 1 376 ? -24.212 -38.424 -18.963 1.00 87.84  ? 396 ILE   A CB  1 
ATOM   2589 C  CG1 . ILE   A 1 376 ? -25.276 -39.388 -18.402 1.00 84.65  ? 396 ILE   A CG1 1 
ATOM   2590 C  CG2 . ILE   A 1 376 ? -24.826 -37.576 -20.059 1.00 72.79  ? 396 ILE   A CG2 1 
ATOM   2591 C  CD1 . ILE   A 1 376 ? -24.978 -40.047 -17.055 1.00 76.84  ? 396 ILE   A CD1 1 
ATOM   2592 N  N   . PRO   A 1 377 ? -21.481 -38.320 -21.297 1.00 74.10  ? 397 PRO   A N   1 
ATOM   2593 C  CA  . PRO   A 1 377 ? -20.476 -37.407 -21.894 1.00 88.45  ? 397 PRO   A CA  1 
ATOM   2594 C  C   . PRO   A 1 377 ? -21.068 -36.064 -22.319 1.00 76.90  ? 397 PRO   A C   1 
ATOM   2595 O  O   . PRO   A 1 377 ? -21.379 -35.809 -23.482 1.00 76.30  ? 397 PRO   A O   1 
ATOM   2596 C  CB  . PRO   A 1 377 ? -19.967 -38.213 -23.092 1.00 90.25  ? 397 PRO   A CB  1 
ATOM   2597 C  CG  . PRO   A 1 377 ? -21.154 -39.034 -23.491 1.00 84.69  ? 397 PRO   A CG  1 
ATOM   2598 C  CD  . PRO   A 1 377 ? -21.791 -39.450 -22.191 1.00 68.06  ? 397 PRO   A CD  1 
ATOM   2599 N  N   . SER   A 1 378 ? -21.215 -35.171 -21.335 1.00 80.25  ? 398 SER   A N   1 
ATOM   2600 C  CA  . SER   A 1 378 ? -21.861 -33.881 -21.570 1.00 83.08  ? 398 SER   A CA  1 
ATOM   2601 C  C   . SER   A 1 378 ? -21.175 -33.102 -22.686 1.00 80.77  ? 398 SER   A C   1 
ATOM   2602 O  O   . SER   A 1 378 ? -21.837 -32.569 -23.584 1.00 72.45  ? 398 SER   A O   1 
ATOM   2603 C  CB  . SER   A 1 378 ? -21.876 -33.061 -20.278 1.00 78.63  ? 398 SER   A CB  1 
ATOM   2604 O  OG  . SER   A 1 378 ? -22.720 -33.651 -19.306 1.00 82.17  ? 398 SER   A OG  1 
ATOM   2605 N  N   . TYR   A 1 379 ? -19.842 -33.024 -22.641 1.00 80.07  ? 399 TYR   A N   1 
ATOM   2606 C  CA  . TYR   A 1 379 ? -19.101 -32.323 -23.685 1.00 80.56  ? 399 TYR   A CA  1 
ATOM   2607 C  C   . TYR   A 1 379 ? -19.413 -32.893 -25.062 1.00 82.98  ? 399 TYR   A C   1 
ATOM   2608 O  O   . TYR   A 1 379 ? -19.700 -32.149 -26.005 1.00 85.10  ? 399 TYR   A O   1 
ATOM   2609 C  CB  . TYR   A 1 379 ? -17.600 -32.406 -23.410 1.00 86.72  ? 399 TYR   A CB  1 
ATOM   2610 C  CG  . TYR   A 1 379 ? -16.753 -31.611 -24.381 1.00 75.10  ? 399 TYR   A CG  1 
ATOM   2611 C  CD1 . TYR   A 1 379 ? -16.440 -30.280 -24.135 1.00 91.86  ? 399 TYR   A CD1 1 
ATOM   2612 C  CD2 . TYR   A 1 379 ? -16.282 -32.188 -25.553 1.00 83.41  ? 399 TYR   A CD2 1 
ATOM   2613 C  CE1 . TYR   A 1 379 ? -15.665 -29.554 -25.021 1.00 89.00  ? 399 TYR   A CE1 1 
ATOM   2614 C  CE2 . TYR   A 1 379 ? -15.508 -31.471 -26.444 1.00 99.75  ? 399 TYR   A CE2 1 
ATOM   2615 C  CZ  . TYR   A 1 379 ? -15.204 -30.154 -26.174 1.00 91.85  ? 399 TYR   A CZ  1 
ATOM   2616 O  OH  . TYR   A 1 379 ? -14.435 -29.438 -27.063 1.00 90.60  ? 399 TYR   A OH  1 
ATOM   2617 N  N   . ALA   A 1 380 ? -19.356 -34.220 -25.194 1.00 81.75  ? 400 ALA   A N   1 
ATOM   2618 C  CA  . ALA   A 1 380 ? -19.587 -34.843 -26.493 1.00 98.01  ? 400 ALA   A CA  1 
ATOM   2619 C  C   . ALA   A 1 380 ? -21.013 -34.611 -26.977 1.00 92.37  ? 400 ALA   A C   1 
ATOM   2620 O  O   . ALA   A 1 380 ? -21.241 -34.387 -28.171 1.00 95.24  ? 400 ALA   A O   1 
ATOM   2621 C  CB  . ALA   A 1 380 ? -19.280 -36.339 -26.419 1.00 100.29 ? 400 ALA   A CB  1 
ATOM   2622 N  N   . LEU   A 1 381 ? -21.985 -34.655 -26.064 1.00 85.19  ? 401 LEU   A N   1 
ATOM   2623 C  CA  . LEU   A 1 381 ? -23.378 -34.476 -26.464 1.00 90.84  ? 401 LEU   A CA  1 
ATOM   2624 C  C   . LEU   A 1 381 ? -23.655 -33.040 -26.892 1.00 91.37  ? 401 LEU   A C   1 
ATOM   2625 O  O   . LEU   A 1 381 ? -24.404 -32.807 -27.848 1.00 98.42  ? 401 LEU   A O   1 
ATOM   2626 C  CB  . LEU   A 1 381 ? -24.309 -34.890 -25.327 1.00 91.99  ? 401 LEU   A CB  1 
ATOM   2627 C  CG  . LEU   A 1 381 ? -24.140 -36.329 -24.838 1.00 90.19  ? 401 LEU   A CG  1 
ATOM   2628 C  CD1 . LEU   A 1 381 ? -24.921 -36.560 -23.556 1.00 80.14  ? 401 LEU   A CD1 1 
ATOM   2629 C  CD2 . LEU   A 1 381 ? -24.559 -37.312 -25.918 1.00 102.90 ? 401 LEU   A CD2 1 
ATOM   2630 N  N   . HIS   A 1 382 ? -23.063 -32.065 -26.199 1.00 84.60  ? 402 HIS   A N   1 
ATOM   2631 C  CA  . HIS   A 1 382 ? -23.231 -30.671 -26.595 1.00 91.18  ? 402 HIS   A CA  1 
ATOM   2632 C  C   . HIS   A 1 382 ? -22.603 -30.374 -27.949 1.00 99.52  ? 402 HIS   A C   1 
ATOM   2633 O  O   . HIS   A 1 382 ? -22.923 -29.347 -28.558 1.00 92.23  ? 402 HIS   A O   1 
ATOM   2634 C  CB  . HIS   A 1 382 ? -22.627 -29.737 -25.544 1.00 80.24  ? 402 HIS   A CB  1 
ATOM   2635 C  CG  . HIS   A 1 382 ? -23.274 -29.830 -24.197 1.00 76.46  ? 402 HIS   A CG  1 
ATOM   2636 N  ND1 . HIS   A 1 382 ? -22.876 -29.054 -23.130 1.00 81.03  ? 402 HIS   A ND1 1 
ATOM   2637 C  CD2 . HIS   A 1 382 ? -24.291 -30.599 -23.744 1.00 82.89  ? 402 HIS   A CD2 1 
ATOM   2638 C  CE1 . HIS   A 1 382 ? -23.617 -29.344 -22.076 1.00 97.07  ? 402 HIS   A CE1 1 
ATOM   2639 N  NE2 . HIS   A 1 382 ? -24.484 -30.279 -22.422 1.00 81.59  ? 402 HIS   A NE2 1 
ATOM   2640 N  N   . ARG   A 1 383 ? -21.717 -31.244 -28.432 1.00 102.71 ? 403 ARG   A N   1 
ATOM   2641 C  CA  . ARG   A 1 383 ? -21.010 -31.025 -29.686 1.00 101.85 ? 403 ARG   A CA  1 
ATOM   2642 C  C   . ARG   A 1 383 ? -21.371 -32.046 -30.754 1.00 110.59 ? 403 ARG   A C   1 
ATOM   2643 O  O   . ARG   A 1 383 ? -20.645 -32.161 -31.746 1.00 112.40 ? 403 ARG   A O   1 
ATOM   2644 C  CB  . ARG   A 1 383 ? -19.498 -31.047 -29.453 1.00 91.68  ? 403 ARG   A CB  1 
ATOM   2645 C  CG  . ARG   A 1 383 ? -19.031 -30.166 -28.314 1.00 95.70  ? 403 ARG   A CG  1 
ATOM   2646 C  CD  . ARG   A 1 383 ? -18.352 -28.922 -28.838 1.00 106.42 ? 403 ARG   A CD  1 
ATOM   2647 N  NE  . ARG   A 1 383 ? -17.693 -28.180 -27.772 1.00 99.94  ? 403 ARG   A NE  1 
ATOM   2648 C  CZ  . ARG   A 1 383 ? -16.606 -27.441 -27.941 1.00 95.79  ? 403 ARG   A CZ  1 
ATOM   2649 N  NH1 . ARG   A 1 383 ? -16.027 -27.326 -29.125 1.00 105.58 ? 403 ARG   A NH1 1 
ATOM   2650 N  NH2 . ARG   A 1 383 ? -16.083 -26.808 -26.895 1.00 91.97  ? 403 ARG   A NH2 1 
ATOM   2651 N  N   . ASP   A 1 384 ? -22.462 -32.786 -30.579 1.00 119.25 ? 404 ASP   A N   1 
ATOM   2652 C  CA  . ASP   A 1 384 ? -22.809 -33.857 -31.506 1.00 127.92 ? 404 ASP   A CA  1 
ATOM   2653 C  C   . ASP   A 1 384 ? -23.542 -33.265 -32.703 1.00 132.41 ? 404 ASP   A C   1 
ATOM   2654 O  O   . ASP   A 1 384 ? -24.603 -32.660 -32.521 1.00 133.70 ? 404 ASP   A O   1 
ATOM   2655 C  CB  . ASP   A 1 384 ? -23.695 -34.885 -30.806 1.00 133.25 ? 404 ASP   A CB  1 
ATOM   2656 C  CG  . ASP   A 1 384 ? -24.040 -36.081 -31.688 1.00 139.46 ? 404 ASP   A CG  1 
ATOM   2657 O  OD1 . ASP   A 1 384 ? -23.936 -35.997 -32.930 1.00 142.01 ? 404 ASP   A OD1 1 
ATOM   2658 O  OD2 . ASP   A 1 384 ? -24.460 -37.110 -31.124 1.00 139.36 ? 404 ASP   A OD2 1 
ATOM   2659 N  N   . PRO   A 1 385 ? -23.020 -33.400 -33.927 1.00 134.66 ? 405 PRO   A N   1 
ATOM   2660 C  CA  . PRO   A 1 385 ? -23.791 -32.955 -35.099 1.00 127.03 ? 405 PRO   A CA  1 
ATOM   2661 C  C   . PRO   A 1 385 ? -25.140 -33.636 -35.236 1.00 132.84 ? 405 PRO   A C   1 
ATOM   2662 O  O   . PRO   A 1 385 ? -26.029 -33.076 -35.887 1.00 138.48 ? 405 PRO   A O   1 
ATOM   2663 C  CB  . PRO   A 1 385 ? -22.878 -33.307 -36.278 1.00 127.07 ? 405 PRO   A CB  1 
ATOM   2664 C  CG  . PRO   A 1 385 ? -21.509 -33.475 -35.713 1.00 136.44 ? 405 PRO   A CG  1 
ATOM   2665 C  CD  . PRO   A 1 385 ? -21.575 -33.484 -34.214 1.00 130.04 ? 405 PRO   A CD  1 
ATOM   2666 N  N   . LYS   A 1 386 ? -25.323 -34.827 -34.657 1.00 132.19 ? 406 LYS   A N   1 
ATOM   2667 C  CA  . LYS   A 1 386 ? -26.617 -35.503 -34.713 1.00 134.98 ? 406 LYS   A CA  1 
ATOM   2668 C  C   . LYS   A 1 386 ? -27.676 -34.808 -33.870 1.00 136.04 ? 406 LYS   A C   1 
ATOM   2669 O  O   . LYS   A 1 386 ? -28.787 -35.334 -33.748 1.00 138.77 ? 406 LYS   A O   1 
ATOM   2670 C  CB  . LYS   A 1 386 ? -26.480 -36.959 -34.262 1.00 145.58 ? 406 LYS   A CB  1 
ATOM   2671 C  CG  . LYS   A 1 386 ? -25.651 -37.839 -35.188 1.00 151.26 ? 406 LYS   A CG  1 
ATOM   2672 C  CD  . LYS   A 1 386 ? -26.361 -39.144 -35.508 1.00 156.97 ? 406 LYS   A CD  1 
ATOM   2673 C  CE  . LYS   A 1 386 ? -25.634 -39.915 -36.596 1.00 161.08 ? 406 LYS   A CE  1 
ATOM   2674 N  NZ  . LYS   A 1 386 ? -26.457 -41.040 -37.114 1.00 152.89 ? 406 LYS   A NZ  1 
ATOM   2675 N  N   . TYR   A 1 387 ? -27.351 -33.661 -33.272 1.00 138.14 ? 407 TYR   A N   1 
ATOM   2676 C  CA  . TYR   A 1 387 ? -28.322 -32.839 -32.564 1.00 140.23 ? 407 TYR   A CA  1 
ATOM   2677 C  C   . TYR   A 1 387 ? -28.134 -31.349 -32.795 1.00 141.30 ? 407 TYR   A C   1 
ATOM   2678 O  O   . TYR   A 1 387 ? -29.045 -30.581 -32.472 1.00 144.09 ? 407 TYR   A O   1 
ATOM   2679 C  CB  . TYR   A 1 387 ? -28.266 -33.110 -31.053 1.00 135.71 ? 407 TYR   A CB  1 
ATOM   2680 C  CG  . TYR   A 1 387 ? -28.594 -34.531 -30.659 1.00 137.76 ? 407 TYR   A CG  1 
ATOM   2681 C  CD1 . TYR   A 1 387 ? -29.904 -34.990 -30.666 1.00 142.86 ? 407 TYR   A CD1 1 
ATOM   2682 C  CD2 . TYR   A 1 387 ? -27.593 -35.411 -30.266 1.00 143.26 ? 407 TYR   A CD2 1 
ATOM   2683 C  CE1 . TYR   A 1 387 ? -30.208 -36.288 -30.302 1.00 145.36 ? 407 TYR   A CE1 1 
ATOM   2684 C  CE2 . TYR   A 1 387 ? -27.887 -36.710 -29.901 1.00 143.21 ? 407 TYR   A CE2 1 
ATOM   2685 C  CZ  . TYR   A 1 387 ? -29.196 -37.143 -29.921 1.00 149.00 ? 407 TYR   A CZ  1 
ATOM   2686 O  OH  . TYR   A 1 387 ? -29.492 -38.436 -29.556 1.00 157.80 ? 407 TYR   A OH  1 
ATOM   2687 N  N   . TRP   A 1 388 ? -27.000 -30.910 -33.338 1.00 134.04 ? 408 TRP   A N   1 
ATOM   2688 C  CA  . TRP   A 1 388 ? -26.700 -29.493 -33.492 1.00 129.63 ? 408 TRP   A CA  1 
ATOM   2689 C  C   . TRP   A 1 388 ? -26.129 -29.250 -34.879 1.00 139.13 ? 408 TRP   A C   1 
ATOM   2690 O  O   . TRP   A 1 388 ? -25.190 -29.936 -35.294 1.00 144.19 ? 408 TRP   A O   1 
ATOM   2691 C  CB  . TRP   A 1 388 ? -25.700 -29.023 -32.429 1.00 122.44 ? 408 TRP   A CB  1 
ATOM   2692 C  CG  . TRP   A 1 388 ? -26.011 -29.502 -31.043 1.00 122.99 ? 408 TRP   A CG  1 
ATOM   2693 C  CD1 . TRP   A 1 388 ? -25.621 -30.681 -30.478 1.00 116.69 ? 408 TRP   A CD1 1 
ATOM   2694 C  CD2 . TRP   A 1 388 ? -26.758 -28.804 -30.039 1.00 114.56 ? 408 TRP   A CD2 1 
ATOM   2695 N  NE1 . TRP   A 1 388 ? -26.090 -30.767 -29.190 1.00 96.91  ? 408 TRP   A NE1 1 
ATOM   2696 C  CE2 . TRP   A 1 388 ? -26.789 -29.627 -28.895 1.00 103.14 ? 408 TRP   A CE2 1 
ATOM   2697 C  CE3 . TRP   A 1 388 ? -27.407 -27.567 -29.998 1.00 105.18 ? 408 TRP   A CE3 1 
ATOM   2698 C  CZ2 . TRP   A 1 388 ? -27.444 -29.252 -27.724 1.00 93.25  ? 408 TRP   A CZ2 1 
ATOM   2699 C  CZ3 . TRP   A 1 388 ? -28.057 -27.197 -28.835 1.00 93.29  ? 408 TRP   A CZ3 1 
ATOM   2700 C  CH2 . TRP   A 1 388 ? -28.070 -28.037 -27.714 1.00 81.58  ? 408 TRP   A CH2 1 
ATOM   2701 N  N   . THR   A 1 389 ? -26.689 -28.275 -35.589 1.00 123.57 ? 409 THR   A N   1 
ATOM   2702 C  CA  . THR   A 1 389 ? -26.154 -27.882 -36.885 1.00 132.32 ? 409 THR   A CA  1 
ATOM   2703 C  C   . THR   A 1 389 ? -24.895 -27.048 -36.687 1.00 128.49 ? 409 THR   A C   1 
ATOM   2704 O  O   . THR   A 1 389 ? -24.923 -26.027 -35.993 1.00 127.40 ? 409 THR   A O   1 
ATOM   2705 C  CB  . THR   A 1 389 ? -27.190 -27.089 -37.682 1.00 138.83 ? 409 THR   A CB  1 
ATOM   2706 O  OG1 . THR   A 1 389 ? -27.579 -25.927 -36.939 1.00 139.94 ? 409 THR   A OG1 1 
ATOM   2707 C  CG2 . THR   A 1 389 ? -28.418 -27.942 -37.960 1.00 131.35 ? 409 THR   A CG2 1 
ATOM   2708 N  N   . GLU   A 1 390 ? -23.792 -27.479 -37.315 1.00 130.60 ? 410 GLU   A N   1 
ATOM   2709 C  CA  . GLU   A 1 390 ? -22.491 -26.823 -37.215 1.00 133.49 ? 410 GLU   A CA  1 
ATOM   2710 C  C   . GLU   A 1 390 ? -22.162 -26.590 -35.743 1.00 123.41 ? 410 GLU   A C   1 
ATOM   2711 O  O   . GLU   A 1 390 ? -22.229 -25.451 -35.263 1.00 119.33 ? 410 GLU   A O   1 
ATOM   2712 C  CB  . GLU   A 1 390 ? -22.483 -25.506 -38.003 1.00 135.43 ? 410 GLU   A CB  1 
ATOM   2713 C  CG  . GLU   A 1 390 ? -23.499 -25.459 -39.149 1.00 143.98 ? 410 GLU   A CG  1 
ATOM   2714 C  CD  . GLU   A 1 390 ? -23.764 -24.053 -39.655 1.00 151.20 ? 410 GLU   A CD  1 
ATOM   2715 O  OE1 . GLU   A 1 390 ? -22.892 -23.492 -40.351 1.00 151.58 ? 410 GLU   A OE1 1 
ATOM   2716 O  OE2 . GLU   A 1 390 ? -24.837 -23.499 -39.336 1.00 149.36 ? 410 GLU   A OE2 1 
ATOM   2717 N  N   . PRO   A 1 391 ? -21.791 -27.638 -35.000 1.00 124.74 ? 411 PRO   A N   1 
ATOM   2718 C  CA  . PRO   A 1 391 ? -21.765 -27.538 -33.536 1.00 122.00 ? 411 PRO   A CA  1 
ATOM   2719 C  C   . PRO   A 1 391 ? -20.574 -26.787 -32.960 1.00 115.70 ? 411 PRO   A C   1 
ATOM   2720 O  O   . PRO   A 1 391 ? -20.608 -26.443 -31.770 1.00 112.14 ? 411 PRO   A O   1 
ATOM   2721 C  CB  . PRO   A 1 391 ? -21.755 -29.012 -33.098 1.00 116.27 ? 411 PRO   A CB  1 
ATOM   2722 C  CG  . PRO   A 1 391 ? -21.228 -29.793 -34.323 1.00 126.38 ? 411 PRO   A CG  1 
ATOM   2723 C  CD  . PRO   A 1 391 ? -21.032 -28.811 -35.455 1.00 134.12 ? 411 PRO   A CD  1 
ATOM   2724 N  N   . GLU   A 1 392 ? -19.538 -26.517 -33.750 1.00 120.20 ? 412 GLU   A N   1 
ATOM   2725 C  CA  . GLU   A 1 392 ? -18.356 -25.831 -33.243 1.00 117.39 ? 412 GLU   A CA  1 
ATOM   2726 C  C   . GLU   A 1 392 ? -18.551 -24.326 -33.119 1.00 115.81 ? 412 GLU   A C   1 
ATOM   2727 O  O   . GLU   A 1 392 ? -17.750 -23.663 -32.452 1.00 117.07 ? 412 GLU   A O   1 
ATOM   2728 C  CB  . GLU   A 1 392 ? -17.162 -26.118 -34.158 1.00 122.07 ? 412 GLU   A CB  1 
ATOM   2729 C  CG  . GLU   A 1 392 ? -16.377 -27.362 -33.792 1.00 139.11 ? 412 GLU   A CG  1 
ATOM   2730 C  CD  . GLU   A 1 392 ? -15.071 -27.048 -33.096 1.00 157.96 ? 412 GLU   A CD  1 
ATOM   2731 O  OE1 . GLU   A 1 392 ? -14.646 -27.861 -32.253 1.00 146.67 ? 412 GLU   A OE1 1 
ATOM   2732 O  OE2 . GLU   A 1 392 ? -14.464 -26.000 -33.402 1.00 148.76 ? 412 GLU   A OE2 1 
ATOM   2733 N  N   . LYS   A 1 393 ? -19.593 -23.779 -33.733 1.00 113.65 ? 413 LYS   A N   1 
ATOM   2734 C  CA  . LYS   A 1 393 ? -19.758 -22.338 -33.832 1.00 110.99 ? 413 LYS   A CA  1 
ATOM   2735 C  C   . LYS   A 1 393 ? -20.628 -21.805 -32.700 1.00 112.10 ? 413 LYS   A C   1 
ATOM   2736 O  O   . LYS   A 1 393 ? -21.599 -22.445 -32.287 1.00 114.36 ? 413 LYS   A O   1 
ATOM   2737 C  CB  . LYS   A 1 393 ? -20.361 -21.970 -35.188 1.00 110.98 ? 413 LYS   A CB  1 
ATOM   2738 C  CG  . LYS   A 1 393 ? -19.731 -22.732 -36.345 1.00 121.33 ? 413 LYS   A CG  1 
ATOM   2739 C  CD  . LYS   A 1 393 ? -19.655 -21.889 -37.604 1.00 122.60 ? 413 LYS   A CD  1 
ATOM   2740 C  CE  . LYS   A 1 393 ? -20.911 -22.036 -38.435 1.00 142.56 ? 413 LYS   A CE  1 
ATOM   2741 N  NZ  . LYS   A 1 393 ? -20.720 -23.043 -39.519 1.00 138.83 ? 413 LYS   A NZ  1 
ATOM   2742 N  N   . PHE   A 1 394 ? -20.265 -20.624 -32.204 1.00 111.64 ? 414 PHE   A N   1 
ATOM   2743 C  CA  . PHE   A 1 394 ? -20.975 -19.966 -31.108 1.00 107.56 ? 414 PHE   A CA  1 
ATOM   2744 C  C   . PHE   A 1 394 ? -22.200 -19.272 -31.688 1.00 107.70 ? 414 PHE   A C   1 
ATOM   2745 O  O   . PHE   A 1 394 ? -22.107 -18.175 -32.242 1.00 110.43 ? 414 PHE   A O   1 
ATOM   2746 C  CB  . PHE   A 1 394 ? -20.043 -18.993 -30.393 1.00 109.03 ? 414 PHE   A CB  1 
ATOM   2747 C  CG  . PHE   A 1 394 ? -20.735 -18.050 -29.443 1.00 106.85 ? 414 PHE   A CG  1 
ATOM   2748 C  CD1 . PHE   A 1 394 ? -20.996 -18.432 -28.138 1.00 101.57 ? 414 PHE   A CD1 1 
ATOM   2749 C  CD2 . PHE   A 1 394 ? -21.074 -16.764 -29.837 1.00 93.35  ? 414 PHE   A CD2 1 
ATOM   2750 C  CE1 . PHE   A 1 394 ? -21.616 -17.565 -27.256 1.00 101.93 ? 414 PHE   A CE1 1 
ATOM   2751 C  CE2 . PHE   A 1 394 ? -21.691 -15.893 -28.960 1.00 86.42  ? 414 PHE   A CE2 1 
ATOM   2752 C  CZ  . PHE   A 1 394 ? -21.963 -16.294 -27.668 1.00 103.43 ? 414 PHE   A CZ  1 
ATOM   2753 N  N   . LEU   A 1 395 ? -23.358 -19.923 -31.572 1.00 106.22 ? 415 LEU   A N   1 
ATOM   2754 C  CA  . LEU   A 1 395 ? -24.605 -19.463 -32.182 1.00 100.71 ? 415 LEU   A CA  1 
ATOM   2755 C  C   . LEU   A 1 395 ? -25.667 -19.361 -31.094 1.00 100.24 ? 415 LEU   A C   1 
ATOM   2756 O  O   . LEU   A 1 395 ? -26.404 -20.323 -30.841 1.00 105.02 ? 415 LEU   A O   1 
ATOM   2757 C  CB  . LEU   A 1 395 ? -25.051 -20.410 -33.296 1.00 99.93  ? 415 LEU   A CB  1 
ATOM   2758 C  CG  . LEU   A 1 395 ? -24.179 -20.613 -34.543 1.00 115.60 ? 415 LEU   A CG  1 
ATOM   2759 C  CD1 . LEU   A 1 395 ? -25.051 -20.913 -35.748 1.00 119.55 ? 415 LEU   A CD1 1 
ATOM   2760 C  CD2 . LEU   A 1 395 ? -23.308 -19.406 -34.836 1.00 115.98 ? 415 LEU   A CD2 1 
ATOM   2761 N  N   . PRO   A 1 396 ? -25.782 -18.204 -30.432 1.00 105.38 ? 416 PRO   A N   1 
ATOM   2762 C  CA  . PRO   A 1 396 ? -26.733 -18.087 -29.313 1.00 109.71 ? 416 PRO   A CA  1 
ATOM   2763 C  C   . PRO   A 1 396 ? -28.193 -18.177 -29.725 1.00 109.18 ? 416 PRO   A C   1 
ATOM   2764 O  O   . PRO   A 1 396 ? -29.053 -18.311 -28.844 1.00 100.95 ? 416 PRO   A O   1 
ATOM   2765 C  CB  . PRO   A 1 396 ? -26.415 -16.707 -28.713 1.00 106.28 ? 416 PRO   A CB  1 
ATOM   2766 C  CG  . PRO   A 1 396 ? -25.136 -16.262 -29.352 1.00 96.47  ? 416 PRO   A CG  1 
ATOM   2767 C  CD  . PRO   A 1 396 ? -25.052 -16.951 -30.673 1.00 101.46 ? 416 PRO   A CD  1 
ATOM   2768 N  N   . GLU   A 1 397 ? -28.506 -18.108 -31.019 1.00 106.26 ? 417 GLU   A N   1 
ATOM   2769 C  CA  . GLU   A 1 397 ? -29.893 -18.244 -31.449 1.00 110.97 ? 417 GLU   A CA  1 
ATOM   2770 C  C   . GLU   A 1 397 ? -30.409 -19.673 -31.338 1.00 108.07 ? 417 GLU   A C   1 
ATOM   2771 O  O   . GLU   A 1 397 ? -31.592 -19.904 -31.614 1.00 115.64 ? 417 GLU   A O   1 
ATOM   2772 C  CB  . GLU   A 1 397 ? -30.054 -17.737 -32.884 1.00 117.18 ? 417 GLU   A CB  1 
ATOM   2773 C  CG  . GLU   A 1 397 ? -30.097 -16.219 -32.995 1.00 128.84 ? 417 GLU   A CG  1 
ATOM   2774 C  CD  . GLU   A 1 397 ? -31.472 -15.649 -32.696 1.00 138.93 ? 417 GLU   A CD  1 
ATOM   2775 O  OE1 . GLU   A 1 397 ? -32.474 -16.365 -32.903 1.00 132.72 ? 417 GLU   A OE1 1 
ATOM   2776 O  OE2 . GLU   A 1 397 ? -31.550 -14.484 -32.250 1.00 137.86 ? 417 GLU   A OE2 1 
ATOM   2777 N  N   . ARG   A 1 398 ? -29.562 -20.631 -30.951 1.00 108.52 ? 418 ARG   A N   1 
ATOM   2778 C  CA  . ARG   A 1 398 ? -30.054 -21.959 -30.606 1.00 95.56  ? 418 ARG   A CA  1 
ATOM   2779 C  C   . ARG   A 1 398 ? -31.000 -21.922 -29.417 1.00 103.72 ? 418 ARG   A C   1 
ATOM   2780 O  O   . ARG   A 1 398 ? -31.846 -22.813 -29.281 1.00 101.50 ? 418 ARG   A O   1 
ATOM   2781 C  CB  . ARG   A 1 398 ? -28.895 -22.904 -30.280 1.00 103.34 ? 418 ARG   A CB  1 
ATOM   2782 C  CG  . ARG   A 1 398 ? -27.914 -23.173 -31.405 1.00 108.15 ? 418 ARG   A CG  1 
ATOM   2783 C  CD  . ARG   A 1 398 ? -26.793 -24.070 -30.892 1.00 106.67 ? 418 ARG   A CD  1 
ATOM   2784 N  NE  . ARG   A 1 398 ? -25.597 -24.025 -31.724 1.00 107.84 ? 418 ARG   A NE  1 
ATOM   2785 C  CZ  . ARG   A 1 398 ? -25.373 -24.828 -32.756 1.00 116.50 ? 418 ARG   A CZ  1 
ATOM   2786 N  NH1 . ARG   A 1 398 ? -26.252 -25.747 -33.120 1.00 128.62 ? 418 ARG   A NH1 1 
ATOM   2787 N  NH2 . ARG   A 1 398 ? -24.236 -24.710 -33.435 1.00 112.30 ? 418 ARG   A NH2 1 
ATOM   2788 N  N   . PHE   A 1 399 ? -30.872 -20.917 -28.551 1.00 111.39 ? 419 PHE   A N   1 
ATOM   2789 C  CA  . PHE   A 1 399 ? -31.625 -20.849 -27.308 1.00 110.12 ? 419 PHE   A CA  1 
ATOM   2790 C  C   . PHE   A 1 399 ? -32.689 -19.757 -27.336 1.00 105.44 ? 419 PHE   A C   1 
ATOM   2791 O  O   . PHE   A 1 399 ? -33.102 -19.269 -26.279 1.00 108.50 ? 419 PHE   A O   1 
ATOM   2792 C  CB  . PHE   A 1 399 ? -30.670 -20.644 -26.131 1.00 98.77  ? 419 PHE   A CB  1 
ATOM   2793 C  CG  . PHE   A 1 399 ? -29.748 -21.809 -25.895 1.00 94.66  ? 419 PHE   A CG  1 
ATOM   2794 C  CD1 . PHE   A 1 399 ? -28.565 -21.929 -26.608 1.00 101.05 ? 419 PHE   A CD1 1 
ATOM   2795 C  CD2 . PHE   A 1 399 ? -30.074 -22.794 -24.979 1.00 100.03 ? 419 PHE   A CD2 1 
ATOM   2796 C  CE1 . PHE   A 1 399 ? -27.718 -23.002 -26.400 1.00 100.40 ? 419 PHE   A CE1 1 
ATOM   2797 C  CE2 . PHE   A 1 399 ? -29.230 -23.869 -24.765 1.00 104.46 ? 419 PHE   A CE2 1 
ATOM   2798 C  CZ  . PHE   A 1 399 ? -28.051 -23.973 -25.477 1.00 88.93  ? 419 PHE   A CZ  1 
ATOM   2799 N  N   . SER   A 1 400 ? -33.137 -19.363 -28.524 1.00 129.03 ? 420 SER   A N   1 
ATOM   2800 C  CA  . SER   A 1 400 ? -34.221 -18.402 -28.645 1.00 129.75 ? 420 SER   A CA  1 
ATOM   2801 C  C   . SER   A 1 400 ? -35.566 -19.111 -28.569 1.00 137.14 ? 420 SER   A C   1 
ATOM   2802 O  O   . SER   A 1 400 ? -35.689 -20.290 -28.909 1.00 129.55 ? 420 SER   A O   1 
ATOM   2803 C  CB  . SER   A 1 400 ? -34.105 -17.620 -29.953 1.00 132.73 ? 420 SER   A CB  1 
ATOM   2804 O  OG  . SER   A 1 400 ? -34.415 -18.436 -31.068 1.00 117.46 ? 420 SER   A OG  1 
ATOM   2805 N  N   . LYS   A 1 401 ? -36.584 -18.370 -28.120 1.00 127.93 ? 421 LYS   A N   1 
ATOM   2806 C  CA  . LYS   A 1 401 ? -37.891 -18.971 -27.868 1.00 129.09 ? 421 LYS   A CA  1 
ATOM   2807 C  C   . LYS   A 1 401 ? -38.462 -19.628 -29.120 1.00 132.57 ? 421 LYS   A C   1 
ATOM   2808 O  O   . LYS   A 1 401 ? -39.230 -20.592 -29.019 1.00 142.45 ? 421 LYS   A O   1 
ATOM   2809 C  CB  . LYS   A 1 401 ? -38.845 -17.912 -27.308 1.00 124.35 ? 421 LYS   A CB  1 
ATOM   2810 C  CG  . LYS   A 1 401 ? -40.269 -17.962 -27.832 1.00 130.86 ? 421 LYS   A CG  1 
ATOM   2811 C  CD  . LYS   A 1 401 ? -40.851 -16.568 -27.974 1.00 127.01 ? 421 LYS   A CD  1 
ATOM   2812 C  CE  . LYS   A 1 401 ? -42.225 -16.606 -28.616 1.00 121.34 ? 421 LYS   A CE  1 
ATOM   2813 N  NZ  . LYS   A 1 401 ? -42.882 -15.272 -28.577 1.00 129.90 ? 421 LYS   A NZ  1 
ATOM   2814 N  N   . LYS   A 1 402 ? -38.082 -19.142 -30.303 1.00 145.77 ? 422 LYS   A N   1 
ATOM   2815 C  CA  . LYS   A 1 402 ? -38.431 -19.847 -31.532 1.00 146.96 ? 422 LYS   A CA  1 
ATOM   2816 C  C   . LYS   A 1 402 ? -37.753 -21.214 -31.570 1.00 147.13 ? 422 LYS   A C   1 
ATOM   2817 O  O   . LYS   A 1 402 ? -38.397 -22.222 -31.882 1.00 146.40 ? 422 LYS   A O   1 
ATOM   2818 C  CB  . LYS   A 1 402 ? -38.053 -18.976 -32.744 1.00 145.00 ? 422 LYS   A CB  1 
ATOM   2819 C  CG  . LYS   A 1 402 ? -38.383 -19.457 -34.196 1.00 152.42 ? 422 LYS   A CG  1 
ATOM   2820 C  CD  . LYS   A 1 402 ? -37.928 -20.859 -34.585 1.00 160.32 ? 422 LYS   A CD  1 
ATOM   2821 C  CE  . LYS   A 1 402 ? -38.466 -21.294 -35.935 1.00 168.07 ? 422 LYS   A CE  1 
ATOM   2822 N  NZ  . LYS   A 1 402 ? -38.132 -22.725 -36.191 1.00 169.80 ? 422 LYS   A NZ  1 
ATOM   2823 N  N   . ASN   A 1 403 ? -36.464 -21.273 -31.233 1.00 139.73 ? 423 ASN   A N   1 
ATOM   2824 C  CA  . ASN   A 1 403 ? -35.674 -22.488 -31.388 1.00 140.33 ? 423 ASN   A CA  1 
ATOM   2825 C  C   . ASN   A 1 403 ? -35.371 -23.208 -30.079 1.00 141.75 ? 423 ASN   A C   1 
ATOM   2826 O  O   . ASN   A 1 403 ? -34.823 -24.314 -30.122 1.00 139.75 ? 423 ASN   A O   1 
ATOM   2827 C  CB  . ASN   A 1 403 ? -34.350 -22.166 -32.097 1.00 134.27 ? 423 ASN   A CB  1 
ATOM   2828 C  CG  . ASN   A 1 403 ? -34.523 -21.926 -33.582 1.00 149.60 ? 423 ASN   A CG  1 
ATOM   2829 O  OD1 . ASN   A 1 403 ? -35.326 -22.584 -34.240 1.00 153.02 ? 423 ASN   A OD1 1 
ATOM   2830 N  ND2 . ASN   A 1 403 ? -33.766 -20.975 -34.119 1.00 142.83 ? 423 ASN   A ND2 1 
ATOM   2831 N  N   . LYS   A 1 404 ? -35.704 -22.624 -28.926 1.00 138.74 ? 424 LYS   A N   1 
ATOM   2832 C  CA  . LYS   A 1 404 ? -35.355 -23.261 -27.659 1.00 139.40 ? 424 LYS   A CA  1 
ATOM   2833 C  C   . LYS   A 1 404 ? -36.160 -24.525 -27.384 1.00 148.98 ? 424 LYS   A C   1 
ATOM   2834 O  O   . LYS   A 1 404 ? -35.795 -25.286 -26.481 1.00 147.55 ? 424 LYS   A O   1 
ATOM   2835 C  CB  . LYS   A 1 404 ? -35.533 -22.276 -26.498 1.00 136.46 ? 424 LYS   A CB  1 
ATOM   2836 C  CG  . LYS   A 1 404 ? -36.944 -22.209 -25.939 1.00 139.85 ? 424 LYS   A CG  1 
ATOM   2837 C  CD  . LYS   A 1 404 ? -36.924 -22.028 -24.429 1.00 145.97 ? 424 LYS   A CD  1 
ATOM   2838 C  CE  . LYS   A 1 404 ? -38.039 -22.814 -23.758 1.00 145.54 ? 424 LYS   A CE  1 
ATOM   2839 N  NZ  . LYS   A 1 404 ? -38.071 -22.588 -22.286 1.00 152.08 ? 424 LYS   A NZ  1 
ATOM   2840 N  N   . ASP   A 1 405 ? -37.235 -24.773 -28.135 1.00 150.22 ? 425 ASP   A N   1 
ATOM   2841 C  CA  . ASP   A 1 405 ? -38.033 -25.975 -27.934 1.00 149.05 ? 425 ASP   A CA  1 
ATOM   2842 C  C   . ASP   A 1 405 ? -37.443 -27.197 -28.624 1.00 146.93 ? 425 ASP   A C   1 
ATOM   2843 O  O   . ASP   A 1 405 ? -37.786 -28.325 -28.253 1.00 143.76 ? 425 ASP   A O   1 
ATOM   2844 C  CB  . ASP   A 1 405 ? -39.463 -25.750 -28.430 1.00 155.53 ? 425 ASP   A CB  1 
ATOM   2845 C  CG  . ASP   A 1 405 ? -39.945 -24.332 -28.201 1.00 158.65 ? 425 ASP   A CG  1 
ATOM   2846 O  OD1 . ASP   A 1 405 ? -40.202 -23.972 -27.033 1.00 166.50 ? 425 ASP   A OD1 1 
ATOM   2847 O  OD2 . ASP   A 1 405 ? -40.069 -23.577 -29.189 1.00 152.36 ? 425 ASP   A OD2 1 
ATOM   2848 N  N   . ASN   A 1 406 ? -36.567 -27.001 -29.612 1.00 165.01 ? 426 ASN   A N   1 
ATOM   2849 C  CA  . ASN   A 1 406 ? -35.956 -28.092 -30.360 1.00 162.67 ? 426 ASN   A CA  1 
ATOM   2850 C  C   . ASN   A 1 406 ? -34.716 -28.649 -29.674 1.00 163.03 ? 426 ASN   A C   1 
ATOM   2851 O  O   . ASN   A 1 406 ? -33.787 -29.107 -30.354 1.00 163.43 ? 426 ASN   A O   1 
ATOM   2852 C  CB  . ASN   A 1 406 ? -35.610 -27.625 -31.775 1.00 166.08 ? 426 ASN   A CB  1 
ATOM   2853 C  CG  . ASN   A 1 406 ? -36.753 -26.887 -32.442 1.00 170.00 ? 426 ASN   A CG  1 
ATOM   2854 O  OD1 . ASN   A 1 406 ? -37.908 -27.014 -32.033 1.00 170.03 ? 426 ASN   A OD1 1 
ATOM   2855 N  ND2 . ASN   A 1 406 ? -36.440 -26.114 -33.476 1.00 171.39 ? 426 ASN   A ND2 1 
ATOM   2856 N  N   . ILE   A 1 407 ? -34.674 -28.627 -28.344 1.00 139.48 ? 427 ILE   A N   1 
ATOM   2857 C  CA  . ILE   A 1 407 ? -33.490 -29.007 -27.588 1.00 133.32 ? 427 ILE   A CA  1 
ATOM   2858 C  C   . ILE   A 1 407 ? -33.916 -29.944 -26.467 1.00 124.02 ? 427 ILE   A C   1 
ATOM   2859 O  O   . ILE   A 1 407 ? -34.811 -29.614 -25.680 1.00 123.92 ? 427 ILE   A O   1 
ATOM   2860 C  CB  . ILE   A 1 407 ? -32.760 -27.770 -27.029 1.00 127.96 ? 427 ILE   A CB  1 
ATOM   2861 C  CG1 . ILE   A 1 407 ? -31.737 -27.261 -28.044 1.00 117.30 ? 427 ILE   A CG1 1 
ATOM   2862 C  CG2 . ILE   A 1 407 ? -32.066 -28.089 -25.712 1.00 111.84 ? 427 ILE   A CG2 1 
ATOM   2863 C  CD1 . ILE   A 1 407 ? -31.120 -25.933 -27.672 1.00 105.77 ? 427 ILE   A CD1 1 
ATOM   2864 N  N   . ASP   A 1 408 ? -33.287 -31.110 -26.409 1.00 111.98 ? 428 ASP   A N   1 
ATOM   2865 C  CA  . ASP   A 1 408 ? -33.577 -32.095 -25.375 1.00 105.14 ? 428 ASP   A CA  1 
ATOM   2866 C  C   . ASP   A 1 408 ? -32.855 -31.718 -24.085 1.00 106.45 ? 428 ASP   A C   1 
ATOM   2867 O  O   . ASP   A 1 408 ? -31.630 -31.557 -24.094 1.00 95.89  ? 428 ASP   A O   1 
ATOM   2868 C  CB  . ASP   A 1 408 ? -33.143 -33.484 -25.842 1.00 99.72  ? 428 ASP   A CB  1 
ATOM   2869 C  CG  . ASP   A 1 408 ? -34.009 -34.599 -25.281 1.00 111.86 ? 428 ASP   A CG  1 
ATOM   2870 O  OD1 . ASP   A 1 408 ? -34.316 -34.582 -24.072 1.00 114.95 ? 428 ASP   A OD1 1 
ATOM   2871 O  OD2 . ASP   A 1 408 ? -34.379 -35.504 -26.062 1.00 116.78 ? 428 ASP   A OD2 1 
ATOM   2872 N  N   . PRO   A 1 409 ? -33.567 -31.571 -22.967 1.00 104.41 ? 429 PRO   A N   1 
ATOM   2873 C  CA  . PRO   A 1 409 ? -32.912 -31.292 -21.683 1.00 97.19  ? 429 PRO   A CA  1 
ATOM   2874 C  C   . PRO   A 1 409 ? -32.108 -32.454 -21.123 1.00 95.63  ? 429 PRO   A C   1 
ATOM   2875 O  O   . PRO   A 1 409 ? -31.630 -32.365 -19.989 1.00 96.30  ? 429 PRO   A O   1 
ATOM   2876 C  CB  . PRO   A 1 409 ? -34.101 -30.965 -20.768 1.00 109.22 ? 429 PRO   A CB  1 
ATOM   2877 C  CG  . PRO   A 1 409 ? -35.216 -31.786 -21.320 1.00 108.25 ? 429 PRO   A CG  1 
ATOM   2878 C  CD  . PRO   A 1 409 ? -35.020 -31.773 -22.817 1.00 110.65 ? 429 PRO   A CD  1 
ATOM   2879 N  N   . TYR   A 1 410 ? -31.961 -33.539 -21.882 1.00 97.31  ? 430 TYR   A N   1 
ATOM   2880 C  CA  . TYR   A 1 410 ? -31.090 -34.643 -21.520 1.00 100.45 ? 430 TYR   A CA  1 
ATOM   2881 C  C   . TYR   A 1 410 ? -29.921 -34.784 -22.477 1.00 99.42  ? 430 TYR   A C   1 
ATOM   2882 O  O   . TYR   A 1 410 ? -29.053 -35.635 -22.257 1.00 94.46  ? 430 TYR   A O   1 
ATOM   2883 C  CB  . TYR   A 1 410 ? -31.908 -35.939 -21.452 1.00 95.49  ? 430 TYR   A CB  1 
ATOM   2884 C  CG  . TYR   A 1 410 ? -32.994 -35.791 -20.423 1.00 98.53  ? 430 TYR   A CG  1 
ATOM   2885 C  CD1 . TYR   A 1 410 ? -32.690 -35.803 -19.069 1.00 86.23  ? 430 TYR   A CD1 1 
ATOM   2886 C  CD2 . TYR   A 1 410 ? -34.306 -35.545 -20.799 1.00 102.56 ? 430 TYR   A CD2 1 
ATOM   2887 C  CE1 . TYR   A 1 410 ? -33.670 -35.631 -18.118 1.00 94.60  ? 430 TYR   A CE1 1 
ATOM   2888 C  CE2 . TYR   A 1 410 ? -35.296 -35.368 -19.854 1.00 93.93  ? 430 TYR   A CE2 1 
ATOM   2889 C  CZ  . TYR   A 1 410 ? -34.970 -35.405 -18.513 1.00 102.00 ? 430 TYR   A CZ  1 
ATOM   2890 O  OH  . TYR   A 1 410 ? -35.946 -35.239 -17.559 1.00 102.22 ? 430 TYR   A OH  1 
ATOM   2891 N  N   . ILE   A 1 411 ? -29.890 -33.974 -23.530 1.00 97.87  ? 431 ILE   A N   1 
ATOM   2892 C  CA  . ILE   A 1 411 ? -28.667 -33.716 -24.279 1.00 96.62  ? 431 ILE   A CA  1 
ATOM   2893 C  C   . ILE   A 1 411 ? -27.966 -32.469 -23.758 1.00 94.17  ? 431 ILE   A C   1 
ATOM   2894 O  O   . ILE   A 1 411 ? -26.740 -32.448 -23.630 1.00 98.20  ? 431 ILE   A O   1 
ATOM   2895 C  CB  . ILE   A 1 411 ? -28.984 -33.596 -25.783 1.00 96.48  ? 431 ILE   A CB  1 
ATOM   2896 C  CG1 . ILE   A 1 411 ? -29.842 -34.777 -26.240 1.00 99.37  ? 431 ILE   A CG1 1 
ATOM   2897 C  CG2 . ILE   A 1 411 ? -27.701 -33.487 -26.595 1.00 98.30  ? 431 ILE   A CG2 1 
ATOM   2898 C  CD1 . ILE   A 1 411 ? -29.041 -35.992 -26.641 1.00 108.10 ? 431 ILE   A CD1 1 
ATOM   2899 N  N   . TYR   A 1 412 ? -28.728 -31.424 -23.441 1.00 84.57  ? 432 TYR   A N   1 
ATOM   2900 C  CA  . TYR   A 1 412 ? -28.183 -30.187 -22.885 1.00 90.78  ? 432 TYR   A CA  1 
ATOM   2901 C  C   . TYR   A 1 412 ? -28.345 -30.231 -21.370 1.00 83.20  ? 432 TYR   A C   1 
ATOM   2902 O  O   . TYR   A 1 412 ? -29.420 -29.939 -20.840 1.00 92.35  ? 432 TYR   A O   1 
ATOM   2903 C  CB  . TYR   A 1 412 ? -28.870 -28.963 -23.481 1.00 79.23  ? 432 TYR   A CB  1 
ATOM   2904 C  CG  . TYR   A 1 412 ? -28.221 -27.671 -23.050 1.00 86.51  ? 432 TYR   A CG  1 
ATOM   2905 C  CD1 . TYR   A 1 412 ? -26.951 -27.336 -23.493 1.00 86.25  ? 432 TYR   A CD1 1 
ATOM   2906 C  CD2 . TYR   A 1 412 ? -28.868 -26.795 -22.188 1.00 84.13  ? 432 TYR   A CD2 1 
ATOM   2907 C  CE1 . TYR   A 1 412 ? -26.345 -26.166 -23.099 1.00 85.34  ? 432 TYR   A CE1 1 
ATOM   2908 C  CE2 . TYR   A 1 412 ? -28.267 -25.616 -21.789 1.00 88.31  ? 432 TYR   A CE2 1 
ATOM   2909 C  CZ  . TYR   A 1 412 ? -27.004 -25.309 -22.249 1.00 87.02  ? 432 TYR   A CZ  1 
ATOM   2910 O  OH  . TYR   A 1 412 ? -26.391 -24.142 -21.860 1.00 92.41  ? 432 TYR   A OH  1 
ATOM   2911 N  N   . THR   A 1 413 ? -27.268 -30.592 -20.673 1.00 81.92  ? 433 THR   A N   1 
ATOM   2912 C  CA  . THR   A 1 413 ? -27.263 -30.717 -19.215 1.00 83.12  ? 433 THR   A CA  1 
ATOM   2913 C  C   . THR   A 1 413 ? -26.020 -30.045 -18.642 1.00 88.03  ? 433 THR   A C   1 
ATOM   2914 O  O   . THR   A 1 413 ? -25.128 -30.716 -18.110 1.00 83.00  ? 433 THR   A O   1 
ATOM   2915 C  CB  . THR   A 1 413 ? -27.313 -32.185 -18.791 1.00 92.22  ? 433 THR   A CB  1 
ATOM   2916 O  OG1 . THR   A 1 413 ? -26.201 -32.885 -19.368 1.00 78.18  ? 433 THR   A OG1 1 
ATOM   2917 C  CG2 . THR   A 1 413 ? -28.605 -32.841 -19.244 1.00 84.30  ? 433 THR   A CG2 1 
ATOM   2918 N  N   . PRO   A 1 414 ? -25.931 -28.713 -18.723 1.00 89.10  ? 434 PRO   A N   1 
ATOM   2919 C  CA  . PRO   A 1 414 ? -24.773 -28.030 -18.125 1.00 85.90  ? 434 PRO   A CA  1 
ATOM   2920 C  C   . PRO   A 1 414 ? -24.782 -28.057 -16.609 1.00 78.16  ? 434 PRO   A C   1 
ATOM   2921 O  O   . PRO   A 1 414 ? -23.738 -27.800 -15.995 1.00 71.34  ? 434 PRO   A O   1 
ATOM   2922 C  CB  . PRO   A 1 414 ? -24.895 -26.596 -18.656 1.00 81.84  ? 434 PRO   A CB  1 
ATOM   2923 C  CG  . PRO   A 1 414 ? -26.349 -26.420 -18.911 1.00 84.99  ? 434 PRO   A CG  1 
ATOM   2924 C  CD  . PRO   A 1 414 ? -26.881 -27.763 -19.329 1.00 83.88  ? 434 PRO   A CD  1 
ATOM   2925 N  N   . PHE   A 1 415 ? -25.922 -28.364 -15.989 1.00 81.90  ? 435 PHE   A N   1 
ATOM   2926 C  CA  . PHE   A 1 415 ? -26.057 -28.384 -14.538 1.00 86.84  ? 435 PHE   A CA  1 
ATOM   2927 C  C   . PHE   A 1 415 ? -26.532 -29.741 -14.032 1.00 74.16  ? 435 PHE   A C   1 
ATOM   2928 O  O   . PHE   A 1 415 ? -26.959 -29.854 -12.879 1.00 66.43  ? 435 PHE   A O   1 
ATOM   2929 C  CB  . PHE   A 1 415 ? -27.017 -27.283 -14.083 1.00 74.67  ? 435 PHE   A CB  1 
ATOM   2930 C  CG  . PHE   A 1 415 ? -26.524 -25.892 -14.362 1.00 87.17  ? 435 PHE   A CG  1 
ATOM   2931 C  CD1 . PHE   A 1 415 ? -26.800 -25.277 -15.572 1.00 89.85  ? 435 PHE   A CD1 1 
ATOM   2932 C  CD2 . PHE   A 1 415 ? -25.775 -25.204 -13.423 1.00 80.86  ? 435 PHE   A CD2 1 
ATOM   2933 C  CE1 . PHE   A 1 415 ? -26.349 -23.999 -15.836 1.00 80.96  ? 435 PHE   A CE1 1 
ATOM   2934 C  CE2 . PHE   A 1 415 ? -25.322 -23.923 -13.680 1.00 89.41  ? 435 PHE   A CE2 1 
ATOM   2935 C  CZ  . PHE   A 1 415 ? -25.607 -23.321 -14.890 1.00 85.44  ? 435 PHE   A CZ  1 
ATOM   2936 N  N   . GLY   A 1 416 ? -26.465 -30.771 -14.871 1.00 76.16  ? 436 GLY   A N   1 
ATOM   2937 C  CA  . GLY   A 1 416 ? -26.985 -32.069 -14.503 1.00 83.82  ? 436 GLY   A CA  1 
ATOM   2938 C  C   . GLY   A 1 416 ? -28.500 -32.113 -14.591 1.00 81.87  ? 436 GLY   A C   1 
ATOM   2939 O  O   . GLY   A 1 416 ? -29.147 -31.277 -15.231 1.00 84.28  ? 436 GLY   A O   1 
ATOM   2940 N  N   . SER   A 1 417 ? -29.071 -33.115 -13.927 1.00 84.92  ? 437 SER   A N   1 
ATOM   2941 C  CA  . SER   A 1 417 ? -30.517 -33.274 -13.882 1.00 76.23  ? 437 SER   A CA  1 
ATOM   2942 C  C   . SER   A 1 417 ? -30.868 -34.240 -12.762 1.00 79.63  ? 437 SER   A C   1 
ATOM   2943 O  O   . SER   A 1 417 ? -30.013 -34.975 -12.260 1.00 82.45  ? 437 SER   A O   1 
ATOM   2944 C  CB  . SER   A 1 417 ? -31.076 -33.772 -15.219 1.00 76.53  ? 437 SER   A CB  1 
ATOM   2945 O  OG  . SER   A 1 417 ? -32.028 -32.859 -15.740 1.00 98.93  ? 437 SER   A OG  1 
ATOM   2946 N  N   . GLY   A 1 418 ? -32.140 -34.227 -12.378 1.00 83.99  ? 438 GLY   A N   1 
ATOM   2947 C  CA  . GLY   A 1 418 ? -32.622 -35.083 -11.323 1.00 73.66  ? 438 GLY   A CA  1 
ATOM   2948 C  C   . GLY   A 1 418 ? -32.329 -34.518 -9.950  1.00 77.38  ? 438 GLY   A C   1 
ATOM   2949 O  O   . GLY   A 1 418 ? -31.902 -33.368 -9.802  1.00 64.58  ? 438 GLY   A O   1 
ATOM   2950 N  N   . PRO   A 1 419 ? -32.550 -35.326 -8.911  1.00 84.32  ? 439 PRO   A N   1 
ATOM   2951 C  CA  . PRO   A 1 419 ? -32.356 -34.827 -7.538  1.00 90.07  ? 439 PRO   A CA  1 
ATOM   2952 C  C   . PRO   A 1 419 ? -30.927 -34.414 -7.223  1.00 82.59  ? 439 PRO   A C   1 
ATOM   2953 O  O   . PRO   A 1 419 ? -30.723 -33.656 -6.267  1.00 84.19  ? 439 PRO   A O   1 
ATOM   2954 C  CB  . PRO   A 1 419 ? -32.802 -35.999 -6.650  1.00 78.33  ? 439 PRO   A CB  1 
ATOM   2955 C  CG  . PRO   A 1 419 ? -33.214 -37.098 -7.545  1.00 91.97  ? 439 PRO   A CG  1 
ATOM   2956 C  CD  . PRO   A 1 419 ? -33.119 -36.683 -8.969  1.00 80.58  ? 439 PRO   A CD  1 
ATOM   2957 N  N   . ARG   A 1 420 ? -29.932 -34.877 -7.981  1.00 82.46  ? 440 ARG   A N   1 
ATOM   2958 C  CA  . ARG   A 1 420 ? -28.542 -34.525 -7.715  1.00 88.10  ? 440 ARG   A CA  1 
ATOM   2959 C  C   . ARG   A 1 420 ? -27.952 -33.602 -8.776  1.00 74.63  ? 440 ARG   A C   1 
ATOM   2960 O  O   . ARG   A 1 420 ? -26.746 -33.634 -9.032  1.00 71.30  ? 440 ARG   A O   1 
ATOM   2961 C  CB  . ARG   A 1 420 ? -27.675 -35.773 -7.559  1.00 83.50  ? 440 ARG   A CB  1 
ATOM   2962 C  CG  . ARG   A 1 420 ? -26.906 -35.734 -6.259  1.00 94.05  ? 440 ARG   A CG  1 
ATOM   2963 C  CD  . ARG   A 1 420 ? -26.134 -36.989 -5.931  1.00 87.64  ? 440 ARG   A CD  1 
ATOM   2964 N  NE  . ARG   A 1 420 ? -25.044 -36.653 -5.024  1.00 75.49  ? 440 ARG   A NE  1 
ATOM   2965 C  CZ  . ARG   A 1 420 ? -24.441 -37.509 -4.211  1.00 79.82  ? 440 ARG   A CZ  1 
ATOM   2966 N  NH1 . ARG   A 1 420 ? -24.790 -38.784 -4.168  1.00 87.52  ? 440 ARG   A NH1 1 
ATOM   2967 N  NH2 . ARG   A 1 420 ? -23.475 -37.071 -3.410  1.00 77.86  ? 440 ARG   A NH2 1 
ATOM   2968 N  N   . ASN   A 1 421 ? -28.782 -32.760 -9.385  1.00 78.45  ? 441 ASN   A N   1 
ATOM   2969 C  CA  . ASN   A 1 421 ? -28.265 -31.723 -10.261 1.00 78.65  ? 441 ASN   A CA  1 
ATOM   2970 C  C   . ASN   A 1 421 ? -27.545 -30.656 -9.436  1.00 73.99  ? 441 ASN   A C   1 
ATOM   2971 O  O   . ASN   A 1 421 ? -27.459 -30.730 -8.207  1.00 73.77  ? 441 ASN   A O   1 
ATOM   2972 C  CB  . ASN   A 1 421 ? -29.391 -31.142 -11.120 1.00 75.63  ? 441 ASN   A CB  1 
ATOM   2973 C  CG  . ASN   A 1 421 ? -30.303 -30.186 -10.357 1.00 81.68  ? 441 ASN   A CG  1 
ATOM   2974 O  OD1 . ASN   A 1 421 ? -30.255 -30.088 -9.131  1.00 75.83  ? 441 ASN   A OD1 1 
ATOM   2975 N  ND2 . ASN   A 1 421 ? -31.142 -29.469 -11.096 1.00 88.07  ? 441 ASN   A ND2 1 
ATOM   2976 N  N   . CYS   A 1 422 ? -27.015 -29.647 -10.126 1.00 75.20  ? 442 CYS   A N   1 
ATOM   2977 C  CA  . CYS   A 1 422 ? -26.280 -28.583 -9.454  1.00 76.83  ? 442 CYS   A CA  1 
ATOM   2978 C  C   . CYS   A 1 422 ? -27.196 -27.815 -8.511  1.00 78.34  ? 442 CYS   A C   1 
ATOM   2979 O  O   . CYS   A 1 422 ? -28.097 -27.099 -8.960  1.00 77.35  ? 442 CYS   A O   1 
ATOM   2980 C  CB  . CYS   A 1 422 ? -25.649 -27.635 -10.474 1.00 72.91  ? 442 CYS   A CB  1 
ATOM   2981 S  SG  . CYS   A 1 422 ? -25.016 -26.099 -9.766  1.00 88.40  ? 442 CYS   A SG  1 
ATOM   2982 N  N   . ILE   A 1 423 ? -26.976 -27.964 -7.201  1.00 74.87  ? 443 ILE   A N   1 
ATOM   2983 C  CA  . ILE   A 1 423 ? -27.806 -27.282 -6.214  1.00 95.07  ? 443 ILE   A CA  1 
ATOM   2984 C  C   . ILE   A 1 423 ? -27.676 -25.770 -6.324  1.00 92.36  ? 443 ILE   A C   1 
ATOM   2985 O  O   . ILE   A 1 423 ? -28.570 -25.038 -5.887  1.00 82.63  ? 443 ILE   A O   1 
ATOM   2986 C  CB  . ILE   A 1 423 ? -27.449 -27.761 -4.790  1.00 85.38  ? 443 ILE   A CB  1 
ATOM   2987 C  CG1 . ILE   A 1 423 ? -28.565 -27.404 -3.804  1.00 86.98  ? 443 ILE   A CG1 1 
ATOM   2988 C  CG2 . ILE   A 1 423 ? -26.141 -27.145 -4.332  1.00 89.33  ? 443 ILE   A CG2 1 
ATOM   2989 C  CD1 . ILE   A 1 423 ? -28.172 -27.559 -2.346  1.00 90.67  ? 443 ILE   A CD1 1 
ATOM   2990 N  N   . GLY   A 1 424 ? -26.586 -25.278 -6.906  1.00 77.34  ? 444 GLY   A N   1 
ATOM   2991 C  CA  . GLY   A 1 424 ? -26.358 -23.858 -7.062  1.00 96.83  ? 444 GLY   A CA  1 
ATOM   2992 C  C   . GLY   A 1 424 ? -26.627 -23.309 -8.445  1.00 91.31  ? 444 GLY   A C   1 
ATOM   2993 O  O   . GLY   A 1 424 ? -26.130 -22.223 -8.765  1.00 90.20  ? 444 GLY   A O   1 
ATOM   2994 N  N   . MET   A 1 425 ? -27.401 -24.018 -9.272  1.00 77.30  ? 445 MET   A N   1 
ATOM   2995 C  CA  . MET   A 1 425 ? -27.643 -23.586 -10.646 1.00 83.63  ? 445 MET   A CA  1 
ATOM   2996 C  C   . MET   A 1 425 ? -28.217 -22.175 -10.698 1.00 91.87  ? 445 MET   A C   1 
ATOM   2997 O  O   . MET   A 1 425 ? -27.638 -21.277 -11.321 1.00 90.14  ? 445 MET   A O   1 
ATOM   2998 C  CB  . MET   A 1 425 ? -28.584 -24.568 -11.348 1.00 67.04  ? 445 MET   A CB  1 
ATOM   2999 C  CG  . MET   A 1 425 ? -29.197 -24.010 -12.626 1.00 85.23  ? 445 MET   A CG  1 
ATOM   3000 S  SD  . MET   A 1 425 ? -30.457 -25.063 -13.370 1.00 87.65  ? 445 MET   A SD  1 
ATOM   3001 C  CE  . MET   A 1 425 ? -30.190 -24.741 -15.112 1.00 100.77 ? 445 MET   A CE  1 
ATOM   3002 N  N   . ARG   A 1 426 ? -29.360 -21.963 -10.041 1.00 85.16  ? 446 ARG   A N   1 
ATOM   3003 C  CA  . ARG   A 1 426 ? -30.047 -20.680 -10.151 1.00 97.33  ? 446 ARG   A CA  1 
ATOM   3004 C  C   . ARG   A 1 426 ? -29.197 -19.539 -9.606  1.00 105.43 ? 446 ARG   A C   1 
ATOM   3005 O  O   . ARG   A 1 426 ? -29.235 -18.423 -10.138 1.00 100.70 ? 446 ARG   A O   1 
ATOM   3006 C  CB  . ARG   A 1 426 ? -31.395 -20.736 -9.435  1.00 101.98 ? 446 ARG   A CB  1 
ATOM   3007 C  CG  . ARG   A 1 426 ? -32.559 -20.315 -10.315 1.00 121.80 ? 446 ARG   A CG  1 
ATOM   3008 C  CD  . ARG   A 1 426 ? -33.901 -20.654 -9.678  1.00 125.29 ? 446 ARG   A CD  1 
ATOM   3009 N  NE  . ARG   A 1 426 ? -34.270 -22.058 -9.830  1.00 141.69 ? 446 ARG   A NE  1 
ATOM   3010 C  CZ  . ARG   A 1 426 ? -34.464 -22.678 -10.987 1.00 146.99 ? 446 ARG   A CZ  1 
ATOM   3011 N  NH1 . ARG   A 1 426 ? -34.366 -22.041 -12.142 1.00 144.25 ? 446 ARG   A NH1 1 
ATOM   3012 N  NH2 . ARG   A 1 426 ? -34.779 -23.971 -10.985 1.00 150.08 ? 446 ARG   A NH2 1 
ATOM   3013 N  N   . PHE   A 1 427 ? -28.427 -19.793 -8.547  1.00 101.53 ? 447 PHE   A N   1 
ATOM   3014 C  CA  . PHE   A 1 427 ? -27.526 -18.763 -8.037  1.00 96.59  ? 447 PHE   A CA  1 
ATOM   3015 C  C   . PHE   A 1 427 ? -26.485 -18.396 -9.084  1.00 103.14 ? 447 PHE   A C   1 
ATOM   3016 O  O   . PHE   A 1 427 ? -26.287 -17.214 -9.390  1.00 108.94 ? 447 PHE   A O   1 
ATOM   3017 C  CB  . PHE   A 1 427 ? -26.860 -19.232 -6.737  1.00 107.66 ? 447 PHE   A CB  1 
ATOM   3018 C  CG  . PHE   A 1 427 ? -25.822 -18.272 -6.189  1.00 114.75 ? 447 PHE   A CG  1 
ATOM   3019 C  CD1 . PHE   A 1 427 ? -24.567 -18.147 -6.775  1.00 115.26 ? 447 PHE   A CD1 1 
ATOM   3020 C  CD2 . PHE   A 1 427 ? -26.087 -17.542 -5.043  1.00 125.32 ? 447 PHE   A CD2 1 
ATOM   3021 C  CE1 . PHE   A 1 427 ? -23.625 -17.276 -6.261  1.00 126.78 ? 447 PHE   A CE1 1 
ATOM   3022 C  CE2 . PHE   A 1 427 ? -25.147 -16.668 -4.525  1.00 132.34 ? 447 PHE   A CE2 1 
ATOM   3023 C  CZ  . PHE   A 1 427 ? -23.914 -16.539 -5.133  1.00 131.15 ? 447 PHE   A CZ  1 
ATOM   3024 N  N   . ALA   A 1 428 ? -25.805 -19.403 -9.638  1.00 104.39 ? 448 ALA   A N   1 
ATOM   3025 C  CA  . ALA   A 1 428 ? -24.738 -19.152 -10.600 1.00 105.56 ? 448 ALA   A CA  1 
ATOM   3026 C  C   . ALA   A 1 428 ? -25.233 -18.311 -11.768 1.00 109.57 ? 448 ALA   A C   1 
ATOM   3027 O  O   . ALA   A 1 428 ? -24.612 -17.307 -12.130 1.00 114.55 ? 448 ALA   A O   1 
ATOM   3028 C  CB  . ALA   A 1 428 ? -24.156 -20.477 -11.094 1.00 97.94  ? 448 ALA   A CB  1 
ATOM   3029 N  N   . LEU   A 1 429 ? -26.368 -18.697 -12.360 1.00 106.15 ? 449 LEU   A N   1 
ATOM   3030 C  CA  . LEU   A 1 429 ? -26.948 -17.897 -13.435 1.00 114.55 ? 449 LEU   A CA  1 
ATOM   3031 C  C   . LEU   A 1 429 ? -27.165 -16.457 -12.992 1.00 126.56 ? 449 LEU   A C   1 
ATOM   3032 O  O   . LEU   A 1 429 ? -26.826 -15.518 -13.718 1.00 108.84 ? 449 LEU   A O   1 
ATOM   3033 C  CB  . LEU   A 1 429 ? -28.275 -18.500 -13.901 1.00 99.06  ? 449 LEU   A CB  1 
ATOM   3034 C  CG  . LEU   A 1 429 ? -28.309 -19.916 -14.473 1.00 101.24 ? 449 LEU   A CG  1 
ATOM   3035 C  CD1 . LEU   A 1 429 ? -29.423 -20.711 -13.814 1.00 100.60 ? 449 LEU   A CD1 1 
ATOM   3036 C  CD2 . LEU   A 1 429 ? -28.487 -19.882 -15.982 1.00 104.14 ? 449 LEU   A CD2 1 
ATOM   3037 N  N   . MET   A 1 430 ? -27.720 -16.266 -11.794 1.00 127.89 ? 450 MET   A N   1 
ATOM   3038 C  CA  A MET   A 1 430 ? -27.972 -14.916 -11.301 0.40 126.23 ? 450 MET   A CA  1 
ATOM   3039 C  CA  B MET   A 1 430 ? -27.971 -14.917 -11.300 0.60 125.30 ? 450 MET   A CA  1 
ATOM   3040 C  C   . MET   A 1 430 ? -26.668 -14.170 -11.053 1.00 129.71 ? 450 MET   A C   1 
ATOM   3041 O  O   . MET   A 1 430 ? -26.483 -13.047 -11.536 1.00 131.88 ? 450 MET   A O   1 
ATOM   3042 C  CB  A MET   A 1 430 ? -28.809 -14.972 -10.023 0.40 122.02 ? 450 MET   A CB  1 
ATOM   3043 C  CB  B MET   A 1 430 ? -28.803 -14.974 -10.021 0.60 122.26 ? 450 MET   A CB  1 
ATOM   3044 C  CG  A MET   A 1 430 ? -29.101 -13.607 -9.418  0.40 123.68 ? 450 MET   A CG  1 
ATOM   3045 C  CG  B MET   A 1 430 ? -28.762 -13.697 -9.202  0.60 123.65 ? 450 MET   A CG  1 
ATOM   3046 S  SD  A MET   A 1 430 ? -29.959 -12.507 -10.561 0.40 133.28 ? 450 MET   A SD  1 
ATOM   3047 S  SD  B MET   A 1 430 ? -30.410 -13.228 -8.658  0.60 123.61 ? 450 MET   A SD  1 
ATOM   3048 C  CE  A MET   A 1 430 ? -31.348 -13.531 -11.038 0.40 135.63 ? 450 MET   A CE  1 
ATOM   3049 C  CE  B MET   A 1 430 ? -31.263 -13.246 -10.234 0.60 137.36 ? 450 MET   A CE  1 
ATOM   3050 N  N   . ASN   A 1 431 ? -25.756 -14.781 -10.297 1.00 128.77 ? 451 ASN   A N   1 
ATOM   3051 C  CA  . ASN   A 1 431 ? -24.486 -14.140 -9.988  1.00 124.59 ? 451 ASN   A CA  1 
ATOM   3052 C  C   . ASN   A 1 431 ? -23.745 -13.740 -11.255 1.00 120.31 ? 451 ASN   A C   1 
ATOM   3053 O  O   . ASN   A 1 431 ? -23.284 -12.601 -11.389 1.00 121.11 ? 451 ASN   A O   1 
ATOM   3054 C  CB  . ASN   A 1 431 ? -23.628 -15.079 -9.148  1.00 125.18 ? 451 ASN   A CB  1 
ATOM   3055 C  CG  . ASN   A 1 431 ? -22.313 -14.465 -8.791  1.00 128.45 ? 451 ASN   A CG  1 
ATOM   3056 O  OD1 . ASN   A 1 431 ? -21.306 -14.684 -9.453  1.00 131.51 ? 451 ASN   A OD1 1 
ATOM   3057 N  ND2 . ASN   A 1 431 ? -22.324 -13.644 -7.762  1.00 140.34 ? 451 ASN   A ND2 1 
ATOM   3058 N  N   . MET   A 1 432 ? -23.625 -14.676 -12.197 1.00 117.79 ? 452 MET   A N   1 
ATOM   3059 C  CA  . MET   A 1 432 ? -22.944 -14.397 -13.456 1.00 118.09 ? 452 MET   A CA  1 
ATOM   3060 C  C   . MET   A 1 432 ? -23.644 -13.285 -14.223 1.00 114.08 ? 452 MET   A C   1 
ATOM   3061 O  O   . MET   A 1 432 ? -22.998 -12.365 -14.735 1.00 106.11 ? 452 MET   A O   1 
ATOM   3062 C  CB  . MET   A 1 432 ? -22.888 -15.668 -14.302 1.00 103.65 ? 452 MET   A CB  1 
ATOM   3063 C  CG  . MET   A 1 432 ? -22.087 -16.795 -13.684 1.00 115.69 ? 452 MET   A CG  1 
ATOM   3064 S  SD  . MET   A 1 432 ? -21.561 -17.986 -14.920 1.00 106.96 ? 452 MET   A SD  1 
ATOM   3065 C  CE  . MET   A 1 432 ? -23.149 -18.526 -15.548 1.00 102.39 ? 452 MET   A CE  1 
ATOM   3066 N  N   . LYS   A 1 433 ? -24.974 -13.360 -14.317 1.00 113.11 ? 453 LYS   A N   1 
ATOM   3067 C  CA  . LYS   A 1 433 ? -25.709 -12.387 -15.116 1.00 119.22 ? 453 LYS   A CA  1 
ATOM   3068 C  C   . LYS   A 1 433 ? -25.517 -10.976 -14.578 1.00 125.72 ? 453 LYS   A C   1 
ATOM   3069 O  O   . LYS   A 1 433 ? -25.273 -10.043 -15.349 1.00 117.48 ? 453 LYS   A O   1 
ATOM   3070 C  CB  . LYS   A 1 433 ? -27.190 -12.765 -15.166 1.00 115.61 ? 453 LYS   A CB  1 
ATOM   3071 C  CG  . LYS   A 1 433 ? -27.510 -13.813 -16.227 1.00 106.96 ? 453 LYS   A CG  1 
ATOM   3072 C  CD  . LYS   A 1 433 ? -28.987 -14.167 -16.246 1.00 102.13 ? 453 LYS   A CD  1 
ATOM   3073 C  CE  . LYS   A 1 433 ? -29.259 -15.354 -17.157 1.00 104.14 ? 453 LYS   A CE  1 
ATOM   3074 N  NZ  . LYS   A 1 433 ? -30.587 -15.968 -16.882 1.00 102.56 ? 453 LYS   A NZ  1 
ATOM   3075 N  N   . LEU   A 1 434 ? -25.594 -10.804 -13.254 1.00 125.41 ? 454 LEU   A N   1 
ATOM   3076 C  CA  . LEU   A 1 434 ? -25.336 -9.493  -12.661 1.00 129.08 ? 454 LEU   A CA  1 
ATOM   3077 C  C   . LEU   A 1 434 ? -23.946 -8.985  -13.026 1.00 133.24 ? 454 LEU   A C   1 
ATOM   3078 O  O   . LEU   A 1 434 ? -23.757 -7.786  -13.262 1.00 120.79 ? 454 LEU   A O   1 
ATOM   3079 C  CB  . LEU   A 1 434 ? -25.502 -9.561  -11.142 1.00 118.62 ? 454 LEU   A CB  1 
ATOM   3080 C  CG  . LEU   A 1 434 ? -26.920 -9.812  -10.625 1.00 133.05 ? 454 LEU   A CG  1 
ATOM   3081 C  CD1 . LEU   A 1 434 ? -26.967 -9.724  -9.110  1.00 137.45 ? 454 LEU   A CD1 1 
ATOM   3082 C  CD2 . LEU   A 1 434 ? -27.879 -8.818  -11.241 1.00 125.83 ? 454 LEU   A CD2 1 
ATOM   3083 N  N   . ALA   A 1 435 ? -22.961 -9.886  -13.079 1.00 120.56 ? 455 ALA   A N   1 
ATOM   3084 C  CA  . ALA   A 1 435 ? -21.626 -9.517  -13.540 1.00 122.66 ? 455 ALA   A CA  1 
ATOM   3085 C  C   . ALA   A 1 435 ? -21.653 -9.042  -14.988 1.00 120.14 ? 455 ALA   A C   1 
ATOM   3086 O  O   . ALA   A 1 435 ? -21.077 -8.002  -15.325 1.00 122.54 ? 455 ALA   A O   1 
ATOM   3087 C  CB  . ALA   A 1 435 ? -20.677 -10.705 -13.396 1.00 121.30 ? 455 ALA   A CB  1 
ATOM   3088 N  N   . LEU   A 1 436 ? -22.303 -9.814  -15.863 1.00 124.72 ? 456 LEU   A N   1 
ATOM   3089 C  CA  . LEU   A 1 436 ? -22.366 -9.475  -17.282 1.00 125.67 ? 456 LEU   A CA  1 
ATOM   3090 C  C   . LEU   A 1 436 ? -23.045 -8.134  -17.522 1.00 122.37 ? 456 LEU   A C   1 
ATOM   3091 O  O   . LEU   A 1 436 ? -22.586 -7.341  -18.352 1.00 118.12 ? 456 LEU   A O   1 
ATOM   3092 C  CB  . LEU   A 1 436 ? -23.077 -10.599 -18.033 1.00 119.20 ? 456 LEU   A CB  1 
ATOM   3093 C  CG  . LEU   A 1 436 ? -22.200 -11.819 -18.281 1.00 112.70 ? 456 LEU   A CG  1 
ATOM   3094 C  CD1 . LEU   A 1 436 ? -22.689 -12.551 -19.500 1.00 103.17 ? 456 LEU   A CD1 1 
ATOM   3095 C  CD2 . LEU   A 1 436 ? -20.802 -11.298 -18.584 1.00 119.69 ? 456 LEU   A CD2 1 
ATOM   3096 N  N   . ILE   A 1 437 ? -24.135 -7.864  -16.806 1.00 125.57 ? 457 ILE   A N   1 
ATOM   3097 C  CA  . ILE   A 1 437 ? -24.829 -6.586  -16.949 1.00 132.77 ? 457 ILE   A CA  1 
ATOM   3098 C  C   . ILE   A 1 437 ? -23.905 -5.428  -16.589 1.00 137.08 ? 457 ILE   A C   1 
ATOM   3099 O  O   . ILE   A 1 437 ? -23.639 -4.543  -17.411 1.00 136.20 ? 457 ILE   A O   1 
ATOM   3100 C  CB  . ILE   A 1 437 ? -26.106 -6.577  -16.093 1.00 133.63 ? 457 ILE   A CB  1 
ATOM   3101 C  CG1 . ILE   A 1 437 ? -26.964 -7.800  -16.423 1.00 130.07 ? 457 ILE   A CG1 1 
ATOM   3102 C  CG2 . ILE   A 1 437 ? -26.860 -5.275  -16.253 1.00 137.23 ? 457 ILE   A CG2 1 
ATOM   3103 C  CD1 . ILE   A 1 437 ? -28.197 -7.918  -15.586 1.00 127.88 ? 457 ILE   A CD1 1 
ATOM   3104 N  N   . ARG   A 1 438 ? -23.401 -5.422  -15.353 1.00 132.15 ? 458 ARG   A N   1 
ATOM   3105 C  CA  . ARG   A 1 438 ? -22.570 -4.314  -14.889 1.00 128.72 ? 458 ARG   A CA  1 
ATOM   3106 C  C   . ARG   A 1 438 ? -21.322 -4.150  -15.749 1.00 128.90 ? 458 ARG   A C   1 
ATOM   3107 O  O   . ARG   A 1 438 ? -20.926 -3.023  -16.071 1.00 141.21 ? 458 ARG   A O   1 
ATOM   3108 C  CB  . ARG   A 1 438 ? -22.184 -4.530  -13.426 1.00 132.07 ? 458 ARG   A CB  1 
ATOM   3109 C  CG  . ARG   A 1 438 ? -22.777 -3.530  -12.436 1.00 137.81 ? 458 ARG   A CG  1 
ATOM   3110 C  CD  . ARG   A 1 438 ? -24.065 -2.890  -12.935 1.00 145.00 ? 458 ARG   A CD  1 
ATOM   3111 N  NE  . ARG   A 1 438 ? -24.480 -1.794  -12.067 1.00 156.03 ? 458 ARG   A NE  1 
ATOM   3112 C  CZ  . ARG   A 1 438 ? -25.276 -0.799  -12.435 1.00 152.73 ? 458 ARG   A CZ  1 
ATOM   3113 N  NH1 . ARG   A 1 438 ? -25.770 -0.726  -13.660 1.00 147.76 ? 458 ARG   A NH1 1 
ATOM   3114 N  NH2 . ARG   A 1 438 ? -25.584 0.146   -11.551 1.00 158.46 ? 458 ARG   A NH2 1 
ATOM   3115 N  N   . VAL   A 1 439 ? -20.691 -5.261  -16.134 1.00 126.71 ? 459 VAL   A N   1 
ATOM   3116 C  CA  . VAL   A 1 439 ? -19.443 -5.185  -16.891 1.00 136.25 ? 459 VAL   A CA  1 
ATOM   3117 C  C   . VAL   A 1 439 ? -19.699 -4.639  -18.291 1.00 148.29 ? 459 VAL   A C   1 
ATOM   3118 O  O   . VAL   A 1 439 ? -19.000 -3.732  -18.759 1.00 144.64 ? 459 VAL   A O   1 
ATOM   3119 C  CB  . VAL   A 1 439 ? -18.761 -6.565  -16.935 1.00 130.04 ? 459 VAL   A CB  1 
ATOM   3120 C  CG1 . VAL   A 1 439 ? -17.904 -6.709  -18.186 1.00 137.49 ? 459 VAL   A CG1 1 
ATOM   3121 C  CG2 . VAL   A 1 439 ? -17.928 -6.787  -15.682 1.00 143.89 ? 459 VAL   A CG2 1 
ATOM   3122 N  N   . LEU   A 1 440 ? -20.709 -5.176  -18.978 1.00 141.09 ? 460 LEU   A N   1 
ATOM   3123 C  CA  . LEU   A 1 440 ? -20.980 -4.779  -20.354 1.00 142.74 ? 460 LEU   A CA  1 
ATOM   3124 C  C   . LEU   A 1 440 ? -21.694 -3.439  -20.455 1.00 142.88 ? 460 LEU   A C   1 
ATOM   3125 O  O   . LEU   A 1 440 ? -21.627 -2.796  -21.508 1.00 139.27 ? 460 LEU   A O   1 
ATOM   3126 C  CB  . LEU   A 1 440 ? -21.805 -5.858  -21.054 1.00 139.63 ? 460 LEU   A CB  1 
ATOM   3127 C  CG  . LEU   A 1 440 ? -21.043 -7.152  -21.334 1.00 135.18 ? 460 LEU   A CG  1 
ATOM   3128 C  CD1 . LEU   A 1 440 ? -22.010 -8.291  -21.553 1.00 125.78 ? 460 LEU   A CD1 1 
ATOM   3129 C  CD2 . LEU   A 1 440 ? -20.131 -6.986  -22.540 1.00 129.38 ? 460 LEU   A CD2 1 
ATOM   3130 N  N   . GLN   A 1 441 ? -22.372 -3.003  -19.390 1.00 141.06 ? 461 GLN   A N   1 
ATOM   3131 C  CA  . GLN   A 1 441 ? -22.992 -1.683  -19.380 1.00 142.07 ? 461 GLN   A CA  1 
ATOM   3132 C  C   . GLN   A 1 441 ? -21.972 -0.560  -19.496 1.00 149.11 ? 461 GLN   A C   1 
ATOM   3133 O  O   . GLN   A 1 441 ? -22.364 0.588   -19.734 1.00 153.88 ? 461 GLN   A O   1 
ATOM   3134 C  CB  . GLN   A 1 441 ? -23.806 -1.497  -18.098 1.00 136.44 ? 461 GLN   A CB  1 
ATOM   3135 C  CG  . GLN   A 1 441 ? -25.310 -1.433  -18.300 1.00 138.82 ? 461 GLN   A CG  1 
ATOM   3136 C  CD  . GLN   A 1 441 ? -26.063 -1.362  -16.986 1.00 142.89 ? 461 GLN   A CD  1 
ATOM   3137 O  OE1 . GLN   A 1 441 ? -25.460 -1.279  -15.916 1.00 141.95 ? 461 GLN   A OE1 1 
ATOM   3138 N  NE2 . GLN   A 1 441 ? -27.389 -1.396  -17.059 1.00 141.33 ? 461 GLN   A NE2 1 
ATOM   3139 N  N   . ASN   A 1 442 ? -20.686 -0.860  -19.341 1.00 148.61 ? 462 ASN   A N   1 
ATOM   3140 C  CA  . ASN   A 1 442 ? -19.633 0.145   -19.300 1.00 144.51 ? 462 ASN   A CA  1 
ATOM   3141 C  C   . ASN   A 1 442 ? -18.547 -0.069  -20.341 1.00 142.52 ? 462 ASN   A C   1 
ATOM   3142 O  O   . ASN   A 1 442 ? -18.019 0.907   -20.879 1.00 157.10 ? 462 ASN   A O   1 
ATOM   3143 C  CB  . ASN   A 1 442 ? -18.990 0.165   -17.906 1.00 147.82 ? 462 ASN   A CB  1 
ATOM   3144 C  CG  . ASN   A 1 442 ? -19.884 0.794   -16.859 1.00 153.14 ? 462 ASN   A CG  1 
ATOM   3145 O  OD1 . ASN   A 1 442 ? -21.031 0.384   -16.680 1.00 156.25 ? 462 ASN   A OD1 1 
ATOM   3146 N  ND2 . ASN   A 1 442 ? -19.360 1.787   -16.152 1.00 164.00 ? 462 ASN   A ND2 1 
ATOM   3147 N  N   . PHE   A 1 443 ? -18.194 -1.318  -20.642 1.00 143.43 ? 463 PHE   A N   1 
ATOM   3148 C  CA  . PHE   A 1 443 ? -17.024 -1.610  -21.455 1.00 147.70 ? 463 PHE   A CA  1 
ATOM   3149 C  C   . PHE   A 1 443 ? -17.379 -2.507  -22.632 1.00 143.62 ? 463 PHE   A C   1 
ATOM   3150 O  O   . PHE   A 1 443 ? -18.258 -3.369  -22.540 1.00 140.87 ? 463 PHE   A O   1 
ATOM   3151 C  CB  . PHE   A 1 443 ? -15.922 -2.294  -20.632 1.00 145.79 ? 463 PHE   A CB  1 
ATOM   3152 C  CG  . PHE   A 1 443 ? -15.613 -1.607  -19.334 1.00 145.40 ? 463 PHE   A CG  1 
ATOM   3153 C  CD1 . PHE   A 1 443 ? -14.729 -0.542  -19.291 1.00 159.28 ? 463 PHE   A CD1 1 
ATOM   3154 C  CD2 . PHE   A 1 443 ? -16.195 -2.038  -18.153 1.00 145.58 ? 463 PHE   A CD2 1 
ATOM   3155 C  CE1 . PHE   A 1 443 ? -14.440 0.088   -18.096 1.00 161.14 ? 463 PHE   A CE1 1 
ATOM   3156 C  CE2 . PHE   A 1 443 ? -15.910 -1.412  -16.955 1.00 148.68 ? 463 PHE   A CE2 1 
ATOM   3157 C  CZ  . PHE   A 1 443 ? -15.031 -0.348  -16.927 1.00 159.85 ? 463 PHE   A CZ  1 
ATOM   3158 N  N   . SER   A 1 444 ? -16.677 -2.289  -23.739 1.00 136.12 ? 464 SER   A N   1 
ATOM   3159 C  CA  . SER   A 1 444 ? -16.621 -3.234  -24.843 1.00 135.95 ? 464 SER   A CA  1 
ATOM   3160 C  C   . SER   A 1 444 ? -15.360 -4.081  -24.711 1.00 132.09 ? 464 SER   A C   1 
ATOM   3161 O  O   . SER   A 1 444 ? -14.467 -3.790  -23.912 1.00 137.68 ? 464 SER   A O   1 
ATOM   3162 C  CB  . SER   A 1 444 ? -16.647 -2.505  -26.190 1.00 133.62 ? 464 SER   A CB  1 
ATOM   3163 O  OG  . SER   A 1 444 ? -16.517 -3.418  -27.266 1.00 137.71 ? 464 SER   A OG  1 
ATOM   3164 N  N   . PHE   A 1 445 ? -15.294 -5.149  -25.502 1.00 130.57 ? 465 PHE   A N   1 
ATOM   3165 C  CA  . PHE   A 1 445 ? -14.190 -6.098  -25.402 1.00 127.38 ? 465 PHE   A CA  1 
ATOM   3166 C  C   . PHE   A 1 445 ? -13.762 -6.528  -26.795 1.00 133.68 ? 465 PHE   A C   1 
ATOM   3167 O  O   . PHE   A 1 445 ? -14.546 -7.139  -27.528 1.00 144.22 ? 465 PHE   A O   1 
ATOM   3168 C  CB  . PHE   A 1 445 ? -14.584 -7.312  -24.555 1.00 129.59 ? 465 PHE   A CB  1 
ATOM   3169 C  CG  . PHE   A 1 445 ? -14.701 -7.012  -23.086 1.00 123.42 ? 465 PHE   A CG  1 
ATOM   3170 C  CD1 . PHE   A 1 445 ? -15.864 -6.469  -22.567 1.00 126.74 ? 465 PHE   A CD1 1 
ATOM   3171 C  CD2 . PHE   A 1 445 ? -13.645 -7.266  -22.227 1.00 132.66 ? 465 PHE   A CD2 1 
ATOM   3172 C  CE1 . PHE   A 1 445 ? -15.975 -6.188  -21.218 1.00 126.50 ? 465 PHE   A CE1 1 
ATOM   3173 C  CE2 . PHE   A 1 445 ? -13.749 -6.988  -20.877 1.00 128.23 ? 465 PHE   A CE2 1 
ATOM   3174 C  CZ  . PHE   A 1 445 ? -14.916 -6.448  -20.372 1.00 122.44 ? 465 PHE   A CZ  1 
ATOM   3175 N  N   . LYS   A 1 446 ? -12.520 -6.209  -27.152 1.00 130.54 ? 466 LYS   A N   1 
ATOM   3176 C  CA  . LYS   A 1 446 ? -11.889 -6.593  -28.400 1.00 125.34 ? 466 LYS   A CA  1 
ATOM   3177 C  C   . LYS   A 1 446 ? -10.810 -7.641  -28.148 1.00 124.92 ? 466 LYS   A C   1 
ATOM   3178 O  O   . LYS   A 1 446 ? -10.233 -7.693  -27.057 1.00 123.49 ? 466 LYS   A O   1 
ATOM   3179 C  CB  . LYS   A 1 446 ? -11.247 -5.386  -29.095 1.00 127.46 ? 466 LYS   A CB  1 
ATOM   3180 C  CG  . LYS   A 1 446 ? -12.213 -4.291  -29.506 1.00 142.12 ? 466 LYS   A CG  1 
ATOM   3181 C  CD  . LYS   A 1 446 ? -13.370 -4.840  -30.319 1.00 149.51 ? 466 LYS   A CD  1 
ATOM   3182 C  CE  . LYS   A 1 446 ? -14.365 -3.742  -30.652 1.00 149.32 ? 466 LYS   A CE  1 
ATOM   3183 N  NZ  . LYS   A 1 446 ? -13.747 -2.677  -31.491 1.00 140.89 ? 466 LYS   A NZ  1 
ATOM   3184 N  N   . PRO   A 1 447 ? -10.521 -8.496  -29.127 1.00 124.18 ? 467 PRO   A N   1 
ATOM   3185 C  CA  . PRO   A 1 447 ? -9.332  -9.346  -29.024 1.00 124.54 ? 467 PRO   A CA  1 
ATOM   3186 C  C   . PRO   A 1 447 ? -8.076  -8.491  -28.968 1.00 145.82 ? 467 PRO   A C   1 
ATOM   3187 O  O   . PRO   A 1 447 ? -8.055  -7.337  -29.403 1.00 156.84 ? 467 PRO   A O   1 
ATOM   3188 C  CB  . PRO   A 1 447 ? -9.377  -10.186 -30.307 1.00 123.83 ? 467 PRO   A CB  1 
ATOM   3189 C  CG  . PRO   A 1 447 ? -10.804 -10.162 -30.723 1.00 131.11 ? 467 PRO   A CG  1 
ATOM   3190 C  CD  . PRO   A 1 447 ? -11.319 -8.810  -30.323 1.00 130.73 ? 467 PRO   A CD  1 
ATOM   3191 N  N   . CYS   A 1 448 ? -7.018  -9.067  -28.420 1.00 147.58 ? 468 CYS   A N   1 
ATOM   3192 C  CA  . CYS   A 1 448 ? -5.758  -8.354  -28.310 1.00 145.83 ? 468 CYS   A CA  1 
ATOM   3193 C  C   . CYS   A 1 448 ? -4.669  -9.145  -29.031 1.00 163.91 ? 468 CYS   A C   1 
ATOM   3194 O  O   . CYS   A 1 448 ? -4.898  -10.251 -29.527 1.00 147.79 ? 468 CYS   A O   1 
ATOM   3195 C  CB  . CYS   A 1 448 ? -5.402  -8.103  -26.844 1.00 153.25 ? 468 CYS   A CB  1 
ATOM   3196 S  SG  . CYS   A 1 448 ? -3.704  -7.584  -26.596 1.00 198.73 ? 468 CYS   A SG  1 
ATOM   3197 N  N   . LYS   A 1 449 ? -3.470  -8.556  -29.090 1.00 186.80 ? 469 LYS   A N   1 
ATOM   3198 C  CA  . LYS   A 1 449 ? -2.382  -9.144  -29.867 1.00 180.48 ? 469 LYS   A CA  1 
ATOM   3199 C  C   . LYS   A 1 449 ? -2.024  -10.543 -29.381 1.00 188.92 ? 469 LYS   A C   1 
ATOM   3200 O  O   . LYS   A 1 449 ? -1.684  -11.413 -30.191 1.00 181.33 ? 469 LYS   A O   1 
ATOM   3201 C  CB  . LYS   A 1 449 ? -1.157  -8.228  -29.819 1.00 179.64 ? 469 LYS   A CB  1 
ATOM   3202 C  CG  . LYS   A 1 449 ? 0.150   -8.891  -30.230 1.00 178.97 ? 469 LYS   A CG  1 
ATOM   3203 C  CD  . LYS   A 1 449 ? 1.243   -8.658  -29.199 1.00 171.20 ? 469 LYS   A CD  1 
ATOM   3204 C  CE  . LYS   A 1 449 ? 2.483   -9.478  -29.521 1.00 160.54 ? 469 LYS   A CE  1 
ATOM   3205 N  NZ  . LYS   A 1 449 ? 2.524   -10.754 -28.754 1.00 173.52 ? 469 LYS   A NZ  1 
ATOM   3206 N  N   . GLU   A 1 450 ? -2.101  -10.781 -28.073 1.00 216.22 ? 470 GLU   A N   1 
ATOM   3207 C  CA  . GLU   A 1 450 ? -1.773  -12.079 -27.500 1.00 205.36 ? 470 GLU   A CA  1 
ATOM   3208 C  C   . GLU   A 1 450 ? -2.971  -13.011 -27.406 1.00 203.80 ? 470 GLU   A C   1 
ATOM   3209 O  O   . GLU   A 1 450 ? -2.787  -14.192 -27.091 1.00 202.04 ? 470 GLU   A O   1 
ATOM   3210 C  CB  . GLU   A 1 450 ? -1.181  -11.912 -26.095 1.00 204.80 ? 470 GLU   A CB  1 
ATOM   3211 C  CG  . GLU   A 1 450 ? -1.812  -10.789 -25.286 1.00 212.02 ? 470 GLU   A CG  1 
ATOM   3212 C  CD  . GLU   A 1 450 ? -1.169  -9.442  -25.545 1.00 224.45 ? 470 GLU   A CD  1 
ATOM   3213 O  OE1 . GLU   A 1 450 ? -0.821  -8.750  -24.566 1.00 229.72 ? 470 GLU   A OE1 1 
ATOM   3214 O  OE2 . GLU   A 1 450 ? -0.994  -9.081  -26.727 1.00 229.37 ? 470 GLU   A OE2 1 
ATOM   3215 N  N   . THR   A 1 451 ? -4.181  -12.513 -27.658 1.00 176.53 ? 471 THR   A N   1 
ATOM   3216 C  CA  . THR   A 1 451 ? -5.386  -13.302 -27.432 1.00 169.31 ? 471 THR   A CA  1 
ATOM   3217 C  C   . THR   A 1 451 ? -5.339  -14.598 -28.228 1.00 158.24 ? 471 THR   A C   1 
ATOM   3218 O  O   . THR   A 1 451 ? -5.040  -14.601 -29.425 1.00 156.95 ? 471 THR   A O   1 
ATOM   3219 C  CB  . THR   A 1 451 ? -6.629  -12.497 -27.807 1.00 155.09 ? 471 THR   A CB  1 
ATOM   3220 O  OG1 . THR   A 1 451 ? -6.845  -11.471 -26.831 1.00 153.26 ? 471 THR   A OG1 1 
ATOM   3221 C  CG2 . THR   A 1 451 ? -7.853  -13.400 -27.858 1.00 130.94 ? 471 THR   A CG2 1 
ATOM   3222 N  N   . GLN   A 1 452 ? -5.632  -15.705 -27.552 1.00 145.90 ? 472 GLN   A N   1 
ATOM   3223 C  CA  . GLN   A 1 452 ? -5.567  -17.022 -28.171 1.00 145.71 ? 472 GLN   A CA  1 
ATOM   3224 C  C   . GLN   A 1 452 ? -6.790  -17.234 -29.057 1.00 140.10 ? 472 GLN   A C   1 
ATOM   3225 O  O   . GLN   A 1 452 ? -7.907  -17.378 -28.550 1.00 135.54 ? 472 GLN   A O   1 
ATOM   3226 C  CB  . GLN   A 1 452 ? -5.491  -18.118 -27.115 1.00 154.08 ? 472 GLN   A CB  1 
ATOM   3227 C  CG  . GLN   A 1 452 ? -5.738  -19.431 -27.778 1.00 144.03 ? 472 GLN   A CG  1 
ATOM   3228 C  CD  . GLN   A 1 452 ? -4.768  -20.481 -27.370 1.00 138.73 ? 472 GLN   A CD  1 
ATOM   3229 O  OE1 . GLN   A 1 452 ? -4.214  -20.447 -26.277 1.00 141.18 ? 472 GLN   A OE1 1 
ATOM   3230 N  NE2 . GLN   A 1 452 ? -4.432  -21.333 -28.309 1.00 138.64 ? 472 GLN   A NE2 1 
ATOM   3231 N  N   . ILE   A 1 453 ? -6.586  -17.274 -30.373 1.00 137.07 ? 473 ILE   A N   1 
ATOM   3232 C  CA  . ILE   A 1 453 ? -7.683  -17.484 -31.317 1.00 130.81 ? 473 ILE   A CA  1 
ATOM   3233 C  C   . ILE   A 1 453 ? -7.259  -18.482 -32.393 1.00 133.87 ? 473 ILE   A C   1 
ATOM   3234 O  O   . ILE   A 1 453 ? -6.355  -18.191 -33.190 1.00 149.08 ? 473 ILE   A O   1 
ATOM   3235 C  CB  . ILE   A 1 453 ? -8.143  -16.158 -31.941 1.00 122.07 ? 473 ILE   A CB  1 
ATOM   3236 C  CG1 . ILE   A 1 453 ? -8.624  -15.188 -30.853 1.00 121.04 ? 473 ILE   A CG1 1 
ATOM   3237 C  CG2 . ILE   A 1 453 ? -9.255  -16.403 -32.943 1.00 121.38 ? 473 ILE   A CG2 1 
ATOM   3238 C  CD1 . ILE   A 1 453 ? -9.124  -13.857 -31.373 1.00 127.11 ? 473 ILE   A CD1 1 
ATOM   3239 N  N   . PRO   A 1 454 ? -7.881  -19.678 -32.453 1.00 126.60 ? 474 PRO   A N   1 
ATOM   3240 C  CA  . PRO   A 1 454 ? -8.982  -20.144 -31.597 1.00 120.72 ? 474 PRO   A CA  1 
ATOM   3241 C  C   . PRO   A 1 454 ? -8.478  -20.543 -30.203 1.00 126.58 ? 474 PRO   A C   1 
ATOM   3242 O  O   . PRO   A 1 454 ? -7.292  -20.793 -30.002 1.00 132.45 ? 474 PRO   A O   1 
ATOM   3243 C  CB  . PRO   A 1 454 ? -9.532  -21.350 -32.400 1.00 122.33 ? 474 PRO   A CB  1 
ATOM   3244 C  CG  . PRO   A 1 454 ? -8.419  -21.703 -33.441 1.00 126.18 ? 474 PRO   A CG  1 
ATOM   3245 C  CD  . PRO   A 1 454 ? -7.227  -20.875 -33.018 1.00 140.76 ? 474 PRO   A CD  1 
ATOM   3246 N  N   . LEU   A 1 455 ? -9.364  -20.610 -29.217 1.00 120.62 ? 475 LEU   A N   1 
ATOM   3247 C  CA  . LEU   A 1 455 ? -8.965  -20.965 -27.861 1.00 120.38 ? 475 LEU   A CA  1 
ATOM   3248 C  C   . LEU   A 1 455 ? -8.820  -22.478 -27.763 1.00 126.71 ? 475 LEU   A C   1 
ATOM   3249 O  O   . LEU   A 1 455 ? -9.761  -23.213 -28.083 1.00 131.09 ? 475 LEU   A O   1 
ATOM   3250 C  CB  . LEU   A 1 455 ? -9.984  -20.433 -26.848 1.00 114.78 ? 475 LEU   A CB  1 
ATOM   3251 C  CG  . LEU   A 1 455 ? -10.040 -20.925 -25.394 1.00 114.91 ? 475 LEU   A CG  1 
ATOM   3252 C  CD1 . LEU   A 1 455 ? -10.680 -19.855 -24.525 1.00 108.74 ? 475 LEU   A CD1 1 
ATOM   3253 C  CD2 . LEU   A 1 455 ? -10.827 -22.225 -25.236 1.00 116.55 ? 475 LEU   A CD2 1 
ATOM   3254 N  N   . LYS   A 1 456 ? -7.641  -22.947 -27.349 1.00 128.37 ? 476 LYS   A N   1 
ATOM   3255 C  CA  . LYS   A 1 456 ? -7.497  -24.363 -27.052 1.00 121.92 ? 476 LYS   A CA  1 
ATOM   3256 C  C   . LYS   A 1 456 ? -8.036  -24.650 -25.660 1.00 126.03 ? 476 LYS   A C   1 
ATOM   3257 O  O   . LYS   A 1 456 ? -7.922  -23.832 -24.743 1.00 127.97 ? 476 LYS   A O   1 
ATOM   3258 C  CB  . LYS   A 1 456 ? -6.042  -24.847 -27.123 1.00 127.37 ? 476 LYS   A CB  1 
ATOM   3259 C  CG  . LYS   A 1 456 ? -5.137  -24.242 -28.181 1.00 139.26 ? 476 LYS   A CG  1 
ATOM   3260 C  CD  . LYS   A 1 456 ? -3.710  -24.809 -28.048 1.00 158.47 ? 476 LYS   A CD  1 
ATOM   3261 C  CE  . LYS   A 1 456 ? -2.597  -23.769 -28.090 1.00 150.83 ? 476 LYS   A CE  1 
ATOM   3262 N  NZ  . LYS   A 1 456 ? -2.532  -22.989 -26.822 1.00 143.97 ? 476 LYS   A NZ  1 
ATOM   3263 N  N   . LEU   A 1 457 ? -8.637  -25.822 -25.513 1.00 130.77 ? 477 LEU   A N   1 
ATOM   3264 C  CA  . LEU   A 1 457 ? -9.021  -26.305 -24.200 1.00 131.41 ? 477 LEU   A CA  1 
ATOM   3265 C  C   . LEU   A 1 457 ? -7.815  -26.932 -23.513 1.00 143.84 ? 477 LEU   A C   1 
ATOM   3266 O  O   . LEU   A 1 457 ? -6.905  -27.451 -24.165 1.00 154.42 ? 477 LEU   A O   1 
ATOM   3267 C  CB  . LEU   A 1 457 ? -10.156 -27.321 -24.316 1.00 115.16 ? 477 LEU   A CB  1 
ATOM   3268 C  CG  . LEU   A 1 457 ? -11.548 -26.704 -24.458 1.00 112.69 ? 477 LEU   A CG  1 
ATOM   3269 C  CD1 . LEU   A 1 457 ? -12.615 -27.779 -24.438 1.00 118.37 ? 477 LEU   A CD1 1 
ATOM   3270 C  CD2 . LEU   A 1 457 ? -11.795 -25.681 -23.356 1.00 120.56 ? 477 LEU   A CD2 1 
ATOM   3271 N  N   . SER   A 1 458 ? -7.802  -26.876 -22.179 1.00 149.64 ? 478 SER   A N   1 
ATOM   3272 C  CA  . SER   A 1 458 ? -6.707  -27.535 -21.423 1.00 159.05 ? 478 SER   A CA  1 
ATOM   3273 C  C   . SER   A 1 458 ? -6.952  -29.044 -21.423 1.00 171.77 ? 478 SER   A C   1 
ATOM   3274 O  O   . SER   A 1 458 ? -7.897  -29.489 -22.098 1.00 170.35 ? 478 SER   A O   1 
ATOM   3275 C  CB  . SER   A 1 458 ? -6.613  -27.009 -20.023 1.00 156.17 ? 478 SER   A CB  1 
ATOM   3276 O  OG  . SER   A 1 458 ? -5.583  -27.668 -19.303 1.00 169.40 ? 478 SER   A OG  1 
ATOM   3277 N  N   . LEU   A 1 459 ? -6.137  -29.800 -20.691 1.00 209.95 ? 479 LEU   A N   1 
ATOM   3278 C  CA  . LEU   A 1 459 ? -6.285  -31.277 -20.731 1.00 207.02 ? 479 LEU   A CA  1 
ATOM   3279 C  C   . LEU   A 1 459 ? -6.850  -31.775 -19.398 1.00 210.72 ? 479 LEU   A C   1 
ATOM   3280 O  O   . LEU   A 1 459 ? -6.273  -31.436 -18.349 1.00 212.44 ? 479 LEU   A O   1 
ATOM   3281 C  CB  . LEU   A 1 459 ? -4.928  -31.912 -21.043 1.00 209.35 ? 479 LEU   A CB  1 
ATOM   3282 C  CG  . LEU   A 1 459 ? -4.375  -31.586 -22.429 1.00 212.84 ? 479 LEU   A CG  1 
ATOM   3283 C  CD1 . LEU   A 1 459 ? -2.967  -32.138 -22.588 1.00 211.47 ? 479 LEU   A CD1 1 
ATOM   3284 C  CD2 . LEU   A 1 459 ? -5.286  -32.128 -23.518 1.00 215.40 ? 479 LEU   A CD2 1 
ATOM   3285 N  N   . GLY   A 1 460 ? -7.945  -32.540 -19.451 1.00 185.25 ? 480 GLY   A N   1 
ATOM   3286 C  CA  . GLY   A 1 460 ? -8.552  -33.097 -18.228 1.00 180.78 ? 480 GLY   A CA  1 
ATOM   3287 C  C   . GLY   A 1 460 ? -8.963  -32.015 -17.249 1.00 184.29 ? 480 GLY   A C   1 
ATOM   3288 O  O   . GLY   A 1 460 ? -9.657  -31.069 -17.670 1.00 179.83 ? 480 GLY   A O   1 
ATOM   3289 N  N   . GLY   A 1 461 ? -8.550  -32.148 -15.987 1.00 175.09 ? 481 GLY   A N   1 
ATOM   3290 C  CA  . GLY   A 1 461 ? -8.960  -31.181 -14.955 1.00 167.93 ? 481 GLY   A CA  1 
ATOM   3291 C  C   . GLY   A 1 461 ? -10.392 -30.752 -15.175 1.00 164.81 ? 481 GLY   A C   1 
ATOM   3292 O  O   . GLY   A 1 461 ? -11.247 -31.636 -15.356 1.00 160.89 ? 481 GLY   A O   1 
ATOM   3293 N  N   . LEU   A 1 462 ? -10.644 -29.440 -15.174 1.00 168.53 ? 482 LEU   A N   1 
ATOM   3294 C  CA  . LEU   A 1 462 ? -11.999 -28.918 -15.487 1.00 166.05 ? 482 LEU   A CA  1 
ATOM   3295 C  C   . LEU   A 1 462 ? -11.957 -28.381 -16.920 1.00 166.80 ? 482 LEU   A C   1 
ATOM   3296 O  O   . LEU   A 1 462 ? -10.868 -28.423 -17.526 1.00 164.53 ? 482 LEU   A O   1 
ATOM   3297 C  CB  . LEU   A 1 462 ? -12.385 -27.870 -14.441 1.00 168.13 ? 482 LEU   A CB  1 
ATOM   3298 C  CG  . LEU   A 1 462 ? -13.465 -28.300 -13.451 1.00 169.52 ? 482 LEU   A CG  1 
ATOM   3299 C  CD1 . LEU   A 1 462 ? -14.634 -27.328 -13.468 1.00 174.06 ? 482 LEU   A CD1 1 
ATOM   3300 C  CD2 . LEU   A 1 462 ? -13.937 -29.716 -13.745 1.00 167.44 ? 482 LEU   A CD2 1 
ATOM   3301 N  N   . LEU   A 1 463 ? -13.084 -27.892 -17.442 1.00 145.40 ? 483 LEU   A N   1 
ATOM   3302 C  CA  . LEU   A 1 463 ? -13.041 -27.203 -18.760 1.00 142.85 ? 483 LEU   A CA  1 
ATOM   3303 C  C   . LEU   A 1 463 ? -12.355 -25.850 -18.550 1.00 142.81 ? 483 LEU   A C   1 
ATOM   3304 O  O   . LEU   A 1 463 ? -13.064 -24.873 -18.247 1.00 134.79 ? 483 LEU   A O   1 
ATOM   3305 C  CB  . LEU   A 1 463 ? -14.457 -27.053 -19.322 1.00 125.76 ? 483 LEU   A CB  1 
ATOM   3306 C  CG  . LEU   A 1 463 ? -14.565 -27.347 -20.817 1.00 118.99 ? 483 LEU   A CG  1 
ATOM   3307 C  CD1 . LEU   A 1 463 ? -13.542 -28.396 -21.223 1.00 116.98 ? 483 LEU   A CD1 1 
ATOM   3308 C  CD2 . LEU   A 1 463 ? -15.964 -27.805 -21.188 1.00 106.51 ? 483 LEU   A CD2 1 
ATOM   3309 N  N   . GLN   A 1 464 ? -11.026 -25.810 -18.691 1.00 138.10 ? 484 GLN   A N   1 
ATOM   3310 C  CA  . GLN   A 1 464 ? -10.262 -24.547 -18.496 1.00 136.68 ? 484 GLN   A CA  1 
ATOM   3311 C  C   . GLN   A 1 464 ? -9.375  -24.303 -19.721 1.00 132.06 ? 484 GLN   A C   1 
ATOM   3312 O  O   . GLN   A 1 464 ? -9.013  -25.286 -20.389 1.00 137.48 ? 484 GLN   A O   1 
ATOM   3313 C  CB  . GLN   A 1 464 ? -9.435  -24.627 -17.212 1.00 144.09 ? 484 GLN   A CB  1 
ATOM   3314 C  CG  . GLN   A 1 464 ? -10.280 -24.668 -15.947 1.00 150.33 ? 484 GLN   A CG  1 
ATOM   3315 C  CD  . GLN   A 1 464 ? -9.439  -24.819 -14.703 1.00 161.80 ? 484 GLN   A CD  1 
ATOM   3316 O  OE1 . GLN   A 1 464 ? -8.325  -25.334 -14.741 1.00 159.20 ? 484 GLN   A OE1 1 
ATOM   3317 N  NE2 . GLN   A 1 464 ? -9.970  -24.360 -13.581 1.00 156.87 ? 484 GLN   A NE2 1 
ATOM   3318 N  N   . PRO   A 1 465 ? -9.053  -23.040 -20.076 1.00 142.96 ? 485 PRO   A N   1 
ATOM   3319 C  CA  . PRO   A 1 465 ? -8.269  -22.747 -21.277 1.00 144.26 ? 485 PRO   A CA  1 
ATOM   3320 C  C   . PRO   A 1 465 ? -6.783  -22.965 -21.043 1.00 139.51 ? 485 PRO   A C   1 
ATOM   3321 O  O   . PRO   A 1 465 ? -6.263  -22.760 -19.944 1.00 132.42 ? 485 PRO   A O   1 
ATOM   3322 C  CB  . PRO   A 1 465 ? -8.573  -21.267 -21.555 1.00 138.69 ? 485 PRO   A CB  1 
ATOM   3323 C  CG  . PRO   A 1 465 ? -9.672  -20.881 -20.601 1.00 128.36 ? 485 PRO   A CG  1 
ATOM   3324 C  CD  . PRO   A 1 465 ? -9.570  -21.814 -19.448 1.00 122.20 ? 485 PRO   A CD  1 
ATOM   3325 N  N   . GLU   A 1 466 ? -6.105  -23.401 -22.105 1.00 137.63 ? 486 GLU   A N   1 
ATOM   3326 C  CA  . GLU   A 1 466 ? -4.654  -23.550 -22.095 1.00 141.28 ? 486 GLU   A CA  1 
ATOM   3327 C  C   . GLU   A 1 466 ? -3.849  -22.304 -21.749 1.00 144.32 ? 486 GLU   A C   1 
ATOM   3328 O  O   . GLU   A 1 466 ? -3.197  -22.250 -20.702 1.00 144.16 ? 486 GLU   A O   1 
ATOM   3329 C  CB  . GLU   A 1 466 ? -4.159  -24.009 -23.468 1.00 145.29 ? 486 GLU   A CB  1 
ATOM   3330 C  CG  . GLU   A 1 466 ? -2.767  -24.609 -23.458 1.00 158.62 ? 486 GLU   A CG  1 
ATOM   3331 C  CD  . GLU   A 1 466 ? -2.476  -25.409 -24.707 1.00 159.50 ? 486 GLU   A CD  1 
ATOM   3332 O  OE1 . GLU   A 1 466 ? -1.315  -25.394 -25.167 1.00 154.29 ? 486 GLU   A OE1 1 
ATOM   3333 O  OE2 . GLU   A 1 466 ? -3.403  -26.070 -25.217 1.00 165.10 ? 486 GLU   A OE2 1 
ATOM   3334 N  N   . LYS   A 1 467 ? -3.879  -21.307 -22.622 1.00 131.32 ? 487 LYS   A N   1 
ATOM   3335 C  CA  . LYS   A 1 467 ? -3.408  -19.979 -22.258 1.00 135.73 ? 487 LYS   A CA  1 
ATOM   3336 C  C   . LYS   A 1 467 ? -4.560  -19.174 -21.662 1.00 133.66 ? 487 LYS   A C   1 
ATOM   3337 O  O   . LYS   A 1 467 ? -5.695  -19.276 -22.135 1.00 137.62 ? 487 LYS   A O   1 
ATOM   3338 C  CB  . LYS   A 1 467 ? -2.842  -19.253 -23.477 1.00 136.40 ? 487 LYS   A CB  1 
ATOM   3339 C  CG  . LYS   A 1 467 ? -1.812  -20.048 -24.270 1.00 142.12 ? 487 LYS   A CG  1 
ATOM   3340 C  CD  . LYS   A 1 467 ? -1.426  -19.321 -25.558 1.00 140.11 ? 487 LYS   A CD  1 
ATOM   3341 C  CE  . LYS   A 1 467 ? 0.037   -19.515 -25.937 1.00 132.80 ? 487 LYS   A CE  1 
ATOM   3342 N  NZ  . LYS   A 1 467 ? 0.930   -18.503 -25.310 1.00 125.01 ? 487 LYS   A NZ  1 
ATOM   3343 N  N   . PRO   A 1 468 ? -4.302  -18.389 -20.611 1.00 130.72 ? 488 PRO   A N   1 
ATOM   3344 C  CA  . PRO   A 1 468 ? -5.362  -17.564 -20.015 1.00 127.20 ? 488 PRO   A CA  1 
ATOM   3345 C  C   . PRO   A 1 468 ? -6.058  -16.660 -21.022 1.00 128.60 ? 488 PRO   A C   1 
ATOM   3346 O  O   . PRO   A 1 468 ? -5.514  -16.371 -22.093 1.00 132.22 ? 488 PRO   A O   1 
ATOM   3347 C  CB  . PRO   A 1 468 ? -4.603  -16.743 -18.971 1.00 123.36 ? 488 PRO   A CB  1 
ATOM   3348 C  CG  . PRO   A 1 468 ? -3.515  -17.660 -18.528 1.00 131.60 ? 488 PRO   A CG  1 
ATOM   3349 C  CD  . PRO   A 1 468 ? -3.103  -18.444 -19.756 1.00 138.42 ? 488 PRO   A CD  1 
ATOM   3350 N  N   . VAL   A 1 469 ? -7.260  -16.204 -20.683 1.00 123.53 ? 489 VAL   A N   1 
ATOM   3351 C  CA  . VAL   A 1 469 ? -8.048  -15.348 -21.561 1.00 134.72 ? 489 VAL   A CA  1 
ATOM   3352 C  C   . VAL   A 1 469 ? -7.659  -13.898 -21.299 1.00 132.64 ? 489 VAL   A C   1 
ATOM   3353 O  O   . VAL   A 1 469 ? -7.899  -13.370 -20.207 1.00 130.59 ? 489 VAL   A O   1 
ATOM   3354 C  CB  . VAL   A 1 469 ? -9.553  -15.564 -21.340 1.00 115.71 ? 489 VAL   A CB  1 
ATOM   3355 C  CG1 . VAL   A 1 469 ? -10.353 -14.448 -21.997 1.00 118.07 ? 489 VAL   A CG1 1 
ATOM   3356 C  CG2 . VAL   A 1 469 ? -9.979  -16.926 -21.866 1.00 120.16 ? 489 VAL   A CG2 1 
ATOM   3357 N  N   . VAL   A 1 470 ? -7.062  -13.251 -22.299 1.00 120.56 ? 490 VAL   A N   1 
ATOM   3358 C  CA  . VAL   A 1 470 ? -6.625  -11.863 -22.196 1.00 141.02 ? 490 VAL   A CA  1 
ATOM   3359 C  C   . VAL   A 1 470 ? -7.149  -11.091 -23.400 1.00 141.03 ? 490 VAL   A C   1 
ATOM   3360 O  O   . VAL   A 1 470 ? -6.926  -11.492 -24.547 1.00 148.08 ? 490 VAL   A O   1 
ATOM   3361 C  CB  . VAL   A 1 470 ? -5.092  -11.747 -22.093 1.00 141.80 ? 490 VAL   A CB  1 
ATOM   3362 C  CG1 . VAL   A 1 470 ? -4.639  -12.085 -20.689 1.00 137.81 ? 490 VAL   A CG1 1 
ATOM   3363 C  CG2 . VAL   A 1 470 ? -4.416  -12.661 -23.098 1.00 145.30 ? 490 VAL   A CG2 1 
ATOM   3364 N  N   . LEU   A 1 471 ? -7.821  -9.973  -23.132 1.00 136.57 ? 491 LEU   A N   1 
ATOM   3365 C  CA  . LEU   A 1 471 ? -8.607  -9.244  -24.116 1.00 138.09 ? 491 LEU   A CA  1 
ATOM   3366 C  C   . LEU   A 1 471 ? -8.406  -7.749  -23.908 1.00 145.05 ? 491 LEU   A C   1 
ATOM   3367 O  O   . LEU   A 1 471 ? -8.100  -7.303  -22.799 1.00 144.91 ? 491 LEU   A O   1 
ATOM   3368 C  CB  . LEU   A 1 471 ? -10.091 -9.609  -23.969 1.00 132.64 ? 491 LEU   A CB  1 
ATOM   3369 C  CG  . LEU   A 1 471 ? -10.618 -10.991 -24.367 1.00 132.87 ? 491 LEU   A CG  1 
ATOM   3370 C  CD1 . LEU   A 1 471 ? -12.048 -10.867 -24.800 1.00 136.09 ? 491 LEU   A CD1 1 
ATOM   3371 C  CD2 . LEU   A 1 471 ? -9.821  -11.564 -25.521 1.00 122.82 ? 491 LEU   A CD2 1 
ATOM   3372 N  N   . LYS   A 1 472 ? -8.571  -6.976  -24.979 1.00 142.58 ? 492 LYS   A N   1 
ATOM   3373 C  CA  . LYS   A 1 472 ? -8.579  -5.527  -24.843 1.00 132.37 ? 492 LYS   A CA  1 
ATOM   3374 C  C   . LYS   A 1 472 ? -9.915  -5.057  -24.279 1.00 130.85 ? 492 LYS   A C   1 
ATOM   3375 O  O   . LYS   A 1 472 ? -10.971 -5.630  -24.562 1.00 130.60 ? 492 LYS   A O   1 
ATOM   3376 C  CB  . LYS   A 1 472 ? -8.320  -4.836  -26.183 1.00 130.63 ? 492 LYS   A CB  1 
ATOM   3377 C  CG  . LYS   A 1 472 ? -7.452  -3.586  -26.065 1.00 135.77 ? 492 LYS   A CG  1 
ATOM   3378 C  CD  . LYS   A 1 472 ? -7.114  -2.990  -27.422 1.00 140.49 ? 492 LYS   A CD  1 
ATOM   3379 C  CE  . LYS   A 1 472 ? -7.846  -1.672  -27.637 1.00 157.94 ? 492 LYS   A CE  1 
ATOM   3380 N  NZ  . LYS   A 1 472 ? -7.992  -1.332  -29.079 1.00 157.13 ? 492 LYS   A NZ  1 
ATOM   3381 N  N   . VAL   A 1 473 ? -9.858  -4.004  -23.467 1.00 132.73 ? 493 VAL   A N   1 
ATOM   3382 C  CA  . VAL   A 1 473 ? -11.040 -3.400  -22.864 1.00 138.21 ? 493 VAL   A CA  1 
ATOM   3383 C  C   . VAL   A 1 473 ? -11.080 -1.928  -23.246 1.00 159.65 ? 493 VAL   A C   1 
ATOM   3384 O  O   . VAL   A 1 473 ? -10.068 -1.225  -23.142 1.00 156.84 ? 493 VAL   A O   1 
ATOM   3385 C  CB  . VAL   A 1 473 ? -11.053 -3.569  -21.334 1.00 145.15 ? 493 VAL   A CB  1 
ATOM   3386 C  CG1 . VAL   A 1 473 ? -12.447 -3.318  -20.791 1.00 140.38 ? 493 VAL   A CG1 1 
ATOM   3387 C  CG2 . VAL   A 1 473 ? -10.591 -4.965  -20.953 1.00 140.06 ? 493 VAL   A CG2 1 
ATOM   3388 N  N   . GLU   A 1 474 ? -12.246 -1.470  -23.693 1.00 165.49 ? 494 GLU   A N   1 
ATOM   3389 C  CA  . GLU   A 1 474 ? -12.461 -0.078  -24.053 1.00 167.43 ? 494 GLU   A CA  1 
ATOM   3390 C  C   . GLU   A 1 474 ? -13.676 0.443   -23.301 1.00 168.44 ? 494 GLU   A C   1 
ATOM   3391 O  O   . GLU   A 1 474 ? -14.632 -0.294  -23.049 1.00 164.09 ? 494 GLU   A O   1 
ATOM   3392 C  CB  . GLU   A 1 474 ? -12.657 0.083   -25.567 1.00 172.79 ? 494 GLU   A CB  1 
ATOM   3393 C  CG  . GLU   A 1 474 ? -11.406 -0.215  -26.379 1.00 167.28 ? 494 GLU   A CG  1 
ATOM   3394 C  CD  . GLU   A 1 474 ? -11.689 -0.351  -27.862 1.00 167.81 ? 494 GLU   A CD  1 
ATOM   3395 O  OE1 . GLU   A 1 474 ? -12.798 -0.801  -28.219 1.00 163.83 ? 494 GLU   A OE1 1 
ATOM   3396 O  OE2 . GLU   A 1 474 ? -10.801 -0.009  -28.671 1.00 174.83 ? 494 GLU   A OE2 1 
ATOM   3397 N  N   . SER   A 1 475 ? -13.628 1.721   -22.938 1.00 161.33 ? 495 SER   A N   1 
ATOM   3398 C  CA  . SER   A 1 475 ? -14.663 2.341   -22.121 1.00 161.31 ? 495 SER   A CA  1 
ATOM   3399 C  C   . SER   A 1 475 ? -15.686 3.032   -23.013 1.00 161.71 ? 495 SER   A C   1 
ATOM   3400 O  O   . SER   A 1 475 ? -15.319 3.767   -23.936 1.00 168.02 ? 495 SER   A O   1 
ATOM   3401 C  CB  . SER   A 1 475 ? -14.052 3.341   -21.139 1.00 163.95 ? 495 SER   A CB  1 
ATOM   3402 O  OG  . SER   A 1 475 ? -14.886 3.515   -20.006 1.00 174.55 ? 495 SER   A OG  1 
ATOM   3403 N  N   . ARG   A 1 476 ? -16.964 2.798   -22.730 1.00 155.45 ? 496 ARG   A N   1 
ATOM   3404 C  CA  . ARG   A 1 476 ? -18.048 3.400   -23.498 1.00 153.14 ? 496 ARG   A CA  1 
ATOM   3405 C  C   . ARG   A 1 476 ? -18.438 4.758   -22.924 1.00 161.00 ? 496 ARG   A C   1 
ATOM   3406 O  O   . ARG   A 1 476 ? -17.868 5.785   -23.292 1.00 169.09 ? 496 ARG   A O   1 
ATOM   3407 C  CB  . ARG   A 1 476 ? -19.264 2.471   -23.523 1.00 149.75 ? 496 ARG   A CB  1 
ATOM   3408 C  CG  . ARG   A 1 476 ? -18.950 1.050   -23.960 1.00 143.20 ? 496 ARG   A CG  1 
ATOM   3409 C  CD  . ARG   A 1 476 ? -20.179 0.160   -23.874 1.00 133.27 ? 496 ARG   A CD  1 
ATOM   3410 N  NE  . ARG   A 1 476 ? -21.067 0.339   -25.016 1.00 134.16 ? 496 ARG   A NE  1 
ATOM   3411 C  CZ  . ARG   A 1 476 ? -22.374 0.117   -24.990 1.00 138.76 ? 496 ARG   A CZ  1 
ATOM   3412 N  NH1 . ARG   A 1 476 ? -22.983 -0.296  -23.890 1.00 138.69 ? 496 ARG   A NH1 1 
ATOM   3413 N  NH2 . ARG   A 1 476 ? -23.088 0.313   -26.094 1.00 140.24 ? 496 ARG   A NH2 1 
HETATM 3414 C  CHA . HEM   B 2 .   ? -23.198 -30.173 -8.935  1.00 73.31  ? 601 HEM   A CHA 1 
HETATM 3415 C  CHB . HEM   B 2 .   ? -22.563 -27.472 -12.929 1.00 76.41  ? 601 HEM   A CHB 1 
HETATM 3416 C  CHC . HEM   B 2 .   ? -21.961 -23.605 -10.074 1.00 80.75  ? 601 HEM   A CHC 1 
HETATM 3417 C  CHD . HEM   B 2 .   ? -22.802 -26.246 -6.092  1.00 76.33  ? 601 HEM   A CHD 1 
HETATM 3418 C  C1A . HEM   B 2 .   ? -23.061 -29.793 -10.254 1.00 77.65  ? 601 HEM   A C1A 1 
HETATM 3419 C  C2A . HEM   B 2 .   ? -23.123 -30.668 -11.408 1.00 84.20  ? 601 HEM   A C2A 1 
HETATM 3420 C  C3A . HEM   B 2 .   ? -22.950 -29.928 -12.506 1.00 71.46  ? 601 HEM   A C3A 1 
HETATM 3421 C  C4A . HEM   B 2 .   ? -22.770 -28.551 -12.097 1.00 74.99  ? 601 HEM   A C4A 1 
HETATM 3422 C  CMA . HEM   B 2 .   ? -22.942 -30.443 -13.961 1.00 66.65  ? 601 HEM   A CMA 1 
HETATM 3423 C  CAA . HEM   B 2 .   ? -23.351 -32.194 -11.369 1.00 69.07  ? 601 HEM   A CAA 1 
HETATM 3424 C  CBA . HEM   B 2 .   ? -24.828 -32.478 -11.619 1.00 69.61  ? 601 HEM   A CBA 1 
HETATM 3425 C  CGA . HEM   B 2 .   ? -25.066 -33.964 -11.657 1.00 85.23  ? 601 HEM   A CGA 1 
HETATM 3426 O  O1A . HEM   B 2 .   ? -26.136 -34.383 -12.170 1.00 76.62  ? 601 HEM   A O1A 1 
HETATM 3427 O  O2A . HEM   B 2 .   ? -24.187 -34.728 -11.182 1.00 89.97  ? 601 HEM   A O2A 1 
HETATM 3428 C  C1B . HEM   B 2 .   ? -22.353 -26.177 -12.508 1.00 79.34  ? 601 HEM   A C1B 1 
HETATM 3429 C  C2B . HEM   B 2 .   ? -22.143 -25.018 -13.355 1.00 79.93  ? 601 HEM   A C2B 1 
HETATM 3430 C  C3B . HEM   B 2 .   ? -21.979 -23.948 -12.552 1.00 86.74  ? 601 HEM   A C3B 1 
HETATM 3431 C  C4B . HEM   B 2 .   ? -22.077 -24.408 -11.185 1.00 81.52  ? 601 HEM   A C4B 1 
HETATM 3432 C  CMB . HEM   B 2 .   ? -22.131 -25.078 -14.900 1.00 81.81  ? 601 HEM   A CMB 1 
HETATM 3433 C  CAB . HEM   B 2 .   ? -21.720 -22.457 -12.890 1.00 86.01  ? 601 HEM   A CAB 1 
HETATM 3434 C  CBB . HEM   B 2 .   ? -21.562 -21.967 -14.124 1.00 84.11  ? 601 HEM   A CBB 1 
HETATM 3435 C  C1C . HEM   B 2 .   ? -22.190 -23.962 -8.766  1.00 85.52  ? 601 HEM   A C1C 1 
HETATM 3436 C  C2C . HEM   B 2 .   ? -22.267 -23.047 -7.652  1.00 95.48  ? 601 HEM   A C2C 1 
HETATM 3437 C  C3C . HEM   B 2 .   ? -22.497 -23.751 -6.544  1.00 94.65  ? 601 HEM   A C3C 1 
HETATM 3438 C  C4C . HEM   B 2 .   ? -22.578 -25.159 -6.915  1.00 87.12  ? 601 HEM   A C4C 1 
HETATM 3439 C  CMC . HEM   B 2 .   ? -22.105 -21.514 -7.735  1.00 98.78  ? 601 HEM   A CMC 1 
HETATM 3440 C  CAC . HEM   B 2 .   ? -22.640 -23.110 -5.145  1.00 87.26  ? 601 HEM   A CAC 1 
HETATM 3441 C  CBC . HEM   B 2 .   ? -22.737 -23.849 -4.040  1.00 93.21  ? 601 HEM   A CBC 1 
HETATM 3442 C  C1D . HEM   B 2 .   ? -22.931 -27.555 -6.506  1.00 83.15  ? 601 HEM   A C1D 1 
HETATM 3443 C  C2D . HEM   B 2 .   ? -23.037 -28.725 -5.656  1.00 80.46  ? 601 HEM   A C2D 1 
HETATM 3444 C  C3D . HEM   B 2 .   ? -23.139 -29.798 -6.445  1.00 82.68  ? 601 HEM   A C3D 1 
HETATM 3445 C  C4D . HEM   B 2 .   ? -23.113 -29.358 -7.824  1.00 80.48  ? 601 HEM   A C4D 1 
HETATM 3446 C  CMD . HEM   B 2 .   ? -23.023 -28.738 -4.111  1.00 68.13  ? 601 HEM   A CMD 1 
HETATM 3447 C  CAD . HEM   B 2 .   ? -23.293 -31.258 -5.975  1.00 73.96  ? 601 HEM   A CAD 1 
HETATM 3448 C  CBD . HEM   B 2 .   ? -24.789 -31.455 -5.754  1.00 80.88  ? 601 HEM   A CBD 1 
HETATM 3449 C  CGD . HEM   B 2 .   ? -25.105 -32.835 -5.245  1.00 88.01  ? 601 HEM   A CGD 1 
HETATM 3450 O  O1D . HEM   B 2 .   ? -26.142 -32.980 -4.547  1.00 82.36  ? 601 HEM   A O1D 1 
HETATM 3451 O  O2D . HEM   B 2 .   ? -24.326 -33.781 -5.527  1.00 80.68  ? 601 HEM   A O2D 1 
HETATM 3452 N  NA  . HEM   B 2 .   ? -22.847 -28.508 -10.715 1.00 74.14  ? 601 HEM   A NA  1 
HETATM 3453 N  NB  . HEM   B 2 .   ? -22.305 -25.767 -11.191 1.00 83.69  ? 601 HEM   A NB  1 
HETATM 3454 N  NC  . HEM   B 2 .   ? -22.385 -25.241 -8.283  1.00 91.77  ? 601 HEM   A NC  1 
HETATM 3455 N  ND  . HEM   B 2 .   ? -22.981 -27.983 -7.822  1.00 88.54  ? 601 HEM   A ND  1 
HETATM 3456 FE FE  . HEM   B 2 .   ? -22.744 -26.853 -9.509  1.00 81.49  ? 601 HEM   A FE  1 
HETATM 3457 C  C02 . A1A06 C 3 .   ? -11.228 -37.109 -10.804 1.00 154.88 ? 602 A1A06 A C02 1 
HETATM 3458 C  C05 . A1A06 C 3 .   ? -12.546 -37.942 -10.613 1.00 153.11 ? 602 A1A06 A C05 1 
HETATM 3459 C  C08 . A1A06 C 3 .   ? -14.031 -35.911 -10.864 1.00 140.82 ? 602 A1A06 A C08 1 
HETATM 3460 C  C09 . A1A06 C 3 .   ? -14.777 -35.003 -9.783  1.00 127.25 ? 602 A1A06 A C09 1 
HETATM 3461 C  C12 . A1A06 C 3 .   ? -16.735 -34.414 -8.175  1.00 103.68 ? 602 A1A06 A C12 1 
HETATM 3462 C  C13 . A1A06 C 3 .   ? -16.558 -35.027 -6.733  1.00 110.89 ? 602 A1A06 A C13 1 
HETATM 3463 C  C15 . A1A06 C 3 .   ? -14.695 -32.540 -5.824  1.00 117.44 ? 602 A1A06 A C15 1 
HETATM 3464 C  C16 . A1A06 C 3 .   ? -13.648 -32.183 -4.736  1.00 122.69 ? 602 A1A06 A C16 1 
HETATM 3465 C  C17 . A1A06 C 3 .   ? -13.410 -30.683 -4.454  1.00 120.93 ? 602 A1A06 A C17 1 
HETATM 3466 C  C18 . A1A06 C 3 .   ? -12.732 -29.847 -5.365  1.00 120.69 ? 602 A1A06 A C18 1 
HETATM 3467 C  C19 . A1A06 C 3 .   ? -12.508 -28.484 -5.108  1.00 114.32 ? 602 A1A06 A C19 1 
HETATM 3468 C  C20 . A1A06 C 3 .   ? -12.961 -27.913 -3.917  1.00 112.08 ? 602 A1A06 A C20 1 
HETATM 3469 C  C21 . A1A06 C 3 .   ? -13.634 -28.717 -2.993  1.00 118.73 ? 602 A1A06 A C21 1 
HETATM 3470 C  C22 . A1A06 C 3 .   ? -13.854 -30.081 -3.256  1.00 121.20 ? 602 A1A06 A C22 1 
HETATM 3471 C  C23 . A1A06 C 3 .   ? -16.023 -31.696 -5.689  1.00 109.59 ? 602 A1A06 A C23 1 
HETATM 3472 C  C26 . A1A06 C 3 .   ? -17.858 -30.166 -6.717  1.00 95.06  ? 602 A1A06 A C26 1 
HETATM 3473 C  C27 . A1A06 C 3 .   ? -17.758 -28.875 -5.822  1.00 101.93 ? 602 A1A06 A C27 1 
HETATM 3474 C  C28 . A1A06 C 3 .   ? -17.909 -27.492 -6.543  1.00 88.04  ? 602 A1A06 A C28 1 
HETATM 3475 C  C29 . A1A06 C 3 .   ? -18.579 -27.480 -7.929  1.00 90.14  ? 602 A1A06 A C29 1 
HETATM 3476 C  C30 . A1A06 C 3 .   ? -17.871 -27.507 -9.145  1.00 87.70  ? 602 A1A06 A C30 1 
HETATM 3477 C  C31 . A1A06 C 3 .   ? -18.527 -27.492 -10.391 1.00 81.52  ? 602 A1A06 A C31 1 
HETATM 3478 C  C32 . A1A06 C 3 .   ? -19.931 -27.448 -10.404 1.00 87.19  ? 602 A1A06 A C32 1 
HETATM 3479 C  C34 . A1A06 C 3 .   ? -19.984 -27.436 -8.064  1.00 85.99  ? 602 A1A06 A C34 1 
HETATM 3480 C  C35 . A1A06 C 3 .   ? -18.277 -34.227 -8.531  1.00 101.57 ? 602 A1A06 A C35 1 
HETATM 3481 C  C36 . A1A06 C 3 .   ? -18.673 -33.015 -9.396  1.00 99.88  ? 602 A1A06 A C36 1 
HETATM 3482 C  C37 . A1A06 C 3 .   ? -19.599 -32.036 -8.964  1.00 95.95  ? 602 A1A06 A C37 1 
HETATM 3483 C  C38 . A1A06 C 3 .   ? -19.952 -30.934 -9.760  1.00 95.20  ? 602 A1A06 A C38 1 
HETATM 3484 C  C39 . A1A06 C 3 .   ? -19.392 -30.778 -11.031 1.00 94.38  ? 602 A1A06 A C39 1 
HETATM 3485 C  C40 . A1A06 C 3 .   ? -18.477 -31.726 -11.489 1.00 111.32 ? 602 A1A06 A C40 1 
HETATM 3486 C  C41 . A1A06 C 3 .   ? -18.132 -32.821 -10.680 1.00 103.90 ? 602 A1A06 A C41 1 
HETATM 3487 F  F01 . A1A06 C 3 .   ? -10.076 -37.802 -10.650 1.00 163.49 ? 602 A1A06 A F01 1 
HETATM 3488 F  F03 . A1A06 C 3 .   ? -11.091 -36.067 -9.926  1.00 154.31 ? 602 A1A06 A F03 1 
HETATM 3489 F  F04 . A1A06 C 3 .   ? -11.099 -36.540 -12.026 1.00 147.12 ? 602 A1A06 A F04 1 
HETATM 3490 N  N07 . A1A06 C 3 .   ? -13.805 -37.355 -10.640 1.00 143.48 ? 602 A1A06 A N07 1 
HETATM 3491 N  N11 . A1A06 C 3 .   ? -16.023 -35.276 -9.191  1.00 118.22 ? 602 A1A06 A N11 1 
HETATM 3492 N  N25 . A1A06 C 3 .   ? -16.605 -30.998 -6.775  1.00 103.83 ? 602 A1A06 A N25 1 
HETATM 3493 N  N33 . A1A06 C 3 .   ? -20.643 -27.421 -9.249  1.00 80.78  ? 602 A1A06 A N33 1 
HETATM 3494 O  O06 . A1A06 C 3 .   ? -12.316 -39.131 -10.435 1.00 156.74 ? 602 A1A06 A O06 1 
HETATM 3495 O  O10 . A1A06 C 3 .   ? -14.182 -33.972 -9.467  1.00 123.41 ? 602 A1A06 A O10 1 
HETATM 3496 O  O24 . A1A06 C 3 .   ? -16.580 -31.632 -4.592  1.00 107.49 ? 602 A1A06 A O24 1 
HETATM 3497 S  S14 . A1A06 C 3 .   ? -15.034 -34.444 -5.784  1.00 125.39 ? 602 A1A06 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   . SER   A 9   ? 1.8803 1.7079 1.8211 0.2499  -0.0821 -0.1159 29  SER   A N   
2    C  CA  . SER   A 9   ? 1.7552 1.6197 1.7209 0.2137  -0.0765 -0.1067 29  SER   A CA  
3    C  C   . SER   A 9   ? 1.6647 1.5797 1.6341 0.2120  -0.0735 -0.1198 29  SER   A C   
4    O  O   . SER   A 9   ? 1.3478 1.2902 1.3364 0.1843  -0.0704 -0.1131 29  SER   A O   
5    C  CB  . SER   A 9   ? 1.6279 1.5309 1.6119 0.2037  -0.0665 -0.0831 29  SER   A CB  
6    O  OG  . SER   A 9   ? 1.6524 1.5964 1.6584 0.1751  -0.0596 -0.0762 29  SER   A OG  
7    N  N   . HIS   A 10  ? 1.6093 1.5347 1.5583 0.2433  -0.0733 -0.1376 30  HIS   A N   
8    C  CA  . HIS   A 10  ? 1.5603 1.5318 1.5055 0.2458  -0.0677 -0.1483 30  HIS   A CA  
9    C  C   . HIS   A 10  ? 1.6305 1.5581 1.5490 0.2419  -0.0813 -0.1704 30  HIS   A C   
10   O  O   . HIS   A 10  ? 1.6712 1.6291 1.5777 0.2450  -0.0783 -0.1799 30  HIS   A O   
11   C  CB  . HIS   A 10  ? 1.5837 1.6008 1.5226 0.2834  -0.0554 -0.1531 30  HIS   A CB  
12   C  CG  . HIS   A 10  ? 1.4876 1.5790 1.4603 0.2780  -0.0420 -0.1333 30  HIS   A CG  
13   N  ND1 . HIS   A 10  ? 1.5198 1.6189 1.5171 0.2542  -0.0432 -0.1134 30  HIS   A ND1 
14   C  CD2 . HIS   A 10  ? 1.4445 1.6041 1.4302 0.2922  -0.0274 -0.1305 30  HIS   A CD2 
15   C  CE1 . HIS   A 10  ? 1.4184 1.5838 1.4410 0.2534  -0.0335 -0.1012 30  HIS   A CE1 
16   N  NE2 . HIS   A 10  ? 1.3683 1.5734 1.3886 0.2747  -0.0235 -0.1100 30  HIS   A NE2 
17   N  N   . GLY   A 11  ? 1.5746 1.4300 1.4822 0.2344  -0.0974 -0.1781 31  GLY   A N   
18   C  CA  . GLY   A 11  ? 1.6427 1.4509 1.5267 0.2273  -0.1161 -0.2003 31  GLY   A CA  
19   C  C   . GLY   A 11  ? 1.6584 1.4500 1.5696 0.1847  -0.1290 -0.1931 31  GLY   A C   
20   O  O   . GLY   A 11  ? 1.7153 1.4604 1.6121 0.1753  -0.1501 -0.2112 31  GLY   A O   
21   N  N   . LEU   A 12  ? 1.5280 1.3561 1.4789 0.1592  -0.1177 -0.1679 32  LEU   A N   
22   C  CA  . LEU   A 12  ? 1.5558 1.3735 1.5395 0.1207  -0.1264 -0.1585 32  LEU   A CA  
23   C  C   . LEU   A 12  ? 1.5408 1.3723 1.5204 0.1100  -0.1412 -0.1733 32  LEU   A C   
24   O  O   . LEU   A 12  ? 1.5469 1.3372 1.5304 0.0927  -0.1632 -0.1845 32  LEU   A O   
25   C  CB  . LEU   A 12  ? 1.3948 1.2565 1.4145 0.1022  -0.1076 -0.1305 32  LEU   A CB  
26   C  CG  . LEU   A 12  ? 1.4137 1.2888 1.4727 0.0665  -0.1092 -0.1179 32  LEU   A CG  
27   C  CD1 . LEU   A 12  ? 1.5280 1.3458 1.6044 0.0450  -0.1238 -0.1186 32  LEU   A CD1 
28   C  CD2 . LEU   A 12  ? 1.3897 1.3031 1.4728 0.0562  -0.0877 -0.0926 32  LEU   A CD2 
29   N  N   . PHE   A 13  ? 1.4180 1.3067 1.3901 0.1194  -0.1307 -0.1725 33  PHE   A N   
30   C  CA  . PHE   A 13  ? 1.3587 1.2622 1.3224 0.1110  -0.1443 -0.1835 33  PHE   A CA  
31   C  C   . PHE   A 13  ? 1.4706 1.3274 1.3852 0.1304  -0.1651 -0.2140 33  PHE   A C   
32   O  O   . PHE   A 13  ? 1.4613 1.3046 1.3676 0.1182  -0.1875 -0.2267 33  PHE   A O   
33   C  CB  . PHE   A 13  ? 1.2620 1.2329 1.2247 0.1180  -0.1257 -0.1729 33  PHE   A CB  
34   C  CG  . PHE   A 13  ? 1.2643 1.2755 1.2714 0.0963  -0.1098 -0.1461 33  PHE   A CG  
35   C  CD1 . PHE   A 13  ? 1.2529 1.2590 1.2970 0.0662  -0.1176 -0.1355 33  PHE   A CD1 
36   C  CD2 . PHE   A 13  ? 1.1336 1.1868 1.1460 0.1066  -0.0877 -0.1321 33  PHE   A CD2 
37   C  CE1 . PHE   A 13  ? 1.1096 1.1479 1.1886 0.0498  -0.1012 -0.1124 33  PHE   A CE1 
38   C  CE2 . PHE   A 13  ? 1.1025 1.1848 1.1485 0.0875  -0.0753 -0.1102 33  PHE   A CE2 
39   C  CZ  . PHE   A 13  ? 1.0589 1.1317 1.1348 0.0606  -0.0808 -0.1009 33  PHE   A CZ  
40   N  N   . LYS   A 14  ? 1.5763 1.4063 1.4562 0.1621  -0.1595 -0.2266 34  LYS   A N   
41   C  CA  . LYS   A 14  ? 1.6458 1.4152 1.4755 0.1815  -0.1803 -0.2576 34  LYS   A CA  
42   C  C   . LYS   A 14  ? 1.6556 1.3576 1.5008 0.1548  -0.2081 -0.2648 34  LYS   A C   
43   O  O   . LYS   A 14  ? 1.7097 1.3731 1.5324 0.1479  -0.2364 -0.2869 34  LYS   A O   
44   C  CB  . LYS   A 14  ? 1.7458 1.4994 1.5407 0.2232  -0.1659 -0.2674 34  LYS   A CB  
45   C  CG  . LYS   A 14  ? 1.9241 1.5894 1.6827 0.2372  -0.1872 -0.2928 34  LYS   A CG  
46   C  CD  . LYS   A 14  ? 1.9685 1.6145 1.7188 0.2687  -0.1722 -0.2901 34  LYS   A CD  
47   C  CE  . LYS   A 14  ? 1.9880 1.6033 1.7789 0.2442  -0.1749 -0.2696 34  LYS   A CE  
48   N  NZ  . LYS   A 14  ? 2.0210 1.6050 1.7978 0.2763  -0.1659 -0.2681 34  LYS   A NZ  
49   N  N   . LYS   A 15  ? 1.5640 1.2510 1.4480 0.1385  -0.2009 -0.2452 35  LYS   A N   
50   C  CA  . LYS   A 15  ? 1.5887 1.2119 1.4936 0.1115  -0.2230 -0.2475 35  LYS   A CA  
51   C  C   . LYS   A 15  ? 1.5347 1.1759 1.4808 0.0724  -0.2406 -0.2423 35  LYS   A C   
52   O  O   . LYS   A 15  ? 1.7936 1.3860 1.7401 0.0551  -0.2713 -0.2589 35  LYS   A O   
53   C  CB  . LYS   A 15  ? 1.6064 1.2156 1.5412 0.1043  -0.2057 -0.2226 35  LYS   A CB  
54   C  CG  . LYS   A 15  ? 1.6880 1.2492 1.6621 0.0672  -0.2199 -0.2129 35  LYS   A CG  
55   C  CD  . LYS   A 15  ? 1.7749 1.3416 1.7824 0.0562  -0.1958 -0.1801 35  LYS   A CD  
56   C  CE  . LYS   A 15  ? 1.9727 1.5460 1.9492 0.0927  -0.1750 -0.1740 35  LYS   A CE  
57   N  NZ  . LYS   A 15  ? 2.1410 1.6549 2.0676 0.1265  -0.1867 -0.1980 35  LYS   A NZ  
58   N  N   . LEU   A 16  ? 1.5708 1.2808 1.5533 0.0586  -0.2233 -0.2198 36  LEU   A N   
59   C  CA  . LEU   A 16  ? 1.4468 1.1810 1.4756 0.0242  -0.2371 -0.2112 36  LEU   A CA  
60   C  C   . LEU   A 16  ? 1.4304 1.1770 1.4315 0.0285  -0.2608 -0.2320 36  LEU   A C   
61   O  O   . LEU   A 16  ? 1.4853 1.2554 1.5239 0.0029  -0.2758 -0.2259 36  LEU   A O   
62   C  CB  . LEU   A 16  ? 1.4006 1.1985 1.4741 0.0113  -0.2090 -0.1799 36  LEU   A CB  
63   C  CG  . LEU   A 16  ? 1.4496 1.2334 1.5695 -0.0107 -0.1949 -0.1556 36  LEU   A CG  
64   C  CD1 . LEU   A 16  ? 1.3411 1.1841 1.4947 -0.0192 -0.1671 -0.1279 36  LEU   A CD1 
65   C  CD2 . LEU   A 16  ? 1.5049 1.2535 1.6649 -0.0429 -0.2195 -0.1576 36  LEU   A CD2 
66   N  N   . GLY   A 17  ? 1.4464 1.1783 1.3822 0.0617  -0.2639 -0.2553 37  GLY   A N   
67   C  CA  . GLY   A 17  ? 1.4942 1.2351 1.3925 0.0693  -0.2845 -0.2743 37  GLY   A CA  
68   C  C   . GLY   A 17  ? 1.3899 1.2041 1.3050 0.0654  -0.2693 -0.2552 37  GLY   A C   
69   O  O   . GLY   A 17  ? 1.4271 1.2528 1.3384 0.0559  -0.2917 -0.2612 37  GLY   A O   
70   N  N   . ILE   A 18  ? 1.4185 1.2796 1.3513 0.0723  -0.2340 -0.2323 38  ILE   A N   
71   C  CA  . ILE   A 18  ? 1.4202 1.3466 1.3704 0.0679  -0.2169 -0.2121 38  ILE   A CA  
72   C  C   . ILE   A 18  ? 1.3379 1.2896 1.2361 0.1010  -0.1971 -0.2171 38  ILE   A C   
73   O  O   . ILE   A 18  ? 1.1878 1.1422 1.0761 0.1205  -0.1752 -0.2151 38  ILE   A O   
74   C  CB  . ILE   A 18  ? 1.3918 1.3510 1.3999 0.0496  -0.1925 -0.1826 38  ILE   A CB  
75   C  CG1 . ILE   A 18  ? 1.2652 1.1957 1.3238 0.0198  -0.2066 -0.1765 38  ILE   A CG1 
76   C  CG2 . ILE   A 18  ? 1.2308 1.2487 1.2569 0.0429  -0.1790 -0.1636 38  ILE   A CG2 
77   C  CD1 . ILE   A 18  ? 1.2980 1.2657 1.4140 -0.0017 -0.1866 -0.1474 38  ILE   A CD1 
78   N  N   . PRO   A 19  ? 1.3061 1.2785 1.1717 0.1090  -0.2032 -0.2221 39  PRO   A N   
79   C  CA  . PRO   A 19  ? 1.3495 1.3460 1.1650 0.1407  -0.1812 -0.2253 39  PRO   A CA  
80   C  C   . PRO   A 19  ? 1.4452 1.4988 1.2930 0.1406  -0.1459 -0.1985 39  PRO   A C   
81   O  O   . PRO   A 19  ? 1.3883 1.4670 1.2872 0.1161  -0.1401 -0.1772 39  PRO   A O   
82   C  CB  . PRO   A 19  ? 1.3418 1.3464 1.1203 0.1429  -0.1974 -0.2312 39  PRO   A CB  
83   C  CG  . PRO   A 19  ? 1.3043 1.3129 1.1327 0.1092  -0.2203 -0.2209 39  PRO   A CG  
84   C  CD  . PRO   A 19  ? 1.2753 1.2533 1.1519 0.0893  -0.2294 -0.2217 39  PRO   A CD  
85   N  N   . GLY   A 20  ? 1.4627 1.5363 1.2799 0.1691  -0.1225 -0.2002 40  GLY   A N   
86   C  CA  . GLY   A 20  ? 1.4608 1.5893 1.3075 0.1696  -0.0917 -0.1768 40  GLY   A CA  
87   C  C   . GLY   A 20  ? 1.4713 1.6216 1.2875 0.2034  -0.0679 -0.1811 40  GLY   A C   
88   O  O   . GLY   A 20  ? 1.5534 1.6703 1.3244 0.2304  -0.0727 -0.2038 40  GLY   A O   
89   N  N   . PRO   A 21  ? 1.5404 1.7475 1.3825 0.2028  -0.0416 -0.1595 41  PRO   A N   
90   C  CA  . PRO   A 21  ? 1.3577 1.5965 1.1851 0.2336  -0.0162 -0.1598 41  PRO   A CA  
91   C  C   . PRO   A 21  ? 1.3622 1.5823 1.2023 0.2499  -0.0157 -0.1683 41  PRO   A C   
92   O  O   . PRO   A 21  ? 1.3158 1.5204 1.1914 0.2318  -0.0252 -0.1619 41  PRO   A O   
93   C  CB  . PRO   A 21  ? 1.3404 1.6439 1.2066 0.2189  0.0065  -0.1316 41  PRO   A CB  
94   C  CG  . PRO   A 21  ? 1.1677 1.4647 1.0757 0.1837  -0.0066 -0.1185 41  PRO   A CG  
95   C  CD  . PRO   A 21  ? 1.2027 1.4458 1.0929 0.1734  -0.0347 -0.1340 41  PRO   A CD  
96   N  N   . THR   A 22  ? 1.4185 1.6383 1.2260 0.2868  -0.0034 -0.1819 42  THR   A N   
97   C  CA  . THR   A 22  ? 1.3721 1.5680 1.1844 0.3089  -0.0043 -0.1920 42  THR   A CA  
98   C  C   . THR   A 22  ? 1.2616 1.5106 1.1301 0.3045  0.0115  -0.1693 42  THR   A C   
99   O  O   . THR   A 22  ? 1.2259 1.5380 1.1111 0.3133  0.0351  -0.1556 42  THR   A O   
100  C  CB  . THR   A 22  ? 1.3916 1.5745 1.1525 0.3539  0.0066  -0.2131 42  THR   A CB  
101  O  OG1 . THR   A 22  ? 1.5470 1.6909 1.2494 0.3573  -0.0064 -0.2322 42  THR   A OG1 
102  C  CG2 . THR   A 22  ? 1.2782 1.4107 1.0320 0.3766  -0.0034 -0.2293 42  THR   A CG2 
103  N  N   . PRO   A 23  ? 1.1466 1.3724 1.0445 0.2905  -0.0011 -0.1641 43  PRO   A N   
104  C  CA  . PRO   A 23  ? 1.2119 1.4848 1.1584 0.2847  0.0091  -0.1432 43  PRO   A CA  
105  C  C   . PRO   A 23  ? 1.2655 1.5604 1.2166 0.3228  0.0212  -0.1464 43  PRO   A C   
106  O  O   . PRO   A 23  ? 1.3494 1.6009 1.2685 0.3524  0.0164  -0.1655 43  PRO   A O   
107  C  CB  . PRO   A 23  ? 1.1546 1.3832 1.1178 0.2600  -0.0096 -0.1385 43  PRO   A CB  
108  C  CG  . PRO   A 23  ? 1.1733 1.3291 1.0987 0.2699  -0.0265 -0.1607 43  PRO   A CG  
109  C  CD  . PRO   A 23  ? 1.1917 1.3461 1.0796 0.2768  -0.0259 -0.1753 43  PRO   A CD  
110  N  N   . LEU   A 24  ? 1.1219 1.4849 1.1156 0.3219  0.0358  -0.1276 44  LEU   A N   
111  C  CA  . LEU   A 24  ? 1.0206 1.4154 1.0342 0.3551  0.0449  -0.1261 44  LEU   A CA  
112  C  C   . LEU   A 24  ? 1.0817 1.4521 1.1167 0.3498  0.0275  -0.1197 44  LEU   A C   
113  O  O   . LEU   A 24  ? 1.1037 1.4551 1.1495 0.3161  0.0150  -0.1101 44  LEU   A O   
114  C  CB  . LEU   A 24  ? 0.9078 1.3921 0.9637 0.3550  0.0669  -0.1076 44  LEU   A CB  
115  C  CG  . LEU   A 24  ? 0.9174 1.4340 0.9513 0.3710  0.0914  -0.1109 44  LEU   A CG  
116  C  CD1 . LEU   A 24  ? 0.8878 1.4884 0.9702 0.3543  0.1112  -0.0865 44  LEU   A CD1 
117  C  CD2 . LEU   A 24  ? 1.0216 1.5327 1.0291 0.4218  0.1041  -0.1279 44  LEU   A CD2 
118  N  N   . PRO   A 25  ? 1.1592 1.5266 1.1972 0.3850  0.0270  -0.1244 45  PRO   A N   
119  C  CA  . PRO   A 25  ? 1.0588 1.4023 1.1126 0.3829  0.0099  -0.1161 45  PRO   A CA  
120  C  C   . PRO   A 25  ? 0.9013 1.2989 1.0010 0.3548  0.0075  -0.0937 45  PRO   A C   
121  O  O   . PRO   A 25  ? 0.9767 1.4469 1.1105 0.3510  0.0207  -0.0835 45  PRO   A O   
122  C  CB  . PRO   A 25  ? 1.1102 1.4603 1.1649 0.4315  0.0137  -0.1230 45  PRO   A CB  
123  C  CG  . PRO   A 25  ? 0.9917 1.3324 1.0110 0.4591  0.0288  -0.1427 45  PRO   A CG  
124  C  CD  . PRO   A 25  ? 1.0361 1.4085 1.0531 0.4314  0.0408  -0.1397 45  PRO   A CD  
125  N  N   . PHE   A 26  ? 1.0222 1.3802 1.1202 0.3341  -0.0094 -0.0860 46  PHE   A N   
126  C  CA  . PHE   A 26  ? 1.1125 1.5053 1.2427 0.3086  -0.0162 -0.0676 46  PHE   A CA  
127  C  C   . PHE   A 26  ? 1.0138 1.4408 1.1588 0.2734  -0.0077 -0.0601 46  PHE   A C   
128  O  O   . PHE   A 26  ? 0.9397 1.3439 1.0816 0.2426  -0.0148 -0.0528 46  PHE   A O   
129  C  CB  . PHE   A 26  ? 1.0499 1.5042 1.2184 0.3317  -0.0178 -0.0588 46  PHE   A CB  
130  C  CG  . PHE   A 26  ? 1.2793 1.6998 1.4353 0.3671  -0.0291 -0.0627 46  PHE   A CG  
131  C  CD1 . PHE   A 26  ? 1.3708 1.7408 1.5101 0.3600  -0.0475 -0.0557 46  PHE   A CD1 
132  C  CD2 . PHE   A 26  ? 1.2812 1.7176 1.4388 0.4095  -0.0200 -0.0726 46  PHE   A CD2 
133  C  CE1 . PHE   A 26  ? 1.3847 1.7189 1.5093 0.3934  -0.0583 -0.0571 46  PHE   A CE1 
134  C  CE2 . PHE   A 26  ? 1.3743 1.7755 1.5194 0.4445  -0.0310 -0.0757 46  PHE   A CE2 
135  C  CZ  . PHE   A 26  ? 1.5613 1.9104 1.6900 0.4358  -0.0511 -0.0674 46  PHE   A CZ  
136  N  N   . LEU   A 27  ? 1.0022 1.4827 1.1620 0.2792  0.0092  -0.0606 47  LEU   A N   
137  C  CA  . LEU   A 27  ? 1.0641 1.5780 1.2388 0.2476  0.0179  -0.0510 47  LEU   A CA  
138  C  C   . LEU   A 27  ? 0.9246 1.3872 1.0658 0.2260  0.0163  -0.0575 47  LEU   A C   
139  O  O   . LEU   A 27  ? 1.0828 1.5564 1.2334 0.1961  0.0179  -0.0479 47  LEU   A O   
140  C  CB  . LEU   A 27  ? 0.9599 1.5400 1.1548 0.2610  0.0393  -0.0478 47  LEU   A CB  
141  C  CG  . LEU   A 27  ? 0.8334 1.4808 1.0753 0.2809  0.0436  -0.0388 47  LEU   A CG  
142  C  CD1 . LEU   A 27  ? 0.7910 1.5097 1.0601 0.2838  0.0690  -0.0298 47  LEU   A CD1 
143  C  CD2 . LEU   A 27  ? 0.9033 1.5658 1.1787 0.2581  0.0246  -0.0255 47  LEU   A CD2 
144  N  N   . GLY   A 28  ? 0.8889 1.2953 0.9937 0.2404  0.0113  -0.0733 48  GLY   A N   
145  C  CA  . GLY   A 28  ? 1.0231 1.3908 1.1023 0.2212  0.0084  -0.0800 48  GLY   A CA  
146  C  C   . GLY   A 28  ? 1.0211 1.4263 1.0950 0.2206  0.0232  -0.0799 48  GLY   A C   
147  O  O   . GLY   A 28  ? 1.0401 1.4790 1.1109 0.2465  0.0372  -0.0837 48  GLY   A O   
148  N  N   . ASN   A 29  ? 0.8248 1.2246 0.8968 0.1923  0.0216  -0.0740 49  ASN   A N   
149  C  CA  . ASN   A 29  ? 0.9458 1.3759 1.0086 0.1888  0.0345  -0.0705 49  ASN   A CA  
150  C  C   . ASN   A 29  ? 0.8214 1.3051 0.9202 0.1675  0.0454  -0.0492 49  ASN   A C   
151  O  O   . ASN   A 29  ? 0.9130 1.4128 1.0058 0.1554  0.0539  -0.0415 49  ASN   A O   
152  C  CB  . ASN   A 29  ? 0.9512 1.3385 0.9857 0.1742  0.0233  -0.0781 49  ASN   A CB  
153  C  CG  . ASN   A 29  ? 1.0676 1.3949 1.0725 0.1873  0.0072  -0.0988 49  ASN   A CG  
154  O  OD1 . ASN   A 29  ? 1.0819 1.3708 1.0955 0.1729  -0.0068 -0.0995 49  ASN   A OD1 
155  N  ND2 . ASN   A 29  ? 1.1694 1.4856 1.1372 0.2145  0.0098  -0.1155 49  ASN   A ND2 
156  N  N   . ILE   A 30  ? 0.7441 1.2526 0.8781 0.1625  0.0434  -0.0394 50  ILE   A N   
157  C  CA  . ILE   A 30  ? 1.0061 1.5543 1.1739 0.1369  0.0480  -0.0209 50  ILE   A CA  
158  C  C   . ILE   A 30  ? 1.0953 1.7048 1.2813 0.1420  0.0687  -0.0100 50  ILE   A C   
159  O  O   . ILE   A 30  ? 1.1364 1.7719 1.3432 0.1176  0.0745  0.0058  50  ILE   A O   
160  C  CB  . ILE   A 30  ? 0.9885 1.5435 1.1853 0.1299  0.0360  -0.0149 50  ILE   A CB  
161  C  CG1 . ILE   A 30  ? 1.0016 1.5994 1.2218 0.1565  0.0399  -0.0154 50  ILE   A CG1 
162  C  CG2 . ILE   A 30  ? 1.0297 1.5232 1.2056 0.1254  0.0198  -0.0225 50  ILE   A CG2 
163  C  CD1 . ILE   A 30  ? 1.1455 1.7760 1.4054 0.1454  0.0294  -0.0042 50  ILE   A CD1 
164  N  N   . LEU   A 31  ? 0.9972 1.6296 1.1760 0.1736  0.0817  -0.0170 51  LEU   A N   
165  C  CA  . LEU   A 31  ? 0.9314 1.6250 1.1279 0.1796  0.1063  -0.0042 51  LEU   A CA  
166  C  C   . LEU   A 31  ? 1.0462 1.7307 1.2114 0.1682  0.1175  0.0011  51  LEU   A C   
167  O  O   . LEU   A 31  ? 1.1706 1.9023 1.3536 0.1611  0.1379  0.0187  51  LEU   A O   
168  C  CB  . LEU   A 31  ? 1.0258 1.7438 1.2171 0.2210  0.1210  -0.0137 51  LEU   A CB  
169  C  CG  . LEU   A 31  ? 0.8388 1.5906 1.0742 0.2364  0.1157  -0.0124 51  LEU   A CG  
170  C  CD1 . LEU   A 31  ? 0.9660 1.7701 1.2129 0.2739  0.1407  -0.0125 51  LEU   A CD1 
171  C  CD2 . LEU   A 31  ? 0.6836 1.4747 0.9749 0.2041  0.1069  0.0066  51  LEU   A CD2 
172  N  N   . SER   A 32  ? 1.1184 1.7440 1.2395 0.1658  0.1040  -0.0120 52  SER   A N   
173  C  CA  . SER   A 32  ? 1.1922 1.8053 1.2822 0.1549  0.1092  -0.0065 52  SER   A CA  
174  C  C   . SER   A 32  ? 1.2176 1.8399 1.3348 0.1188  0.1072  0.0136  52  SER   A C   
175  O  O   . SER   A 32  ? 1.2794 1.8989 1.3765 0.1093  0.1140  0.0233  52  SER   A O   
176  C  CB  . SER   A 32  ? 1.1867 1.7362 1.2299 0.1607  0.0899  -0.0265 52  SER   A CB  
177  O  OG  . SER   A 32  ? 1.0890 1.6166 1.1100 0.1906  0.0856  -0.0475 52  SER   A OG  
178  N  N   . TYR   A 33  ? 1.1430 1.7720 1.3005 0.1002  0.0973  0.0196  53  TYR   A N   
179  C  CA  . TYR   A 33  ? 1.2127 1.8434 1.3932 0.0671  0.0939  0.0361  53  TYR   A CA  
180  C  C   . TYR   A 33  ? 1.3509 2.0372 1.5636 0.0557  0.1131  0.0576  53  TYR   A C   
181  O  O   . TYR   A 33  ? 1.3874 2.0797 1.6281 0.0278  0.1092  0.0712  53  TYR   A O   
182  C  CB  . TYR   A 33  ? 1.1433 1.7556 1.3474 0.0530  0.0753  0.0330  53  TYR   A CB  
183  C  CG  . TYR   A 33  ? 1.0940 1.6491 1.2731 0.0549  0.0582  0.0181  53  TYR   A CG  
184  C  CD1 . TYR   A 33  ? 1.1848 1.7056 1.3321 0.0557  0.0549  0.0123  53  TYR   A CD1 
185  C  CD2 . TYR   A 33  ? 1.0155 1.5519 1.2045 0.0551  0.0447  0.0117  53  TYR   A CD2 
186  C  CE1 . TYR   A 33  ? 1.2094 1.6832 1.3434 0.0547  0.0399  0.0009  53  TYR   A CE1 
187  C  CE2 . TYR   A 33  ? 1.1012 1.5869 1.2707 0.0553  0.0326  0.0015  53  TYR   A CE2 
188  C  CZ  . TYR   A 33  ? 1.1732 1.6298 1.3192 0.0540  0.0308  -0.0036 53  TYR   A CZ  
189  O  OH  . TYR   A 33  ? 1.1756 1.5870 1.3110 0.0518  0.0194  -0.0119 53  TYR   A OH  
190  N  N   . HIS   A 34  ? 1.5031 2.2289 1.7124 0.0767  0.1348  0.0612  54  HIS   A N   
191  C  CA  . HIS   A 34  ? 1.5165 2.3012 1.7639 0.0651  0.1564  0.0844  54  HIS   A CA  
192  C  C   . HIS   A 34  ? 1.5534 2.3305 1.7822 0.0464  0.1683  0.1028  54  HIS   A C   
193  O  O   . HIS   A 34  ? 1.6113 2.4329 1.8707 0.0329  0.1879  0.1255  54  HIS   A O   
194  C  CB  . HIS   A 34  ? 1.5798 2.4153 1.8344 0.0967  0.1801  0.0841  54  HIS   A CB  
195  C  CG  . HIS   A 34  ? 1.6672 2.4888 1.8632 0.1224  0.1979  0.0788  54  HIS   A CG  
196  N  ND1 . HIS   A 34  ? 1.6633 2.4321 1.8043 0.1455  0.1846  0.0540  54  HIS   A ND1 
197  C  CD2 . HIS   A 34  ? 1.7008 2.5523 1.8814 0.1288  0.2274  0.0954  54  HIS   A CD2 
198  C  CE1 . HIS   A 34  ? 1.7097 2.4747 1.8008 0.1657  0.2023  0.0532  54  HIS   A CE1 
199  N  NE2 . HIS   A 34  ? 1.7293 2.5439 1.8406 0.1573  0.2299  0.0788  54  HIS   A NE2 
200  N  N   . LYS   A 35  ? 1.5559 2.2787 1.7385 0.0448  0.1564  0.0953  55  LYS   A N   
201  C  CA  . LYS   A 35  ? 1.6466 2.3540 1.8119 0.0259  0.1619  0.1133  55  LYS   A CA  
202  C  C   . LYS   A 35  ? 1.6380 2.2974 1.8044 0.0032  0.1381  0.1105  55  LYS   A C   
203  O  O   . LYS   A 35  ? 1.6805 2.3147 1.8257 -0.0080 0.1375  0.1215  55  LYS   A O   
204  C  CB  . LYS   A 35  ? 1.7039 2.3948 1.8087 0.0488  0.1715  0.1102  55  LYS   A CB  
205  C  CG  . LYS   A 35  ? 1.6796 2.4189 1.7774 0.0687  0.2034  0.1210  55  LYS   A CG  
206  C  CD  . LYS   A 35  ? 1.8329 2.5491 1.8599 0.0910  0.2118  0.1186  55  LYS   A CD  
207  C  CE  . LYS   A 35  ? 1.7584 2.4980 1.7780 0.0802  0.2387  0.1503  55  LYS   A CE  
208  N  NZ  . LYS   A 35  ? 1.8648 2.5616 1.8631 0.0593  0.2236  0.1615  55  LYS   A NZ  
209  N  N   . GLY   A 36  ? 1.6945 2.3396 1.8823 -0.0014 0.1198  0.0968  56  GLY   A N   
210  C  CA  . GLY   A 36  ? 1.7463 2.3481 1.9359 -0.0200 0.1008  0.0937  56  GLY   A CA  
211  C  C   . GLY   A 36  ? 1.5984 2.1569 1.7586 -0.0061 0.0847  0.0739  56  GLY   A C   
212  O  O   . GLY   A 36  ? 1.4935 2.0468 1.6238 0.0152  0.0857  0.0630  56  GLY   A O   
213  N  N   . PHE   A 37  ? 1.3671 1.8929 1.5361 -0.0190 0.0699  0.0691  57  PHE   A N   
214  C  CA  . PHE   A 37  ? 1.3908 1.8754 1.5413 -0.0125 0.0558  0.0552  57  PHE   A CA  
215  C  C   . PHE   A 37  ? 1.3497 1.8207 1.4701 -0.0045 0.0546  0.0555  57  PHE   A C   
216  O  O   . PHE   A 37  ? 1.2334 1.6849 1.3351 0.0090  0.0444  0.0407  57  PHE   A O   
217  C  CB  . PHE   A 37  ? 1.4241 1.8785 1.5872 -0.0303 0.0471  0.0579  57  PHE   A CB  
218  C  CG  . PHE   A 37  ? 1.4585 1.9044 1.6350 -0.0310 0.0399  0.0489  57  PHE   A CG  
219  C  CD1 . PHE   A 37  ? 1.3298 1.7917 1.5087 -0.0157 0.0387  0.0390  57  PHE   A CD1 
220  C  CD2 . PHE   A 37  ? 1.5292 1.9473 1.7112 -0.0447 0.0346  0.0508  57  PHE   A CD2 
221  C  CE1 . PHE   A 37  ? 1.3251 1.7758 1.5119 -0.0151 0.0307  0.0327  57  PHE   A CE1 
222  C  CE2 . PHE   A 37  ? 1.4947 1.9010 1.6806 -0.0440 0.0279  0.0435  57  PHE   A CE2 
223  C  CZ  . PHE   A 37  ? 1.4821 1.9047 1.6703 -0.0297 0.0252  0.0352  57  PHE   A CZ  
224  N  N   . CYS   A 38  ? 1.5750 2.0540 1.6896 -0.0135 0.0634  0.0728  58  CYS   A N   
225  C  CA  . CYS   A 38  ? 1.5694 2.0293 1.6565 -0.0102 0.0584  0.0775  58  CYS   A CA  
226  C  C   . CYS   A 38  ? 1.6118 2.0847 1.6618 0.0099  0.0643  0.0746  58  CYS   A C   
227  O  O   . CYS   A 38  ? 1.5706 2.0218 1.5924 0.0219  0.0503  0.0635  58  CYS   A O   
228  C  CB  . CYS   A 38  ? 1.5212 1.9771 1.6155 -0.0283 0.0648  0.0995  58  CYS   A CB  
229  S  SG  . CYS   A 38  ? 1.6032 2.0293 1.7263 -0.0470 0.0554  0.0998  58  CYS   A SG  
230  N  N   . MET   A 39  ? 1.4610 1.9691 1.5099 0.0140  0.0849  0.0848  59  MET   A N   
231  C  CA  . MET   A 39  ? 1.4818 2.0012 1.4892 0.0371  0.0943  0.0811  59  MET   A CA  
232  C  C   . MET   A 39  ? 1.3749 1.8821 1.3666 0.0585  0.0829  0.0541  59  MET   A C   
233  O  O   . MET   A 39  ? 1.4292 1.9246 1.3753 0.0792  0.0798  0.0430  59  MET   A O   
234  C  CB  . MET   A 39  ? 1.6122 2.1775 1.6292 0.0380  0.1231  0.0988  59  MET   A CB  
235  C  CG  . MET   A 39  ? 1.7202 2.2895 1.7244 0.0259  0.1368  0.1262  59  MET   A CG  
236  S  SD  . MET   A 39  ? 1.9972 2.5407 1.9263 0.0484  0.1335  0.1255  59  MET   A SD  
237  C  CE  . MET   A 39  ? 1.6470 2.2287 1.5593 0.0506  0.1718  0.1566  59  MET   A CE  
238  N  N   . PHE   A 40  ? 1.3427 1.8469 1.3674 0.0541  0.0751  0.0430  60  PHE   A N   
239  C  CA  . PHE   A 40  ? 1.2534 1.7372 1.2655 0.0719  0.0623  0.0185  60  PHE   A CA  
240  C  C   . PHE   A 40  ? 1.3398 1.7801 1.3343 0.0696  0.0378  0.0062  60  PHE   A C   
241  O  O   . PHE   A 40  ? 1.3688 1.7879 1.3290 0.0868  0.0265  -0.0116 60  PHE   A O   
242  C  CB  . PHE   A 40  ? 1.2703 1.7612 1.3215 0.0669  0.0610  0.0141  60  PHE   A CB  
243  C  CG  . PHE   A 40  ? 1.2080 1.6734 1.2484 0.0841  0.0486  -0.0084 60  PHE   A CG  
244  C  CD1 . PHE   A 40  ? 1.3378 1.8039 1.3456 0.1113  0.0532  -0.0225 60  PHE   A CD1 
245  C  CD2 . PHE   A 40  ? 1.1725 1.6093 1.2322 0.0738  0.0336  -0.0149 60  PHE   A CD2 
246  C  CE1 . PHE   A 40  ? 1.3174 1.7529 1.3137 0.1270  0.0406  -0.0434 60  PHE   A CE1 
247  C  CE2 . PHE   A 40  ? 1.2209 1.6298 1.2709 0.0879  0.0226  -0.0332 60  PHE   A CE2 
248  C  CZ  . PHE   A 40  ? 1.2451 1.6515 1.2640 0.1139  0.0249  -0.0479 60  PHE   A CZ  
249  N  N   . ASP   A 41  ? 1.4135 1.8400 1.4328 0.0486  0.0285  0.0151  61  ASP   A N   
250  C  CA  . ASP   A 41  ? 1.2469 1.6402 1.2611 0.0450  0.0060  0.0066  61  ASP   A CA  
251  C  C   . ASP   A 41  ? 1.3202 1.7073 1.2942 0.0538  -0.0017 0.0081  61  ASP   A C   
252  O  O   . ASP   A 41  ? 1.3366 1.7003 1.2879 0.0630  -0.0220 -0.0082 61  ASP   A O   
253  C  CB  . ASP   A 41  ? 1.1883 1.5729 1.2393 0.0240  0.0027  0.0179  61  ASP   A CB  
254  C  CG  . ASP   A 41  ? 1.2161 1.5988 1.2977 0.0168  0.0068  0.0147  61  ASP   A CG  
255  O  OD1 . ASP   A 41  ? 1.2104 1.5987 1.2879 0.0281  0.0100  0.0040  61  ASP   A OD1 
256  O  OD2 . ASP   A 41  ? 1.1227 1.4961 1.2289 0.0022  0.0069  0.0228  61  ASP   A OD2 
257  N  N   . MET   A 42  ? 1.2735 1.6788 1.2371 0.0504  0.0127  0.0284  62  MET   A N   
258  C  CA  A MET   A 42  ? 1.3080 1.7067 1.2257 0.0611  0.0070  0.0328  62  MET   A CA  
259  C  CA  B MET   A 42  ? 1.4329 1.8315 1.3506 0.0611  0.0069  0.0327  62  MET   A CA  
260  C  C   . MET   A 42  ? 1.3787 1.7725 1.2471 0.0860  0.0053  0.0141  62  MET   A C   
261  O  O   . MET   A 42  ? 1.4467 1.8179 1.2742 0.0970  -0.0147 0.0038  62  MET   A O   
262  C  CB  A MET   A 42  ? 1.3615 1.7811 1.2739 0.0544  0.0289  0.0602  62  MET   A CB  
263  C  CB  B MET   A 42  ? 1.2858 1.7050 1.1983 0.0543  0.0285  0.0602  62  MET   A CB  
264  C  CG  A MET   A 42  ? 1.3145 1.7273 1.2617 0.0328  0.0266  0.0783  62  MET   A CG  
265  C  CG  B MET   A 42  ? 1.3149 1.7238 1.2549 0.0349  0.0230  0.0780  62  MET   A CG  
266  S  SD  A MET   A 42  ? 1.2518 1.6376 1.1772 0.0351  0.0021  0.0846  62  MET   A SD  
267  S  SD  B MET   A 42  ? 1.4405 1.8601 1.3595 0.0296  0.0434  0.1105  62  MET   A SD  
268  C  CE  A MET   A 42  ? 1.3313 1.7254 1.1963 0.0484  0.0173  0.1033  62  MET   A CE  
269  C  CE  B MET   A 42  ? 1.3309 1.7269 1.1918 0.0475  0.0218  0.1099  62  MET   A CE  
270  N  N   . GLU   A 43  ? 1.4609 1.8747 1.3315 0.0966  0.0249  0.0086  63  GLU   A N   
271  C  CA  . GLU   A 43  ? 1.5287 1.9357 1.3510 0.1242  0.0266  -0.0106 63  GLU   A CA  
272  C  C   . GLU   A 43  ? 1.4835 1.8510 1.2986 0.1297  -0.0027 -0.0389 63  GLU   A C   
273  O  O   . GLU   A 43  ? 1.4966 1.8361 1.2617 0.1446  -0.0209 -0.0554 63  GLU   A O   
274  C  CB  . GLU   A 43  ? 1.5985 2.0409 1.4353 0.1352  0.0557  -0.0079 63  GLU   A CB  
275  C  CG  . GLU   A 43  ? 1.7542 2.2338 1.5729 0.1425  0.0871  0.0138  63  GLU   A CG  
276  C  CD  . GLU   A 43  ? 1.9469 2.4658 1.7834 0.1576  0.1143  0.0139  63  GLU   A CD  
277  O  OE1 . GLU   A 43  ? 1.9832 2.4928 1.8304 0.1692  0.1063  -0.0067 63  GLU   A OE1 
278  O  OE2 . GLU   A 43  ? 2.0818 2.6418 1.9246 0.1578  0.1438  0.0360  63  GLU   A OE2 
279  N  N   . CYS   A 44  ? 1.4252 1.7873 1.2879 0.1173  -0.0084 -0.0444 64  CYS   A N   
280  C  CA  . CYS   A 44  ? 1.3315 1.6553 1.1929 0.1202  -0.0333 -0.0687 64  CYS   A CA  
281  C  C   . CYS   A 44  ? 1.3744 1.6703 1.2296 0.1095  -0.0641 -0.0740 64  CYS   A C   
282  O  O   . CYS   A 44  ? 1.3786 1.6401 1.2101 0.1170  -0.0883 -0.0964 64  CYS   A O   
283  C  CB  . CYS   A 44  ? 1.2160 1.5400 1.1298 0.1069  -0.0307 -0.0677 64  CYS   A CB  
284  S  SG  . CYS   A 44  ? 1.2355 1.5871 1.1578 0.1237  -0.0044 -0.0678 64  CYS   A SG  
285  N  N   . HIS   A 45  ? 1.4263 1.7356 1.3052 0.0922  -0.0652 -0.0539 65  HIS   A N   
286  C  CA  . HIS   A 45  ? 1.3369 1.6277 1.2112 0.0852  -0.0943 -0.0561 65  HIS   A CA  
287  C  C   . HIS   A 45  ? 1.4354 1.7099 1.2411 0.1058  -0.1087 -0.0689 65  HIS   A C   
288  O  O   . HIS   A 45  ? 1.4379 1.6839 1.2288 0.1066  -0.1417 -0.0864 65  HIS   A O   
289  C  CB  . HIS   A 45  ? 1.3529 1.6629 1.2563 0.0697  -0.0882 -0.0301 65  HIS   A CB  
290  C  CG  . HIS   A 45  ? 1.4887 1.7858 1.4101 0.0601  -0.1178 -0.0297 65  HIS   A CG  
291  N  ND1 . HIS   A 45  ? 1.4005 1.6750 1.3343 0.0566  -0.1467 -0.0493 65  HIS   A ND1 
292  C  CD2 . HIS   A 45  ? 1.4281 1.7331 1.3608 0.0536  -0.1236 -0.0113 65  HIS   A CD2 
293  C  CE1 . HIS   A 45  ? 1.3746 1.6495 1.3316 0.0478  -0.1693 -0.0426 65  HIS   A CE1 
294  N  NE2 . HIS   A 45  ? 1.4694 1.7621 1.4246 0.0476  -0.1557 -0.0198 65  HIS   A NE2 
295  N  N   . LYS   A 46  ? 1.4887 1.7804 1.2510 0.1224  -0.0845 -0.0604 66  LYS   A N   
296  C  CA  . LYS   A 46  ? 1.5381 1.8129 1.2245 0.1451  -0.0940 -0.0706 66  LYS   A CA  
297  C  C   . LYS   A 46  ? 1.5583 1.8032 1.2055 0.1655  -0.1036 -0.1023 66  LYS   A C   
298  O  O   . LYS   A 46  ? 1.6676 1.8785 1.2620 0.1778  -0.1319 -0.1223 66  LYS   A O   
299  C  CB  . LYS   A 46  ? 1.5422 1.8462 1.1957 0.1565  -0.0596 -0.0481 66  LYS   A CB  
300  C  CG  . LYS   A 46  ? 1.6537 1.9439 1.2367 0.1714  -0.0704 -0.0439 66  LYS   A CG  
301  C  CD  . LYS   A 46  ? 1.7543 2.0706 1.3442 0.1619  -0.0488 -0.0083 66  LYS   A CD  
302  C  CE  . LYS   A 46  ? 1.8929 2.1889 1.4244 0.1711  -0.0706 -0.0016 66  LYS   A CE  
303  N  NZ  . LYS   A 46  ? 1.8660 2.1756 1.4266 0.1538  -0.0651 0.0311  66  LYS   A NZ  
304  N  N   . LYS   A 47  ? 1.5654 1.8193 1.2355 0.1705  -0.0826 -0.1080 67  LYS   A N   
305  C  CA  . LYS   A 47  ? 1.5758 1.7983 1.2061 0.1937  -0.0886 -0.1374 67  LYS   A CA  
306  C  C   . LYS   A 47  ? 1.5855 1.7622 1.2293 0.1822  -0.1284 -0.1610 67  LYS   A C   
307  O  O   . LYS   A 47  ? 1.7179 1.8522 1.3086 0.1992  -0.1501 -0.1885 67  LYS   A O   
308  C  CB  . LYS   A 47  ? 1.5160 1.7624 1.1723 0.2035  -0.0566 -0.1351 67  LYS   A CB  
309  C  CG  . LYS   A 47  ? 1.5240 1.8059 1.1467 0.2276  -0.0189 -0.1240 67  LYS   A CG  
310  C  CD  . LYS   A 47  ? 1.5578 1.8683 1.2184 0.2363  0.0082  -0.1215 67  LYS   A CD  
311  C  CE  . LYS   A 47  ? 1.6581 2.0195 1.3845 0.2125  0.0297  -0.0909 67  LYS   A CE  
312  N  NZ  . LYS   A 47  ? 1.5188 1.9094 1.2845 0.2207  0.0505  -0.0891 67  LYS   A NZ  
313  N  N   . TYR   A 48  ? 1.5209 1.7034 1.2343 0.1535  -0.1382 -0.1507 68  TYR   A N   
314  C  CA  . TYR   A 48  ? 1.5199 1.6648 1.2607 0.1404  -0.1672 -0.1690 68  TYR   A CA  
315  C  C   . TYR   A 48  ? 1.5874 1.7267 1.3651 0.1149  -0.1989 -0.1644 68  TYR   A C   
316  O  O   . TYR   A 48  ? 1.4800 1.5839 1.2683 0.1056  -0.2298 -0.1828 68  TYR   A O   
317  C  CB  . TYR   A 48  ? 1.3626 1.5152 1.1570 0.1314  -0.1481 -0.1628 68  TYR   A CB  
318  C  CG  . TYR   A 48  ? 1.4772 1.6437 1.2481 0.1563  -0.1173 -0.1647 68  TYR   A CG  
319  C  CD1 . TYR   A 48  ? 1.4502 1.5821 1.1720 0.1827  -0.1217 -0.1904 68  TYR   A CD1 
320  C  CD2 . TYR   A 48  ? 1.4130 1.6274 1.2127 0.1541  -0.0848 -0.1410 68  TYR   A CD2 
321  C  CE1 . TYR   A 48  ? 1.4501 1.5997 1.1555 0.2085  -0.0924 -0.1912 68  TYR   A CE1 
322  C  CE2 . TYR   A 48  ? 1.3300 1.5645 1.1173 0.1764  -0.0579 -0.1413 68  TYR   A CE2 
323  C  CZ  . TYR   A 48  ? 1.4685 1.6730 1.2103 0.2048  -0.0606 -0.1658 68  TYR   A CZ  
324  O  OH  . TYR   A 48  ? 1.3703 1.5994 1.1048 0.2300  -0.0326 -0.1652 68  TYR   A OH  
325  N  N   . GLY   A 49  ? 1.4552 1.6278 1.2564 0.1035  -0.1925 -0.1402 69  GLY   A N   
326  C  CA  . GLY   A 49  ? 1.3797 1.5509 1.2152 0.0842  -0.2231 -0.1355 69  GLY   A CA  
327  C  C   . GLY   A 49  ? 1.3085 1.4954 1.2261 0.0586  -0.2177 -0.1201 69  GLY   A C   
328  O  O   . GLY   A 49  ? 1.3178 1.5285 1.2633 0.0542  -0.1862 -0.1025 69  GLY   A O   
329  N  N   . LYS   A 50  ? 1.3202 1.4935 1.2769 0.0416  -0.2489 -0.1268 70  LYS   A N   
330  C  CA  . LYS   A 50  ? 1.3111 1.5045 1.3457 0.0187  -0.2438 -0.1085 70  LYS   A CA  
331  C  C   . LYS   A 50  ? 1.3144 1.5054 1.3814 0.0116  -0.2162 -0.1041 70  LYS   A C   
332  O  O   . LYS   A 50  ? 1.1835 1.3958 1.2991 -0.0007 -0.1972 -0.0844 70  LYS   A O   
333  C  CB  . LYS   A 50  ? 1.2435 1.4263 1.3176 0.0021  -0.2831 -0.1167 70  LYS   A CB  
334  C  CG  . LYS   A 50  ? 1.2883 1.4321 1.3675 -0.0056 -0.3014 -0.1392 70  LYS   A CG  
335  C  CD  . LYS   A 50  ? 1.6179 1.7486 1.7208 -0.0199 -0.3486 -0.1517 70  LYS   A CD  
336  C  CE  . LYS   A 50  ? 1.6045 1.6835 1.6836 -0.0219 -0.3730 -0.1805 70  LYS   A CE  
337  N  NZ  . LYS   A 50  ? 1.5651 1.6171 1.5716 0.0032  -0.3519 -0.1949 70  LYS   A NZ  
338  N  N   . VAL   A 51  ? 1.2848 1.4477 1.3221 0.0213  -0.2138 -0.1220 71  VAL   A N   
339  C  CA  . VAL   A 51  ? 1.2399 1.3939 1.3048 0.0158  -0.1934 -0.1189 71  VAL   A CA  
340  C  C   . VAL   A 51  ? 1.3592 1.4981 1.3729 0.0386  -0.1797 -0.1324 71  VAL   A C   
341  O  O   . VAL   A 51  ? 1.3182 1.4305 1.2832 0.0539  -0.1967 -0.1541 71  VAL   A O   
342  C  CB  . VAL   A 51  ? 1.1178 1.2435 1.2256 -0.0036 -0.2138 -0.1259 71  VAL   A CB  
343  C  CG1 . VAL   A 51  ? 1.1797 1.2793 1.2893 -0.0016 -0.1984 -0.1299 71  VAL   A CG1 
344  C  CG2 . VAL   A 51  ? 1.1668 1.3188 1.3416 -0.0255 -0.2125 -0.1052 71  VAL   A CG2 
345  N  N   . TRP   A 52  ? 1.2735 1.4295 1.2978 0.0424  -0.1497 -0.1202 72  TRP   A N   
346  C  CA  . TRP   A 52  ? 1.1771 1.3249 1.1654 0.0646  -0.1353 -0.1305 72  TRP   A CA  
347  C  C   . TRP   A 52  ? 1.1304 1.2853 1.1510 0.0599  -0.1137 -0.1178 72  TRP   A C   
348  O  O   . TRP   A 52  ? 1.1252 1.2948 1.1870 0.0414  -0.1055 -0.1001 72  TRP   A O   
349  C  CB  . TRP   A 52  ? 1.1939 1.3709 1.1402 0.0845  -0.1200 -0.1281 72  TRP   A CB  
350  C  CG  . TRP   A 52  ? 1.1910 1.4122 1.1616 0.0768  -0.0954 -0.1031 72  TRP   A CG  
351  C  CD1 . TRP   A 52  ? 1.2818 1.5270 1.2658 0.0807  -0.0705 -0.0924 72  TRP   A CD1 
352  C  CD2 . TRP   A 52  ? 1.1107 1.3544 1.0946 0.0639  -0.0959 -0.0863 72  TRP   A CD2 
353  N  NE1 . TRP   A 52  ? 1.2052 1.4834 1.2094 0.0688  -0.0563 -0.0711 72  TRP   A NE1 
354  C  CE2 . TRP   A 52  ? 1.1592 1.4354 1.1624 0.0593  -0.0702 -0.0667 72  TRP   A CE2 
355  C  CE3 . TRP   A 52  ? 1.2404 1.4787 1.2224 0.0563  -0.1177 -0.0860 72  TRP   A CE3 
356  C  CZ2 . TRP   A 52  ? 1.1681 1.4656 1.1855 0.0477  -0.0640 -0.0472 72  TRP   A CZ2 
357  C  CZ3 . TRP   A 52  ? 1.2342 1.4976 1.2318 0.0471  -0.1109 -0.0653 72  TRP   A CZ3 
358  C  CH2 . TRP   A 52  ? 1.1507 1.4407 1.1643 0.0430  -0.0834 -0.0464 72  TRP   A CH2 
359  N  N   . GLY   A 53  ? 1.2428 1.3855 1.2411 0.0790  -0.1049 -0.1274 73  GLY   A N   
360  C  CA  . GLY   A 53  ? 0.9750 1.1200 0.9968 0.0781  -0.0886 -0.1171 73  GLY   A CA  
361  C  C   . GLY   A 53  ? 0.9593 1.1291 0.9606 0.1021  -0.0697 -0.1173 73  GLY   A C   
362  O  O   . GLY   A 53  ? 1.3144 1.4842 1.2782 0.1245  -0.0696 -0.1312 73  GLY   A O   
363  N  N   . PHE   A 54  ? 1.0676 1.2599 1.0943 0.0979  -0.0539 -0.1016 74  PHE   A N   
364  C  CA  . PHE   A 54  ? 0.9163 1.1387 0.9369 0.1178  -0.0375 -0.0989 74  PHE   A CA  
365  C  C   . PHE   A 54  ? 0.8837 1.1024 0.9286 0.1134  -0.0327 -0.0884 74  PHE   A C   
366  O  O   . PHE   A 54  ? 0.8777 1.0673 0.9378 0.0968  -0.0391 -0.0836 74  PHE   A O   
367  C  CB  . PHE   A 54  ? 0.9631 1.2372 0.9867 0.1158  -0.0226 -0.0865 74  PHE   A CB  
368  C  CG  . PHE   A 54  ? 0.9376 1.2293 0.9918 0.0897  -0.0184 -0.0675 74  PHE   A CG  
369  C  CD1 . PHE   A 54  ? 0.9727 1.2573 1.0301 0.0730  -0.0264 -0.0637 74  PHE   A CD1 
370  C  CD2 . PHE   A 54  ? 0.9558 1.2695 1.0342 0.0835  -0.0082 -0.0542 74  PHE   A CD2 
371  C  CE1 . PHE   A 54  ? 1.0408 1.3380 1.1242 0.0525  -0.0212 -0.0471 74  PHE   A CE1 
372  C  CE2 . PHE   A 54  ? 0.9263 1.2491 1.0263 0.0615  -0.0048 -0.0392 74  PHE   A CE2 
373  C  CZ  . PHE   A 54  ? 0.9203 1.2340 1.0225 0.0469  -0.0098 -0.0356 74  PHE   A CZ  
374  N  N   . TYR   A 55  ? 1.0807 1.3305 1.1294 0.1291  -0.0211 -0.0840 75  TYR   A N   
375  C  CA  . TYR   A 55  ? 0.9843 1.2305 1.0491 0.1298  -0.0197 -0.0753 75  TYR   A CA  
376  C  C   . TYR   A 55  ? 0.8959 1.1945 0.9828 0.1247  -0.0087 -0.0604 75  TYR   A C   
377  O  O   . TYR   A 55  ? 0.9933 1.3342 1.0824 0.1367  0.0008  -0.0601 75  TYR   A O   
378  C  CB  . TYR   A 55  ? 0.8823 1.1060 0.9310 0.1584  -0.0233 -0.0869 75  TYR   A CB  
379  C  CG  . TYR   A 55  ? 1.0285 1.1928 1.0532 0.1638  -0.0365 -0.1034 75  TYR   A CG  
380  C  CD1 . TYR   A 55  ? 0.9960 1.1510 0.9947 0.1735  -0.0410 -0.1202 75  TYR   A CD1 
381  C  CD2 . TYR   A 55  ? 1.0041 1.1185 1.0298 0.1586  -0.0452 -0.1019 75  TYR   A CD2 
382  C  CE1 . TYR   A 55  ? 1.1273 1.2239 1.1035 0.1766  -0.0572 -0.1374 75  TYR   A CE1 
383  C  CE2 . TYR   A 55  ? 1.1065 1.1639 1.1143 0.1601  -0.0587 -0.1163 75  TYR   A CE2 
384  C  CZ  . TYR   A 55  ? 1.2499 1.2981 1.2340 0.1684  -0.0664 -0.1352 75  TYR   A CZ  
385  O  OH  . TYR   A 55  ? 1.3934 1.3808 1.3590 0.1680  -0.0840 -0.1516 75  TYR   A OH  
386  N  N   . ASP   A 56  ? 0.8736 1.1679 0.9763 0.1067  -0.0097 -0.0480 76  ASP   A N   
387  C  CA  . ASP   A 56  ? 1.0280 1.3619 1.1503 0.1015  -0.0050 -0.0358 76  ASP   A CA  
388  C  C   . ASP   A 56  ? 1.0208 1.3484 1.1429 0.1194  -0.0110 -0.0362 76  ASP   A C   
389  O  O   . ASP   A 56  ? 1.0903 1.3884 1.2080 0.1132  -0.0169 -0.0307 76  ASP   A O   
390  C  CB  . ASP   A 56  ? 1.0248 1.3518 1.1561 0.0749  -0.0044 -0.0243 76  ASP   A CB  
391  C  CG  . ASP   A 56  ? 1.0600 1.4083 1.1975 0.0599  0.0021  -0.0199 76  ASP   A CG  
392  O  OD1 . ASP   A 56  ? 0.9746 1.3478 1.1085 0.0693  0.0070  -0.0238 76  ASP   A OD1 
393  O  OD2 . ASP   A 56  ? 1.1521 1.4902 1.2951 0.0405  0.0032  -0.0118 76  ASP   A OD2 
394  N  N   . GLY   A 57  ? 1.0358 1.3914 1.1611 0.1441  -0.0085 -0.0419 77  GLY   A N   
395  C  CA  . GLY   A 57  ? 1.0776 1.4242 1.2011 0.1671  -0.0157 -0.0436 77  GLY   A CA  
396  C  C   . GLY   A 57  ? 1.0722 1.3548 1.1682 0.1778  -0.0224 -0.0535 77  GLY   A C   
397  O  O   . GLY   A 57  ? 1.0692 1.3346 1.1488 0.1902  -0.0208 -0.0670 77  GLY   A O   
398  N  N   . GLN   A 58  ? 1.1407 1.3843 1.2288 0.1728  -0.0302 -0.0467 78  GLN   A N   
399  C  CA  . GLN   A 58  ? 1.2623 1.4404 1.3277 0.1770  -0.0358 -0.0521 78  GLN   A CA  
400  C  C   . GLN   A 58  ? 1.1669 1.3131 1.2307 0.1481  -0.0340 -0.0493 78  GLN   A C   
401  O  O   . GLN   A 58  ? 1.2045 1.2977 1.2563 0.1458  -0.0383 -0.0520 78  GLN   A O   
402  C  CB  . GLN   A 58  ? 1.2810 1.4307 1.3362 0.1891  -0.0433 -0.0432 78  GLN   A CB  
403  C  CG  . GLN   A 58  ? 1.3819 1.5480 1.4370 0.2244  -0.0485 -0.0477 78  GLN   A CG  
404  C  CD  . GLN   A 58  ? 1.4412 1.5798 1.4805 0.2477  -0.0483 -0.0648 78  GLN   A CD  
405  O  OE1 . GLN   A 58  ? 1.5389 1.6177 1.5585 0.2416  -0.0517 -0.0708 78  GLN   A OE1 
406  N  NE2 . GLN   A 58  ? 1.4417 1.6230 1.4901 0.2748  -0.0441 -0.0728 78  GLN   A NE2 
407  N  N   . GLN   A 59  ? 1.0094 1.1865 1.0881 0.1261  -0.0279 -0.0430 79  GLN   A N   
408  C  CA  . GLN   A 59  ? 1.0441 1.1973 1.1274 0.1004  -0.0251 -0.0372 79  GLN   A CA  
409  C  C   . GLN   A 59  ? 0.8805 1.0339 0.9666 0.0937  -0.0269 -0.0479 79  GLN   A C   
410  O  O   . GLN   A 59  ? 0.8747 1.0675 0.9658 0.0929  -0.0235 -0.0503 79  GLN   A O   
411  C  CB  . GLN   A 59  ? 0.9911 1.1706 1.0858 0.0826  -0.0184 -0.0244 79  GLN   A CB  
412  C  CG  . GLN   A 59  ? 0.9861 1.1530 1.0904 0.0593  -0.0127 -0.0190 79  GLN   A CG  
413  C  CD  . GLN   A 59  ? 1.0789 1.1974 1.1793 0.0526  -0.0107 -0.0129 79  GLN   A CD  
414  O  OE1 . GLN   A 59  ? 1.1392 1.2358 1.2254 0.0580  -0.0089 -0.0048 79  GLN   A OE1 
415  N  NE2 . GLN   A 59  ? 0.8193 0.9213 0.9328 0.0406  -0.0115 -0.0156 79  GLN   A NE2 
416  N  N   . PRO   A 60  ? 0.8232 0.9332 0.9058 0.0879  -0.0336 -0.0537 80  PRO   A N   
417  C  CA  . PRO   A 60  ? 1.0030 1.1123 1.0876 0.0800  -0.0403 -0.0645 80  PRO   A CA  
418  C  C   . PRO   A 60  ? 1.0417 1.1736 1.1478 0.0566  -0.0352 -0.0538 80  PRO   A C   
419  O  O   . PRO   A 60  ? 0.8445 0.9674 0.9657 0.0415  -0.0283 -0.0403 80  PRO   A O   
420  C  CB  . PRO   A 60  ? 0.9288 0.9822 1.0097 0.0767  -0.0517 -0.0718 80  PRO   A CB  
421  C  CG  . PRO   A 60  ? 0.9637 0.9895 1.0468 0.0746  -0.0455 -0.0580 80  PRO   A CG  
422  C  CD  . PRO   A 60  ? 0.8834 0.9413 0.9595 0.0886  -0.0369 -0.0502 80  PRO   A CD  
423  N  N   . VAL   A 61  ? 0.8926 1.0523 0.9970 0.0559  -0.0373 -0.0593 81  VAL   A N   
424  C  CA  . VAL   A 61  ? 0.8481 1.0280 0.9710 0.0371  -0.0344 -0.0499 81  VAL   A CA  
425  C  C   . VAL   A 61  ? 0.8834 1.0560 1.0029 0.0342  -0.0489 -0.0611 81  VAL   A C   
426  O  O   . VAL   A 61  ? 0.8338 1.0130 0.9280 0.0493  -0.0545 -0.0738 81  VAL   A O   
427  C  CB  . VAL   A 61  ? 1.0369 1.2602 1.1599 0.0379  -0.0233 -0.0413 81  VAL   A CB  
428  C  CG1 . VAL   A 61  ? 0.6805 0.9175 0.8192 0.0209  -0.0215 -0.0320 81  VAL   A CG1 
429  C  CG2 . VAL   A 61  ? 0.9971 1.2266 1.1234 0.0392  -0.0142 -0.0317 81  VAL   A CG2 
430  N  N   . LEU   A 62  ? 0.9306 1.0906 1.0749 0.0159  -0.0553 -0.0563 82  LEU   A N   
431  C  CA  . LEU   A 62  ? 1.0014 1.1570 1.1477 0.0105  -0.0737 -0.0658 82  LEU   A CA  
432  C  C   . LEU   A 62  ? 0.9262 1.1150 1.0863 0.0017  -0.0702 -0.0544 82  LEU   A C   
433  O  O   . LEU   A 62  ? 0.8751 1.0730 1.0638 -0.0109 -0.0592 -0.0390 82  LEU   A O   
434  C  CB  . LEU   A 62  ? 0.7815 0.9041 0.9545 -0.0048 -0.0867 -0.0677 82  LEU   A CB  
435  C  CG  . LEU   A 62  ? 0.8915 1.0155 1.0764 -0.0145 -0.1095 -0.0752 82  LEU   A CG  
436  C  CD1 . LEU   A 62  ? 0.9991 1.1035 1.1409 0.0011  -0.1294 -0.0987 82  LEU   A CD1 
437  C  CD2 . LEU   A 62  ? 0.8149 0.9210 1.0461 -0.0363 -0.1183 -0.0696 82  LEU   A CD2 
438  N  N   . ALA   A 63  ? 0.8667 1.0703 1.0026 0.0103  -0.0785 -0.0614 83  ALA   A N   
439  C  CA  . ALA   A 63  ? 0.9502 1.1806 1.0932 0.0044  -0.0774 -0.0502 83  ALA   A CA  
440  C  C   . ALA   A 63  ? 1.0667 1.2887 1.2218 -0.0034 -0.1016 -0.0558 83  ALA   A C   
441  O  O   . ALA   A 63  ? 1.0912 1.2941 1.2222 0.0036  -0.1217 -0.0733 83  ALA   A O   
442  C  CB  . ALA   A 63  ? 0.9464 1.2000 1.0537 0.0187  -0.0692 -0.0502 83  ALA   A CB  
443  N  N   . ILE   A 64  ? 0.9448 1.1803 1.1371 -0.0166 -0.1012 -0.0416 84  ILE   A N   
444  C  CA  . ILE   A 64  ? 1.0717 1.3069 1.2872 -0.0251 -0.1257 -0.0438 84  ILE   A CA  
445  C  C   . ILE   A 64  ? 0.8839 1.1447 1.0983 -0.0228 -0.1261 -0.0313 84  ILE   A C   
446  O  O   . ILE   A 64  ? 0.8575 1.1335 1.0774 -0.0230 -0.1042 -0.0159 84  ILE   A O   
447  C  CB  . ILE   A 64  ? 1.1524 1.3812 1.4248 -0.0426 -0.1261 -0.0367 84  ILE   A CB  
448  C  CG1 . ILE   A 64  ? 1.0535 1.3028 1.3584 -0.0481 -0.1019 -0.0154 84  ILE   A CG1 
449  C  CG2 . ILE   A 64  ? 1.0273 1.2261 1.2971 -0.0447 -0.1217 -0.0450 84  ILE   A CG2 
450  C  CD1 . ILE   A 64  ? 0.8470 1.0889 1.1986 -0.0612 -0.0901 -0.0061 84  ILE   A CD1 
451  N  N   . THR   A 65  ? 0.9577 1.2193 1.1610 -0.0200 -0.1531 -0.0383 85  THR   A N   
452  C  CA  . THR   A 65  ? 0.9972 1.2789 1.1975 -0.0164 -0.1582 -0.0257 85  THR   A CA  
453  C  C   . THR   A 65  ? 1.2864 1.5748 1.5273 -0.0247 -0.1870 -0.0246 85  THR   A C   
454  O  O   . THR   A 65  ? 1.2955 1.5971 1.5291 -0.0189 -0.1997 -0.0167 85  THR   A O   
455  C  CB  . THR   A 65  ? 1.2156 1.4960 1.3508 0.0002  -0.1626 -0.0316 85  THR   A CB  
456  O  OG1 . THR   A 65  ? 1.2470 1.5115 1.3582 0.0049  -0.1963 -0.0497 85  THR   A OG1 
457  C  CG2 . THR   A 65  ? 1.1690 1.4450 1.2695 0.0092  -0.1390 -0.0371 85  THR   A CG2 
458  N  N   . ASP   A 66  ? 1.1945 1.4752 1.4802 -0.0384 -0.1979 -0.0308 86  ASP   A N   
459  C  CA  . ASP   A 66  ? 1.1341 1.4269 1.4704 -0.0489 -0.2267 -0.0292 86  ASP   A CA  
460  C  C   . ASP   A 66  ? 1.1149 1.4352 1.5143 -0.0556 -0.2078 -0.0064 86  ASP   A C   
461  O  O   . ASP   A 66  ? 1.0754 1.3939 1.5083 -0.0645 -0.1836 0.0005  86  ASP   A O   
462  C  CB  . ASP   A 66  ? 1.1771 1.4486 1.5376 -0.0632 -0.2470 -0.0451 86  ASP   A CB  
463  C  CG  . ASP   A 66  ? 1.2457 1.5325 1.6633 -0.0767 -0.2820 -0.0449 86  ASP   A CG  
464  O  OD1 . ASP   A 66  ? 1.1896 1.5036 1.6776 -0.0874 -0.2709 -0.0267 86  ASP   A OD1 
465  O  OD2 . ASP   A 66  ? 1.4367 1.7087 1.8299 -0.0761 -0.3208 -0.0631 86  ASP   A OD2 
466  N  N   . PRO   A 67  ? 1.2044 1.5478 1.6192 -0.0497 -0.2181 0.0058  87  PRO   A N   
467  C  CA  . PRO   A 67  ? 1.0873 1.4552 1.5595 -0.0514 -0.1976 0.0272  87  PRO   A CA  
468  C  C   . PRO   A 67  ? 0.9755 1.3535 1.5206 -0.0675 -0.1908 0.0318  87  PRO   A C   
469  O  O   . PRO   A 67  ? 0.7115 1.0946 1.2821 -0.0681 -0.1570 0.0455  87  PRO   A O   
470  C  CB  . PRO   A 67  ? 1.0871 1.4759 1.5689 -0.0424 -0.2240 0.0350  87  PRO   A CB  
471  C  CG  . PRO   A 67  ? 1.0879 1.4585 1.4914 -0.0310 -0.2408 0.0236  87  PRO   A CG  
472  C  CD  . PRO   A 67  ? 1.2041 1.5490 1.5766 -0.0375 -0.2466 0.0016  87  PRO   A CD  
473  N  N   . ASP   A 68  ? 1.0168 1.3959 1.5948 -0.0808 -0.2219 0.0212  88  ASP   A N   
474  C  CA  . ASP   A 68  ? 0.9235 1.3126 1.5750 -0.0990 -0.2141 0.0280  88  ASP   A CA  
475  C  C   . ASP   A 68  ? 0.9215 1.2825 1.5528 -0.1039 -0.1813 0.0266  88  ASP   A C   
476  O  O   . ASP   A 68  ? 0.7396 1.1089 1.4086 -0.1080 -0.1489 0.0424  88  ASP   A O   
477  C  CB  . ASP   A 68  ? 1.0056 1.3955 1.6922 -0.1155 -0.2579 0.0148  88  ASP   A CB  
478  C  CG  . ASP   A 68  ? 1.2485 1.6725 1.9714 -0.1124 -0.2928 0.0192  88  ASP   A CG  
479  O  OD1 . ASP   A 68  ? 1.1159 1.5595 1.8303 -0.0951 -0.2822 0.0325  88  ASP   A OD1 
480  O  OD2 . ASP   A 68  ? 1.3244 1.7538 2.0846 -0.1272 -0.3328 0.0095  88  ASP   A OD2 
481  N  N   . MET   A 69  ? 1.0153 1.3420 1.5847 -0.1014 -0.1891 0.0080  89  MET   A N   
482  C  CA  . MET   A 69  ? 0.9208 1.2195 1.4662 -0.1030 -0.1615 0.0064  89  MET   A CA  
483  C  C   . MET   A 69  ? 0.9003 1.2041 1.4238 -0.0910 -0.1234 0.0201  89  MET   A C   
484  O  O   . MET   A 69  ? 0.8648 1.1585 1.3972 -0.0945 -0.0949 0.0288  89  MET   A O   
485  C  CB  . MET   A 69  ? 1.0168 1.2811 1.4975 -0.0969 -0.1776 -0.0162 89  MET   A CB  
486  C  CG  . MET   A 69  ? 1.0840 1.3157 1.5700 -0.1077 -0.1736 -0.0226 89  MET   A CG  
487  S  SD  . MET   A 69  ? 1.1924 1.3811 1.6015 -0.0953 -0.1911 -0.0502 89  MET   A SD  
488  C  CE  . MET   A 69  ? 1.2286 1.4319 1.6019 -0.0832 -0.2234 -0.0630 89  MET   A CE  
489  N  N   . ILE   A 70  ? 0.9009 1.2162 1.3911 -0.0771 -0.1236 0.0219  90  ILE   A N   
490  C  CA  . ILE   A 70  ? 0.8547 1.1741 1.3297 -0.0679 -0.0917 0.0351  90  ILE   A CA  
491  C  C   . ILE   A 70  ? 0.8467 1.1819 1.3800 -0.0723 -0.0703 0.0529  90  ILE   A C   
492  O  O   . ILE   A 70  ? 0.7790 1.1019 1.3127 -0.0739 -0.0420 0.0594  90  ILE   A O   
493  C  CB  . ILE   A 70  ? 1.0010 1.3301 1.4405 -0.0552 -0.0993 0.0367  90  ILE   A CB  
494  C  CG1 . ILE   A 70  ? 0.8566 1.1709 1.2362 -0.0492 -0.1142 0.0204  90  ILE   A CG1 
495  C  CG2 . ILE   A 70  ? 0.8225 1.1505 1.2455 -0.0479 -0.0703 0.0490  90  ILE   A CG2 
496  C  CD1 . ILE   A 70  ? 0.8471 1.1678 1.1842 -0.0372 -0.1149 0.0245  90  ILE   A CD1 
497  N  N   . LYS   A 71  ? 0.7967 1.1599 1.3806 -0.0732 -0.0841 0.0612  91  LYS   A N   
498  C  CA  . LYS   A 71  ? 0.8120 1.1963 1.4587 -0.0749 -0.0624 0.0790  91  LYS   A CA  
499  C  C   . LYS   A 71  ? 0.8233 1.1984 1.5009 -0.0887 -0.0447 0.0827  91  LYS   A C   
500  O  O   . LYS   A 71  ? 0.6571 1.0346 1.3552 -0.0861 -0.0109 0.0970  91  LYS   A O   
501  C  CB  . LYS   A 71  ? 0.8670 1.2874 1.5732 -0.0753 -0.0877 0.0855  91  LYS   A CB  
502  C  CG  . LYS   A 71  ? 0.7847 1.2349 1.5589 -0.0712 -0.0640 0.1058  91  LYS   A CG  
503  C  CD  . LYS   A 71  ? 0.9016 1.3915 1.7596 -0.0815 -0.0898 0.1115  91  LYS   A CD  
504  C  CE  . LYS   A 71  ? 1.0606 1.5869 1.9858 -0.0709 -0.0656 0.1330  91  LYS   A CE  
505  N  NZ  . LYS   A 71  ? 0.9970 1.5480 1.9344 -0.0547 -0.0891 0.1376  91  LYS   A NZ  
506  N  N   . THR   A 72  ? 0.7631 1.1237 1.4406 -0.1025 -0.0665 0.0702  92  THR   A N   
507  C  CA  . THR   A 72  ? 0.7857 1.1311 1.4885 -0.1168 -0.0505 0.0750  92  THR   A CA  
508  C  C   . THR   A 72  ? 0.9834 1.2978 1.6320 -0.1087 -0.0179 0.0768  92  THR   A C   
509  O  O   . THR   A 72  ? 1.0112 1.3210 1.6788 -0.1113 0.0131  0.0914  92  THR   A O   
510  C  CB  . THR   A 72  ? 0.9246 1.2516 1.6297 -0.1323 -0.0842 0.0589  92  THR   A CB  
511  O  OG1 . THR   A 72  ? 0.8145 1.1706 1.5741 -0.1417 -0.1178 0.0572  92  THR   A OG1 
512  C  CG2 . THR   A 72  ? 0.8355 1.1396 1.5627 -0.1477 -0.0673 0.0655  92  THR   A CG2 
513  N  N   . VAL   A 73  ? 0.7632 1.0578 1.3439 -0.0981 -0.0245 0.0631  93  VAL   A N   
514  C  CA  . VAL   A 73  ? 0.8727 1.1393 1.4028 -0.0911 -0.0006 0.0629  93  VAL   A CA  
515  C  C   . VAL   A 73  ? 0.8215 1.0938 1.3463 -0.0809 0.0308  0.0768  93  VAL   A C   
516  O  O   . VAL   A 73  ? 0.8816 1.1360 1.3960 -0.0797 0.0574  0.0852  93  VAL   A O   
517  C  CB  . VAL   A 73  ? 0.9686 1.2203 1.4368 -0.0822 -0.0165 0.0455  93  VAL   A CB  
518  C  CG1 . VAL   A 73  ? 0.8197 1.0537 1.2407 -0.0726 0.0064  0.0472  93  VAL   A CG1 
519  C  CG2 . VAL   A 73  ? 0.8233 1.0547 1.2848 -0.0891 -0.0397 0.0307  93  VAL   A CG2 
520  N  N   . LEU   A 74  ? 0.7570 1.0492 1.2839 -0.0721 0.0278  0.0793  94  LEU   A N   
521  C  CA  . LEU   A 74  ? 0.8689 1.1568 1.3793 -0.0607 0.0554  0.0889  94  LEU   A CA  
522  C  C   . LEU   A 74  ? 0.8202 1.1239 1.3838 -0.0592 0.0789  0.1058  94  LEU   A C   
523  O  O   . LEU   A 74  ? 0.7388 1.0288 1.2846 -0.0497 0.1081  0.1136  94  LEU   A O   
524  C  CB  . LEU   A 74  ? 0.7684 1.0637 1.2540 -0.0510 0.0454  0.0860  94  LEU   A CB  
525  C  CG  . LEU   A 74  ? 0.9304 1.2188 1.3675 -0.0500 0.0254  0.0728  94  LEU   A CG  
526  C  CD1 . LEU   A 74  ? 0.8890 1.1985 1.3443 -0.0504 -0.0024 0.0699  94  LEU   A CD1 
527  C  CD2 . LEU   A 74  ? 0.9492 1.2252 1.3433 -0.0422 0.0374  0.0742  94  LEU   A CD2 
528  N  N   . VAL   A 75  ? 0.7283 1.0611 1.3570 -0.0675 0.0666  0.1116  95  VAL   A N   
529  C  CA  . VAL   A 75  ? 0.9294 1.2870 1.6181 -0.0639 0.0899  0.1296  95  VAL   A CA  
530  C  C   . VAL   A 75  ? 0.9145 1.2810 1.6580 -0.0804 0.0976  0.1390  95  VAL   A C   
531  O  O   . VAL   A 75  ? 0.7733 1.1306 1.5219 -0.0786 0.1330  0.1521  95  VAL   A O   
532  C  CB  . VAL   A 75  ? 0.7226 1.1162 1.4548 -0.0570 0.0714  0.1335  95  VAL   A CB  
533  C  CG1 . VAL   A 75  ? 0.5783 1.0011 1.3751 -0.0489 0.0992  0.1530  95  VAL   A CG1 
534  C  CG2 . VAL   A 75  ? 0.7949 1.1747 1.4708 -0.0425 0.0635  0.1262  95  VAL   A CG2 
535  N  N   . LYS   A 76  ? 0.8062 1.1882 1.5891 -0.0968 0.0643  0.1328  96  LYS   A N   
536  C  CA  . LYS   A 76  ? 0.8621 1.2569 1.7116 -0.1163 0.0676  0.1436  96  LYS   A CA  
537  C  C   . LYS   A 76  ? 0.8680 1.2234 1.6839 -0.1231 0.0915  0.1468  96  LYS   A C   
538  O  O   . LYS   A 76  ? 0.8211 1.1822 1.6789 -0.1305 0.1205  0.1656  96  LYS   A O   
539  C  CB  . LYS   A 76  ? 1.0296 1.4367 1.9129 -0.1338 0.0205  0.1311  96  LYS   A CB  
540  C  CG  . LYS   A 76  ? 0.9763 1.4294 1.9143 -0.1305 -0.0046 0.1334  96  LYS   A CG  
541  C  CD  . LYS   A 76  ? 1.0921 1.5872 2.1044 -0.1247 0.0261  0.1575  96  LYS   A CD  
542  C  CE  . LYS   A 76  ? 1.2112 1.7338 2.3044 -0.1451 0.0127  0.1656  96  LYS   A CE  
543  N  NZ  . LYS   A 76  ? 1.1684 1.7019 2.2929 -0.1401 0.0571  0.1868  96  LYS   A NZ  
544  N  N   . GLU   A 77  ? 1.0019 1.3183 1.7430 -0.1195 0.0809  0.1305  97  GLU   A N   
545  C  CA  . GLU   A 77  ? 1.0393 1.3156 1.7461 -0.1253 0.0951  0.1319  97  GLU   A CA  
546  C  C   . GLU   A 77  ? 0.9126 1.1595 1.5442 -0.1071 0.1195  0.1311  97  GLU   A C   
547  O  O   . GLU   A 77  ? 0.8162 1.0269 1.4005 -0.1071 0.1204  0.1260  97  GLU   A O   
548  C  CB  . GLU   A 77  ? 0.9394 1.1921 1.6270 -0.1365 0.0589  0.1132  97  GLU   A CB  
549  C  CG  . GLU   A 77  ? 0.8652 1.1369 1.6215 -0.1575 0.0296  0.1113  97  GLU   A CG  
550  C  CD  . GLU   A 77  ? 0.9472 1.2362 1.7801 -0.1743 0.0523  0.1350  97  GLU   A CD  
551  O  OE1 . GLU   A 77  ? 0.9170 1.1802 1.7363 -0.1761 0.0839  0.1490  97  GLU   A OE1 
552  O  OE2 . GLU   A 77  ? 1.0389 1.3690 1.9469 -0.1855 0.0385  0.1411  97  GLU   A OE2 
553  N  N   . CYS   A 78  ? 0.8688 1.1283 1.4881 -0.0912 0.1375  0.1355  98  CYS   A N   
554  C  CA  . CYS   A 78  ? 0.7763 1.0062 1.3226 -0.0755 0.1542  0.1317  98  CYS   A CA  
555  C  C   . CYS   A 78  ? 0.8306 1.0311 1.3552 -0.0740 0.1867  0.1452  98  CYS   A C   
556  O  O   . CYS   A 78  ? 0.8203 0.9868 1.2896 -0.0715 0.1846  0.1392  98  CYS   A O   
557  C  CB  . CYS   A 78  ? 0.8579 1.1017 1.3970 -0.0599 0.1650  0.1332  98  CYS   A CB  
558  S  SG  . CYS   A 78  ? 0.9791 1.1832 1.4318 -0.0431 0.1839  0.1282  98  CYS   A SG  
559  N  N   . TYR   A 79  ? 1.0337 1.2482 1.6015 -0.0738 0.2178  0.1649  99  TYR   A N   
560  C  CA  . TYR   A 79  ? 0.9110 1.0964 1.4508 -0.0688 0.2545  0.1806  99  TYR   A CA  
561  C  C   . TYR   A 79  ? 0.9402 1.0996 1.4777 -0.0840 0.2498  0.1852  99  TYR   A C   
562  O  O   . TYR   A 79  ? 0.9450 1.0679 1.4339 -0.0778 0.2720  0.1941  99  TYR   A O   
563  C  CB  . TYR   A 79  ? 0.9473 1.1590 1.5407 -0.0644 0.2923  0.2025  99  TYR   A CB  
564  C  CG  . TYR   A 79  ? 1.2783 1.4918 1.8432 -0.0409 0.3114  0.2007  99  TYR   A CG  
565  C  CD1 . TYR   A 79  ? 1.4873 1.6591 1.9725 -0.0234 0.3343  0.1997  99  TYR   A CD1 
566  C  CD2 . TYR   A 79  ? 1.1796 1.4324 1.7938 -0.0355 0.3039  0.1994  99  TYR   A CD2 
567  C  CE1 . TYR   A 79  ? 1.3480 1.5136 1.8026 -0.0021 0.3498  0.1957  99  TYR   A CE1 
568  C  CE2 . TYR   A 79  ? 1.1772 1.4249 1.7630 -0.0129 0.3209  0.1973  99  TYR   A CE2 
569  C  CZ  . TYR   A 79  ? 1.2523 1.4546 1.7578 0.0032  0.3440  0.1947  99  TYR   A CZ  
570  O  OH  . TYR   A 79  ? 1.1342 1.3241 1.6075 0.0255  0.3590  0.1905  99  TYR   A OH  
571  N  N   . SER   A 80  ? 0.9861 1.1587 1.5701 -0.1028 0.2200  0.1791  100 SER   A N   
572  C  CA  . SER   A 80  ? 0.9941 1.1365 1.5787 -0.1180 0.2139  0.1831  100 SER   A CA  
573  C  C   . SER   A 80  ? 1.0679 1.1771 1.5886 -0.1127 0.1845  0.1618  100 SER   A C   
574  O  O   . SER   A 80  ? 1.1192 1.1883 1.5876 -0.1064 0.1940  0.1654  100 SER   A O   
575  C  CB  . SER   A 80  ? 1.0192 1.1879 1.6900 -0.1426 0.1967  0.1876  100 SER   A CB  
576  O  OG  . SER   A 80  ? 1.0367 1.2358 1.7306 -0.1443 0.1604  0.1687  100 SER   A OG  
577  N  N   . VAL   A 81  ? 1.0551 1.1814 1.5785 -0.1132 0.1496  0.1408  101 VAL   A N   
578  C  CA  . VAL   A 81  ? 1.1283 1.2297 1.6041 -0.1089 0.1211  0.1206  101 VAL   A CA  
579  C  C   . VAL   A 81  ? 0.8308 0.9361 1.2502 -0.0902 0.1162  0.1074  101 VAL   A C   
580  O  O   . VAL   A 81  ? 0.8381 0.9170 1.2033 -0.0797 0.1136  0.1011  101 VAL   A O   
581  C  CB  . VAL   A 81  ? 1.1192 1.2321 1.6324 -0.1225 0.0849  0.1057  101 VAL   A CB  
582  C  CG1 . VAL   A 81  ? 0.9699 1.0455 1.4402 -0.1195 0.0625  0.0894  101 VAL   A CG1 
583  C  CG2 . VAL   A 81  ? 0.9033 1.0292 1.4927 -0.1446 0.0882  0.1203  101 VAL   A CG2 
584  N  N   . PHE   A 82  ? 0.8695 1.0075 1.3036 -0.0861 0.1138  0.1040  102 PHE   A N   
585  C  CA  . PHE   A 82  ? 0.8080 0.9523 1.1980 -0.0729 0.1042  0.0910  102 PHE   A CA  
586  C  C   . PHE   A 82  ? 0.6970 0.8419 1.0682 -0.0624 0.1305  0.1003  102 PHE   A C   
587  O  O   . PHE   A 82  ? 0.8083 0.9754 1.1922 -0.0584 0.1308  0.0997  102 PHE   A O   
588  C  CB  . PHE   A 82  ? 0.9037 1.0774 1.3164 -0.0758 0.0776  0.0789  102 PHE   A CB  
589  C  CG  . PHE   A 82  ? 0.8518 1.0228 1.2871 -0.0867 0.0516  0.0693  102 PHE   A CG  
590  C  CD1 . PHE   A 82  ? 0.9641 1.1146 1.3605 -0.0820 0.0337  0.0539  102 PHE   A CD1 
591  C  CD2 . PHE   A 82  ? 0.9137 1.1018 1.4100 -0.1008 0.0440  0.0750  102 PHE   A CD2 
592  C  CE1 . PHE   A 82  ? 1.0626 1.2030 1.4730 -0.0901 0.0091  0.0426  102 PHE   A CE1 
593  C  CE2 . PHE   A 82  ? 1.0198 1.1997 1.5338 -0.1122 0.0162  0.0639  102 PHE   A CE2 
594  C  CZ  . PHE   A 82  ? 0.9353 1.0877 1.4024 -0.1063 -0.0011 0.0468  102 PHE   A CZ  
595  N  N   . THR   A 83  ? 0.8022 0.9175 1.1376 -0.0563 0.1518  0.1088  103 THR   A N   
596  C  CA  . THR   A 83  ? 0.9513 1.0574 1.2577 -0.0445 0.1768  0.1158  103 THR   A CA  
597  C  C   . THR   A 83  ? 0.8497 0.9442 1.0986 -0.0347 0.1651  0.1025  103 THR   A C   
598  O  O   . THR   A 83  ? 0.8544 0.9493 1.0872 -0.0272 0.1734  0.1014  103 THR   A O   
599  C  CB  . THR   A 83  ? 0.8702 0.9473 1.1600 -0.0414 0.2067  0.1325  103 THR   A CB  
600  O  OG1 . THR   A 83  ? 0.8995 0.9897 1.2504 -0.0542 0.2176  0.1469  103 THR   A OG1 
601  C  CG2 . THR   A 83  ? 0.8267 0.8919 1.0850 -0.0270 0.2350  0.1392  103 THR   A CG2 
602  N  N   . ASN   A 84  ? 0.9136 0.9982 1.1345 -0.0345 0.1451  0.0925  104 ASN   A N   
603  C  CA  . ASN   A 84  ? 0.8677 0.9414 1.0374 -0.0262 0.1354  0.0829  104 ASN   A CA  
604  C  C   . ASN   A 84  ? 0.9331 1.0305 1.1079 -0.0287 0.1082  0.0686  104 ASN   A C   
605  O  O   . ASN   A 84  ? 0.8440 0.9559 1.0479 -0.0342 0.0953  0.0644  104 ASN   A O   
606  C  CB  . ASN   A 84  ? 0.9388 0.9789 1.0653 -0.0193 0.1394  0.0867  104 ASN   A CB  
607  C  CG  . ASN   A 84  ? 1.0835 1.0987 1.2061 -0.0172 0.1690  0.1040  104 ASN   A CG  
608  O  OD1 . ASN   A 84  ? 1.1520 1.1650 1.2726 -0.0133 0.1904  0.1106  104 ASN   A OD1 
609  N  ND2 . ASN   A 84  ? 1.1016 1.0959 1.2217 -0.0187 0.1720  0.1124  104 ASN   A ND2 
610  N  N   . ARG   A 85  ? 1.0436 1.1438 1.1886 -0.0248 0.0997  0.0612  105 ARG   A N   
611  C  CA  . ARG   A 85  ? 0.7786 0.9034 0.9256 -0.0260 0.0784  0.0502  105 ARG   A CA  
612  C  C   . ARG   A 85  ? 0.9113 1.0284 1.0332 -0.0192 0.0668  0.0449  105 ARG   A C   
613  O  O   . ARG   A 85  ? 1.0805 1.1707 1.1832 -0.0140 0.0732  0.0501  105 ARG   A O   
614  C  CB  . ARG   A 85  ? 0.8851 1.0208 1.0223 -0.0282 0.0755  0.0474  105 ARG   A CB  
615  C  CG  . ARG   A 85  ? 0.8289 0.9583 0.9758 -0.0296 0.0906  0.0540  105 ARG   A CG  
616  C  CD  . ARG   A 85  ? 0.8809 1.0185 1.0196 -0.0331 0.0835  0.0505  105 ARG   A CD  
617  N  NE  . ARG   A 85  ? 0.9741 1.1186 1.1369 -0.0341 0.0904  0.0558  105 ARG   A NE  
618  C  CZ  . ARG   A 85  ? 0.9747 1.0986 1.1295 -0.0296 0.1057  0.0603  105 ARG   A CZ  
619  N  NH1 . ARG   A 85  ? 1.0750 1.1670 1.1929 -0.0244 0.1158  0.0590  105 ARG   A NH1 
620  N  NH2 . ARG   A 85  ? 0.8588 0.9922 1.0400 -0.0280 0.1102  0.0658  105 ARG   A NH2 
621  N  N   . ARG   A 86  ? 1.0281 1.1697 1.1500 -0.0176 0.0508  0.0360  106 ARG   A N   
622  C  CA  . ARG   A 86  ? 1.0707 1.2121 1.1741 -0.0083 0.0392  0.0310  106 ARG   A CA  
623  C  C   . ARG   A 86  ? 1.2862 1.4093 1.3561 -0.0047 0.0397  0.0341  106 ARG   A C   
624  O  O   . ARG   A 86  ? 1.3114 1.4354 1.3730 -0.0107 0.0419  0.0345  106 ARG   A O   
625  C  CB  . ARG   A 86  ? 1.1368 1.3151 1.2517 -0.0066 0.0261  0.0226  106 ARG   A CB  
626  C  CG  . ARG   A 86  ? 1.2112 1.3954 1.3209 0.0068  0.0153  0.0162  106 ARG   A CG  
627  C  CD  . ARG   A 86  ? 1.1481 1.3735 1.2685 0.0102  0.0072  0.0101  106 ARG   A CD  
628  N  NE  . ARG   A 86  ? 0.7987 1.0407 0.9348 0.0053  0.0091  0.0071  106 ARG   A NE  
629  C  CZ  . ARG   A 86  ? 0.9449 1.2099 1.0850 0.0141  0.0047  0.0000  106 ARG   A CZ  
630  N  NH1 . ARG   A 86  ? 0.9611 1.2387 1.0965 0.0292  -0.0002 -0.0051 106 ARG   A NH1 
631  N  NH2 . ARG   A 86  ? 0.7421 1.0174 0.8890 0.0099  0.0053  -0.0019 106 ARG   A NH2 
632  N  N   . PRO   A 87  ? 1.3330 1.4352 1.3797 0.0057  0.0358  0.0358  107 PRO   A N   
633  C  CA  . PRO   A 87  ? 1.5111 1.5842 1.5177 0.0102  0.0380  0.0406  107 PRO   A CA  
634  C  C   . PRO   A 87  ? 1.6018 1.6877 1.5944 0.0065  0.0258  0.0350  107 PRO   A C   
635  O  O   . PRO   A 87  ? 1.6970 1.7571 1.6608 0.0045  0.0323  0.0369  107 PRO   A O   
636  C  CB  . PRO   A 87  ? 1.4962 1.5515 1.4833 0.0242  0.0298  0.0429  107 PRO   A CB  
637  C  CG  . PRO   A 87  ? 1.3865 1.4645 1.4049 0.0275  0.0219  0.0367  107 PRO   A CG  
638  C  CD  . PRO   A 87  ? 1.2684 1.3635 1.3200 0.0148  0.0306  0.0346  107 PRO   A CD  
639  N  N   . PHE   A 88  ? 1.4330 1.5563 1.4448 0.0055  0.0087  0.0282  108 PHE   A N   
640  C  CA  . PHE   A 88  ? 1.5684 1.7076 1.5750 -0.0012 -0.0063 0.0238  108 PHE   A CA  
641  C  C   . PHE   A 88  ? 1.6772 1.7924 1.6438 0.0066  -0.0202 0.0234  108 PHE   A C   
642  O  O   . PHE   A 88  ? 1.7740 1.8455 1.7010 0.0115  -0.0110 0.0273  108 PHE   A O   
643  C  CB  . PHE   A 88  ? 1.5353 1.6681 1.5433 -0.0154 0.0023  0.0236  108 PHE   A CB  
644  C  CG  . PHE   A 88  ? 1.6273 1.7833 1.6446 -0.0275 -0.0137 0.0192  108 PHE   A CG  
645  C  CD1 . PHE   A 88  ? 1.7855 1.9893 1.8411 -0.0327 -0.0208 0.0187  108 PHE   A CD1 
646  C  CD2 . PHE   A 88  ? 1.6750 1.8025 1.6611 -0.0337 -0.0212 0.0158  108 PHE   A CD2 
647  C  CE1 . PHE   A 88  ? 1.7473 1.9742 1.8173 -0.0467 -0.0339 0.0175  108 PHE   A CE1 
648  C  CE2 . PHE   A 88  ? 1.7687 1.9146 1.7667 -0.0483 -0.0383 0.0120  108 PHE   A CE2 
649  C  CZ  . PHE   A 88  ? 1.7177 1.9153 1.7614 -0.0561 -0.0440 0.0141  108 PHE   A CZ  
650  N  N   . GLY   A 89  ? 1.7274 1.8730 1.7047 0.0083  -0.0424 0.0194  109 GLY   A N   
651  C  CA  . GLY   A 89  ? 1.8139 1.9437 1.7574 0.0147  -0.0629 0.0179  109 GLY   A CA  
652  C  C   . GLY   A 89  ? 1.7448 1.9254 1.7217 0.0122  -0.0876 0.0139  109 GLY   A C   
653  O  O   . GLY   A 89  ? 1.7203 1.9471 1.7435 0.0096  -0.0844 0.0138  109 GLY   A O   
654  N  N   . PRO   A 90  ? 1.7212 1.8959 1.6757 0.0134  -0.1128 0.0110  110 PRO   A N   
655  C  CA  . PRO   A 90  ? 1.8984 2.0169 1.7887 0.0187  -0.1202 0.0100  110 PRO   A CA  
656  C  C   . PRO   A 90  ? 1.9866 2.0749 1.8531 0.0013  -0.1157 0.0042  110 PRO   A C   
657  O  O   . PRO   A 90  ? 1.9651 2.0777 1.8580 -0.0170 -0.1291 -0.0013 110 PRO   A O   
658  C  CB  . PRO   A 90  ? 1.8340 1.9726 1.7223 0.0264  -0.1557 0.0076  110 PRO   A CB  
659  C  CG  . PRO   A 90  ? 1.8173 2.0231 1.7733 0.0116  -0.1677 0.0049  110 PRO   A CG  
660  C  CD  . PRO   A 90  ? 1.6912 1.9212 1.6868 0.0096  -0.1383 0.0087  110 PRO   A CD  
661  N  N   . VAL   A 91  ? 2.0999 2.1332 1.9165 0.0075  -0.0955 0.0063  111 VAL   A N   
662  C  CA  . VAL   A 91  ? 2.0976 2.0974 1.8901 -0.0038 -0.0846 0.0011  111 VAL   A CA  
663  C  C   . VAL   A 91  ? 2.1599 2.1071 1.8811 0.0013  -0.1006 -0.0062 111 VAL   A C   
664  O  O   . VAL   A 91  ? 2.1337 2.0630 1.8396 -0.0116 -0.1118 -0.0163 111 VAL   A O   
665  C  CB  . VAL   A 91  ? 2.0912 2.0711 1.8845 0.0004  -0.0465 0.0087  111 VAL   A CB  
666  C  CG1 . VAL   A 91  ? 2.0188 2.0439 1.8766 -0.0114 -0.0360 0.0109  111 VAL   A CG1 
667  C  CG2 . VAL   A 91  ? 2.1601 2.1212 1.9329 0.0186  -0.0321 0.0191  111 VAL   A CG2 
668  N  N   . GLY   A 92  ? 2.0443 1.9617 1.7170 0.0206  -0.1028 -0.0013 112 GLY   A N   
669  C  CA  . GLY   A 92  ? 2.0855 1.9458 1.6780 0.0290  -0.1158 -0.0078 112 GLY   A CA  
670  C  C   . GLY   A 92  ? 2.0047 1.8113 1.5496 0.0363  -0.0795 -0.0053 112 GLY   A C   
671  O  O   . GLY   A 92  ? 2.0037 1.8059 1.5560 0.0456  -0.0460 0.0079  112 GLY   A O   
672  N  N   . PHE   A 93  ? 1.8935 1.6589 1.3915 0.0321  -0.0858 -0.0180 113 PHE   A N   
673  C  CA  . PHE   A 93  ? 1.9370 1.6521 1.3897 0.0420  -0.0494 -0.0166 113 PHE   A CA  
674  C  C   . PHE   A 93  ? 1.8523 1.5941 1.3671 0.0314  -0.0199 -0.0122 113 PHE   A C   
675  O  O   . PHE   A 93  ? 1.7913 1.5035 1.2855 0.0414  0.0154  -0.0073 113 PHE   A O   
676  C  CB  . PHE   A 93  ? 1.9726 1.6297 1.3506 0.0435  -0.0665 -0.0340 113 PHE   A CB  
677  C  CG  . PHE   A 93  ? 1.9554 1.6206 1.3658 0.0216  -0.0809 -0.0480 113 PHE   A CG  
678  C  CD1 . PHE   A 93  ? 2.0330 1.7435 1.4961 -0.0004 -0.1190 -0.0544 113 PHE   A CD1 
679  C  CD2 . PHE   A 93  ? 1.9748 1.6013 1.3634 0.0239  -0.0554 -0.0535 113 PHE   A CD2 
680  C  CE1 . PHE   A 93  ? 2.0917 1.8065 1.5846 -0.0225 -0.1310 -0.0646 113 PHE   A CE1 
681  C  CE2 . PHE   A 93  ? 2.0199 1.6473 1.4355 0.0041  -0.0690 -0.0651 113 PHE   A CE2 
682  C  CZ  . PHE   A 93  ? 2.0088 1.6789 1.4758 -0.0205 -0.1069 -0.0700 113 PHE   A CZ  
683  N  N   . MET   A 94  ? 1.8644 1.6623 1.4539 0.0131  -0.0330 -0.0129 114 MET   A N   
684  C  CA  . MET   A 94  ? 1.8102 1.6351 1.4573 0.0035  -0.0097 -0.0082 114 MET   A CA  
685  C  C   . MET   A 94  ? 1.8224 1.6717 1.5068 0.0113  0.0190  0.0072  114 MET   A C   
686  O  O   . MET   A 94  ? 1.6100 1.4842 1.3436 0.0045  0.0363  0.0118  114 MET   A O   
687  C  CB  . MET   A 94  ? 1.8049 1.6781 1.5115 -0.0182 -0.0337 -0.0132 114 MET   A CB  
688  C  CG  . MET   A 94  ? 1.9336 1.7833 1.6156 -0.0319 -0.0615 -0.0277 114 MET   A CG  
689  S  SD  . MET   A 94  ? 1.7096 1.5103 1.3681 -0.0340 -0.0403 -0.0339 114 MET   A SD  
690  C  CE  . MET   A 94  ? 1.5118 1.3680 1.2542 -0.0436 -0.0184 -0.0208 114 MET   A CE  
691  N  N   . LYS   A 95  ? 1.7757 1.6161 1.4375 0.0247  0.0224  0.0157  115 LYS   A N   
692  C  CA  . LYS   A 95  ? 1.7514 1.6040 1.4436 0.0306  0.0507  0.0305  115 LYS   A CA  
693  C  C   . LYS   A 95  ? 1.6687 1.4959 1.3522 0.0362  0.0878  0.0371  115 LYS   A C   
694  O  O   . LYS   A 95  ? 1.6014 1.4511 1.3332 0.0337  0.1098  0.0473  115 LYS   A O   
695  C  CB  . LYS   A 95  ? 1.7857 1.6219 1.4462 0.0445  0.0477  0.0396  115 LYS   A CB  
696  C  CG  . LYS   A 95  ? 1.8532 1.6318 1.4271 0.0601  0.0485  0.0400  115 LYS   A CG  
697  C  CD  . LYS   A 95  ? 1.9427 1.6830 1.4852 0.0715  0.0912  0.0525  115 LYS   A CD  
698  C  CE  . LYS   A 95  ? 1.9430 1.6226 1.3898 0.0884  0.0928  0.0501  115 LYS   A CE  
699  N  NZ  . LYS   A 95  ? 2.0843 1.7305 1.5025 0.0983  0.1348  0.0560  115 LYS   A NZ  
700  N  N   . SER   A 96  ? 1.7852 1.5662 1.4084 0.0446  0.0942  0.0309  116 SER   A N   
701  C  CA  . SER   A 96  ? 1.7710 1.5261 1.3809 0.0543  0.1316  0.0366  116 SER   A CA  
702  C  C   . SER   A 96  ? 1.5448 1.3140 1.1919 0.0451  0.1345  0.0292  116 SER   A C   
703  O  O   . SER   A 96  ? 1.4892 1.2434 1.1357 0.0546  0.1655  0.0341  116 SER   A O   
704  C  CB  . SER   A 96  ? 1.8406 1.5327 1.3581 0.0723  0.1395  0.0325  116 SER   A CB  
705  O  OG  . SER   A 96  ? 1.8871 1.5587 1.3614 0.0677  0.1013  0.0143  116 SER   A OG  
706  N  N   . ALA   A 97  ? 1.5411 1.3380 1.2199 0.0283  0.1043  0.0191  117 ALA   A N   
707  C  CA  . ALA   A 97  ? 1.4655 1.2789 1.1860 0.0187  0.1075  0.0161  117 ALA   A CA  
708  C  C   . ALA   A 97  ? 1.3708 1.2199 1.1525 0.0197  0.1328  0.0303  117 ALA   A C   
709  O  O   . ALA   A 97  ? 1.4313 1.3114 1.2461 0.0167  0.1322  0.0386  117 ALA   A O   
710  C  CB  . ALA   A 97  ? 1.4858 1.3303 1.2370 -0.0012 0.0732  0.0077  117 ALA   A CB  
711  N  N   . ILE   A 98  ? 1.2958 1.1382 1.0922 0.0246  0.1534  0.0325  118 ILE   A N   
712  C  CA  . ILE   A 98  ? 1.2085 1.0814 1.0606 0.0280  0.1786  0.0466  118 ILE   A CA  
713  C  C   . ILE   A 98  ? 1.1650 1.0907 1.0800 0.0125  0.1610  0.0498  118 ILE   A C   
714  O  O   . ILE   A 98  ? 1.1880 1.1391 1.1404 0.0118  0.1703  0.0599  118 ILE   A O   
715  C  CB  . ILE   A 98  ? 1.2861 1.1459 1.1463 0.0376  0.1993  0.0477  118 ILE   A CB  
716  C  CG1 . ILE   A 98  ? 1.0504 0.9538 0.9829 0.0374  0.2160  0.0618  118 ILE   A CG1 
717  C  CG2 . ILE   A 98  ? 1.1567 1.0059 1.0097 0.0284  0.1765  0.0356  118 ILE   A CG2 
718  C  CD1 . ILE   A 98  ? 1.2094 1.1007 1.1496 0.0551  0.2482  0.0687  118 ILE   A CD1 
719  N  N   . SER   A 99  ? 1.2681 1.2090 1.1937 -0.0003 0.1356  0.0414  119 SER   A N   
720  C  CA  . SER   A 99  ? 1.2394 1.2279 1.2158 -0.0124 0.1202  0.0437  119 SER   A CA  
721  C  C   . SER   A 99  ? 1.1942 1.1978 1.1719 -0.0134 0.1106  0.0445  119 SER   A C   
722  O  O   . SER   A 99  ? 1.0732 1.1108 1.0911 -0.0183 0.1051  0.0475  119 SER   A O   
723  C  CB  . SER   A 99  ? 1.2740 1.2734 1.2551 -0.0254 0.0978  0.0366  119 SER   A CB  
724  O  OG  . SER   A 99  ? 1.3558 1.3403 1.3008 -0.0302 0.0786  0.0276  119 SER   A OG  
725  N  N   . ILE   A 100 ? 1.3366 1.3118 1.2674 -0.0071 0.1075  0.0416  120 ILE   A N   
726  C  CA  . ILE   A 100 ? 1.2336 1.2182 1.1605 -0.0057 0.0958  0.0425  120 ILE   A CA  
727  C  C   . ILE   A 100 ? 1.2443 1.2061 1.1556 0.0052  0.1173  0.0533  120 ILE   A C   
728  O  O   . ILE   A 100 ? 1.2998 1.2733 1.2269 0.0057  0.1136  0.0579  120 ILE   A O   
729  C  CB  . ILE   A 100 ? 1.3699 1.3439 1.2587 -0.0069 0.0704  0.0328  120 ILE   A CB  
730  C  CG1 . ILE   A 100 ? 1.4239 1.4329 1.3440 -0.0212 0.0490  0.0259  120 ILE   A CG1 
731  C  CG2 . ILE   A 100 ? 1.3305 1.3042 1.2041 0.0007  0.0603  0.0352  120 ILE   A CG2 
732  C  CD1 . ILE   A 100 ? 1.6073 1.6058 1.4978 -0.0269 0.0243  0.0164  120 ILE   A CD1 
733  N  N   . ALA   A 101 ? 1.2950 1.2235 1.1767 0.0146  0.1417  0.0583  121 ALA   A N   
734  C  CA  . ALA   A 101 ? 1.3662 1.2704 1.2278 0.0250  0.1659  0.0713  121 ALA   A CA  
735  C  C   . ALA   A 101 ? 1.2513 1.1836 1.1733 0.0189  0.1788  0.0833  121 ALA   A C   
736  O  O   . ALA   A 101 ? 0.8730 0.8381 0.8484 0.0104  0.1773  0.0824  121 ALA   A O   
737  C  CB  . ALA   A 101 ? 1.3494 1.2169 1.1714 0.0378  0.1944  0.0749  121 ALA   A CB  
738  N  N   . GLU   A 102 ? 1.1965 1.1124 1.1076 0.0230  0.1901  0.0952  122 GLU   A N   
739  C  CA  . GLU   A 102 ? 1.2069 1.1427 1.1717 0.0147  0.1964  0.1056  122 GLU   A CA  
740  C  C   . GLU   A 102 ? 1.2949 1.2191 1.2730 0.0175  0.2340  0.1245  122 GLU   A C   
741  O  O   . GLU   A 102 ? 1.4313 1.3225 1.3602 0.0300  0.2569  0.1319  122 GLU   A O   
742  C  CB  . GLU   A 102 ? 1.3254 1.2505 1.2755 0.0153  0.1793  0.1064  122 GLU   A CB  
743  C  CG  . GLU   A 102 ? 1.3089 1.2668 1.2951 0.0072  0.1499  0.0941  122 GLU   A CG  
744  C  CD  . GLU   A 102 ? 1.6196 1.5641 1.5828 0.0134  0.1315  0.0924  122 GLU   A CD  
745  O  OE1 . GLU   A 102 ? 1.6697 1.5802 1.5816 0.0244  0.1350  0.0988  122 GLU   A OE1 
746  O  OE2 . GLU   A 102 ? 1.5606 1.5269 1.5550 0.0094  0.1137  0.0849  122 GLU   A OE2 
747  N  N   . ASP   A 103 ? 1.1834 1.1360 1.2290 0.0057  0.2397  0.1324  123 ASP   A N   
748  C  CA  . ASP   A 103 ? 1.4030 1.3531 1.4794 0.0032  0.2726  0.1535  123 ASP   A CA  
749  C  C   . ASP   A 103 ? 1.5126 1.4491 1.5672 0.0168  0.3096  0.1639  123 ASP   A C   
750  O  O   . ASP   A 103 ? 1.3850 1.3380 1.4530 0.0215  0.3132  0.1571  123 ASP   A O   
751  C  CB  . ASP   A 103 ? 1.4597 1.3792 1.5128 0.0021  0.2758  0.1655  123 ASP   A CB  
752  C  CG  . ASP   A 103 ? 1.3980 1.3320 1.4940 -0.0124 0.2493  0.1606  123 ASP   A CG  
753  O  OD1 . ASP   A 103 ? 1.2488 1.2088 1.4122 -0.0268 0.2524  0.1662  123 ASP   A OD1 
754  O  OD2 . ASP   A 103 ? 1.3764 1.2955 1.4388 -0.0085 0.2244  0.1505  123 ASP   A OD2 
755  N  N   . GLU   A 104 ? 1.6939 1.5975 1.7121 0.0250  0.3387  0.1814  124 GLU   A N   
756  C  CA  . GLU   A 104 ? 1.7653 1.6554 1.7627 0.0403  0.3806  0.1939  124 GLU   A CA  
757  C  C   . GLU   A 104 ? 1.6778 1.5378 1.5993 0.0585  0.3760  0.1772  124 GLU   A C   
758  O  O   . GLU   A 104 ? 1.6800 1.5384 1.5963 0.0716  0.4009  0.1779  124 GLU   A O   
759  C  CB  . GLU   A 104 ? 1.8887 1.7481 1.8597 0.0447  0.4142  0.2188  124 GLU   A CB  
760  C  CG  . GLU   A 104 ? 1.9007 1.7731 1.9290 0.0242  0.4088  0.2329  124 GLU   A CG  
761  C  CD  . GLU   A 104 ? 1.9306 1.8570 2.0634 0.0061  0.4089  0.2368  124 GLU   A CD  
762  O  OE1 . GLU   A 104 ? 1.8936 1.8455 2.0609 0.0120  0.4350  0.2432  124 GLU   A OE1 
763  O  OE2 . GLU   A 104 ? 1.9861 1.9281 2.1652 -0.0127 0.3812  0.2327  124 GLU   A OE2 
764  N  N   . GLU   A 105 ? 1.6602 1.4954 1.5239 0.0600  0.3436  0.1620  125 GLU   A N   
765  C  CA  . GLU   A 105 ? 1.7216 1.5283 1.5178 0.0729  0.3317  0.1439  125 GLU   A CA  
766  C  C   . GLU   A 105 ? 1.6314 1.4665 1.4671 0.0681  0.3193  0.1291  125 GLU   A C   
767  O  O   . GLU   A 105 ? 1.6199 1.4311 1.4148 0.0806  0.3256  0.1193  125 GLU   A O   
768  C  CB  . GLU   A 105 ? 1.9178 1.7037 1.6620 0.0717  0.2939  0.1314  125 GLU   A CB  
769  C  CG  . GLU   A 105 ? 2.0715 1.8342 1.7580 0.0783  0.2704  0.1100  125 GLU   A CG  
770  C  CD  . GLU   A 105 ? 2.1196 1.8825 1.7843 0.0723  0.2273  0.0977  125 GLU   A CD  
771  O  OE1 . GLU   A 105 ? 2.0585 1.8573 1.7770 0.0595  0.2090  0.0982  125 GLU   A OE1 
772  O  OE2 . GLU   A 105 ? 2.1642 1.8916 1.7585 0.0814  0.2110  0.0872  125 GLU   A OE2 
773  N  N   . TRP   A 106 ? 1.4425 1.3240 1.3533 0.0513  0.3016  0.1275  126 TRP   A N   
774  C  CA  . TRP   A 106 ? 1.3841 1.2928 1.3339 0.0471  0.2905  0.1169  126 TRP   A CA  
775  C  C   . TRP   A 106 ? 1.2912 1.2130 1.2791 0.0563  0.3254  0.1287  126 TRP   A C   
776  O  O   . TRP   A 106 ? 1.1206 1.0358 1.0998 0.0658  0.3293  0.1209  126 TRP   A O   
777  C  CB  . TRP   A 106 ? 1.1385 1.0901 1.1486 0.0287  0.2605  0.1122  126 TRP   A CB  
778  C  CG  . TRP   A 106 ? 1.0775 1.0622 1.1408 0.0246  0.2564  0.1091  126 TRP   A CG  
779  C  CD1 . TRP   A 106 ? 0.9578 0.9412 1.0087 0.0253  0.2405  0.0963  126 TRP   A CD1 
780  C  CD2 . TRP   A 106 ? 1.0836 1.1061 1.2209 0.0195  0.2673  0.1205  126 TRP   A CD2 
781  N  NE1 . TRP   A 106 ? 0.9974 1.0132 1.1057 0.0229  0.2414  0.0998  126 TRP   A NE1 
782  C  CE2 . TRP   A 106 ? 1.0370 1.0792 1.1997 0.0197  0.2563  0.1139  126 TRP   A CE2 
783  C  CE3 . TRP   A 106 ? 1.2047 1.2458 1.3912 0.0134  0.2835  0.1364  126 TRP   A CE3 
784  C  CZ2 . TRP   A 106 ? 1.1740 1.2553 1.4072 0.0166  0.2590  0.1220  126 TRP   A CZ2 
785  C  CZ3 . TRP   A 106 ? 1.0630 1.1453 1.3247 0.0076  0.2854  0.1436  126 TRP   A CZ3 
786  C  CH2 . TRP   A 106 ? 1.1050 1.2078 1.3884 0.0103  0.2723  0.1360  126 TRP   A CH2 
787  N  N   . LYS   A 107 ? 1.3800 1.3210 1.4144 0.0535  0.3506  0.1482  127 LYS   A N   
788  C  CA  . LYS   A 107 ? 1.2951 1.2580 1.3783 0.0623  0.3856  0.1624  127 LYS   A CA  
789  C  C   . LYS   A 107 ? 1.3934 1.3176 1.4149 0.0877  0.4164  0.1613  127 LYS   A C   
790  O  O   . LYS   A 107 ? 1.1043 1.0415 1.1530 0.1000  0.4342  0.1627  127 LYS   A O   
791  C  CB  . LYS   A 107 ? 1.0986 1.0815 1.2327 0.0537  0.4099  0.1858  127 LYS   A CB  
792  C  CG  . LYS   A 107 ? 1.0861 1.1244 1.3215 0.0450  0.4181  0.1977  127 LYS   A CG  
793  C  CD  . LYS   A 107 ? 1.4981 1.5494 1.7781 0.0364  0.4476  0.2232  127 LYS   A CD  
794  C  CE  . LYS   A 107 ? 1.3641 1.4102 1.6385 0.0572  0.5016  0.2420  127 LYS   A CE  
795  N  NZ  . LYS   A 107 ? 1.2821 1.3396 1.5988 0.0470  0.5339  0.2703  127 LYS   A NZ  
796  N  N   . ARG   A 108 ? 1.4095 1.2832 1.3443 0.0979  0.4217  0.1580  128 ARG   A N   
797  C  CA  . ARG   A 108 ? 1.4592 1.2867 1.3210 0.1239  0.4498  0.1546  128 ARG   A CA  
798  C  C   . ARG   A 108 ? 1.5287 1.3331 1.3528 0.1294  0.4241  0.1300  128 ARG   A C   
799  O  O   . ARG   A 108 ? 1.4679 1.2523 1.2714 0.1496  0.4464  0.1262  128 ARG   A O   
800  C  CB  . ARG   A 108 ? 1.4347 1.2125 1.2101 0.1330  0.4598  0.1591  128 ARG   A CB  
801  C  CG  . ARG   A 108 ? 1.8537 1.5813 1.5490 0.1626  0.4975  0.1602  128 ARG   A CG  
802  C  CD  . ARG   A 108 ? 2.0961 1.7660 1.6869 0.1704  0.4874  0.1552  128 ARG   A CD  
803  N  NE  . ARG   A 108 ? 2.2415 1.8636 1.7515 0.1807  0.4612  0.1280  128 ARG   A NE  
804  C  CZ  . ARG   A 108 ? 2.2371 1.8369 1.6996 0.1711  0.4159  0.1113  128 ARG   A CZ  
805  N  NH1 . ARG   A 108 ? 2.1320 1.7517 1.6158 0.1543  0.3926  0.1183  128 ARG   A NH1 
806  N  NH2 . ARG   A 108 ? 2.3312 1.8872 1.7252 0.1788  0.3927  0.0870  128 ARG   A NH2 
807  N  N   . LEU   A 109 ? 1.5157 1.3214 1.3315 0.1120  0.3785  0.1139  129 LEU   A N   
808  C  CA  . LEU   A 109 ? 1.4638 1.2499 1.2521 0.1120  0.3521  0.0927  129 LEU   A CA  
809  C  C   . LEU   A 109 ? 1.4466 1.2681 1.3045 0.1107  0.3544  0.0940  129 LEU   A C   
810  O  O   . LEU   A 109 ? 1.4371 1.2323 1.2714 0.1238  0.3590  0.0844  129 LEU   A O   
811  C  CB  . LEU   A 109 ? 1.4468 1.2365 1.2230 0.0918  0.3055  0.0792  129 LEU   A CB  
812  C  CG  . LEU   A 109 ? 1.4456 1.2051 1.1582 0.0927  0.2950  0.0777  129 LEU   A CG  
813  C  CD1 . LEU   A 109 ? 1.3355 1.1135 1.0577 0.0733  0.2498  0.0663  129 LEU   A CD1 
814  C  CD2 . LEU   A 109 ? 1.6186 1.3137 1.2353 0.1125  0.3040  0.0675  129 LEU   A CD2 
815  N  N   . ARG   A 110 ? 1.3347 1.2124 1.2760 0.0958  0.3493  0.1055  130 ARG   A N   
816  C  CA  . ARG   A 110 ? 1.2595 1.1738 1.2678 0.0941  0.3456  0.1076  130 ARG   A CA  
817  C  C   . ARG   A 110 ? 1.3050 1.2148 1.3255 0.1186  0.3853  0.1168  130 ARG   A C   
818  O  O   . ARG   A 110 ? 1.4438 1.3526 1.4778 0.1278  0.3831  0.1119  130 ARG   A O   
819  C  CB  . ARG   A 110 ? 1.0523 1.0240 1.1415 0.0750  0.3324  0.1181  130 ARG   A CB  
820  C  CG  . ARG   A 110 ? 0.9560 0.9677 1.1133 0.0727  0.3229  0.1208  130 ARG   A CG  
821  C  CD  . ARG   A 110 ? 0.9526 0.9812 1.1204 0.0535  0.2813  0.1100  130 ARG   A CD  
822  N  NE  . ARG   A 110 ? 0.9698 1.0169 1.1726 0.0561  0.2706  0.1096  130 ARG   A NE  
823  C  CZ  . ARG   A 110 ? 0.9922 1.0563 1.2079 0.0425  0.2390  0.1034  130 ARG   A CZ  
824  N  NH1 . ARG   A 110 ? 1.2151 1.2835 1.4150 0.0261  0.2155  0.0959  130 ARG   A NH1 
825  N  NH2 . ARG   A 110 ? 0.7987 0.8755 1.0424 0.0475  0.2321  0.1060  130 ARG   A NH2 
826  N  N   . SER   A 111 ? 1.3877 1.2944 1.4039 0.1309  0.4235  0.1317  131 SER   A N   
827  C  CA  . SER   A 111 ? 1.3925 1.2965 1.4185 0.1579  0.4668  0.1416  131 SER   A CA  
828  C  C   . SER   A 111 ? 1.4188 1.2568 1.3549 0.1812  0.4740  0.1243  131 SER   A C   
829  O  O   . SER   A 111 ? 1.5271 1.3588 1.4727 0.2006  0.4874  0.1216  131 SER   A O   
830  C  CB  . SER   A 111 ? 1.4311 1.3468 1.4705 0.1643  0.5089  0.1637  131 SER   A CB  
831  O  OG  . SER   A 111 ? 1.6713 1.6533 1.8172 0.1533  0.5175  0.1832  131 SER   A OG  
832  N  N   . LEU   A 112 ? 1.4395 1.2252 1.2862 0.1802  0.4628  0.1116  132 LEU   A N   
833  C  CA  . LEU   A 112 ? 1.6631 1.3785 1.4154 0.2016  0.4671  0.0932  132 LEU   A CA  
834  C  C   . LEU   A 112 ? 1.6342 1.3337 1.3839 0.1947  0.4320  0.0741  132 LEU   A C   
835  O  O   . LEU   A 112 ? 1.7180 1.3664 1.4154 0.2154  0.4403  0.0609  132 LEU   A O   
836  C  CB  . LEU   A 112 ? 1.7397 1.4067 1.4003 0.1997  0.4570  0.0847  132 LEU   A CB  
837  C  CG  . LEU   A 112 ? 2.0331 1.6207 1.5802 0.2132  0.4443  0.0610  132 LEU   A CG  
838  C  CD1 . LEU   A 112 ? 2.3009 1.8581 1.7766 0.2177  0.4513  0.0650  132 LEU   A CD1 
839  C  CD2 . LEU   A 112 ? 2.0590 1.6326 1.5941 0.1911  0.3905  0.0391  132 LEU   A CD2 
840  N  N   . LEU   A 113 ? 1.5748 1.3141 1.3778 0.1668  0.3941  0.0728  133 LEU   A N   
841  C  CA  . LEU   A 113 ? 1.6386 1.3664 1.4438 0.1568  0.3613  0.0586  133 LEU   A CA  
842  C  C   . LEU   A 113 ? 1.6493 1.4205 1.5354 0.1593  0.3651  0.0692  133 LEU   A C   
843  O  O   . LEU   A 113 ? 1.7511 1.5074 1.6368 0.1552  0.3435  0.0603  133 LEU   A O   
844  C  CB  . LEU   A 113 ? 1.6604 1.4011 1.4645 0.1260  0.3168  0.0504  133 LEU   A CB  
845  C  CG  . LEU   A 113 ? 1.5238 1.2165 1.2438 0.1238  0.3031  0.0367  133 LEU   A CG  
846  C  CD1 . LEU   A 113 ? 1.4925 1.2026 1.2196 0.0953  0.2589  0.0287  133 LEU   A CD1 
847  C  CD2 . LEU   A 113 ? 1.6644 1.2869 1.3106 0.1416  0.3073  0.0198  133 LEU   A CD2 
848  N  N   . SER   A 114 ? 1.5366 1.3600 1.4922 0.1653  0.3903  0.0886  134 SER   A N   
849  C  CA  . SER   A 114 ? 1.5577 1.4259 1.5932 0.1694  0.3915  0.0995  134 SER   A CA  
850  C  C   . SER   A 114 ? 1.5735 1.4047 1.5891 0.1967  0.4061  0.0942  134 SER   A C   
851  O  O   . SER   A 114 ? 1.5636 1.3992 1.6032 0.1922  0.3830  0.0918  134 SER   A O   
852  C  CB  . SER   A 114 ? 1.4417 1.3697 1.5540 0.1722  0.4184  0.1214  134 SER   A CB  
853  O  OG  . SER   A 114 ? 1.6283 1.6024 1.7886 0.1436  0.3923  0.1267  134 SER   A OG  
854  N  N   . PRO   A 115 ? 1.6588 1.4489 1.6268 0.2269  0.4439  0.0922  135 PRO   A N   
855  C  CA  . PRO   A 115 ? 1.7656 1.5249 1.7253 0.2573  0.4609  0.0887  135 PRO   A CA  
856  C  C   . PRO   A 115 ? 1.8166 1.5082 1.7098 0.2539  0.4311  0.0670  135 PRO   A C   
857  O  O   . PRO   A 115 ? 1.8897 1.5342 1.7520 0.2812  0.4453  0.0597  135 PRO   A O   
858  C  CB  . PRO   A 115 ? 1.8968 1.6277 1.8134 0.2905  0.5114  0.0914  135 PRO   A CB  
859  C  CG  . PRO   A 115 ? 1.7323 1.4990 1.6631 0.2753  0.5235  0.1042  135 PRO   A CG  
860  C  CD  . PRO   A 115 ? 1.6815 1.4496 1.5991 0.2381  0.4753  0.0942  135 PRO   A CD  
861  N  N   . THR   A 116 ? 1.9422 1.6274 1.8147 0.2210  0.3903  0.0570  136 THR   A N   
862  C  CA  . THR   A 116 ? 1.9120 1.5375 1.7306 0.2121  0.3598  0.0386  136 THR   A CA  
863  C  C   . THR   A 116 ? 1.9690 1.6153 1.8426 0.2059  0.3404  0.0459  136 THR   A C   
864  O  O   . THR   A 116 ? 2.0387 1.6295 1.8769 0.2118  0.3297  0.0356  136 THR   A O   
865  C  CB  . THR   A 116 ? 1.8026 1.4178 1.5822 0.1798  0.3254  0.0268  136 THR   A CB  
866  O  OG1 . THR   A 116 ? 2.0115 1.5946 1.7261 0.1896  0.3415  0.0190  136 THR   A OG1 
867  C  CG2 . THR   A 116 ? 1.8451 1.4062 1.5816 0.1648  0.2913  0.0100  136 THR   A CG2 
868  N  N   . PHE   A 117 ? 1.8014 1.5223 1.7577 0.1949  0.3350  0.0636  137 PHE   A N   
869  C  CA  . PHE   A 117 ? 1.7721 1.5162 1.7787 0.1898  0.3151  0.0727  137 PHE   A CA  
870  C  C   . PHE   A 117 ? 1.7182 1.5115 1.7985 0.2141  0.3380  0.0911  137 PHE   A C   
871  O  O   . PHE   A 117 ? 1.7132 1.5629 1.8600 0.2039  0.3217  0.1046  137 PHE   A O   
872  C  CB  . PHE   A 117 ? 1.7453 1.5309 1.7796 0.1537  0.2796  0.0758  137 PHE   A CB  
873  C  CG  . PHE   A 117 ? 1.7642 1.5152 1.7392 0.1294  0.2577  0.0599  137 PHE   A CG  
874  C  CD1 . PHE   A 117 ? 1.8767 1.5668 1.8008 0.1230  0.2404  0.0475  137 PHE   A CD1 
875  C  CD2 . PHE   A 117 ? 1.7068 1.4855 1.6795 0.1130  0.2531  0.0580  137 PHE   A CD2 
876  C  CE1 . PHE   A 117 ? 1.8708 1.5343 1.7481 0.0994  0.2176  0.0335  137 PHE   A CE1 
877  C  CE2 . PHE   A 117 ? 1.7388 1.4902 1.6618 0.0926  0.2311  0.0443  137 PHE   A CE2 
878  C  CZ  . PHE   A 117 ? 1.8336 1.5303 1.7115 0.0852  0.2127  0.0320  137 PHE   A CZ  
879  N  N   . THR   A 118 ? 1.8213 1.5939 1.8900 0.2481  0.3756  0.0918  138 THR   A N   
880  C  CA  . THR   A 118 ? 1.8262 1.6376 1.9635 0.2764  0.3970  0.1085  138 THR   A CA  
881  C  C   . THR   A 118 ? 1.8466 1.6203 1.9764 0.2899  0.3821  0.1071  138 THR   A C   
882  O  O   . THR   A 118 ? 1.8554 1.5546 1.9125 0.2881  0.3705  0.0909  138 THR   A O   
883  C  CB  . THR   A 118 ? 1.8421 1.6432 1.9685 0.3116  0.4464  0.1107  138 THR   A CB  
884  O  OG1 . THR   A 118 ? 1.8672 1.5784 1.9002 0.3315  0.4570  0.0914  138 THR   A OG1 
885  C  CG2 . THR   A 118 ? 1.7360 1.5681 1.8646 0.2981  0.4633  0.1148  138 THR   A CG2 
886  N  N   . SER   A 119 ? 1.8705 1.6944 2.0768 0.3037  0.3810  0.1249  139 SER   A N   
887  C  CA  . SER   A 119 ? 1.8769 1.6692 2.0821 0.3177  0.3653  0.1277  139 SER   A CA  
888  C  C   . SER   A 119 ? 1.9345 1.6386 2.0688 0.3485  0.3857  0.1137  139 SER   A C   
889  O  O   . SER   A 119 ? 1.9911 1.6408 2.0942 0.3508  0.3668  0.1097  139 SER   A O   
890  C  CB  . SER   A 119 ? 1.9364 1.7975 2.2356 0.3374  0.3677  0.1498  139 SER   A CB  
891  O  OG  . SER   A 119 ? 1.9329 1.8536 2.2821 0.3074  0.3334  0.1600  139 SER   A OG  
892  N  N   . GLY   A 120 ? 1.9805 1.6648 2.0846 0.3724  0.4241  0.1061  140 GLY   A N   
893  C  CA  . GLY   A 120 ? 1.9813 1.5748 2.0063 0.4032  0.4441  0.0891  140 GLY   A CA  
894  C  C   . GLY   A 120 ? 1.9634 1.4796 1.8901 0.3787  0.4248  0.0646  140 GLY   A C   
895  O  O   . GLY   A 120 ? 1.9174 1.3483 1.7790 0.3871  0.4155  0.0490  140 GLY   A O   
896  N  N   . LYS   A 121 ? 1.9608 1.5046 1.8775 0.3480  0.4168  0.0609  141 LYS   A N   
897  C  CA  . LYS   A 121 ? 1.9704 1.4503 1.8022 0.3222  0.3930  0.0388  141 LYS   A CA  
898  C  C   . LYS   A 121 ? 1.9800 1.4382 1.8092 0.2912  0.3487  0.0363  141 LYS   A C   
899  O  O   . LYS   A 121 ? 2.0774 1.4556 1.8360 0.2841  0.3318  0.0177  141 LYS   A O   
900  C  CB  . LYS   A 121 ? 1.9300 1.4506 1.7595 0.2976  0.3920  0.0384  141 LYS   A CB  
901  C  CG  . LYS   A 121 ? 1.8992 1.4208 1.7061 0.3254  0.4365  0.0387  141 LYS   A CG  
902  C  CD  . LYS   A 121 ? 2.0380 1.4639 1.7323 0.3418  0.4455  0.0139  141 LYS   A CD  
903  C  CE  . LYS   A 121 ? 2.0474 1.4731 1.7170 0.3758  0.4963  0.0173  141 LYS   A CE  
904  N  NZ  . LYS   A 121 ? 1.9240 1.4340 1.6566 0.3606  0.5094  0.0378  141 LYS   A NZ  
905  N  N   . LEU   A 122 ? 2.0044 1.5308 1.9083 0.2723  0.3296  0.0551  142 LEU   A N   
906  C  CA  . LEU   A 122 ? 1.9614 1.4691 1.8658 0.2471  0.2933  0.0574  142 LEU   A CA  
907  C  C   . LEU   A 122 ? 2.0425 1.4818 1.9231 0.2732  0.2963  0.0560  142 LEU   A C   
908  O  O   . LEU   A 122 ? 2.0566 1.4299 1.8904 0.2568  0.2732  0.0464  142 LEU   A O   
909  C  CB  . LEU   A 122 ? 1.8603 1.4519 1.8440 0.2289  0.2758  0.0787  142 LEU   A CB  
910  C  CG  . LEU   A 122 ? 1.7473 1.4028 1.7584 0.1942  0.2588  0.0819  142 LEU   A CG  
911  C  CD1 . LEU   A 122 ? 1.9066 1.6114 1.9470 0.2058  0.2845  0.0850  142 LEU   A CD1 
912  C  CD2 . LEU   A 122 ? 1.5405 1.2489 1.6076 0.1779  0.2346  0.0996  142 LEU   A CD2 
913  N  N   . LYS   A 123 ? 1.8994 1.3553 1.8168 0.3135  0.3239  0.0669  143 LYS   A N   
914  C  CA  . LYS   A 123 ? 1.9806 1.3699 1.8763 0.3439  0.3287  0.0662  143 LYS   A CA  
915  C  C   . LYS   A 123 ? 2.1340 1.4159 1.9318 0.3522  0.3331  0.0394  143 LYS   A C   
916  O  O   . LYS   A 123 ? 2.2168 1.4219 1.9764 0.3561  0.3190  0.0335  143 LYS   A O   
917  C  CB  . LYS   A 123 ? 1.9672 1.3967 1.9194 0.3907  0.3623  0.0809  143 LYS   A CB  
918  C  CG  . LYS   A 123 ? 2.0790 1.4523 2.0242 0.4247  0.3643  0.0853  143 LYS   A CG  
919  C  CD  . LYS   A 123 ? 1.9361 1.3798 1.9677 0.4616  0.3845  0.1081  143 LYS   A CD  
920  C  CE  . LYS   A 123 ? 2.1504 1.5325 2.1700 0.5036  0.3912  0.1113  143 LYS   A CE  
921  N  NZ  . LYS   A 123 ? 2.1313 1.5820 2.2396 0.5185  0.3809  0.1392  143 LYS   A NZ  
922  N  N   . GLU   A 124 ? 2.0517 1.3223 1.8042 0.3546  0.3506  0.0229  144 GLU   A N   
923  C  CA  . GLU   A 124 ? 2.1375 1.3039 1.7891 0.3583  0.3479  -0.0053 144 GLU   A CA  
924  C  C   . GLU   A 124 ? 2.2787 1.4029 1.8946 0.3111  0.3025  -0.0160 144 GLU   A C   
925  O  O   . GLU   A 124 ? 2.2672 1.2945 1.8063 0.3113  0.2910  -0.0380 144 GLU   A O   
926  C  CB  . GLU   A 124 ? 2.2441 1.4087 1.8492 0.3698  0.3739  -0.0194 144 GLU   A CB  
927  C  CG  . GLU   A 124 ? 2.4631 1.5912 2.0371 0.4259  0.4208  -0.0252 144 GLU   A CG  
928  C  CD  . GLU   A 124 ? 2.5445 1.7093 2.1074 0.4399  0.4563  -0.0252 144 GLU   A CD  
929  O  OE1 . GLU   A 124 ? 2.6527 1.7599 2.1277 0.4351  0.4539  -0.0472 144 GLU   A OE1 
930  O  OE2 . GLU   A 124 ? 2.4193 1.6684 2.0601 0.4556  0.4859  -0.0026 144 GLU   A OE2 
931  N  N   . MET   A 125 ? 2.2914 1.4845 1.9620 0.2713  0.2767  -0.0010 145 MET   A N   
932  C  CA  . MET   A 125 ? 2.3159 1.4813 1.9608 0.2250  0.2368  -0.0090 145 MET   A CA  
933  C  C   . MET   A 125 ? 2.4268 1.5640 2.0893 0.2115  0.2143  0.0031  145 MET   A C   
934  O  O   . MET   A 125 ? 2.4178 1.5133 2.0522 0.1760  0.1840  -0.0043 145 MET   A O   
935  C  CB  . MET   A 125 ? 2.1882 1.4403 1.8765 0.1890  0.2220  -0.0002 145 MET   A CB  
936  C  CG  . MET   A 125 ? 2.1313 1.4497 1.8478 0.2066  0.2499  0.0048  145 MET   A CG  
937  S  SD  . MET   A 125 ? 2.0684 1.4580 1.8043 0.1696  0.2342  0.0056  145 MET   A SD  
938  C  CE  . MET   A 125 ? 2.2318 1.5337 1.8695 0.1563  0.2161  -0.0245 145 MET   A CE  
939  N  N   . VAL   A 126 ? 2.5622 1.7237 2.2732 0.2378  0.2276  0.0234  146 VAL   A N   
940  C  CA  . VAL   A 126 ? 2.5708 1.7010 2.2943 0.2286  0.2079  0.0381  146 VAL   A CA  
941  C  C   . VAL   A 126 ? 2.6607 1.6701 2.3096 0.2289  0.1968  0.0191  146 VAL   A C   
942  O  O   . VAL   A 126 ? 2.6877 1.6624 2.3297 0.1962  0.1691  0.0247  146 VAL   A O   
943  C  CB  . VAL   A 126 ? 2.5036 1.6771 2.2869 0.2633  0.2239  0.0620  146 VAL   A CB  
944  C  CG1 . VAL   A 126 ? 2.4840 1.6150 2.2709 0.2583  0.2044  0.0785  146 VAL   A CG1 
945  C  CG2 . VAL   A 126 ? 2.4385 1.7287 2.2959 0.2542  0.2262  0.0797  146 VAL   A CG2 
946  N  N   . PRO   A 127 ? 2.7262 1.6652 2.3162 0.2639  0.2171  -0.0030 147 PRO   A N   
947  C  CA  . PRO   A 127 ? 2.8416 1.6580 2.3537 0.2591  0.2007  -0.0248 147 PRO   A CA  
948  C  C   . PRO   A 127 ? 2.8523 1.6415 2.3236 0.2096  0.1682  -0.0434 147 PRO   A C   
949  O  O   . PRO   A 127 ? 2.9471 1.6637 2.3893 0.1828  0.1403  -0.0487 147 PRO   A O   
950  C  CB  . PRO   A 127 ? 2.8784 1.6369 2.3361 0.3131  0.2342  -0.0452 147 PRO   A CB  
951  C  CG  . PRO   A 127 ? 2.8068 1.6530 2.3340 0.3508  0.2684  -0.0234 147 PRO   A CG  
952  C  CD  . PRO   A 127 ? 2.7127 1.6727 2.3082 0.3149  0.2576  -0.0055 147 PRO   A CD  
953  N  N   . ILE   A 128 ? 2.7003 1.5439 2.1701 0.1964  0.1697  -0.0526 148 ILE   A N   
954  C  CA  . ILE   A 128 ? 2.6454 1.4634 2.0770 0.1523  0.1365  -0.0710 148 ILE   A CA  
955  C  C   . ILE   A 128 ? 2.6451 1.5226 2.1364 0.1019  0.1078  -0.0505 148 ILE   A C   
956  O  O   . ILE   A 128 ? 2.6539 1.4878 2.1244 0.0629  0.0755  -0.0587 148 ILE   A O   
957  C  CB  . ILE   A 128 ? 2.6694 1.5151 2.0696 0.1573  0.1456  -0.0886 148 ILE   A CB  
958  C  CG1 . ILE   A 128 ? 2.7490 1.5495 2.0943 0.2113  0.1824  -0.1044 148 ILE   A CG1 
959  C  CG2 . ILE   A 128 ? 2.7593 1.5621 2.1100 0.1173  0.1076  -0.1110 148 ILE   A CG2 
960  C  CD1 . ILE   A 128 ? 2.6151 1.4912 2.0175 0.2478  0.2228  -0.0836 148 ILE   A CD1 
961  N  N   . ILE   A 129 ? 2.5840 1.5612 2.1497 0.1012  0.1187  -0.0239 149 ILE   A N   
962  C  CA  . ILE   A 129 ? 2.5455 1.5753 2.1630 0.0583  0.0955  -0.0031 149 ILE   A CA  
963  C  C   . ILE   A 129 ? 2.6409 1.6030 2.2520 0.0460  0.0804  0.0074  149 ILE   A C   
964  O  O   . ILE   A 129 ? 2.6062 1.5683 2.2306 0.0026  0.0551  0.0153  149 ILE   A O   
965  C  CB  . ILE   A 129 ? 2.3835 1.5227 2.0739 0.0656  0.1103  0.0222  149 ILE   A CB  
966  C  CG1 . ILE   A 129 ? 2.3436 1.5482 2.0426 0.0690  0.1211  0.0133  149 ILE   A CG1 
967  C  CG2 . ILE   A 129 ? 2.2122 1.3974 1.9484 0.0274  0.0898  0.0449  149 ILE   A CG2 
968  C  CD1 . ILE   A 129 ? 2.0315 1.3410 1.8008 0.0680  0.1289  0.0353  149 ILE   A CD1 
969  N  N   . ALA   A 130 ? 2.6315 1.5323 2.2217 0.0844  0.0965  0.0082  150 ALA   A N   
970  C  CA  . ALA   A 130 ? 2.6998 1.5349 2.2858 0.0782  0.0851  0.0222  150 ALA   A CA  
971  C  C   . ALA   A 130 ? 2.8286 1.5763 2.3689 0.0387  0.0547  0.0067  150 ALA   A C   
972  O  O   . ALA   A 130 ? 2.8527 1.5520 2.3963 0.0208  0.0410  0.0221  150 ALA   A O   
973  C  CB  . ALA   A 130 ? 2.7230 1.5003 2.2876 0.1327  0.1086  0.0214  150 ALA   A CB  
974  N  N   . GLN   A 131 ? 2.7952 1.5202 2.2934 0.0237  0.0421  -0.0223 151 GLN   A N   
975  C  CA  . GLN   A 131 ? 2.8348 1.4820 2.2957 -0.0180 0.0079  -0.0379 151 GLN   A CA  
976  C  C   . GLN   A 131 ? 2.7778 1.4910 2.2954 -0.0739 -0.0152 -0.0175 151 GLN   A C   
977  O  O   . GLN   A 131 ? 2.8273 1.5058 2.3598 -0.1034 -0.0306 -0.0007 151 GLN   A O   
978  C  CB  . GLN   A 131 ? 2.8878 1.4891 2.2821 -0.0151 -0.0021 -0.0762 151 GLN   A CB  
979  C  CG  . GLN   A 131 ? 3.0018 1.5415 2.3687 -0.0657 -0.0445 -0.0926 151 GLN   A CG  
980  C  CD  . GLN   A 131 ? 3.0649 1.5712 2.3678 -0.0657 -0.0599 -0.1295 151 GLN   A CD  
981  O  OE1 . GLN   A 131 ? 3.1820 1.6642 2.4331 -0.0206 -0.0371 -0.1484 151 GLN   A OE1 
982  N  NE2 . GLN   A 131 ? 3.0165 1.5235 2.3235 -0.1158 -0.0988 -0.1386 151 GLN   A NE2 
983  N  N   . TYR   A 132 ? 2.7355 1.5441 2.2856 -0.0879 -0.0160 -0.0175 152 TYR   A N   
984  C  CA  . TYR   A 132 ? 2.7227 1.5903 2.3193 -0.1401 -0.0390 -0.0046 152 TYR   A CA  
985  C  C   . TYR   A 132 ? 2.6329 1.5523 2.2898 -0.1544 -0.0321 0.0335  152 TYR   A C   
986  O  O   . TYR   A 132 ? 2.6018 1.5527 2.2947 -0.1989 -0.0494 0.0480  152 TYR   A O   
987  C  CB  . TYR   A 132 ? 2.6313 1.5871 2.2459 -0.1439 -0.0387 -0.0135 152 TYR   A CB  
988  C  CG  . TYR   A 132 ? 2.7014 1.6053 2.2512 -0.1338 -0.0489 -0.0496 152 TYR   A CG  
989  C  CD1 . TYR   A 132 ? 2.6988 1.5651 2.2258 -0.1718 -0.0850 -0.0682 152 TYR   A CD1 
990  C  CD2 . TYR   A 132 ? 2.6875 1.5796 2.1983 -0.0860 -0.0228 -0.0641 152 TYR   A CD2 
991  C  CE1 . TYR   A 132 ? 2.7289 1.5436 2.1886 -0.1610 -0.0973 -0.1019 152 TYR   A CE1 
992  C  CE2 . TYR   A 132 ? 2.7036 1.5445 2.1464 -0.0743 -0.0301 -0.0959 152 TYR   A CE2 
993  C  CZ  . TYR   A 132 ? 2.7812 1.5813 2.1948 -0.1112 -0.0687 -0.1154 152 TYR   A CZ  
994  O  OH  . TYR   A 132 ? 2.9570 1.7027 2.2955 -0.0979 -0.0786 -0.1477 152 TYR   A OH  
995  N  N   . GLY   A 133 ? 2.5997 1.5308 2.2687 -0.1169 -0.0073 0.0509  153 GLY   A N   
996  C  CA  . GLY   A 133 ? 2.5657 1.5212 2.2756 -0.1277 -0.0038 0.0865  153 GLY   A CA  
997  C  C   . GLY   A 133 ? 2.6589 1.5239 2.3504 -0.1570 -0.0219 0.0943  153 GLY   A C   
998  O  O   . GLY   A 133 ? 2.6695 1.5598 2.3962 -0.1926 -0.0296 0.1206  153 GLY   A O   
999  N  N   . ASP   A 134 ? 2.6619 1.4173 2.2962 -0.1425 -0.0281 0.0715  154 ASP   A N   
1000 C  CA  . ASP   A 134 ? 2.7001 1.3574 2.3122 -0.1742 -0.0494 0.0743  154 ASP   A CA  
1001 C  C   . ASP   A 134 ? 2.7484 1.4100 2.3691 -0.2303 -0.0793 0.0624  154 ASP   A C   
1002 O  O   . ASP   A 134 ? 2.7727 1.4019 2.4103 -0.2735 -0.0966 0.0788  154 ASP   A O   
1003 C  CB  . ASP   A 134 ? 2.7826 1.3163 2.3259 -0.1397 -0.0484 0.0499  154 ASP   A CB  
1004 C  CG  . ASP   A 134 ? 2.8488 1.3797 2.3899 -0.0822 -0.0192 0.0629  154 ASP   A CG  
1005 O  OD1 . ASP   A 134 ? 2.8570 1.4530 2.4462 -0.0786 -0.0075 0.0970  154 ASP   A OD1 
1006 O  OD2 . ASP   A 134 ? 2.8362 1.3010 2.3271 -0.0393 -0.0082 0.0391  154 ASP   A OD2 
1007 N  N   . VAL   A 135 ? 2.8440 1.5446 2.4550 -0.2308 -0.0864 0.0354  155 VAL   A N   
1008 C  CA  . VAL   A 135 ? 2.8458 1.5815 2.4824 -0.2829 -0.1143 0.0296  155 VAL   A CA  
1009 C  C   . VAL   A 135 ? 2.8174 1.6622 2.5301 -0.3105 -0.1069 0.0655  155 VAL   A C   
1010 O  O   . VAL   A 135 ? 2.8211 1.6760 2.5693 -0.3599 -0.1253 0.0794  155 VAL   A O   
1011 C  CB  . VAL   A 135 ? 2.8975 1.6566 2.5054 -0.2715 -0.1223 -0.0046 155 VAL   A CB  
1012 C  CG1 . VAL   A 135 ? 2.8808 1.7024 2.5293 -0.3208 -0.1494 -0.0059 155 VAL   A CG1 
1013 C  CG2 . VAL   A 135 ? 2.9501 1.5890 2.4742 -0.2512 -0.1341 -0.0415 155 VAL   A CG2 
1014 N  N   . LEU   A 136 ? 2.6841 1.6098 2.4229 -0.2787 -0.0792 0.0818  156 LEU   A N   
1015 C  CA  . LEU   A 136 ? 2.5333 1.5567 2.3348 -0.2985 -0.0697 0.1152  156 LEU   A CA  
1016 C  C   . LEU   A 136 ? 2.5173 1.5017 2.3337 -0.3208 -0.0691 0.1481  156 LEU   A C   
1017 O  O   . LEU   A 136 ? 2.5293 1.5454 2.3856 -0.3655 -0.0781 0.1676  156 LEU   A O   
1018 C  CB  . LEU   A 136 ? 2.3374 1.4386 2.1545 -0.2564 -0.0430 0.1232  156 LEU   A CB  
1019 C  CG  . LEU   A 136 ? 2.2342 1.4352 2.1044 -0.2634 -0.0294 0.1546  156 LEU   A CG  
1020 C  CD1 . LEU   A 136 ? 2.0943 1.3681 2.0032 -0.3018 -0.0412 0.1544  156 LEU   A CD1 
1021 C  CD2 . LEU   A 136 ? 2.2029 1.4604 2.0785 -0.2186 -0.0083 0.1549  156 LEU   A CD2 
1022 N  N   . VAL   A 137 ? 2.5806 1.4938 2.3652 -0.2896 -0.0579 0.1556  157 VAL   A N   
1023 C  CA  . VAL   A 137 ? 2.5462 1.4141 2.3380 -0.3054 -0.0557 0.1895  157 VAL   A CA  
1024 C  C   . VAL   A 137 ? 2.5936 1.4013 2.3886 -0.3606 -0.0807 0.1900  157 VAL   A C   
1025 O  O   . VAL   A 137 ? 2.5585 1.3963 2.3941 -0.3997 -0.0811 0.2213  157 VAL   A O   
1026 C  CB  . VAL   A 137 ? 2.4952 1.2802 2.2447 -0.2593 -0.0443 0.1912  157 VAL   A CB  
1027 C  CG1 . VAL   A 137 ? 2.6381 1.3519 2.3844 -0.2790 -0.0472 0.2231  157 VAL   A CG1 
1028 C  CG2 . VAL   A 137 ? 2.4904 1.3480 2.2539 -0.2114 -0.0203 0.2012  157 VAL   A CG2 
1029 N  N   . ARG   A 138 ? 2.6799 1.4004 2.4314 -0.3645 -0.1020 0.1553  158 ARG   A N   
1030 C  CA  . ARG   A 138 ? 2.6898 1.3432 2.4428 -0.4181 -0.1310 0.1524  158 ARG   A CA  
1031 C  C   . ARG   A 138 ? 2.7141 1.4611 2.5296 -0.4689 -0.1435 0.1612  158 ARG   A C   
1032 O  O   . ARG   A 138 ? 2.7387 1.4927 2.5940 -0.5095 -0.1514 0.1768  158 ARG   A O   
1033 C  CB  . ARG   A 138 ? 2.8134 1.3675 2.5044 -0.4081 -0.1535 0.1071  158 ARG   A CB  
1034 C  CG  . ARG   A 138 ? 2.7766 1.2242 2.4181 -0.3730 -0.1463 0.1011  158 ARG   A CG  
1035 C  CD  . ARG   A 138 ? 2.8950 1.2590 2.4916 -0.3769 -0.1717 0.0599  158 ARG   A CD  
1036 N  NE  . ARG   A 138 ? 2.9083 1.3081 2.5061 -0.4024 -0.1967 0.0310  158 ARG   A NE  
1037 C  CZ  . ARG   A 138 ? 3.0089 1.4122 2.5640 -0.3744 -0.1970 0.0015  158 ARG   A CZ  
1038 N  NH1 . ARG   A 138 ? 2.9819 1.3583 2.4927 -0.3196 -0.1710 -0.0040 158 ARG   A NH1 
1039 N  NH2 . ARG   A 138 ? 2.9880 1.4250 2.5464 -0.4003 -0.2228 -0.0220 158 ARG   A NH2 
1040 N  N   . ASN   A 139 ? 2.7202 1.5664 2.5560 -0.4563 -0.1384 0.1482  159 ASN   A N   
1041 C  CA  . ASN   A 139 ? 2.7241 1.6673 2.6238 -0.4990 -0.1472 0.1591  159 ASN   A CA  
1042 C  C   . ASN   A 139 ? 2.6757 1.6928 2.6288 -0.5117 -0.1225 0.2054  159 ASN   A C   
1043 O  O   . ASN   A 139 ? 2.6898 1.7475 2.6960 -0.5591 -0.1292 0.2264  159 ASN   A O   
1044 C  CB  . ASN   A 139 ? 2.6894 1.7139 2.5932 -0.4794 -0.1482 0.1337  159 ASN   A CB  
1045 C  CG  . ASN   A 139 ? 2.7504 1.7043 2.5952 -0.4659 -0.1715 0.0888  159 ASN   A CG  
1046 O  OD1 . ASN   A 139 ? 2.7928 1.6750 2.6214 -0.4984 -0.2031 0.0722  159 ASN   A OD1 
1047 N  ND2 . ASN   A 139 ? 2.7770 1.7521 2.5891 -0.4188 -0.1567 0.0692  159 ASN   A ND2 
1048 N  N   . LEU   A 140 ? 2.5957 1.6332 2.5362 -0.4696 -0.0940 0.2226  160 LEU   A N   
1049 C  CA  . LEU   A 140 ? 2.5056 1.5982 2.4839 -0.4799 -0.0719 0.2670  160 LEU   A CA  
1050 C  C   . LEU   A 140 ? 2.6056 1.6127 2.5778 -0.5064 -0.0738 0.2955  160 LEU   A C   
1051 O  O   . LEU   A 140 ? 2.5976 1.6514 2.6078 -0.5280 -0.0582 0.3311  160 LEU   A O   
1052 C  CB  . LEU   A 140 ? 2.3166 1.4553 2.2824 -0.4286 -0.0453 0.2781  160 LEU   A CB  
1053 C  CG  . LEU   A 140 ? 2.2804 1.5098 2.2545 -0.3964 -0.0360 0.2597  160 LEU   A CG  
1054 C  CD1 . LEU   A 140 ? 2.3239 1.5114 2.2531 -0.3451 -0.0312 0.2365  160 LEU   A CD1 
1055 C  CD2 . LEU   A 140 ? 2.0745 1.3987 2.0813 -0.3907 -0.0141 0.2902  160 LEU   A CD2 
1056 N  N   . ARG   A 141 ? 2.5939 1.4853 2.5183 -0.4970 -0.0876 0.2772  161 ARG   A N   
1057 C  CA  . ARG   A 141 ? 2.6338 1.4617 2.5570 -0.5090 -0.0838 0.2953  161 ARG   A CA  
1058 C  C   . ARG   A 141 ? 2.7282 1.5815 2.7010 -0.5609 -0.0951 0.2964  161 ARG   A C   
1059 O  O   . ARG   A 141 ? 2.9146 1.7500 2.9056 -0.5796 -0.0842 0.3236  161 ARG   A O   
1060 C  CB  . ARG   A 141 ? 2.6521 1.3571 2.5137 -0.4798 -0.0945 0.2701  161 ARG   A CB  
1061 C  CG  . ARG   A 141 ? 2.7157 1.3582 2.5569 -0.4578 -0.0778 0.2989  161 ARG   A CG  
1062 C  CD  . ARG   A 141 ? 2.7413 1.2841 2.5197 -0.4098 -0.0813 0.2747  161 ARG   A CD  
1063 N  NE  . ARG   A 141 ? 2.8300 1.3481 2.5906 -0.3712 -0.0612 0.3051  161 ARG   A NE  
1064 C  CZ  . ARG   A 141 ? 2.9441 1.3884 2.6581 -0.3217 -0.0580 0.2926  161 ARG   A CZ  
1065 N  NH1 . ARG   A 141 ? 3.0595 1.4435 2.7346 -0.3030 -0.0703 0.2497  161 ARG   A NH1 
1066 N  NH2 . ARG   A 141 ? 3.0176 1.4511 2.7233 -0.2877 -0.0416 0.3238  161 ARG   A NH2 
1067 N  N   . ARG   A 142 ? 2.6968 1.5915 2.6920 -0.5837 -0.1167 0.2685  162 ARG   A N   
1068 C  CA  . ARG   A 142 ? 2.7409 1.6624 2.7871 -0.6318 -0.1308 0.2676  162 ARG   A CA  
1069 C  C   . ARG   A 142 ? 2.7798 1.8184 2.8940 -0.6550 -0.1092 0.3013  162 ARG   A C   
1070 O  O   . ARG   A 142 ? 2.9086 1.9616 3.0650 -0.6891 -0.1041 0.3204  162 ARG   A O   
1071 C  CB  . ARG   A 142 ? 2.7828 1.7007 2.8235 -0.6438 -0.1655 0.2237  162 ARG   A CB  
1072 C  CG  . ARG   A 142 ? 2.7766 1.5725 2.7486 -0.6259 -0.1880 0.1876  162 ARG   A CG  
1073 C  CD  . ARG   A 142 ? 2.7865 1.5836 2.7344 -0.6228 -0.2176 0.1438  162 ARG   A CD  
1074 N  NE  . ARG   A 142 ? 2.8743 1.5587 2.7615 -0.6142 -0.2420 0.1078  162 ARG   A NE  
1075 C  CZ  . ARG   A 142 ? 2.9867 1.6362 2.8209 -0.5948 -0.2632 0.0666  162 ARG   A CZ  
1076 N  NH1 . ARG   A 142 ? 2.8736 1.5883 2.7084 -0.5834 -0.2643 0.0560  162 ARG   A NH1 
1077 N  NH2 . ARG   A 142 ? 2.9809 1.5261 2.7569 -0.5853 -0.2828 0.0355  162 ARG   A NH2 
1078 N  N   . GLU   A 143 ? 2.8843 2.0061 3.0087 -0.6358 -0.0950 0.3086  163 GLU   A N   
1079 C  CA  . GLU   A 143 ? 2.7671 2.0029 2.9498 -0.6502 -0.0719 0.3379  163 GLU   A CA  
1080 C  C   . GLU   A 143 ? 2.7750 2.0172 2.9487 -0.6341 -0.0373 0.3797  163 GLU   A C   
1081 O  O   . GLU   A 143 ? 2.6920 2.0241 2.9034 -0.6400 -0.0138 0.4051  163 GLU   A O   
1082 C  CB  . GLU   A 143 ? 2.7428 2.0678 2.9409 -0.6366 -0.0739 0.3243  163 GLU   A CB  
1083 C  CG  . GLU   A 143 ? 2.7711 2.1486 3.0127 -0.6640 -0.0989 0.2989  163 GLU   A CG  
1084 C  CD  . GLU   A 143 ? 2.8445 2.1359 3.0482 -0.6683 -0.1364 0.2582  163 GLU   A CD  
1085 O  OE1 . GLU   A 143 ? 2.8911 2.1027 3.0818 -0.6850 -0.1484 0.2537  163 GLU   A OE1 
1086 O  OE2 . GLU   A 143 ? 2.8378 2.1391 3.0209 -0.6536 -0.1534 0.2299  163 GLU   A OE2 
1087 N  N   . ALA   A 144 ? 2.8343 1.9828 2.9558 -0.6111 -0.0338 0.3867  164 ALA   A N   
1088 C  CA  . ALA   A 144 ? 2.8472 1.9892 2.9524 -0.5939 -0.0048 0.4265  164 ALA   A CA  
1089 C  C   . ALA   A 144 ? 2.9917 2.0655 3.0965 -0.6158 0.0014  0.4465  164 ALA   A C   
1090 O  O   . ALA   A 144 ? 2.9284 2.0292 3.0439 -0.6212 0.0280  0.4834  164 ALA   A O   
1091 C  CB  . ALA   A 144 ? 2.7673 1.8590 2.8149 -0.5459 -0.0033 0.4252  164 ALA   A CB  
1092 N  N   . GLU   A 145 ? 3.2628 2.2455 3.3517 -0.6276 -0.0222 0.4226  165 GLU   A N   
1093 C  CA  . GLU   A 145 ? 3.3699 2.2916 3.4675 -0.6556 -0.0189 0.4391  165 GLU   A CA  
1094 C  C   . GLU   A 145 ? 3.3209 2.3186 3.4853 -0.7024 -0.0114 0.4530  165 GLU   A C   
1095 O  O   . GLU   A 145 ? 3.4550 2.4249 3.6342 -0.7271 0.0019  0.4785  165 GLU   A O   
1096 C  CB  . GLU   A 145 ? 3.4299 2.2433 3.4980 -0.6592 -0.0492 0.4049  165 GLU   A CB  
1097 C  CG  . GLU   A 145 ? 3.5732 2.2979 3.5741 -0.6106 -0.0526 0.3937  165 GLU   A CG  
1098 C  CD  . GLU   A 145 ? 3.7275 2.3397 3.6956 -0.6124 -0.0785 0.3617  165 GLU   A CD  
1099 O  OE1 . GLU   A 145 ? 3.7805 2.3895 3.7748 -0.6507 -0.1005 0.3406  165 GLU   A OE1 
1100 O  OE2 . GLU   A 145 ? 3.8327 2.3610 3.7487 -0.5737 -0.0776 0.3572  165 GLU   A OE2 
1101 N  N   . THR   A 146 ? 3.0074 2.0994 3.2131 -0.7139 -0.0191 0.4373  166 THR   A N   
1102 C  CA  . THR   A 146 ? 2.8364 2.0209 3.1105 -0.7504 -0.0081 0.4519  166 THR   A CA  
1103 C  C   . THR   A 146 ? 2.8403 2.1277 3.1252 -0.7280 0.0202  0.4723  166 THR   A C   
1104 O  O   . THR   A 146 ? 2.7957 2.1385 3.0830 -0.7100 0.0110  0.4518  166 THR   A O   
1105 C  CB  . THR   A 146 ? 2.6977 1.9100 3.0123 -0.7785 -0.0416 0.4165  166 THR   A CB  
1106 O  OG1 . THR   A 146 ? 2.6564 1.9513 2.9810 -0.7596 -0.0465 0.3993  166 THR   A OG1 
1107 C  CG2 . THR   A 146 ? 2.8041 1.9042 3.0773 -0.7792 -0.0768 0.3821  166 THR   A CG2 
1108 N  N   . GLY   A 147 ? 2.7775 2.0870 3.0648 -0.7283 0.0547  0.5121  167 GLY   A N   
1109 C  CA  . GLY   A 147 ? 2.7342 2.1268 3.0174 -0.7020 0.0833  0.5334  167 GLY   A CA  
1110 C  C   . GLY   A 147 ? 2.6200 2.1292 2.9537 -0.7062 0.0838  0.5204  167 GLY   A C   
1111 O  O   . GLY   A 147 ? 2.5263 2.1150 2.8902 -0.7112 0.1116  0.5431  167 GLY   A O   
1112 N  N   . LYS   A 148 ? 2.4887 2.0062 2.8278 -0.7014 0.0541  0.4837  168 LYS   A N   
1113 C  CA  . LYS   A 148 ? 2.3466 1.9675 2.7327 -0.7040 0.0498  0.4678  168 LYS   A CA  
1114 C  C   . LYS   A 148 ? 2.2107 1.8691 2.5656 -0.6631 0.0550  0.4608  168 LYS   A C   
1115 O  O   . LYS   A 148 ? 2.2968 1.8946 2.6072 -0.6428 0.0363  0.4416  168 LYS   A O   
1116 C  CB  . LYS   A 148 ? 2.3633 1.9688 2.7761 -0.7283 0.0110  0.4315  168 LYS   A CB  
1117 C  CG  . LYS   A 148 ? 2.3816 2.0911 2.8469 -0.7328 0.0030  0.4150  168 LYS   A CG  
1118 C  CD  . LYS   A 148 ? 2.4620 2.1452 2.9443 -0.7555 -0.0396 0.3791  168 LYS   A CD  
1119 C  CE  . LYS   A 148 ? 2.4916 2.2760 3.0240 -0.7568 -0.0500 0.3627  168 LYS   A CE  
1120 N  NZ  . LYS   A 148 ? 2.3158 2.1764 2.9220 -0.7855 -0.0370 0.3807  168 LYS   A NZ  
1121 N  N   . PRO   A 149 ? 2.0972 1.8498 2.4712 -0.6487 0.0805  0.4756  169 PRO   A N   
1122 C  CA  . PRO   A 149 ? 2.1235 1.9159 2.4714 -0.6112 0.0840  0.4672  169 PRO   A CA  
1123 C  C   . PRO   A 149 ? 2.0462 1.8345 2.3961 -0.6083 0.0515  0.4289  169 PRO   A C   
1124 O  O   . PRO   A 149 ? 2.0887 1.8950 2.4782 -0.6331 0.0309  0.4088  169 PRO   A O   
1125 C  CB  . PRO   A 149 ? 2.0146 1.9156 2.3978 -0.6055 0.1120  0.4820  169 PRO   A CB  
1126 C  CG  . PRO   A 149 ? 2.0371 1.9355 2.4410 -0.6303 0.1340  0.5110  169 PRO   A CG  
1127 C  CD  . PRO   A 149 ? 2.1121 1.9267 2.5224 -0.6631 0.1117  0.5047  169 PRO   A CD  
1128 N  N   . VAL   A 150 ? 1.9786 1.7427 2.2843 -0.5773 0.0464  0.4196  170 VAL   A N   
1129 C  CA  . VAL   A 150 ? 2.0580 1.7946 2.3492 -0.5717 0.0169  0.3849  170 VAL   A CA  
1130 C  C   . VAL   A 150 ? 1.8776 1.7020 2.1784 -0.5447 0.0230  0.3700  170 VAL   A C   
1131 O  O   . VAL   A 150 ? 1.7925 1.6631 2.0818 -0.5165 0.0474  0.3846  170 VAL   A O   
1132 C  CB  . VAL   A 150 ? 2.0193 1.6546 2.2465 -0.5454 0.0088  0.3750  170 VAL   A CB  
1133 C  CG1 . VAL   A 150 ? 1.8088 1.4171 2.0103 -0.5256 -0.0153 0.3289  170 VAL   A CG1 
1134 C  CG2 . VAL   A 150 ? 2.0749 1.6183 2.2899 -0.5696 0.0036  0.3902  170 VAL   A CG2 
1135 N  N   . THR   A 151 ? 1.9806 1.8249 2.2971 -0.5490 -0.0001 0.3373  171 THR   A N   
1136 C  CA  . THR   A 151 ? 1.9294 1.8366 2.2417 -0.5151 0.0016  0.3135  171 THR   A CA  
1137 C  C   . THR   A 151 ? 1.9263 1.7698 2.1781 -0.4768 -0.0064 0.2859  171 THR   A C   
1138 O  O   . THR   A 151 ? 1.9474 1.7284 2.1775 -0.4818 -0.0300 0.2606  171 THR   A O   
1139 C  CB  . THR   A 151 ? 1.9608 1.9192 2.3178 -0.5365 -0.0194 0.2943  171 THR   A CB  
1140 O  OG1 . THR   A 151 ? 2.1192 2.0032 2.4585 -0.5534 -0.0522 0.2690  171 THR   A OG1 
1141 C  CG2 . THR   A 151 ? 1.9458 1.9707 2.3711 -0.5738 -0.0101 0.3225  171 THR   A CG2 
1142 N  N   . LEU   A 152 ? 1.8247 1.6843 2.0492 -0.4382 0.0130  0.2907  172 LEU   A N   
1143 C  CA  . LEU   A 152 ? 1.7325 1.5298 1.9061 -0.4032 0.0097  0.2726  172 LEU   A CA  
1144 C  C   . LEU   A 152 ? 1.7981 1.6063 1.9593 -0.3823 -0.0029 0.2362  172 LEU   A C   
1145 O  O   . LEU   A 152 ? 1.7760 1.5180 1.9006 -0.3675 -0.0132 0.2152  172 LEU   A O   
1146 C  CB  . LEU   A 152 ? 1.6908 1.5020 1.8439 -0.3709 0.0311  0.2914  172 LEU   A CB  
1147 C  CG  . LEU   A 152 ? 1.6874 1.4726 1.8342 -0.3802 0.0453  0.3289  172 LEU   A CG  
1148 C  CD1 . LEU   A 152 ? 1.7524 1.4354 1.8743 -0.3911 0.0343  0.3317  172 LEU   A CD1 
1149 C  CD2 . LEU   A 152 ? 1.7654 1.6090 1.9525 -0.4123 0.0584  0.3571  172 LEU   A CD2 
1150 N  N   . LYS   A 153 ? 1.6060 1.4941 1.7944 -0.3788 -0.0007 0.2291  173 LYS   A N   
1151 C  CA  . LYS   A 153 ? 1.6839 1.5809 1.8597 -0.3605 -0.0126 0.1972  173 LYS   A CA  
1152 C  C   . LYS   A 153 ? 1.6938 1.5351 1.8575 -0.3802 -0.0386 0.1753  173 LYS   A C   
1153 O  O   . LYS   A 153 ? 1.7517 1.5594 1.8806 -0.3596 -0.0472 0.1492  173 LYS   A O   
1154 C  CB  . LYS   A 153 ? 1.7139 1.7020 1.9242 -0.3580 -0.0086 0.1952  173 LYS   A CB  
1155 C  CG  . LYS   A 153 ? 1.5840 1.6076 1.7800 -0.3201 0.0072  0.1914  173 LYS   A CG  
1156 C  CD  . LYS   A 153 ? 1.5994 1.6958 1.8185 -0.3118 0.0071  0.1810  173 LYS   A CD  
1157 C  CE  . LYS   A 153 ? 1.4643 1.5500 1.6550 -0.2803 0.0049  0.1573  173 LYS   A CE  
1158 N  NZ  . LYS   A 153 ? 1.6143 1.7657 1.8226 -0.2673 0.0071  0.1493  173 LYS   A NZ  
1159 N  N   . ASP   A 154 ? 1.8368 1.6674 2.0279 -0.4203 -0.0517 0.1857  174 ASP   A N   
1160 C  CA  . ASP   A 154 ? 1.8686 1.6479 2.0491 -0.4424 -0.0820 0.1631  174 ASP   A CA  
1161 C  C   . ASP   A 154 ? 1.8882 1.5596 2.0131 -0.4330 -0.0882 0.1513  174 ASP   A C   
1162 O  O   . ASP   A 154 ? 1.9227 1.5432 2.0079 -0.4234 -0.1058 0.1220  174 ASP   A O   
1163 C  CB  . ASP   A 154 ? 1.8670 1.6719 2.1020 -0.4911 -0.0959 0.1789  174 ASP   A CB  
1164 C  CG  . ASP   A 154 ? 1.9496 1.8458 2.2333 -0.5004 -0.1046 0.1744  174 ASP   A CG  
1165 O  OD1 . ASP   A 154 ? 1.9160 1.8393 2.1817 -0.4708 -0.1054 0.1544  174 ASP   A OD1 
1166 O  OD2 . ASP   A 154 ? 2.0371 1.9783 2.3793 -0.5368 -0.1097 0.1923  174 ASP   A OD2 
1167 N  N   . VAL   A 155 ? 1.9357 1.5685 2.0531 -0.4330 -0.0732 0.1742  175 VAL   A N   
1168 C  CA  . VAL   A 155 ? 1.9234 1.4521 1.9884 -0.4197 -0.0772 0.1641  175 VAL   A CA  
1169 C  C   . VAL   A 155 ? 1.8670 1.3870 1.8923 -0.3690 -0.0615 0.1496  175 VAL   A C   
1170 O  O   . VAL   A 155 ? 1.9300 1.3753 1.9076 -0.3499 -0.0673 0.1279  175 VAL   A O   
1171 C  CB  . VAL   A 155 ? 1.7781 1.2653 1.8491 -0.4364 -0.0678 0.1955  175 VAL   A CB  
1172 C  CG1 . VAL   A 155 ? 1.8867 1.4439 1.9828 -0.4234 -0.0399 0.2271  175 VAL   A CG1 
1173 C  CG2 . VAL   A 155 ? 1.9656 1.3444 1.9816 -0.4162 -0.0696 0.1864  175 VAL   A CG2 
1174 N  N   . PHE   A 156 ? 1.7938 1.3896 1.8386 -0.3464 -0.0414 0.1608  176 PHE   A N   
1175 C  CA  . PHE   A 156 ? 1.8438 1.4429 1.8619 -0.3022 -0.0282 0.1470  176 PHE   A CA  
1176 C  C   . PHE   A 156 ? 1.7790 1.3866 1.7813 -0.2938 -0.0392 0.1165  176 PHE   A C   
1177 O  O   . PHE   A 156 ? 1.6710 1.2319 1.6329 -0.2664 -0.0366 0.0970  176 PHE   A O   
1178 C  CB  . PHE   A 156 ? 1.6476 1.3233 1.6916 -0.2841 -0.0082 0.1661  176 PHE   A CB  
1179 C  CG  . PHE   A 156 ? 1.6408 1.3035 1.6879 -0.2826 0.0041  0.1958  176 PHE   A CG  
1180 C  CD1 . PHE   A 156 ? 1.7615 1.3401 1.7803 -0.2785 0.0026  0.2008  176 PHE   A CD1 
1181 C  CD2 . PHE   A 156 ? 1.5245 1.2552 1.5978 -0.2829 0.0170  0.2188  176 PHE   A CD2 
1182 C  CE1 . PHE   A 156 ? 1.7890 1.3530 1.8075 -0.2754 0.0129  0.2301  176 PHE   A CE1 
1183 C  CE2 . PHE   A 156 ? 1.4191 1.1354 1.4881 -0.2799 0.0275  0.2473  176 PHE   A CE2 
1184 C  CZ  . PHE   A 156 ? 1.5355 1.1689 1.5781 -0.2764 0.0250  0.2540  176 PHE   A CZ  
1185 N  N   . GLY   A 157 ? 1.7906 1.4589 1.8239 -0.3149 -0.0503 0.1134  177 GLY   A N   
1186 C  CA  . GLY   A 157 ? 1.8142 1.4912 1.8308 -0.3067 -0.0626 0.0868  177 GLY   A CA  
1187 C  C   . GLY   A 157 ? 1.8864 1.4774 1.8569 -0.3135 -0.0840 0.0628  177 GLY   A C   
1188 O  O   . GLY   A 157 ? 1.8663 1.4289 1.7946 -0.2894 -0.0849 0.0400  177 GLY   A O   
1189 N  N   . ALA   A 158 ? 1.9476 1.4932 1.9232 -0.3468 -0.1013 0.0677  178 ALA   A N   
1190 C  CA  . ALA   A 158 ? 1.9077 1.3566 1.8320 -0.3525 -0.1228 0.0440  178 ALA   A CA  
1191 C  C   . ALA   A 158 ? 1.9478 1.3266 1.8170 -0.3124 -0.1042 0.0346  178 ALA   A C   
1192 O  O   . ALA   A 158 ? 2.0649 1.3863 1.8787 -0.2938 -0.1111 0.0077  178 ALA   A O   
1193 C  CB  . ALA   A 158 ? 2.0002 1.4088 1.9444 -0.3962 -0.1423 0.0551  178 ALA   A CB  
1194 N  N   . TYR   A 159 ? 1.8979 1.2815 1.7806 -0.2967 -0.0802 0.0573  179 TYR   A N   
1195 C  CA  . TYR   A 159 ? 2.0034 1.3381 1.8460 -0.2542 -0.0598 0.0515  179 TYR   A CA  
1196 C  C   . TYR   A 159 ? 1.8855 1.2661 1.7192 -0.2200 -0.0441 0.0389  179 TYR   A C   
1197 O  O   . TYR   A 159 ? 1.9077 1.2383 1.6930 -0.1925 -0.0386 0.0179  179 TYR   A O   
1198 C  CB  . TYR   A 159 ? 1.9871 1.3299 1.8536 -0.2451 -0.0407 0.0813  179 TYR   A CB  
1199 C  CG  . TYR   A 159 ? 2.0822 1.4118 1.9295 -0.1977 -0.0166 0.0812  179 TYR   A CG  
1200 C  CD1 . TYR   A 159 ? 2.1587 1.4184 1.9547 -0.1687 -0.0122 0.0578  179 TYR   A CD1 
1201 C  CD2 . TYR   A 159 ? 2.1277 1.5199 2.0094 -0.1806 0.0018  0.1038  179 TYR   A CD2 
1202 C  CE1 . TYR   A 159 ? 2.2522 1.5090 2.0401 -0.1248 0.0119  0.0597  179 TYR   A CE1 
1203 C  CE2 . TYR   A 159 ? 2.1297 1.5182 2.0034 -0.1390 0.0211  0.1045  179 TYR   A CE2 
1204 C  CZ  . TYR   A 159 ? 2.1252 1.4491 1.9563 -0.1114 0.0273  0.0835  179 TYR   A CZ  
1205 O  OH  . TYR   A 159 ? 1.9193 1.2472 1.7514 -0.0693 0.0486  0.0864  179 TYR   A OH  
1206 N  N   . SER   A 160 ? 2.0317 1.5053 1.9104 -0.2210 -0.0355 0.0522  180 SER   A N   
1207 C  CA  . SER   A 160 ? 1.9678 1.4865 1.8442 -0.1909 -0.0199 0.0440  180 SER   A CA  
1208 C  C   . SER   A 160 ? 1.9495 1.4394 1.7831 -0.1862 -0.0315 0.0162  180 SER   A C   
1209 O  O   . SER   A 160 ? 1.8492 1.3246 1.6523 -0.1541 -0.0156 0.0045  180 SER   A O   
1210 C  CB  . SER   A 160 ? 1.7648 1.3807 1.6932 -0.1989 -0.0152 0.0598  180 SER   A CB  
1211 O  OG  . SER   A 160 ? 1.8670 1.5061 1.8297 -0.2143 -0.0119 0.0851  180 SER   A OG  
1212 N  N   . MET   A 161 ? 1.9210 1.4039 1.7528 -0.2180 -0.0596 0.0066  181 MET   A N   
1213 C  CA  . MET   A 161 ? 1.9355 1.3846 1.7192 -0.2138 -0.0755 -0.0203 181 MET   A CA  
1214 C  C   . MET   A 161 ? 2.0633 1.4097 1.7787 -0.1948 -0.0742 -0.0396 181 MET   A C   
1215 O  O   . MET   A 161 ? 2.0138 1.3311 1.6784 -0.1673 -0.0664 -0.0580 181 MET   A O   
1216 C  CB  . MET   A 161 ? 1.9356 1.4011 1.7374 -0.2533 -0.1106 -0.0259 181 MET   A CB  
1217 C  CG  . MET   A 161 ? 1.9735 1.4167 1.7281 -0.2485 -0.1312 -0.0521 181 MET   A CG  
1218 S  SD  . MET   A 161 ? 2.0021 1.5068 1.7529 -0.2135 -0.1083 -0.0527 181 MET   A SD  
1219 C  CE  . MET   A 161 ? 2.0211 1.5403 1.7577 -0.2317 -0.1470 -0.0704 181 MET   A CE  
1220 N  N   . ASP   A 162 ? 2.1528 1.4407 1.8636 -0.2075 -0.0801 -0.0348 182 ASP   A N   
1221 C  CA  . ASP   A 162 ? 2.2200 1.4033 1.8640 -0.1873 -0.0784 -0.0535 182 ASP   A CA  
1222 C  C   . ASP   A 162 ? 2.2145 1.3923 1.8360 -0.1378 -0.0418 -0.0539 182 ASP   A C   
1223 O  O   . ASP   A 162 ? 2.2558 1.3634 1.8124 -0.1111 -0.0354 -0.0754 182 ASP   A O   
1224 C  CB  . ASP   A 162 ? 2.2562 1.3823 1.9075 -0.2080 -0.0876 -0.0430 182 ASP   A CB  
1225 C  CG  . ASP   A 162 ? 2.3337 1.4280 1.9852 -0.2548 -0.1272 -0.0521 182 ASP   A CG  
1226 O  OD1 . ASP   A 162 ? 2.3848 1.4924 2.0217 -0.2666 -0.1496 -0.0706 182 ASP   A OD1 
1227 O  OD2 . ASP   A 162 ? 2.4438 1.5003 2.1118 -0.2803 -0.1369 -0.0395 182 ASP   A OD2 
1228 N  N   . VAL   A 163 ? 2.1569 1.4078 1.8309 -0.1244 -0.0176 -0.0306 183 VAL   A N   
1229 C  CA  . VAL   A 163 ? 2.1901 1.4428 1.8534 -0.0796 0.0159  -0.0292 183 VAL   A CA  
1230 C  C   . VAL   A 163 ? 2.2426 1.5290 1.8879 -0.0627 0.0259  -0.0415 183 VAL   A C   
1231 O  O   . VAL   A 163 ? 2.3885 1.6329 1.9862 -0.0299 0.0447  -0.0552 183 VAL   A O   
1232 C  CB  . VAL   A 163 ? 2.0667 1.3788 1.7908 -0.0711 0.0343  -0.0006 183 VAL   A CB  
1233 C  CG1 . VAL   A 163 ? 2.1036 1.5167 1.8789 -0.0769 0.0394  0.0118  183 VAL   A CG1 
1234 C  CG2 . VAL   A 163 ? 2.0223 1.3028 1.7328 -0.0278 0.0625  0.0013  183 VAL   A CG2 
1235 N  N   . ILE   A 164 ? 2.1560 1.5127 1.8343 -0.0843 0.0134  -0.0370 184 ILE   A N   
1236 C  CA  . ILE   A 164 ? 2.0765 1.4703 1.7441 -0.0670 0.0253  -0.0435 184 ILE   A CA  
1237 C  C   . ILE   A 164 ? 2.2104 1.5376 1.8014 -0.0603 0.0138  -0.0702 184 ILE   A C   
1238 O  O   . ILE   A 164 ? 2.3118 1.6328 1.8680 -0.0321 0.0341  -0.0775 184 ILE   A O   
1239 C  CB  . ILE   A 164 ? 1.8941 1.3770 1.6164 -0.0892 0.0147  -0.0313 184 ILE   A CB  
1240 C  CG1 . ILE   A 164 ? 1.8473 1.3812 1.5817 -0.0652 0.0384  -0.0266 184 ILE   A CG1 
1241 C  CG2 . ILE   A 164 ? 1.9013 1.3802 1.6094 -0.1191 -0.0197 -0.0440 184 ILE   A CG2 
1242 C  CD1 . ILE   A 164 ? 1.9594 1.5000 1.7121 -0.0352 0.0710  -0.0148 184 ILE   A CD1 
1243 N  N   . THR   A 165 ? 2.3012 1.5746 1.8626 -0.0860 -0.0188 -0.0846 185 THR   A N   
1244 C  CA  . THR   A 165 ? 2.3415 1.5469 1.8238 -0.0809 -0.0358 -0.1122 185 THR   A CA  
1245 C  C   . THR   A 165 ? 2.4502 1.5681 1.8633 -0.0444 -0.0136 -0.1270 185 THR   A C   
1246 O  O   . THR   A 165 ? 2.5222 1.5917 1.8620 -0.0239 -0.0117 -0.1474 185 THR   A O   
1247 C  CB  . THR   A 165 ? 2.3441 1.5197 1.8214 -0.1221 -0.0815 -0.1236 185 THR   A CB  
1248 O  OG1 . THR   A 165 ? 2.2801 1.5401 1.8388 -0.1550 -0.0941 -0.1029 185 THR   A OG1 
1249 C  CG2 . THR   A 165 ? 2.4052 1.5476 1.8188 -0.1238 -0.1082 -0.1486 185 THR   A CG2 
1250 N  N   . SER   A 166 ? 2.6396 1.7350 2.0718 -0.0333 0.0040  -0.1166 186 SER   A N   
1251 C  CA  . SER   A 166 ? 2.7860 1.8012 2.1596 0.0052  0.0281  -0.1288 186 SER   A CA  
1252 C  C   . SER   A 166 ? 2.7221 1.7817 2.1226 0.0453  0.0745  -0.1127 186 SER   A C   
1253 O  O   . SER   A 166 ? 2.7621 1.7755 2.1082 0.0837  0.1013  -0.1244 186 SER   A O   
1254 C  CB  . SER   A 166 ? 2.9684 1.9186 2.3413 -0.0048 0.0164  -0.1284 186 SER   A CB  
1255 O  OG  . SER   A 166 ? 2.9831 1.9979 2.4386 -0.0263 0.0154  -0.1002 186 SER   A OG  
1256 N  N   . THR   A 167 ? 2.6018 1.7499 2.0853 0.0375  0.0845  -0.0863 187 THR   A N   
1257 C  CA  . THR   A 167 ? 2.5780 1.7756 2.0976 0.0712  0.1241  -0.0700 187 THR   A CA  
1258 C  C   . THR   A 167 ? 2.6386 1.8615 2.1346 0.0896  0.1439  -0.0752 187 THR   A C   
1259 O  O   . THR   A 167 ? 2.6625 1.9091 2.1738 0.1219  0.1805  -0.0658 187 THR   A O   
1260 C  CB  . THR   A 167 ? 2.4638 1.7497 2.0724 0.0546  0.1231  -0.0431 187 THR   A CB  
1261 O  OG1 . THR   A 167 ? 2.4333 1.7643 2.0647 0.0163  0.0944  -0.0415 187 THR   A OG1 
1262 C  CG2 . THR   A 167 ? 2.4584 1.7179 2.0892 0.0525  0.1186  -0.0320 187 THR   A CG2 
1263 N  N   . SER   A 168 ? 2.5297 1.7490 1.9912 0.0697  0.1204  -0.0884 188 SER   A N   
1264 C  CA  . SER   A 168 ? 2.5015 1.7474 1.9414 0.0832  0.1357  -0.0901 188 SER   A CA  
1265 C  C   . SER   A 168 ? 2.5102 1.6795 1.8512 0.0924  0.1256  -0.1162 188 SER   A C   
1266 O  O   . SER   A 168 ? 2.5151 1.6835 1.8187 0.1171  0.1502  -0.1177 188 SER   A O   
1267 C  CB  . SER   A 168 ? 2.3681 1.6974 1.8647 0.0538  0.1172  -0.0775 188 SER   A CB  
1268 O  OG  . SER   A 168 ? 2.2427 1.6411 1.8234 0.0469  0.1258  -0.0548 188 SER   A OG  
1269 N  N   . PHE   A 169 ? 2.5899 1.6935 1.8862 0.0728  0.0897  -0.1361 189 PHE   A N   
1270 C  CA  . PHE   A 169 ? 2.5236 1.5502 1.7211 0.0789  0.0720  -0.1635 189 PHE   A CA  
1271 C  C   . PHE   A 169 ? 2.6405 1.5626 1.7745 0.0898  0.0655  -0.1849 189 PHE   A C   
1272 O  O   . PHE   A 169 ? 2.7653 1.6180 1.8177 0.1259  0.0871  -0.2014 189 PHE   A O   
1273 C  CB  . PHE   A 169 ? 2.4555 1.5033 1.6557 0.0397  0.0238  -0.1708 189 PHE   A CB  
1274 C  CG  . PHE   A 169 ? 2.3104 1.4610 1.5810 0.0261  0.0259  -0.1493 189 PHE   A CG  
1275 C  CD1 . PHE   A 169 ? 2.2258 1.4532 1.5923 0.0081  0.0301  -0.1260 189 PHE   A CD1 
1276 C  CD2 . PHE   A 169 ? 2.3293 1.4940 1.5640 0.0333  0.0231  -0.1528 189 PHE   A CD2 
1277 C  CE1 . PHE   A 169 ? 2.1692 1.4833 1.5936 -0.0020 0.0317  -0.1089 189 PHE   A CE1 
1278 C  CE2 . PHE   A 169 ? 2.2692 1.5207 1.5650 0.0229  0.0248  -0.1340 189 PHE   A CE2 
1279 C  CZ  . PHE   A 169 ? 2.1267 1.4519 1.5171 0.0054  0.0291  -0.1132 189 PHE   A CZ  
1280 N  N   . GLY   A 170 ? 2.6464 1.5535 1.8147 0.0598  0.0374  -0.1844 190 GLY   A N   
1281 C  CA  . GLY   A 170 ? 2.6917 1.4994 1.8101 0.0693  0.0325  -0.2014 190 GLY   A CA  
1282 C  C   . GLY   A 170 ? 2.8208 1.5626 1.9027 0.0318  -0.0207 -0.2233 190 GLY   A C   
1283 O  O   . GLY   A 170 ? 3.0353 1.6714 2.0406 0.0434  -0.0302 -0.2479 190 GLY   A O   
1284 N  N   . VAL   A 171 ? 2.7617 1.5637 1.8994 -0.0132 -0.0559 -0.2148 191 VAL   A N   
1285 C  CA  . VAL   A 171 ? 2.9716 1.7260 2.0910 -0.0549 -0.1093 -0.2325 191 VAL   A CA  
1286 C  C   . VAL   A 171 ? 3.0034 1.7670 2.1937 -0.0870 -0.1201 -0.2147 191 VAL   A C   
1287 O  O   . VAL   A 171 ? 2.8473 1.7037 2.1264 -0.1035 -0.1107 -0.1860 191 VAL   A O   
1288 C  CB  . VAL   A 171 ? 2.8078 1.6243 1.9458 -0.0834 -0.1422 -0.2337 191 VAL   A CB  
1289 C  CG1 . VAL   A 171 ? 2.8658 1.6462 2.0041 -0.1309 -0.1992 -0.2483 191 VAL   A CG1 
1290 C  CG2 . VAL   A 171 ? 2.8062 1.6013 1.8624 -0.0507 -0.1334 -0.2509 191 VAL   A CG2 
1291 N  N   . ASN   A 172 ? 3.3263 1.9893 2.4732 -0.0955 -0.1399 -0.2316 192 ASN   A N   
1292 C  CA  . ASN   A 172 ? 3.3777 2.0318 2.5806 -0.1241 -0.1487 -0.2144 192 ASN   A CA  
1293 C  C   . ASN   A 172 ? 3.3553 2.0185 2.5923 -0.1831 -0.1998 -0.2163 192 ASN   A C   
1294 O  O   . ASN   A 172 ? 3.4209 2.0167 2.5991 -0.1987 -0.2383 -0.2451 192 ASN   A O   
1295 C  CB  . ASN   A 172 ? 3.5422 2.0774 2.6825 -0.0997 -0.1399 -0.2292 192 ASN   A CB  
1296 C  CG  . ASN   A 172 ? 3.6992 2.1202 2.7320 -0.0938 -0.1680 -0.2704 192 ASN   A CG  
1297 O  OD1 . ASN   A 172 ? 3.7762 2.1678 2.7357 -0.0526 -0.1488 -0.2894 192 ASN   A OD1 
1298 N  ND2 . ASN   A 172 ? 3.7517 2.1059 2.7732 -0.1355 -0.2140 -0.2840 192 ASN   A ND2 
1299 N  N   . ILE   A 173 ? 3.0897 1.8367 2.4218 -0.2152 -0.2002 -0.1853 193 ILE   A N   
1300 C  CA  . ILE   A 173 ? 2.9671 1.7441 2.3508 -0.2720 -0.2425 -0.1803 193 ILE   A CA  
1301 C  C   . ILE   A 173 ? 2.9002 1.7173 2.3654 -0.2977 -0.2318 -0.1457 193 ILE   A C   
1302 O  O   . ILE   A 173 ? 2.7323 1.6211 2.2442 -0.2789 -0.1962 -0.1196 193 ILE   A O   
1303 C  CB  . ILE   A 173 ? 2.8365 1.7117 2.2549 -0.2838 -0.2554 -0.1782 193 ILE   A CB  
1304 C  CG1 . ILE   A 173 ? 2.8293 1.6503 2.1649 -0.2750 -0.2845 -0.2138 193 ILE   A CG1 
1305 C  CG2 . ILE   A 173 ? 2.7833 1.7299 2.2911 -0.3374 -0.2819 -0.1579 193 ILE   A CG2 
1306 C  CD1 . ILE   A 173 ? 2.7504 1.6608 2.1075 -0.2743 -0.2916 -0.2117 193 ILE   A CD1 
1307 N  N   . ASP   A 174 ? 2.9578 1.7262 2.4380 -0.3410 -0.2632 -0.1449 194 ASP   A N   
1308 C  CA  . ASP   A 174 ? 2.9449 1.7566 2.5053 -0.3736 -0.2572 -0.1094 194 ASP   A CA  
1309 C  C   . ASP   A 174 ? 2.8322 1.7667 2.4735 -0.4048 -0.2660 -0.0909 194 ASP   A C   
1310 O  O   . ASP   A 174 ? 2.8779 1.8220 2.5388 -0.4444 -0.3046 -0.1000 194 ASP   A O   
1311 C  CB  . ASP   A 174 ? 2.9703 1.6855 2.5199 -0.4118 -0.2877 -0.1139 194 ASP   A CB  
1312 C  CG  . ASP   A 174 ? 2.8894 1.6468 2.5204 -0.4490 -0.2811 -0.0742 194 ASP   A CG  
1313 O  OD1 . ASP   A 174 ? 2.8340 1.6808 2.5166 -0.4358 -0.2480 -0.0443 194 ASP   A OD1 
1314 O  OD2 . ASP   A 174 ? 2.9307 1.6319 2.5731 -0.4911 -0.3088 -0.0726 194 ASP   A OD2 
1315 N  N   . SER   A 175 ? 2.7158 1.7452 2.4058 -0.3863 -0.2315 -0.0651 195 SER   A N   
1316 C  CA  . SER   A 175 ? 2.5666 1.7128 2.3268 -0.4070 -0.2353 -0.0495 195 SER   A CA  
1317 C  C   . SER   A 175 ? 2.6420 1.8268 2.4778 -0.4571 -0.2470 -0.0222 195 SER   A C   
1318 O  O   . SER   A 175 ? 2.4933 1.7695 2.3922 -0.4618 -0.2258 0.0066  195 SER   A O   
1319 C  CB  . SER   A 175 ? 2.4390 1.6674 2.2212 -0.3700 -0.1958 -0.0332 195 SER   A CB  
1320 O  OG  . SER   A 175 ? 2.4085 1.6265 2.1363 -0.3317 -0.1884 -0.0564 195 SER   A OG  
1321 N  N   . LEU   A 176 ? 2.7460 1.8591 2.5744 -0.4948 -0.2799 -0.0308 196 LEU   A N   
1322 C  CA  . LEU   A 176 ? 2.7212 1.8777 2.6256 -0.5501 -0.3001 -0.0098 196 LEU   A CA  
1323 C  C   . LEU   A 176 ? 2.8437 1.9889 2.7501 -0.5847 -0.3503 -0.0347 196 LEU   A C   
1324 O  O   . LEU   A 176 ? 2.7710 1.9777 2.7525 -0.6258 -0.3659 -0.0187 196 LEU   A O   
1325 C  CB  . LEU   A 176 ? 2.7366 1.8259 2.6503 -0.5743 -0.2953 0.0112  196 LEU   A CB  
1326 C  CG  . LEU   A 176 ? 2.5948 1.7616 2.6016 -0.6186 -0.2901 0.0499  196 LEU   A CG  
1327 C  CD1 . LEU   A 176 ? 2.4175 1.6802 2.4624 -0.5944 -0.2468 0.0810  196 LEU   A CD1 
1328 C  CD2 . LEU   A 176 ? 2.4340 1.5386 2.4468 -0.6367 -0.2877 0.0628  196 LEU   A CD2 
1329 N  N   . ASP   A 197 ? 1.9954 2.6524 2.4152 -0.1488 -0.0215 0.0911  217 ASP   A N   
1330 C  CA  . ASP   A 197 ? 2.0546 2.7380 2.4722 -0.1162 -0.0141 0.0842  217 ASP   A CA  
1331 C  C   . ASP   A 197 ? 2.1460 2.8894 2.6114 -0.1104 -0.0265 0.0855  217 ASP   A C   
1332 O  O   . ASP   A 197 ? 2.1743 2.9791 2.6782 -0.1020 -0.0103 0.0954  217 ASP   A O   
1333 C  CB  . ASP   A 197 ? 1.9962 2.7010 2.4098 -0.1029 0.0149  0.0922  217 ASP   A CB  
1334 C  CG  . ASP   A 197 ? 1.9656 2.6725 2.3580 -0.0675 0.0220  0.0805  217 ASP   A CG  
1335 O  OD1 . ASP   A 197 ? 1.9908 2.7295 2.4039 -0.0508 0.0147  0.0756  217 ASP   A OD1 
1336 O  OD2 . ASP   A 197 ? 1.9930 2.6677 2.3480 -0.0563 0.0333  0.0760  217 ASP   A OD2 
1337 N  N   . PRO   A 198 ? 2.2436 2.9710 2.7067 -0.1137 -0.0552 0.0763  218 PRO   A N   
1338 C  CA  . PRO   A 198 ? 2.2698 3.0556 2.7801 -0.1057 -0.0711 0.0775  218 PRO   A CA  
1339 C  C   . PRO   A 198 ? 2.3425 3.1088 2.8251 -0.0759 -0.0864 0.0640  218 PRO   A C   
1340 O  O   . PRO   A 198 ? 2.3207 3.1364 2.8346 -0.0535 -0.0882 0.0649  218 PRO   A O   
1341 C  CB  . PRO   A 198 ? 2.2619 3.0493 2.7990 -0.1408 -0.0977 0.0809  218 PRO   A CB  
1342 C  CG  . PRO   A 198 ? 2.2573 2.9602 2.7346 -0.1560 -0.1021 0.0728  218 PRO   A CG  
1343 C  CD  . PRO   A 198 ? 2.2247 2.8913 2.6558 -0.1345 -0.0756 0.0693  218 PRO   A CD  
1344 N  N   . PHE   A 199 ? 2.6716 3.3658 3.0960 -0.0741 -0.0962 0.0528  219 PHE   A N   
1345 C  CA  . PHE   A 199 ? 2.6863 3.3501 3.0777 -0.0516 -0.1140 0.0422  219 PHE   A CA  
1346 C  C   . PHE   A 199 ? 2.7007 3.3072 3.0372 -0.0321 -0.0980 0.0348  219 PHE   A C   
1347 O  O   . PHE   A 199 ? 2.6955 3.2921 3.0153 -0.0057 -0.1014 0.0297  219 PHE   A O   
1348 C  CB  . PHE   A 199 ? 2.7383 3.3686 3.1114 -0.0705 -0.1454 0.0370  219 PHE   A CB  
1349 C  CG  . PHE   A 199 ? 2.8008 3.3616 3.1079 -0.0555 -0.1542 0.0268  219 PHE   A CG  
1350 C  CD1 . PHE   A 199 ? 2.8095 3.3708 3.1053 -0.0318 -0.1726 0.0233  219 PHE   A CD1 
1351 C  CD2 . PHE   A 199 ? 2.7327 3.2283 2.9900 -0.0641 -0.1431 0.0226  219 PHE   A CD2 
1352 C  CE1 . PHE   A 199 ? 2.8307 3.3261 3.0630 -0.0184 -0.1781 0.0170  219 PHE   A CE1 
1353 C  CE2 . PHE   A 199 ? 2.7348 3.1697 2.9338 -0.0502 -0.1469 0.0158  219 PHE   A CE2 
1354 C  CZ  . PHE   A 199 ? 2.7351 3.1686 2.9197 -0.0282 -0.1637 0.0136  219 PHE   A CZ  
1355 N  N   . PHE   A 200 ? 2.4447 3.0141 2.7562 -0.0446 -0.0812 0.0350  220 PHE   A N   
1356 C  CA  . PHE   A 200 ? 2.3832 2.9056 2.6531 -0.0288 -0.0664 0.0293  220 PHE   A CA  
1357 C  C   . PHE   A 200 ? 2.2881 2.8375 2.5687 -0.0048 -0.0505 0.0283  220 PHE   A C   
1358 O  O   . PHE   A 200 ? 2.1130 2.6256 2.3631 0.0110  -0.0435 0.0221  220 PHE   A O   
1359 C  CB  . PHE   A 200 ? 2.2858 2.7715 2.5356 -0.0470 -0.0537 0.0310  220 PHE   A CB  
1360 C  CG  . PHE   A 200 ? 2.3636 2.8297 2.6095 -0.0726 -0.0666 0.0325  220 PHE   A CG  
1361 C  CD1 . PHE   A 200 ? 2.3333 2.8354 2.6164 -0.0949 -0.0707 0.0403  220 PHE   A CD1 
1362 C  CD2 . PHE   A 200 ? 2.3219 2.7295 2.5242 -0.0736 -0.0746 0.0258  220 PHE   A CD2 
1363 C  CE1 . PHE   A 200 ? 2.2793 2.7543 2.5550 -0.1189 -0.0851 0.0396  220 PHE   A CE1 
1364 C  CE2 . PHE   A 200 ? 2.2755 2.6564 2.4657 -0.0944 -0.0873 0.0242  220 PHE   A CE2 
1365 C  CZ  . PHE   A 200 ? 2.2819 2.6944 2.5085 -0.1176 -0.0943 0.0302  220 PHE   A CZ  
1366 N  N   . LEU   A 201 ? 2.2661 2.8779 2.5893 -0.0016 -0.0442 0.0344  221 LEU   A N   
1367 C  CA  . LEU   A 201 ? 2.1723 2.8101 2.5021 0.0264  -0.0302 0.0316  221 LEU   A CA  
1368 C  C   . LEU   A 201 ? 2.0708 2.6891 2.3838 0.0536  -0.0423 0.0233  221 LEU   A C   
1369 O  O   . LEU   A 201 ? 1.9695 2.5663 2.2603 0.0758  -0.0330 0.0160  221 LEU   A O   
1370 C  CB  . LEU   A 201 ? 2.1834 2.8969 2.5655 0.0262  -0.0206 0.0416  221 LEU   A CB  
1371 C  CG  . LEU   A 201 ? 2.1701 2.9388 2.6052 0.0143  -0.0367 0.0502  221 LEU   A CG  
1372 C  CD1 . LEU   A 201 ? 2.1984 2.9721 2.6400 0.0327  -0.0612 0.0448  221 LEU   A CD1 
1373 C  CD2 . LEU   A 201 ? 2.1397 2.9850 2.6285 0.0136  -0.0168 0.0632  221 LEU   A CD2 
1374 N  N   . SER   A 202 ? 2.0895 2.7084 2.4083 0.0519  -0.0651 0.0241  222 SER   A N   
1375 C  CA  . SER   A 202 ? 2.0748 2.6706 2.3736 0.0784  -0.0779 0.0187  222 SER   A CA  
1376 C  C   . SER   A 202 ? 2.1298 2.6484 2.3732 0.0796  -0.0774 0.0134  222 SER   A C   
1377 O  O   . SER   A 202 ? 2.1325 2.6235 2.3544 0.1035  -0.0788 0.0094  222 SER   A O   
1378 C  CB  . SER   A 202 ? 2.1936 2.8146 2.5132 0.0775  -0.1054 0.0223  222 SER   A CB  
1379 O  OG  . SER   A 202 ? 2.1255 2.8235 2.5063 0.0729  -0.1068 0.0293  222 SER   A OG  
1380 N  N   . ILE   A 203 ? 1.9727 2.4551 2.1939 0.0552  -0.0747 0.0142  223 ILE   A N   
1381 C  CA  . ILE   A 203 ? 1.9040 2.3186 2.0781 0.0568  -0.0724 0.0117  223 ILE   A CA  
1382 C  C   . ILE   A 203 ? 1.9185 2.3104 2.0805 0.0725  -0.0572 0.0071  223 ILE   A C   
1383 O  O   . ILE   A 203 ? 1.9495 2.2955 2.0823 0.0841  -0.0583 0.0060  223 ILE   A O   
1384 C  CB  . ILE   A 203 ? 1.9383 2.3217 2.0943 0.0309  -0.0677 0.0134  223 ILE   A CB  
1385 C  CG1 . ILE   A 203 ? 2.0457 2.4338 2.2014 0.0149  -0.0867 0.0150  223 ILE   A CG1 
1386 C  CG2 . ILE   A 203 ? 1.9521 2.2741 2.0685 0.0342  -0.0577 0.0126  223 ILE   A CG2 
1387 C  CD1 . ILE   A 203 ? 2.1946 2.5716 2.3494 -0.0118 -0.0806 0.0163  223 ILE   A CD1 
1388 N  N   . THR   A 204 ? 1.9060 2.3263 2.0875 0.0729  -0.0436 0.0047  224 THR   A N   
1389 C  CA  . THR   A 204 ? 1.8172 2.2083 1.9821 0.0840  -0.0328 -0.0019 224 THR   A CA  
1390 C  C   . THR   A 204 ? 1.8057 2.2005 1.9699 0.1142  -0.0352 -0.0083 224 THR   A C   
1391 O  O   . THR   A 204 ? 1.7067 2.0567 1.8477 0.1247  -0.0339 -0.0140 224 THR   A O   
1392 C  CB  . THR   A 204 ? 1.5905 2.0001 1.7652 0.0729  -0.0190 -0.0029 224 THR   A CB  
1393 O  OG1 . THR   A 204 ? 1.5877 2.0472 1.7838 0.0870  -0.0131 -0.0044 224 THR   A OG1 
1394 C  CG2 . THR   A 204 ? 1.6682 2.0847 1.8508 0.0458  -0.0178 0.0050  224 THR   A CG2 
1395 N  N   . VAL   A 205 ? 1.7606 2.2071 1.9519 0.1287  -0.0385 -0.0071 225 VAL   A N   
1396 C  CA  . VAL   A 205 ? 1.8424 2.2897 2.0321 0.1617  -0.0419 -0.0127 225 VAL   A CA  
1397 C  C   . VAL   A 205 ? 1.9626 2.3841 2.1392 0.1719  -0.0599 -0.0086 225 VAL   A C   
1398 O  O   . VAL   A 205 ? 1.9787 2.3755 2.1411 0.1986  -0.0641 -0.0124 225 VAL   A O   
1399 C  CB  . VAL   A 205 ? 1.8008 2.3184 2.0285 0.1779  -0.0353 -0.0122 225 VAL   A CB  
1400 C  CG1 . VAL   A 205 ? 1.6662 2.1763 1.8849 0.2157  -0.0320 -0.0216 225 VAL   A CG1 
1401 C  CG2 . VAL   A 205 ? 1.5552 2.1043 1.7958 0.1609  -0.0179 -0.0106 225 VAL   A CG2 
1402 N  N   . PHE   A 206 ? 2.2752 2.6968 2.4515 0.1526  -0.0714 -0.0009 226 PHE   A N   
1403 C  CA  . PHE   A 206 ? 2.2648 2.6510 2.4155 0.1602  -0.0889 0.0038  226 PHE   A CA  
1404 C  C   . PHE   A 206 ? 2.3052 2.6380 2.4204 0.1371  -0.0863 0.0073  226 PHE   A C   
1405 O  O   . PHE   A 206 ? 2.3098 2.6418 2.4170 0.1233  -0.0978 0.0118  226 PHE   A O   
1406 C  CB  . PHE   A 206 ? 2.4042 2.8397 2.5823 0.1640  -0.1095 0.0088  226 PHE   A CB  
1407 C  CG  . PHE   A 206 ? 2.4773 2.9867 2.7076 0.1768  -0.1062 0.0080  226 PHE   A CG  
1408 C  CD1 . PHE   A 206 ? 2.5186 3.0358 2.7549 0.2098  -0.0994 0.0033  226 PHE   A CD1 
1409 C  CD2 . PHE   A 206 ? 2.4686 3.0382 2.7419 0.1565  -0.1086 0.0125  226 PHE   A CD2 
1410 C  CE1 . PHE   A 206 ? 2.4846 3.0721 2.7684 0.2247  -0.0920 0.0033  226 PHE   A CE1 
1411 C  CE2 . PHE   A 206 ? 2.4307 3.0727 2.7561 0.1679  -0.1014 0.0146  226 PHE   A CE2 
1412 C  CZ  . PHE   A 206 ? 2.4331 3.0860 2.7635 0.2034  -0.0918 0.0101  226 PHE   A CZ  
1413 N  N   . PRO   A 207 ? 2.1204 2.4070 2.2140 0.1330  -0.0716 0.0052  227 PRO   A N   
1414 C  CA  . PRO   A 207 ? 2.0211 2.2570 2.0824 0.1163  -0.0668 0.0109  227 PRO   A CA  
1415 C  C   . PRO   A 207 ? 2.0395 2.2302 2.0639 0.1303  -0.0764 0.0180  227 PRO   A C   
1416 O  O   . PRO   A 207 ? 2.0302 2.1894 2.0248 0.1195  -0.0761 0.0244  227 PRO   A O   
1417 C  CB  . PRO   A 207 ? 1.9525 2.1630 2.0136 0.1087  -0.0494 0.0073  227 PRO   A CB  
1418 C  CG  . PRO   A 207 ? 1.9965 2.2207 2.0710 0.1299  -0.0498 -0.0013 227 PRO   A CG  
1419 C  CD  . PRO   A 207 ? 2.0688 2.3344 2.1583 0.1501  -0.0633 -0.0013 227 PRO   A CD  
1420 N  N   . PHE   A 208 ? 1.9833 2.1674 2.0053 0.1561  -0.0840 0.0175  228 PHE   A N   
1421 C  CA  . PHE   A 208 ? 1.9752 2.1218 1.9624 0.1735  -0.0968 0.0260  228 PHE   A CA  
1422 C  C   . PHE   A 208 ? 1.9869 2.1565 1.9676 0.1722  -0.1174 0.0298  228 PHE   A C   
1423 O  O   . PHE   A 208 ? 2.0022 2.1332 1.9417 0.1813  -0.1282 0.0382  228 PHE   A O   
1424 C  CB  . PHE   A 208 ? 1.9925 2.1373 1.9860 0.2044  -0.1033 0.0235  228 PHE   A CB  
1425 C  CG  . PHE   A 208 ? 2.0800 2.2944 2.1176 0.2183  -0.1114 0.0157  228 PHE   A CG  
1426 C  CD1 . PHE   A 208 ? 2.1063 2.3592 2.1573 0.2317  -0.1327 0.0195  228 PHE   A CD1 
1427 C  CD2 . PHE   A 208 ? 2.0079 2.2511 2.0743 0.2182  -0.0974 0.0053  228 PHE   A CD2 
1428 C  CE1 . PHE   A 208 ? 2.0540 2.3775 2.1538 0.2441  -0.1376 0.0148  228 PHE   A CE1 
1429 C  CE2 . PHE   A 208 ? 2.0432 2.3525 2.1498 0.2327  -0.1001 0.0004  228 PHE   A CE2 
1430 C  CZ  . PHE   A 208 ? 2.1039 2.4560 2.2312 0.2451  -0.1188 0.0059  228 PHE   A CZ  
1431 N  N   . LEU   A 209 ? 1.9939 2.2233 2.0125 0.1605  -0.1241 0.0243  229 LEU   A N   
1432 C  CA  . LEU   A 209 ? 1.9275 2.1807 1.9457 0.1552  -0.1477 0.0260  229 LEU   A CA  
1433 C  C   . LEU   A 209 ? 1.8698 2.0879 1.8522 0.1315  -0.1452 0.0274  229 LEU   A C   
1434 O  O   . LEU   A 209 ? 1.9769 2.1948 1.9413 0.1287  -0.1675 0.0280  229 LEU   A O   
1435 C  CB  . LEU   A 209 ? 1.9409 2.2726 2.0196 0.1490  -0.1552 0.0213  229 LEU   A CB  
1436 C  CG  . LEU   A 209 ? 2.0104 2.3919 2.1241 0.1752  -0.1737 0.0223  229 LEU   A CG  
1437 C  CD1 . LEU   A 209 ? 2.0153 2.4773 2.1922 0.1625  -0.1789 0.0208  229 LEU   A CD1 
1438 C  CD2 . LEU   A 209 ? 1.9849 2.3429 2.0662 0.1907  -0.2024 0.0280  229 LEU   A CD2 
1439 N  N   . ILE   A 210 ? 1.7796 1.9670 1.7501 0.1160  -0.1204 0.0273  230 ILE   A N   
1440 C  CA  . ILE   A 210 ? 1.7805 1.9448 1.7262 0.0943  -0.1156 0.0269  230 ILE   A CA  
1441 C  C   . ILE   A 210 ? 1.9431 2.0540 1.8264 0.1026  -0.1251 0.0327  230 ILE   A C   
1442 O  O   . ILE   A 210 ? 1.9111 2.0190 1.7736 0.0939  -0.1418 0.0293  230 ILE   A O   
1443 C  CB  . ILE   A 210 ? 1.7893 1.9358 1.7403 0.0794  -0.0865 0.0269  230 ILE   A CB  
1444 C  CG1 . ILE   A 210 ? 1.6855 1.8838 1.6859 0.0639  -0.0825 0.0206  230 ILE   A CG1 
1445 C  CG2 . ILE   A 210 ? 1.7827 1.8820 1.6903 0.0681  -0.0759 0.0301  230 ILE   A CG2 
1446 C  CD1 . ILE   A 210 ? 1.7165 1.9015 1.7231 0.0487  -0.0590 0.0205  230 ILE   A CD1 
1447 N  N   . PRO   A 211 ? 2.0612 2.1257 1.9095 0.1193  -0.1161 0.0418  231 PRO   A N   
1448 C  CA  . PRO   A 211 ? 2.0506 2.0649 1.8335 0.1302  -0.1262 0.0493  231 PRO   A CA  
1449 C  C   . PRO   A 211 ? 2.0103 2.0475 1.7874 0.1436  -0.1640 0.0470  231 PRO   A C   
1450 O  O   . PRO   A 211 ? 2.0264 2.0299 1.7484 0.1473  -0.1794 0.0489  231 PRO   A O   
1451 C  CB  . PRO   A 211 ? 2.0227 1.9901 1.7822 0.1453  -0.1076 0.0619  231 PRO   A CB  
1452 C  CG  . PRO   A 211 ? 1.9290 1.9342 1.7471 0.1481  -0.1030 0.0565  231 PRO   A CG  
1453 C  CD  . PRO   A 211 ? 1.9965 2.0368 1.8511 0.1241  -0.0921 0.0471  231 PRO   A CD  
1454 N  N   . ILE   A 212 ? 2.1005 2.1938 1.9316 0.1527  -0.1795 0.0431  232 ILE   A N   
1455 C  CA  . ILE   A 212 ? 2.1523 2.2830 1.9952 0.1625  -0.2173 0.0406  232 ILE   A CA  
1456 C  C   . ILE   A 212 ? 2.1754 2.3180 2.0135 0.1388  -0.2343 0.0323  232 ILE   A C   
1457 O  O   . ILE   A 212 ? 2.1781 2.2962 1.9704 0.1429  -0.2609 0.0319  232 ILE   A O   
1458 C  CB  . ILE   A 212 ? 2.2066 2.4080 2.1223 0.1725  -0.2240 0.0375  232 ILE   A CB  
1459 C  CG1 . ILE   A 212 ? 2.3178 2.5039 2.2298 0.2044  -0.2209 0.0444  232 ILE   A CG1 
1460 C  CG2 . ILE   A 212 ? 2.1890 2.4485 2.1395 0.1705  -0.2602 0.0336  232 ILE   A CG2 
1461 C  CD1 . ILE   A 212 ? 2.4165 2.6095 2.3166 0.2316  -0.2555 0.0501  232 ILE   A CD1 
1462 N  N   . LEU   A 213 ? 2.1581 2.3337 2.0394 0.1141  -0.2206 0.0252  233 LEU   A N   
1463 C  CA  . LEU   A 213 ? 2.1823 2.3649 2.0613 0.0900  -0.2372 0.0169  233 LEU   A CA  
1464 C  C   . LEU   A 213 ? 2.2971 2.4074 2.1025 0.0833  -0.2262 0.0155  233 LEU   A C   
1465 O  O   . LEU   A 213 ? 2.3923 2.4881 2.1711 0.0706  -0.2471 0.0076  233 LEU   A O   
1466 C  CB  . LEU   A 213 ? 2.0339 2.2685 1.9781 0.0659  -0.2249 0.0121  233 LEU   A CB  
1467 C  CG  . LEU   A 213 ? 1.8812 2.1863 1.8993 0.0714  -0.2194 0.0144  233 LEU   A CG  
1468 C  CD1 . LEU   A 213 ? 1.8226 2.1153 1.8453 0.0787  -0.1843 0.0171  233 LEU   A CD1 
1469 C  CD2 . LEU   A 213 ? 1.9455 2.3075 2.0214 0.0460  -0.2257 0.0111  233 LEU   A CD2 
1470 N  N   . GLU   A 214 ? 2.0959 2.1603 1.8684 0.0917  -0.1937 0.0229  234 GLU   A N   
1471 C  CA  . GLU   A 214 ? 2.0272 2.0253 1.7302 0.0893  -0.1783 0.0239  234 GLU   A CA  
1472 C  C   . GLU   A 214 ? 2.1019 2.0559 1.7315 0.1054  -0.2036 0.0255  234 GLU   A C   
1473 O  O   . GLU   A 214 ? 2.2216 2.1248 1.7883 0.1025  -0.1997 0.0221  234 GLU   A O   
1474 C  CB  . GLU   A 214 ? 2.0207 1.9862 1.7138 0.0948  -0.1378 0.0345  234 GLU   A CB  
1475 C  CG  . GLU   A 214 ? 2.0473 1.9901 1.7324 0.0785  -0.1083 0.0323  234 GLU   A CG  
1476 C  CD  . GLU   A 214 ? 2.1722 2.1151 1.8882 0.0767  -0.0731 0.0406  234 GLU   A CD  
1477 O  OE1 . GLU   A 214 ? 2.1755 2.1363 1.9264 0.0607  -0.0568 0.0365  234 GLU   A OE1 
1478 O  OE2 . GLU   A 214 ? 2.1675 2.0904 1.8727 0.0910  -0.0637 0.0516  234 GLU   A OE2 
1479 N  N   . VAL   A 215 ? 2.2792 2.2493 1.9115 0.1247  -0.2298 0.0305  235 VAL   A N   
1480 C  CA  . VAL   A 215 ? 2.3729 2.3043 1.9350 0.1414  -0.2601 0.0322  235 VAL   A CA  
1481 C  C   . VAL   A 215 ? 2.3955 2.3667 1.9784 0.1324  -0.3081 0.0197  235 VAL   A C   
1482 O  O   . VAL   A 215 ? 2.5075 2.4506 2.0335 0.1446  -0.3415 0.0184  235 VAL   A O   
1483 C  CB  . VAL   A 215 ? 2.2856 2.2003 1.8276 0.1713  -0.2629 0.0476  235 VAL   A CB  
1484 C  CG1 . VAL   A 215 ? 2.2001 2.0763 1.7298 0.1762  -0.2166 0.0609  235 VAL   A CG1 
1485 C  CG2 . VAL   A 215 ? 2.3646 2.3481 1.9793 0.1806  -0.2881 0.0468  235 VAL   A CG2 
1486 N  N   . LEU   A 216 ? 2.3970 2.4325 2.0599 0.1107  -0.3132 0.0113  236 LEU   A N   
1487 C  CA  . LEU   A 216 ? 2.4862 2.5661 2.1831 0.0961  -0.3570 0.0007  236 LEU   A CA  
1488 C  C   . LEU   A 216 ? 2.5792 2.6362 2.2578 0.0676  -0.3605 -0.0131 236 LEU   A C   
1489 O  O   . LEU   A 216 ? 2.6510 2.7429 2.3639 0.0488  -0.3956 -0.0226 236 LEU   A O   
1490 C  CB  . LEU   A 216 ? 2.4300 2.5995 2.2313 0.0902  -0.3605 0.0027  236 LEU   A CB  
1491 C  CG  . LEU   A 216 ? 2.3921 2.5916 2.2277 0.1172  -0.3485 0.0142  236 LEU   A CG  
1492 C  CD1 . LEU   A 216 ? 2.3057 2.5972 2.2406 0.1116  -0.3570 0.0139  236 LEU   A CD1 
1493 C  CD2 . LEU   A 216 ? 2.4605 2.6285 2.2429 0.1481  -0.3742 0.0214  236 LEU   A CD2 
1494 N  N   . ASN   A 217 ? 2.7768 2.7761 2.4054 0.0641  -0.3250 -0.0139 237 ASN   A N   
1495 C  CA  . ASN   A 217 ? 2.9174 2.8944 2.5359 0.0389  -0.3192 -0.0263 237 ASN   A CA  
1496 C  C   . ASN   A 217 ? 2.7766 2.8208 2.4888 0.0124  -0.3175 -0.0289 237 ASN   A C   
1497 O  O   . ASN   A 217 ? 2.6975 2.7357 2.4159 -0.0120 -0.3276 -0.0395 237 ASN   A O   
1498 C  CB  . ASN   A 217 ? 2.9530 2.8857 2.5054 0.0345  -0.3596 -0.0405 237 ASN   A CB  
1499 C  CG  . ASN   A 217 ? 3.1336 3.0161 2.6004 0.0636  -0.3746 -0.0361 237 ASN   A CG  
1500 O  OD1 . ASN   A 217 ? 3.1714 3.0230 2.6023 0.0851  -0.3416 -0.0228 237 ASN   A OD1 
1501 N  ND2 . ASN   A 217 ? 3.1272 2.9998 2.5603 0.0638  -0.4256 -0.0464 237 ASN   A ND2 
1502 N  N   . ILE   A 218 ? 2.4642 2.5686 2.2460 0.0178  -0.3043 -0.0189 238 ILE   A N   
1503 C  CA  . ILE   A 218 ? 2.2715 2.4386 2.1373 -0.0040 -0.2954 -0.0183 238 ILE   A CA  
1504 C  C   . ILE   A 218 ? 2.2652 2.4058 2.1256 -0.0133 -0.2535 -0.0172 238 ILE   A C   
1505 O  O   . ILE   A 218 ? 2.1853 2.2986 2.0213 0.0028  -0.2229 -0.0106 238 ILE   A O   
1506 C  CB  . ILE   A 218 ? 2.1248 2.3613 2.0583 0.0096  -0.2931 -0.0088 238 ILE   A CB  
1507 C  CG1 . ILE   A 218 ? 2.1100 2.3913 2.0722 0.0140  -0.3376 -0.0097 238 ILE   A CG1 
1508 C  CG2 . ILE   A 218 ? 2.0144 2.3035 2.0196 -0.0080 -0.2694 -0.0057 238 ILE   A CG2 
1509 C  CD1 . ILE   A 218 ? 1.9358 2.2964 1.9779 0.0244  -0.3346 -0.0014 238 ILE   A CD1 
1510 N  N   . CYS   A 219 ? 2.1967 2.3446 2.0817 -0.0397 -0.2533 -0.0227 239 CYS   A N   
1511 C  CA  . CYS   A 219 ? 2.1210 2.2503 2.0088 -0.0488 -0.2171 -0.0210 239 CYS   A CA  
1512 C  C   . CYS   A 219 ? 2.0501 2.2426 2.0167 -0.0680 -0.2106 -0.0161 239 CYS   A C   
1513 O  O   . CYS   A 219 ? 2.0655 2.3004 2.0751 -0.0846 -0.2364 -0.0174 239 CYS   A O   
1514 C  CB  . CYS   A 219 ? 2.1599 2.2237 1.9903 -0.0595 -0.2183 -0.0313 239 CYS   A CB  
1515 S  SG  . CYS   A 219 ? 2.1803 2.1625 1.9058 -0.0350 -0.2185 -0.0361 239 CYS   A SG  
1516 N  N   . VAL   A 220 ? 2.2218 2.4215 2.2077 -0.0658 -0.1762 -0.0095 240 VAL   A N   
1517 C  CA  . VAL   A 220 ? 2.1276 2.3722 2.1723 -0.0848 -0.1660 -0.0045 240 VAL   A CA  
1518 C  C   . VAL   A 220 ? 2.1932 2.4099 2.2290 -0.1103 -0.1747 -0.0098 240 VAL   A C   
1519 O  O   . VAL   A 220 ? 2.0768 2.3304 2.1615 -0.1318 -0.1777 -0.0052 240 VAL   A O   
1520 C  CB  . VAL   A 220 ? 2.0336 2.2825 2.0898 -0.0757 -0.1306 0.0023  240 VAL   A CB  
1521 C  CG1 . VAL   A 220 ? 1.9084 2.1743 1.9680 -0.0509 -0.1242 0.0056  240 VAL   A CG1 
1522 C  CG2 . VAL   A 220 ? 2.0064 2.1937 2.0162 -0.0746 -0.1110 0.0000  240 VAL   A CG2 
1523 N  N   . PHE   A 221 ? 2.1411 2.2897 2.1126 -0.1076 -0.1777 -0.0188 241 PHE   A N   
1524 C  CA  . PHE   A 221 ? 2.1862 2.2953 2.1377 -0.1287 -0.1900 -0.0271 241 PHE   A CA  
1525 C  C   . PHE   A 221 ? 2.3115 2.4169 2.2500 -0.1378 -0.2330 -0.0371 241 PHE   A C   
1526 O  O   . PHE   A 221 ? 2.3178 2.3828 2.1964 -0.1209 -0.2458 -0.0449 241 PHE   A O   
1527 C  CB  . PHE   A 221 ? 2.1781 2.2138 2.0637 -0.1171 -0.1690 -0.0329 241 PHE   A CB  
1528 C  CG  . PHE   A 221 ? 2.0775 2.1172 1.9686 -0.0997 -0.1309 -0.0231 241 PHE   A CG  
1529 C  CD1 . PHE   A 221 ? 2.0145 2.0779 1.9480 -0.1084 -0.1095 -0.0149 241 PHE   A CD1 
1530 C  CD2 . PHE   A 221 ? 2.0446 2.0641 1.8993 -0.0756 -0.1182 -0.0213 241 PHE   A CD2 
1531 C  CE1 . PHE   A 221 ? 1.9912 2.0594 1.9320 -0.0937 -0.0795 -0.0071 241 PHE   A CE1 
1532 C  CE2 . PHE   A 221 ? 2.0271 2.0514 1.8932 -0.0631 -0.0859 -0.0123 241 PHE   A CE2 
1533 C  CZ  . PHE   A 221 ? 2.0159 2.0655 1.9260 -0.0724 -0.0683 -0.0062 241 PHE   A CZ  
1534 N  N   . PRO   A 222 ? 2.4179 2.5643 2.4102 -0.1641 -0.2569 -0.0361 242 PRO   A N   
1535 C  CA  . PRO   A 222 ? 2.4886 2.6429 2.4806 -0.1739 -0.3029 -0.0449 242 PRO   A CA  
1536 C  C   . PRO   A 222 ? 2.5926 2.6622 2.4959 -0.1696 -0.3232 -0.0624 242 PRO   A C   
1537 O  O   . PRO   A 222 ? 2.5969 2.6083 2.4637 -0.1802 -0.3164 -0.0706 242 PRO   A O   
1538 C  CB  . PRO   A 222 ? 2.5253 2.7233 2.5888 -0.2099 -0.3177 -0.0401 242 PRO   A CB  
1539 C  CG  . PRO   A 222 ? 2.4910 2.6815 2.5697 -0.2180 -0.2794 -0.0311 242 PRO   A CG  
1540 C  CD  . PRO   A 222 ? 2.4138 2.6023 2.4713 -0.1870 -0.2429 -0.0253 242 PRO   A CD  
1541 N  N   . ARG   A 223 ? 2.6857 2.7461 2.5504 -0.1515 -0.3485 -0.0682 243 ARG   A N   
1542 C  CA  . ARG   A 223 ? 2.6944 2.6712 2.4593 -0.1377 -0.3620 -0.0833 243 ARG   A CA  
1543 C  C   . ARG   A 223 ? 2.6540 2.5810 2.3897 -0.1632 -0.3945 -0.1009 243 ARG   A C   
1544 O  O   . ARG   A 223 ? 2.7509 2.6001 2.3960 -0.1524 -0.4057 -0.1163 243 ARG   A O   
1545 C  CB  . ARG   A 223 ? 2.7616 2.7455 2.4966 -0.1149 -0.3885 -0.0836 243 ARG   A CB  
1546 C  CG  . ARG   A 223 ? 2.7806 2.7963 2.5438 -0.1321 -0.4458 -0.0912 243 ARG   A CG  
1547 C  CD  . ARG   A 223 ? 2.7962 2.7991 2.5070 -0.1049 -0.4736 -0.0931 243 ARG   A CD  
1548 N  NE  . ARG   A 223 ? 2.8317 2.7531 2.4380 -0.0769 -0.4493 -0.0964 243 ARG   A NE  
1549 C  CZ  . ARG   A 223 ? 2.8861 2.7263 2.3968 -0.0729 -0.4676 -0.1129 243 ARG   A CZ  
1550 N  NH1 . ARG   A 223 ? 2.8513 2.6745 2.3532 -0.0960 -0.5152 -0.1303 243 ARG   A NH1 
1551 N  NH2 . ARG   A 223 ? 2.9464 2.7197 2.3677 -0.0452 -0.4372 -0.1119 243 ARG   A NH2 
1552 N  N   . GLU   A 224 ? 2.7654 2.7331 2.5740 -0.1970 -0.4091 -0.0987 244 GLU   A N   
1553 C  CA  . GLU   A 224 ? 2.7915 2.7075 2.5787 -0.2253 -0.4372 -0.1146 244 GLU   A CA  
1554 C  C   . GLU   A 224 ? 2.7507 2.6176 2.5209 -0.2315 -0.4012 -0.1148 244 GLU   A C   
1555 O  O   . GLU   A 224 ? 2.8445 2.6376 2.5619 -0.2429 -0.4170 -0.1318 244 GLU   A O   
1556 C  CB  . GLU   A 224 ? 2.7708 2.7531 2.6485 -0.2622 -0.4745 -0.1106 244 GLU   A CB  
1557 C  CG  . GLU   A 224 ? 2.6732 2.7526 2.6548 -0.2691 -0.4478 -0.0869 244 GLU   A CG  
1558 C  CD  . GLU   A 224 ? 2.6871 2.8448 2.7595 -0.2980 -0.4851 -0.0805 244 GLU   A CD  
1559 O  OE1 . GLU   A 224 ? 2.6746 2.8267 2.7326 -0.3034 -0.5345 -0.0930 244 GLU   A OE1 
1560 O  OE2 . GLU   A 224 ? 2.6183 2.8447 2.7768 -0.3148 -0.4650 -0.0624 244 GLU   A OE2 
1561 N  N   . VAL   A 225 ? 2.7032 2.6159 2.4396 -0.2048 -0.3600 -0.0719 245 VAL   A N   
1562 C  CA  . VAL   A 225 ? 2.4639 2.3299 2.1830 -0.2073 -0.3255 -0.0708 245 VAL   A CA  
1563 C  C   . VAL   A 225 ? 2.4912 2.2845 2.1202 -0.1773 -0.3036 -0.0779 245 VAL   A C   
1564 O  O   . VAL   A 225 ? 2.5418 2.2701 2.1261 -0.1783 -0.2919 -0.0877 245 VAL   A O   
1565 C  CB  . VAL   A 225 ? 2.2087 2.1314 1.9984 -0.2091 -0.2900 -0.0497 245 VAL   A CB  
1566 C  CG1 . VAL   A 225 ? 2.2047 2.0810 1.9792 -0.2111 -0.2584 -0.0478 245 VAL   A CG1 
1567 C  CG2 . VAL   A 225 ? 2.0978 2.0931 1.9731 -0.2369 -0.3078 -0.0413 245 VAL   A CG2 
1568 N  N   . THR   A 226 ? 2.4009 2.2026 2.0018 -0.1495 -0.2965 -0.0723 246 THR   A N   
1569 C  CA  . THR   A 226 ? 2.2880 2.0247 1.8061 -0.1211 -0.2717 -0.0758 246 THR   A CA  
1570 C  C   . THR   A 226 ? 2.4578 2.1261 1.8880 -0.1167 -0.3016 -0.0970 246 THR   A C   
1571 O  O   . THR   A 226 ? 2.5005 2.0982 1.8622 -0.1050 -0.2835 -0.1068 246 THR   A O   
1572 C  CB  . THR   A 226 ? 2.0680 1.8330 1.5865 -0.0944 -0.2511 -0.0601 246 THR   A CB  
1573 O  OG1 . THR   A 226 ? 2.2171 2.0150 1.7398 -0.0910 -0.2867 -0.0604 246 THR   A OG1 
1574 C  CG2 . THR   A 226 ? 1.7097 1.5310 1.3041 -0.0964 -0.2197 -0.0420 246 THR   A CG2 
1575 N  N   . ASN   A 227 ? 2.6071 2.2950 2.0361 -0.1241 -0.3478 -0.1048 247 ASN   A N   
1576 C  CA  . ASN   A 227 ? 2.8359 2.4573 2.1790 -0.1220 -0.3828 -0.1272 247 ASN   A CA  
1577 C  C   . ASN   A 227 ? 2.8686 2.4359 2.1942 -0.1441 -0.3902 -0.1455 247 ASN   A C   
1578 O  O   . ASN   A 227 ? 3.0869 2.5754 2.3218 -0.1354 -0.4018 -0.1655 247 ASN   A O   
1579 C  CB  . ASN   A 227 ? 2.9481 2.6090 2.3084 -0.1306 -0.4375 -0.1325 247 ASN   A CB  
1580 C  CG  . ASN   A 227 ? 3.0024 2.6590 2.3084 -0.0979 -0.4419 -0.1260 247 ASN   A CG  
1581 O  OD1 . ASN   A 227 ? 3.0404 2.6432 2.2712 -0.0706 -0.4105 -0.1232 247 ASN   A OD1 
1582 N  ND2 . ASN   A 227 ? 2.9968 2.7101 2.3417 -0.0998 -0.4802 -0.1222 247 ASN   A ND2 
1583 N  N   . PHE   A 228 ? 2.6567 2.2612 2.0638 -0.1716 -0.3836 -0.1388 248 PHE   A N   
1584 C  CA  . PHE   A 228 ? 2.5502 2.0979 1.9426 -0.1889 -0.3789 -0.1514 248 PHE   A CA  
1585 C  C   . PHE   A 228 ? 2.5392 2.0134 1.8532 -0.1594 -0.3378 -0.1556 248 PHE   A C   
1586 O  O   . PHE   A 228 ? 2.6462 2.0411 1.8922 -0.1587 -0.3447 -0.1762 248 PHE   A O   
1587 C  CB  . PHE   A 228 ? 2.3694 1.9723 1.8611 -0.2151 -0.3634 -0.1350 248 PHE   A CB  
1588 C  CG  . PHE   A 228 ? 2.4100 1.9573 1.8961 -0.2353 -0.3599 -0.1446 248 PHE   A CG  
1589 C  CD1 . PHE   A 228 ? 2.6119 2.0729 2.0216 -0.2391 -0.3845 -0.1709 248 PHE   A CD1 
1590 C  CD2 . PHE   A 228 ? 2.2546 1.8325 1.8089 -0.2496 -0.3330 -0.1272 248 PHE   A CD2 
1591 C  CE1 . PHE   A 228 ? 2.6051 2.0097 2.0094 -0.2567 -0.3815 -0.1799 248 PHE   A CE1 
1592 C  CE2 . PHE   A 228 ? 2.2804 1.8045 1.8294 -0.2669 -0.3299 -0.1338 248 PHE   A CE2 
1593 C  CZ  . PHE   A 228 ? 2.4281 1.8645 1.9035 -0.2707 -0.3542 -0.1603 248 PHE   A CZ  
1594 N  N   . LEU   A 229 ? 2.3862 1.8856 1.7088 -0.1341 -0.2950 -0.1367 249 LEU   A N   
1595 C  CA  . LEU   A 229 ? 2.2065 1.6543 1.4799 -0.1082 -0.2489 -0.1351 249 LEU   A CA  
1596 C  C   . LEU   A 229 ? 2.4080 1.8265 1.6048 -0.0740 -0.2327 -0.1340 249 LEU   A C   
1597 O  O   . LEU   A 229 ? 2.4960 1.8539 1.6284 -0.0518 -0.2022 -0.1394 249 LEU   A O   
1598 C  CB  . LEU   A 229 ? 1.7601 1.2579 1.1107 -0.1087 -0.2087 -0.1128 249 LEU   A CB  
1599 C  CG  . LEU   A 229 ? 1.6844 1.2314 1.1202 -0.1438 -0.2288 -0.1078 249 LEU   A CG  
1600 C  CD1 . LEU   A 229 ? 1.3829 0.9894 0.8985 -0.1462 -0.1960 -0.0846 249 LEU   A CD1 
1601 C  CD2 . LEU   A 229 ? 1.9410 1.4255 1.3512 -0.1630 -0.2465 -0.1263 249 LEU   A CD2 
1602 N  N   . ARG   A 230 ? 2.5545 2.0126 1.7551 -0.0682 -0.2521 -0.1265 250 ARG   A N   
1603 C  CA  . ARG   A 230 ? 2.7825 2.2034 1.8982 -0.0378 -0.2456 -0.1264 250 ARG   A CA  
1604 C  C   . ARG   A 230 ? 3.1211 2.4517 2.1286 -0.0283 -0.2604 -0.1514 250 ARG   A C   
1605 O  O   . ARG   A 230 ? 3.0686 2.3521 1.9898 0.0006  -0.2443 -0.1518 250 ARG   A O   
1606 C  CB  . ARG   A 230 ? 2.7304 2.2008 1.8636 -0.0372 -0.2790 -0.1188 250 ARG   A CB  
1607 C  CG  . ARG   A 230 ? 2.6165 2.1679 1.8414 -0.0385 -0.2596 -0.0944 250 ARG   A CG  
1608 C  CD  . ARG   A 230 ? 2.6645 2.2570 1.8976 -0.0299 -0.2872 -0.0859 250 ARG   A CD  
1609 N  NE  . ARG   A 230 ? 2.8600 2.4126 2.0149 0.0018  -0.2701 -0.0780 250 ARG   A NE  
1610 C  CZ  . ARG   A 230 ? 2.9251 2.5056 2.0818 0.0169  -0.2802 -0.0646 250 ARG   A CZ  
1611 N  NH1 . ARG   A 230 ? 2.8686 2.5202 2.1032 0.0051  -0.3071 -0.0590 250 ARG   A NH1 
1612 N  NH2 . ARG   A 230 ? 2.9779 2.5141 2.0580 0.0449  -0.2618 -0.0556 250 ARG   A NH2 
1613 N  N   . LYS   A 231 ? 3.3886 2.6921 2.3973 -0.0522 -0.2908 -0.1720 251 LYS   A N   
1614 C  CA  . LYS   A 231 ? 3.5071 2.7172 2.4197 -0.0454 -0.2997 -0.1986 251 LYS   A CA  
1615 C  C   . LYS   A 231 ? 3.3627 2.5400 2.2950 -0.0557 -0.2775 -0.2058 251 LYS   A C   
1616 O  O   . LYS   A 231 ? 3.5115 2.6103 2.3626 -0.0358 -0.2580 -0.2209 251 LYS   A O   
1617 C  CB  . LYS   A 231 ? 3.6434 2.8331 2.5227 -0.0645 -0.3662 -0.2220 251 LYS   A CB  
1618 C  CG  . LYS   A 231 ? 3.5799 2.8499 2.5672 -0.1014 -0.4047 -0.2158 251 LYS   A CG  
1619 C  CD  . LYS   A 231 ? 3.6187 2.8752 2.5766 -0.1185 -0.4722 -0.2375 251 LYS   A CD  
1620 C  CE  . LYS   A 231 ? 3.4771 2.8324 2.5385 -0.1419 -0.5051 -0.2236 251 LYS   A CE  
1621 N  NZ  . LYS   A 231 ? 3.3208 2.7396 2.4972 -0.1681 -0.4835 -0.2069 251 LYS   A NZ  
1622 N  N   . SER   A 232 ? 3.1342 2.3671 2.1687 -0.0835 -0.2778 -0.1947 252 SER   A N   
1623 C  CA  . SER   A 232 ? 3.0049 2.2015 2.0553 -0.0933 -0.2605 -0.2007 252 SER   A CA  
1624 C  C   . SER   A 232 ? 3.0587 2.2274 2.0831 -0.0609 -0.2016 -0.1918 252 SER   A C   
1625 O  O   . SER   A 232 ? 3.1574 2.2643 2.1500 -0.0551 -0.1866 -0.2041 252 SER   A O   
1626 C  CB  . SER   A 232 ? 2.7660 2.0314 1.9298 -0.1263 -0.2662 -0.1851 252 SER   A CB  
1627 O  OG  . SER   A 232 ? 2.7403 2.0260 1.9338 -0.1599 -0.3191 -0.1949 252 SER   A OG  
1628 N  N   . VAL   A 233 ? 2.9900 2.2037 2.0321 -0.0400 -0.1681 -0.1701 253 VAL   A N   
1629 C  CA  . VAL   A 233 ? 2.9404 2.1314 1.9610 -0.0094 -0.1125 -0.1609 253 VAL   A CA  
1630 C  C   . VAL   A 233 ? 3.0954 2.2088 1.9979 0.0216  -0.1014 -0.1764 253 VAL   A C   
1631 O  O   . VAL   A 233 ? 3.1513 2.2121 2.0106 0.0444  -0.0657 -0.1822 253 VAL   A O   
1632 C  CB  . VAL   A 233 ? 2.7381 2.0061 1.8289 -0.0022 -0.0812 -0.1314 253 VAL   A CB  
1633 C  CG1 . VAL   A 233 ? 2.7624 2.0210 1.8621 0.0210  -0.0264 -0.1201 253 VAL   A CG1 
1634 C  CG2 . VAL   A 233 ? 2.4613 1.8068 1.6555 -0.0329 -0.1017 -0.1187 253 VAL   A CG2 
1635 N  N   . LYS   A 234 ? 3.1342 2.2379 1.9800 0.0248  -0.1319 -0.1834 254 LYS   A N   
1636 C  CA  . LYS   A 234 ? 3.2109 2.2297 1.9310 0.0506  -0.1324 -0.2033 254 LYS   A CA  
1637 C  C   . LYS   A 234 ? 3.3992 2.3411 2.0664 0.0414  -0.1592 -0.2351 254 LYS   A C   
1638 O  O   . LYS   A 234 ? 3.5121 2.3717 2.0710 0.0662  -0.1515 -0.2546 254 LYS   A O   
1639 C  CB  . LYS   A 234 ? 3.0947 2.1192 1.7656 0.0540  -0.1680 -0.2043 254 LYS   A CB  
1640 C  CG  . LYS   A 234 ? 2.9750 2.0580 1.6766 0.0684  -0.1409 -0.1741 254 LYS   A CG  
1641 C  CD  . LYS   A 234 ? 2.9440 2.0259 1.5919 0.0732  -0.1805 -0.1757 254 LYS   A CD  
1642 C  CE  . LYS   A 234 ? 2.8009 1.9341 1.4776 0.0874  -0.1551 -0.1454 254 LYS   A CE  
1643 N  NZ  . LYS   A 234 ? 2.8088 1.9312 1.4221 0.0968  -0.1932 -0.1466 254 LYS   A NZ  
1644 N  N   . ARG   A 235 ? 3.5000 2.4641 2.2394 0.0066  -0.1891 -0.2403 255 ARG   A N   
1645 C  CA  . ARG   A 235 ? 3.7628 2.6566 2.4655 -0.0094 -0.2204 -0.2695 255 ARG   A CA  
1646 C  C   . ARG   A 235 ? 3.8241 2.6851 2.5461 -0.0027 -0.1828 -0.2699 255 ARG   A C   
1647 O  O   . ARG   A 235 ? 3.9334 2.7567 2.6650 -0.0254 -0.2078 -0.2862 255 ARG   A O   
1648 C  CB  . ARG   A 235 ? 3.8097 2.7466 2.5826 -0.0547 -0.2779 -0.2734 255 ARG   A CB  
1649 C  CG  . ARG   A 235 ? 3.9434 2.8058 2.6633 -0.0760 -0.3293 -0.3074 255 ARG   A CG  
1650 C  CD  . ARG   A 235 ? 3.8983 2.8144 2.7187 -0.1247 -0.3714 -0.3038 255 ARG   A CD  
1651 N  NE  . ARG   A 235 ? 3.8243 2.8392 2.7166 -0.1369 -0.3879 -0.2828 255 ARG   A NE  
1652 C  CZ  . ARG   A 235 ? 3.7159 2.8024 2.7107 -0.1745 -0.4143 -0.2714 255 ARG   A CZ  
1653 N  NH1 . ARG   A 235 ? 3.6697 2.7397 2.7083 -0.2064 -0.4275 -0.2772 255 ARG   A NH1 
1654 N  NH2 . ARG   A 235 ? 3.6487 2.8221 2.7018 -0.1791 -0.4256 -0.2531 255 ARG   A NH2 
1655 N  N   . MET   A 236 ? 3.7246 2.5988 2.4553 0.0275  -0.1243 -0.2516 256 MET   A N   
1656 C  CA  . MET   A 236 ? 3.6460 2.4915 2.3962 0.0386  -0.0877 -0.2507 256 MET   A CA  
1657 C  C   . MET   A 236 ? 3.5330 2.3515 2.2332 0.0842  -0.0278 -0.2447 256 MET   A C   
1658 O  O   . MET   A 236 ? 3.4408 2.3057 2.2061 0.0956  0.0148  -0.2216 256 MET   A O   
1659 C  CB  . MET   A 236 ? 3.6154 2.5417 2.4907 0.0161  -0.0785 -0.2247 256 MET   A CB  
1660 C  CG  . MET   A 236 ? 3.6678 2.6190 2.6050 -0.0287 -0.1266 -0.2275 256 MET   A CG  
1661 S  SD  . MET   A 236 ? 3.6043 2.6349 2.6705 -0.0468 -0.1053 -0.1966 256 MET   A SD  
1662 C  CE  . MET   A 236 ? 3.6006 2.6633 2.7251 -0.0991 -0.1633 -0.1995 256 MET   A CE  
1663 N  N   . ASP   A 250 ? 2.9839 2.0661 2.2515 0.2813  0.3248  -0.1023 270 ASP   A N   
1664 C  CA  . ASP   A 250 ? 2.8497 1.9815 2.1643 0.2334  0.2814  -0.0969 270 ASP   A CA  
1665 C  C   . ASP   A 250 ? 2.7531 1.9641 2.1065 0.2217  0.2889  -0.0807 270 ASP   A C   
1666 O  O   . ASP   A 250 ? 2.7909 2.0080 2.1204 0.2469  0.3239  -0.0759 270 ASP   A O   
1667 C  CB  . ASP   A 250 ? 2.8404 1.9011 2.0820 0.2080  0.2354  -0.1232 270 ASP   A CB  
1668 C  CG  . ASP   A 250 ? 2.9200 1.9269 2.1611 0.1963  0.2106  -0.1323 270 ASP   A CG  
1669 O  OD1 . ASP   A 250 ? 2.8919 1.9323 2.2017 0.1994  0.2213  -0.1145 270 ASP   A OD1 
1670 O  OD2 . ASP   A 250 ? 3.0050 1.9344 2.1766 0.1830  0.1783  -0.1568 270 ASP   A OD2 
1671 N  N   . PHE   A 251 ? 2.6596 1.9295 2.0743 0.1838  0.2568  -0.0713 271 PHE   A N   
1672 C  CA  . PHE   A 251 ? 2.5573 1.8913 2.0009 0.1660  0.2512  -0.0605 271 PHE   A CA  
1673 C  C   . PHE   A 251 ? 2.6334 1.9216 1.9883 0.1718  0.2469  -0.0762 271 PHE   A C   
1674 O  O   . PHE   A 251 ? 2.6402 1.9533 1.9889 0.1852  0.2723  -0.0661 271 PHE   A O   
1675 C  CB  . PHE   A 251 ? 2.5265 1.9077 2.0287 0.1254  0.2111  -0.0553 271 PHE   A CB  
1676 C  CG  . PHE   A 251 ? 2.3365 1.7699 1.8575 0.1033  0.1938  -0.0500 271 PHE   A CG  
1677 C  CD1 . PHE   A 251 ? 2.2506 1.7593 1.8392 0.1021  0.2100  -0.0296 271 PHE   A CD1 
1678 C  CD2 . PHE   A 251 ? 2.3577 1.7654 1.8333 0.0824  0.1574  -0.0657 271 PHE   A CD2 
1679 C  CE1 . PHE   A 251 ? 2.1526 1.7038 1.7567 0.0835  0.1935  -0.0255 271 PHE   A CE1 
1680 C  CE2 . PHE   A 251 ? 2.2536 1.7100 1.7488 0.0649  0.1408  -0.0603 271 PHE   A CE2 
1681 C  CZ  . PHE   A 251 ? 2.1614 1.6878 1.7197 0.0662  0.1597  -0.0402 271 PHE   A CZ  
1682 N  N   . LEU   A 252 ? 2.8945 2.1110 2.1769 0.1626  0.2144  -0.1006 272 LEU   A N   
1683 C  CA  . LEU   A 252 ? 2.7747 1.9325 1.9572 0.1739  0.2087  -0.1188 272 LEU   A CA  
1684 C  C   . LEU   A 252 ? 2.8314 1.9523 1.9576 0.2192  0.2598  -0.1181 272 LEU   A C   
1685 O  O   . LEU   A 252 ? 2.8434 1.9589 1.9200 0.2330  0.2750  -0.1163 272 LEU   A O   
1686 C  CB  . LEU   A 252 ? 2.6313 1.7079 1.7449 0.1600  0.1663  -0.1474 272 LEU   A CB  
1687 C  CG  . LEU   A 252 ? 2.5395 1.5768 1.5720 0.1514  0.1330  -0.1662 272 LEU   A CG  
1688 C  CD1 . LEU   A 252 ? 2.5840 1.6966 1.6549 0.1377  0.1277  -0.1492 272 LEU   A CD1 
1689 C  CD2 . LEU   A 252 ? 2.8065 1.7910 1.8093 0.1218  0.0783  -0.1900 272 LEU   A CD2 
1690 N  N   . GLN   A 253 ? 2.9694 2.0628 2.1001 0.2445  0.2877  -0.1187 273 GLN   A N   
1691 C  CA  . GLN   A 253 ? 3.0976 2.1578 2.1803 0.2910  0.3406  -0.1174 273 GLN   A CA  
1692 C  C   . GLN   A 253 ? 3.0565 2.1964 2.1986 0.3007  0.3815  -0.0883 273 GLN   A C   
1693 O  O   . GLN   A 253 ? 3.0574 2.1861 2.1444 0.3143  0.4005  -0.0861 273 GLN   A O   
1694 C  CB  . GLN   A 253 ? 3.1201 2.1490 2.2173 0.3153  0.3610  -0.1202 273 GLN   A CB  
1695 C  CG  . GLN   A 253 ? 3.2690 2.2400 2.2948 0.3672  0.4110  -0.1271 273 GLN   A CG  
1696 C  CD  . GLN   A 253 ? 3.5217 2.3736 2.4277 0.3814  0.3922  -0.1621 273 GLN   A CD  
1697 O  OE1 . GLN   A 253 ? 3.6219 2.4235 2.5201 0.3947  0.3910  -0.1735 273 GLN   A OE1 
1698 N  NE2 . GLN   A 253 ? 3.5550 2.3571 2.3641 0.3797  0.3757  -0.1799 273 GLN   A NE2 
1699 N  N   . LEU   A 254 ? 2.8984 2.1175 2.1519 0.2916  0.3921  -0.0655 274 LEU   A N   
1700 C  CA  . LEU   A 254 ? 2.8628 2.1576 2.1856 0.3009  0.4322  -0.0372 274 LEU   A CA  
1701 C  C   . LEU   A 254 ? 2.8244 2.1522 2.1421 0.2825  0.4250  -0.0279 274 LEU   A C   
1702 O  O   . LEU   A 254 ? 2.7340 2.1185 2.1038 0.2873  0.4569  -0.0043 274 LEU   A O   
1703 C  CB  . LEU   A 254 ? 2.6845 2.0561 2.1270 0.2867  0.4291  -0.0181 274 LEU   A CB  
1704 C  CG  . LEU   A 254 ? 2.7438 2.0875 2.2012 0.2986  0.4253  -0.0252 274 LEU   A CG  
1705 C  CD1 . LEU   A 254 ? 2.3251 1.7449 1.8938 0.2789  0.4115  -0.0065 274 LEU   A CD1 
1706 C  CD2 . LEU   A 254 ? 2.7614 2.0690 2.1884 0.3466  0.4752  -0.0252 274 LEU   A CD2 
1707 N  N   . MET   A 255 ? 2.7967 2.0901 2.0557 0.2612  0.3824  -0.0453 275 MET   A N   
1708 C  CA  . MET   A 255 ? 2.7579 2.0671 1.9929 0.2500  0.3745  -0.0390 275 MET   A CA  
1709 C  C   . MET   A 255 ? 2.9441 2.1913 2.0712 0.2801  0.4015  -0.0445 275 MET   A C   
1710 O  O   . MET   A 255 ? 3.0110 2.2846 2.1423 0.2906  0.4347  -0.0242 275 MET   A O   
1711 C  CB  . MET   A 255 ? 2.6442 1.9524 1.8720 0.2146  0.3150  -0.0532 275 MET   A CB  
1712 C  CG  . MET   A 255 ? 2.5498 1.9411 1.8846 0.1852  0.2984  -0.0370 275 MET   A CG  
1713 S  SD  . MET   A 255 ? 2.4971 1.8983 1.8367 0.1457  0.2344  -0.0505 275 MET   A SD  
1714 C  CE  . MET   A 255 ? 2.0683 1.5624 1.5364 0.1221  0.2305  -0.0303 275 MET   A CE  
1715 N  N   . ILE   A 256 ? 3.0363 2.1983 2.0622 0.2920  0.3839  -0.0719 276 ILE   A N   
1716 C  CA  . ILE   A 256 ? 3.1203 2.2155 2.0304 0.3230  0.4073  -0.0795 276 ILE   A CA  
1717 C  C   . ILE   A 256 ? 3.2729 2.3650 2.1804 0.3639  0.4755  -0.0650 276 ILE   A C   
1718 O  O   . ILE   A 256 ? 3.3079 2.3770 2.1523 0.3884  0.5087  -0.0564 276 ILE   A O   
1719 C  CB  . ILE   A 256 ? 3.0725 2.0726 1.8734 0.3252  0.3673  -0.1155 276 ILE   A CB  
1720 C  CG1 . ILE   A 256 ? 2.9028 1.9215 1.7504 0.2812  0.3027  -0.1280 276 ILE   A CG1 
1721 C  CG2 . ILE   A 256 ? 2.9366 1.8808 1.6196 0.3406  0.3643  -0.1238 276 ILE   A CG2 
1722 C  CD1 . ILE   A 256 ? 2.6754 1.6048 1.4356 0.2773  0.2600  -0.1630 276 ILE   A CD1 
1723 N  N   . ASP   A 257 ? 3.4097 2.5318 2.3939 0.3707  0.4950  -0.0588 277 ASP   A N   
1724 C  CA  . ASP   A 257 ? 3.5007 2.6333 2.5012 0.4093  0.5594  -0.0423 277 ASP   A CA  
1725 C  C   . ASP   A 257 ? 3.4251 2.6396 2.5023 0.4040  0.5932  -0.0061 277 ASP   A C   
1726 O  O   . ASP   A 257 ? 3.3998 2.6180 2.4644 0.4229  0.6262  0.0119  277 ASP   A O   
1727 C  CB  . ASP   A 257 ? 3.5633 2.7134 2.6358 0.4168  0.5663  -0.0432 277 ASP   A CB  
1728 C  CG  . ASP   A 257 ? 3.6677 2.7482 2.6907 0.4080  0.5198  -0.0747 277 ASP   A CG  
1729 O  OD1 . ASP   A 257 ? 3.7581 2.7670 2.6788 0.4031  0.4888  -0.0991 277 ASP   A OD1 
1730 O  OD2 . ASP   A 257 ? 3.6479 2.7447 2.7354 0.4047  0.5124  -0.0743 277 ASP   A OD2 
1731 N  N   . ALA   A 269 ? 2.8311 2.2938 2.0771 0.2735  0.5890  0.1468  289 ALA   A N   
1732 C  CA  . ALA   A 269 ? 2.8191 2.2706 2.0633 0.2779  0.5684  0.1193  289 ALA   A CA  
1733 C  C   . ALA   A 269 ? 2.7775 2.2198 2.0064 0.2546  0.5008  0.0938  289 ALA   A C   
1734 O  O   . ALA   A 269 ? 2.6895 2.1625 1.9549 0.2311  0.4718  0.1002  289 ALA   A O   
1735 C  CB  . ALA   A 269 ? 2.9007 2.2855 2.0466 0.3135  0.5948  0.1073  289 ALA   A CB  
1736 N  N   . LEU   A 270 ? 3.0121 2.4116 2.1883 0.2611  0.4758  0.0656  290 LEU   A N   
1737 C  CA  . LEU   A 270 ? 2.9840 2.3830 2.1620 0.2364  0.4135  0.0427  290 LEU   A CA  
1738 C  C   . LEU   A 270 ? 3.0450 2.3763 2.1057 0.2437  0.3828  0.0242  290 LEU   A C   
1739 O  O   . LEU   A 270 ? 3.2159 2.4831 2.1777 0.2720  0.4055  0.0181  290 LEU   A O   
1740 C  CB  . LEU   A 270 ? 2.9511 2.3521 2.1635 0.2321  0.3997  0.0246  290 LEU   A CB  
1741 C  CG  . LEU   A 270 ? 2.9673 2.3665 2.1845 0.2057  0.3391  0.0021  290 LEU   A CG  
1742 C  CD1 . LEU   A 270 ? 2.8153 2.2864 2.1239 0.1755  0.3137  0.0137  290 LEU   A CD1 
1743 C  CD2 . LEU   A 270 ? 3.0714 2.4557 2.3045 0.2069  0.3341  -0.0134 290 LEU   A CD2 
1744 N  N   . SER   A 271 ? 2.7092 2.0563 1.7816 0.2190  0.3301  0.0152  291 SER   A N   
1745 C  CA  . SER   A 271 ? 2.6503 1.9454 1.6281 0.2205  0.2893  -0.0027 291 SER   A CA  
1746 C  C   . SER   A 271 ? 2.5996 1.8678 1.5603 0.2087  0.2460  -0.0333 291 SER   A C   
1747 O  O   . SER   A 271 ? 2.5941 1.8664 1.5925 0.2077  0.2572  -0.0402 291 SER   A O   
1748 C  CB  . SER   A 271 ? 2.5612 1.8948 1.5697 0.2025  0.2596  0.0088  291 SER   A CB  
1749 O  OG  . SER   A 271 ? 2.5257 1.8331 1.4822 0.1937  0.2039  -0.0119 291 SER   A OG  
1750 N  N   . ASP   A 272 ? 2.4633 1.7037 1.3696 0.1993  0.1950  -0.0508 292 ASP   A N   
1751 C  CA  . ASP   A 272 ? 2.4437 1.6530 1.3283 0.1850  0.1496  -0.0798 292 ASP   A CA  
1752 C  C   . ASP   A 272 ? 2.2788 1.5456 1.2410 0.1497  0.0988  -0.0829 292 ASP   A C   
1753 O  O   . ASP   A 272 ? 2.1804 1.4690 1.2020 0.1290  0.0826  -0.0915 292 ASP   A O   
1754 C  CB  . ASP   A 272 ? 2.5525 1.6756 1.3038 0.2031  0.1279  -0.1012 292 ASP   A CB  
1755 C  CG  . ASP   A 272 ? 2.8350 1.8872 1.5048 0.2356  0.1687  -0.1105 292 ASP   A CG  
1756 O  OD1 . ASP   A 272 ? 2.7844 1.8591 1.5069 0.2449  0.2154  -0.0983 292 ASP   A OD1 
1757 O  OD2 . ASP   A 272 ? 2.9971 1.9706 1.5487 0.2534  0.1533  -0.1304 292 ASP   A OD2 
1758 N  N   . LEU   A 273 ? 2.2755 1.5656 1.2356 0.1438  0.0739  -0.0755 293 LEU   A N   
1759 C  CA  . LEU   A 273 ? 2.2667 1.6178 1.3048 0.1138  0.0303  -0.0763 293 LEU   A CA  
1760 C  C   . LEU   A 273 ? 2.1609 1.5852 1.3140 0.0985  0.0518  -0.0598 293 LEU   A C   
1761 O  O   . LEU   A 273 ? 2.0870 1.5544 1.3087 0.0732  0.0243  -0.0645 293 LEU   A O   
1762 C  CB  . LEU   A 273 ? 2.3138 1.6738 1.3245 0.1174  0.0051  -0.0691 293 LEU   A CB  
1763 C  CG  . LEU   A 273 ? 2.1708 1.5956 1.2521 0.0956  -0.0357 -0.0653 293 LEU   A CG  
1764 C  CD1 . LEU   A 273 ? 2.1069 1.6006 1.2854 0.0884  -0.0085 -0.0436 293 LEU   A CD1 
1765 C  CD2 . LEU   A 273 ? 2.2382 1.6767 1.3529 0.0686  -0.0812 -0.0854 293 LEU   A CD2 
1766 N  N   . GLU   A 274 ? 2.1284 1.5671 1.3034 0.1132  0.1005  -0.0398 294 GLU   A N   
1767 C  CA  . GLU   A 274 ? 1.9944 1.4958 1.2720 0.1007  0.1206  -0.0259 294 GLU   A CA  
1768 C  C   . GLU   A 274 ? 1.9972 1.4892 1.2972 0.0973  0.1305  -0.0353 294 GLU   A C   
1769 O  O   . GLU   A 274 ? 1.8078 1.3505 1.1913 0.0812  0.1304  -0.0294 294 GLU   A O   
1770 C  CB  . GLU   A 274 ? 2.0801 1.5982 1.3763 0.1157  0.1668  -0.0017 294 GLU   A CB  
1771 C  CG  . GLU   A 274 ? 2.2265 1.7490 1.5008 0.1198  0.1592  0.0104  294 GLU   A CG  
1772 C  CD  . GLU   A 274 ? 2.2722 1.8121 1.5746 0.1295  0.2039  0.0363  294 GLU   A CD  
1773 O  OE1 . GLU   A 274 ? 2.0377 1.5468 1.3052 0.1485  0.2458  0.0441  294 GLU   A OE1 
1774 O  OE2 . GLU   A 274 ? 2.1823 1.7646 1.5402 0.1186  0.1977  0.0490  294 GLU   A OE2 
1775 N  N   . LEU   A 275 ? 2.1116 1.5358 1.3343 0.1141  0.1385  -0.0500 295 LEU   A N   
1776 C  CA  . LEU   A 275 ? 2.1568 1.5615 1.3921 0.1110  0.1403  -0.0619 295 LEU   A CA  
1777 C  C   . LEU   A 275 ? 2.0498 1.4699 1.3187 0.0803  0.0914  -0.0754 295 LEU   A C   
1778 O  O   . LEU   A 275 ? 1.8880 1.3306 1.2160 0.0670  0.0911  -0.0743 295 LEU   A O   
1779 C  CB  . LEU   A 275 ? 2.1968 1.5165 1.3307 0.1375  0.1558  -0.0779 295 LEU   A CB  
1780 C  CG  . LEU   A 275 ? 2.1856 1.4730 1.3213 0.1460  0.1724  -0.0874 295 LEU   A CG  
1781 C  CD1 . LEU   A 275 ? 2.3789 1.6038 1.4332 0.1846  0.2154  -0.0906 295 LEU   A CD1 
1782 C  CD2 . LEU   A 275 ? 2.1690 1.4195 1.2859 0.1248  0.1252  -0.1114 295 LEU   A CD2 
1783 N  N   . VAL   A 276 ? 2.0130 1.4212 1.2451 0.0689  0.0496  -0.0869 296 VAL   A N   
1784 C  CA  . VAL   A 276 ? 2.0277 1.4649 1.3061 0.0370  0.0039  -0.0954 296 VAL   A CA  
1785 C  C   . VAL   A 276 ? 2.0004 1.5215 1.3845 0.0201  0.0100  -0.0767 296 VAL   A C   
1786 O  O   . VAL   A 276 ? 1.9004 1.4442 1.3397 0.0019  0.0038  -0.0763 296 VAL   A O   
1787 C  CB  . VAL   A 276 ? 2.0460 1.4721 1.2802 0.0298  -0.0405 -0.1063 296 VAL   A CB  
1788 C  CG1 . VAL   A 276 ? 2.0827 1.5603 1.3863 -0.0040 -0.0832 -0.1088 296 VAL   A CG1 
1789 C  CG2 . VAL   A 276 ? 2.3755 1.7121 1.5001 0.0434  -0.0550 -0.1291 296 VAL   A CG2 
1790 N  N   . ALA   A 277 ? 1.8589 1.4219 1.2676 0.0275  0.0239  -0.0607 297 ALA   A N   
1791 C  CA  . ALA   A 277 ? 1.7122 1.3505 1.2122 0.0134  0.0266  -0.0453 297 ALA   A CA  
1792 C  C   . ALA   A 277 ? 1.6231 1.2801 1.1773 0.0106  0.0516  -0.0380 297 ALA   A C   
1793 O  O   . ALA   A 277 ? 1.6304 1.3302 1.2468 -0.0090 0.0384  -0.0349 297 ALA   A O   
1794 C  CB  . ALA   A 277 ? 1.7508 1.4137 1.2569 0.0266  0.0445  -0.0298 297 ALA   A CB  
1795 N  N   . GLN   A 278 ? 1.6315 1.2582 1.1631 0.0315  0.0885  -0.0340 298 GLN   A N   
1796 C  CA  . GLN   A 278 ? 1.5871 1.2316 1.1704 0.0321  0.1109  -0.0263 298 GLN   A CA  
1797 C  C   . GLN   A 278 ? 1.7197 1.3434 1.3058 0.0170  0.0892  -0.0380 298 GLN   A C   
1798 O  O   . GLN   A 278 ? 1.6651 1.3245 1.3122 0.0048  0.0886  -0.0303 298 GLN   A O   
1799 C  CB  . GLN   A 278 ? 1.5324 1.1460 1.0885 0.0599  0.1539  -0.0206 298 GLN   A CB  
1800 C  CG  . GLN   A 278 ? 1.6617 1.2842 1.2050 0.0750  0.1791  -0.0076 298 GLN   A CG  
1801 C  CD  . GLN   A 278 ? 1.5617 1.2485 1.1715 0.0605  0.1719  0.0062  298 GLN   A CD  
1802 O  OE1 . GLN   A 278 ? 1.5382 1.2719 1.2199 0.0502  0.1737  0.0143  298 GLN   A OE1 
1803 N  NE2 . GLN   A 278 ? 1.6386 1.3241 1.2204 0.0615  0.1625  0.0086  298 GLN   A NE2 
1804 N  N   . SER   A 279 ? 1.7185 1.2809 1.2362 0.0173  0.0702  -0.0564 299 SER   A N   
1805 C  CA  . SER   A 279 ? 1.7173 1.2498 1.2334 0.0011  0.0483  -0.0680 299 SER   A CA  
1806 C  C   . SER   A 279 ? 1.7062 1.2943 1.2886 -0.0308 0.0184  -0.0627 299 SER   A C   
1807 O  O   . SER   A 279 ? 1.5905 1.1858 1.2114 -0.0442 0.0158  -0.0587 299 SER   A O   
1808 C  CB  . SER   A 279 ? 1.8397 1.2951 1.2675 0.0044  0.0265  -0.0909 299 SER   A CB  
1809 O  OG  . SER   A 279 ? 1.8744 1.2753 1.2338 0.0372  0.0579  -0.0959 299 SER   A OG  
1810 N  N   . ILE   A 280 ? 1.5972 1.2244 1.1926 -0.0416 -0.0028 -0.0612 300 ILE   A N   
1811 C  CA  . ILE   A 280 ? 1.5507 1.2367 1.2110 -0.0690 -0.0273 -0.0549 300 ILE   A CA  
1812 C  C   . ILE   A 280 ? 1.4974 1.2372 1.2272 -0.0705 -0.0052 -0.0370 300 ILE   A C   
1813 O  O   . ILE   A 280 ? 1.4460 1.2083 1.2187 -0.0897 -0.0144 -0.0317 300 ILE   A O   
1814 C  CB  . ILE   A 280 ? 1.4616 1.1834 1.1251 -0.0735 -0.0501 -0.0553 300 ILE   A CB  
1815 C  CG1 . ILE   A 280 ? 1.8200 1.4995 1.4285 -0.0814 -0.0869 -0.0734 300 ILE   A CG1 
1816 C  CG2 . ILE   A 280 ? 1.4493 1.2462 1.1906 -0.0932 -0.0612 -0.0437 300 ILE   A CG2 
1817 C  CD1 . ILE   A 280 ? 1.8777 1.4737 1.3958 -0.0629 -0.0825 -0.0891 300 ILE   A CD1 
1818 N  N   . ILE   A 281 ? 1.3391 1.0985 1.0797 -0.0509 0.0235  -0.0269 301 ILE   A N   
1819 C  CA  . ILE   A 281 ? 1.4595 1.2679 1.2627 -0.0513 0.0410  -0.0115 301 ILE   A CA  
1820 C  C   . ILE   A 281 ? 1.4525 1.2389 1.2662 -0.0527 0.0496  -0.0092 301 ILE   A C   
1821 O  O   . ILE   A 281 ? 1.3135 1.1336 1.1739 -0.0661 0.0450  0.0000  301 ILE   A O   
1822 C  CB  . ILE   A 281 ? 1.5047 1.3284 1.3147 -0.0309 0.0691  -0.0024 301 ILE   A CB  
1823 C  CG1 . ILE   A 281 ? 1.5519 1.3936 1.3510 -0.0295 0.0594  -0.0028 301 ILE   A CG1 
1824 C  CG2 . ILE   A 281 ? 1.3202 1.1906 1.1930 -0.0315 0.0830  0.0115  301 ILE   A CG2 
1825 C  CD1 . ILE   A 281 ? 1.4350 1.3379 1.2882 -0.0425 0.0454  0.0038  301 ILE   A CD1 
1826 N  N   . PHE   A 282 ? 1.4595 1.1862 1.2261 -0.0368 0.0631  -0.0171 302 PHE   A N   
1827 C  CA  . PHE   A 282 ? 1.4702 1.1701 1.2439 -0.0332 0.0730  -0.0146 302 PHE   A CA  
1828 C  C   . PHE   A 282 ? 1.5005 1.1812 1.2745 -0.0585 0.0451  -0.0198 302 PHE   A C   
1829 O  O   . PHE   A 282 ? 1.4295 1.1253 1.2416 -0.0678 0.0452  -0.0090 302 PHE   A O   
1830 C  CB  . PHE   A 282 ? 1.6027 1.2409 1.3227 -0.0061 0.0962  -0.0228 302 PHE   A CB  
1831 C  CG  . PHE   A 282 ? 1.7261 1.3889 1.4670 0.0185  0.1314  -0.0108 302 PHE   A CG  
1832 C  CD1 . PHE   A 282 ? 1.6390 1.3408 1.3929 0.0210  0.1388  -0.0042 302 PHE   A CD1 
1833 C  CD2 . PHE   A 282 ? 1.8135 1.4625 1.5671 0.0383  0.1564  -0.0045 302 PHE   A CD2 
1834 C  CE1 . PHE   A 282 ? 1.6158 1.3414 1.3958 0.0397  0.1705  0.0083  302 PHE   A CE1 
1835 C  CE2 . PHE   A 282 ? 1.8422 1.5213 1.6259 0.0587  0.1879  0.0081  302 PHE   A CE2 
1836 C  CZ  . PHE   A 282 ? 1.7210 1.4385 1.5190 0.0577  0.1949  0.0147  302 PHE   A CZ  
1837 N  N   . ILE   A 283 ? 1.5379 1.1842 1.2699 -0.0707 0.0200  -0.0353 303 ILE   A N   
1838 C  CA  . ILE   A 283 ? 1.5778 1.2053 1.3145 -0.0989 -0.0086 -0.0400 303 ILE   A CA  
1839 C  C   . ILE   A 283 ? 1.5194 1.2180 1.3259 -0.1221 -0.0175 -0.0235 303 ILE   A C   
1840 O  O   . ILE   A 283 ? 1.6227 1.3190 1.4550 -0.1388 -0.0226 -0.0152 303 ILE   A O   
1841 C  CB  . ILE   A 283 ? 1.5235 1.1127 1.2101 -0.1099 -0.0391 -0.0596 303 ILE   A CB  
1842 C  CG1 . ILE   A 283 ? 1.5595 1.0641 1.1651 -0.0866 -0.0308 -0.0776 303 ILE   A CG1 
1843 C  CG2 . ILE   A 283 ? 1.5426 1.1289 1.2517 -0.1454 -0.0720 -0.0615 303 ILE   A CG2 
1844 C  CD1 . ILE   A 283 ? 1.6310 1.1071 1.1761 -0.0834 -0.0518 -0.0952 303 ILE   A CD1 
1845 N  N   . PHE   A 284 ? 1.4047 1.1645 1.2397 -0.1216 -0.0179 -0.0178 304 PHE   A N   
1846 C  CA  . PHE   A 284 ? 1.3907 1.2190 1.2873 -0.1388 -0.0227 -0.0029 304 PHE   A CA  
1847 C  C   . PHE   A 284 ? 1.3383 1.1851 1.2675 -0.1311 -0.0007 0.0129  304 PHE   A C   
1848 O  O   . PHE   A 284 ? 1.3918 1.2480 1.3479 -0.1476 -0.0050 0.0235  304 PHE   A O   
1849 C  CB  . PHE   A 284 ? 1.3647 1.2470 1.2784 -0.1336 -0.0252 -0.0018 304 PHE   A CB  
1850 C  CG  . PHE   A 284 ? 1.3442 1.2959 1.3158 -0.1457 -0.0267 0.0120  304 PHE   A CG  
1851 C  CD1 . PHE   A 284 ? 1.2963 1.2734 1.2960 -0.1712 -0.0467 0.0152  304 PHE   A CD1 
1852 C  CD2 . PHE   A 284 ? 1.2688 1.2592 1.2665 -0.1314 -0.0077 0.0218  304 PHE   A CD2 
1853 C  CE1 . PHE   A 284 ? 1.2112 1.2525 1.2607 -0.1792 -0.0438 0.0286  304 PHE   A CE1 
1854 C  CE2 . PHE   A 284 ? 1.4760 1.5247 1.5178 -0.1394 -0.0084 0.0326  304 PHE   A CE2 
1855 C  CZ  . PHE   A 284 ? 1.2572 1.3317 1.3233 -0.1618 -0.0244 0.0364  304 PHE   A CZ  
1856 N  N   . ALA   A 285 ? 1.3852 1.2383 1.3135 -0.1066 0.0221  0.0159  305 ALA   A N   
1857 C  CA  . ALA   A 285 ? 1.3658 1.2411 1.3273 -0.0976 0.0394  0.0304  305 ALA   A CA  
1858 C  C   . ALA   A 285 ? 1.4725 1.3040 1.4260 -0.1002 0.0408  0.0345  305 ALA   A C   
1859 O  O   . ALA   A 285 ? 1.4923 1.3431 1.4743 -0.1121 0.0376  0.0479  305 ALA   A O   
1860 C  CB  . ALA   A 285 ? 1.2753 1.1556 1.2361 -0.0717 0.0620  0.0314  305 ALA   A CB  
1861 N  N   . GLY   A 286 ? 1.4052 1.1734 1.3155 -0.0878 0.0462  0.0234  306 GLY   A N   
1862 C  CA  . GLY   A 286 ? 1.4801 1.1956 1.3762 -0.0868 0.0477  0.0254  306 GLY   A CA  
1863 C  C   . GLY   A 286 ? 1.5905 1.2949 1.4941 -0.1177 0.0255  0.0289  306 GLY   A C   
1864 O  O   . GLY   A 286 ? 1.5678 1.2411 1.4735 -0.1209 0.0264  0.0376  306 GLY   A O   
1865 N  N   . TYR   A 287 ? 1.5634 1.2942 1.4741 -0.1407 0.0056  0.0239  307 TYR   A N   
1866 C  CA  . TYR   A 287 ? 1.5990 1.3325 1.5292 -0.1738 -0.0148 0.0302  307 TYR   A CA  
1867 C  C   . TYR   A 287 ? 1.5002 1.3052 1.4841 -0.1842 -0.0096 0.0514  307 TYR   A C   
1868 O  O   . TYR   A 287 ? 1.5667 1.3676 1.5665 -0.1899 -0.0038 0.0678  307 TYR   A O   
1869 C  CB  . TYR   A 287 ? 1.6619 1.3900 1.5774 -0.1934 -0.0408 0.0146  307 TYR   A CB  
1870 C  CG  . TYR   A 287 ? 1.7098 1.4633 1.6628 -0.2303 -0.0614 0.0238  307 TYR   A CG  
1871 C  CD1 . TYR   A 287 ? 1.8048 1.5022 1.7470 -0.2531 -0.0766 0.0226  307 TYR   A CD1 
1872 C  CD2 . TYR   A 287 ? 1.6767 1.5093 1.6771 -0.2422 -0.0650 0.0339  307 TYR   A CD2 
1873 C  CE1 . TYR   A 287 ? 1.8437 1.5673 1.8269 -0.2895 -0.0939 0.0336  307 TYR   A CE1 
1874 C  CE2 . TYR   A 287 ? 1.7499 1.6119 1.7905 -0.2751 -0.0801 0.0446  307 TYR   A CE2 
1875 C  CZ  . TYR   A 287 ? 1.8008 1.6101 1.8352 -0.3002 -0.0943 0.0454  307 TYR   A CZ  
1876 O  OH  . TYR   A 287 ? 1.8043 1.6457 1.8853 -0.3359 -0.1080 0.0585  307 TYR   A OH  
1877 N  N   . GLU   A 288 ? 1.5215 1.3889 1.5287 -0.1843 -0.0111 0.0513  308 GLU   A N   
1878 C  CA  . GLU   A 288 ? 1.5380 1.4704 1.5906 -0.1983 -0.0105 0.0682  308 GLU   A CA  
1879 C  C   . GLU   A 288 ? 1.5060 1.4608 1.5741 -0.1818 0.0086  0.0836  308 GLU   A C   
1880 O  O   . GLU   A 288 ? 1.5203 1.4954 1.6101 -0.1934 0.0114  0.1013  308 GLU   A O   
1881 C  CB  . GLU   A 288 ? 1.5111 1.4992 1.5810 -0.1990 -0.0176 0.0621  308 GLU   A CB  
1882 C  CG  . GLU   A 288 ? 1.5347 1.5756 1.6458 -0.2235 -0.0264 0.0736  308 GLU   A CG  
1883 C  CD  . GLU   A 288 ? 1.6061 1.6942 1.7460 -0.2196 -0.0096 0.0927  308 GLU   A CD  
1884 O  OE1 . GLU   A 288 ? 1.6325 1.7254 1.7645 -0.1964 0.0043  0.0937  308 GLU   A OE1 
1885 O  OE2 . GLU   A 288 ? 1.6599 1.7797 1.8297 -0.2399 -0.0105 0.1072  308 GLU   A OE2 
1886 N  N   . THR   A 289 ? 1.3757 1.3282 1.4334 -0.1552 0.0212  0.0783  309 THR   A N   
1887 C  CA  . THR   A 289 ? 1.4018 1.3757 1.4761 -0.1395 0.0346  0.0917  309 THR   A CA  
1888 C  C   . THR   A 289 ? 1.3961 1.3313 1.4647 -0.1417 0.0373  0.1048  309 THR   A C   
1889 O  O   . THR   A 289 ? 1.2516 1.2102 1.3370 -0.1456 0.0397  0.1222  309 THR   A O   
1890 C  CB  . THR   A 289 ? 1.2812 1.2540 1.3500 -0.1131 0.0465  0.0838  309 THR   A CB  
1891 O  OG1 . THR   A 289 ? 1.2723 1.1875 1.3160 -0.1003 0.0536  0.0789  309 THR   A OG1 
1892 C  CG2 . THR   A 289 ? 1.2343 1.2266 1.2982 -0.1112 0.0435  0.0703  309 THR   A CG2 
1893 N  N   . THR   A 290 ? 1.2912 1.1628 1.3316 -0.1375 0.0370  0.0967  310 THR   A N   
1894 C  CA  . THR   A 290 ? 1.4100 1.2352 1.4415 -0.1378 0.0388  0.1086  310 THR   A CA  
1895 C  C   . THR   A 290 ? 1.4790 1.3097 1.5234 -0.1678 0.0293  0.1237  310 THR   A C   
1896 O  O   . THR   A 290 ? 1.4168 1.2551 1.4723 -0.1681 0.0343  0.1441  310 THR   A O   
1897 C  CB  . THR   A 290 ? 1.4888 1.2386 1.4821 -0.1295 0.0384  0.0937  310 THR   A CB  
1898 O  OG1 . THR   A 290 ? 1.4136 1.1637 1.3947 -0.1034 0.0501  0.0799  310 THR   A OG1 
1899 C  CG2 . THR   A 290 ? 1.5662 1.2663 1.5504 -0.1207 0.0433  0.1061  310 THR   A CG2 
1900 N  N   . SER   A 291 ? 1.4243 1.2525 1.4685 -0.1934 0.0155  0.1154  311 SER   A N   
1901 C  CA  . SER   A 291 ? 1.3817 1.2209 1.4466 -0.2253 0.0078  0.1313  311 SER   A CA  
1902 C  C   . SER   A 291 ? 1.3958 1.3049 1.4918 -0.2258 0.0181  0.1510  311 SER   A C   
1903 O  O   . SER   A 291 ? 1.4473 1.3552 1.5512 -0.2356 0.0235  0.1734  311 SER   A O   
1904 C  CB  . SER   A 291 ? 1.5281 1.3709 1.5984 -0.2513 -0.0108 0.1178  311 SER   A CB  
1905 O  OG  . SER   A 291 ? 1.5665 1.4861 1.6691 -0.2566 -0.0107 0.1201  311 SER   A OG  
1906 N  N   . SER   A 292 ? 1.3544 1.3202 1.4633 -0.2137 0.0212  0.1431  312 SER   A N   
1907 C  CA  . SER   A 292 ? 1.3445 1.3746 1.4771 -0.2126 0.0299  0.1580  312 SER   A CA  
1908 C  C   . SER   A 292 ? 1.2059 1.2306 1.3303 -0.1947 0.0406  0.1742  312 SER   A C   
1909 O  O   . SER   A 292 ? 1.2458 1.2905 1.3773 -0.2024 0.0469  0.1953  312 SER   A O   
1910 C  CB  . SER   A 292 ? 1.4040 1.4840 1.5461 -0.1993 0.0299  0.1434  312 SER   A CB  
1911 O  OG  . SER   A 292 ? 1.3389 1.4737 1.4963 -0.1932 0.0386  0.1549  312 SER   A OG  
1912 N  N   . VAL   A 293 ? 1.1608 1.1600 1.2707 -0.1697 0.0429  0.1659  313 VAL   A N   
1913 C  CA  . VAL   A 293 ? 1.2441 1.2414 1.3498 -0.1506 0.0489  0.1805  313 VAL   A CA  
1914 C  C   . VAL   A 293 ? 1.1977 1.1464 1.2910 -0.1594 0.0494  0.1996  313 VAL   A C   
1915 O  O   . VAL   A 293 ? 1.1862 1.1442 1.2773 -0.1560 0.0533  0.2207  313 VAL   A O   
1916 C  CB  . VAL   A 293 ? 1.2019 1.1889 1.3047 -0.1226 0.0510  0.1677  313 VAL   A CB  
1917 C  CG1 . VAL   A 293 ? 1.1136 1.1039 1.2181 -0.1026 0.0529  0.1828  313 VAL   A CG1 
1918 C  CG2 . VAL   A 293 ? 1.0716 1.1024 1.1864 -0.1164 0.0509  0.1512  313 VAL   A CG2 
1919 N  N   . LEU   A 294 ? 1.2183 1.1096 1.2988 -0.1700 0.0448  0.1925  314 LEU   A N   
1920 C  CA  . LEU   A 294 ? 1.4966 1.3331 1.5645 -0.1816 0.0440  0.2102  314 LEU   A CA  
1921 C  C   . LEU   A 294 ? 1.3922 1.2558 1.4736 -0.2084 0.0465  0.2333  314 LEU   A C   
1922 O  O   . LEU   A 294 ? 1.2855 1.1244 1.3581 -0.2110 0.0508  0.2575  314 LEU   A O   
1923 C  CB  . LEU   A 294 ? 1.4755 1.2454 1.5255 -0.1929 0.0356  0.1945  314 LEU   A CB  
1924 C  CG  . LEU   A 294 ? 1.3154 1.0236 1.3401 -0.1651 0.0384  0.1857  314 LEU   A CG  
1925 C  CD1 . LEU   A 294 ? 1.4846 1.1703 1.5048 -0.1518 0.0437  0.2102  314 LEU   A CD1 
1926 C  CD2 . LEU   A 294 ? 1.5599 1.2965 1.5872 -0.1361 0.0449  0.1681  314 LEU   A CD2 
1927 N  N   . SER   A 295 ? 1.1605 1.0759 1.2638 -0.2270 0.0452  0.2281  315 SER   A N   
1928 C  CA  . SER   A 295 ? 1.2851 1.2356 1.4069 -0.2513 0.0518  0.2510  315 SER   A CA  
1929 C  C   . SER   A 295 ? 1.2465 1.2420 1.3643 -0.2327 0.0641  0.2678  315 SER   A C   
1930 O  O   . SER   A 295 ? 1.2893 1.2818 1.4013 -0.2402 0.0732  0.2951  315 SER   A O   
1931 C  CB  . SER   A 295 ? 1.3964 1.3924 1.5473 -0.2734 0.0465  0.2395  315 SER   A CB  
1932 O  OG  . SER   A 295 ? 1.5636 1.5125 1.7122 -0.2906 0.0308  0.2232  315 SER   A OG  
1933 N  N   . PHE   A 296 ? 1.2267 1.2597 1.3437 -0.2078 0.0637  0.2518  316 PHE   A N   
1934 C  CA  . PHE   A 296 ? 1.1873 1.2557 1.2942 -0.1876 0.0706  0.2635  316 PHE   A CA  
1935 C  C   . PHE   A 296 ? 1.1581 1.1834 1.2411 -0.1736 0.0707  0.2825  316 PHE   A C   
1936 O  O   . PHE   A 296 ? 1.2202 1.2602 1.2883 -0.1680 0.0771  0.3039  316 PHE   A O   
1937 C  CB  . PHE   A 296 ? 1.2733 1.3755 1.3836 -0.1643 0.0659  0.2405  316 PHE   A CB  
1938 C  CG  . PHE   A 296 ? 1.1981 1.3542 1.3265 -0.1715 0.0681  0.2284  316 PHE   A CG  
1939 C  CD1 . PHE   A 296 ? 1.1302 1.3257 1.2663 -0.1845 0.0786  0.2437  316 PHE   A CD1 
1940 C  CD2 . PHE   A 296 ? 1.1454 1.3127 1.2830 -0.1635 0.0614  0.2034  316 PHE   A CD2 
1941 C  CE1 . PHE   A 296 ? 1.1852 1.4318 1.3404 -0.1875 0.0814  0.2328  316 PHE   A CE1 
1942 C  CE2 . PHE   A 296 ? 1.1743 1.3882 1.3276 -0.1674 0.0624  0.1930  316 PHE   A CE2 
1943 C  CZ  . PHE   A 296 ? 1.1786 1.4331 1.3421 -0.1785 0.0718  0.2071  316 PHE   A CZ  
1944 N  N   . ILE   A 297 ? 1.2247 1.1946 1.3008 -0.1659 0.0638  0.2755  317 ILE   A N   
1945 C  CA  . ILE   A 297 ? 1.2285 1.1567 1.2845 -0.1479 0.0623  0.2926  317 ILE   A CA  
1946 C  C   . ILE   A 297 ? 1.2900 1.1833 1.3333 -0.1683 0.0683  0.3220  317 ILE   A C   
1947 O  O   . ILE   A 297 ? 1.3447 1.2343 1.3689 -0.1579 0.0714  0.3464  317 ILE   A O   
1948 C  CB  . ILE   A 297 ? 1.2612 1.1410 1.3152 -0.1308 0.0563  0.2763  317 ILE   A CB  
1949 C  CG1 . ILE   A 297 ? 1.2262 1.1424 1.2919 -0.1035 0.0529  0.2582  317 ILE   A CG1 
1950 C  CG2 . ILE   A 297 ? 1.3138 1.1342 1.3486 -0.1196 0.0552  0.2964  317 ILE   A CG2 
1951 C  CD1 . ILE   A 297 ? 1.3966 1.2745 1.4643 -0.0840 0.0519  0.2431  317 ILE   A CD1 
1952 N  N   . MET   A 298 ? 1.2766 1.1422 1.3296 -0.1984 0.0686  0.3211  318 MET   A N   
1953 C  CA  . MET   A 298 ? 1.3537 1.1804 1.3990 -0.2218 0.0742  0.3502  318 MET   A CA  
1954 C  C   . MET   A 298 ? 1.4286 1.3074 1.4770 -0.2336 0.0884  0.3758  318 MET   A C   
1955 O  O   . MET   A 298 ? 1.3854 1.2388 1.4159 -0.2388 0.0966  0.4073  318 MET   A O   
1956 C  CB  . MET   A 298 ? 1.4313 1.2191 1.4908 -0.2548 0.0679  0.3412  318 MET   A CB  
1957 C  CG  . MET   A 298 ? 1.5340 1.2569 1.5795 -0.2425 0.0558  0.3172  318 MET   A CG  
1958 S  SD  . MET   A 298 ? 1.7118 1.3860 1.7278 -0.1991 0.0555  0.3227  318 MET   A SD  
1959 C  CE  . MET   A 298 ? 1.6077 1.2266 1.6047 -0.2131 0.0603  0.3637  318 MET   A CE  
1960 N  N   . TYR   A 299 ? 1.4132 1.3622 1.4812 -0.2363 0.0931  0.3638  319 TYR   A N   
1961 C  CA  . TYR   A 299 ? 1.3811 1.3828 1.4473 -0.2403 0.1096  0.3859  319 TYR   A CA  
1962 C  C   . TYR   A 299 ? 1.4367 1.4367 1.4644 -0.2094 0.1117  0.4010  319 TYR   A C   
1963 O  O   . TYR   A 299 ? 1.3754 1.3726 1.3819 -0.2130 0.1248  0.4326  319 TYR   A O   
1964 C  CB  . TYR   A 299 ? 1.4026 1.4768 1.4939 -0.2411 0.1129  0.3660  319 TYR   A CB  
1965 C  CG  . TYR   A 299 ? 1.4459 1.5758 1.5260 -0.2324 0.1305  0.3827  319 TYR   A CG  
1966 C  CD1 . TYR   A 299 ? 1.2734 1.4311 1.3691 -0.2569 0.1504  0.4084  319 TYR   A CD1 
1967 C  CD2 . TYR   A 299 ? 1.3214 1.4755 1.3748 -0.1996 0.1275  0.3727  319 TYR   A CD2 
1968 C  CE1 . TYR   A 299 ? 1.2912 1.4983 1.3712 -0.2456 0.1701  0.4237  319 TYR   A CE1 
1969 C  CE2 . TYR   A 299 ? 1.3111 1.5095 1.3452 -0.1891 0.1429  0.3856  319 TYR   A CE2 
1970 C  CZ  . TYR   A 299 ? 1.4159 1.6403 1.4607 -0.2105 0.1658  0.4110  319 TYR   A CZ  
1971 O  OH  . TYR   A 299 ? 1.5014 1.7687 1.5218 -0.1968 0.1848  0.4238  319 TYR   A OH  
1972 N  N   . GLU   A 300 ? 1.3123 1.3142 1.3308 -0.1792 0.0981  0.3797  320 GLU   A N   
1973 C  CA  . GLU   A 300 ? 1.3442 1.3490 1.3294 -0.1493 0.0941  0.3909  320 GLU   A CA  
1974 C  C   . GLU   A 300 ? 1.4482 1.3894 1.4083 -0.1431 0.0910  0.4168  320 GLU   A C   
1975 O  O   . GLU   A 300 ? 1.4046 1.3436 1.3307 -0.1284 0.0929  0.4405  320 GLU   A O   
1976 C  CB  . GLU   A 300 ? 1.2076 1.2328 1.1995 -0.1221 0.0783  0.3616  320 GLU   A CB  
1977 C  CG  . GLU   A 300 ? 1.3110 1.3985 1.3160 -0.1210 0.0804  0.3403  320 GLU   A CG  
1978 C  CD  . GLU   A 300 ? 1.3731 1.4981 1.3508 -0.1152 0.0906  0.3557  320 GLU   A CD  
1979 O  OE1 . GLU   A 300 ? 1.4259 1.5325 1.3684 -0.1019 0.0894  0.3780  320 GLU   A OE1 
1980 O  OE2 . GLU   A 300 ? 1.3543 1.5258 1.3429 -0.1218 0.0999  0.3455  320 GLU   A OE2 
1981 N  N   . LEU   A 301 ? 1.5588 1.4441 1.5304 -0.1520 0.0855  0.4126  321 LEU   A N   
1982 C  CA  . LEU   A 301 ? 1.6614 1.4795 1.6088 -0.1447 0.0826  0.4371  321 LEU   A CA  
1983 C  C   . LEU   A 301 ? 1.7454 1.5443 1.6763 -0.1694 0.0982  0.4742  321 LEU   A C   
1984 O  O   . LEU   A 301 ? 1.8305 1.5885 1.7293 -0.1578 0.0983  0.5029  321 LEU   A O   
1985 C  CB  . LEU   A 301 ? 1.6688 1.4269 1.6290 -0.1470 0.0742  0.4208  321 LEU   A CB  
1986 C  CG  . LEU   A 301 ? 1.4526 1.2158 1.4242 -0.1167 0.0620  0.3915  321 LEU   A CG  
1987 C  CD1 . LEU   A 301 ? 1.6291 1.3202 1.6004 -0.1132 0.0575  0.3823  321 LEU   A CD1 
1988 C  CD2 . LEU   A 301 ? 1.4129 1.1963 1.3702 -0.0815 0.0534  0.4007  321 LEU   A CD2 
1989 N  N   . ALA   A 302 ? 2.1043 1.9336 2.0584 -0.2029 0.1117  0.4763  322 ALA   A N   
1990 C  CA  . ALA   A 302 ? 2.2019 2.0175 2.1482 -0.2298 0.1298  0.5141  322 ALA   A CA  
1991 C  C   . ALA   A 302 ? 2.1828 2.0444 2.0989 -0.2162 0.1451  0.5376  322 ALA   A C   
1992 O  O   . ALA   A 302 ? 2.2357 2.0654 2.1173 -0.2146 0.1546  0.5739  322 ALA   A O   
1993 C  CB  . ALA   A 302 ? 2.1558 1.9909 2.1463 -0.2719 0.1379  0.5092  322 ALA   A CB  
1994 N  N   . THR   A 303 ? 1.7855 1.7180 1.7092 -0.2055 0.1480  0.5176  323 THR   A N   
1995 C  CA  . THR   A 303 ? 1.7972 1.7712 1.6850 -0.1889 0.1619  0.5353  323 THR   A CA  
1996 C  C   . THR   A 303 ? 1.6115 1.5575 1.4485 -0.1519 0.1469  0.5435  323 THR   A C   
1997 O  O   . THR   A 303 ? 1.7773 1.7337 1.5691 -0.1386 0.1573  0.5677  323 THR   A O   
1998 C  CB  . THR   A 303 ? 1.6399 1.6887 1.5466 -0.1829 0.1651  0.5068  323 THR   A CB  
1999 O  OG1 . THR   A 303 ? 1.6381 1.7157 1.5947 -0.2165 0.1776  0.5020  323 THR   A OG1 
2000 C  CG2 . THR   A 303 ? 1.7427 1.8319 1.6067 -0.1639 0.1805  0.5216  323 THR   A CG2 
2001 N  N   . HIS   A 304 ? 1.7672 1.6780 1.6105 -0.1343 0.1229  0.5250  324 HIS   A N   
2002 C  CA  . HIS   A 304 ? 1.7525 1.6368 1.5590 -0.0989 0.1040  0.5318  324 HIS   A CA  
2003 C  C   . HIS   A 304 ? 1.7928 1.6012 1.6011 -0.0999 0.0961  0.5453  324 HIS   A C   
2004 O  O   . HIS   A 304 ? 1.7079 1.4968 1.5379 -0.0855 0.0788  0.5224  324 HIS   A O   
2005 C  CB  . HIS   A 304 ? 1.4452 1.3657 1.2654 -0.0725 0.0822  0.4955  324 HIS   A CB  
2006 C  CG  . HIS   A 304 ? 1.5215 1.5086 1.3428 -0.0719 0.0879  0.4768  324 HIS   A CG  
2007 N  ND1 . HIS   A 304 ? 1.6225 1.6362 1.3981 -0.0576 0.0928  0.4899  324 HIS   A ND1 
2008 C  CD2 . HIS   A 304 ? 1.4079 1.4364 1.2671 -0.0822 0.0898  0.4459  324 HIS   A CD2 
2009 C  CE1 . HIS   A 304 ? 1.5074 1.5751 1.2939 -0.0585 0.0976  0.4662  324 HIS   A CE1 
2010 N  NE2 . HIS   A 304 ? 1.4295 1.5078 1.2683 -0.0735 0.0956  0.4402  324 HIS   A NE2 
2011 N  N   . PRO   A 305 ? 1.8445 1.6069 1.6281 -0.1148 0.1098  0.5836  325 PRO   A N   
2012 C  CA  . PRO   A 305 ? 1.7890 1.4703 1.5721 -0.1175 0.1032  0.5971  325 PRO   A CA  
2013 C  C   . PRO   A 305 ? 1.7863 1.4324 1.5450 -0.0762 0.0808  0.6004  325 PRO   A C   
2014 O  O   . PRO   A 305 ? 1.7291 1.3206 1.5014 -0.0701 0.0710  0.5937  325 PRO   A O   
2015 C  CB  . PRO   A 305 ? 1.7244 1.3760 1.4858 -0.1456 0.1261  0.6403  325 PRO   A CB  
2016 C  CG  . PRO   A 305 ? 1.7759 1.5048 1.5226 -0.1495 0.1456  0.6483  325 PRO   A CG  
2017 C  CD  . PRO   A 305 ? 1.7789 1.5511 1.5142 -0.1122 0.1257  0.6202  325 PRO   A CD  
2018 N  N   . ASP   A 306 ? 1.8578 1.5334 1.5817 -0.0465 0.0711  0.6091  326 ASP   A N   
2019 C  CA  . ASP   A 306 ? 1.8795 1.5333 1.5905 -0.0062 0.0452  0.6089  326 ASP   A CA  
2020 C  C   . ASP   A 306 ? 1.8240 1.4953 1.5847 0.0072  0.0295  0.5685  326 ASP   A C   
2021 O  O   . ASP   A 306 ? 1.8131 1.4465 1.5829 0.0312  0.0150  0.5675  326 ASP   A O   
2022 C  CB  . ASP   A 306 ? 1.9161 1.6088 1.5841 0.0197  0.0340  0.6190  326 ASP   A CB  
2023 C  CG  . ASP   A 306 ? 1.9359 1.7051 1.6156 0.0132  0.0375  0.5910  326 ASP   A CG  
2024 O  OD1 . ASP   A 306 ? 1.9310 1.7220 1.6169 -0.0169 0.0624  0.5921  326 ASP   A OD1 
2025 O  OD2 . ASP   A 306 ? 1.9129 1.7200 1.5973 0.0381  0.0149  0.5687  326 ASP   A OD2 
2026 N  N   . VAL   A 307 ? 1.7304 1.4595 1.5233 -0.0063 0.0337  0.5365  327 VAL   A N   
2027 C  CA  . VAL   A 307 ? 1.6809 1.4254 1.5200 0.0028  0.0236  0.5001  327 VAL   A CA  
2028 C  C   . VAL   A 307 ? 1.6625 1.3506 1.5225 -0.0142 0.0325  0.4940  327 VAL   A C   
2029 O  O   . VAL   A 307 ? 1.6556 1.3180 1.5356 0.0052  0.0237  0.4796  327 VAL   A O   
2030 C  CB  . VAL   A 307 ? 1.6337 1.4498 1.4963 -0.0074 0.0260  0.4699  327 VAL   A CB  
2031 C  CG1 . VAL   A 307 ? 1.3201 1.1472 1.2287 -0.0025 0.0203  0.4353  327 VAL   A CG1 
2032 C  CG2 . VAL   A 307 ? 1.3939 1.2577 1.2330 0.0137  0.0125  0.4712  327 VAL   A CG2 
2033 N  N   . GLN   A 308 ? 1.6274 1.2948 1.4829 -0.0503 0.0498  0.5048  328 GLN   A N   
2034 C  CA  . GLN   A 308 ? 1.6543 1.2631 1.5253 -0.0699 0.0548  0.4972  328 GLN   A CA  
2035 C  C   . GLN   A 308 ? 1.8287 1.3574 1.6801 -0.0493 0.0476  0.5154  328 GLN   A C   
2036 O  O   . GLN   A 308 ? 1.7241 1.2096 1.5892 -0.0411 0.0435  0.4969  328 GLN   A O   
2037 C  CB  . GLN   A 308 ? 1.7676 1.3705 1.6400 -0.1144 0.0716  0.5105  328 GLN   A CB  
2038 C  CG  . GLN   A 308 ? 1.7320 1.2749 1.6203 -0.1397 0.0725  0.4991  328 GLN   A CG  
2039 C  CD  . GLN   A 308 ? 1.7277 1.2792 1.6304 -0.1870 0.0856  0.5090  328 GLN   A CD  
2040 O  OE1 . GLN   A 308 ? 1.6882 1.1938 1.6045 -0.2134 0.0836  0.5003  328 GLN   A OE1 
2041 N  NE2 . GLN   A 308 ? 1.7373 1.3481 1.6376 -0.1972 0.0987  0.5271  328 GLN   A NE2 
2042 N  N   . GLN   A 309 ? 1.6874 1.1925 1.5028 -0.0384 0.0466  0.5519  329 GLN   A N   
2043 C  CA  . GLN   A 309 ? 1.7182 1.1434 1.5125 -0.0168 0.0392  0.5724  329 GLN   A CA  
2044 C  C   . GLN   A 309 ? 1.7917 1.2284 1.5991 0.0300  0.0210  0.5577  329 GLN   A C   
2045 O  O   . GLN   A 309 ? 1.7304 1.1141 1.5471 0.0479  0.0170  0.5492  329 GLN   A O   
2046 C  CB  . GLN   A 309 ? 1.8751 1.2705 1.6237 -0.0183 0.0436  0.6187  329 GLN   A CB  
2047 C  CG  . GLN   A 309 ? 1.9289 1.2354 1.6527 0.0045  0.0356  0.6429  329 GLN   A CG  
2048 C  CD  . GLN   A 309 ? 1.8834 1.1595 1.5566 0.0067  0.0392  0.6913  329 GLN   A CD  
2049 O  OE1 . GLN   A 309 ? 2.0193 1.2921 1.6769 -0.0288 0.0578  0.7141  329 GLN   A OE1 
2050 N  NE2 . GLN   A 309 ? 1.9217 1.1769 1.5700 0.0494  0.0216  0.7087  329 GLN   A NE2 
2051 N  N   . LYS   A 310 ? 1.7866 1.2918 1.5957 0.0509  0.0096  0.5549  330 LYS   A N   
2052 C  CA  . LYS   A 310 ? 1.8079 1.3358 1.6404 0.0924  -0.0093 0.5411  330 LYS   A CA  
2053 C  C   . LYS   A 310 ? 1.7629 1.2984 1.6407 0.0944  -0.0051 0.5039  330 LYS   A C   
2054 O  O   . LYS   A 310 ? 1.8316 1.3515 1.7301 0.1269  -0.0130 0.4969  330 LYS   A O   
2055 C  CB  . LYS   A 310 ? 1.8636 1.4687 1.6948 0.1061  -0.0241 0.5383  330 LYS   A CB  
2056 C  CG  . LYS   A 310 ? 1.7391 1.3862 1.6112 0.1406  -0.0439 0.5177  330 LYS   A CG  
2057 C  CD  . LYS   A 310 ? 1.7963 1.4916 1.6528 0.1620  -0.0678 0.5277  330 LYS   A CD  
2058 C  CE  . LYS   A 310 ? 1.7673 1.5108 1.6752 0.1916  -0.0891 0.5070  330 LYS   A CE  
2059 N  NZ  . LYS   A 310 ? 2.0274 1.7807 1.9203 0.2254  -0.1194 0.5277  330 LYS   A NZ  
2060 N  N   . LEU   A 311 ? 1.7469 1.3061 1.6396 0.0617  0.0080  0.4811  331 LEU   A N   
2061 C  CA  . LEU   A 311 ? 1.7532 1.3031 1.6768 0.0615  0.0142  0.4489  331 LEU   A CA  
2062 C  C   . LEU   A 311 ? 1.8462 1.3032 1.7544 0.0640  0.0195  0.4548  331 LEU   A C   
2063 O  O   . LEU   A 311 ? 1.8466 1.2773 1.7678 0.0957  0.0171  0.4452  331 LEU   A O   
2064 C  CB  . LEU   A 311 ? 1.6964 1.2863 1.6336 0.0259  0.0246  0.4257  331 LEU   A CB  
2065 C  CG  . LEU   A 311 ? 1.6882 1.2976 1.6580 0.0318  0.0280  0.3895  331 LEU   A CG  
2066 C  CD1 . LEU   A 311 ? 1.5922 1.2729 1.5908 0.0561  0.0189  0.3781  331 LEU   A CD1 
2067 C  CD2 . LEU   A 311 ? 1.5377 1.1634 1.5124 -0.0053 0.0372  0.3708  331 LEU   A CD2 
2068 N  N   . GLN   A 312 ? 1.9642 1.3692 1.8449 0.0320  0.0270  0.4724  332 GLN   A N   
2069 C  CA  . GLN   A 312 ? 1.8897 1.1963 1.7509 0.0303  0.0299  0.4787  332 GLN   A CA  
2070 C  C   . GLN   A 312 ? 1.9464 1.2085 1.7982 0.0764  0.0213  0.4937  332 GLN   A C   
2071 O  O   . GLN   A 312 ? 1.9156 1.1102 1.7635 0.0928  0.0231  0.4836  332 GLN   A O   
2072 C  CB  . GLN   A 312 ? 1.8633 1.1253 1.6974 -0.0092 0.0363  0.5065  332 GLN   A CB  
2073 C  CG  . GLN   A 312 ? 2.0096 1.2962 1.8578 -0.0572 0.0449  0.4915  332 GLN   A CG  
2074 C  CD  . GLN   A 312 ? 1.9519 1.2248 1.7838 -0.0950 0.0534  0.5255  332 GLN   A CD  
2075 O  OE1 . GLN   A 312 ? 1.8877 1.1663 1.6972 -0.0851 0.0550  0.5590  332 GLN   A OE1 
2076 N  NE2 . GLN   A 312 ? 1.9647 1.2204 1.8084 -0.1385 0.0586  0.5180  332 GLN   A NE2 
2077 N  N   . GLU   A 313 ? 2.0204 1.3180 1.8663 0.0995  0.0108  0.5177  333 GLU   A N   
2078 C  CA  . GLU   A 313 ? 2.1244 1.3902 1.9670 0.1465  -0.0008 0.5331  333 GLU   A CA  
2079 C  C   . GLU   A 313 ? 2.0495 1.3441 1.9344 0.1806  -0.0022 0.5030  333 GLU   A C   
2080 O  O   . GLU   A 313 ? 2.1034 1.3425 1.9898 0.2124  -0.0018 0.5026  333 GLU   A O   
2081 C  CB  . GLU   A 313 ? 2.1901 1.4981 2.0178 0.1633  -0.0157 0.5622  333 GLU   A CB  
2082 C  CG  . GLU   A 313 ? 2.2694 1.5264 2.0462 0.1444  -0.0130 0.6023  333 GLU   A CG  
2083 C  CD  . GLU   A 313 ? 2.2316 1.5489 1.9872 0.1465  -0.0224 0.6230  333 GLU   A CD  
2084 O  OE1 . GLU   A 313 ? 2.2407 1.5525 1.9640 0.1150  -0.0109 0.6442  333 GLU   A OE1 
2085 O  OE2 . GLU   A 313 ? 2.1826 1.5533 1.9542 0.1799  -0.0413 0.6178  333 GLU   A OE2 
2086 N  N   . GLU   A 314 ? 2.0765 1.4566 1.9962 0.1753  -0.0021 0.4784  334 GLU   A N   
2087 C  CA  . GLU   A 314 ? 2.0540 1.4688 2.0181 0.2052  -0.0004 0.4524  334 GLU   A CA  
2088 C  C   . GLU   A 314 ? 2.0943 1.4521 2.0561 0.2009  0.0169  0.4274  334 GLU   A C   
2089 O  O   . GLU   A 314 ? 2.1246 1.4650 2.1056 0.2364  0.0222  0.4166  334 GLU   A O   
2090 C  CB  . GLU   A 314 ? 1.8535 1.3674 1.8525 0.1955  -0.0041 0.4335  334 GLU   A CB  
2091 C  CG  . GLU   A 314 ? 1.8381 1.3992 1.8897 0.2276  -0.0037 0.4137  334 GLU   A CG  
2092 C  CD  . GLU   A 314 ? 1.6823 1.3256 1.7660 0.2100  -0.0027 0.3905  334 GLU   A CD  
2093 O  OE1 . GLU   A 314 ? 1.7629 1.4020 1.8378 0.1803  0.0114  0.3707  334 GLU   A OE1 
2094 O  OE2 . GLU   A 314 ? 1.5963 1.3061 1.7143 0.2261  -0.0177 0.3918  334 GLU   A OE2 
2095 N  N   . ILE   A 315 ? 2.2572 1.5859 2.1954 0.1588  0.0256  0.4178  335 ILE   A N   
2096 C  CA  . ILE   A 315 ? 2.2855 1.5578 2.2146 0.1523  0.0383  0.3912  335 ILE   A CA  
2097 C  C   . ILE   A 315 ? 2.3350 1.5047 2.2356 0.1759  0.0395  0.4015  335 ILE   A C   
2098 O  O   . ILE   A 315 ? 2.4058 1.5407 2.3095 0.2048  0.0484  0.3821  335 ILE   A O   
2099 C  CB  . ILE   A 315 ? 2.2235 1.4895 2.1362 0.1001  0.0421  0.3800  335 ILE   A CB  
2100 C  CG1 . ILE   A 315 ? 2.1504 1.5065 2.0803 0.0754  0.0382  0.3851  335 ILE   A CG1 
2101 C  CG2 . ILE   A 315 ? 2.1962 1.4455 2.1101 0.0955  0.0517  0.3436  335 ILE   A CG2 
2102 C  CD1 . ILE   A 315 ? 2.0996 1.4581 2.0207 0.0264  0.0421  0.3769  335 ILE   A CD1 
2103 N  N   . ASP   A 316 ? 2.1779 1.2950 2.0481 0.1655  0.0320  0.4328  336 ASP   A N   
2104 C  CA  . ASP   A 316 ? 2.1818 1.1925 2.0215 0.1869  0.0321  0.4441  336 ASP   A CA  
2105 C  C   . ASP   A 316 ? 2.1558 1.1710 2.0132 0.2459  0.0280  0.4548  336 ASP   A C   
2106 O  O   . ASP   A 316 ? 2.2831 1.2145 2.1216 0.2749  0.0309  0.4566  336 ASP   A O   
2107 C  CB  . ASP   A 316 ? 2.2268 1.1775 2.0293 0.1565  0.0263  0.4778  336 ASP   A CB  
2108 C  CG  . ASP   A 316 ? 2.2989 1.2422 2.0910 0.0976  0.0305  0.4689  336 ASP   A CG  
2109 O  OD1 . ASP   A 316 ? 2.2675 1.1875 2.0596 0.0843  0.0355  0.4361  336 ASP   A OD1 
2110 O  OD2 . ASP   A 316 ? 2.1948 1.1571 1.9788 0.0656  0.0290  0.4953  336 ASP   A OD2 
2111 N  N   . ALA   A 317 ? 2.1812 1.2914 2.0760 0.2648  0.0200  0.4615  337 ALA   A N   
2112 C  CA  . ALA   A 317 ? 2.1435 1.2724 2.0680 0.3206  0.0142  0.4693  337 ALA   A CA  
2113 C  C   . ALA   A 317 ? 2.1163 1.2656 2.0761 0.3475  0.0300  0.4365  337 ALA   A C   
2114 O  O   . ALA   A 317 ? 2.0752 1.1737 2.0365 0.3891  0.0371  0.4348  337 ALA   A O   
2115 C  CB  . ALA   A 317 ? 1.9017 1.1243 1.8542 0.3287  -0.0042 0.4875  337 ALA   A CB  
2116 N  N   . VAL   A 318 ? 2.0991 1.3209 2.0858 0.3258  0.0375  0.4114  338 VAL   A N   
2117 C  CA  . VAL   A 318 ? 2.0976 1.3422 2.1154 0.3488  0.0559  0.3820  338 VAL   A CA  
2118 C  C   . VAL   A 318 ? 2.0982 1.2433 2.0727 0.3476  0.0726  0.3615  338 VAL   A C   
2119 O  O   . VAL   A 318 ? 2.1570 1.2779 2.1398 0.3861  0.0888  0.3467  338 VAL   A O   
2120 C  CB  . VAL   A 318 ? 1.9774 1.3166 2.0281 0.3222  0.0590  0.3625  338 VAL   A CB  
2121 C  CG1 . VAL   A 318 ? 1.9977 1.3302 2.0528 0.3266  0.0824  0.3295  338 VAL   A CG1 
2122 C  CG2 . VAL   A 318 ? 1.9257 1.3626 2.0333 0.3430  0.0460  0.3743  338 VAL   A CG2 
2123 N  N   . LEU   A 319 ? 2.2736 1.3585 2.2009 0.3042  0.0686  0.3605  339 LEU   A N   
2124 C  CA  . LEU   A 319 ? 2.4560 1.4397 2.3364 0.2955  0.0782  0.3397  339 LEU   A CA  
2125 C  C   . LEU   A 319 ? 2.5342 1.4177 2.3713 0.2887  0.0673  0.3639  339 LEU   A C   
2126 O  O   . LEU   A 319 ? 2.5102 1.3600 2.3194 0.2410  0.0593  0.3700  339 LEU   A O   
2127 C  CB  . LEU   A 319 ? 2.1410 1.1397 2.0081 0.2465  0.0805  0.3149  339 LEU   A CB  
2128 C  CG  . LEU   A 319 ? 2.2234 1.3017 2.1232 0.2541  0.0939  0.2884  339 LEU   A CG  
2129 C  CD1 . LEU   A 319 ? 2.3209 1.4109 2.2044 0.2058  0.0925  0.2668  339 LEU   A CD1 
2130 C  CD2 . LEU   A 319 ? 2.0792 1.1216 1.9761 0.3019  0.1136  0.2690  339 LEU   A CD2 
2131 N  N   . PRO   A 320 ? 2.3533 1.1871 2.1865 0.3356  0.0674  0.3793  340 PRO   A N   
2132 C  CA  . PRO   A 320 ? 2.4547 1.1864 2.2449 0.3318  0.0571  0.4050  340 PRO   A CA  
2133 C  C   . PRO   A 320 ? 2.6015 1.2172 2.3398 0.3118  0.0617  0.3830  340 PRO   A C   
2134 O  O   . PRO   A 320 ? 2.6965 1.2955 2.4266 0.3215  0.0743  0.3477  340 PRO   A O   
2135 C  CB  . PRO   A 320 ? 2.3700 1.0881 2.1759 0.3959  0.0569  0.4225  340 PRO   A CB  
2136 C  CG  . PRO   A 320 ? 2.3401 1.1062 2.1811 0.4332  0.0753  0.3922  340 PRO   A CG  
2137 C  CD  . PRO   A 320 ? 2.3366 1.2020 2.2061 0.3957  0.0784  0.3736  340 PRO   A CD  
2138 N  N   . ASN   A 321 ? 2.7104 1.2424 2.4111 0.2831  0.0505  0.4050  341 ASN   A N   
2139 C  CA  . ASN   A 321 ? 2.7979 1.2303 2.4568 0.2511  0.0467  0.3839  341 ASN   A CA  
2140 C  C   . ASN   A 321 ? 2.7162 1.1724 2.3709 0.2111  0.0510  0.3522  341 ASN   A C   
2141 O  O   . ASN   A 321 ? 2.7557 1.1555 2.3826 0.2164  0.0562  0.3169  341 ASN   A O   
2142 C  CB  . ASN   A 321 ? 2.8342 1.2001 2.4783 0.2940  0.0496  0.3605  341 ASN   A CB  
2143 C  CG  . ASN   A 321 ? 2.7369 1.0708 2.3844 0.3232  0.0396  0.3892  341 ASN   A CG  
2144 O  OD1 . ASN   A 321 ? 2.7346 1.0998 2.3945 0.3154  0.0299  0.4271  341 ASN   A OD1 
2145 N  ND2 . ASN   A 321 ? 2.7797 1.0494 2.4128 0.3580  0.0420  0.3710  341 ASN   A ND2 
2146 N  N   . LYS   A 322 ? 2.6783 1.2303 2.3637 0.1709  0.0466  0.3628  342 LYS   A N   
2147 C  CA  . LYS   A 322 ? 2.5220 1.1302 2.2187 0.1311  0.0473  0.3348  342 LYS   A CA  
2148 C  C   . LYS   A 322 ? 2.5296 1.1393 2.2213 0.1612  0.0594  0.2936  342 LYS   A C   
2149 O  O   . LYS   A 322 ? 2.5527 1.1222 2.2176 0.1376  0.0572  0.2634  342 LYS   A O   
2150 C  CB  . LYS   A 322 ? 2.5016 1.0478 2.1732 0.0705  0.0349  0.3353  342 LYS   A CB  
2151 C  CG  . LYS   A 322 ? 2.5520 0.9530 2.1737 0.0727  0.0283  0.3306  342 LYS   A CG  
2152 C  CD  . LYS   A 322 ? 2.7478 1.1072 2.3661 0.0367  0.0177  0.3683  342 LYS   A CD  
2153 C  CE  . LYS   A 322 ? 2.7385 0.9990 2.3354 0.0353  0.0083  0.3562  342 LYS   A CE  
2154 N  NZ  . LYS   A 322 ? 2.4966 0.7287 2.1019 0.0031  0.0012  0.3931  342 LYS   A NZ  
2155 N  N   . ALA   A 323 ? 2.4582 1.1181 2.1770 0.2140  0.0722  0.2938  343 ALA   A N   
2156 C  CA  . ALA   A 323 ? 2.5425 1.2044 2.2589 0.2522  0.0896  0.2611  343 ALA   A CA  
2157 C  C   . ALA   A 323 ? 2.4195 1.1451 2.1444 0.2226  0.0934  0.2331  343 ALA   A C   
2158 O  O   . ALA   A 323 ? 2.3329 1.1297 2.0824 0.1821  0.0840  0.2421  343 ALA   A O   
2159 C  CB  . ALA   A 323 ? 2.4604 1.1888 2.2221 0.3079  0.1018  0.2742  343 ALA   A CB  
2160 N  N   . PRO   A 324 ? 2.5118 1.2131 2.2143 0.2446  0.1080  0.1996  344 PRO   A N   
2161 C  CA  . PRO   A 324 ? 2.5234 1.2790 2.2281 0.2172  0.1103  0.1742  344 PRO   A CA  
2162 C  C   . PRO   A 324 ? 2.4252 1.3021 2.1867 0.2371  0.1248  0.1780  344 PRO   A C   
2163 O  O   . PRO   A 324 ? 2.3824 1.2803 2.1674 0.2865  0.1424  0.1816  344 PRO   A O   
2164 C  CB  . PRO   A 324 ? 2.6058 1.2694 2.2511 0.2363  0.1198  0.1384  344 PRO   A CB  
2165 C  CG  . PRO   A 324 ? 2.6272 1.2246 2.2592 0.2935  0.1338  0.1444  344 PRO   A CG  
2166 C  CD  . PRO   A 324 ? 2.6218 1.2645 2.3024 0.3028  0.1275  0.1847  344 PRO   A CD  
2167 N  N   . PRO   A 325 ? 2.3691 1.3279 2.1569 0.1996  0.1174  0.1780  345 PRO   A N   
2168 C  CA  . PRO   A 325 ? 2.3059 1.3766 2.1479 0.2142  0.1286  0.1814  345 PRO   A CA  
2169 C  C   . PRO   A 325 ? 2.2615 1.3360 2.0966 0.2460  0.1525  0.1555  345 PRO   A C   
2170 O  O   . PRO   A 325 ? 2.3399 1.3612 2.1272 0.2364  0.1557  0.1289  345 PRO   A O   
2171 C  CB  . PRO   A 325 ? 2.2294 1.3637 2.0862 0.1638  0.1143  0.1827  345 PRO   A CB  
2172 C  CG  . PRO   A 325 ? 2.2357 1.2928 2.0433 0.1268  0.1013  0.1683  345 PRO   A CG  
2173 C  CD  . PRO   A 325 ? 2.3621 1.3143 2.1341 0.1424  0.0982  0.1751  345 PRO   A CD  
2174 N  N   . THR   A 326 ? 2.3337 1.4706 2.2167 0.2850  0.1692  0.1645  346 THR   A N   
2175 C  CA  . THR   A 326 ? 2.3090 1.4690 2.1987 0.3164  0.1969  0.1461  346 THR   A CA  
2176 C  C   . THR   A 326 ? 2.2192 1.4986 2.1748 0.3106  0.2006  0.1551  346 THR   A C   
2177 O  O   . THR   A 326 ? 2.0521 1.3889 2.0428 0.2866  0.1810  0.1735  346 THR   A O   
2178 C  CB  . THR   A 326 ? 2.1208 1.2384 2.0107 0.3740  0.2183  0.1481  346 THR   A CB  
2179 O  OG1 . THR   A 326 ? 2.1922 1.3216 2.1182 0.3893  0.2055  0.1770  346 THR   A OG1 
2180 C  CG2 . THR   A 326 ? 2.3599 1.3524 2.1700 0.3837  0.2229  0.1256  346 THR   A CG2 
2181 N  N   . TYR   A 327 ? 2.0964 1.4096 2.0660 0.3329  0.2267  0.1422  347 TYR   A N   
2182 C  CA  . TYR   A 327 ? 1.9878 1.4078 2.0185 0.3249  0.2310  0.1489  347 TYR   A CA  
2183 C  C   . TYR   A 327 ? 1.9307 1.4194 2.0327 0.3406  0.2217  0.1757  347 TYR   A C   
2184 O  O   . TYR   A 327 ? 1.9512 1.5074 2.0892 0.3143  0.2025  0.1870  347 TYR   A O   
2185 C  CB  . TYR   A 327 ? 2.1040 1.5402 2.1372 0.3505  0.2651  0.1339  347 TYR   A CB  
2186 C  CG  . TYR   A 327 ? 2.0216 1.5585 2.1125 0.3377  0.2705  0.1390  347 TYR   A CG  
2187 C  CD1 . TYR   A 327 ? 1.9036 1.4583 1.9739 0.2994  0.2617  0.1273  347 TYR   A CD1 
2188 C  CD2 . TYR   A 327 ? 1.9763 1.5889 2.1442 0.3640  0.2835  0.1556  347 TYR   A CD2 
2189 C  CE1 . TYR   A 327 ? 1.8434 1.4824 1.9634 0.2878  0.2661  0.1318  347 TYR   A CE1 
2190 C  CE2 . TYR   A 327 ? 1.9364 1.6355 2.1577 0.3496  0.2870  0.1600  347 TYR   A CE2 
2191 C  CZ  . TYR   A 327 ? 1.9116 1.6202 2.1062 0.3117  0.2785  0.1480  347 TYR   A CZ  
2192 O  OH  . TYR   A 327 ? 2.0042 1.7915 2.2491 0.2976  0.2813  0.1523  347 TYR   A OH  
2193 N  N   . ASP   A 328 ? 2.0272 1.4970 2.1477 0.3849  0.2333  0.1858  348 ASP   A N   
2194 C  CA  . ASP   A 328 ? 2.0058 1.5465 2.1995 0.4053  0.2242  0.2106  348 ASP   A CA  
2195 C  C   . ASP   A 328 ? 1.9980 1.5277 2.1858 0.3874  0.1903  0.2306  348 ASP   A C   
2196 O  O   . ASP   A 328 ? 1.9542 1.5554 2.1951 0.3867  0.1726  0.2491  348 ASP   A O   
2197 C  CB  . ASP   A 328 ? 1.8788 1.4065 2.0982 0.4621  0.2485  0.2157  348 ASP   A CB  
2198 C  CG  . ASP   A 328 ? 1.9529 1.4832 2.1691 0.4832  0.2875  0.1971  348 ASP   A CG  
2199 O  OD1 . ASP   A 328 ? 1.9024 1.5200 2.1819 0.4865  0.3009  0.2015  348 ASP   A OD1 
2200 O  OD2 . ASP   A 328 ? 1.8765 1.3186 2.0242 0.4958  0.3046  0.1783  348 ASP   A OD2 
2201 N  N   . THR   A 329 ? 2.0338 1.4741 2.1570 0.3726  0.1805  0.2279  349 THR   A N   
2202 C  CA  . THR   A 329 ? 2.0287 1.4572 2.1418 0.3519  0.1515  0.2492  349 THR   A CA  
2203 C  C   . THR   A 329 ? 2.0452 1.5359 2.1676 0.3058  0.1341  0.2508  349 THR   A C   
2204 O  O   . THR   A 329 ? 2.0134 1.5443 2.1566 0.2976  0.1130  0.2715  349 THR   A O   
2205 C  CB  . THR   A 329 ? 2.0686 1.3842 2.1129 0.3428  0.1470  0.2467  349 THR   A CB  
2206 O  OG1 . THR   A 329 ? 2.1145 1.3813 2.1130 0.3272  0.1607  0.2179  349 THR   A OG1 
2207 C  CG2 . THR   A 329 ? 2.1131 1.3689 2.1529 0.3909  0.1532  0.2578  349 THR   A CG2 
2208 N  N   . VAL   A 330 ? 2.0506 1.5483 2.1546 0.2780  0.1423  0.2288  350 VAL   A N   
2209 C  CA  . VAL   A 330 ? 1.9683 1.5201 2.0780 0.2359  0.1275  0.2284  350 VAL   A CA  
2210 C  C   . VAL   A 330 ? 1.8813 1.5315 2.0537 0.2428  0.1219  0.2373  350 VAL   A C   
2211 O  O   . VAL   A 330 ? 1.8976 1.5921 2.0801 0.2198  0.1025  0.2474  350 VAL   A O   
2212 C  CB  . VAL   A 330 ? 1.9150 1.4500 1.9920 0.2097  0.1372  0.2026  350 VAL   A CB  
2213 C  CG1 . VAL   A 330 ? 1.7917 1.3915 1.8827 0.1726  0.1247  0.2012  350 VAL   A CG1 
2214 C  CG2 . VAL   A 330 ? 2.0241 1.4628 2.0398 0.1951  0.1341  0.1944  350 VAL   A CG2 
2215 N  N   . LEU   A 331 ? 1.7440 1.4290 1.9595 0.2746  0.1387  0.2337  351 LEU   A N   
2216 C  CA  . LEU   A 331 ? 1.8663 1.6438 2.1485 0.2805  0.1320  0.2418  351 LEU   A CA  
2217 C  C   . LEU   A 331 ? 1.8455 1.6463 2.1626 0.3040  0.1122  0.2660  351 LEU   A C   
2218 O  O   . LEU   A 331 ? 1.7925 1.6686 2.1698 0.3123  0.1028  0.2733  351 LEU   A O   
2219 C  CB  . LEU   A 331 ? 1.7575 1.5682 2.0786 0.3019  0.1597  0.2305  351 LEU   A CB  
2220 C  CG  . LEU   A 331 ? 1.6827 1.4964 1.9799 0.2754  0.1738  0.2092  351 LEU   A CG  
2221 C  CD1 . LEU   A 331 ? 1.8280 1.5903 2.0957 0.2973  0.2061  0.1938  351 LEU   A CD1 
2222 C  CD2 . LEU   A 331 ? 1.5700 1.4714 1.9249 0.2641  0.1717  0.2097  351 LEU   A CD2 
2223 N  N   . GLN   A 332 ? 1.8338 1.5705 2.1146 0.3144  0.1038  0.2791  352 GLN   A N   
2224 C  CA  . GLN   A 332 ? 1.8206 1.5729 2.1232 0.3344  0.0807  0.3044  352 GLN   A CA  
2225 C  C   . GLN   A 332 ? 1.8618 1.6062 2.1268 0.3040  0.0553  0.3178  352 GLN   A C   
2226 O  O   . GLN   A 332 ? 1.8881 1.6739 2.1746 0.3110  0.0314  0.3357  352 GLN   A O   
2227 C  CB  . GLN   A 332 ? 1.9656 1.6505 2.2553 0.3739  0.0891  0.3144  352 GLN   A CB  
2228 C  CG  . GLN   A 332 ? 1.9285 1.6315 2.2458 0.4024  0.0654  0.3419  352 GLN   A CG  
2229 C  CD  . GLN   A 332 ? 1.9920 1.6147 2.2850 0.4392  0.0718  0.3533  352 GLN   A CD  
2230 O  OE1 . GLN   A 332 ? 2.1194 1.6909 2.3971 0.4570  0.0982  0.3385  352 GLN   A OE1 
2231 N  NE2 . GLN   A 332 ? 2.0194 1.6264 2.3040 0.4524  0.0473  0.3796  352 GLN   A NE2 
2232 N  N   . MET   A 333 ? 2.0481 1.7420 2.2580 0.2709  0.0599  0.3100  353 MET   A N   
2233 C  CA  . MET   A 333 ? 1.9572 1.6456 2.1318 0.2401  0.0417  0.3235  353 MET   A CA  
2234 C  C   . MET   A 333 ? 1.9216 1.6938 2.1226 0.2209  0.0291  0.3192  353 MET   A C   
2235 O  O   . MET   A 333 ? 1.8193 1.6145 2.0193 0.1951  0.0376  0.3002  353 MET   A O   
2236 C  CB  . MET   A 333 ? 1.9073 1.5311 2.0290 0.2074  0.0514  0.3145  353 MET   A CB  
2237 C  CG  . MET   A 333 ? 2.0353 1.5646 2.1227 0.2223  0.0597  0.3184  353 MET   A CG  
2238 S  SD  . MET   A 333 ? 2.1549 1.6112 2.1866 0.1784  0.0659  0.3059  353 MET   A SD  
2239 C  CE  . MET   A 333 ? 2.1787 1.5459 2.1879 0.2083  0.0832  0.2888  353 MET   A CE  
2240 N  N   . GLU   A 334 ? 1.7396 1.5544 1.9617 0.2348  0.0068  0.3364  354 GLU   A N   
2241 C  CA  . GLU   A 334 ? 1.6019 1.4899 1.8446 0.2186  -0.0085 0.3312  354 GLU   A CA  
2242 C  C   . GLU   A 334 ? 1.5253 1.4047 1.7185 0.1845  -0.0142 0.3352  354 GLU   A C   
2243 O  O   . GLU   A 334 ? 1.4936 1.4039 1.6867 0.1588  -0.0093 0.3184  354 GLU   A O   
2244 C  CB  . GLU   A 334 ? 1.6296 1.5647 1.9101 0.2455  -0.0342 0.3462  354 GLU   A CB  
2245 C  CG  . GLU   A 334 ? 1.7557 1.7245 2.1035 0.2761  -0.0283 0.3410  354 GLU   A CG  
2246 C  CD  . GLU   A 334 ? 1.9231 1.9631 2.3230 0.2908  -0.0576 0.3485  354 GLU   A CD  
2247 O  OE1 . GLU   A 334 ? 1.8697 1.9489 2.2633 0.2689  -0.0762 0.3434  354 GLU   A OE1 
2248 O  OE2 . GLU   A 334 ? 1.9108 1.9673 2.3585 0.3248  -0.0631 0.3588  354 GLU   A OE2 
2249 N  N   . TYR   A 335 ? 1.5790 1.4160 1.7305 0.1848  -0.0225 0.3586  355 TYR   A N   
2250 C  CA  . TYR   A 335 ? 1.4423 1.2755 1.5492 0.1544  -0.0248 0.3666  355 TYR   A CA  
2251 C  C   . TYR   A 335 ? 1.4133 1.2307 1.5063 0.1210  -0.0048 0.3488  355 TYR   A C   
2252 O  O   . TYR   A 335 ? 1.4506 1.2951 1.5280 0.0951  -0.0045 0.3456  355 TYR   A O   
2253 C  CB  . TYR   A 335 ? 1.4677 1.2460 1.5304 0.1596  -0.0307 0.3975  355 TYR   A CB  
2254 C  CG  . TYR   A 335 ? 1.4867 1.2770 1.5077 0.1370  -0.0357 0.4123  355 TYR   A CG  
2255 C  CD1 . TYR   A 335 ? 1.4980 1.3432 1.5174 0.1444  -0.0553 0.4153  355 TYR   A CD1 
2256 C  CD2 . TYR   A 335 ? 1.5576 1.3038 1.5409 0.1086  -0.0206 0.4234  355 TYR   A CD2 
2257 C  CE1 . TYR   A 335 ? 1.5811 1.4350 1.5561 0.1273  -0.0567 0.4284  355 TYR   A CE1 
2258 C  CE2 . TYR   A 335 ? 1.5123 1.2731 1.4600 0.0895  -0.0203 0.4390  355 TYR   A CE2 
2259 C  CZ  . TYR   A 335 ? 1.4869 1.3005 1.4273 0.1007  -0.0369 0.4413  355 TYR   A CZ  
2260 O  OH  . TYR   A 335 ? 1.5400 1.3659 1.4387 0.0852  -0.0335 0.4565  355 TYR   A OH  
2261 N  N   . LEU   A 336 ? 1.4219 1.1957 1.5192 0.1228  0.0111  0.3365  356 LEU   A N   
2262 C  CA  . LEU   A 336 ? 1.4960 1.2617 1.5848 0.0934  0.0257  0.3158  356 LEU   A CA  
2263 C  C   . LEU   A 336 ? 1.4621 1.2968 1.5812 0.0867  0.0259  0.2946  356 LEU   A C   
2264 O  O   . LEU   A 336 ? 1.2440 1.1049 1.3532 0.0601  0.0264  0.2880  356 LEU   A O   
2265 C  CB  . LEU   A 336 ? 1.4559 1.1587 1.5381 0.1012  0.0400  0.3042  356 LEU   A CB  
2266 C  CG  . LEU   A 336 ? 1.4688 1.1570 1.5386 0.0733  0.0515  0.2812  356 LEU   A CG  
2267 C  CD1 . LEU   A 336 ? 1.3174 0.9869 1.3582 0.0366  0.0485  0.2911  356 LEU   A CD1 
2268 C  CD2 . LEU   A 336 ? 1.6311 1.2539 1.6884 0.0877  0.0637  0.2676  356 LEU   A CD2 
2269 N  N   . ASP   A 337 ? 1.3133 1.1796 1.4724 0.1114  0.0255  0.2857  357 ASP   A N   
2270 C  CA  . ASP   A 337 ? 1.2915 1.2204 1.4827 0.1056  0.0250  0.2678  357 ASP   A CA  
2271 C  C   . ASP   A 337 ? 1.3063 1.2819 1.4910 0.0913  0.0083  0.2724  357 ASP   A C   
2272 O  O   . ASP   A 337 ? 1.0712 1.0792 1.2587 0.0726  0.0105  0.2572  357 ASP   A O   
2273 C  CB  . ASP   A 337 ? 1.2756 1.2348 1.5173 0.1353  0.0251  0.2649  357 ASP   A CB  
2274 C  CG  . ASP   A 337 ? 1.2018 1.2244 1.4807 0.1282  0.0228  0.2496  357 ASP   A CG  
2275 O  OD1 . ASP   A 337 ? 1.3342 1.3567 1.6104 0.1135  0.0383  0.2320  357 ASP   A OD1 
2276 O  OD2 . ASP   A 337 ? 1.2074 1.2771 1.5170 0.1370  0.0037  0.2553  357 ASP   A OD2 
2277 N  N   . MET   A 338 ? 1.2697 1.2461 1.4414 0.1022  -0.0085 0.2931  358 MET   A N   
2278 C  CA  . MET   A 338 ? 1.2252 1.2397 1.3805 0.0921  -0.0241 0.2973  358 MET   A CA  
2279 C  C   . MET   A 338 ? 1.2439 1.2471 1.3611 0.0624  -0.0129 0.2969  358 MET   A C   
2280 O  O   . MET   A 338 ? 1.2016 1.2433 1.3149 0.0491  -0.0156 0.2865  358 MET   A O   
2281 C  CB  . MET   A 338 ? 1.1884 1.1976 1.3277 0.1120  -0.0444 0.3214  358 MET   A CB  
2282 C  CG  . MET   A 338 ? 1.2463 1.2469 1.4193 0.1434  -0.0520 0.3294  358 MET   A CG  
2283 S  SD  . MET   A 338 ? 1.3741 1.4044 1.5505 0.1695  -0.0874 0.3480  358 MET   A SD  
2284 C  CE  . MET   A 338 ? 1.5694 1.5991 1.8052 0.2055  -0.0898 0.3524  358 MET   A CE  
2285 N  N   . VAL   A 339 ? 1.1658 1.1162 1.2572 0.0519  -0.0006 0.3083  359 VAL   A N   
2286 C  CA  . VAL   A 339 ? 1.3469 1.2902 1.4110 0.0219  0.0102  0.3106  359 VAL   A CA  
2287 C  C   . VAL   A 339 ? 1.2049 1.1713 1.2871 0.0041  0.0200  0.2845  359 VAL   A C   
2288 O  O   . VAL   A 339 ? 1.2039 1.2033 1.2796 -0.0133 0.0223  0.2790  359 VAL   A O   
2289 C  CB  . VAL   A 339 ? 1.3374 1.2155 1.3763 0.0121  0.0191  0.3290  359 VAL   A CB  
2290 C  CG1 . VAL   A 339 ? 1.2233 1.0927 1.2544 -0.0221 0.0323  0.3225  359 VAL   A CG1 
2291 C  CG2 . VAL   A 339 ? 1.2484 1.1106 1.2559 0.0197  0.0119  0.3600  359 VAL   A CG2 
2292 N  N   . VAL   A 340 ? 1.1612 1.1098 1.2639 0.0107  0.0265  0.2684  360 VAL   A N   
2293 C  CA  . VAL   A 340 ? 1.2323 1.1991 1.3479 -0.0032 0.0348  0.2445  360 VAL   A CA  
2294 C  C   . VAL   A 340 ? 1.1728 1.2007 1.3071 -0.0013 0.0277  0.2332  360 VAL   A C   
2295 O  O   . VAL   A 340 ? 1.0664 1.1191 1.1965 -0.0189 0.0304  0.2232  360 VAL   A O   
2296 C  CB  . VAL   A 340 ? 1.2568 1.1925 1.3851 0.0091  0.0442  0.2306  360 VAL   A CB  
2297 C  CG1 . VAL   A 340 ? 1.3540 1.2899 1.4792 -0.0095 0.0527  0.2099  360 VAL   A CG1 
2298 C  CG2 . VAL   A 340 ? 1.3616 1.2312 1.4701 0.0156  0.0478  0.2425  360 VAL   A CG2 
2299 N  N   . ASN   A 341 ? 1.2147 1.2667 1.3718 0.0204  0.0170  0.2344  361 ASN   A N   
2300 C  CA  . ASN   A 341 ? 1.0693 1.1732 1.2454 0.0214  0.0073  0.2223  361 ASN   A CA  
2301 C  C   . ASN   A 341 ? 1.0375 1.1638 1.1855 0.0101  -0.0001 0.2270  361 ASN   A C   
2302 O  O   . ASN   A 341 ? 0.9823 1.1381 1.1319 0.0001  0.0002  0.2125  361 ASN   A O   
2303 C  CB  . ASN   A 341 ? 1.0673 1.1927 1.2763 0.0448  -0.0069 0.2255  361 ASN   A CB  
2304 C  CG  . ASN   A 341 ? 1.0449 1.1605 1.2895 0.0582  0.0047  0.2191  361 ASN   A CG  
2305 O  OD1 . ASN   A 341 ? 1.0756 1.1805 1.3221 0.0495  0.0214  0.2054  361 ASN   A OD1 
2306 N  ND2 . ASN   A 341 ? 0.9598 1.0802 1.2319 0.0813  -0.0038 0.2295  361 ASN   A ND2 
2307 N  N   . GLU   A 342 ? 1.1202 1.2306 1.2394 0.0133  -0.0053 0.2480  362 GLU   A N   
2308 C  CA  . GLU   A 342 ? 1.0924 1.2234 1.1795 0.0061  -0.0091 0.2546  362 GLU   A CA  
2309 C  C   . GLU   A 342 ? 1.1095 1.2431 1.1850 -0.0179 0.0082  0.2501  362 GLU   A C   
2310 O  O   . GLU   A 342 ? 1.1847 1.3501 1.2486 -0.0234 0.0088  0.2435  362 GLU   A O   
2311 C  CB  . GLU   A 342 ? 1.0971 1.2058 1.1515 0.0157  -0.0157 0.2815  362 GLU   A CB  
2312 C  CG  . GLU   A 342 ? 1.2298 1.3523 1.2417 0.0085  -0.0130 0.2929  362 GLU   A CG  
2313 C  CD  . GLU   A 342 ? 1.1844 1.3462 1.1858 0.0198  -0.0298 0.2803  362 GLU   A CD  
2314 O  OE1 . GLU   A 342 ? 1.1785 1.3626 1.2125 0.0255  -0.0417 0.2591  362 GLU   A OE1 
2315 O  OE2 . GLU   A 342 ? 1.2013 1.3690 1.1592 0.0227  -0.0307 0.2920  362 GLU   A OE2 
2316 N  N   . THR   A 343 ? 1.0794 1.1796 1.1585 -0.0315 0.0211  0.2529  363 THR   A N   
2317 C  CA  . THR   A 343 ? 1.0849 1.1922 1.1635 -0.0552 0.0338  0.2461  363 THR   A CA  
2318 C  C   . THR   A 343 ? 0.9758 1.1157 1.0756 -0.0561 0.0330  0.2205  363 THR   A C   
2319 O  O   . THR   A 343 ? 0.7994 0.9705 0.8961 -0.0655 0.0368  0.2141  363 THR   A O   
2320 C  CB  . THR   A 343 ? 1.0748 1.1351 1.1544 -0.0696 0.0423  0.2506  363 THR   A CB  
2321 O  OG1 . THR   A 343 ? 1.2207 1.2398 1.2847 -0.0615 0.0403  0.2722  363 THR   A OG1 
2322 C  CG2 . THR   A 343 ? 1.1364 1.2043 1.2129 -0.0972 0.0521  0.2540  363 THR   A CG2 
2323 N  N   . LEU   A 344 ? 1.1015 1.2341 1.2231 -0.0448 0.0296  0.2070  364 LEU   A N   
2324 C  CA  . LEU   A 344 ? 1.0709 1.2289 1.2114 -0.0451 0.0298  0.1852  364 LEU   A CA  
2325 C  C   . LEU   A 344 ? 1.0184 1.2164 1.1600 -0.0372 0.0192  0.1789  364 LEU   A C   
2326 O  O   . LEU   A 344 ? 0.9581 1.1780 1.1081 -0.0410 0.0198  0.1628  364 LEU   A O   
2327 C  CB  . LEU   A 344 ? 0.9932 1.1335 1.1560 -0.0336 0.0320  0.1762  364 LEU   A CB  
2328 C  CG  . LEU   A 344 ? 0.9369 1.0342 1.0922 -0.0412 0.0431  0.1740  364 LEU   A CG  
2329 C  CD1 . LEU   A 344 ? 0.8707 0.9500 1.0431 -0.0246 0.0490  0.1667  364 LEU   A CD1 
2330 C  CD2 . LEU   A 344 ? 0.7459 0.8493 0.8939 -0.0605 0.0475  0.1620  364 LEU   A CD2 
2331 N  N   . ARG   A 345 ? 0.8594 1.0634 0.9895 -0.0253 0.0076  0.1905  365 ARG   A N   
2332 C  CA  . ARG   A 345 ? 1.0054 1.2412 1.1250 -0.0190 -0.0043 0.1836  365 ARG   A CA  
2333 C  C   . ARG   A 345 ? 1.0284 1.2793 1.1217 -0.0298 0.0059  0.1845  365 ARG   A C   
2334 O  O   . ARG   A 345 ? 0.9261 1.2008 1.0197 -0.0303 0.0050  0.1687  365 ARG   A O   
2335 C  CB  . ARG   A 345 ? 0.9724 1.2074 1.0783 -0.0030 -0.0218 0.1964  365 ARG   A CB  
2336 C  CG  . ARG   A 345 ? 0.9068 1.1688 1.0041 0.0060  -0.0406 0.1842  365 ARG   A CG  
2337 C  CD  . ARG   A 345 ? 0.9606 1.2199 1.0258 0.0203  -0.0582 0.1986  365 ARG   A CD  
2338 N  NE  . ARG   A 345 ? 1.2042 1.4481 1.2281 0.0166  -0.0441 0.2198  365 ARG   A NE  
2339 C  CZ  . ARG   A 345 ? 1.1487 1.4028 1.1291 0.0172  -0.0396 0.2230  365 ARG   A CZ  
2340 N  NH1 . ARG   A 345 ? 1.1748 1.4505 1.1422 0.0228  -0.0494 0.2039  365 ARG   A NH1 
2341 N  NH2 . ARG   A 345 ? 1.2650 1.5051 1.2132 0.0126  -0.0237 0.2464  365 ARG   A NH2 
2342 N  N   . LEU   A 346 ? 1.0625 1.2996 1.1355 -0.0383 0.0168  0.2039  366 LEU   A N   
2343 C  CA  . LEU   A 346 ? 1.0767 1.3339 1.1311 -0.0485 0.0299  0.2085  366 LEU   A CA  
2344 C  C   . LEU   A 346 ? 1.0195 1.2871 1.0969 -0.0644 0.0407  0.1958  366 LEU   A C   
2345 O  O   . LEU   A 346 ? 0.9671 1.2645 1.0410 -0.0671 0.0477  0.1898  366 LEU   A O   
2346 C  CB  . LEU   A 346 ? 1.1375 1.3772 1.1687 -0.0556 0.0401  0.2363  366 LEU   A CB  
2347 C  CG  . LEU   A 346 ? 1.2001 1.4371 1.1934 -0.0391 0.0322  0.2520  366 LEU   A CG  
2348 C  CD1 . LEU   A 346 ? 1.3797 1.5926 1.3511 -0.0480 0.0449  0.2828  366 LEU   A CD1 
2349 C  CD2 . LEU   A 346 ? 1.1325 1.4033 1.1000 -0.0291 0.0317  0.2424  366 LEU   A CD2 
2350 N  N   . PHE   A 347 ? 1.0599 1.3027 1.1585 -0.0727 0.0416  0.1914  367 PHE   A N   
2351 C  CA  . PHE   A 347 ? 1.0287 1.2750 1.1441 -0.0885 0.0488  0.1813  367 PHE   A CA  
2352 C  C   . PHE   A 347 ? 1.0095 1.2425 1.1423 -0.0834 0.0435  0.1626  367 PHE   A C   
2353 O  O   . PHE   A 347 ? 0.9875 1.1885 1.1254 -0.0898 0.0456  0.1616  367 PHE   A O   
2354 C  CB  . PHE   A 347 ? 0.9919 1.2138 1.1070 -0.1082 0.0566  0.1970  367 PHE   A CB  
2355 C  CG  . PHE   A 347 ? 1.0244 1.2565 1.1234 -0.1145 0.0654  0.2202  367 PHE   A CG  
2356 C  CD1 . PHE   A 347 ? 1.1285 1.4041 1.2244 -0.1154 0.0738  0.2217  367 PHE   A CD1 
2357 C  CD2 . PHE   A 347 ? 1.0267 1.2235 1.1117 -0.1175 0.0670  0.2417  367 PHE   A CD2 
2358 C  CE1 . PHE   A 347 ? 1.0042 1.2904 1.0828 -0.1198 0.0862  0.2452  367 PHE   A CE1 
2359 C  CE2 . PHE   A 347 ? 1.3125 1.5166 1.3796 -0.1235 0.0774  0.2661  367 PHE   A CE2 
2360 C  CZ  . PHE   A 347 ? 1.1388 1.3889 1.2023 -0.1249 0.0882  0.2683  367 PHE   A CZ  
2361 N  N   . PRO   A 348 ? 0.9744 1.2283 1.1141 -0.0718 0.0375  0.1475  368 PRO   A N   
2362 C  CA  . PRO   A 348 ? 0.9819 1.2261 1.1381 -0.0689 0.0365  0.1318  368 PRO   A CA  
2363 C  C   . PRO   A 348 ? 0.9542 1.2047 1.1128 -0.0806 0.0412  0.1220  368 PRO   A C   
2364 O  O   . PRO   A 348 ? 1.0545 1.3332 1.2139 -0.0792 0.0401  0.1140  368 PRO   A O   
2365 C  CB  . PRO   A 348 ? 1.0359 1.3001 1.1995 -0.0553 0.0273  0.1221  368 PRO   A CB  
2366 C  CG  . PRO   A 348 ? 0.9925 1.2821 1.1376 -0.0532 0.0243  0.1249  368 PRO   A CG  
2367 C  CD  . PRO   A 348 ? 0.9970 1.2800 1.1261 -0.0609 0.0315  0.1441  368 PRO   A CD  
2368 N  N   . ILE   A 349 ? 1.0260 1.2480 1.1839 -0.0905 0.0446  0.1220  369 ILE   A N   
2369 C  CA  . ILE   A 349 ? 1.0443 1.2709 1.2031 -0.1039 0.0448  0.1150  369 ILE   A CA  
2370 C  C   . ILE   A 349 ? 0.8909 1.1333 1.0543 -0.0966 0.0424  0.0991  369 ILE   A C   
2371 O  O   . ILE   A 349 ? 1.1541 1.4130 1.3203 -0.1039 0.0401  0.0937  369 ILE   A O   
2372 C  CB  . ILE   A 349 ? 1.0000 1.1831 1.1508 -0.1141 0.0448  0.1147  369 ILE   A CB  
2373 C  CG1 . ILE   A 349 ? 0.9114 1.0606 1.0573 -0.0992 0.0484  0.1115  369 ILE   A CG1 
2374 C  CG2 . ILE   A 349 ? 1.0406 1.2123 1.1889 -0.1299 0.0456  0.1307  369 ILE   A CG2 
2375 C  CD1 . ILE   A 349 ? 1.0330 1.1349 1.1630 -0.1035 0.0496  0.1052  369 ILE   A CD1 
2376 N  N   . ALA   A 350 ? 0.9411 1.1795 1.1083 -0.0825 0.0424  0.0927  370 ALA   A N   
2377 C  CA  . ALA   A 350 ? 0.9427 1.1906 1.1131 -0.0762 0.0410  0.0798  370 ALA   A CA  
2378 C  C   . ALA   A 350 ? 0.8892 1.1718 1.0625 -0.0710 0.0367  0.0763  370 ALA   A C   
2379 O  O   . ALA   A 350 ? 0.8447 1.1391 1.0180 -0.0688 0.0349  0.0673  370 ALA   A O   
2380 C  CB  . ALA   A 350 ? 0.8482 1.0785 1.0260 -0.0656 0.0444  0.0762  370 ALA   A CB  
2381 N  N   . MET   A 351 ? 0.7743 1.0701 0.9461 -0.0664 0.0345  0.0828  371 MET   A N   
2382 C  CA  . MET   A 351 ? 0.9726 1.2967 1.1377 -0.0594 0.0315  0.0797  371 MET   A CA  
2383 C  C   . MET   A 351 ? 0.9283 1.2526 1.0967 -0.0482 0.0241  0.0662  371 MET   A C   
2384 O  O   . MET   A 351 ? 0.7904 1.1265 0.9497 -0.0394 0.0175  0.0622  371 MET   A O   
2385 C  CB  . MET   A 351 ? 1.0833 1.4312 1.2480 -0.0647 0.0364  0.0794  371 MET   A CB  
2386 C  CG  . MET   A 351 ? 1.1723 1.5372 1.3326 -0.0724 0.0435  0.0945  371 MET   A CG  
2387 S  SD  . MET   A 351 ? 1.6313 2.0316 1.8057 -0.0809 0.0501  0.0961  371 MET   A SD  
2388 C  CE  . MET   A 351 ? 1.4056 1.7818 1.5912 -0.0907 0.0421  0.0868  371 MET   A CE  
2389 N  N   . ARG   A 352 ? 0.8803 1.1883 1.0589 -0.0487 0.0249  0.0593  372 ARG   A N   
2390 C  CA  . ARG   A 352 ? 0.7777 1.0819 0.9623 -0.0413 0.0190  0.0482  372 ARG   A CA  
2391 C  C   . ARG   A 352 ? 0.7248 1.0061 0.9241 -0.0434 0.0239  0.0489  372 ARG   A C   
2392 O  O   . ARG   A 352 ? 0.8174 1.0841 1.0147 -0.0481 0.0324  0.0541  372 ARG   A O   
2393 C  CB  . ARG   A 352 ? 0.8613 1.1751 1.0374 -0.0366 0.0185  0.0385  372 ARG   A CB  
2394 C  CG  . ARG   A 352 ? 0.9758 1.3158 1.1387 -0.0304 0.0176  0.0368  372 ARG   A CG  
2395 C  CD  . ARG   A 352 ? 1.0771 1.4234 1.2352 -0.0205 0.0160  0.0255  372 ARG   A CD  
2396 N  NE  . ARG   A 352 ? 1.0109 1.3785 1.1541 -0.0084 0.0158  0.0206  372 ARG   A NE  
2397 C  CZ  . ARG   A 352 ? 1.0166 1.3945 1.1540 0.0043  0.0164  0.0114  372 ARG   A CZ  
2398 N  NH1 . ARG   A 352 ? 1.1051 1.4738 1.2505 0.0060  0.0149  0.0070  372 ARG   A NH1 
2399 N  NH2 . ARG   A 352 ? 1.1640 1.5601 1.2841 0.0180  0.0191  0.0070  372 ARG   A NH2 
2400 N  N   . LEU   A 353 ? 0.7282 1.0051 0.9416 -0.0398 0.0188  0.0435  373 LEU   A N   
2401 C  CA  . LEU   A 353 ? 0.7646 1.0234 0.9941 -0.0410 0.0268  0.0450  373 LEU   A CA  
2402 C  C   . LEU   A 353 ? 0.7448 0.9971 0.9743 -0.0388 0.0231  0.0362  373 LEU   A C   
2403 O  O   . LEU   A 353 ? 0.7358 0.9954 0.9658 -0.0360 0.0103  0.0284  373 LEU   A O   
2404 C  CB  . LEU   A 353 ? 0.8134 1.0736 1.0720 -0.0410 0.0261  0.0519  373 LEU   A CB  
2405 C  CG  . LEU   A 353 ? 0.8459 1.1099 1.1051 -0.0400 0.0271  0.0614  373 LEU   A CG  
2406 C  CD1 . LEU   A 353 ? 0.7789 1.0525 1.0709 -0.0370 0.0199  0.0671  373 LEU   A CD1 
2407 C  CD2 . LEU   A 353 ? 0.5872 0.8309 0.8354 -0.0409 0.0433  0.0667  373 LEU   A CD2 
2408 N  N   . GLU   A 354 ? 0.6557 0.8896 0.8798 -0.0389 0.0337  0.0375  374 GLU   A N   
2409 C  CA  . GLU   A 354 ? 0.7402 0.9622 0.9583 -0.0358 0.0312  0.0312  374 GLU   A CA  
2410 C  C   . GLU   A 354 ? 0.7608 0.9604 0.9906 -0.0381 0.0441  0.0382  374 GLU   A C   
2411 O  O   . GLU   A 354 ? 0.7870 0.9766 1.0131 -0.0385 0.0587  0.0460  374 GLU   A O   
2412 C  CB  . GLU   A 354 ? 0.8498 1.0722 1.0404 -0.0308 0.0303  0.0269  374 GLU   A CB  
2413 C  CG  . GLU   A 354 ? 0.8924 1.1395 1.0748 -0.0261 0.0200  0.0199  374 GLU   A CG  
2414 C  CD  . GLU   A 354 ? 1.0386 1.2944 1.2047 -0.0216 0.0196  0.0178  374 GLU   A CD  
2415 O  OE1 . GLU   A 354 ? 1.1356 1.3743 1.2922 -0.0221 0.0237  0.0206  374 GLU   A OE1 
2416 O  OE2 . GLU   A 354 ? 1.0229 1.3038 1.1857 -0.0167 0.0152  0.0141  374 GLU   A OE2 
2417 N  N   . ARG   A 355 ? 0.7070 0.8963 0.9490 -0.0393 0.0395  0.0356  375 ARG   A N   
2418 C  CA  . ARG   A 355 ? 0.9406 1.1073 1.1927 -0.0422 0.0535  0.0443  375 ARG   A CA  
2419 C  C   . ARG   A 355 ? 0.8596 1.0058 1.0987 -0.0394 0.0463  0.0388  375 ARG   A C   
2420 O  O   . ARG   A 355 ? 0.7499 0.8996 0.9925 -0.0386 0.0290  0.0280  375 ARG   A O   
2421 C  CB  . ARG   A 355 ? 0.8247 0.9996 1.1230 -0.0509 0.0571  0.0520  375 ARG   A CB  
2422 C  CG  . ARG   A 355 ? 0.7817 0.9763 1.0983 -0.0508 0.0635  0.0585  375 ARG   A CG  
2423 C  CD  . ARG   A 355 ? 0.7635 0.9439 1.0679 -0.0462 0.0891  0.0691  375 ARG   A CD  
2424 N  NE  . ARG   A 355 ? 0.9019 1.0968 1.2251 -0.0435 0.0962  0.0751  375 ARG   A NE  
2425 C  CZ  . ARG   A 355 ? 0.8894 1.0910 1.1950 -0.0401 0.0890  0.0713  375 ARG   A CZ  
2426 N  NH1 . ARG   A 355 ? 0.9774 1.1780 1.2502 -0.0403 0.0761  0.0621  375 ARG   A NH1 
2427 N  NH2 . ARG   A 355 ? 0.6276 0.8375 0.9515 -0.0361 0.0958  0.0782  375 ARG   A NH2 
2428 N  N   . VAL   A 356 ? 0.8916 1.0123 1.1110 -0.0360 0.0594  0.0462  376 VAL   A N   
2429 C  CA  . VAL   A 356 ? 0.9968 1.0907 1.2049 -0.0327 0.0547  0.0447  376 VAL   A CA  
2430 C  C   . VAL   A 356 ? 0.9693 1.0488 1.2131 -0.0448 0.0608  0.0535  376 VAL   A C   
2431 O  O   . VAL   A 356 ? 0.8703 0.9440 1.1277 -0.0501 0.0818  0.0685  376 VAL   A O   
2432 C  CB  . VAL   A 356 ? 0.9810 1.0515 1.1490 -0.0228 0.0638  0.0505  376 VAL   A CB  
2433 C  CG1 . VAL   A 356 ? 0.8361 0.8739 0.9930 -0.0184 0.0599  0.0519  376 VAL   A CG1 
2434 C  CG2 . VAL   A 356 ? 0.8668 0.9560 1.0088 -0.0134 0.0531  0.0412  376 VAL   A CG2 
2435 N  N   . CYS   A 357 ? 1.0122 1.0858 1.2719 -0.0493 0.0428  0.0440  377 CYS   A N   
2436 C  CA  . CYS   A 357 ? 1.0687 1.1267 1.3668 -0.0642 0.0438  0.0514  377 CYS   A CA  
2437 C  C   . CYS   A 357 ? 1.0161 1.0333 1.2959 -0.0628 0.0573  0.0632  377 CYS   A C   
2438 O  O   . CYS   A 357 ? 0.9838 0.9743 1.2343 -0.0536 0.0458  0.0552  377 CYS   A O   
2439 C  CB  . CYS   A 357 ? 1.0201 1.0773 1.3330 -0.0691 0.0158  0.0346  377 CYS   A CB  
2440 S  SG  . CYS   A 357 ? 1.0608 1.0821 1.4090 -0.0873 0.0094  0.0395  377 CYS   A SG  
2441 N  N   . LYS   A 358 ? 0.9593 0.9702 1.2545 -0.0699 0.0831  0.0834  378 LYS   A N   
2442 C  CA  . LYS   A 358 ? 1.1682 1.1401 1.4338 -0.0652 0.1011  0.0985  378 LYS   A CA  
2443 C  C   . LYS   A 358 ? 1.2472 1.1869 1.5402 -0.0799 0.1022  0.1086  378 LYS   A C   
2444 O  O   . LYS   A 358 ? 1.1464 1.0506 1.4173 -0.0777 0.1204  0.1256  378 LYS   A O   
2445 C  CB  . LYS   A 358 ? 1.0069 0.9834 1.2618 -0.0615 0.1323  0.1158  378 LYS   A CB  
2446 C  CG  . LYS   A 358 ? 1.1709 1.1637 1.4813 -0.0766 0.1543  0.1329  378 LYS   A CG  
2447 C  CD  . LYS   A 358 ? 1.1284 1.1126 1.4139 -0.0678 0.1898  0.1511  378 LYS   A CD  
2448 C  CE  . LYS   A 358 ? 1.1538 1.1715 1.4442 -0.0609 0.1964  0.1461  378 LYS   A CE  
2449 N  NZ  . LYS   A 358 ? 1.1220 1.1474 1.4359 -0.0610 0.2331  0.1663  378 LYS   A NZ  
2450 N  N   . LYS   A 359 ? 1.1349 1.0826 1.4724 -0.0951 0.0820  0.0992  379 LYS   A N   
2451 C  CA  . LYS   A 359 ? 1.1343 1.0446 1.4948 -0.1104 0.0755  0.1045  379 LYS   A CA  
2452 C  C   . LYS   A 359 ? 1.2370 1.1570 1.6314 -0.1222 0.0422  0.0841  379 LYS   A C   
2453 O  O   . LYS   A 359 ? 1.2124 1.1733 1.6228 -0.1217 0.0300  0.0722  379 LYS   A O   
2454 C  CB  . LYS   A 359 ? 1.1492 1.0557 1.5527 -0.1287 0.1051  0.1331  379 LYS   A CB  
2455 C  CG  . LYS   A 359 ? 1.1725 1.1295 1.6428 -0.1439 0.1122  0.1396  379 LYS   A CG  
2456 C  CD  . LYS   A 359 ? 1.1822 1.1397 1.6875 -0.1555 0.1507  0.1712  379 LYS   A CD  
2457 C  CE  . LYS   A 359 ? 1.1679 1.1774 1.7544 -0.1720 0.1562  0.1794  379 LYS   A CE  
2458 N  NZ  . LYS   A 359 ? 1.2476 1.2665 1.8635 -0.1766 0.2015  0.2111  379 LYS   A NZ  
2459 N  N   . ASP   A 360 ? 1.3223 1.1992 1.7233 -0.1325 0.0265  0.0802  380 ASP   A N   
2460 C  CA  . ASP   A 360 ? 1.1971 1.0718 1.6238 -0.1444 -0.0084 0.0590  380 ASP   A CA  
2461 C  C   . ASP   A 360 ? 1.1720 1.0923 1.6684 -0.1663 -0.0117 0.0647  380 ASP   A C   
2462 O  O   . ASP   A 360 ? 1.2164 1.1518 1.7597 -0.1817 0.0129  0.0894  380 ASP   A O   
2463 C  CB  . ASP   A 360 ? 1.1850 0.9983 1.6134 -0.1562 -0.0219 0.0577  380 ASP   A CB  
2464 C  CG  . ASP   A 360 ? 1.3937 1.1623 1.7542 -0.1306 -0.0322 0.0422  380 ASP   A CG  
2465 O  OD1 . ASP   A 360 ? 1.4126 1.1974 1.7283 -0.1056 -0.0212 0.0405  380 ASP   A OD1 
2466 O  OD2 . ASP   A 360 ? 1.5527 1.2695 1.9068 -0.1355 -0.0528 0.0313  380 ASP   A OD2 
2467 N  N   . VAL   A 361 ? 1.2215 1.1640 1.7242 -0.1659 -0.0426 0.0422  381 VAL   A N   
2468 C  CA  . VAL   A 361 ? 1.3009 1.2931 1.8630 -0.1805 -0.0512 0.0447  381 VAL   A CA  
2469 C  C   . VAL   A 361 ? 1.3569 1.3499 1.9173 -0.1829 -0.0949 0.0171  381 VAL   A C   
2470 O  O   . VAL   A 361 ? 1.2885 1.2605 1.7890 -0.1639 -0.1112 -0.0052 381 VAL   A O   
2471 C  CB  . VAL   A 361 ? 1.3308 1.3706 1.8860 -0.1653 -0.0272 0.0543  381 VAL   A CB  
2472 C  CG1 . VAL   A 361 ? 1.3245 1.4090 1.9102 -0.1678 -0.0479 0.0455  381 VAL   A CG1 
2473 C  CG2 . VAL   A 361 ? 1.2641 1.3171 1.8563 -0.1734 0.0113  0.0842  381 VAL   A CG2 
2474 N  N   . GLU   A 362 ? 1.6036 1.6214 2.2296 -0.2053 -0.1141 0.0189  382 GLU   A N   
2475 C  CA  . GLU   A 362 ? 1.6113 1.6377 2.2387 -0.2078 -0.1573 -0.0054 382 GLU   A CA  
2476 C  C   . GLU   A 362 ? 1.5470 1.6374 2.2195 -0.2091 -0.1568 0.0041  382 GLU   A C   
2477 O  O   . GLU   A 362 ? 1.5884 1.7077 2.3390 -0.2307 -0.1564 0.0204  382 GLU   A O   
2478 C  CB  . GLU   A 362 ? 1.6793 1.6712 2.3457 -0.2350 -0.1899 -0.0142 382 GLU   A CB  
2479 C  CG  . GLU   A 362 ? 1.6923 1.6734 2.3397 -0.2352 -0.2406 -0.0454 382 GLU   A CG  
2480 C  CD  . GLU   A 362 ? 1.8958 1.8065 2.5211 -0.2455 -0.2695 -0.0659 382 GLU   A CD  
2481 O  OE1 . GLU   A 362 ? 1.9990 1.8779 2.6558 -0.2646 -0.2564 -0.0509 382 GLU   A OE1 
2482 O  OE2 . GLU   A 362 ? 1.9627 1.8464 2.5369 -0.2340 -0.3048 -0.0966 382 GLU   A OE2 
2483 N  N   . ILE   A 363 ? 1.4684 1.5817 2.0953 -0.1858 -0.1563 -0.0043 383 ILE   A N   
2484 C  CA  . ILE   A 363 ? 1.3642 1.5313 2.0235 -0.1830 -0.1600 0.0026  383 ILE   A CA  
2485 C  C   . ILE   A 363 ? 1.3859 1.5552 2.0256 -0.1798 -0.2051 -0.0210 383 ILE   A C   
2486 O  O   . ILE   A 363 ? 1.3911 1.5287 1.9617 -0.1652 -0.2200 -0.0430 383 ILE   A O   
2487 C  CB  . ILE   A 363 ? 1.4085 1.5984 2.0337 -0.1610 -0.1262 0.0136  383 ILE   A CB  
2488 C  CG1 . ILE   A 363 ? 1.2289 1.4053 1.7741 -0.1383 -0.1349 -0.0056 383 ILE   A CG1 
2489 C  CG2 . ILE   A 363 ? 1.3749 1.5575 2.0078 -0.1615 -0.0840 0.0346  383 ILE   A CG2 
2490 C  CD1 . ILE   A 363 ? 0.9357 1.1226 1.4452 -0.1207 -0.1014 0.0046  383 ILE   A CD1 
2491 N  N   . ASN   A 364 ? 1.2696 1.4762 1.9704 -0.1924 -0.2269 -0.0160 384 ASN   A N   
2492 C  CA  . ASN   A 364 ? 1.2808 1.4973 1.9655 -0.1876 -0.2702 -0.0344 384 ASN   A CA  
2493 C  C   . ASN   A 364 ? 1.4289 1.5925 2.0543 -0.1860 -0.3042 -0.0647 384 ASN   A C   
2494 O  O   . ASN   A 364 ? 1.4762 1.6307 2.0361 -0.1670 -0.3232 -0.0833 384 ASN   A O   
2495 C  CB  . ASN   A 364 ? 1.2786 1.5231 1.9208 -0.1623 -0.2586 -0.0310 384 ASN   A CB  
2496 C  CG  . ASN   A 364 ? 1.1584 1.4545 1.8633 -0.1630 -0.2375 -0.0051 384 ASN   A CG  
2497 O  OD1 . ASN   A 364 ? 1.1438 1.4478 1.8506 -0.1563 -0.1958 0.0120  384 ASN   A OD1 
2498 N  ND2 . ASN   A 364 ? 1.1904 1.5204 1.9455 -0.1694 -0.2677 -0.0028 384 ASN   A ND2 
2499 N  N   . GLY   A 365 ? 1.4556 1.5806 2.1012 -0.2051 -0.3102 -0.0690 385 GLY   A N   
2500 C  CA  . GLY   A 365 ? 1.4543 1.5220 2.0490 -0.2050 -0.3444 -0.0988 385 GLY   A CA  
2501 C  C   . GLY   A 365 ? 1.5096 1.5347 2.0180 -0.1799 -0.3254 -0.1119 385 GLY   A C   
2502 O  O   . GLY   A 365 ? 1.5297 1.5057 1.9853 -0.1731 -0.3523 -0.1390 385 GLY   A O   
2503 N  N   . MET   A 366 ? 1.5837 1.6252 2.0756 -0.1648 -0.2814 -0.0946 386 MET   A N   
2504 C  CA  . MET   A 366 ? 1.5482 1.5565 1.9679 -0.1410 -0.2626 -0.1043 386 MET   A CA  
2505 C  C   . MET   A 366 ? 1.4937 1.4887 1.9319 -0.1461 -0.2265 -0.0842 386 MET   A C   
2506 O  O   . MET   A 366 ? 1.4399 1.4708 1.9137 -0.1502 -0.1966 -0.0595 386 MET   A O   
2507 C  CB  . MET   A 366 ? 1.5251 1.5643 1.8932 -0.1139 -0.2477 -0.1053 386 MET   A CB  
2508 C  CG  . MET   A 366 ? 1.5030 1.5125 1.8000 -0.0883 -0.2344 -0.1183 386 MET   A CG  
2509 S  SD  . MET   A 366 ? 1.6420 1.6822 1.8755 -0.0584 -0.2261 -0.1249 386 MET   A SD  
2510 C  CE  . MET   A 366 ? 1.5711 1.6663 1.8525 -0.0709 -0.2282 -0.1060 386 MET   A CE  
2511 N  N   . PHE   A 367 ? 1.3720 1.3119 1.7807 -0.1435 -0.2296 -0.0949 387 PHE   A N   
2512 C  CA  . PHE   A 367 ? 1.3218 1.2413 1.7332 -0.1436 -0.1971 -0.0767 387 PHE   A CA  
2513 C  C   . PHE   A 367 ? 1.3248 1.2621 1.6861 -0.1153 -0.1685 -0.0724 387 PHE   A C   
2514 O  O   . PHE   A 367 ? 1.4124 1.3544 1.7225 -0.0928 -0.1764 -0.0900 387 PHE   A O   
2515 C  CB  . PHE   A 367 ? 1.2851 1.1353 1.6771 -0.1474 -0.2121 -0.0896 387 PHE   A CB  
2516 C  CG  . PHE   A 367 ? 1.3059 1.1275 1.6790 -0.1385 -0.1814 -0.0741 387 PHE   A CG  
2517 C  CD1 . PHE   A 367 ? 1.3176 1.1385 1.7390 -0.1590 -0.1576 -0.0456 387 PHE   A CD1 
2518 C  CD2 . PHE   A 367 ? 1.2341 1.0305 1.5408 -0.1080 -0.1759 -0.0870 387 PHE   A CD2 
2519 C  CE1 . PHE   A 367 ? 1.3894 1.1805 1.7860 -0.1491 -0.1308 -0.0304 387 PHE   A CE1 
2520 C  CE2 . PHE   A 367 ? 1.3484 1.1189 1.6369 -0.0981 -0.1514 -0.0723 387 PHE   A CE2 
2521 C  CZ  . PHE   A 367 ? 1.3530 1.1184 1.6830 -0.1186 -0.1298 -0.0441 387 PHE   A CZ  
2522 N  N   . ILE   A 368 ? 1.3367 1.2839 1.7129 -0.1168 -0.1350 -0.0483 388 ILE   A N   
2523 C  CA  . ILE   A 368 ? 1.2409 1.2057 1.5762 -0.0936 -0.1098 -0.0426 388 ILE   A CA  
2524 C  C   . ILE   A 368 ? 1.1533 1.0861 1.4814 -0.0925 -0.0867 -0.0266 388 ILE   A C   
2525 O  O   . ILE   A 368 ? 1.2262 1.1570 1.5953 -0.1110 -0.0708 -0.0056 388 ILE   A O   
2526 C  CB  . ILE   A 368 ? 1.3279 1.3479 1.6840 -0.0944 -0.0939 -0.0288 388 ILE   A CB  
2527 C  CG1 . ILE   A 368 ? 1.2875 1.3348 1.6199 -0.0826 -0.1117 -0.0451 388 ILE   A CG1 
2528 C  CG2 . ILE   A 368 ? 1.2455 1.2749 1.5780 -0.0813 -0.0630 -0.0144 388 ILE   A CG2 
2529 C  CD1 . ILE   A 368 ? 1.1513 1.2465 1.5118 -0.0869 -0.1026 -0.0319 388 ILE   A CD1 
2530 N  N   . PRO   A 369 ? 1.2191 1.1272 1.4968 -0.0701 -0.0834 -0.0343 389 PRO   A N   
2531 C  CA  . PRO   A 369 ? 1.2763 1.1481 1.5421 -0.0671 -0.0654 -0.0190 389 PRO   A CA  
2532 C  C   . PRO   A 369 ? 1.2243 1.1238 1.4818 -0.0598 -0.0365 0.0007  389 PRO   A C   
2533 O  O   . PRO   A 369 ? 1.2017 1.1439 1.4509 -0.0511 -0.0316 -0.0017 389 PRO   A O   
2534 C  CB  . PRO   A 369 ? 1.1449 0.9806 1.3602 -0.0424 -0.0787 -0.0381 389 PRO   A CB  
2535 C  CG  . PRO   A 369 ? 1.2607 1.1254 1.4561 -0.0288 -0.0959 -0.0615 389 PRO   A CG  
2536 C  CD  . PRO   A 369 ? 1.2566 1.1710 1.4865 -0.0447 -0.0949 -0.0559 389 PRO   A CD  
2537 N  N   . LYS   A 370 ? 1.2071 1.0768 1.4639 -0.0639 -0.0179 0.0206  390 LYS   A N   
2538 C  CA  . LYS   A 370 ? 1.1128 0.9965 1.3516 -0.0555 0.0080  0.0386  390 LYS   A CA  
2539 C  C   . LYS   A 370 ? 1.2112 1.1114 1.4049 -0.0297 0.0039  0.0271  390 LYS   A C   
2540 O  O   . LYS   A 370 ? 1.1235 1.0046 1.2902 -0.0133 -0.0113 0.0126  390 LYS   A O   
2541 C  CB  . LYS   A 370 ? 1.1509 0.9882 1.3809 -0.0589 0.0251  0.0597  390 LYS   A CB  
2542 C  CG  . LYS   A 370 ? 1.1565 0.9936 1.3464 -0.0428 0.0458  0.0740  390 LYS   A CG  
2543 C  CD  . LYS   A 370 ? 1.4006 1.1946 1.5836 -0.0489 0.0676  0.0998  390 LYS   A CD  
2544 C  CE  . LYS   A 370 ? 1.5073 1.3055 1.6503 -0.0351 0.0891  0.1145  390 LYS   A CE  
2545 N  NZ  . LYS   A 370 ? 1.4986 1.2464 1.6164 -0.0340 0.1084  0.1391  390 LYS   A NZ  
2546 N  N   . GLY   A 371 ? 1.1973 1.1334 1.3852 -0.0262 0.0175  0.0338  391 GLY   A N   
2547 C  CA  . GLY   A 371 ? 1.1735 1.1284 1.3259 -0.0060 0.0153  0.0272  391 GLY   A CA  
2548 C  C   . GLY   A 371 ? 1.1088 1.1053 1.2639 -0.0006 0.0025  0.0102  391 GLY   A C   
2549 O  O   . GLY   A 371 ? 1.1065 1.1292 1.2433 0.0108  0.0040  0.0082  391 GLY   A O   
2550 N  N   . VAL   A 372 ? 1.0482 1.0503 1.2247 -0.0090 -0.0107 -0.0013 392 VAL   A N   
2551 C  CA  . VAL   A 372 ? 1.0267 1.0650 1.2000 -0.0028 -0.0213 -0.0156 392 VAL   A CA  
2552 C  C   . VAL   A 372 ? 0.9829 1.0594 1.1699 -0.0110 -0.0099 -0.0061 392 VAL   A C   
2553 O  O   . VAL   A 372 ? 0.9772 1.0538 1.1893 -0.0255 0.0011  0.0068  392 VAL   A O   
2554 C  CB  . VAL   A 372 ? 1.0255 1.0542 1.2119 -0.0095 -0.0407 -0.0302 392 VAL   A CB  
2555 C  CG1 . VAL   A 372 ? 0.7936 0.8597 0.9740 -0.0043 -0.0493 -0.0413 392 VAL   A CG1 
2556 C  CG2 . VAL   A 372 ? 1.2120 1.1980 1.3762 0.0025  -0.0537 -0.0434 392 VAL   A CG2 
2557 N  N   . VAL   A 373 ? 0.9493 1.0576 1.1210 -0.0012 -0.0110 -0.0115 393 VAL   A N   
2558 C  CA  . VAL   A 373 ? 0.8393 0.9794 1.0207 -0.0084 -0.0027 -0.0041 393 VAL   A CA  
2559 C  C   . VAL   A 373 ? 0.7286 0.8865 0.9261 -0.0145 -0.0136 -0.0106 393 VAL   A C   
2560 O  O   . VAL   A 373 ? 0.7656 0.9355 0.9476 -0.0051 -0.0244 -0.0226 393 VAL   A O   
2561 C  CB  . VAL   A 373 ? 0.9680 1.1324 1.1290 0.0018  0.0007  -0.0045 393 VAL   A CB  
2562 C  CG1 . VAL   A 373 ? 0.8029 0.9962 0.9729 -0.0065 0.0057  0.0009  393 VAL   A CG1 
2563 C  CG2 . VAL   A 373 ? 0.8109 0.9584 0.9563 0.0062  0.0087  0.0035  393 VAL   A CG2 
2564 N  N   . VAL   A 374 ? 0.7631 0.9232 0.9906 -0.0284 -0.0107 -0.0022 394 VAL   A N   
2565 C  CA  . VAL   A 374 ? 0.8196 0.9992 1.0635 -0.0337 -0.0228 -0.0058 394 VAL   A CA  
2566 C  C   . VAL   A 374 ? 0.8122 1.0201 1.0481 -0.0312 -0.0152 0.0002  394 VAL   A C   
2567 O  O   . VAL   A 374 ? 0.8520 1.0620 1.0884 -0.0332 0.0009  0.0110  394 VAL   A O   
2568 C  CB  . VAL   A 374 ? 0.8463 1.0216 1.1337 -0.0488 -0.0240 0.0022  394 VAL   A CB  
2569 C  CG1 . VAL   A 374 ? 0.8090 1.0049 1.1135 -0.0526 -0.0419 -0.0022 394 VAL   A CG1 
2570 C  CG2 . VAL   A 374 ? 0.8149 0.9579 1.1120 -0.0546 -0.0303 -0.0015 394 VAL   A CG2 
2571 N  N   . MET   A 375 ? 0.7616 0.9872 0.9862 -0.0266 -0.0268 -0.0065 395 MET   A N   
2572 C  CA  A MET   A 375 ? 0.9859 1.2353 1.1988 -0.0242 -0.0199 -0.0001 395 MET   A CA  
2573 C  CA  B MET   A 375 ? 1.1125 1.3618 1.3258 -0.0243 -0.0198 0.0000  395 MET   A CA  
2574 C  C   . MET   A 375 ? 0.8637 1.1267 1.0843 -0.0263 -0.0315 0.0014  395 MET   A C   
2575 O  O   . MET   A 375 ? 0.9452 1.2038 1.1633 -0.0243 -0.0496 -0.0089 395 MET   A O   
2576 C  CB  A MET   A 375 ? 0.9470 1.2077 1.1292 -0.0126 -0.0181 -0.0067 395 MET   A CB  
2577 C  CB  B MET   A 375 ? 0.9387 1.1990 1.1215 -0.0129 -0.0178 -0.0065 395 MET   A CB  
2578 C  CG  A MET   A 375 ? 0.8455 1.1308 1.0193 -0.0134 -0.0093 0.0023  395 MET   A CG  
2579 C  CG  B MET   A 375 ? 0.8511 1.1343 1.0265 -0.0141 -0.0076 0.0030  395 MET   A CG  
2580 S  SD  A MET   A 375 ? 0.7552 1.0588 0.9120 -0.0081 -0.0181 0.0010  395 MET   A SD  
2581 S  SD  B MET   A 375 ? 0.8901 1.1960 1.0394 -0.0002 -0.0061 -0.0039 395 MET   A SD  
2582 C  CE  A MET   A 375 ? 0.9205 1.2323 1.0475 0.0094  -0.0187 -0.0126 395 MET   A CE  
2583 C  CE  B MET   A 375 ? 0.9119 1.2238 1.0436 0.0063  -0.0175 -0.0097 395 MET   A CE  
2584 N  N   . ILE   A 376 ? 0.7700 1.0459 0.9968 -0.0296 -0.0231 0.0137  396 ILE   A N   
2585 C  CA  . ILE   A 376 ? 0.8846 1.1730 1.1158 -0.0294 -0.0336 0.0184  396 ILE   A CA  
2586 C  C   . ILE   A 376 ? 0.8157 1.1177 1.0186 -0.0251 -0.0269 0.0242  396 ILE   A C   
2587 O  O   . ILE   A 376 ? 0.7712 1.0742 0.9759 -0.0293 -0.0124 0.0345  396 ILE   A O   
2588 C  CB  . ILE   A 376 ? 0.9266 1.2160 1.1948 -0.0358 -0.0295 0.0305  396 ILE   A CB  
2589 C  CG1 . ILE   A 376 ? 0.8766 1.1578 1.1817 -0.0424 -0.0333 0.0285  396 ILE   A CG1 
2590 C  CG2 . ILE   A 376 ? 0.7309 1.0333 1.0016 -0.0328 -0.0423 0.0367  396 ILE   A CG2 
2591 C  CD1 . ILE   A 376 ? 0.7828 1.0466 1.0901 -0.0456 -0.0164 0.0288  396 ILE   A CD1 
2592 N  N   . PRO   A 377 ? 0.7767 1.0873 0.9515 -0.0169 -0.0364 0.0184  397 PRO   A N   
2593 C  CA  . PRO   A 377 ? 0.9619 1.2878 1.1110 -0.0135 -0.0265 0.0269  397 PRO   A CA  
2594 C  C   . PRO   A 377 ? 0.8136 1.1422 0.9660 -0.0169 -0.0268 0.0427  397 PRO   A C   
2595 O  O   . PRO   A 377 ? 0.8109 1.1433 0.9447 -0.0107 -0.0377 0.0453  397 PRO   A O   
2596 C  CB  . PRO   A 377 ? 0.9945 1.3249 1.1096 -0.0006 -0.0355 0.0149  397 PRO   A CB  
2597 C  CG  . PRO   A 377 ? 0.9268 1.2419 1.0491 0.0006  -0.0582 0.0034  397 PRO   A CG  
2598 C  CD  . PRO   A 377 ? 0.7069 1.0103 0.8686 -0.0100 -0.0558 0.0030  397 PRO   A CD  
2599 N  N   . SER   A 378 ? 0.8514 1.1741 1.0236 -0.0254 -0.0149 0.0533  398 SER   A N   
2600 C  CA  . SER   A 378 ? 0.8866 1.2053 1.0648 -0.0271 -0.0144 0.0684  398 SER   A CA  
2601 C  C   . SER   A 378 ? 0.8647 1.1916 1.0125 -0.0245 -0.0126 0.0790  398 SER   A C   
2602 O  O   . SER   A 378 ? 0.7625 1.0881 0.9020 -0.0191 -0.0227 0.0874  398 SER   A O   
2603 C  CB  . SER   A 378 ? 0.8293 1.1342 1.0240 -0.0348 0.0005  0.0756  398 SER   A CB  
2604 O  OG  . SER   A 378 ? 0.8683 1.1645 1.0895 -0.0353 0.0016  0.0698  398 SER   A OG  
2605 N  N   . TYR   A 379 ? 0.8576 1.1947 0.9900 -0.0280 0.0004  0.0805  399 TYR   A N   
2606 C  CA  . TYR   A 379 ? 0.8692 1.2169 0.9747 -0.0267 0.0068  0.0933  399 TYR   A CA  
2607 C  C   . TYR   A 379 ? 0.9080 1.2613 0.9835 -0.0126 -0.0057 0.0888  399 TYR   A C   
2608 O  O   . TYR   A 379 ? 0.9430 1.2932 0.9972 -0.0083 -0.0092 0.1020  399 TYR   A O   
2609 C  CB  . TYR   A 379 ? 0.9420 1.3082 1.0449 -0.0322 0.0227  0.0940  399 TYR   A CB  
2610 C  CG  . TYR   A 379 ? 0.7969 1.1776 0.8788 -0.0339 0.0348  0.1111  399 TYR   A CG  
2611 C  CD1 . TYR   A 379 ? 1.0090 1.3823 1.0991 -0.0486 0.0444  0.1297  399 TYR   A CD1 
2612 C  CD2 . TYR   A 379 ? 0.9065 1.3049 0.9580 -0.0204 0.0377  0.1093  399 TYR   A CD2 
2613 C  CE1 . TYR   A 379 ? 0.9740 1.3599 1.0476 -0.0524 0.0575  0.1486  399 TYR   A CE1 
2614 C  CE2 . TYR   A 379 ? 1.1153 1.5281 1.1465 -0.0212 0.0530  0.1278  399 TYR   A CE2 
2615 C  CZ  . TYR   A 379 ? 1.0125 1.4203 1.0573 -0.0385 0.0633  0.1487  399 TYR   A CZ  
2616 O  OH  . TYR   A 379 ? 0.9979 1.4194 1.0251 -0.0416 0.0804  0.1702  399 TYR   A OH  
2617 N  N   . ALA   A 380 ? 0.8934 1.2506 0.9623 -0.0041 -0.0139 0.0698  400 ALA   A N   
2618 C  CA  . ALA   A 380 ? 1.1114 1.4684 1.1441 0.0105  -0.0281 0.0615  400 ALA   A CA  
2619 C  C   . ALA   A 380 ? 1.0430 1.3871 1.0795 0.0128  -0.0515 0.0631  400 ALA   A C   
2620 O  O   . ALA   A 380 ? 1.0921 1.4339 1.0928 0.0230  -0.0625 0.0673  400 ALA   A O   
2621 C  CB  . ALA   A 380 ? 1.1429 1.4987 1.1688 0.0188  -0.0338 0.0387  400 ALA   A CB  
2622 N  N   . LEU   A 381 ? 0.9401 1.2769 1.0198 0.0046  -0.0592 0.0610  401 LEU   A N   
2623 C  CA  . LEU   A 381 ? 1.0083 1.3399 1.1034 0.0070  -0.0823 0.0631  401 LEU   A CA  
2624 C  C   . LEU   A 381 ? 1.0179 1.3477 1.1060 0.0090  -0.0798 0.0852  401 LEU   A C   
2625 O  O   . LEU   A 381 ? 1.1125 1.4405 1.1866 0.0178  -0.1005 0.0896  401 LEU   A O   
2626 C  CB  . LEU   A 381 ? 1.0057 1.3349 1.1545 -0.0017 -0.0858 0.0577  401 LEU   A CB  
2627 C  CG  . LEU   A 381 ? 0.9814 1.3064 1.1391 -0.0048 -0.0889 0.0381  401 LEU   A CG  
2628 C  CD1 . LEU   A 381 ? 0.8377 1.1600 1.0472 -0.0148 -0.0837 0.0388  401 LEU   A CD1 
2629 C  CD2 . LEU   A 381 ? 1.1507 1.4707 1.2882 0.0021  -0.1169 0.0221  401 LEU   A CD2 
2630 N  N   . HIS   A 382 ? 0.9305 1.2575 1.0265 0.0012  -0.0569 0.0993  402 HIS   A N   
2631 C  CA  . HIS   A 382 ? 1.0200 1.3382 1.1062 0.0027  -0.0532 0.1213  402 HIS   A CA  
2632 C  C   . HIS   A 382 ? 1.1426 1.4626 1.1762 0.0108  -0.0533 0.1314  402 HIS   A C   
2633 O  O   . HIS   A 382 ? 1.0591 1.3687 1.0767 0.0154  -0.0562 0.1504  402 HIS   A O   
2634 C  CB  . HIS   A 382 ? 0.8794 1.1880 0.9816 -0.0095 -0.0299 0.1320  402 HIS   A CB  
2635 C  CG  . HIS   A 382 ? 0.8196 1.1211 0.9644 -0.0147 -0.0266 0.1250  402 HIS   A CG  
2636 N  ND1 . HIS   A 382 ? 0.8787 1.1653 1.0348 -0.0240 -0.0092 0.1306  402 HIS   A ND1 
2637 C  CD2 . HIS   A 382 ? 0.8889 1.1948 1.0658 -0.0117 -0.0375 0.1138  402 HIS   A CD2 
2638 C  CE1 . HIS   A 382 ? 1.0731 1.3542 1.2608 -0.0240 -0.0077 0.1228  402 HIS   A CE1 
2639 N  NE2 . HIS   A 382 ? 0.8670 1.1619 1.0711 -0.0173 -0.0231 0.1140  402 HIS   A NE2 
2640 N  N   . ARG   A 383 ? 1.1891 1.5202 1.1931 0.0146  -0.0485 0.1200  403 ARG   A N   
2641 C  CA  . ARG   A 383 ? 1.1953 1.5296 1.1450 0.0242  -0.0426 0.1299  403 ARG   A CA  
2642 C  C   . ARG   A 383 ? 1.3195 1.6526 1.2299 0.0408  -0.0648 0.1132  403 ARG   A C   
2643 O  O   . ARG   A 383 ? 1.3588 1.6949 1.2170 0.0519  -0.0566 0.1160  403 ARG   A O   
2644 C  CB  . ARG   A 383 ? 1.0633 1.4136 1.0065 0.0176  -0.0133 0.1334  403 ARG   A CB  
2645 C  CG  . ARG   A 383 ? 1.1015 1.4512 1.0834 -0.0012 0.0048  0.1454  403 ARG   A CG  
2646 C  CD  . ARG   A 383 ? 1.2441 1.5919 1.2073 -0.0076 0.0229  0.1727  403 ARG   A CD  
2647 N  NE  . ARG   A 383 ? 1.1511 1.4976 1.1487 -0.0277 0.0389  0.1812  403 ARG   A NE  
2648 C  CZ  . ARG   A 383 ? 1.0966 1.4519 1.0911 -0.0398 0.0597  0.1999  403 ARG   A CZ  
2649 N  NH1 . ARG   A 383 ? 1.2285 1.5965 1.1867 -0.0329 0.0719  0.2146  403 ARG   A NH1 
2650 N  NH2 . ARG   A 383 ? 1.0386 1.3892 1.0665 -0.0597 0.0683  0.2043  403 ARG   A NH2 
2651 N  N   . ASP   A 384 ? 1.4234 1.7511 1.3565 0.0425  -0.0921 0.0961  404 ASP   A N   
2652 C  CA  . ASP   A 384 ? 1.5472 1.8687 1.4446 0.0558  -0.1176 0.0760  404 ASP   A CA  
2653 C  C   . ASP   A 384 ? 1.6202 1.9318 1.4791 0.0683  -0.1409 0.0870  404 ASP   A C   
2654 O  O   . ASP   A 384 ? 1.6257 1.9360 1.5181 0.0653  -0.1578 0.0967  404 ASP   A O   
2655 C  CB  . ASP   A 384 ? 1.6001 1.9191 1.5435 0.0488  -0.1393 0.0547  404 ASP   A CB  
2656 C  CG  . ASP   A 384 ? 1.6944 2.0010 1.6033 0.0595  -0.1691 0.0305  404 ASP   A CG  
2657 O  OD1 . ASP   A 384 ? 1.7501 2.0480 1.5978 0.0748  -0.1807 0.0304  404 ASP   A OD1 
2658 O  OD2 . ASP   A 384 ? 1.6840 1.9858 1.6254 0.0523  -0.1821 0.0115  404 ASP   A OD2 
2659 N  N   . PRO   A 385 ? 1.6747 1.9794 1.4625 0.0844  -0.1418 0.0867  405 PRO   A N   
2660 C  CA  . PRO   A 385 ? 1.5972 1.8885 1.3407 0.0985  -0.1695 0.0952  405 PRO   A CA  
2661 C  C   . PRO   A 385 ? 1.6653 1.9508 1.4312 0.0998  -0.2152 0.0764  405 PRO   A C   
2662 O  O   . PRO   A 385 ? 1.7422 2.0221 1.4973 0.1077  -0.2424 0.0868  405 PRO   A O   
2663 C  CB  . PRO   A 385 ? 1.6291 1.9121 1.2868 0.1170  -0.1597 0.0917  405 PRO   A CB  
2664 C  CG  . PRO   A 385 ? 1.7399 2.0388 1.4053 0.1112  -0.1177 0.0928  405 PRO   A CG  
2665 C  CD  . PRO   A 385 ? 1.6273 1.9393 1.3745 0.0899  -0.1080 0.0902  405 PRO   A CD  
2666 N  N   . LYS   A 386 ? 1.6458 1.9324 1.4443 0.0919  -0.2258 0.0501  406 LYS   A N   
2667 C  CA  . LYS   A 386 ? 1.6712 1.9548 1.5025 0.0884  -0.2692 0.0332  406 LYS   A CA  
2668 C  C   . LYS   A 386 ? 1.6522 1.9529 1.5639 0.0760  -0.2754 0.0484  406 LYS   A C   
2669 O  O   . LYS   A 386 ? 1.6696 1.9761 1.6268 0.0698  -0.3079 0.0375  406 LYS   A O   
2670 C  CB  . LYS   A 386 ? 1.8028 2.0790 1.6495 0.0811  -0.2756 0.0034  406 LYS   A CB  
2671 C  CG  . LYS   A 386 ? 1.9090 2.1632 1.6750 0.0976  -0.2778 -0.0176 406 LYS   A CG  
2672 C  CD  . LYS   A 386 ? 1.9894 2.2221 1.7525 0.0964  -0.3196 -0.0489 406 LYS   A CD  
2673 C  CE  . LYS   A 386 ? 2.0823 2.2859 1.7519 0.1179  -0.3255 -0.0709 406 LYS   A CE  
2674 N  NZ  . LYS   A 386 ? 1.9928 2.1675 1.6490 0.1175  -0.3751 -0.1017 406 LYS   A NZ  
2675 N  N   . TYR   A 387 ? 1.6693 1.9779 1.6014 0.0723  -0.2445 0.0730  407 TYR   A N   
2676 C  CA  . TYR   A 387 ? 1.6696 1.9905 1.6679 0.0663  -0.2471 0.0893  407 TYR   A CA  
2677 C  C   . TYR   A 387 ? 1.6915 2.0066 1.6706 0.0738  -0.2308 0.1187  407 TYR   A C   
2678 O  O   . TYR   A 387 ? 1.7102 2.0311 1.7334 0.0753  -0.2384 0.1332  407 TYR   A O   
2679 C  CB  . TYR   A 387 ? 1.5872 1.9179 1.6513 0.0496  -0.2227 0.0849  407 TYR   A CB  
2680 C  CG  . TYR   A 387 ? 1.6020 1.9360 1.6963 0.0400  -0.2374 0.0598  407 TYR   A CG  
2681 C  CD1 . TYR   A 387 ? 1.6460 1.9911 1.7909 0.0358  -0.2702 0.0531  407 TYR   A CD1 
2682 C  CD2 . TYR   A 387 ? 1.6805 2.0065 1.7563 0.0349  -0.2188 0.0441  407 TYR   A CD2 
2683 C  CE1 . TYR   A 387 ? 1.6680 2.0124 1.8426 0.0241  -0.2835 0.0319  407 TYR   A CE1 
2684 C  CE2 . TYR   A 387 ? 1.6727 1.9951 1.7736 0.0263  -0.2322 0.0225  407 TYR   A CE2 
2685 C  CZ  . TYR   A 387 ? 1.7273 2.0570 1.8769 0.0196  -0.2642 0.0167  407 TYR   A CZ  
2686 O  OH  . TYR   A 387 ? 1.8321 2.1549 2.0087 0.0082  -0.2774 -0.0031 407 TYR   A OH  
2687 N  N   . TRP   A 388 ? 1.6240 1.9275 1.5416 0.0788  -0.2079 0.1293  408 TRP   A N   
2688 C  CA  . TRP   A 388 ? 1.5774 1.8706 1.4774 0.0822  -0.1887 0.1590  408 TRP   A CA  
2689 C  C   . TRP   A 388 ? 1.7304 2.0100 1.5458 0.0971  -0.1905 0.1697  408 TRP   A C   
2690 O  O   . TRP   A 388 ? 1.8094 2.0894 1.5799 0.0993  -0.1779 0.1584  408 TRP   A O   
2691 C  CB  . TRP   A 388 ? 1.4787 1.7721 1.4012 0.0668  -0.1474 0.1668  408 TRP   A CB  
2692 C  CG  . TRP   A 388 ? 1.4595 1.7636 1.4499 0.0533  -0.1410 0.1524  408 TRP   A CG  
2693 C  CD1 . TRP   A 388 ? 1.3715 1.6854 1.3769 0.0451  -0.1364 0.1296  408 TRP   A CD1 
2694 C  CD2 . TRP   A 388 ? 1.3342 1.6371 1.3816 0.0484  -0.1365 0.1611  408 TRP   A CD2 
2695 N  NE1 . TRP   A 388 ? 1.0989 1.4178 1.1654 0.0345  -0.1294 0.1249  408 TRP   A NE1 
2696 C  CE2 . TRP   A 388 ? 1.1711 1.4842 1.2637 0.0368  -0.1282 0.1434  408 TRP   A CE2 
2697 C  CE3 . TRP   A 388 ? 1.2144 1.5057 1.2761 0.0550  -0.1376 0.1825  408 TRP   A CE3 
2698 C  CZ2 . TRP   A 388 ? 1.0270 1.3406 1.1754 0.0319  -0.1192 0.1463  408 TRP   A CZ2 
2699 C  CZ3 . TRP   A 388 ? 1.0444 1.3361 1.1639 0.0512  -0.1292 0.1837  408 TRP   A CZ3 
2700 C  CH2 . TRP   A 388 ? 0.8784 1.1819 1.0393 0.0398  -0.1191 0.1658  408 TRP   A CH2 
2701 N  N   . THR   A 389 ? 1.5454 1.8123 1.3374 0.1094  -0.2046 0.1923  409 THR   A N   
2702 C  CA  . THR   A 389 ? 1.6904 1.9404 1.3969 0.1244  -0.2025 0.2083  409 THR   A CA  
2703 C  C   . THR   A 389 ? 1.6500 1.8936 1.3387 0.1151  -0.1563 0.2313  409 THR   A C   
2704 O  O   . THR   A 389 ? 1.6258 1.8623 1.3523 0.1051  -0.1402 0.2507  409 THR   A O   
2705 C  CB  . THR   A 389 ? 1.7840 2.0200 1.4707 0.1415  -0.2344 0.2274  409 THR   A CB  
2706 O  OG1 . THR   A 389 ? 1.7829 2.0137 1.5206 0.1361  -0.2232 0.2498  409 THR   A OG1 
2707 C  CG2 . THR   A 389 ? 1.6788 1.9256 1.3862 0.1494  -0.2843 0.2045  409 THR   A CG2 
2708 N  N   . GLU   A 390 ? 1.6950 1.9406 1.3266 0.1187  -0.1352 0.2293  410 GLU   A N   
2709 C  CA  . GLU   A 390 ? 1.7357 1.9827 1.3535 0.1083  -0.0907 0.2509  410 GLU   A CA  
2710 C  C   . GLU   A 390 ? 1.5785 1.8369 1.2734 0.0845  -0.0699 0.2482  410 GLU   A C   
2711 O  O   . GLU   A 390 ? 1.5227 1.7675 1.2439 0.0743  -0.0589 0.2703  410 GLU   A O   
2712 C  CB  . GLU   A 390 ? 1.7831 2.0060 1.3568 0.1151  -0.0832 0.2887  410 GLU   A CB  
2713 C  CG  . GLU   A 390 ? 1.9159 2.1199 1.4345 0.1396  -0.1216 0.2928  410 GLU   A CG  
2714 C  CD  . GLU   A 390 ? 2.0259 2.2015 1.5176 0.1459  -0.1199 0.3315  410 GLU   A CD  
2715 O  OE1 . GLU   A 390 ? 2.0535 2.2170 1.4889 0.1478  -0.0914 0.3578  410 GLU   A OE1 
2716 O  OE2 . GLU   A 390 ? 1.9934 2.1588 1.5227 0.1493  -0.1453 0.3371  410 GLU   A OE2 
2717 N  N   . PRO   A 391 ? 1.5776 1.8563 1.3055 0.0764  -0.0648 0.2214  411 PRO   A N   
2718 C  CA  . PRO   A 391 ? 1.5166 1.8025 1.3162 0.0569  -0.0544 0.2147  411 PRO   A CA  
2719 C  C   . PRO   A 391 ? 1.4305 1.7202 1.2453 0.0388  -0.0182 0.2319  411 PRO   A C   
2720 O  O   . PRO   A 391 ? 1.3689 1.6563 1.2356 0.0233  -0.0117 0.2300  411 PRO   A O   
2721 C  CB  . PRO   A 391 ? 1.4321 1.7352 1.2505 0.0573  -0.0637 0.1812  411 PRO   A CB  
2722 C  CG  . PRO   A 391 ? 1.5815 1.8880 1.3324 0.0744  -0.0653 0.1726  411 PRO   A CG  
2723 C  CD  . PRO   A 391 ? 1.7032 1.9967 1.3960 0.0845  -0.0579 0.2012  411 PRO   A CD  
2724 N  N   . GLU   A 392 ? 1.4999 1.7952 1.2719 0.0400  0.0051  0.2489  412 GLU   A N   
2725 C  CA  . GLU   A 392 ? 1.4545 1.7582 1.2476 0.0199  0.0381  0.2662  412 GLU   A CA  
2726 C  C   . GLU   A 392 ? 1.4415 1.7163 1.2423 0.0085  0.0438  0.2960  412 GLU   A C   
2727 O  O   . GLU   A 392 ? 1.4475 1.7225 1.2782 -0.0131 0.0650  0.3079  412 GLU   A O   
2728 C  CB  . GLU   A 392 ? 1.5208 1.8463 1.2710 0.0254  0.0644  0.2757  412 GLU   A CB  
2729 C  CG  . GLU   A 392 ? 1.7205 2.0791 1.4858 0.0271  0.0740  0.2503  412 GLU   A CG  
2730 C  CD  . GLU   A 392 ? 1.9369 2.3217 1.7433 0.0060  0.1046  0.2605  412 GLU   A CD  
2731 O  OE1 . GLU   A 392 ? 1.7745 2.1807 1.6177 0.0015  0.1057  0.2389  412 GLU   A OE1 
2732 O  OE2 . GLU   A 392 ? 1.8220 2.2056 1.6246 -0.0065 0.1263  0.2909  412 GLU   A OE2 
2733 N  N   . LYS   A 393 ? 1.4316 1.6796 1.2069 0.0225  0.0234  0.3077  413 LYS   A N   
2734 C  CA  . LYS   A 393 ? 1.4107 1.6252 1.1812 0.0164  0.0290  0.3390  413 LYS   A CA  
2735 C  C   . LYS   A 393 ? 1.4146 1.6078 1.2370 0.0104  0.0155  0.3327  413 LYS   A C   
2736 O  O   . LYS   A 393 ? 1.4325 1.6327 1.2800 0.0206  -0.0074 0.3104  413 LYS   A O   
2737 C  CB  . LYS   A 393 ? 1.4379 1.6326 1.1461 0.0386  0.0149  0.3587  413 LYS   A CB  
2738 C  CG  . LYS   A 393 ? 1.5829 1.7972 1.2300 0.0521  0.0234  0.3579  413 LYS   A CG  
2739 C  CD  . LYS   A 393 ? 1.6300 1.8194 1.2087 0.0640  0.0302  0.3931  413 LYS   A CD  
2740 C  CE  . LYS   A 393 ? 1.9031 2.0743 1.4391 0.0914  -0.0085 0.3898  413 LYS   A CE  
2741 N  NZ  . LYS   A 393 ? 1.8739 2.0584 1.3426 0.1122  -0.0146 0.3767  413 LYS   A NZ  
2742 N  N   . PHE   A 394 ? 1.4127 1.5785 1.2508 -0.0062 0.0309  0.3529  414 PHE   A N   
2743 C  CA  . PHE   A 394 ? 1.3561 1.4943 1.2363 -0.0108 0.0229  0.3486  414 PHE   A CA  
2744 C  C   . PHE   A 394 ? 1.3737 1.4820 1.2363 0.0111  0.0021  0.3638  414 PHE   A C   
2745 O  O   . PHE   A 394 ? 1.4291 1.5033 1.2636 0.0115  0.0080  0.3935  414 PHE   A O   
2746 C  CB  . PHE   A 394 ? 1.3765 1.4916 1.2747 -0.0372 0.0452  0.3622  414 PHE   A CB  
2747 C  CG  . PHE   A 394 ? 1.3542 1.4263 1.2793 -0.0390 0.0389  0.3628  414 PHE   A CG  
2748 C  CD1 . PHE   A 394 ? 1.2724 1.3481 1.2388 -0.0435 0.0356  0.3365  414 PHE   A CD1 
2749 C  CD2 . PHE   A 394 ? 1.2058 1.2301 1.1109 -0.0351 0.0384  0.3904  414 PHE   A CD2 
2750 C  CE1 . PHE   A 394 ? 1.2847 1.3183 1.2699 -0.0421 0.0326  0.3360  414 PHE   A CE1 
2751 C  CE2 . PHE   A 394 ? 1.1255 1.1060 1.0520 -0.0337 0.0339  0.3895  414 PHE   A CE2 
2752 C  CZ  . PHE   A 394 ? 1.3262 1.3118 1.2920 -0.0366 0.0317  0.3615  414 PHE   A CZ  
2753 N  N   . LEU   A 395 ? 1.3440 1.4661 1.2258 0.0293  -0.0230 0.3449  415 LEU   A N   
2754 C  CA  . LEU   A 395 ? 1.2832 1.3886 1.1547 0.0535  -0.0482 0.3567  415 LEU   A CA  
2755 C  C   . LEU   A 395 ? 1.2593 1.3610 1.1883 0.0598  -0.0589 0.3426  415 LEU   A C   
2756 O  O   . LEU   A 395 ? 1.2993 1.4316 1.2593 0.0677  -0.0759 0.3202  415 LEU   A O   
2757 C  CB  . LEU   A 395 ? 1.2755 1.4072 1.1141 0.0718  -0.0725 0.3488  415 LEU   A CB  
2758 C  CG  . LEU   A 395 ? 1.4955 1.6310 1.2658 0.0739  -0.0640 0.3616  415 LEU   A CG  
2759 C  CD1 . LEU   A 395 ? 1.5597 1.6963 1.2865 0.1000  -0.0968 0.3643  415 LEU   A CD1 
2760 C  CD2 . LEU   A 395 ? 1.5209 1.6248 1.2610 0.0628  -0.0368 0.3956  415 LEU   A CD2 
2761 N  N   . PRO   A 396 ? 1.3324 1.3951 1.2766 0.0571  -0.0483 0.3556  416 PRO   A N   
2762 C  CA  . PRO   A 396 ? 1.3712 1.4294 1.3678 0.0651  -0.0525 0.3418  416 PRO   A CA  
2763 C  C   . PRO   A 396 ? 1.3535 1.4247 1.3702 0.0932  -0.0803 0.3432  416 PRO   A C   
2764 O  O   . PRO   A 396 ? 1.2294 1.3099 1.2963 0.1016  -0.0830 0.3301  416 PRO   A O   
2765 C  CB  . PRO   A 396 ? 1.3472 1.3507 1.3403 0.0579  -0.0350 0.3579  416 PRO   A CB  
2766 C  CG  . PRO   A 396 ? 1.2432 1.2298 1.1926 0.0381  -0.0195 0.3772  416 PRO   A CG  
2767 C  CD  . PRO   A 396 ? 1.3080 1.3260 1.2210 0.0467  -0.0309 0.3837  416 PRO   A CD  
2768 N  N   . GLU   A 397 ? 1.3278 1.4016 1.3080 0.1086  -0.1010 0.3592  417 GLU   A N   
2769 C  CA  . GLU   A 397 ? 1.3736 1.4655 1.3772 0.1349  -0.1327 0.3600  417 GLU   A CA  
2770 C  C   . GLU   A 397 ? 1.3077 1.4513 1.3470 0.1341  -0.1509 0.3322  417 GLU   A C   
2771 O  O   . GLU   A 397 ? 1.3856 1.5518 1.4564 0.1526  -0.1794 0.3304  417 GLU   A O   
2772 C  CB  . GLU   A 397 ? 1.4766 1.5521 1.4236 0.1524  -0.1530 0.3856  417 GLU   A CB  
2773 C  CG  . GLU   A 397 ? 1.6492 1.6707 1.5753 0.1625  -0.1444 0.4168  417 GLU   A CG  
2774 C  CD  . GLU   A 397 ? 1.7632 1.7804 1.7350 0.1898  -0.1631 0.4224  417 GLU   A CD  
2775 O  OE1 . GLU   A 397 ? 1.6587 1.7183 1.6656 0.2051  -0.1917 0.4104  417 GLU   A OE1 
2776 O  OE2 . GLU   A 397 ? 1.7639 1.7352 1.7389 0.1962  -0.1495 0.4387  417 GLU   A OE2 
2777 N  N   . ARG   A 398 ? 1.3076 1.4701 1.3454 0.1131  -0.1365 0.3116  418 ARG   A N   
2778 C  CA  . ARG   A 398 ? 1.1161 1.3201 1.1946 0.1099  -0.1501 0.2846  418 ARG   A CA  
2779 C  C   . ARG   A 398 ? 1.1918 1.4068 1.3423 0.1138  -0.1463 0.2763  418 ARG   A C   
2780 O  O   . ARG   A 398 ? 1.1370 1.3871 1.3323 0.1170  -0.1645 0.2615  418 ARG   A O   
2781 C  CB  . ARG   A 398 ? 1.2159 1.4315 1.2792 0.0882  -0.1316 0.2656  418 ARG   A CB  
2782 C  CG  . ARG   A 398 ? 1.3000 1.5132 1.2961 0.0853  -0.1312 0.2701  418 ARG   A CG  
2783 C  CD  . ARG   A 398 ? 1.2774 1.5049 1.2707 0.0661  -0.1100 0.2511  418 ARG   A CD  
2784 N  NE  . ARG   A 398 ? 1.3139 1.5361 1.2477 0.0617  -0.0957 0.2605  418 ARG   A NE  
2785 C  CZ  . ARG   A 398 ? 1.4340 1.6690 1.3236 0.0698  -0.1078 0.2530  418 ARG   A CZ  
2786 N  NH1 . ARG   A 398 ? 1.5802 1.8306 1.4764 0.0806  -0.1390 0.2347  418 ARG   A NH1 
2787 N  NH2 . ARG   A 398 ? 1.3993 1.6308 1.2368 0.0669  -0.0880 0.2639  418 ARG   A NH2 
2788 N  N   . PHE   A 399 ? 1.2955 1.4796 1.4571 0.1135  -0.1222 0.2855  419 PHE   A N   
2789 C  CA  . PHE   A 399 ? 1.2576 1.4473 1.4791 0.1182  -0.1107 0.2770  419 PHE   A CA  
2790 C  C   . PHE   A 399 ? 1.1956 1.3698 1.4407 0.1441  -0.1177 0.2954  419 PHE   A C   
2791 O  O   . PHE   A 399 ? 1.2274 1.3886 1.5064 0.1511  -0.0992 0.2937  419 PHE   A O   
2792 C  CB  . PHE   A 399 ? 1.1247 1.2887 1.3394 0.0997  -0.0777 0.2683  419 PHE   A CB  
2793 C  CG  . PHE   A 399 ? 1.0688 1.2539 1.2739 0.0775  -0.0705 0.2487  419 PHE   A CG  
2794 C  CD1 . PHE   A 399 ? 1.1683 1.3479 1.3233 0.0639  -0.0678 0.2517  419 PHE   A CD1 
2795 C  CD2 . PHE   A 399 ? 1.1143 1.3253 1.3610 0.0718  -0.0653 0.2288  419 PHE   A CD2 
2796 C  CE1 . PHE   A 399 ? 1.1555 1.3555 1.3036 0.0471  -0.0610 0.2339  419 PHE   A CE1 
2797 C  CE2 . PHE   A 399 ? 1.1686 1.3954 1.4050 0.0538  -0.0598 0.2117  419 PHE   A CE2 
2798 C  CZ  . PHE   A 399 ? 0.9898 1.2116 1.1776 0.0425  -0.0584 0.2135  419 PHE   A CZ  
2799 N  N   . SER   A 400 ? 1.5015 1.6750 1.7258 0.1609  -0.1440 0.3129  420 SER   A N   
2800 C  CA  . SER   A 400 ? 1.5054 1.6689 1.7555 0.1894  -0.1552 0.3311  420 SER   A CA  
2801 C  C   . SER   A 400 ? 1.5568 1.7749 1.8791 0.2037  -0.1781 0.3228  420 SER   A C   
2802 O  O   . SER   A 400 ? 1.4424 1.7013 1.7788 0.1929  -0.1971 0.3076  420 SER   A O   
2803 C  CB  . SER   A 400 ? 1.5714 1.7072 1.7647 0.2027  -0.1746 0.3564  420 SER   A CB  
2804 O  OG  . SER   A 400 ? 1.3704 1.5414 1.5510 0.2064  -0.2092 0.3538  420 SER   A OG  
2805 N  N   . LYS   A 401 ? 1.4242 1.6423 1.7944 0.2286  -0.1763 0.3334  421 LYS   A N   
2806 C  CA  . LYS   A 401 ? 1.3920 1.6671 1.8455 0.2415  -0.1922 0.3274  421 LYS   A CA  
2807 C  C   . LYS   A 401 ? 1.4206 1.7361 1.8805 0.2460  -0.2392 0.3292  421 LYS   A C   
2808 O  O   . LYS   A 401 ? 1.5068 1.8761 2.0296 0.2420  -0.2567 0.3171  421 LYS   A O   
2809 C  CB  . LYS   A 401 ? 1.3199 1.5860 1.8187 0.2728  -0.1813 0.3422  421 LYS   A CB  
2810 C  CG  . LYS   A 401 ? 1.3627 1.6800 1.9296 0.2993  -0.2146 0.3528  421 LYS   A CG  
2811 C  CD  . LYS   A 401 ? 1.3239 1.6100 1.8921 0.3356  -0.2151 0.3768  421 LYS   A CD  
2812 C  CE  . LYS   A 401 ? 1.2112 1.5522 1.8471 0.3634  -0.2535 0.3892  421 LYS   A CE  
2813 N  NZ  . LYS   A 401 ? 1.3245 1.6383 1.9729 0.4033  -0.2500 0.4120  421 LYS   A NZ  
2814 N  N   . LYS   A 402 ? 1.6193 1.9074 2.0121 0.2531  -0.2607 0.3442  422 LYS   A N   
2815 C  CA  . LYS   A 402 ? 1.6287 1.9469 2.0081 0.2550  -0.3065 0.3423  422 LYS   A CA  
2816 C  C   . LYS   A 402 ? 1.6302 1.9672 1.9928 0.2255  -0.3077 0.3164  422 LYS   A C   
2817 O  O   . LYS   A 402 ? 1.5937 1.9744 1.9944 0.2210  -0.3388 0.3025  422 LYS   A O   
2818 C  CB  . LYS   A 402 ? 1.6451 1.9214 1.9426 0.2700  -0.3233 0.3657  422 LYS   A CB  
2819 C  CG  . LYS   A 402 ? 1.7458 2.0394 2.0060 0.2789  -0.3740 0.3682  422 LYS   A CG  
2820 C  CD  . LYS   A 402 ? 1.8454 2.1626 2.0836 0.2555  -0.3887 0.3419  422 LYS   A CD  
2821 C  CE  . LYS   A 402 ? 1.9484 2.2815 2.1559 0.2681  -0.4436 0.3421  422 LYS   A CE  
2822 N  NZ  . LYS   A 402 ? 1.9680 2.3220 2.1618 0.2462  -0.4585 0.3125  422 LYS   A NZ  
2823 N  N   . ASN   A 403 ? 1.5650 1.8695 1.8746 0.2051  -0.2750 0.3096  423 ASN   A N   
2824 C  CA  . ASN   A 403 ? 1.5784 1.8938 1.8597 0.1810  -0.2752 0.2872  423 ASN   A CA  
2825 C  C   . ASN   A 403 ? 1.5777 1.9063 1.9019 0.1601  -0.2447 0.2670  423 ASN   A C   
2826 O  O   . ASN   A 403 ? 1.5532 1.8933 1.8634 0.1416  -0.2462 0.2472  423 ASN   A O   
2827 C  CB  . ASN   A 403 ? 1.5460 1.8216 1.7339 0.1737  -0.2625 0.2947  423 ASN   A CB  
2828 C  CG  . ASN   A 403 ? 1.7626 2.0293 1.8923 0.1906  -0.2970 0.3090  423 ASN   A CG  
2829 O  OD1 . ASN   A 403 ? 1.7914 2.0871 1.9356 0.1988  -0.3371 0.3008  423 ASN   A OD1 
2830 N  ND2 . ASN   A 403 ? 1.7134 1.9382 1.7754 0.1953  -0.2824 0.3311  423 ASN   A ND2 
2831 N  N   . LYS   A 404 ? 1.5257 1.8494 1.8965 0.1644  -0.2172 0.2713  424 LYS   A N   
2832 C  CA  . LYS   A 404 ? 1.5218 1.8521 1.9225 0.1459  -0.1867 0.2537  424 LYS   A CA  
2833 C  C   . LYS   A 404 ? 1.6051 1.9842 2.0711 0.1380  -0.2020 0.2373  424 LYS   A C   
2834 O  O   . LYS   A 404 ? 1.5799 1.9644 2.0619 0.1205  -0.1806 0.2219  424 LYS   A O   
2835 C  CB  . LYS   A 404 ? 1.4840 1.7913 1.9095 0.1554  -0.1534 0.2620  424 LYS   A CB  
2836 C  CG  . LYS   A 404 ? 1.4882 1.8293 1.9962 0.1736  -0.1555 0.2659  424 LYS   A CG  
2837 C  CD  . LYS   A 404 ? 1.5607 1.8899 2.0957 0.1721  -0.1148 0.2597  424 LYS   A CD  
2838 C  CE  . LYS   A 404 ? 1.5096 1.8903 2.1299 0.1747  -0.1125 0.2537  424 LYS   A CE  
2839 N  NZ  . LYS   A 404 ? 1.5909 1.9570 2.2304 0.1775  -0.0703 0.2494  424 LYS   A NZ  
2840 N  N   . ASP   A 405 ? 1.5966 2.0101 2.1009 0.1493  -0.2397 0.2411  425 ASP   A N   
2841 C  CA  . ASP   A 405 ? 1.5437 2.0038 2.1157 0.1384  -0.2575 0.2268  425 ASP   A CA  
2842 C  C   . ASP   A 405 ? 1.5295 1.9910 2.0622 0.1191  -0.2800 0.2068  425 ASP   A C   
2843 O  O   . ASP   A 405 ? 1.4653 1.9531 2.0438 0.1030  -0.2865 0.1913  425 ASP   A O   
2844 C  CB  . ASP   A 405 ? 1.5901 2.0907 2.2287 0.1572  -0.2922 0.2386  425 ASP   A CB  
2845 C  CG  . ASP   A 405 ? 1.6284 2.1177 2.2819 0.1850  -0.2784 0.2616  425 ASP   A CG  
2846 O  OD1 . ASP   A 405 ? 1.7129 2.2037 2.4097 0.1898  -0.2423 0.2650  425 ASP   A OD1 
2847 O  OD2 . ASP   A 405 ? 1.5653 2.0405 2.1831 0.2036  -0.3034 0.2765  425 ASP   A OD2 
2848 N  N   . ASN   A 406 ? 1.7967 2.2282 2.2447 0.1210  -0.2904 0.2074  426 ASN   A N   
2849 C  CA  . ASN   A 406 ? 1.7846 2.2120 2.1840 0.1078  -0.3106 0.1881  426 ASN   A CA  
2850 C  C   . ASN   A 406 ? 1.8067 2.2142 2.1733 0.0894  -0.2755 0.1739  426 ASN   A C   
2851 O  O   . ASN   A 406 ? 1.8400 2.2298 2.1398 0.0847  -0.2793 0.1641  426 ASN   A O   
2852 C  CB  . ASN   A 406 ? 1.8615 2.2673 2.1815 0.1220  -0.3357 0.1967  426 ASN   A CB  
2853 C  CG  . ASN   A 406 ? 1.8980 2.3185 2.2428 0.1440  -0.3698 0.2146  426 ASN   A CG  
2854 O  OD1 . ASN   A 406 ? 1.8584 2.3151 2.2871 0.1469  -0.3846 0.2157  426 ASN   A OD1 
2855 N  ND2 . ASN   A 406 ? 1.9482 2.3420 2.2217 0.1603  -0.3819 0.2304  426 ASN   A ND2 
2856 N  N   . ILE   A 407 ? 1.4929 1.9032 1.9034 0.0808  -0.2414 0.1729  427 ILE   A N   
2857 C  CA  . ILE   A 407 ? 1.4313 1.8220 1.8122 0.0656  -0.2080 0.1622  427 ILE   A CA  
2858 C  C   . ILE   A 407 ? 1.2865 1.6964 1.7293 0.0520  -0.1963 0.1498  427 ILE   A C   
2859 O  O   . ILE   A 407 ? 1.2591 1.6855 1.7640 0.0566  -0.1857 0.1582  427 ILE   A O   
2860 C  CB  . ILE   A 407 ? 1.3827 1.7437 1.7355 0.0697  -0.1736 0.1770  427 ILE   A CB  
2861 C  CG1 . ILE   A 407 ? 1.2821 1.6181 1.5568 0.0726  -0.1753 0.1845  427 ILE   A CG1 
2862 C  CG2 . ILE   A 407 ? 1.1789 1.5304 1.5402 0.0552  -0.1388 0.1673  427 ILE   A CG2 
2863 C  CD1 . ILE   A 407 ? 1.1549 1.4594 1.4047 0.0753  -0.1476 0.2021  427 ILE   A CD1 
2864 N  N   . ASP   A 408 ? 1.1412 1.5479 1.5658 0.0371  -0.1969 0.1311  428 ASP   A N   
2865 C  CA  . ASP   A 408 ? 1.0338 1.4526 1.5086 0.0229  -0.1851 0.1202  428 ASP   A CA  
2866 C  C   . ASP   A 408 ? 1.0588 1.4594 1.5266 0.0190  -0.1422 0.1232  428 ASP   A C   
2867 O  O   . ASP   A 408 ? 0.9516 1.3289 1.3629 0.0162  -0.1277 0.1198  428 ASP   A O   
2868 C  CB  . ASP   A 408 ? 0.9741 1.3890 1.4259 0.0104  -0.2039 0.0990  428 ASP   A CB  
2869 C  CG  . ASP   A 408 ? 1.0991 1.5334 1.6177 -0.0037 -0.2126 0.0903  428 ASP   A CG  
2870 O  OD1 . ASP   A 408 ? 1.1204 1.5619 1.6852 -0.0087 -0.1846 0.0968  428 ASP   A OD1 
2871 O  OD2 . ASP   A 408 ? 1.1583 1.5980 1.6808 -0.0100 -0.2477 0.0770  428 ASP   A OD2 
2872 N  N   . PRO   A 409 ? 1.0110 1.4221 1.5341 0.0192  -0.1216 0.1297  429 PRO   A N   
2873 C  CA  . PRO   A 409 ? 0.9308 1.3205 1.4415 0.0161  -0.0833 0.1303  429 PRO   A CA  
2874 C  C   . PRO   A 409 ? 0.9202 1.3001 1.4133 0.0006  -0.0737 0.1150  429 PRO   A C   
2875 O  O   . PRO   A 409 ? 0.9368 1.3003 1.4217 -0.0023 -0.0450 0.1145  429 PRO   A O   
2876 C  CB  . PRO   A 409 ? 1.0553 1.4624 1.6319 0.0237  -0.0668 0.1411  429 PRO   A CB  
2877 C  CG  . PRO   A 409 ? 1.0106 1.4552 1.6471 0.0194  -0.0948 0.1401  429 PRO   A CG  
2878 C  CD  . PRO   A 409 ? 1.0523 1.4978 1.6540 0.0219  -0.1329 0.1362  429 PRO   A CD  
2879 N  N   . TYR   A 410 ? 0.9422 1.3287 1.4265 -0.0078 -0.0982 0.1020  430 TYR   A N   
2880 C  CA  . TYR   A 410 ? 0.9946 1.3675 1.4545 -0.0194 -0.0921 0.0871  430 TYR   A CA  
2881 C  C   . TYR   A 410 ? 1.0077 1.3672 1.4028 -0.0177 -0.1031 0.0775  430 TYR   A C   
2882 O  O   . TYR   A 410 ? 0.9573 1.3050 1.3266 -0.0237 -0.0976 0.0651  430 TYR   A O   
2883 C  CB  . TYR   A 410 ? 0.9117 1.2981 1.4185 -0.0307 -0.1079 0.0787  430 TYR   A CB  
2884 C  CG  . TYR   A 410 ? 0.9223 1.3257 1.4958 -0.0323 -0.0898 0.0912  430 TYR   A CG  
2885 C  CD1 . TYR   A 410 ? 0.7709 1.1606 1.3449 -0.0343 -0.0548 0.0950  430 TYR   A CD1 
2886 C  CD2 . TYR   A 410 ? 0.9429 1.3770 1.5768 -0.0292 -0.1065 0.1006  430 TYR   A CD2 
2887 C  CE1 . TYR   A 410 ? 0.8536 1.2579 1.4830 -0.0329 -0.0334 0.1075  430 TYR   A CE1 
2888 C  CE2 . TYR   A 410 ? 0.8052 1.2597 1.5039 -0.0283 -0.0855 0.1139  430 TYR   A CE2 
2889 C  CZ  . TYR   A 410 ? 0.9145 1.3529 1.6083 -0.0295 -0.0469 0.1175  430 TYR   A CZ  
2890 O  OH  . TYR   A 410 ? 0.8911 1.3486 1.6442 -0.0262 -0.0216 0.1315  430 TYR   A OH  
2891 N  N   . ILE   A 411 ? 0.9965 1.3575 1.3645 -0.0080 -0.1172 0.0844  431 ILE   A N   
2892 C  CA  . ILE   A 411 ? 1.0064 1.3547 1.3101 -0.0041 -0.1156 0.0823  431 ILE   A CA  
2893 C  C   . ILE   A 411 ? 0.9858 1.3216 1.2708 -0.0023 -0.0889 0.0963  431 ILE   A C   
2894 O  O   . ILE   A 411 ? 1.0519 1.3783 1.3010 -0.0061 -0.0737 0.0936  431 ILE   A O   
2895 C  CB  . ILE   A 411 ? 1.0122 1.3650 1.2885 0.0054  -0.1460 0.0829  431 ILE   A CB  
2896 C  CG1 . ILE   A 411 ? 1.0374 1.3999 1.3383 0.0018  -0.1778 0.0678  431 ILE   A CG1 
2897 C  CG2 . ILE   A 411 ? 1.0621 1.4033 1.2697 0.0102  -0.1407 0.0810  431 ILE   A CG2 
2898 C  CD1 . ILE   A 411 ? 1.1656 1.5152 1.4265 -0.0012 -0.1851 0.0470  431 ILE   A CD1 
2899 N  N   . TYR   A 412 ? 0.8556 1.1907 1.1670 0.0036  -0.0836 0.1110  432 TYR   A N   
2900 C  CA  . TYR   A 412 ? 0.9461 1.2618 1.2414 0.0048  -0.0605 0.1234  432 TYR   A CA  
2901 C  C   . TYR   A 412 ? 0.8429 1.1510 1.1674 0.0003  -0.0374 0.1207  432 TYR   A C   
2902 O  O   . TYR   A 412 ? 0.9435 1.2562 1.3090 0.0069  -0.0333 0.1267  432 TYR   A O   
2903 C  CB  . TYR   A 412 ? 0.8006 1.1116 1.0983 0.0174  -0.0683 0.1411  432 TYR   A CB  
2904 C  CG  . TYR   A 412 ? 0.9101 1.1929 1.1840 0.0173  -0.0472 0.1534  432 TYR   A CG  
2905 C  CD1 . TYR   A 412 ? 0.9266 1.1968 1.1536 0.0099  -0.0403 0.1568  432 TYR   A CD1 
2906 C  CD2 . TYR   A 412 ? 0.8763 1.1443 1.1759 0.0246  -0.0335 0.1614  432 TYR   A CD2 
2907 C  CE1 . TYR   A 412 ? 0.9303 1.1729 1.1394 0.0060  -0.0235 0.1681  432 TYR   A CE1 
2908 C  CE2 . TYR   A 412 ? 0.9487 1.1833 1.2232 0.0235  -0.0169 0.1706  432 TYR   A CE2 
2909 C  CZ  . TYR   A 412 ? 0.9513 1.1729 1.1820 0.0123  -0.0134 0.1739  432 TYR   A CZ  
2910 O  OH  . TYR   A 412 ? 1.0383 1.2252 1.2478 0.0075  0.0007  0.1832  432 TYR   A OH  
2911 N  N   . THR   A 413 ? 0.8377 1.1349 1.1400 -0.0093 -0.0220 0.1123  433 THR   A N   
2912 C  CA  . THR   A 413 ? 0.8519 1.1372 1.1689 -0.0131 -0.0008 0.1086  433 THR   A CA  
2913 C  C   . THR   A 413 ? 0.9337 1.1964 1.2145 -0.0194 0.0146  0.1088  433 THR   A C   
2914 O  O   . THR   A 413 ? 0.8755 1.1364 1.1417 -0.0273 0.0203  0.0992  433 THR   A O   
2915 C  CB  . THR   A 413 ? 0.9584 1.2543 1.2911 -0.0196 -0.0026 0.0958  433 THR   A CB  
2916 O  OG1 . THR   A 413 ? 0.7908 1.0893 1.0903 -0.0249 -0.0107 0.0859  433 THR   A OG1 
2917 C  CG2 . THR   A 413 ? 0.8363 1.1537 1.2131 -0.0173 -0.0191 0.0957  433 THR   A CG2 
2918 N  N   . PRO   A 414 ? 0.9581 1.2019 1.2256 -0.0164 0.0199  0.1201  434 PRO   A N   
2919 C  CA  . PRO   A 414 ? 0.9353 1.1554 1.1731 -0.0257 0.0319  0.1200  434 PRO   A CA  
2920 C  C   . PRO   A 414 ? 0.8436 1.0429 1.0832 -0.0268 0.0477  0.1126  434 PRO   A C   
2921 O  O   . PRO   A 414 ? 0.7708 0.9535 0.9865 -0.0365 0.0533  0.1083  434 PRO   A O   
2922 C  CB  . PRO   A 414 ? 0.8946 1.0943 1.1206 -0.0218 0.0315  0.1351  434 PRO   A CB  
2923 C  CG  . PRO   A 414 ? 0.9226 1.1283 1.1783 -0.0058 0.0262  0.1417  434 PRO   A CG  
2924 C  CD  . PRO   A 414 ? 0.8888 1.1293 1.1688 -0.0044 0.0136  0.1336  434 PRO   A CD  
2925 N  N   . PHE   A 415 ? 0.8814 1.0820 1.1485 -0.0170 0.0549  0.1117  435 PHE   A N   
2926 C  CA  . PHE   A 415 ? 0.9525 1.1309 1.2160 -0.0144 0.0731  0.1063  435 PHE   A CA  
2927 C  C   . PHE   A 415 ? 0.7782 0.9750 1.0646 -0.0144 0.0773  0.1003  435 PHE   A C   
2928 O  O   . PHE   A 415 ? 0.6845 0.8665 0.9731 -0.0089 0.0950  0.0990  435 PHE   A O   
2929 C  CB  . PHE   A 415 ? 0.8031 0.9588 1.0753 0.0002  0.0859  0.1139  435 PHE   A CB  
2930 C  CG  . PHE   A 415 ? 0.9809 1.1057 1.2256 -0.0003 0.0837  0.1196  435 PHE   A CG  
2931 C  CD1 . PHE   A 415 ? 1.0094 1.1424 1.2619 0.0036  0.0712  0.1315  435 PHE   A CD1 
2932 C  CD2 . PHE   A 415 ? 0.9264 1.0105 1.1354 -0.0053 0.0921  0.1135  435 PHE   A CD2 
2933 C  CE1 . PHE   A 415 ? 0.9163 1.0165 1.1432 0.0020  0.0701  0.1392  435 PHE   A CE1 
2934 C  CE2 . PHE   A 415 ? 1.0535 1.1045 1.2393 -0.0086 0.0887  0.1191  435 PHE   A CE2 
2935 C  CZ  . PHE   A 415 ? 0.9974 1.0560 1.1930 -0.0053 0.0790  0.1329  435 PHE   A CZ  
2936 N  N   . GLY   A 416 ? 0.7896 1.0144 1.0897 -0.0199 0.0620  0.0969  436 GLY   A N   
2937 C  CA  . GLY   A 416 ? 0.8736 1.1123 1.1987 -0.0216 0.0636  0.0924  436 GLY   A CA  
2938 C  C   . GLY   A 416 ? 0.8266 1.0828 1.2015 -0.0141 0.0660  0.1008  436 GLY   A C   
2939 O  O   . GLY   A 416 ? 0.8488 1.1130 1.2404 -0.0061 0.0600  0.1090  436 GLY   A O   
2940 N  N   . SER   A 417 ? 0.8540 1.1171 1.2554 -0.0167 0.0749  0.1001  437 SER   A N   
2941 C  CA  . SER   A 417 ? 0.7173 1.0029 1.1763 -0.0118 0.0798  0.1096  437 SER   A CA  
2942 C  C   . SER   A 417 ? 0.7560 1.0380 1.2315 -0.0159 0.0998  0.1111  437 SER   A C   
2943 O  O   . SER   A 417 ? 0.8086 1.0726 1.2515 -0.0231 0.1025  0.1036  437 SER   A O   
2944 C  CB  . SER   A 417 ? 0.6990 1.0157 1.1930 -0.0167 0.0503  0.1090  437 SER   A CB  
2945 O  OG  . SER   A 417 ? 0.9660 1.3002 1.4928 -0.0055 0.0451  0.1196  437 SER   A OG  
2946 N  N   . GLY   A 418 ? 0.7875 1.0882 1.3157 -0.0104 0.1147  0.1228  438 GLY   A N   
2947 C  CA  . GLY   A 418 ? 0.6501 0.9495 1.1992 -0.0140 0.1381  0.1289  438 GLY   A CA  
2948 C  C   . GLY   A 418 ? 0.7224 0.9884 1.2295 -0.0021 0.1713  0.1313  438 GLY   A C   
2949 O  O   . GLY   A 418 ? 0.5801 0.8245 1.0492 0.0092  0.1757  0.1281  438 GLY   A O   
2950 N  N   . PRO   A 419 ? 0.8126 1.0693 1.3217 -0.0046 0.1946  0.1372  439 PRO   A N   
2951 C  CA  . PRO   A 419 ? 0.9126 1.1343 1.3753 0.0092  0.2273  0.1396  439 PRO   A CA  
2952 C  C   . PRO   A 419 ? 0.8573 1.0389 1.2419 0.0099  0.2182  0.1254  439 PRO   A C   
2953 O  O   . PRO   A 419 ? 0.9034 1.0521 1.2432 0.0230  0.2379  0.1239  439 PRO   A O   
2954 C  CB  . PRO   A 419 ? 0.7589 0.9796 1.2378 0.0034  0.2500  0.1503  439 PRO   A CB  
2955 C  CG  . PRO   A 419 ? 0.9015 1.1547 1.4383 -0.0154 0.2280  0.1526  439 PRO   A CG  
2956 C  CD  . PRO   A 419 ? 0.7428 1.0196 1.2992 -0.0195 0.1926  0.1434  439 PRO   A CD  
2957 N  N   . ARG   A 420 ? 0.8607 1.0442 1.2281 -0.0031 0.1890  0.1145  440 ARG   A N   
2958 C  CA  . ARG   A 420 ? 0.9634 1.1171 1.2671 -0.0041 0.1790  0.1023  440 ARG   A CA  
2959 C  C   . ARG   A 420 ? 0.7930 0.9535 1.0890 -0.0066 0.1564  0.0956  440 ARG   A C   
2960 O  O   . ARG   A 420 ? 0.7643 0.9174 1.0272 -0.0138 0.1397  0.0863  440 ARG   A O   
2961 C  CB  . ARG   A 420 ? 0.9140 1.0615 1.1973 -0.0142 0.1681  0.0964  440 ARG   A CB  
2962 C  CG  . ARG   A 420 ? 1.0800 1.1893 1.3041 -0.0084 0.1802  0.0931  440 ARG   A CG  
2963 C  CD  . ARG   A 420 ? 1.0088 1.1089 1.2121 -0.0143 0.1720  0.0899  440 ARG   A CD  
2964 N  NE  . ARG   A 420 ? 0.8861 0.9544 1.0280 -0.0093 0.1701  0.0826  440 ARG   A NE  
2965 C  CZ  . ARG   A 420 ? 0.9593 1.0065 1.0672 -0.0075 0.1705  0.0824  440 ARG   A CZ  
2966 N  NH1 . ARG   A 420 ? 1.0494 1.0997 1.1764 -0.0107 0.1747  0.0897  440 ARG   A NH1 
2967 N  NH2 . ARG   A 420 ? 0.9618 0.9818 1.0148 -0.0026 0.1647  0.0750  440 ARG   A NH2 
2968 N  N   . ASN   A 421 ? 0.8260 1.0013 1.1534 0.0002  0.1566  0.1019  441 ASN   A N   
2969 C  CA  . ASN   A 421 ? 0.8339 1.0074 1.1471 -0.0002 0.1396  0.0989  441 ASN   A CA  
2970 C  C   . ASN   A 421 ? 0.8061 0.9382 1.0672 0.0048  0.1486  0.0938  441 ASN   A C   
2971 O  O   . ASN   A 421 ? 0.8222 0.9268 1.0541 0.0102  0.1663  0.0911  441 ASN   A O   
2972 C  CB  . ASN   A 421 ? 0.7720 0.9699 1.1315 0.0078  0.1357  0.1085  441 ASN   A CB  
2973 C  CG  . ASN   A 421 ? 0.8510 1.0339 1.2187 0.0260  0.1606  0.1162  441 ASN   A CG  
2974 O  OD1 . ASN   A 421 ? 0.7955 0.9501 1.1355 0.0332  0.1838  0.1144  441 ASN   A OD1 
2975 N  ND2 . ASN   A 421 ? 0.9145 1.1147 1.3172 0.0361  0.1555  0.1248  441 ASN   A ND2 
2976 N  N   . CYS   A 422 ? 0.8289 0.9532 1.0752 0.0023  0.1352  0.0926  442 CYS   A N   
2977 C  CA  . CYS   A 422 ? 0.8794 0.9614 1.0785 0.0032  0.1385  0.0869  442 CYS   A CA  
2978 C  C   . CYS   A 422 ? 0.9112 0.9628 1.1024 0.0219  0.1626  0.0894  442 CYS   A C   
2979 O  O   . CYS   A 422 ? 0.8886 0.9446 1.1058 0.0340  0.1677  0.0976  442 CYS   A O   
2980 C  CB  . CYS   A 422 ? 0.8327 0.9128 1.0247 -0.0047 0.1209  0.0888  442 CYS   A CB  
2981 S  SG  . CYS   A 422 ? 1.0642 1.0867 1.2078 -0.0046 0.1235  0.0837  442 CYS   A SG  
2982 N  N   . ILE   A 423 ? 0.8907 0.9105 1.0435 0.0268  0.1776  0.0825  443 ILE   A N   
2983 C  CA  . ILE   A 423 ? 1.1632 1.1498 1.2992 0.0478  0.2041  0.0835  443 ILE   A CA  
2984 C  C   . ILE   A 423 ? 1.1505 1.0980 1.2609 0.0546  0.2005  0.0800  443 ILE   A C   
2985 O  O   . ILE   A 423 ? 1.0351 0.9606 1.1439 0.0762  0.2212  0.0829  443 ILE   A O   
2986 C  CB  . ILE   A 423 ? 1.0678 1.0220 1.1540 0.0519  0.2187  0.0759  443 ILE   A CB  
2987 C  CG1 . ILE   A 423 ? 1.0988 1.0301 1.1760 0.0773  0.2538  0.0802  443 ILE   A CG1 
2988 C  CG2 . ILE   A 423 ? 1.1527 1.0637 1.1778 0.0424  0.2008  0.0613  443 ILE   A CG2 
2989 C  CD1 . ILE   A 423 ? 1.1838 1.0683 1.1929 0.0855  0.2685  0.0715  443 ILE   A CD1 
2990 N  N   . GLY   A 424 ? 0.9698 0.9072 1.0616 0.0372  0.1759  0.0749  444 GLY   A N   
2991 C  CA  . GLY   A 424 ? 1.2387 1.1344 1.3060 0.0392  0.1699  0.0727  444 GLY   A CA  
2992 C  C   . GLY   A 424 ? 1.1491 1.0673 1.2530 0.0368  0.1576  0.0849  444 GLY   A C   
2993 O  O   . GLY   A 424 ? 1.1530 1.0382 1.2359 0.0311  0.1470  0.0848  444 GLY   A O   
2994 N  N   . MET   A 425 ? 0.9370 0.9072 1.0927 0.0406  0.1574  0.0958  445 MET   A N   
2995 C  CA  . MET   A 425 ? 0.9997 0.9926 1.1852 0.0392  0.1425  0.1078  445 MET   A CA  
2996 C  C   . MET   A 425 ? 1.1195 1.0739 1.2972 0.0567  0.1487  0.1138  445 MET   A C   
2997 O  O   . MET   A 425 ? 1.1115 1.0422 1.2711 0.0485  0.1352  0.1178  445 MET   A O   
2998 C  CB  . MET   A 425 ? 0.7520 0.8020 0.9933 0.0441  0.1407  0.1164  445 MET   A CB  
2999 C  CG  . MET   A 425 ? 0.9658 1.0351 1.2373 0.0512  0.1273  0.1298  445 MET   A CG  
3000 S  SD  . MET   A 425 ? 0.9524 1.0855 1.2926 0.0580  0.1209  0.1386  445 MET   A SD  
3001 C  CE  . MET   A 425 ? 1.1117 1.2631 1.4540 0.0517  0.0903  0.1478  445 MET   A CE  
3002 N  N   . ARG   A 426 ? 1.0325 0.9791 1.2243 0.0819  0.1707  0.1157  446 ARG   A N   
3003 C  CA  . ARG   A 426 ? 1.1982 1.1113 1.3885 0.1040  0.1775  0.1224  446 ARG   A CA  
3004 C  C   . ARG   A 426 ? 1.3455 1.1860 1.4744 0.0997  0.1753  0.1124  446 ARG   A C   
3005 O  O   . ARG   A 426 ? 1.2995 1.1074 1.4195 0.1053  0.1682  0.1192  446 ARG   A O   
3006 C  CB  . ARG   A 426 ? 1.2447 1.1665 1.4634 0.1342  0.2057  0.1258  446 ARG   A CB  
3007 C  CG  . ARG   A 426 ? 1.4675 1.4194 1.7408 0.1550  0.2039  0.1425  446 ARG   A CG  
3008 C  CD  . ARG   A 426 ? 1.4864 1.4679 1.8060 0.1815  0.2322  0.1483  446 ARG   A CD  
3009 N  NE  . ARG   A 426 ? 1.6554 1.7019 2.0263 0.1690  0.2314  0.1525  446 ARG   A NE  
3010 C  CZ  . ARG   A 426 ? 1.6892 1.7884 2.1074 0.1561  0.2065  0.1611  446 ARG   A CZ  
3011 N  NH1 . ARG   A 426 ? 1.6532 1.7530 2.0746 0.1557  0.1813  0.1683  446 ARG   A NH1 
3012 N  NH2 . ARG   A 426 ? 1.6978 1.8466 2.1580 0.1439  0.2065  0.1626  446 ARG   A NH2 
3013 N  N   . PHE   A 427 ? 1.3205 1.1318 1.4055 0.0895  0.1794  0.0965  447 PHE   A N   
3014 C  CA  . PHE   A 427 ? 1.3002 1.0423 1.3275 0.0806  0.1713  0.0849  447 PHE   A CA  
3015 C  C   . PHE   A 427 ? 1.3818 1.1272 1.4100 0.0524  0.1449  0.0915  447 PHE   A C   
3016 O  O   . PHE   A 427 ? 1.4768 1.1759 1.4863 0.0510  0.1376  0.0951  447 PHE   A O   
3017 C  CB  . PHE   A 427 ? 1.4645 1.1807 1.4454 0.0737  0.1756  0.0665  447 PHE   A CB  
3018 C  CG  . PHE   A 427 ? 1.5968 1.2438 1.5192 0.0596  0.1607  0.0521  447 PHE   A CG  
3019 C  CD1 . PHE   A 427 ? 1.6022 1.2539 1.5231 0.0268  0.1339  0.0526  447 PHE   A CD1 
3020 C  CD2 . PHE   A 427 ? 1.7718 1.3494 1.6403 0.0790  0.1736  0.0375  447 PHE   A CD2 
3021 C  CE1 . PHE   A 427 ? 1.7840 1.3745 1.6585 0.0106  0.1179  0.0400  447 PHE   A CE1 
3022 C  CE2 . PHE   A 427 ? 1.9018 1.4113 1.7153 0.0644  0.1559  0.0222  447 PHE   A CE2 
3023 C  CZ  . PHE   A 427 ? 1.8818 1.3993 1.7018 0.0284  0.1267  0.0238  447 PHE   A CZ  
3024 N  N   . ALA   A 428 ? 1.3730 1.1712 1.4222 0.0304  0.1320  0.0939  448 ALA   A N   
3025 C  CA  . ALA   A 428 ? 1.3843 1.1918 1.4346 0.0039  0.1110  0.1010  448 ALA   A CA  
3026 C  C   . ALA   A 428 ? 1.4302 1.2350 1.4981 0.0110  0.1066  0.1193  448 ALA   A C   
3027 O  O   . ALA   A 428 ? 1.5122 1.2794 1.5606 -0.0019 0.0970  0.1251  448 ALA   A O   
3028 C  CB  . ALA   A 428 ? 1.2587 1.1296 1.3331 -0.0125 0.1023  0.1017  448 ALA   A CB  
3029 N  N   . LEU   A 429 ? 1.3615 1.2048 1.4671 0.0311  0.1122  0.1298  449 LEU   A N   
3030 C  CA  . LEU   A 429 ? 1.4641 1.3037 1.5845 0.0424  0.1064  0.1480  449 LEU   A CA  
3031 C  C   . LEU   A 429 ? 1.6504 1.4172 1.7410 0.0556  0.1124  0.1486  449 LEU   A C   
3032 O  O   . LEU   A 429 ? 1.4404 1.1772 1.5180 0.0489  0.1023  0.1611  449 LEU   A O   
3033 C  CB  . LEU   A 429 ? 1.2356 1.1248 1.4035 0.0656  0.1104  0.1565  449 LEU   A CB  
3034 C  CG  . LEU   A 429 ? 1.2293 1.1871 1.4304 0.0561  0.1020  0.1566  449 LEU   A CG  
3035 C  CD1 . LEU   A 429 ? 1.1988 1.1870 1.4367 0.0738  0.1166  0.1521  449 LEU   A CD1 
3036 C  CD2 . LEU   A 429 ? 1.2500 1.2381 1.4688 0.0557  0.0834  0.1730  449 LEU   A CD2 
3037 N  N   . MET   A 430 ? 1.6833 1.4169 1.7590 0.0753  0.1299  0.1353  450 MET   A N   
3038 C  CA  A MET   A 430 ? 1.6989 1.3563 1.7409 0.0918  0.1367  0.1327  450 MET   A CA  
3039 C  CA  B MET   A 430 ? 1.6871 1.3445 1.7291 0.0918  0.1367  0.1327  450 MET   A CA  
3040 C  C   . MET   A 430 ? 1.7781 1.3769 1.7735 0.0634  0.1229  0.1249  450 MET   A C   
3041 O  O   . MET   A 430 ? 1.8271 1.3775 1.8064 0.0605  0.1148  0.1345  450 MET   A O   
3042 C  CB  A MET   A 430 ? 1.6566 1.2923 1.6873 0.1208  0.1613  0.1186  450 MET   A CB  
3043 C  CB  B MET   A 430 ? 1.6597 1.2955 1.6903 0.1207  0.1612  0.1185  450 MET   A CB  
3044 C  CG  A MET   A 430 ? 1.7199 1.2704 1.7089 0.1426  0.1703  0.1123  450 MET   A CG  
3045 C  CG  B MET   A 430 ? 1.7257 1.2697 1.7028 0.1344  0.1680  0.1070  450 MET   A CG  
3046 S  SD  A MET   A 430 ? 1.8381 1.3738 1.8523 0.1666  0.1662  0.1357  450 MET   A SD  
3047 S  SD  B MET   A 430 ? 1.7261 1.2542 1.7161 0.1878  0.1987  0.1087  450 MET   A SD  
3048 C  CE  A MET   A 430 ? 1.8111 1.4414 1.9010 0.1925  0.1781  0.1496  450 MET   A CE  
3049 C  CE  B MET   A 430 ? 1.8561 1.4470 1.9159 0.1987  0.1887  0.1377  450 MET   A CE  
3050 N  N   . ASN   A 431 ? 1.7718 1.3738 1.7469 0.0418  0.1188  0.1085  451 ASN   A N   
3051 C  CA  . ASN   A 431 ? 1.7479 1.3003 1.6856 0.0122  0.1026  0.0999  451 ASN   A CA  
3052 C  C   . ASN   A 431 ? 1.6837 1.2494 1.6380 -0.0138 0.0863  0.1196  451 ASN   A C   
3053 O  O   . ASN   A 431 ? 1.7210 1.2277 1.6528 -0.0261 0.0775  0.1239  451 ASN   A O   
3054 C  CB  . ASN   A 431 ? 1.7528 1.3261 1.6775 -0.0066 0.0974  0.0824  451 ASN   A CB  
3055 C  CG  . ASN   A 431 ? 1.8193 1.3483 1.7128 -0.0383 0.0773  0.0730  451 ASN   A CG  
3056 O  OD1 . ASN   A 431 ? 1.8402 1.4031 1.7537 -0.0685 0.0624  0.0815  451 ASN   A OD1 
3057 N  ND2 . ASN   A 431 ? 2.0121 1.4634 1.8567 -0.0314 0.0767  0.0557  451 ASN   A ND2 
3058 N  N   . MET   A 432 ? 1.6145 1.2548 1.6061 -0.0221 0.0831  0.1321  452 MET   A N   
3059 C  CA  . MET   A 432 ? 1.6078 1.2666 1.6125 -0.0440 0.0716  0.1526  452 MET   A CA  
3060 C  C   . MET   A 432 ? 1.5706 1.1916 1.5725 -0.0279 0.0726  0.1719  452 MET   A C   
3061 O  O   . MET   A 432 ? 1.4865 1.0705 1.4748 -0.0466 0.0647  0.1852  452 MET   A O   
3062 C  CB  . MET   A 432 ? 1.3857 1.1281 1.4244 -0.0475 0.0701  0.1599  452 MET   A CB  
3063 C  CG  . MET   A 432 ? 1.5240 1.3048 1.5667 -0.0638 0.0677  0.1438  452 MET   A CG  
3064 S  SD  . MET   A 432 ? 1.3758 1.2394 1.4490 -0.0760 0.0621  0.1549  452 MET   A SD  
3065 C  CE  . MET   A 432 ? 1.2984 1.1949 1.3970 -0.0435 0.0677  0.1619  452 MET   A CE  
3066 N  N   . LYS   A 433 ? 1.5498 1.1806 1.5673 0.0068  0.0822  0.1754  453 LYS   A N   
3067 C  CA  . LYS   A 433 ? 1.6365 1.2381 1.6550 0.0265  0.0812  0.1956  453 LYS   A CA  
3068 C  C   . LYS   A 433 ? 1.7630 1.2708 1.7429 0.0267  0.0814  0.1931  453 LYS   A C   
3069 O  O   . LYS   A 433 ? 1.6746 1.1457 1.6433 0.0193  0.0740  0.2124  453 LYS   A O   
3070 C  CB  . LYS   A 433 ? 1.5697 1.2037 1.6191 0.0650  0.0906  0.1979  453 LYS   A CB  
3071 C  CG  . LYS   A 433 ? 1.4202 1.1357 1.5080 0.0656  0.0828  0.2097  453 LYS   A CG  
3072 C  CD  . LYS   A 433 ? 1.3346 1.0846 1.4612 0.1008  0.0890  0.2122  453 LYS   A CD  
3073 C  CE  . LYS   A 433 ? 1.3213 1.1506 1.4849 0.0976  0.0778  0.2185  453 LYS   A CE  
3074 N  NZ  . LYS   A 433 ? 1.2715 1.1435 1.4820 0.1244  0.0846  0.2157  453 LYS   A NZ  
3075 N  N   . LEU   A 434 ? 1.7823 1.2459 1.7369 0.0346  0.0893  0.1694  454 LEU   A N   
3076 C  CA  . LEU   A 434 ? 1.8757 1.2420 1.7866 0.0332  0.0868  0.1623  454 LEU   A CA  
3077 C  C   . LEU   A 434 ? 1.9422 1.2816 1.8386 -0.0112 0.0695  0.1691  454 LEU   A C   
3078 O  O   . LEU   A 434 ? 1.8156 1.0841 1.6896 -0.0171 0.0632  0.1788  454 LEU   A O   
3079 C  CB  . LEU   A 434 ? 1.7671 1.0941 1.6457 0.0465  0.0967  0.1325  454 LEU   A CB  
3080 C  CG  . LEU   A 434 ? 1.9428 1.2809 1.8316 0.0932  0.1194  0.1266  454 LEU   A CG  
3081 C  CD1 . LEU   A 434 ? 2.0312 1.3169 1.8743 0.1060  0.1310  0.0980  454 LEU   A CD1 
3082 C  CD2 . LEU   A 434 ? 1.8607 1.1643 1.7561 0.1248  0.1244  0.1440  454 LEU   A CD2 
3083 N  N   . ALA   A 435 ? 1.7576 1.1536 1.6697 -0.0425 0.0621  0.1653  455 ALA   A N   
3084 C  CA  . ALA   A 435 ? 1.7867 1.1753 1.6985 -0.0855 0.0477  0.1756  455 ALA   A CA  
3085 C  C   . ALA   A 435 ? 1.7464 1.1452 1.6733 -0.0898 0.0471  0.2090  455 ALA   A C   
3086 O  O   . ALA   A 435 ? 1.7995 1.1440 1.7125 -0.1111 0.0401  0.2231  455 ALA   A O   
3087 C  CB  . ALA   A 435 ? 1.7384 1.1988 1.6716 -0.1112 0.0426  0.1669  455 ALA   A CB  
3088 N  N   . LEU   A 436 ? 1.7728 1.2396 1.7263 -0.0708 0.0533  0.2224  456 LEU   A N   
3089 C  CA  . LEU   A 436 ? 1.7776 1.2583 1.7390 -0.0715 0.0519  0.2543  456 LEU   A CA  
3090 C  C   . LEU   A 436 ? 1.7692 1.1719 1.7085 -0.0521 0.0519  0.2694  456 LEU   A C   
3091 O  O   . LEU   A 436 ? 1.7290 1.1013 1.6580 -0.0681 0.0482  0.2947  456 LEU   A O   
3092 C  CB  . LEU   A 436 ? 1.6593 1.2217 1.6480 -0.0503 0.0548  0.2601  456 LEU   A CB  
3093 C  CG  . LEU   A 436 ? 1.5455 1.1833 1.5534 -0.0736 0.0535  0.2552  456 LEU   A CG  
3094 C  CD1 . LEU   A 436 ? 1.3987 1.0988 1.4226 -0.0591 0.0523  0.2708  456 LEU   A CD1 
3095 C  CD2 . LEU   A 436 ? 1.6418 1.2640 1.6419 -0.1131 0.0503  0.2674  456 LEU   A CD2 
3096 N  N   . ILE   A 437 ? 1.8237 1.1923 1.7553 -0.0162 0.0578  0.2555  457 ILE   A N   
3097 C  CA  . ILE   A 437 ? 1.9482 1.2384 1.8581 0.0077  0.0583  0.2679  457 ILE   A CA  
3098 C  C   . ILE   A 437 ? 2.0442 1.2443 1.9201 -0.0217 0.0513  0.2678  457 ILE   A C   
3099 O  O   . ILE   A 437 ? 2.0505 1.2092 1.9151 -0.0325 0.0465  0.2942  457 ILE   A O   
3100 C  CB  . ILE   A 437 ? 1.9643 1.2384 1.8747 0.0528  0.0693  0.2498  457 ILE   A CB  
3101 C  CG1 . ILE   A 437 ? 1.8734 1.2424 1.8262 0.0756  0.0746  0.2502  457 ILE   A CG1 
3102 C  CG2 . ILE   A 437 ? 2.0435 1.2376 1.9331 0.0828  0.0706  0.2624  457 ILE   A CG2 
3103 C  CD1 . ILE   A 437 ? 1.8423 1.2102 1.8063 0.1176  0.0889  0.2348  457 ILE   A CD1 
3104 N  N   . ARG   A 438 ? 1.9990 1.1654 1.8567 -0.0359 0.0493  0.2385  458 ARG   A N   
3105 C  CA  . ARG   A 438 ? 1.9971 1.0716 1.8221 -0.0644 0.0386  0.2339  458 ARG   A CA  
3106 C  C   . ARG   A 438 ? 1.9892 1.0798 1.8285 -0.1127 0.0293  0.2578  458 ARG   A C   
3107 O  O   . ARG   A 438 ? 2.1750 1.1933 1.9971 -0.1309 0.0228  0.2745  458 ARG   A O   
3108 C  CB  . ARG   A 438 ? 2.0561 1.1035 1.8584 -0.0727 0.0343  0.1962  458 ARG   A CB  
3109 C  CG  . ARG   A 438 ? 2.1801 1.1213 1.9346 -0.0464 0.0355  0.1754  458 ARG   A CG  
3110 C  CD  . ARG   A 438 ? 2.2830 1.1926 2.0338 0.0005  0.0480  0.1914  458 ARG   A CD  
3111 N  NE  . ARG   A 438 ? 2.4769 1.2737 2.1779 0.0234  0.0489  0.1730  458 ARG   A NE  
3112 C  CZ  . ARG   A 438 ? 2.4618 1.1937 2.1477 0.0555  0.0539  0.1870  458 ARG   A CZ  
3113 N  NH1 . ARG   A 438 ? 2.3768 1.1447 2.0926 0.0689  0.0568  0.2209  458 ARG   A NH1 
3114 N  NH2 . ARG   A 438 ? 2.5866 1.2120 2.2224 0.0769  0.0550  0.1661  458 ARG   A NH2 
3115 N  N   . VAL   A 439 ? 1.9196 1.1036 1.7913 -0.1332 0.0301  0.2610  459 VAL   A N   
3116 C  CA  . VAL   A 439 ? 2.0263 1.2348 1.9158 -0.1784 0.0253  0.2831  459 VAL   A CA  
3117 C  C   . VAL   A 439 ? 2.1801 1.3845 2.0698 -0.1730 0.0313  0.3229  459 VAL   A C   
3118 O  O   . VAL   A 439 ? 2.1514 1.3094 2.0348 -0.2024 0.0283  0.3457  459 VAL   A O   
3119 C  CB  . VAL   A 439 ? 1.9025 1.2133 1.8251 -0.1951 0.0268  0.2752  459 VAL   A CB  
3120 C  CG1 . VAL   A 439 ? 1.9719 1.3341 1.9181 -0.2231 0.0311  0.3074  459 VAL   A CG1 
3121 C  CG2 . VAL   A 439 ? 2.0816 1.3828 2.0030 -0.2203 0.0150  0.2450  459 VAL   A CG2 
3122 N  N   . LEU   A 440 ? 2.0711 1.3220 1.9674 -0.1358 0.0388  0.3326  460 LEU   A N   
3123 C  CA  . LEU   A 440 ? 2.0927 1.3462 1.9844 -0.1273 0.0424  0.3703  460 LEU   A CA  
3124 C  C   . LEU   A 440 ? 2.1366 1.2934 1.9987 -0.1057 0.0402  0.3848  460 LEU   A C   
3125 O  O   . LEU   A 440 ? 2.1026 1.2364 1.9526 -0.1089 0.0413  0.4198  460 LEU   A O   
3126 C  CB  . LEU   A 440 ? 2.0199 1.3572 1.9284 -0.0956 0.0460  0.3737  460 LEU   A CB  
3127 C  CG  . LEU   A 440 ? 1.9238 1.3551 1.8572 -0.1163 0.0490  0.3682  460 LEU   A CG  
3128 C  CD1 . LEU   A 440 ? 1.7760 1.2771 1.7258 -0.0828 0.0489  0.3576  460 LEU   A CD1 
3129 C  CD2 . LEU   A 440 ? 1.8448 1.2960 1.7752 -0.1432 0.0539  0.4016  460 LEU   A CD2 
3130 N  N   . GLN   A 441 ? 2.1384 1.2360 1.9853 -0.0818 0.0382  0.3596  461 GLN   A N   
3131 C  CA  . GLN   A 441 ? 2.1950 1.1916 2.0113 -0.0600 0.0362  0.3704  461 GLN   A CA  
3132 C  C   . GLN   A 441 ? 2.3184 1.2331 2.1141 -0.1014 0.0299  0.3868  461 GLN   A C   
3133 O  O   . GLN   A 441 ? 2.4170 1.2440 2.1856 -0.0878 0.0278  0.4036  461 GLN   A O   
3134 C  CB  . GLN   A 441 ? 2.1443 1.0939 1.9458 -0.0269 0.0380  0.3360  461 GLN   A CB  
3135 C  CG  . GLN   A 441 ? 2.1721 1.1251 1.9772 0.0312  0.0445  0.3404  461 GLN   A CG  
3136 C  CD  . GLN   A 441 ? 2.2397 1.1567 2.0329 0.0643  0.0520  0.3060  461 GLN   A CD  
3137 O  OE1 . GLN   A 441 ? 2.2477 1.1255 2.0202 0.0444  0.0504  0.2782  461 GLN   A OE1 
3138 N  NE2 . GLN   A 441 ? 2.2107 1.1422 2.0170 0.1160  0.0601  0.3082  461 GLN   A NE2 
3139 N  N   . ASN   A 442 ? 2.2980 1.2393 2.1090 -0.1512 0.0265  0.3834  462 ASN   A N   
3140 C  CA  . ASN   A 442 ? 2.2737 1.1424 2.0747 -0.1972 0.0189  0.3957  462 ASN   A CA  
3141 C  C   . ASN   A 442 ? 2.2215 1.1455 2.0480 -0.2395 0.0245  0.4293  462 ASN   A C   
3142 O  O   . ASN   A 442 ? 2.4288 1.2939 2.2464 -0.2665 0.0242  0.4590  462 ASN   A O   
3143 C  CB  . ASN   A 442 ? 2.3280 1.1633 2.1252 -0.2225 0.0063  0.3567  462 ASN   A CB  
3144 C  CG  . ASN   A 442 ? 2.4386 1.1836 2.1964 -0.1868 0.0016  0.3273  462 ASN   A CG  
3145 O  OD1 . ASN   A 442 ? 2.4728 1.2389 2.2251 -0.1374 0.0108  0.3158  462 ASN   A OD1 
3146 N  ND2 . ASN   A 442 ? 2.6188 1.2627 2.3497 -0.2116 -0.0127 0.3146  462 ASN   A ND2 
3147 N  N   . PHE   A 443 ? 2.1862 1.2199 2.0436 -0.2454 0.0312  0.4262  463 PHE   A N   
3148 C  CA  . PHE   A 443 ? 2.2119 1.3040 2.0962 -0.2867 0.0388  0.4527  463 PHE   A CA  
3149 C  C   . PHE   A 443 ? 2.1288 1.3088 2.0194 -0.2637 0.0522  0.4735  463 PHE   A C   
3150 O  O   . PHE   A 443 ? 2.0776 1.3057 1.9689 -0.2261 0.0520  0.4552  463 PHE   A O   
3151 C  CB  . PHE   A 443 ? 2.1597 1.3020 2.0777 -0.3241 0.0325  0.4271  463 PHE   A CB  
3152 C  CG  . PHE   A 443 ? 2.1844 1.2473 2.0927 -0.3438 0.0143  0.3982  463 PHE   A CG  
3153 C  CD1 . PHE   A 443 ? 2.3817 1.3771 2.2929 -0.3886 0.0058  0.4131  463 PHE   A CD1 
3154 C  CD2 . PHE   A 443 ? 2.1944 1.2483 2.0886 -0.3183 0.0053  0.3563  463 PHE   A CD2 
3155 C  CE1 . PHE   A 443 ? 2.4359 1.3530 2.3336 -0.4073 -0.0151 0.3838  463 PHE   A CE1 
3156 C  CE2 . PHE   A 443 ? 2.2657 1.2418 2.1414 -0.3341 -0.0126 0.3279  463 PHE   A CE2 
3157 C  CZ  . PHE   A 443 ? 2.4303 1.3366 2.3066 -0.3787 -0.0248 0.3402  463 PHE   A CZ  
3158 N  N   . SER   A 444 ? 2.0264 1.2250 1.9204 -0.2875 0.0639  0.5123  464 SER   A N   
3159 C  CA  . SER   A 444 ? 1.9922 1.2813 1.8918 -0.2768 0.0773  0.5305  464 SER   A CA  
3160 C  C   . SER   A 444 ? 1.9035 1.2728 1.8427 -0.3135 0.0845  0.5232  464 SER   A C   
3161 O  O   . SER   A 444 ? 1.9715 1.3240 1.9356 -0.3513 0.0785  0.5116  464 SER   A O   
3162 C  CB  . SER   A 444 ? 1.9814 1.2424 1.8531 -0.2755 0.0888  0.5795  464 SER   A CB  
3163 O  OG  . SER   A 444 ? 2.0057 1.3511 1.8755 -0.2656 0.1018  0.5960  464 SER   A OG  
3164 N  N   . PHE   A 445 ? 1.8531 1.3101 1.7980 -0.3007 0.0958  0.5292  465 PHE   A N   
3165 C  CA  . PHE   A 445 ? 1.7721 1.3130 1.7548 -0.3268 0.1038  0.5202  465 PHE   A CA  
3166 C  C   . PHE   A 445 ? 1.8341 1.4351 1.8100 -0.3261 0.1251  0.5534  465 PHE   A C   
3167 O  O   . PHE   A 445 ? 1.9665 1.5974 1.9156 -0.2896 0.1270  0.5556  465 PHE   A O   
3168 C  CB  . PHE   A 445 ? 1.7776 1.3711 1.7752 -0.3056 0.0935  0.4770  465 PHE   A CB  
3169 C  CG  . PHE   A 445 ? 1.7129 1.2580 1.7186 -0.3124 0.0760  0.4431  465 PHE   A CG  
3170 C  CD1 . PHE   A 445 ? 1.7868 1.2638 1.7649 -0.2829 0.0655  0.4297  465 PHE   A CD1 
3171 C  CD2 . PHE   A 445 ? 1.8113 1.3786 1.8504 -0.3464 0.0698  0.4248  465 PHE   A CD2 
3172 C  CE1 . PHE   A 445 ? 1.8003 1.2287 1.7775 -0.2861 0.0517  0.3979  465 PHE   A CE1 
3173 C  CE2 . PHE   A 445 ? 1.7722 1.2903 1.8095 -0.3511 0.0519  0.3928  465 PHE   A CE2 
3174 C  CZ  . PHE   A 445 ? 1.7342 1.1807 1.7372 -0.3205 0.0440  0.3790  465 PHE   A CZ  
3175 N  N   . LYS   A 446 ? 1.7804 1.3989 1.7805 -0.3665 0.1408  0.5792  466 LYS   A N   
3176 C  CA  . LYS   A 446 ? 1.6959 1.3744 1.6922 -0.3706 0.1665  0.6119  466 LYS   A CA  
3177 C  C   . LYS   A 446 ? 1.6441 1.4147 1.6875 -0.3890 0.1758  0.5959  466 LYS   A C   
3178 O  O   . LYS   A 446 ? 1.6102 1.3860 1.6958 -0.4144 0.1634  0.5717  466 LYS   A O   
3179 C  CB  . LYS   A 446 ? 1.7418 1.3747 1.7264 -0.3929 0.1828  0.6409  466 LYS   A CB  
3180 C  CG  . LYS   A 446 ? 1.9751 1.5154 1.9094 -0.3741 0.1766  0.6622  466 LYS   A CG  
3181 C  CD  . LYS   A 446 ? 2.0796 1.6329 1.9682 -0.3277 0.1740  0.6747  466 LYS   A CD  
3182 C  CE  . LYS   A 446 ? 2.1234 1.5844 1.9656 -0.3055 0.1642  0.6944  466 LYS   A CE  
3183 N  NZ  . LYS   A 446 ? 2.0397 1.4571 1.8565 -0.3237 0.1827  0.7240  466 LYS   A NZ  
3184 N  N   . PRO   A 447 ? 1.6142 1.4561 1.6479 -0.3735 0.1959  0.6058  467 PRO   A N   
3185 C  CA  . PRO   A 447 ? 1.5758 1.5017 1.6544 -0.3894 0.2090  0.5924  467 PRO   A CA  
3186 C  C   . PRO   A 447 ? 1.8355 1.7540 1.9509 -0.4284 0.2203  0.6012  467 PRO   A C   
3187 O  O   . PRO   A 447 ? 2.0019 1.8596 2.0978 -0.4403 0.2269  0.6242  467 PRO   A O   
3188 C  CB  . PRO   A 447 ? 1.5591 1.5421 1.6037 -0.3601 0.2309  0.6064  467 PRO   A CB  
3189 C  CG  . PRO   A 447 ? 1.6838 1.6256 1.6723 -0.3245 0.2185  0.6137  467 PRO   A CG  
3190 C  CD  . PRO   A 447 ? 1.7133 1.5621 1.6918 -0.3360 0.2047  0.6255  467 PRO   A CD  
3191 N  N   . CYS   A 448 ? 1.8186 1.7995 1.9891 -0.4481 0.2218  0.5831  468 CYS   A N   
3192 C  CA  . CYS   A 448 ? 1.7800 1.7650 1.9957 -0.4860 0.2306  0.5901  468 CYS   A CA  
3193 C  C   . CYS   A 448 ? 1.9693 2.0456 2.2131 -0.4850 0.2582  0.5964  468 CYS   A C   
3194 O  O   . CYS   A 448 ? 1.7528 1.8838 1.9786 -0.4547 0.2683  0.5917  468 CYS   A O   
3195 C  CB  . CYS   A 448 ? 1.8651 1.8310 2.1269 -0.5142 0.2017  0.5621  468 CYS   A CB  
3196 S  SG  . CYS   A 448 ? 2.4063 2.4053 2.7392 -0.5598 0.2082  0.5646  468 CYS   A SG  
3197 N  N   . LYS   A 449 ? 2.2394 2.3302 2.5281 -0.5180 0.2706  0.6070  469 LYS   A N   
3198 C  CA  . LYS   A 449 ? 2.1232 2.2951 2.4392 -0.5175 0.3010  0.6177  469 LYS   A CA  
3199 C  C   . LYS   A 449 ? 2.1914 2.4453 2.5413 -0.5017 0.2954  0.5900  469 LYS   A C   
3200 O  O   . LYS   A 449 ? 2.0770 2.3930 2.4196 -0.4790 0.3196  0.5947  469 LYS   A O   
3201 C  CB  . LYS   A 449 ? 2.0944 2.2673 2.4637 -0.5598 0.3112  0.6321  469 LYS   A CB  
3202 C  CG  . LYS   A 449 ? 2.0377 2.3038 2.4583 -0.5648 0.3365  0.6360  469 LYS   A CG  
3203 C  CD  . LYS   A 449 ? 1.9029 2.1962 2.4056 -0.6024 0.3194  0.6211  469 LYS   A CD  
3204 C  CE  . LYS   A 449 ? 1.7163 2.1094 2.2740 -0.6015 0.3418  0.6219  469 LYS   A CE  
3205 N  NZ  . LYS   A 449 ? 1.8533 2.3043 2.4351 -0.5806 0.3230  0.5891  469 LYS   A NZ  
3206 N  N   . GLU   A 450 ? 2.5273 2.7786 2.9096 -0.5115 0.2636  0.5605  470 GLU   A N   
3207 C  CA  . GLU   A 450 ? 2.3555 2.6782 2.7692 -0.4971 0.2551  0.5334  470 GLU   A CA  
3208 C  C   . GLU   A 450 ? 2.3519 2.6722 2.7193 -0.4609 0.2447  0.5173  470 GLU   A C   
3209 O  O   . GLU   A 450 ? 2.3045 2.6834 2.6888 -0.4436 0.2413  0.4964  470 GLU   A O   
3210 C  CB  . GLU   A 450 ? 2.3292 2.6523 2.8000 -0.5264 0.2243  0.5091  470 GLU   A CB  
3211 C  CG  . GLU   A 450 ? 2.4564 2.6876 2.9119 -0.5483 0.1969  0.5043  470 GLU   A CG  
3212 C  CD  . GLU   A 450 ? 2.6211 2.8117 3.0953 -0.5836 0.2040  0.5261  470 GLU   A CD  
3213 O  OE1 . GLU   A 450 ? 2.6901 2.8444 3.1939 -0.6140 0.1782  0.5131  470 GLU   A OE1 
3214 O  OE2 . GLU   A 450 ? 2.6880 2.8818 3.1453 -0.5811 0.2352  0.5560  470 GLU   A OE2 
3215 N  N   . THR   A 451 ? 2.0473 2.3012 2.3588 -0.4487 0.2389  0.5267  471 THR   A N   
3216 C  CA  . THR   A 451 ? 1.9708 2.2180 2.2444 -0.4182 0.2251  0.5112  471 THR   A CA  
3217 C  C   . THR   A 451 ? 1.8129 2.1296 2.0699 -0.3851 0.2440  0.5083  471 THR   A C   
3218 O  O   . THR   A 451 ? 1.7982 2.1340 2.0315 -0.3735 0.2710  0.5293  471 THR   A O   
3219 C  CB  . THR   A 451 ? 1.8357 2.0044 2.0526 -0.4075 0.2199  0.5283  471 THR   A CB  
3220 O  OG1 . THR   A 451 ? 1.8323 1.9301 2.0607 -0.4327 0.1968  0.5224  471 THR   A OG1 
3221 C  CG2 . THR   A 451 ? 1.5420 1.7147 1.7185 -0.3706 0.2104  0.5156  471 THR   A CG2 
3222 N  N   . GLN   A 452 ? 1.6421 1.9932 1.9082 -0.3695 0.2297  0.4811  472 GLN   A N   
3223 C  CA  . GLN   A 452 ? 1.6235 2.0378 1.8751 -0.3376 0.2444  0.4729  472 GLN   A CA  
3224 C  C   . GLN   A 452 ? 1.5846 1.9720 1.7664 -0.3046 0.2474  0.4803  472 GLN   A C   
3225 O  O   . GLN   A 452 ? 1.5501 1.8941 1.7056 -0.2868 0.2221  0.4557  472 GLN   A O   
3226 C  CB  . GLN   A 452 ? 1.7060 2.1595 1.9887 -0.3314 0.2263  0.4399  472 GLN   A CB  
3227 C  CG  . GLN   A 452 ? 1.5753 2.0706 1.8265 -0.2918 0.2364  0.4258  472 GLN   A CG  
3228 C  CD  . GLN   A 452 ? 1.4693 2.0359 1.7659 -0.2888 0.2406  0.4098  472 GLN   A CD  
3229 O  OE1 . GLN   A 452 ? 1.4808 2.0569 1.8265 -0.3091 0.2236  0.3953  472 GLN   A OE1 
3230 N  NE2 . GLN   A 452 ? 1.4594 2.0709 1.7372 -0.2617 0.2629  0.4111  472 GLN   A NE2 
3231 N  N   . ILE   A 453 ? 1.5523 1.9568 1.6989 -0.2895 0.2740  0.5035  473 ILE   A N   
3232 C  CA  . ILE   A 453 ? 1.5057 1.8843 1.5803 -0.2557 0.2739  0.5094  473 ILE   A CA  
3233 C  C   . ILE   A 453 ? 1.5353 1.9705 1.5805 -0.2285 0.2991  0.5129  473 ILE   A C   
3234 O  O   . ILE   A 453 ? 1.7230 2.1741 1.7674 -0.2325 0.3253  0.5298  473 ILE   A O   
3235 C  CB  . ILE   A 453 ? 1.4277 1.7436 1.4670 -0.2647 0.2785  0.5448  473 ILE   A CB  
3236 C  CG1 . ILE   A 453 ? 1.4281 1.6801 1.4908 -0.2872 0.2525  0.5375  473 ILE   A CG1 
3237 C  CG2 . ILE   A 453 ? 1.4532 1.7423 1.4164 -0.2259 0.2732  0.5467  473 ILE   A CG2 
3238 C  CD1 . ILE   A 453 ? 1.5398 1.7213 1.5685 -0.2946 0.2542  0.5707  473 ILE   A CD1 
3239 N  N   . PRO   A 454 ? 1.4486 1.8971 1.4644 -0.1943 0.2851  0.4806  474 PRO   A N   
3240 C  CA  . PRO   A 454 ? 1.3857 1.8030 1.3983 -0.1808 0.2489  0.4438  474 PRO   A CA  
3241 C  C   . PRO   A 454 ? 1.4309 1.8710 1.5075 -0.1987 0.2359  0.4177  474 PRO   A C   
3242 O  O   . PRO   A 454 ? 1.4734 1.9650 1.5942 -0.2134 0.2523  0.4218  474 PRO   A O   
3243 C  CB  . PRO   A 454 ? 1.4180 1.8520 1.3780 -0.1408 0.2459  0.4250  474 PRO   A CB  
3244 C  CG  . PRO   A 454 ? 1.4541 1.9401 1.3999 -0.1337 0.2832  0.4454  474 PRO   A CG  
3245 C  CD  . PRO   A 454 ? 1.6101 2.1205 1.6178 -0.1717 0.3048  0.4710  474 PRO   A CD  
3246 N  N   . LEU   A 455 ? 1.3656 1.7693 1.4481 -0.1963 0.2066  0.3915  475 LEU   A N   
3247 C  CA  . LEU   A 455 ? 1.3411 1.7587 1.4741 -0.2110 0.1924  0.3669  475 LEU   A CA  
3248 C  C   . LEU   A 455 ? 1.4052 1.8689 1.5403 -0.1872 0.1904  0.3393  475 LEU   A C   
3249 O  O   . LEU   A 455 ? 1.4770 1.9288 1.5748 -0.1592 0.1797  0.3222  475 LEU   A O   
3250 C  CB  . LEU   A 455 ? 1.2904 1.6480 1.4226 -0.2151 0.1658  0.3510  475 LEU   A CB  
3251 C  CG  . LEU   A 455 ? 1.2825 1.6379 1.4455 -0.2197 0.1454  0.3194  475 LEU   A CG  
3252 C  CD1 . LEU   A 455 ? 1.2259 1.5166 1.3893 -0.2336 0.1290  0.3173  475 LEU   A CD1 
3253 C  CD2 . LEU   A 455 ? 1.3053 1.6721 1.4511 -0.1892 0.1338  0.2904  475 LEU   A CD2 
3254 N  N   . LYS   A 456 ? 1.3939 1.9096 1.5740 -0.1980 0.1997  0.3355  476 LYS   A N   
3255 C  CA  . LYS   A 456 ? 1.2983 1.8502 1.4838 -0.1758 0.1946  0.3075  476 LYS   A CA  
3256 C  C   . LYS   A 456 ? 1.3536 1.8789 1.5562 -0.1790 0.1663  0.2791  476 LYS   A C   
3257 O  O   . LYS   A 456 ? 1.3774 1.8784 1.6067 -0.2042 0.1550  0.2807  476 LYS   A O   
3258 C  CB  . LYS   A 456 ? 1.3298 1.9511 1.5584 -0.1808 0.2147  0.3136  476 LYS   A CB  
3259 C  CG  . LYS   A 456 ? 1.4667 2.1225 1.7021 -0.1909 0.2480  0.3490  476 LYS   A CG  
3260 C  CD  . LYS   A 456 ? 1.6659 2.3978 1.9575 -0.1946 0.2660  0.3520  476 LYS   A CD  
3261 C  CE  . LYS   A 456 ? 1.5502 2.2920 1.8886 -0.2254 0.2777  0.3740  476 LYS   A CE  
3262 N  NZ  . LYS   A 456 ? 1.4572 2.1733 1.8396 -0.2605 0.2511  0.3694  476 LYS   A NZ  
3263 N  N   . LEU   A 457 ? 1.4195 1.9459 1.6032 -0.1530 0.1553  0.2532  477 LEU   A N   
3264 C  CA  . LEU   A 457 ? 1.4280 1.9372 1.6277 -0.1532 0.1332  0.2271  477 LEU   A CA  
3265 C  C   . LEU   A 457 ? 1.5556 2.1117 1.7977 -0.1592 0.1344  0.2187  477 LEU   A C   
3266 O  O   . LEU   A 457 ? 1.6689 2.2757 1.9225 -0.1511 0.1520  0.2254  477 LEU   A O   
3267 C  CB  . LEU   A 457 ? 1.2395 1.7303 1.4060 -0.1253 0.1211  0.2052  477 LEU   A CB  
3268 C  CG  . LEU   A 457 ? 1.2347 1.6741 1.3731 -0.1214 0.1097  0.2072  477 LEU   A CG  
3269 C  CD1 . LEU   A 457 ? 1.3169 1.7448 1.4357 -0.0979 0.0954  0.1848  477 LEU   A CD1 
3270 C  CD2 . LEU   A 457 ? 1.3408 1.7422 1.4978 -0.1424 0.0997  0.2087  477 LEU   A CD2 
3271 N  N   . SER   A 458 ? 1.6274 2.1664 1.8917 -0.1718 0.1157  0.2046  478 SER   A N   
3272 C  CA  . SER   A 458 ? 1.7199 2.3006 2.0227 -0.1749 0.1110  0.1949  478 SER   A CA  
3273 C  C   . SER   A 458 ? 1.8772 2.4827 2.1666 -0.1435 0.1133  0.1773  478 SER   A C   
3274 O  O   . SER   A 458 ? 1.8770 2.4516 2.1440 -0.1288 0.0994  0.1573  478 SER   A O   
3275 C  CB  . SER   A 458 ? 1.6898 2.2383 2.0056 -0.1904 0.0873  0.1807  478 SER   A CB  
3276 O  OG  . SER   A 458 ? 1.8330 2.4211 2.1823 -0.1902 0.0791  0.1706  478 SER   A OG  
3277 N  N   . LEU   A 459 ? 2.3383 2.9978 2.6411 -0.1327 0.1323  0.1853  479 LEU   A N   
3278 C  CA  . LEU   A 459 ? 2.2983 2.9796 2.5878 -0.1013 0.1352  0.1680  479 LEU   A CA  
3279 C  C   . LEU   A 459 ? 2.3399 3.0192 2.6474 -0.0964 0.1150  0.1469  479 LEU   A C   
3280 O  O   . LEU   A 459 ? 2.3668 3.0474 2.6574 -0.0703 0.1126  0.1297  479 LEU   A O   
3281 C  CB  . LEU   A 459 ? 2.3010 3.0448 2.6084 -0.0905 0.1614  0.1812  479 LEU   A CB  
3282 C  CG  . LEU   A 459 ? 2.3569 3.1053 2.6247 -0.0762 0.1857  0.1952  479 LEU   A CG  
3283 C  CD1 . LEU   A 459 ? 2.3529 3.0731 2.6090 -0.0999 0.1905  0.2185  479 LEU   A CD1 
3284 C  CD2 . LEU   A 459 ? 2.3595 3.1747 2.6500 -0.0630 0.2143  0.2068  479 LEU   A CD2 
3285 N  N   . GLY   A 460 ? 2.0101 2.6817 2.3469 -0.1202 0.0995  0.1476  480 GLY   A N   
3286 C  CA  . GLY   A 460 ? 1.9529 2.6165 2.2993 -0.1158 0.0789  0.1292  480 GLY   A CA  
3287 C  C   . GLY   A 460 ? 2.0303 2.6345 2.3373 -0.1064 0.0650  0.1120  480 GLY   A C   
3288 O  O   . GLY   A 460 ? 1.9903 2.5769 2.2655 -0.0878 0.0705  0.1058  480 GLY   A O   
3289 N  N   . GLY   A 461 ? 1.9237 2.4966 2.2323 -0.1192 0.0467  0.1045  481 GLY   A N   
3290 C  CA  . GLY   A 461 ? 1.8603 2.3834 2.1370 -0.1087 0.0362  0.0891  481 GLY   A CA  
3291 C  C   . GLY   A 461 ? 1.8454 2.3203 2.0962 -0.1150 0.0380  0.0919  481 GLY   A C   
3292 O  O   . GLY   A 461 ? 1.8047 2.2716 2.0366 -0.1025 0.0459  0.0923  481 GLY   A O   
3293 N  N   . LEU   A 462 ? 1.9045 2.3457 2.1533 -0.1329 0.0289  0.0929  482 LEU   A N   
3294 C  CA  . LEU   A 462 ? 1.8971 2.2895 2.1225 -0.1355 0.0302  0.0943  482 LEU   A CA  
3295 C  C   . LEU   A 462 ? 1.9048 2.3016 2.1311 -0.1435 0.0416  0.1119  482 LEU   A C   
3296 O  O   . LEU   A 462 ? 1.8573 2.2914 2.1027 -0.1522 0.0494  0.1246  482 LEU   A O   
3297 C  CB  . LEU   A 462 ? 1.9398 2.2911 2.1573 -0.1493 0.0181  0.0887  482 LEU   A CB  
3298 C  CG  . LEU   A 462 ? 1.9475 2.3075 2.1860 -0.1744 0.0089  0.0950  482 LEU   A CG  
3299 C  CD1 . LEU   A 462 ? 2.0307 2.3329 2.2499 -0.1885 0.0021  0.0941  482 LEU   A CD1 
3300 C  CD2 . LEU   A 462 ? 1.9071 2.2936 2.1613 -0.1747 -0.0055 0.0854  482 LEU   A CD2 
3301 N  N   . LEU   A 463 ? 1.6532 2.0122 1.8591 -0.1393 0.0436  0.1143  483 LEU   A N   
3302 C  CA  . LEU   A 463 ? 1.6236 1.9815 1.8227 -0.1416 0.0531  0.1315  483 LEU   A CA  
3303 C  C   . LEU   A 463 ? 1.6279 1.9641 1.8341 -0.1656 0.0528  0.1453  483 LEU   A C   
3304 O  O   . LEU   A 463 ? 1.5465 1.8355 1.7394 -0.1691 0.0488  0.1457  483 LEU   A O   
3305 C  CB  . LEU   A 463 ? 1.4231 1.7534 1.6016 -0.1252 0.0524  0.1290  483 LEU   A CB  
3306 C  CG  . LEU   A 463 ? 1.3382 1.6785 1.5044 -0.1203 0.0600  0.1451  483 LEU   A CG  
3307 C  CD1 . LEU   A 463 ? 1.2984 1.6833 1.4629 -0.1092 0.0663  0.1433  483 LEU   A CD1 
3308 C  CD2 . LEU   A 463 ? 1.1946 1.5072 1.3453 -0.1060 0.0549  0.1447  483 LEU   A CD2 
3309 N  N   . GLN   A 464 ? 1.5491 1.9198 1.7782 -0.1818 0.0579  0.1572  484 GLN   A N   
3310 C  CA  . GLN   A 464 ? 1.5315 1.8876 1.7740 -0.2089 0.0580  0.1732  484 GLN   A CA  
3311 C  C   . GLN   A 464 ? 1.4575 1.8501 1.7101 -0.2147 0.0759  0.1971  484 GLN   A C   
3312 O  O   . GLN   A 464 ? 1.5130 1.9471 1.7634 -0.1972 0.0870  0.1977  484 GLN   A O   
3313 C  CB  . GLN   A 464 ? 1.6132 1.9786 1.8830 -0.2291 0.0443  0.1653  484 GLN   A CB  
3314 C  CG  . GLN   A 464 ? 1.7122 2.0359 1.9638 -0.2237 0.0272  0.1430  484 GLN   A CG  
3315 C  CD  . GLN   A 464 ? 1.8555 2.1685 2.1236 -0.2483 0.0091  0.1377  484 GLN   A CD  
3316 O  OE1 . GLN   A 464 ? 1.8461 2.1044 2.0983 -0.2618 -0.0003 0.1355  484 GLN   A OE1 
3317 N  NE2 . GLN   A 464 ? 1.7655 2.1295 2.0652 -0.2532 0.0022  0.1347  484 GLN   A NE2 
3318 N  N   . PRO   A 465 ? 1.5991 1.9734 1.8591 -0.2380 0.0803  0.2175  485 PRO   A N   
3319 C  CA  . PRO   A 465 ? 1.5985 2.0112 1.8716 -0.2467 0.1006  0.2437  485 PRO   A CA  
3320 C  C   . PRO   A 465 ? 1.5028 1.9727 1.8253 -0.2651 0.1039  0.2483  485 PRO   A C   
3321 O  O   . PRO   A 465 ? 1.4055 1.8709 1.7548 -0.2837 0.0864  0.2380  485 PRO   A O   
3322 C  CB  . PRO   A 465 ? 1.5483 1.9106 1.8106 -0.2662 0.1025  0.2649  485 PRO   A CB  
3323 C  CG  . PRO   A 465 ? 1.4471 1.7444 1.6857 -0.2608 0.0840  0.2472  485 PRO   A CG  
3324 C  CD  . PRO   A 465 ? 1.3614 1.6713 1.6101 -0.2536 0.0695  0.2192  485 PRO   A CD  
3325 N  N   . GLU   A 466 ? 1.4568 1.9823 1.7904 -0.2580 0.1263  0.2638  486 GLU   A N   
3326 C  CA  . GLU   A 466 ? 1.4633 2.0535 1.8511 -0.2740 0.1352  0.2741  486 GLU   A CA  
3327 C  C   . GLU   A 466 ? 1.4932 2.0709 1.9192 -0.3155 0.1294  0.2918  486 GLU   A C   
3328 O  O   . GLU   A 466 ? 1.4828 2.0559 1.9386 -0.3340 0.1063  0.2786  486 GLU   A O   
3329 C  CB  . GLU   A 466 ? 1.4970 2.1407 1.8825 -0.2581 0.1667  0.2929  486 GLU   A CB  
3330 C  CG  . GLU   A 466 ? 1.6209 2.3438 2.0622 -0.2607 0.1783  0.2973  486 GLU   A CG  
3331 C  CD  . GLU   A 466 ? 1.6217 2.3924 2.0463 -0.2317 0.2091  0.3062  486 GLU   A CD  
3332 O  OE1 . GLU   A 466 ? 1.5310 2.3432 1.9880 -0.2330 0.2269  0.3168  486 GLU   A OE1 
3333 O  OE2 . GLU   A 466 ? 1.7201 2.4650 2.0881 -0.2011 0.2098  0.2928  486 GLU   A OE2 
3334 N  N   . LYS   A 467 ? 1.3324 1.9015 1.7555 -0.3307 0.1487  0.3218  487 LYS   A N   
3335 C  CA  . LYS   A 467 ? 1.3874 1.9290 1.8407 -0.3719 0.1413  0.3389  487 LYS   A CA  
3336 C  C   . LYS   A 467 ? 1.4058 1.8565 1.8160 -0.3744 0.1206  0.3278  487 LYS   A C   
3337 O  O   . LYS   A 467 ? 1.4854 1.8999 1.8438 -0.3484 0.1250  0.3248  487 LYS   A O   
3338 C  CB  . LYS   A 467 ? 1.3911 1.9425 1.8488 -0.3810 0.1697  0.3703  487 LYS   A CB  
3339 C  CG  . LYS   A 467 ? 1.4312 2.0564 1.9124 -0.3641 0.1949  0.3751  487 LYS   A CG  
3340 C  CD  . LYS   A 467 ? 1.4094 2.0339 1.8804 -0.3686 0.2258  0.4056  487 LYS   A CD  
3341 C  CE  . LYS   A 467 ? 1.2783 1.9666 1.8007 -0.3736 0.2454  0.4133  487 LYS   A CE  
3342 N  NZ  . LYS   A 467 ? 1.1634 1.8446 1.7420 -0.4141 0.2335  0.4194  487 LYS   A NZ  
3343 N  N   . PRO   A 468 ? 1.3746 1.7874 1.8048 -0.4038 0.0968  0.3202  488 PRO   A N   
3344 C  CA  . PRO   A 468 ? 1.3743 1.6971 1.7618 -0.4042 0.0792  0.3091  488 PRO   A CA  
3345 C  C   . PRO   A 468 ? 1.4186 1.6958 1.7718 -0.4022 0.0958  0.3348  488 PRO   A C   
3346 O  O   . PRO   A 468 ? 1.4494 1.7573 1.8169 -0.4125 0.1193  0.3658  488 PRO   A O   
3347 C  CB  . PRO   A 468 ? 1.3225 1.6205 1.7441 -0.4431 0.0548  0.3040  488 PRO   A CB  
3348 C  CG  . PRO   A 468 ? 1.3846 1.7591 1.8564 -0.4480 0.0479  0.2941  488 PRO   A CG  
3349 C  CD  . PRO   A 468 ? 1.4395 1.8913 1.9287 -0.4312 0.0799  0.3137  488 PRO   A CD  
3350 N  N   . VAL   A 469 ? 1.3939 1.5982 1.7015 -0.3874 0.0848  0.3235  489 VAL   A N   
3351 C  CA  . VAL   A 469 ? 1.5642 1.7191 1.8356 -0.3806 0.0965  0.3462  489 VAL   A CA  
3352 C  C   . VAL   A 469 ? 1.5537 1.6500 1.8361 -0.4175 0.0893  0.3626  489 VAL   A C   
3353 O  O   . VAL   A 469 ? 1.5492 1.5880 1.8246 -0.4269 0.0667  0.3427  489 VAL   A O   
3354 C  CB  . VAL   A 469 ? 1.3547 1.4637 1.5780 -0.3446 0.0882  0.3272  489 VAL   A CB  
3355 C  CG1 . VAL   A 469 ? 1.4173 1.4623 1.6066 -0.3403 0.0933  0.3492  489 VAL   A CG1 
3356 C  CG2 . VAL   A 469 ? 1.3970 1.5602 1.6084 -0.3106 0.0966  0.3168  489 VAL   A CG2 
3357 N  N   . VAL   A 470 ? 1.3924 1.4994 1.6888 -0.4381 0.1090  0.3991  490 VAL   A N   
3358 C  CA  . VAL   A 470 ? 1.6655 1.7168 1.9757 -0.4768 0.1044  0.4198  490 VAL   A CA  
3359 C  C   . VAL   A 470 ? 1.6899 1.7038 1.9647 -0.4699 0.1248  0.4553  490 VAL   A C   
3360 O  O   . VAL   A 470 ? 1.7641 1.8280 2.0343 -0.4576 0.1507  0.4771  490 VAL   A O   
3361 C  CB  . VAL   A 470 ? 1.6383 1.7403 2.0093 -0.5107 0.1071  0.4247  490 VAL   A CB  
3362 C  CG1 . VAL   A 470 ? 1.5747 1.6846 1.9767 -0.5263 0.0768  0.3928  490 VAL   A CG1 
3363 C  CG2 . VAL   A 470 ? 1.6457 1.8389 2.0361 -0.4951 0.1356  0.4364  490 VAL   A CG2 
3364 N  N   . LEU   A 471 ? 1.6740 1.5960 1.9189 -0.4743 0.1128  0.4584  491 LEU   A N   
3365 C  CA  . LEU   A 471 ? 1.7253 1.5965 1.9252 -0.4586 0.1259  0.4868  491 LEU   A CA  
3366 C  C   . LEU   A 471 ? 1.8424 1.6286 2.0403 -0.4881 0.1187  0.5006  491 LEU   A C   
3367 O  O   . LEU   A 471 ? 1.8475 1.5950 2.0634 -0.5111 0.0964  0.4788  491 LEU   A O   
3368 C  CB  . LEU   A 471 ? 1.6832 1.5227 1.8338 -0.4111 0.1158  0.4641  491 LEU   A CB  
3369 C  CG  . LEU   A 471 ? 1.6683 1.5744 1.8059 -0.3723 0.1219  0.4486  491 LEU   A CG  
3370 C  CD1 . LEU   A 471 ? 1.7390 1.6039 1.8281 -0.3331 0.1183  0.4489  491 LEU   A CD1 
3371 C  CD2 . LEU   A 471 ? 1.5123 1.4928 1.6616 -0.3758 0.1473  0.4739  491 LEU   A CD2 
3372 N  N   . LYS   A 472 ? 1.8311 1.5851 2.0011 -0.4834 0.1369  0.5318  492 LYS   A N   
3373 C  CA  . LYS   A 472 ? 1.7369 1.3988 1.8937 -0.5024 0.1307  0.5417  492 LYS   A CA  
3374 C  C   . LYS   A 472 ? 1.7617 1.3349 1.8751 -0.4803 0.1102  0.5326  492 LYS   A C   
3375 O  O   . LYS   A 472 ? 1.7666 1.3472 1.8485 -0.4421 0.1103  0.5316  492 LYS   A O   
3376 C  CB  . LYS   A 472 ? 1.7246 1.3768 1.8619 -0.5039 0.1579  0.5796  492 LYS   A CB  
3377 C  CG  . LYS   A 472 ? 1.7992 1.4020 1.9575 -0.5424 0.1597  0.5890  492 LYS   A CG  
3378 C  CD  . LYS   A 472 ? 1.8668 1.4656 2.0058 -0.5454 0.1903  0.6282  492 LYS   A CD  
3379 C  CE  . LYS   A 472 ? 2.1401 1.6286 2.2322 -0.5412 0.1865  0.6460  492 LYS   A CE  
3380 N  NZ  . LYS   A 472 ? 2.1467 1.6276 2.1960 -0.5272 0.2141  0.6851  492 LYS   A NZ  
3381 N  N   . VAL   A 473 ? 1.8141 1.3039 1.9250 -0.4996 0.0926  0.5207  493 VAL   A N   
3382 C  CA  . VAL   A 473 ? 1.9298 1.3236 1.9981 -0.4782 0.0740  0.5098  493 VAL   A CA  
3383 C  C   . VAL   A 473 ? 2.2393 1.5432 2.2835 -0.4862 0.0780  0.5294  493 VAL   A C   
3384 O  O   . VAL   A 473 ? 2.1994 1.4901 2.2698 -0.5221 0.0797  0.5315  493 VAL   A O   
3385 C  CB  . VAL   A 473 ? 2.0242 1.3910 2.0999 -0.4853 0.0467  0.4665  493 VAL   A CB  
3386 C  CG1 . VAL   A 473 ? 2.0034 1.3008 2.0297 -0.4404 0.0366  0.4427  493 VAL   A CG1 
3387 C  CG2 . VAL   A 473 ? 1.9147 1.3837 2.0234 -0.4823 0.0464  0.4419  493 VAL   A CG2 
3388 N  N   . GLU   A 474 ? 2.3492 1.5926 2.3462 -0.4519 0.0790  0.5444  494 GLU   A N   
3389 C  CA  . GLU   A 474 ? 2.4148 1.5648 2.3820 -0.4520 0.0824  0.5632  494 GLU   A CA  
3390 C  C   . GLU   A 474 ? 2.4716 1.5281 2.4001 -0.4208 0.0629  0.5452  494 GLU   A C   
3391 O  O   . GLU   A 474 ? 2.4163 1.4881 2.3304 -0.3866 0.0549  0.5331  494 GLU   A O   
3392 C  CB  . GLU   A 474 ? 2.4859 1.6517 2.4275 -0.4358 0.1065  0.6052  494 GLU   A CB  
3393 C  CG  . GLU   A 474 ? 2.3800 1.6233 2.3525 -0.4657 0.1305  0.6247  494 GLU   A CG  
3394 C  CD  . GLU   A 474 ? 2.3897 1.6592 2.3269 -0.4430 0.1534  0.6616  494 GLU   A CD  
3395 O  OE1 . GLU   A 474 ? 2.3501 1.6219 2.2528 -0.4022 0.1479  0.6663  494 GLU   A OE1 
3396 O  OE2 . GLU   A 474 ? 2.4707 1.7584 2.4138 -0.4654 0.1762  0.6858  494 GLU   A OE2 
3397 N  N   . SER   A 475 ? 2.4184 1.3796 2.3318 -0.4304 0.0565  0.5422  495 SER   A N   
3398 C  CA  . SER   A 475 ? 2.4624 1.3275 2.3390 -0.4006 0.0393  0.5207  495 SER   A CA  
3399 C  C   . SER   A 475 ? 2.4991 1.3098 2.3352 -0.3616 0.0485  0.5505  495 SER   A C   
3400 O  O   . SER   A 475 ? 2.5865 1.3798 2.4177 -0.3726 0.0639  0.5829  495 SER   A O   
3401 C  CB  . SER   A 475 ? 2.5190 1.3092 2.4013 -0.4296 0.0248  0.4963  495 SER   A CB  
3402 O  OG  . SER   A 475 ? 2.6867 1.4076 2.5376 -0.4025 0.0058  0.4606  495 SER   A OG  
3403 N  N   . ARG   A 476 ? 2.4385 1.2223 2.2455 -0.3150 0.0392  0.5397  496 ARG   A N   
3404 C  CA  . ARG   A 476 ? 2.4372 1.1730 2.2085 -0.2712 0.0437  0.5653  496 ARG   A CA  
3405 C  C   . ARG   A 476 ? 2.5815 1.2046 2.3310 -0.2582 0.0366  0.5549  496 ARG   A C   
3406 O  O   . ARG   A 476 ? 2.6984 1.2765 2.4498 -0.2803 0.0435  0.5736  496 ARG   A O   
3407 C  CB  . ARG   A 476 ? 2.3813 1.1643 2.1441 -0.2197 0.0401  0.5542  496 ARG   A CB  
3408 C  CG  . ARG   A 476 ? 2.2447 1.1579 2.0385 -0.2234 0.0488  0.5505  496 ARG   A CG  
3409 C  CD  . ARG   A 476 ? 2.0997 1.0692 1.8947 -0.1699 0.0468  0.5290  496 ARG   A CD  
3410 N  NE  . ARG   A 476 ? 2.1178 1.0886 1.8912 -0.1323 0.0487  0.5606  496 ARG   A NE  
3411 C  CZ  . ARG   A 476 ? 2.1745 1.1544 1.9434 -0.0805 0.0428  0.5503  496 ARG   A CZ  
3412 N  NH1 . ARG   A 476 ? 2.1656 1.1545 1.9495 -0.0588 0.0388  0.5108  496 ARG   A NH1 
3413 N  NH2 . ARG   A 476 ? 2.1990 1.1808 1.9488 -0.0494 0.0409  0.5816  496 ARG   A NH2 
3414 C  CHA . HEM   B .   ? 0.8538 0.9388 0.9929 -0.0277 0.1088  0.0662  601 HEM   A CHA 
3415 C  CHB . HEM   B .   ? 0.8709 0.9911 1.0415 -0.0458 0.0741  0.0893  601 HEM   A CHB 
3416 C  CHC . HEM   B .   ? 1.0148 0.9672 1.0861 -0.0478 0.0873  0.0769  601 HEM   A CHC 
3417 C  CHD . HEM   B .   ? 0.9903 0.9113 0.9986 -0.0137 0.1253  0.0477  601 HEM   A CHD 
3418 C  C1A . HEM   B .   ? 0.8939 1.0025 1.0538 -0.0338 0.0962  0.0710  601 HEM   A C1A 
3419 C  C2A . HEM   B .   ? 0.9544 1.1021 1.1428 -0.0371 0.0853  0.0733  601 HEM   A C2A 
3420 C  C3A . HEM   B .   ? 0.7877 0.9458 0.9815 -0.0408 0.0758  0.0789  601 HEM   A C3A 
3421 C  C4A . HEM   B .   ? 0.8504 0.9755 1.0235 -0.0416 0.0802  0.0813  601 HEM   A C4A 
3422 C  CMA . HEM   B .   ? 0.7091 0.9020 0.9213 -0.0428 0.0622  0.0819  601 HEM   A CMA 
3423 C  CAA . HEM   B .   ? 0.7506 0.9181 0.9555 -0.0362 0.0843  0.0700  601 HEM   A CAA 
3424 C  CBA . HEM   B .   ? 0.7407 0.9205 0.9838 -0.0290 0.0912  0.0769  601 HEM   A CBA 
3425 C  CGA . HEM   B .   ? 0.9270 1.1223 1.1889 -0.0315 0.0879  0.0741  601 HEM   A CGA 
3426 O  O1A . HEM   B .   ? 0.7988 1.0127 1.0996 -0.0303 0.0858  0.0788  601 HEM   A O1A 
3427 O  O2A . HEM   B .   ? 0.9969 1.1850 1.2365 -0.0349 0.0858  0.0675  601 HEM   A O2A 
3428 C  C1B . HEM   B .   ? 0.9278 1.0095 1.0772 -0.0481 0.0770  0.0910  601 HEM   A C1B 
3429 C  C2B . HEM   B .   ? 0.9404 1.0105 1.0860 -0.0534 0.0714  0.1017  601 HEM   A C2B 
3430 C  C3B . HEM   B .   ? 1.0506 1.0734 1.1719 -0.0552 0.0751  0.0989  601 HEM   A C3B 
3431 C  C4B . HEM   B .   ? 0.9960 1.0003 1.1010 -0.0495 0.0831  0.0855  601 HEM   A C4B 
3432 C  CMB . HEM   B .   ? 0.9481 1.0509 1.1093 -0.0554 0.0625  0.1139  601 HEM   A CMB 
3433 C  CAB . HEM   B .   ? 1.0591 1.0435 1.1654 -0.0619 0.0717  0.1076  601 HEM   A CAB 
3434 C  CBB . HEM   B .   ? 1.0282 1.0243 1.1432 -0.0676 0.0657  0.1227  601 HEM   A CBB 
3435 C  C1C . HEM   B .   ? 1.0911 1.0199 1.1382 -0.0380 0.0971  0.0652  601 HEM   A C1C 
3436 C  C2C . HEM   B .   ? 1.2519 1.1194 1.2564 -0.0309 0.1028  0.0554  601 HEM   A C2C 
3437 C  C3C . HEM   B .   ? 1.2514 1.1100 1.2347 -0.0201 0.1136  0.0464  601 HEM   A C3C 
3438 C  C4C . HEM   B .   ? 1.1269 1.0405 1.1430 -0.0216 0.1148  0.0514  601 HEM   A C4C 
3439 C  CMC . HEM   B .   ? 1.3185 1.1337 1.3010 -0.0346 0.0972  0.0553  601 HEM   A CMC 
3440 C  CAC . HEM   B .   ? 1.1982 0.9920 1.1254 -0.0074 0.1228  0.0330  601 HEM   A CAC 
3441 C  CBC . HEM   B .   ? 1.2864 1.0701 1.1848 0.0026  0.1330  0.0254  601 HEM   A CBC 
3442 C  C1D . HEM   B .   ? 1.0506 1.0177 1.0911 -0.0156 0.1256  0.0528  601 HEM   A C1D 
3443 C  C2D . HEM   B .   ? 1.0187 0.9892 1.0491 -0.0098 0.1349  0.0508  601 HEM   A C2D 
3444 C  C3D . HEM   B .   ? 1.0190 1.0339 1.0885 -0.0149 0.1302  0.0565  601 HEM   A C3D 
3445 C  C4D . HEM   B .   ? 0.9711 1.0135 1.0733 -0.0225 0.1179  0.0617  601 HEM   A C4D 
3446 C  CMD . HEM   B .   ? 0.8954 0.8207 0.8724 0.0012  0.1473  0.0433  601 HEM   A CMD 
3447 C  CAD . HEM   B .   ? 0.9022 0.9309 0.9770 -0.0123 0.1369  0.0581  601 HEM   A CAD 
3448 C  CBD . HEM   B .   ? 0.9796 1.0117 1.0815 0.0008  0.1620  0.0681  601 HEM   A CBD 
3449 C  CGD . HEM   B .   ? 1.0645 1.1051 1.1745 0.0023  0.1723  0.0729  601 HEM   A CGD 
3450 O  O1D . HEM   B .   ? 0.9934 1.0256 1.1103 0.0136  0.1984  0.0813  601 HEM   A O1D 
3451 O  O2D . HEM   B .   ? 0.9668 1.0216 1.0771 -0.0070 0.1562  0.0694  601 HEM   A O2D 
3452 N  NA  . HEM   B .   ? 0.8569 0.9514 1.0088 -0.0370 0.0917  0.0748  601 HEM   A NA  
3453 N  NB  . HEM   B .   ? 1.0048 1.0467 1.1283 -0.0454 0.0851  0.0825  601 HEM   A NB  
3454 N  NC  . HEM   B .   ? 1.1598 1.1138 1.2134 -0.0323 0.1037  0.0613  601 HEM   A NC  
3455 N  ND  . HEM   B .   ? 1.0891 1.1020 1.1731 -0.0229 0.1162  0.0608  601 HEM   A ND  
3456 FE FE  . HEM   B .   ? 0.9865 1.0153 1.0946 -0.0334 0.1006  0.0703  601 HEM   A FE  
3457 C  C02 . A1A06 C .   ? 1.7591 2.1420 1.9835 -0.0400 -0.0109 0.0429  602 A1A06 A C02 
3458 C  C05 . A1A06 C .   ? 1.7582 2.0998 1.9595 -0.0290 -0.0024 0.0391  602 A1A06 A C05 
3459 C  C08 . A1A06 C .   ? 1.6140 1.9231 1.8134 -0.0532 0.0071  0.0441  602 A1A06 A C08 
3460 C  C09 . A1A06 C .   ? 1.4628 1.7307 1.6412 -0.0594 0.0086  0.0431  602 A1A06 A C09 
3461 C  C12 . A1A06 C .   ? 1.2017 1.3971 1.3407 -0.0518 0.0254  0.0423  602 A1A06 A C12 
3462 C  C13 . A1A06 C .   ? 1.3128 1.4825 1.4179 -0.0411 0.0242  0.0387  602 A1A06 A C13 
3463 C  C15 . A1A06 C .   ? 1.4126 1.5613 1.4885 -0.0677 -0.0122 0.0255  602 A1A06 A C15 
3464 C  C16 . A1A06 C .   ? 1.4931 1.6270 1.5416 -0.0728 -0.0364 0.0161  602 A1A06 A C16 
3465 C  C17 . A1A06 C .   ? 1.4864 1.5887 1.5197 -0.0896 -0.0498 0.0091  602 A1A06 A C17 
3466 C  C18 . A1A06 C .   ? 1.4626 1.5897 1.5336 -0.1129 -0.0592 0.0131  602 A1A06 A C18 
3467 C  C19 . A1A06 C .   ? 1.3984 1.4895 1.4557 -0.1308 -0.0728 0.0073  602 A1A06 A C19 
3468 C  C20 . A1A06 C .   ? 1.4109 1.4372 1.4105 -0.1229 -0.0785 -0.0058 602 A1A06 A C20 
3469 C  C21 . A1A06 C .   ? 1.5167 1.5201 1.4744 -0.0967 -0.0671 -0.0101 602 A1A06 A C21 
3470 C  C22 . A1A06 C .   ? 1.5287 1.5706 1.5057 -0.0818 -0.0525 -0.0013 602 A1A06 A C22 
3471 C  C23 . A1A06 C .   ? 1.3325 1.4406 1.3907 -0.0632 0.0054  0.0265  602 A1A06 A C23 
3472 C  C26 . A1A06 C .   ? 1.1525 1.2342 1.2252 -0.0623 0.0303  0.0352  602 A1A06 A C26 
3473 C  C27 . A1A06 C .   ? 1.2710 1.2993 1.3024 -0.0643 0.0238  0.0263  602 A1A06 A C27 
3474 C  C28 . A1A06 C .   ? 1.0988 1.1089 1.1376 -0.0750 0.0220  0.0294  602 A1A06 A C28 
3475 C  C29 . A1A06 C .   ? 1.1017 1.1426 1.1807 -0.0746 0.0334  0.0427  602 A1A06 A C29 
3476 C  C30 . A1A06 C .   ? 1.0466 1.1268 1.1588 -0.0905 0.0254  0.0508  602 A1A06 A C30 
3477 C  C31 . A1A06 C .   ? 0.9521 1.0548 1.0904 -0.0869 0.0339  0.0622  602 A1A06 A C31 
3478 C  C32 . A1A06 C .   ? 1.0275 1.1180 1.1672 -0.0687 0.0481  0.0656  602 A1A06 A C32 
3479 C  C34 . A1A06 C .   ? 1.0502 1.0830 1.1341 -0.0561 0.0526  0.0486  602 A1A06 A C34 
3480 C  C35 . A1A06 C .   ? 1.1756 1.3583 1.3251 -0.0475 0.0421  0.0478  602 A1A06 A C35 
3481 C  C36 . A1A06 C .   ? 1.1491 1.3337 1.3121 -0.0550 0.0432  0.0516  602 A1A06 A C36 
3482 C  C37 . A1A06 C .   ? 1.1129 1.2676 1.2652 -0.0509 0.0533  0.0536  602 A1A06 A C37 
3483 C  C38 . A1A06 C .   ? 1.1010 1.2530 1.2631 -0.0552 0.0535  0.0584  602 A1A06 A C38 
3484 C  C39 . A1A06 C .   ? 1.0750 1.2548 1.2560 -0.0650 0.0447  0.0627  602 A1A06 A C39 
3485 C  C40 . A1A06 C .   ? 1.2756 1.4875 1.4665 -0.0689 0.0371  0.0607  602 A1A06 A C40 
3486 C  C41 . A1A06 C .   ? 1.1834 1.3975 1.3667 -0.0634 0.0359  0.0546  602 A1A06 A C41 
3487 F  F01 . A1A06 C .   ? 1.8533 2.2688 2.0896 -0.0288 -0.0188 0.0426  602 A1A06 A F01 
3488 F  F03 . A1A06 C .   ? 1.7590 2.1269 1.9774 -0.0554 -0.0204 0.0426  602 A1A06 A F03 
3489 F  F04 . A1A06 C .   ? 1.6459 2.0545 1.8897 -0.0478 -0.0032 0.0488  602 A1A06 A F04 
3490 N  N07 . A1A06 C .   ? 1.6484 1.9606 1.8424 -0.0370 0.0058  0.0403  602 A1A06 A N07 
3491 N  N11 . A1A06 C .   ? 1.3646 1.5994 1.5279 -0.0515 0.0194  0.0430  602 A1A06 A N11 
3492 N  N25 . A1A06 C .   ? 1.2483 1.3641 1.3324 -0.0700 0.0143  0.0329  602 A1A06 A N25 
3493 N  N33 . A1A06 C .   ? 0.9644 1.0234 1.0814 -0.0539 0.0584  0.0596  602 A1A06 A N33 
3494 O  O06 . A1A06 C .   ? 1.8069 2.1473 2.0014 -0.0128 -0.0038 0.0363  602 A1A06 A O06 
3495 O  O10 . A1A06 C .   ? 1.4158 1.6813 1.5920 -0.0717 0.0004  0.0429  602 A1A06 A O10 
3496 O  O24 . A1A06 C .   ? 1.3327 1.4005 1.3509 -0.0507 0.0124  0.0224  602 A1A06 A O24 
3497 S  S14 . A1A06 C .   ? 1.5062 1.6719 1.5863 -0.0474 -0.0005 0.0303  602 A1A06 A S14 
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