data_9COU
# 
_entry.id   9COU 
# 
_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   9COU         pdb_00009cou 10.2210/pdb9cou/pdb 
WWPDB D_1000285843 ?            ?                   
# 
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                        9COU 
_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               'Sevrioiukova, I.F.' 
_audit_author.pdbx_ordinal       1 
_audit_author.identifier_ORCID   0000-0002-4498-6057 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Chem.Biol.Drug Des.' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           1747-0285 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            105 
_citation.language                  ? 
_citation.page_first                e70043 
_citation.page_last                 e70043 
_citation.title                     
'Evaluation of Larger Side-Group Functionalities and the Side/End-Group Interplay in Ritonavir-Like Inhibitors of CYP3A4.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1111/cbdd.70043 
_citation.pdbx_database_id_PubMed   39792691 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Samuels, E.R.'     1 ?                   
primary 'Sevrioukova, I.F.' 2 0000-0002-4498-6057 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Cytochrome P450 3A4'                                                                                          
55757.812 1 1.14.14.1,1.14.14.56,1.14.14.73,1.14.14.55 'residues 3-22 deleted, C-terminal 4-histidine tag' ? ? 
2 non-polymer nat 'PROTOPORPHYRIN IX CONTAINING FE'                                                                              
616.487   1 ?                                          ?                                                   ? ? 
3 non-polymer syn '(2R)-2-{[(2S)-2-(benzenesulfonamido)-3-phenylpropyl]sulfanyl}-3-phenyl-N-[3-(pyridin-3-yl)propyl]propanamide' 
573.769   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)-2-{[(2S)-2-(benzenesulfonamido)-3-phenylpropyl]sulfanyl}-3-phenyl-N-[3-(pyridin-3-yl)propyl]propanamide' A1A4U 
# 
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 
A1A4U non-polymer         . 
'(2R)-2-{[(2S)-2-(benzenesulfonamido)-3-phenylpropyl]sulfanyl}-3-phenyl-N-[3-(pyridin-3-yl)propyl]propanamide' ?    
'C32 H35 N3 O3 S2' 573.769 
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 258 278 278 SER SER A . n 
A 1 259 GLN 259 279 279 GLN GLN A . n 
A 1 260 ASN 260 280 280 ASN ASN A . n 
A 1 261 SER 261 281 ?   ?   ?   A . n 
A 1 262 LYS 262 282 ?   ?   ?   A . n 
A 1 263 GLU 263 283 ?   ?   ?   A . n 
A 1 264 THR 264 284 ?   ?   ?   A . n 
A 1 265 GLU 265 285 ?   ?   ?   A . n 
A 1 266 SER 266 286 ?   ?   ?   A . n 
A 1 267 HIS 267 287 ?   ?   ?   A . n 
A 1 268 LYS 268 288 288 LYS LYS A . n 
A 1 269 ALA 269 289 289 ALA ALA A . n 
A 1 270 LEU 270 290 290 LEU LEU A . n 
A 1 271 SER 271 291 291 SER SER A . n 
A 1 272 ASP 272 292 292 ASP ASP A . n 
A 1 273 LEU 273 293 293 LEU LEU A . n 
A 1 274 GLU 274 294 294 GLU GLU A . n 
A 1 275 LEU 275 295 295 LEU LEU A . n 
A 1 276 VAL 276 296 296 VAL VAL A . n 
A 1 277 ALA 277 297 297 ALA ALA A . n 
A 1 278 GLN 278 298 298 GLN GLN A . n 
A 1 279 SER 279 299 299 SER SER A . n 
A 1 280 ILE 280 300 300 ILE ILE A . n 
A 1 281 ILE 281 301 301 ILE ILE A . n 
A 1 282 PHE 282 302 302 PHE PHE A . n 
A 1 283 ILE 283 303 303 ILE ILE A . n 
A 1 284 PHE 284 304 304 PHE PHE A . n 
A 1 285 ALA 285 305 305 ALA ALA A . n 
A 1 286 GLY 286 306 306 GLY GLY A . n 
A 1 287 TYR 287 307 307 TYR TYR A . n 
A 1 288 GLU 288 308 308 GLU GLU A . n 
A 1 289 THR 289 309 309 THR THR A . n 
A 1 290 THR 290 310 310 THR THR A . n 
A 1 291 SER 291 311 311 SER SER A . n 
A 1 292 SER 292 312 312 SER SER A . n 
A 1 293 VAL 293 313 313 VAL VAL A . n 
A 1 294 LEU 294 314 314 LEU LEU A . n 
A 1 295 SER 295 315 315 SER SER A . n 
A 1 296 PHE 296 316 316 PHE PHE A . n 
A 1 297 ILE 297 317 317 ILE ILE A . n 
A 1 298 MET 298 318 318 MET MET A . n 
A 1 299 TYR 299 319 319 TYR TYR A . n 
A 1 300 GLU 300 320 320 GLU GLU A . n 
A 1 301 LEU 301 321 321 LEU LEU A . n 
A 1 302 ALA 302 322 322 ALA ALA A . n 
A 1 303 THR 303 323 323 THR THR A . n 
A 1 304 HIS 304 324 324 HIS HIS A . n 
A 1 305 PRO 305 325 325 PRO PRO A . n 
A 1 306 ASP 306 326 326 ASP ASP A . n 
A 1 307 VAL 307 327 327 VAL VAL A . n 
A 1 308 GLN 308 328 328 GLN GLN A . n 
A 1 309 GLN 309 329 329 GLN GLN A . n 
A 1 310 LYS 310 330 330 LYS LYS A . n 
A 1 311 LEU 311 331 331 LEU LEU A . n 
A 1 312 GLN 312 332 332 GLN GLN A . n 
A 1 313 GLU 313 333 333 GLU GLU A . n 
A 1 314 GLU 314 334 334 GLU GLU A . n 
A 1 315 ILE 315 335 335 ILE ILE A . n 
A 1 316 ASP 316 336 336 ASP ASP A . n 
A 1 317 ALA 317 337 337 ALA ALA A . n 
A 1 318 VAL 318 338 338 VAL VAL A . n 
A 1 319 LEU 319 339 339 LEU LEU A . n 
A 1 320 PRO 320 340 340 PRO PRO A . n 
A 1 321 ASN 321 341 341 ASN ASN A . n 
A 1 322 LYS 322 342 342 LYS LYS A . n 
A 1 323 ALA 323 343 343 ALA ALA A . n 
A 1 324 PRO 324 344 344 PRO PRO A . n 
A 1 325 PRO 325 345 345 PRO PRO A . n 
A 1 326 THR 326 346 346 THR THR A . n 
A 1 327 TYR 327 347 347 TYR TYR A . n 
A 1 328 ASP 328 348 348 ASP ASP A . n 
A 1 329 THR 329 349 349 THR THR A . n 
A 1 330 VAL 330 350 350 VAL VAL A . n 
A 1 331 LEU 331 351 351 LEU LEU A . n 
A 1 332 GLN 332 352 352 GLN GLN A . n 
A 1 333 MET 333 353 353 MET MET A . n 
A 1 334 GLU 334 354 354 GLU GLU A . n 
A 1 335 TYR 335 355 355 TYR TYR A . n 
A 1 336 LEU 336 356 356 LEU LEU A . n 
A 1 337 ASP 337 357 357 ASP ASP A . n 
A 1 338 MET 338 358 358 MET MET A . n 
A 1 339 VAL 339 359 359 VAL VAL A . n 
A 1 340 VAL 340 360 360 VAL VAL A . n 
A 1 341 ASN 341 361 361 ASN ASN A . n 
A 1 342 GLU 342 362 362 GLU GLU A . n 
A 1 343 THR 343 363 363 THR THR A . n 
A 1 344 LEU 344 364 364 LEU LEU A . n 
A 1 345 ARG 345 365 365 ARG ARG A . n 
A 1 346 LEU 346 366 366 LEU LEU A . n 
A 1 347 PHE 347 367 367 PHE PHE A . n 
A 1 348 PRO 348 368 368 PRO PRO A . n 
A 1 349 ILE 349 369 369 ILE ILE A . n 
A 1 350 ALA 350 370 370 ALA ALA A . n 
A 1 351 MET 351 371 371 MET MET A . n 
A 1 352 ARG 352 372 372 ARG ARG A . n 
A 1 353 LEU 353 373 373 LEU LEU A . n 
A 1 354 GLU 354 374 374 GLU GLU A . n 
A 1 355 ARG 355 375 375 ARG ARG A . n 
A 1 356 VAL 356 376 376 VAL VAL A . n 
A 1 357 CYS 357 377 377 CYS CYS A . n 
A 1 358 LYS 358 378 378 LYS LYS A . n 
A 1 359 LYS 359 379 379 LYS LYS A . n 
A 1 360 ASP 360 380 380 ASP ASP A . n 
A 1 361 VAL 361 381 381 VAL VAL A . n 
A 1 362 GLU 362 382 382 GLU GLU A . n 
A 1 363 ILE 363 383 383 ILE ILE A . n 
A 1 364 ASN 364 384 384 ASN ASN A . n 
A 1 365 GLY 365 385 385 GLY GLY A . n 
A 1 366 MET 366 386 386 MET MET A . n 
A 1 367 PHE 367 387 387 PHE PHE A . n 
A 1 368 ILE 368 388 388 ILE ILE A . n 
A 1 369 PRO 369 389 389 PRO PRO A . n 
A 1 370 LYS 370 390 390 LYS LYS A . n 
A 1 371 GLY 371 391 391 GLY GLY A . n 
A 1 372 VAL 372 392 392 VAL VAL A . n 
A 1 373 VAL 373 393 393 VAL VAL A . n 
A 1 374 VAL 374 394 394 VAL VAL A . n 
A 1 375 MET 375 395 395 MET MET A . n 
A 1 376 ILE 376 396 396 ILE ILE A . n 
A 1 377 PRO 377 397 397 PRO PRO A . n 
A 1 378 SER 378 398 398 SER SER A . n 
A 1 379 TYR 379 399 399 TYR TYR A . n 
A 1 380 ALA 380 400 400 ALA ALA A . n 
A 1 381 LEU 381 401 401 LEU LEU A . n 
A 1 382 HIS 382 402 402 HIS HIS A . n 
A 1 383 ARG 383 403 403 ARG ARG A . n 
A 1 384 ASP 384 404 404 ASP ASP A . n 
A 1 385 PRO 385 405 405 PRO PRO A . n 
A 1 386 LYS 386 406 406 LYS LYS A . n 
A 1 387 TYR 387 407 407 TYR TYR A . n 
A 1 388 TRP 388 408 408 TRP TRP A . n 
A 1 389 THR 389 409 409 THR THR A . n 
A 1 390 GLU 390 410 410 GLU GLU A . n 
A 1 391 PRO 391 411 411 PRO PRO A . n 
A 1 392 GLU 392 412 412 GLU GLU A . n 
A 1 393 LYS 393 413 413 LYS LYS A . n 
A 1 394 PHE 394 414 414 PHE PHE A . n 
A 1 395 LEU 395 415 415 LEU LEU A . n 
A 1 396 PRO 396 416 416 PRO PRO A . n 
A 1 397 GLU 397 417 417 GLU GLU A . n 
A 1 398 ARG 398 418 418 ARG ARG A . n 
A 1 399 PHE 399 419 419 PHE PHE A . n 
A 1 400 SER 400 420 420 SER SER A . n 
A 1 401 LYS 401 421 421 LYS LYS A . n 
A 1 402 LYS 402 422 422 LYS LYS A . n 
A 1 403 ASN 403 423 423 ASN ASN A . n 
A 1 404 LYS 404 424 424 LYS LYS A . n 
A 1 405 ASP 405 425 425 ASP ASP A . n 
A 1 406 ASN 406 426 426 ASN ASN A . n 
A 1 407 ILE 407 427 427 ILE ILE A . n 
A 1 408 ASP 408 428 428 ASP ASP A . n 
A 1 409 PRO 409 429 429 PRO PRO A . n 
A 1 410 TYR 410 430 430 TYR TYR A . n 
A 1 411 ILE 411 431 431 ILE ILE A . n 
A 1 412 TYR 412 432 432 TYR TYR A . n 
A 1 413 THR 413 433 433 THR THR A . n 
A 1 414 PRO 414 434 434 PRO PRO A . n 
A 1 415 PHE 415 435 435 PHE PHE A . n 
A 1 416 GLY 416 436 436 GLY GLY A . n 
A 1 417 SER 417 437 437 SER SER A . n 
A 1 418 GLY 418 438 438 GLY GLY A . n 
A 1 419 PRO 419 439 439 PRO PRO A . n 
A 1 420 ARG 420 440 440 ARG ARG A . n 
A 1 421 ASN 421 441 441 ASN ASN A . n 
A 1 422 CYS 422 442 442 CYS CYS A . n 
A 1 423 ILE 423 443 443 ILE ILE A . n 
A 1 424 GLY 424 444 444 GLY GLY A . n 
A 1 425 MET 425 445 445 MET MET A . n 
A 1 426 ARG 426 446 446 ARG ARG A . n 
A 1 427 PHE 427 447 447 PHE PHE A . n 
A 1 428 ALA 428 448 448 ALA ALA A . n 
A 1 429 LEU 429 449 449 LEU LEU A . n 
A 1 430 MET 430 450 450 MET MET A . n 
A 1 431 ASN 431 451 451 ASN ASN A . n 
A 1 432 MET 432 452 452 MET MET A . n 
A 1 433 LYS 433 453 453 LYS LYS A . n 
A 1 434 LEU 434 454 454 LEU LEU A . n 
A 1 435 ALA 435 455 455 ALA ALA A . n 
A 1 436 LEU 436 456 456 LEU LEU A . n 
A 1 437 ILE 437 457 457 ILE ILE A . n 
A 1 438 ARG 438 458 458 ARG ARG A . n 
A 1 439 VAL 439 459 459 VAL VAL A . n 
A 1 440 LEU 440 460 460 LEU LEU A . n 
A 1 441 GLN 441 461 461 GLN GLN A . n 
A 1 442 ASN 442 462 462 ASN ASN A . n 
A 1 443 PHE 443 463 463 PHE PHE A . n 
A 1 444 SER 444 464 464 SER SER A . n 
A 1 445 PHE 445 465 465 PHE PHE A . n 
A 1 446 LYS 446 466 466 LYS LYS A . n 
A 1 447 PRO 447 467 467 PRO PRO A . n 
A 1 448 CYS 448 468 468 CYS CYS A . n 
A 1 449 LYS 449 469 469 LYS LYS A . n 
A 1 450 GLU 450 470 470 GLU GLU A . n 
A 1 451 THR 451 471 471 THR THR A . n 
A 1 452 GLN 452 472 472 GLN GLN A . n 
A 1 453 ILE 453 473 473 ILE ILE A . n 
A 1 454 PRO 454 474 474 PRO PRO A . n 
A 1 455 LEU 455 475 475 LEU LEU A . n 
A 1 456 LYS 456 476 476 LYS LYS A . n 
A 1 457 LEU 457 477 477 LEU LEU A . n 
A 1 458 SER 458 478 478 SER SER A . n 
A 1 459 LEU 459 479 479 LEU LEU A . n 
A 1 460 GLY 460 480 480 GLY GLY A . n 
A 1 461 GLY 461 481 481 GLY GLY A . n 
A 1 462 LEU 462 482 482 LEU LEU A . n 
A 1 463 LEU 463 483 483 LEU LEU A . n 
A 1 464 GLN 464 484 484 GLN GLN A . n 
A 1 465 PRO 465 485 485 PRO PRO A . n 
A 1 466 GLU 466 486 486 GLU GLU A . n 
A 1 467 LYS 467 487 487 LYS LYS A . n 
A 1 468 PRO 468 488 488 PRO PRO A . n 
A 1 469 VAL 469 489 489 VAL VAL A . n 
A 1 470 VAL 470 490 490 VAL VAL A . n 
A 1 471 LEU 471 491 491 LEU LEU A . n 
A 1 472 LYS 472 492 492 LYS LYS A . n 
A 1 473 VAL 473 493 493 VAL VAL A . n 
A 1 474 GLU 474 494 494 GLU GLU A . n 
A 1 475 SER 475 495 495 SER SER A . n 
A 1 476 ARG 476 496 496 ARG ARG A . n 
A 1 477 ASP 477 497 ?   ?   ?   A . n 
A 1 478 GLY 478 498 ?   ?   ?   A . n 
A 1 479 THR 479 499 ?   ?   ?   A . n 
A 1 480 VAL 480 500 ?   ?   ?   A . n 
A 1 481 SER 481 501 ?   ?   ?   A . n 
A 1 482 GLY 482 502 ?   ?   ?   A . n 
A 1 483 ALA 483 503 ?   ?   ?   A . n 
A 1 484 HIS 484 504 ?   ?   ?   A . n 
A 1 485 HIS 485 505 ?   ?   ?   A . n 
A 1 486 HIS 486 506 ?   ?   ?   A . n 
A 1 487 HIS 487 507 ?   ?   ?   A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1A4U 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1A4U 
_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 A1A4U 1 602 700 A1A4U 156 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                     9COU 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     76.760 
_cell.length_a_esd                 ? 
_cell.length_b                     100.760 
_cell.length_b_esd                 ? 
_cell.length_c                     126.490 
_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                         9COU 
_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                   9COU 
_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             2.19 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          43.92 
_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              6.0 
_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' 
_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         2017-08-18 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.0 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'ALS BEAMLINE 8.2.1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.0 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   8.2.1 
_diffrn_source.pdbx_synchrotron_site       ALS 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9COU 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.75 
_reflns.d_resolution_low                               79.00 
_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                                     12960 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           98.6 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                3.0 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          5.5 
_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                                0.055 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.995 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.083 
_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                             1911 
_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                               2.272 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.370 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  3.469 
_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                                 9COU 
_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                            2.81 
_refine.ls_d_res_low                             78.81 
_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                     10715 
_refine.ls_number_reflns_R_free                  547 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    86.81 
_refine.ls_percent_reflns_R_free                 5.10 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2486 
_refine.ls_R_factor_R_free                       0.2760 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2472 
_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                 38.76 
_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                            0.50 
_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                       2.81 
_refine_hist.d_res_low                        78.81 
_refine_hist.number_atoms_solvent             0 
_refine_hist.number_atoms_total               3513 
_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        3430 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         83 
_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' ? 0.003  ? 3717 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.586  ? 5046 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 14.437 ? 1411 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.039  ? 553  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.005  ? 634  ? 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' 2.81 3.09  . . 105 2023 70.00 . . . . 0.3867 . . . . . . . . . . . 0.4003 
'X-RAY DIFFRACTION' 3.09 3.54  . . 145 2751 96.00 . . . . 0.3377 . . . . . . . . . . . 0.3897 
'X-RAY DIFFRACTION' 3.54 4.45  . . 144 2723 93.00 . . . . 0.2732 . . . . . . . . . . . 0.3060 
'X-RAY DIFFRACTION' 4.45 78.81 . . 153 2671 88.00 . . . . 0.1931 . . . . . . . . . . . 0.2181 
# 
_struct.entry_id                     9COU 
_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        9COU 
_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              9COU 
_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 9COU ?   A ?   ? UNP P08684 LEU 3  deletion         ?   1  
1 9COU ?   A ?   ? UNP P08684 ILE 4  deletion         ?   2  
1 9COU ?   A ?   ? UNP P08684 PRO 5  deletion         ?   3  
1 9COU ?   A ?   ? UNP P08684 ASP 6  deletion         ?   4  
1 9COU ?   A ?   ? UNP P08684 LEU 7  deletion         ?   5  
1 9COU ?   A ?   ? UNP P08684 ALA 8  deletion         ?   6  
1 9COU ?   A ?   ? UNP P08684 MET 9  deletion         ?   7  
1 9COU ?   A ?   ? UNP P08684 GLU 10 deletion         ?   8  
1 9COU ?   A ?   ? UNP P08684 THR 11 deletion         ?   9  
1 9COU ?   A ?   ? UNP P08684 TRP 12 deletion         ?   10 
1 9COU ?   A ?   ? UNP P08684 LEU 13 deletion         ?   11 
1 9COU ?   A ?   ? UNP P08684 LEU 14 deletion         ?   12 
1 9COU ?   A ?   ? UNP P08684 LEU 15 deletion         ?   13 
1 9COU ?   A ?   ? UNP P08684 ALA 16 deletion         ?   14 
1 9COU ?   A ?   ? UNP P08684 VAL 17 deletion         ?   15 
1 9COU ?   A ?   ? UNP P08684 SER 18 deletion         ?   16 
1 9COU ?   A ?   ? UNP P08684 LEU 19 deletion         ?   17 
1 9COU ?   A ?   ? UNP P08684 VAL 20 deletion         ?   18 
1 9COU ?   A ?   ? UNP P08684 LEU 21 deletion         ?   19 
1 9COU ?   A ?   ? UNP P08684 LEU 22 deletion         ?   20 
1 9COU HIS A 484 ? UNP P08684 ?   ?  'expression tag' 504 21 
1 9COU HIS A 485 ? UNP P08684 ?   ?  'expression tag' 505 22 
1 9COU HIS A 486 ? UNP P08684 ?   ?  'expression tag' 506 23 
1 9COU HIS A 487 ? UNP P08684 ?   ?  'expression tag' 507 24 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,B,C 
1 2 A,B,C 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
loop_
_pdbx_struct_oper_list.id 
_pdbx_struct_oper_list.type 
_pdbx_struct_oper_list.name 
_pdbx_struct_oper_list.symmetry_operation 
_pdbx_struct_oper_list.matrix[1][1] 
_pdbx_struct_oper_list.matrix[1][2] 
_pdbx_struct_oper_list.matrix[1][3] 
_pdbx_struct_oper_list.vector[1] 
_pdbx_struct_oper_list.matrix[2][1] 
_pdbx_struct_oper_list.matrix[2][2] 
_pdbx_struct_oper_list.matrix[2][3] 
_pdbx_struct_oper_list.vector[2] 
_pdbx_struct_oper_list.matrix[3][1] 
_pdbx_struct_oper_list.matrix[3][2] 
_pdbx_struct_oper_list.matrix[3][3] 
_pdbx_struct_oper_list.vector[3] 
1 'identity operation'         1_555 x,y,z     1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000  
0.0000000000 0.0000000000    0.0000000000 0.0000000000 1.0000000000  0.0000000000 
2 'crystal symmetry operation' 4_545 x,-y-1,-z 1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 -1.0000000000 
0.0000000000 -100.7600000000 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 ? ALA A 130 ? MET A 145 ALA A 150 1 ? 6  
HELX_P HELX_P10 AB1 GLN A 131 ? GLY A 147 ? GLN A 151 GLY A 167 1 ? 17 
HELX_P HELX_P11 AB2 LEU A 152 ? SER A 168 ? LEU A 172 SER A 188 1 ? 17 
HELX_P HELX_P12 AB3 PHE A 199 ? PHE A 206 ? PHE A 219 PHE A 226 1 ? 8  
HELX_P HELX_P13 AB4 LEU A 209 ? VAL A 215 ? LEU A 229 VAL A 235 1 ? 7  
HELX_P HELX_P14 AB5 PRO A 222 ? LYS A 231 ? PRO A 242 LYS A 251 1 ? 10 
HELX_P HELX_P15 AB6 LEU A 252 ? ASP A 257 ? LEU A 272 ASP A 277 1 ? 6  
HELX_P HELX_P16 AB7 ASP A 272 ? HIS A 304 ? ASP A 292 HIS A 324 1 ? 33 
HELX_P HELX_P17 AB8 HIS A 304 ? LEU A 319 ? HIS A 324 LEU A 339 1 ? 16 
HELX_P HELX_P18 AB9 THR A 326 ? LEU A 331 ? THR A 346 LEU A 351 1 ? 6  
HELX_P HELX_P19 AC1 MET A 333 ? PHE A 347 ? MET A 353 PHE A 367 1 ? 15 
HELX_P HELX_P20 AC2 SER A 378 ? HIS A 382 ? SER A 398 HIS A 402 1 ? 5  
HELX_P HELX_P21 AC3 LEU A 395 ? SER A 400 ? LEU A 415 SER A 420 5 ? 6  
HELX_P HELX_P22 AC4 SER A 417 ? ASN A 421 ? SER A 437 ASN A 441 5 ? 5  
HELX_P HELX_P23 AC5 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 ? ? ? ? ? ? ? 2.385 ? ? 
metalc2 metalc ? ? B HEM .   FE ? ? ? 1_555 C A1A4U . N09 ? ? A HEM 601 A A1A4U 602 1_555 ? ? ? ? ? ? ? 2.200 ? ? 
# 
_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 91.0  ? 
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 80.0  ? 
3  NA ? B HEM .   ? A HEM 601 ? 1_555 FE ? B HEM . ? A HEM 601 ? 1_555 NB  ? B HEM   . ? A HEM   601 ? 1_555 90.0  ? 
4  SG ? A CYS 422 ? A CYS 442 ? 1_555 FE ? B HEM . ? A HEM 601 ? 1_555 NC  ? B HEM   . ? A HEM   601 ? 1_555 88.9  ? 
5  NA ? B HEM .   ? A HEM 601 ? 1_555 FE ? B HEM . ? A HEM 601 ? 1_555 NC  ? B HEM   . ? A HEM   601 ? 1_555 179.9 ? 
6  NB ? B HEM .   ? A HEM 601 ? 1_555 FE ? B HEM . ? A HEM 601 ? 1_555 NC  ? B HEM   . ? A HEM   601 ? 1_555 90.1  ? 
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 98.1  ? 
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 89.6  ? 
9  NB ? B HEM .   ? A HEM 601 ? 1_555 FE ? B HEM . ? A HEM 601 ? 1_555 ND  ? B HEM   . ? A HEM   601 ? 1_555 178.0 ? 
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 90.3  ? 
11 SG ? A CYS 422 ? A CYS 442 ? 1_555 FE ? B HEM . ? A HEM 601 ? 1_555 N09 ? C A1A4U . ? A A1A4U 602 ? 1_555 170.1 ? 
12 NA ? B HEM .   ? A HEM 601 ? 1_555 FE ? B HEM . ? A HEM 601 ? 1_555 N09 ? C A1A4U . ? A A1A4U 602 ? 1_555 83.1  ? 
13 NB ? B HEM .   ? A HEM 601 ? 1_555 FE ? B HEM . ? A HEM 601 ? 1_555 N09 ? C A1A4U . ? A A1A4U 602 ? 1_555 92.0  ? 
14 NC ? B HEM .   ? A HEM 601 ? 1_555 FE ? B HEM . ? A HEM 601 ? 1_555 N09 ? C A1A4U . ? A A1A4U 602 ? 1_555 97.0  ? 
15 ND ? B HEM .   ? A HEM 601 ? 1_555 FE ? B HEM . ? A HEM 601 ? 1_555 N09 ? C A1A4U . ? A A1A4U 602 ? 1_555 89.9  ? 
# 
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 0.47  
2 ILE 453 A . ? ILE 473 A PRO 454 A ? PRO 474 A 1 -0.43 
# 
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 ? PRO A 377 ? VAL A 393 PRO A 397 
AA1 4 ARG A 352 ? VAL A 356 ? ARG A 372 VAL A 376 
AA2 1 PRO A 149 ? THR A 151 ? PRO A 169 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 VAL A 374 ? O VAL A 394 N ARG A 355 ? N ARG A 375 
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                   9COU 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 PHE A 46  ? ? 66.78   -54.11  
2  1 PHE A 102 ? ? -114.49 67.99   
3  1 ASP A 123 ? ? 58.39   -132.08 
4  1 ALA A 150 ? ? -69.15  0.13    
5  1 PHE A 226 ? ? -119.45 63.32   
6  1 ASN A 237 ? ? 58.24   11.98   
7  1 LEU A 274 ? ? -67.80  1.28    
8  1 ALA A 289 ? ? -115.57 -163.01 
9  1 MET A 371 ? ? 68.42   -53.33  
10 1 GLU A 410 ? ? 50.09   72.45   
11 1 ASN A 426 ? ? -91.58  32.53   
12 1 PRO A 429 ? ? -67.79  5.82    
13 1 LEU A 479 ? ? -69.63  2.61    
# 
_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         -19.5290 
_pdbx_refine_tls.origin_y         -26.8931 
_pdbx_refine_tls.origin_z         -13.4716 
_pdbx_refine_tls.T[1][1]          0.5784 
_pdbx_refine_tls.T[1][1]_esd      ? 
_pdbx_refine_tls.T[1][2]          -0.1035 
_pdbx_refine_tls.T[1][2]_esd      ? 
_pdbx_refine_tls.T[1][3]          0.1228 
_pdbx_refine_tls.T[1][3]_esd      ? 
_pdbx_refine_tls.T[2][2]          0.6942 
_pdbx_refine_tls.T[2][2]_esd      ? 
_pdbx_refine_tls.T[2][3]          0.0730 
_pdbx_refine_tls.T[2][3]_esd      ? 
_pdbx_refine_tls.T[3][3]          0.6852 
_pdbx_refine_tls.T[3][3]_esd      ? 
_pdbx_refine_tls.L[1][1]          2.9946 
_pdbx_refine_tls.L[1][1]_esd      ? 
_pdbx_refine_tls.L[1][2]          -1.6992 
_pdbx_refine_tls.L[1][2]_esd      ? 
_pdbx_refine_tls.L[1][3]          0.5438 
_pdbx_refine_tls.L[1][3]_esd      ? 
_pdbx_refine_tls.L[2][2]          5.0938 
_pdbx_refine_tls.L[2][2]_esd      ? 
_pdbx_refine_tls.L[2][3]          -0.3948 
_pdbx_refine_tls.L[2][3]_esd      ? 
_pdbx_refine_tls.L[3][3]          3.3780 
_pdbx_refine_tls.L[3][3]_esd      ? 
_pdbx_refine_tls.S[1][1]          -0.0162 
_pdbx_refine_tls.S[1][1]_esd      ? 
_pdbx_refine_tls.S[1][2]          0.2583 
_pdbx_refine_tls.S[1][2]_esd      ? 
_pdbx_refine_tls.S[1][3]          0.2398 
_pdbx_refine_tls.S[1][3]_esd      ? 
_pdbx_refine_tls.S[2][1]          0.3774 
_pdbx_refine_tls.S[2][1]_esd      ? 
_pdbx_refine_tls.S[2][2]          0.0347 
_pdbx_refine_tls.S[2][2]_esd      ? 
_pdbx_refine_tls.S[2][3]          0.0383 
_pdbx_refine_tls.S[2][3]_esd      ? 
_pdbx_refine_tls.S[3][1]          -0.5725 
_pdbx_refine_tls.S[3][1]_esd      ? 
_pdbx_refine_tls.S[3][2]          0.3694 
_pdbx_refine_tls.S[3][2]_esd      ? 
_pdbx_refine_tls.S[3][3]          -0.0025 
_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 281 ? A SER 261 
43 1 Y 1 A LYS 282 ? A LYS 262 
44 1 Y 1 A GLU 283 ? A GLU 263 
45 1 Y 1 A THR 284 ? A THR 264 
46 1 Y 1 A GLU 285 ? A GLU 265 
47 1 Y 1 A SER 286 ? A SER 266 
48 1 Y 1 A HIS 287 ? A HIS 267 
49 1 Y 1 A ASP 497 ? A ASP 477 
50 1 Y 1 A GLY 498 ? A GLY 478 
51 1 Y 1 A THR 499 ? A THR 479 
52 1 Y 1 A VAL 500 ? A VAL 480 
53 1 Y 1 A SER 501 ? A SER 481 
54 1 Y 1 A GLY 502 ? A GLY 482 
55 1 Y 1 A ALA 503 ? A ALA 483 
56 1 Y 1 A HIS 504 ? A HIS 484 
57 1 Y 1 A HIS 505 ? A HIS 485 
58 1 Y 1 A HIS 506 ? A HIS 486 
59 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 
A1A4U C10  C  Y N 1   
A1A4U C11  C  Y N 2   
A1A4U C12  C  Y N 3   
A1A4U C13  C  N R 4   
A1A4U C14  C  N N 5   
A1A4U C15  C  Y N 6   
A1A4U C16  C  Y N 7   
A1A4U C17  C  Y N 8   
A1A4U C18  C  Y N 9   
A1A4U C19  C  Y N 10  
A1A4U C20  C  Y N 11  
A1A4U C22  C  N N 12  
A1A4U C23  C  N S 13  
A1A4U C24  C  N N 14  
A1A4U C02  C  N N 15  
A1A4U C04  C  N N 16  
A1A4U C05  C  N N 17  
A1A4U C06  C  N N 18  
A1A4U C07  C  Y N 19  
A1A4U C08  C  Y N 20  
A1A4U C25  C  Y N 21  
A1A4U C26  C  Y N 22  
A1A4U C27  C  Y N 23  
A1A4U C28  C  Y N 24  
A1A4U C29  C  Y N 25  
A1A4U C30  C  Y N 26  
A1A4U C35  C  Y N 27  
A1A4U C36  C  Y N 28  
A1A4U C37  C  Y N 29  
A1A4U C38  C  Y N 30  
A1A4U C39  C  Y N 31  
A1A4U C40  C  Y N 32  
A1A4U N03  N  N N 33  
A1A4U N09  N  Y N 34  
A1A4U N31  N  N N 35  
A1A4U O01  O  N N 36  
A1A4U O33  O  N N 37  
A1A4U O34  O  N N 38  
A1A4U S21  S  N N 39  
A1A4U S32  S  N N 40  
A1A4U H1   H  N N 41  
A1A4U H2   H  N N 42  
A1A4U H3   H  N N 43  
A1A4U H4   H  N N 44  
A1A4U H5   H  N N 45  
A1A4U H6   H  N N 46  
A1A4U H7   H  N N 47  
A1A4U H8   H  N N 48  
A1A4U H9   H  N N 49  
A1A4U H10  H  N N 50  
A1A4U H11  H  N N 51  
A1A4U H12  H  N N 52  
A1A4U H13  H  N N 53  
A1A4U H14  H  N N 54  
A1A4U H15  H  N N 55  
A1A4U H16  H  N N 56  
A1A4U H17  H  N N 57  
A1A4U H18  H  N N 58  
A1A4U H19  H  N N 59  
A1A4U H20  H  N N 60  
A1A4U H21  H  N N 61  
A1A4U H22  H  N N 62  
A1A4U H23  H  N N 63  
A1A4U H24  H  N N 64  
A1A4U H25  H  N N 65  
A1A4U H26  H  N N 66  
A1A4U H27  H  N N 67  
A1A4U H28  H  N N 68  
A1A4U H29  H  N N 69  
A1A4U H30  H  N N 70  
A1A4U H31  H  N N 71  
A1A4U H32  H  N N 72  
A1A4U H33  H  N N 73  
A1A4U H34  H  N N 74  
A1A4U H35  H  N N 75  
ALA   N    N  N N 76  
ALA   CA   C  N S 77  
ALA   C    C  N N 78  
ALA   O    O  N N 79  
ALA   CB   C  N N 80  
ALA   OXT  O  N N 81  
ALA   H    H  N N 82  
ALA   H2   H  N N 83  
ALA   HA   H  N N 84  
ALA   HB1  H  N N 85  
ALA   HB2  H  N N 86  
ALA   HB3  H  N N 87  
ALA   HXT  H  N N 88  
ARG   N    N  N N 89  
ARG   CA   C  N S 90  
ARG   C    C  N N 91  
ARG   O    O  N N 92  
ARG   CB   C  N N 93  
ARG   CG   C  N N 94  
ARG   CD   C  N N 95  
ARG   NE   N  N N 96  
ARG   CZ   C  N N 97  
ARG   NH1  N  N N 98  
ARG   NH2  N  N N 99  
ARG   OXT  O  N N 100 
ARG   H    H  N N 101 
ARG   H2   H  N N 102 
ARG   HA   H  N N 103 
ARG   HB2  H  N N 104 
ARG   HB3  H  N N 105 
ARG   HG2  H  N N 106 
ARG   HG3  H  N N 107 
ARG   HD2  H  N N 108 
ARG   HD3  H  N N 109 
ARG   HE   H  N N 110 
ARG   HH11 H  N N 111 
ARG   HH12 H  N N 112 
ARG   HH21 H  N N 113 
ARG   HH22 H  N N 114 
ARG   HXT  H  N N 115 
ASN   N    N  N N 116 
ASN   CA   C  N S 117 
ASN   C    C  N N 118 
ASN   O    O  N N 119 
ASN   CB   C  N N 120 
ASN   CG   C  N N 121 
ASN   OD1  O  N N 122 
ASN   ND2  N  N N 123 
ASN   OXT  O  N N 124 
ASN   H    H  N N 125 
ASN   H2   H  N N 126 
ASN   HA   H  N N 127 
ASN   HB2  H  N N 128 
ASN   HB3  H  N N 129 
ASN   HD21 H  N N 130 
ASN   HD22 H  N N 131 
ASN   HXT  H  N N 132 
ASP   N    N  N N 133 
ASP   CA   C  N S 134 
ASP   C    C  N N 135 
ASP   O    O  N N 136 
ASP   CB   C  N N 137 
ASP   CG   C  N N 138 
ASP   OD1  O  N N 139 
ASP   OD2  O  N N 140 
ASP   OXT  O  N N 141 
ASP   H    H  N N 142 
ASP   H2   H  N N 143 
ASP   HA   H  N N 144 
ASP   HB2  H  N N 145 
ASP   HB3  H  N N 146 
ASP   HD2  H  N N 147 
ASP   HXT  H  N N 148 
CYS   N    N  N N 149 
CYS   CA   C  N R 150 
CYS   C    C  N N 151 
CYS   O    O  N N 152 
CYS   CB   C  N N 153 
CYS   SG   S  N N 154 
CYS   OXT  O  N N 155 
CYS   H    H  N N 156 
CYS   H2   H  N N 157 
CYS   HA   H  N N 158 
CYS   HB2  H  N N 159 
CYS   HB3  H  N N 160 
CYS   HG   H  N N 161 
CYS   HXT  H  N N 162 
GLN   N    N  N N 163 
GLN   CA   C  N S 164 
GLN   C    C  N N 165 
GLN   O    O  N N 166 
GLN   CB   C  N N 167 
GLN   CG   C  N N 168 
GLN   CD   C  N N 169 
GLN   OE1  O  N N 170 
GLN   NE2  N  N N 171 
GLN   OXT  O  N N 172 
GLN   H    H  N N 173 
GLN   H2   H  N N 174 
GLN   HA   H  N N 175 
GLN   HB2  H  N N 176 
GLN   HB3  H  N N 177 
GLN   HG2  H  N N 178 
GLN   HG3  H  N N 179 
GLN   HE21 H  N N 180 
GLN   HE22 H  N N 181 
GLN   HXT  H  N N 182 
GLU   N    N  N N 183 
GLU   CA   C  N S 184 
GLU   C    C  N N 185 
GLU   O    O  N N 186 
GLU   CB   C  N N 187 
GLU   CG   C  N N 188 
GLU   CD   C  N N 189 
GLU   OE1  O  N N 190 
GLU   OE2  O  N N 191 
GLU   OXT  O  N N 192 
GLU   H    H  N N 193 
GLU   H2   H  N N 194 
GLU   HA   H  N N 195 
GLU   HB2  H  N N 196 
GLU   HB3  H  N N 197 
GLU   HG2  H  N N 198 
GLU   HG3  H  N N 199 
GLU   HE2  H  N N 200 
GLU   HXT  H  N N 201 
GLY   N    N  N N 202 
GLY   CA   C  N N 203 
GLY   C    C  N N 204 
GLY   O    O  N N 205 
GLY   OXT  O  N N 206 
GLY   H    H  N N 207 
GLY   H2   H  N N 208 
GLY   HA2  H  N N 209 
GLY   HA3  H  N N 210 
GLY   HXT  H  N N 211 
HEM   CHA  C  N N 212 
HEM   CHB  C  N N 213 
HEM   CHC  C  N N 214 
HEM   CHD  C  N N 215 
HEM   C1A  C  Y N 216 
HEM   C2A  C  Y N 217 
HEM   C3A  C  Y N 218 
HEM   C4A  C  Y N 219 
HEM   CMA  C  N N 220 
HEM   CAA  C  N N 221 
HEM   CBA  C  N N 222 
HEM   CGA  C  N N 223 
HEM   O1A  O  N N 224 
HEM   O2A  O  N N 225 
HEM   C1B  C  N N 226 
HEM   C2B  C  N N 227 
HEM   C3B  C  N N 228 
HEM   C4B  C  N N 229 
HEM   CMB  C  N N 230 
HEM   CAB  C  N N 231 
HEM   CBB  C  N N 232 
HEM   C1C  C  Y N 233 
HEM   C2C  C  Y N 234 
HEM   C3C  C  Y N 235 
HEM   C4C  C  Y N 236 
HEM   CMC  C  N N 237 
HEM   CAC  C  N N 238 
HEM   CBC  C  N N 239 
HEM   C1D  C  N N 240 
HEM   C2D  C  N N 241 
HEM   C3D  C  N N 242 
HEM   C4D  C  N N 243 
HEM   CMD  C  N N 244 
HEM   CAD  C  N N 245 
HEM   CBD  C  N N 246 
HEM   CGD  C  N N 247 
HEM   O1D  O  N N 248 
HEM   O2D  O  N N 249 
HEM   NA   N  Y N 250 
HEM   NB   N  N N 251 
HEM   NC   N  Y N 252 
HEM   ND   N  N N 253 
HEM   FE   FE N N 254 
HEM   HHB  H  N N 255 
HEM   HHC  H  N N 256 
HEM   HHD  H  N N 257 
HEM   HMA  H  N N 258 
HEM   HMAA H  N N 259 
HEM   HMAB H  N N 260 
HEM   HAA  H  N N 261 
HEM   HAAA H  N N 262 
HEM   HBA  H  N N 263 
HEM   HBAA H  N N 264 
HEM   HMB  H  N N 265 
HEM   HMBA H  N N 266 
HEM   HMBB H  N N 267 
HEM   HAB  H  N N 268 
HEM   HBB  H  N N 269 
HEM   HBBA H  N N 270 
HEM   HMC  H  N N 271 
HEM   HMCA H  N N 272 
HEM   HMCB H  N N 273 
HEM   HAC  H  N N 274 
HEM   HBC  H  N N 275 
HEM   HBCA H  N N 276 
HEM   HMD  H  N N 277 
HEM   HMDA H  N N 278 
HEM   HMDB H  N N 279 
HEM   HAD  H  N N 280 
HEM   HADA H  N N 281 
HEM   HBD  H  N N 282 
HEM   HBDA H  N N 283 
HEM   H2A  H  N N 284 
HEM   H2D  H  N N 285 
HEM   HHA  H  N N 286 
HIS   N    N  N N 287 
HIS   CA   C  N S 288 
HIS   C    C  N N 289 
HIS   O    O  N N 290 
HIS   CB   C  N N 291 
HIS   CG   C  Y N 292 
HIS   ND1  N  Y N 293 
HIS   CD2  C  Y N 294 
HIS   CE1  C  Y N 295 
HIS   NE2  N  Y N 296 
HIS   OXT  O  N N 297 
HIS   H    H  N N 298 
HIS   H2   H  N N 299 
HIS   HA   H  N N 300 
HIS   HB2  H  N N 301 
HIS   HB3  H  N N 302 
HIS   HD1  H  N N 303 
HIS   HD2  H  N N 304 
HIS   HE1  H  N N 305 
HIS   HE2  H  N N 306 
HIS   HXT  H  N N 307 
ILE   N    N  N N 308 
ILE   CA   C  N S 309 
ILE   C    C  N N 310 
ILE   O    O  N N 311 
ILE   CB   C  N S 312 
ILE   CG1  C  N N 313 
ILE   CG2  C  N N 314 
ILE   CD1  C  N N 315 
ILE   OXT  O  N N 316 
ILE   H    H  N N 317 
ILE   H2   H  N N 318 
ILE   HA   H  N N 319 
ILE   HB   H  N N 320 
ILE   HG12 H  N N 321 
ILE   HG13 H  N N 322 
ILE   HG21 H  N N 323 
ILE   HG22 H  N N 324 
ILE   HG23 H  N N 325 
ILE   HD11 H  N N 326 
ILE   HD12 H  N N 327 
ILE   HD13 H  N N 328 
ILE   HXT  H  N N 329 
LEU   N    N  N N 330 
LEU   CA   C  N S 331 
LEU   C    C  N N 332 
LEU   O    O  N N 333 
LEU   CB   C  N N 334 
LEU   CG   C  N N 335 
LEU   CD1  C  N N 336 
LEU   CD2  C  N N 337 
LEU   OXT  O  N N 338 
LEU   H    H  N N 339 
LEU   H2   H  N N 340 
LEU   HA   H  N N 341 
LEU   HB2  H  N N 342 
LEU   HB3  H  N N 343 
LEU   HG   H  N N 344 
LEU   HD11 H  N N 345 
LEU   HD12 H  N N 346 
LEU   HD13 H  N N 347 
LEU   HD21 H  N N 348 
LEU   HD22 H  N N 349 
LEU   HD23 H  N N 350 
LEU   HXT  H  N N 351 
LYS   N    N  N N 352 
LYS   CA   C  N S 353 
LYS   C    C  N N 354 
LYS   O    O  N N 355 
LYS   CB   C  N N 356 
LYS   CG   C  N N 357 
LYS   CD   C  N N 358 
LYS   CE   C  N N 359 
LYS   NZ   N  N N 360 
LYS   OXT  O  N N 361 
LYS   H    H  N N 362 
LYS   H2   H  N N 363 
LYS   HA   H  N N 364 
LYS   HB2  H  N N 365 
LYS   HB3  H  N N 366 
LYS   HG2  H  N N 367 
LYS   HG3  H  N N 368 
LYS   HD2  H  N N 369 
LYS   HD3  H  N N 370 
LYS   HE2  H  N N 371 
LYS   HE3  H  N N 372 
LYS   HZ1  H  N N 373 
LYS   HZ2  H  N N 374 
LYS   HZ3  H  N N 375 
LYS   HXT  H  N N 376 
MET   N    N  N N 377 
MET   CA   C  N S 378 
MET   C    C  N N 379 
MET   O    O  N N 380 
MET   CB   C  N N 381 
MET   CG   C  N N 382 
MET   SD   S  N N 383 
MET   CE   C  N N 384 
MET   OXT  O  N N 385 
MET   H    H  N N 386 
MET   H2   H  N N 387 
MET   HA   H  N N 388 
MET   HB2  H  N N 389 
MET   HB3  H  N N 390 
MET   HG2  H  N N 391 
MET   HG3  H  N N 392 
MET   HE1  H  N N 393 
MET   HE2  H  N N 394 
MET   HE3  H  N N 395 
MET   HXT  H  N N 396 
PHE   N    N  N N 397 
PHE   CA   C  N S 398 
PHE   C    C  N N 399 
PHE   O    O  N N 400 
PHE   CB   C  N N 401 
PHE   CG   C  Y N 402 
PHE   CD1  C  Y N 403 
PHE   CD2  C  Y N 404 
PHE   CE1  C  Y N 405 
PHE   CE2  C  Y N 406 
PHE   CZ   C  Y N 407 
PHE   OXT  O  N N 408 
PHE   H    H  N N 409 
PHE   H2   H  N N 410 
PHE   HA   H  N N 411 
PHE   HB2  H  N N 412 
PHE   HB3  H  N N 413 
PHE   HD1  H  N N 414 
PHE   HD2  H  N N 415 
PHE   HE1  H  N N 416 
PHE   HE2  H  N N 417 
PHE   HZ   H  N N 418 
PHE   HXT  H  N N 419 
PRO   N    N  N N 420 
PRO   CA   C  N S 421 
PRO   C    C  N N 422 
PRO   O    O  N N 423 
PRO   CB   C  N N 424 
PRO   CG   C  N N 425 
PRO   CD   C  N N 426 
PRO   OXT  O  N N 427 
PRO   H    H  N N 428 
PRO   HA   H  N N 429 
PRO   HB2  H  N N 430 
PRO   HB3  H  N N 431 
PRO   HG2  H  N N 432 
PRO   HG3  H  N N 433 
PRO   HD2  H  N N 434 
PRO   HD3  H  N N 435 
PRO   HXT  H  N N 436 
SER   N    N  N N 437 
SER   CA   C  N S 438 
SER   C    C  N N 439 
SER   O    O  N N 440 
SER   CB   C  N N 441 
SER   OG   O  N N 442 
SER   OXT  O  N N 443 
SER   H    H  N N 444 
SER   H2   H  N N 445 
SER   HA   H  N N 446 
SER   HB2  H  N N 447 
SER   HB3  H  N N 448 
SER   HG   H  N N 449 
SER   HXT  H  N N 450 
THR   N    N  N N 451 
THR   CA   C  N S 452 
THR   C    C  N N 453 
THR   O    O  N N 454 
THR   CB   C  N R 455 
THR   OG1  O  N N 456 
THR   CG2  C  N N 457 
THR   OXT  O  N N 458 
THR   H    H  N N 459 
THR   H2   H  N N 460 
THR   HA   H  N N 461 
THR   HB   H  N N 462 
THR   HG1  H  N N 463 
THR   HG21 H  N N 464 
THR   HG22 H  N N 465 
THR   HG23 H  N N 466 
THR   HXT  H  N N 467 
TRP   N    N  N N 468 
TRP   CA   C  N S 469 
TRP   C    C  N N 470 
TRP   O    O  N N 471 
TRP   CB   C  N N 472 
TRP   CG   C  Y N 473 
TRP   CD1  C  Y N 474 
TRP   CD2  C  Y N 475 
TRP   NE1  N  Y N 476 
TRP   CE2  C  Y N 477 
TRP   CE3  C  Y N 478 
TRP   CZ2  C  Y N 479 
TRP   CZ3  C  Y N 480 
TRP   CH2  C  Y N 481 
TRP   OXT  O  N N 482 
TRP   H    H  N N 483 
TRP   H2   H  N N 484 
TRP   HA   H  N N 485 
TRP   HB2  H  N N 486 
TRP   HB3  H  N N 487 
TRP   HD1  H  N N 488 
TRP   HE1  H  N N 489 
TRP   HE3  H  N N 490 
TRP   HZ2  H  N N 491 
TRP   HZ3  H  N N 492 
TRP   HH2  H  N N 493 
TRP   HXT  H  N N 494 
TYR   N    N  N N 495 
TYR   CA   C  N S 496 
TYR   C    C  N N 497 
TYR   O    O  N N 498 
TYR   CB   C  N N 499 
TYR   CG   C  Y N 500 
TYR   CD1  C  Y N 501 
TYR   CD2  C  Y N 502 
TYR   CE1  C  Y N 503 
TYR   CE2  C  Y N 504 
TYR   CZ   C  Y N 505 
TYR   OH   O  N N 506 
TYR   OXT  O  N N 507 
TYR   H    H  N N 508 
TYR   H2   H  N N 509 
TYR   HA   H  N N 510 
TYR   HB2  H  N N 511 
TYR   HB3  H  N N 512 
TYR   HD1  H  N N 513 
TYR   HD2  H  N N 514 
TYR   HE1  H  N N 515 
TYR   HE2  H  N N 516 
TYR   HH   H  N N 517 
TYR   HXT  H  N N 518 
VAL   N    N  N N 519 
VAL   CA   C  N S 520 
VAL   C    C  N N 521 
VAL   O    O  N N 522 
VAL   CB   C  N N 523 
VAL   CG1  C  N N 524 
VAL   CG2  C  N N 525 
VAL   OXT  O  N N 526 
VAL   H    H  N N 527 
VAL   H2   H  N N 528 
VAL   HA   H  N N 529 
VAL   HB   H  N N 530 
VAL   HG11 H  N N 531 
VAL   HG12 H  N N 532 
VAL   HG13 H  N N 533 
VAL   HG21 H  N N 534 
VAL   HG22 H  N N 535 
VAL   HG23 H  N N 536 
VAL   HXT  H  N N 537 
# 
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 
A1A4U C29 C28  doub Y N 1   
A1A4U C29 C30  sing Y N 2   
A1A4U C39 C38  doub Y N 3   
A1A4U C39 C40  sing Y N 4   
A1A4U C28 C27  sing Y N 5   
A1A4U C38 C37  sing Y N 6   
A1A4U C40 C35  doub Y N 7   
A1A4U O34 S32  doub N N 8   
A1A4U C10 C11  doub Y N 9   
A1A4U C10 N09  sing Y N 10  
A1A4U C11 C12  sing Y N 11  
A1A4U C30 C25  doub Y N 12  
A1A4U C37 C36  doub Y N 13  
A1A4U C35 C36  sing Y N 14  
A1A4U C35 S32  sing N N 15  
A1A4U C27 C26  doub Y N 16  
A1A4U S32 O33  doub N N 17  
A1A4U S32 N31  sing N N 18  
A1A4U N09 C08  doub Y N 19  
A1A4U C12 C07  doub Y N 20  
A1A4U C25 C26  sing Y N 21  
A1A4U C25 C24  sing N N 22  
A1A4U N31 C23  sing N N 23  
A1A4U C24 C23  sing N N 24  
A1A4U C08 C07  sing Y N 25  
A1A4U C07 C06  sing N N 26  
A1A4U C23 C22  sing N N 27  
A1A4U N03 C04  sing N N 28  
A1A4U N03 C02  sing N N 29  
A1A4U C04 C05  sing N N 30  
A1A4U C06 C05  sing N N 31  
A1A4U C22 S21  sing N N 32  
A1A4U S21 C13  sing N N 33  
A1A4U C13 C02  sing N N 34  
A1A4U C13 C14  sing N N 35  
A1A4U C02 O01  doub N N 36  
A1A4U C16 C17  doub Y N 37  
A1A4U C16 C15  sing Y N 38  
A1A4U C17 C18  sing Y N 39  
A1A4U C14 C15  sing N N 40  
A1A4U C15 C20  doub Y N 41  
A1A4U C18 C19  doub Y N 42  
A1A4U C20 C19  sing Y N 43  
A1A4U C10 H1   sing N N 44  
A1A4U C11 H2   sing N N 45  
A1A4U C12 H3   sing N N 46  
A1A4U C13 H4   sing N N 47  
A1A4U C14 H5   sing N N 48  
A1A4U C14 H6   sing N N 49  
A1A4U C16 H7   sing N N 50  
A1A4U C17 H8   sing N N 51  
A1A4U C18 H9   sing N N 52  
A1A4U C19 H10  sing N N 53  
A1A4U C20 H11  sing N N 54  
A1A4U C22 H12  sing N N 55  
A1A4U C22 H13  sing N N 56  
A1A4U C23 H14  sing N N 57  
A1A4U C24 H15  sing N N 58  
A1A4U C24 H16  sing N N 59  
A1A4U C04 H17  sing N N 60  
A1A4U C04 H18  sing N N 61  
A1A4U C05 H19  sing N N 62  
A1A4U C05 H20  sing N N 63  
A1A4U C06 H21  sing N N 64  
A1A4U C06 H22  sing N N 65  
A1A4U C08 H23  sing N N 66  
A1A4U C26 H24  sing N N 67  
A1A4U C27 H25  sing N N 68  
A1A4U C28 H26  sing N N 69  
A1A4U C29 H27  sing N N 70  
A1A4U C30 H28  sing N N 71  
A1A4U C36 H29  sing N N 72  
A1A4U C37 H30  sing N N 73  
A1A4U C38 H31  sing N N 74  
A1A4U C39 H32  sing N N 75  
A1A4U C40 H33  sing N N 76  
A1A4U N03 H34  sing N N 77  
A1A4U N31 H35  sing N N 78  
ALA   N   CA   sing N N 79  
ALA   N   H    sing N N 80  
ALA   N   H2   sing N N 81  
ALA   CA  C    sing N N 82  
ALA   CA  CB   sing N N 83  
ALA   CA  HA   sing N N 84  
ALA   C   O    doub N N 85  
ALA   C   OXT  sing N N 86  
ALA   CB  HB1  sing N N 87  
ALA   CB  HB2  sing N N 88  
ALA   CB  HB3  sing N N 89  
ALA   OXT HXT  sing N N 90  
ARG   N   CA   sing N N 91  
ARG   N   H    sing N N 92  
ARG   N   H2   sing N N 93  
ARG   CA  C    sing N N 94  
ARG   CA  CB   sing N N 95  
ARG   CA  HA   sing N N 96  
ARG   C   O    doub N N 97  
ARG   C   OXT  sing N N 98  
ARG   CB  CG   sing N N 99  
ARG   CB  HB2  sing N N 100 
ARG   CB  HB3  sing N N 101 
ARG   CG  CD   sing N N 102 
ARG   CG  HG2  sing N N 103 
ARG   CG  HG3  sing N N 104 
ARG   CD  NE   sing N N 105 
ARG   CD  HD2  sing N N 106 
ARG   CD  HD3  sing N N 107 
ARG   NE  CZ   sing N N 108 
ARG   NE  HE   sing N N 109 
ARG   CZ  NH1  sing N N 110 
ARG   CZ  NH2  doub N N 111 
ARG   NH1 HH11 sing N N 112 
ARG   NH1 HH12 sing N N 113 
ARG   NH2 HH21 sing N N 114 
ARG   NH2 HH22 sing N N 115 
ARG   OXT HXT  sing N N 116 
ASN   N   CA   sing N N 117 
ASN   N   H    sing N N 118 
ASN   N   H2   sing N N 119 
ASN   CA  C    sing N N 120 
ASN   CA  CB   sing N N 121 
ASN   CA  HA   sing N N 122 
ASN   C   O    doub N N 123 
ASN   C   OXT  sing N N 124 
ASN   CB  CG   sing N N 125 
ASN   CB  HB2  sing N N 126 
ASN   CB  HB3  sing N N 127 
ASN   CG  OD1  doub N N 128 
ASN   CG  ND2  sing N N 129 
ASN   ND2 HD21 sing N N 130 
ASN   ND2 HD22 sing N N 131 
ASN   OXT HXT  sing N N 132 
ASP   N   CA   sing N N 133 
ASP   N   H    sing N N 134 
ASP   N   H2   sing N N 135 
ASP   CA  C    sing N N 136 
ASP   CA  CB   sing N N 137 
ASP   CA  HA   sing N N 138 
ASP   C   O    doub N N 139 
ASP   C   OXT  sing N N 140 
ASP   CB  CG   sing N N 141 
ASP   CB  HB2  sing N N 142 
ASP   CB  HB3  sing N N 143 
ASP   CG  OD1  doub N N 144 
ASP   CG  OD2  sing N N 145 
ASP   OD2 HD2  sing N N 146 
ASP   OXT HXT  sing N N 147 
CYS   N   CA   sing N N 148 
CYS   N   H    sing N N 149 
CYS   N   H2   sing N N 150 
CYS   CA  C    sing N N 151 
CYS   CA  CB   sing N N 152 
CYS   CA  HA   sing N N 153 
CYS   C   O    doub N N 154 
CYS   C   OXT  sing N N 155 
CYS   CB  SG   sing N N 156 
CYS   CB  HB2  sing N N 157 
CYS   CB  HB3  sing N N 158 
CYS   SG  HG   sing N N 159 
CYS   OXT HXT  sing N N 160 
GLN   N   CA   sing N N 161 
GLN   N   H    sing N N 162 
GLN   N   H2   sing N N 163 
GLN   CA  C    sing N N 164 
GLN   CA  CB   sing N N 165 
GLN   CA  HA   sing N N 166 
GLN   C   O    doub N N 167 
GLN   C   OXT  sing N N 168 
GLN   CB  CG   sing N N 169 
GLN   CB  HB2  sing N N 170 
GLN   CB  HB3  sing N N 171 
GLN   CG  CD   sing N N 172 
GLN   CG  HG2  sing N N 173 
GLN   CG  HG3  sing N N 174 
GLN   CD  OE1  doub N N 175 
GLN   CD  NE2  sing N N 176 
GLN   NE2 HE21 sing N N 177 
GLN   NE2 HE22 sing N N 178 
GLN   OXT HXT  sing N N 179 
GLU   N   CA   sing N N 180 
GLU   N   H    sing N N 181 
GLU   N   H2   sing N N 182 
GLU   CA  C    sing N N 183 
GLU   CA  CB   sing N N 184 
GLU   CA  HA   sing N N 185 
GLU   C   O    doub N N 186 
GLU   C   OXT  sing N N 187 
GLU   CB  CG   sing N N 188 
GLU   CB  HB2  sing N N 189 
GLU   CB  HB3  sing N N 190 
GLU   CG  CD   sing N N 191 
GLU   CG  HG2  sing N N 192 
GLU   CG  HG3  sing N N 193 
GLU   CD  OE1  doub N N 194 
GLU   CD  OE2  sing N N 195 
GLU   OE2 HE2  sing N N 196 
GLU   OXT HXT  sing N N 197 
GLY   N   CA   sing N N 198 
GLY   N   H    sing N N 199 
GLY   N   H2   sing N N 200 
GLY   CA  C    sing N N 201 
GLY   CA  HA2  sing N N 202 
GLY   CA  HA3  sing N N 203 
GLY   C   O    doub N N 204 
GLY   C   OXT  sing N N 205 
GLY   OXT HXT  sing N N 206 
HEM   CHA C1A  sing N N 207 
HEM   CHA C4D  doub N N 208 
HEM   CHA HHA  sing N N 209 
HEM   CHB C4A  sing N N 210 
HEM   CHB C1B  doub N N 211 
HEM   CHB HHB  sing N N 212 
HEM   CHC C4B  sing N N 213 
HEM   CHC C1C  doub N N 214 
HEM   CHC HHC  sing N N 215 
HEM   CHD C4C  doub N N 216 
HEM   CHD C1D  sing N N 217 
HEM   CHD HHD  sing N N 218 
HEM   C1A C2A  doub Y N 219 
HEM   C1A NA   sing Y N 220 
HEM   C2A C3A  sing Y N 221 
HEM   C2A CAA  sing N N 222 
HEM   C3A C4A  doub Y N 223 
HEM   C3A CMA  sing N N 224 
HEM   C4A NA   sing Y N 225 
HEM   CMA HMA  sing N N 226 
HEM   CMA HMAA sing N N 227 
HEM   CMA HMAB sing N N 228 
HEM   CAA CBA  sing N N 229 
HEM   CAA HAA  sing N N 230 
HEM   CAA HAAA sing N N 231 
HEM   CBA CGA  sing N N 232 
HEM   CBA HBA  sing N N 233 
HEM   CBA HBAA sing N N 234 
HEM   CGA O1A  doub N N 235 
HEM   CGA O2A  sing N N 236 
HEM   C1B C2B  sing N N 237 
HEM   C1B NB   sing N N 238 
HEM   C2B C3B  doub N N 239 
HEM   C2B CMB  sing N N 240 
HEM   C3B C4B  sing N N 241 
HEM   C3B CAB  sing N N 242 
HEM   C4B NB   doub N N 243 
HEM   CMB HMB  sing N N 244 
HEM   CMB HMBA sing N N 245 
HEM   CMB HMBB sing N N 246 
HEM   CAB CBB  doub N N 247 
HEM   CAB HAB  sing N N 248 
HEM   CBB HBB  sing N N 249 
HEM   CBB HBBA sing N N 250 
HEM   C1C C2C  sing Y N 251 
HEM   C1C NC   sing Y N 252 
HEM   C2C C3C  doub Y N 253 
HEM   C2C CMC  sing N N 254 
HEM   C3C C4C  sing Y N 255 
HEM   C3C CAC  sing N N 256 
HEM   C4C NC   sing Y N 257 
HEM   CMC HMC  sing N N 258 
HEM   CMC HMCA sing N N 259 
HEM   CMC HMCB sing N N 260 
HEM   CAC CBC  doub N N 261 
HEM   CAC HAC  sing N N 262 
HEM   CBC HBC  sing N N 263 
HEM   CBC HBCA sing N N 264 
HEM   C1D C2D  sing N N 265 
HEM   C1D ND   doub N N 266 
HEM   C2D C3D  doub N N 267 
HEM   C2D CMD  sing N N 268 
HEM   C3D C4D  sing N N 269 
HEM   C3D CAD  sing N N 270 
HEM   C4D ND   sing N N 271 
HEM   CMD HMD  sing N N 272 
HEM   CMD HMDA sing N N 273 
HEM   CMD HMDB sing N N 274 
HEM   CAD CBD  sing N N 275 
HEM   CAD HAD  sing N N 276 
HEM   CAD HADA sing N N 277 
HEM   CBD CGD  sing N N 278 
HEM   CBD HBD  sing N N 279 
HEM   CBD HBDA sing N N 280 
HEM   CGD O1D  doub N N 281 
HEM   CGD O2D  sing N N 282 
HEM   O2A H2A  sing N N 283 
HEM   O2D H2D  sing N N 284 
HEM   FE  NA   sing N N 285 
HEM   FE  NB   sing N N 286 
HEM   FE  NC   sing N N 287 
HEM   FE  ND   sing N N 288 
HIS   N   CA   sing N N 289 
HIS   N   H    sing N N 290 
HIS   N   H2   sing N N 291 
HIS   CA  C    sing N N 292 
HIS   CA  CB   sing N N 293 
HIS   CA  HA   sing N N 294 
HIS   C   O    doub N N 295 
HIS   C   OXT  sing N N 296 
HIS   CB  CG   sing N N 297 
HIS   CB  HB2  sing N N 298 
HIS   CB  HB3  sing N N 299 
HIS   CG  ND1  sing Y N 300 
HIS   CG  CD2  doub Y N 301 
HIS   ND1 CE1  doub Y N 302 
HIS   ND1 HD1  sing N N 303 
HIS   CD2 NE2  sing Y N 304 
HIS   CD2 HD2  sing N N 305 
HIS   CE1 NE2  sing Y N 306 
HIS   CE1 HE1  sing N N 307 
HIS   NE2 HE2  sing N N 308 
HIS   OXT HXT  sing N N 309 
ILE   N   CA   sing N N 310 
ILE   N   H    sing N N 311 
ILE   N   H2   sing N N 312 
ILE   CA  C    sing N N 313 
ILE   CA  CB   sing N N 314 
ILE   CA  HA   sing N N 315 
ILE   C   O    doub N N 316 
ILE   C   OXT  sing N N 317 
ILE   CB  CG1  sing N N 318 
ILE   CB  CG2  sing N N 319 
ILE   CB  HB   sing N N 320 
ILE   CG1 CD1  sing N N 321 
ILE   CG1 HG12 sing N N 322 
ILE   CG1 HG13 sing N N 323 
ILE   CG2 HG21 sing N N 324 
ILE   CG2 HG22 sing N N 325 
ILE   CG2 HG23 sing N N 326 
ILE   CD1 HD11 sing N N 327 
ILE   CD1 HD12 sing N N 328 
ILE   CD1 HD13 sing N N 329 
ILE   OXT HXT  sing N N 330 
LEU   N   CA   sing N N 331 
LEU   N   H    sing N N 332 
LEU   N   H2   sing N N 333 
LEU   CA  C    sing N N 334 
LEU   CA  CB   sing N N 335 
LEU   CA  HA   sing N N 336 
LEU   C   O    doub N N 337 
LEU   C   OXT  sing N N 338 
LEU   CB  CG   sing N N 339 
LEU   CB  HB2  sing N N 340 
LEU   CB  HB3  sing N N 341 
LEU   CG  CD1  sing N N 342 
LEU   CG  CD2  sing N N 343 
LEU   CG  HG   sing N N 344 
LEU   CD1 HD11 sing N N 345 
LEU   CD1 HD12 sing N N 346 
LEU   CD1 HD13 sing N N 347 
LEU   CD2 HD21 sing N N 348 
LEU   CD2 HD22 sing N N 349 
LEU   CD2 HD23 sing N N 350 
LEU   OXT HXT  sing N N 351 
LYS   N   CA   sing N N 352 
LYS   N   H    sing N N 353 
LYS   N   H2   sing N N 354 
LYS   CA  C    sing N N 355 
LYS   CA  CB   sing N N 356 
LYS   CA  HA   sing N N 357 
LYS   C   O    doub N N 358 
LYS   C   OXT  sing N N 359 
LYS   CB  CG   sing N N 360 
LYS   CB  HB2  sing N N 361 
LYS   CB  HB3  sing N N 362 
LYS   CG  CD   sing N N 363 
LYS   CG  HG2  sing N N 364 
LYS   CG  HG3  sing N N 365 
LYS   CD  CE   sing N N 366 
LYS   CD  HD2  sing N N 367 
LYS   CD  HD3  sing N N 368 
LYS   CE  NZ   sing N N 369 
LYS   CE  HE2  sing N N 370 
LYS   CE  HE3  sing N N 371 
LYS   NZ  HZ1  sing N N 372 
LYS   NZ  HZ2  sing N N 373 
LYS   NZ  HZ3  sing N N 374 
LYS   OXT HXT  sing N N 375 
MET   N   CA   sing N N 376 
MET   N   H    sing N N 377 
MET   N   H2   sing N N 378 
MET   CA  C    sing N N 379 
MET   CA  CB   sing N N 380 
MET   CA  HA   sing N N 381 
MET   C   O    doub N N 382 
MET   C   OXT  sing N N 383 
MET   CB  CG   sing N N 384 
MET   CB  HB2  sing N N 385 
MET   CB  HB3  sing N N 386 
MET   CG  SD   sing N N 387 
MET   CG  HG2  sing N N 388 
MET   CG  HG3  sing N N 389 
MET   SD  CE   sing N N 390 
MET   CE  HE1  sing N N 391 
MET   CE  HE2  sing N N 392 
MET   CE  HE3  sing N N 393 
MET   OXT HXT  sing N N 394 
PHE   N   CA   sing N N 395 
PHE   N   H    sing N N 396 
PHE   N   H2   sing N N 397 
PHE   CA  C    sing N N 398 
PHE   CA  CB   sing N N 399 
PHE   CA  HA   sing N N 400 
PHE   C   O    doub N N 401 
PHE   C   OXT  sing N N 402 
PHE   CB  CG   sing N N 403 
PHE   CB  HB2  sing N N 404 
PHE   CB  HB3  sing N N 405 
PHE   CG  CD1  doub Y N 406 
PHE   CG  CD2  sing Y N 407 
PHE   CD1 CE1  sing Y N 408 
PHE   CD1 HD1  sing N N 409 
PHE   CD2 CE2  doub Y N 410 
PHE   CD2 HD2  sing N N 411 
PHE   CE1 CZ   doub Y N 412 
PHE   CE1 HE1  sing N N 413 
PHE   CE2 CZ   sing Y N 414 
PHE   CE2 HE2  sing N N 415 
PHE   CZ  HZ   sing N N 416 
PHE   OXT HXT  sing N N 417 
PRO   N   CA   sing N N 418 
PRO   N   CD   sing N N 419 
PRO   N   H    sing N N 420 
PRO   CA  C    sing N N 421 
PRO   CA  CB   sing N N 422 
PRO   CA  HA   sing N N 423 
PRO   C   O    doub N N 424 
PRO   C   OXT  sing N N 425 
PRO   CB  CG   sing N N 426 
PRO   CB  HB2  sing N N 427 
PRO   CB  HB3  sing N N 428 
PRO   CG  CD   sing N N 429 
PRO   CG  HG2  sing N N 430 
PRO   CG  HG3  sing N N 431 
PRO   CD  HD2  sing N N 432 
PRO   CD  HD3  sing N N 433 
PRO   OXT HXT  sing N N 434 
SER   N   CA   sing N N 435 
SER   N   H    sing N N 436 
SER   N   H2   sing N N 437 
SER   CA  C    sing N N 438 
SER   CA  CB   sing N N 439 
SER   CA  HA   sing N N 440 
SER   C   O    doub N N 441 
SER   C   OXT  sing N N 442 
SER   CB  OG   sing N N 443 
SER   CB  HB2  sing N N 444 
SER   CB  HB3  sing N N 445 
SER   OG  HG   sing N N 446 
SER   OXT HXT  sing N N 447 
THR   N   CA   sing N N 448 
THR   N   H    sing N N 449 
THR   N   H2   sing N N 450 
THR   CA  C    sing N N 451 
THR   CA  CB   sing N N 452 
THR   CA  HA   sing N N 453 
THR   C   O    doub N N 454 
THR   C   OXT  sing N N 455 
THR   CB  OG1  sing N N 456 
THR   CB  CG2  sing N N 457 
THR   CB  HB   sing N N 458 
THR   OG1 HG1  sing N N 459 
THR   CG2 HG21 sing N N 460 
THR   CG2 HG22 sing N N 461 
THR   CG2 HG23 sing N N 462 
THR   OXT HXT  sing N N 463 
TRP   N   CA   sing N N 464 
TRP   N   H    sing N N 465 
TRP   N   H2   sing N N 466 
TRP   CA  C    sing N N 467 
TRP   CA  CB   sing N N 468 
TRP   CA  HA   sing N N 469 
TRP   C   O    doub N N 470 
TRP   C   OXT  sing N N 471 
TRP   CB  CG   sing N N 472 
TRP   CB  HB2  sing N N 473 
TRP   CB  HB3  sing N N 474 
TRP   CG  CD1  doub Y N 475 
TRP   CG  CD2  sing Y N 476 
TRP   CD1 NE1  sing Y N 477 
TRP   CD1 HD1  sing N N 478 
TRP   CD2 CE2  doub Y N 479 
TRP   CD2 CE3  sing Y N 480 
TRP   NE1 CE2  sing Y N 481 
TRP   NE1 HE1  sing N N 482 
TRP   CE2 CZ2  sing Y N 483 
TRP   CE3 CZ3  doub Y N 484 
TRP   CE3 HE3  sing N N 485 
TRP   CZ2 CH2  doub Y N 486 
TRP   CZ2 HZ2  sing N N 487 
TRP   CZ3 CH2  sing Y N 488 
TRP   CZ3 HZ3  sing N N 489 
TRP   CH2 HH2  sing N N 490 
TRP   OXT HXT  sing N N 491 
TYR   N   CA   sing N N 492 
TYR   N   H    sing N N 493 
TYR   N   H2   sing N N 494 
TYR   CA  C    sing N N 495 
TYR   CA  CB   sing N N 496 
TYR   CA  HA   sing N N 497 
TYR   C   O    doub N N 498 
TYR   C   OXT  sing N N 499 
TYR   CB  CG   sing N N 500 
TYR   CB  HB2  sing N N 501 
TYR   CB  HB3  sing N N 502 
TYR   CG  CD1  doub Y N 503 
TYR   CG  CD2  sing Y N 504 
TYR   CD1 CE1  sing Y N 505 
TYR   CD1 HD1  sing N N 506 
TYR   CD2 CE2  doub Y N 507 
TYR   CD2 HD2  sing N N 508 
TYR   CE1 CZ   doub Y N 509 
TYR   CE1 HE1  sing N N 510 
TYR   CE2 CZ   sing Y N 511 
TYR   CE2 HE2  sing N N 512 
TYR   CZ  OH   sing N N 513 
TYR   OH  HH   sing N N 514 
TYR   OXT HXT  sing N N 515 
VAL   N   CA   sing N N 516 
VAL   N   H    sing N N 517 
VAL   N   H2   sing N N 518 
VAL   CA  C    sing N N 519 
VAL   CA  CB   sing N N 520 
VAL   CA  HA   sing N N 521 
VAL   C   O    doub N N 522 
VAL   C   OXT  sing N N 523 
VAL   CB  CG1  sing N N 524 
VAL   CB  CG2  sing N N 525 
VAL   CB  HB   sing N N 526 
VAL   CG1 HG11 sing N N 527 
VAL   CG1 HG12 sing N N 528 
VAL   CG1 HG13 sing N N 529 
VAL   CG2 HG21 sing N N 530 
VAL   CG2 HG22 sing N N 531 
VAL   CG2 HG23 sing N N 532 
VAL   OXT HXT  sing N N 533 
# 
_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                    9COU 
_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]   0.013028 
_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]   0.009925 
_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]   0.007906 
_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  
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   ? -11.726 -59.295 -14.865 1.00 130.90 ? 29  SER   A N   1 
ATOM   2    C  CA  . SER   A 1 9   ? -12.583 -58.129 -14.684 1.00 128.90 ? 29  SER   A CA  1 
ATOM   3    C  C   . SER   A 1 9   ? -12.644 -57.282 -15.953 1.00 122.02 ? 29  SER   A C   1 
ATOM   4    O  O   . SER   A 1 9   ? -13.500 -56.408 -16.085 1.00 110.39 ? 29  SER   A O   1 
ATOM   5    C  CB  . SER   A 1 9   ? -12.091 -57.280 -13.509 1.00 106.34 ? 29  SER   A CB  1 
ATOM   6    O  OG  . SER   A 1 9   ? -12.909 -56.137 -13.327 1.00 125.55 ? 29  SER   A OG  1 
ATOM   7    N  N   . HIS   A 1 10  ? -11.732 -57.550 -16.886 1.00 115.23 ? 30  HIS   A N   1 
ATOM   8    C  CA  . HIS   A 1 10  ? -11.656 -56.809 -18.139 1.00 106.17 ? 30  HIS   A CA  1 
ATOM   9    C  C   . HIS   A 1 10  ? -12.507 -57.415 -19.248 1.00 110.84 ? 30  HIS   A C   1 
ATOM   10   O  O   . HIS   A 1 10  ? -12.541 -56.861 -20.352 1.00 116.09 ? 30  HIS   A O   1 
ATOM   11   C  CB  . HIS   A 1 10  ? -10.201 -56.709 -18.608 1.00 117.14 ? 30  HIS   A CB  1 
ATOM   12   C  CG  . HIS   A 1 10  ? -9.443  -55.581 -17.981 1.00 124.09 ? 30  HIS   A CG  1 
ATOM   13   N  ND1 . HIS   A 1 10  ? -8.561  -54.793 -18.689 1.00 123.30 ? 30  HIS   A ND1 1 
ATOM   14   C  CD2 . HIS   A 1 10  ? -9.439  -55.105 -16.714 1.00 123.74 ? 30  HIS   A CD2 1 
ATOM   15   C  CE1 . HIS   A 1 10  ? -8.045  -53.881 -17.884 1.00 125.46 ? 30  HIS   A CE1 1 
ATOM   16   N  NE2 . HIS   A 1 10  ? -8.561  -54.049 -16.680 1.00 111.36 ? 30  HIS   A NE2 1 
ATOM   17   N  N   . GLY   A 1 11  ? -13.188 -58.527 -18.989 1.00 114.43 ? 31  GLY   A N   1 
ATOM   18   C  CA  . GLY   A 1 11  ? -14.062 -59.148 -19.959 1.00 109.50 ? 31  GLY   A CA  1 
ATOM   19   C  C   . GLY   A 1 11  ? -15.536 -58.864 -19.768 1.00 117.80 ? 31  GLY   A C   1 
ATOM   20   O  O   . GLY   A 1 11  ? -16.363 -59.506 -20.426 1.00 130.92 ? 31  GLY   A O   1 
ATOM   21   N  N   . LEU   A 1 12  ? -15.893 -57.919 -18.894 1.00 129.43 ? 32  LEU   A N   1 
ATOM   22   C  CA  . LEU   A 1 12  ? -17.301 -57.672 -18.597 1.00 119.78 ? 32  LEU   A CA  1 
ATOM   23   C  C   . LEU   A 1 12  ? -18.046 -57.151 -19.821 1.00 120.37 ? 32  LEU   A C   1 
ATOM   24   O  O   . LEU   A 1 12  ? -19.205 -57.516 -20.053 1.00 129.58 ? 32  LEU   A O   1 
ATOM   25   C  CB  . LEU   A 1 12  ? -17.418 -56.688 -17.434 1.00 108.83 ? 32  LEU   A CB  1 
ATOM   26   C  CG  . LEU   A 1 12  ? -18.826 -56.225 -17.051 1.00 115.59 ? 32  LEU   A CG  1 
ATOM   27   C  CD1 . LEU   A 1 12  ? -19.717 -57.414 -16.730 1.00 132.52 ? 32  LEU   A CD1 1 
ATOM   28   C  CD2 . LEU   A 1 12  ? -18.765 -55.264 -15.876 1.00 113.30 ? 32  LEU   A CD2 1 
ATOM   29   N  N   . PHE   A 1 13  ? -17.397 -56.302 -20.621 1.00 117.18 ? 33  PHE   A N   1 
ATOM   30   C  CA  . PHE   A 1 13  ? -18.033 -55.748 -21.809 1.00 117.20 ? 33  PHE   A CA  1 
ATOM   31   C  C   . PHE   A 1 13  ? -17.950 -56.676 -23.014 1.00 132.73 ? 33  PHE   A C   1 
ATOM   32   O  O   . PHE   A 1 13  ? -18.819 -56.614 -23.891 1.00 135.55 ? 33  PHE   A O   1 
ATOM   33   C  CB  . PHE   A 1 13  ? -17.415 -54.388 -22.139 1.00 117.66 ? 33  PHE   A CB  1 
ATOM   34   C  CG  . PHE   A 1 13  ? -17.763 -53.317 -21.144 1.00 118.11 ? 33  PHE   A CG  1 
ATOM   35   C  CD1 . PHE   A 1 13  ? -19.068 -53.167 -20.705 1.00 113.46 ? 33  PHE   A CD1 1 
ATOM   36   C  CD2 . PHE   A 1 13  ? -16.787 -52.481 -20.625 1.00 105.39 ? 33  PHE   A CD2 1 
ATOM   37   C  CE1 . PHE   A 1 13  ? -19.400 -52.195 -19.783 1.00 108.04 ? 33  PHE   A CE1 1 
ATOM   38   C  CE2 . PHE   A 1 13  ? -17.112 -51.506 -19.700 1.00 99.93  ? 33  PHE   A CE2 1 
ATOM   39   C  CZ  . PHE   A 1 13  ? -18.421 -51.363 -19.278 1.00 112.10 ? 33  PHE   A CZ  1 
ATOM   40   N  N   . LYS   A 1 14  ? -16.931 -57.539 -23.083 1.00 137.23 ? 34  LYS   A N   1 
ATOM   41   C  CA  . LYS   A 1 14  ? -16.950 -58.605 -24.081 1.00 142.50 ? 34  LYS   A CA  1 
ATOM   42   C  C   . LYS   A 1 14  ? -18.055 -59.608 -23.778 1.00 140.77 ? 34  LYS   A C   1 
ATOM   43   O  O   . LYS   A 1 14  ? -18.696 -60.134 -24.696 1.00 143.90 ? 34  LYS   A O   1 
ATOM   44   C  CB  . LYS   A 1 14  ? -15.595 -59.310 -24.140 1.00 154.67 ? 34  LYS   A CB  1 
ATOM   45   C  CG  . LYS   A 1 14  ? -14.468 -58.490 -24.742 1.00 161.41 ? 34  LYS   A CG  1 
ATOM   46   C  CD  . LYS   A 1 14  ? -13.188 -59.310 -24.815 1.00 176.93 ? 34  LYS   A CD  1 
ATOM   47   C  CE  . LYS   A 1 14  ? -12.038 -58.503 -25.391 1.00 178.80 ? 34  LYS   A CE  1 
ATOM   48   N  NZ  . LYS   A 1 14  ? -10.775 -59.290 -25.409 1.00 179.26 ? 34  LYS   A NZ  1 
ATOM   49   N  N   . LYS   A 1 15  ? -18.285 -59.888 -22.493 1.00 130.05 ? 35  LYS   A N   1 
ATOM   50   C  CA  . LYS   A 1 15  ? -19.360 -60.795 -22.103 1.00 130.68 ? 35  LYS   A CA  1 
ATOM   51   C  C   . LYS   A 1 15  ? -20.722 -60.220 -22.470 1.00 133.98 ? 35  LYS   A C   1 
ATOM   52   O  O   . LYS   A 1 15  ? -21.543 -60.891 -23.106 1.00 136.12 ? 35  LYS   A O   1 
ATOM   53   C  CB  . LYS   A 1 15  ? -19.284 -61.074 -20.601 1.00 135.56 ? 35  LYS   A CB  1 
ATOM   54   C  CG  . LYS   A 1 15  ? -20.604 -61.519 -19.989 1.00 145.44 ? 35  LYS   A CG  1 
ATOM   55   C  CD  . LYS   A 1 15  ? -20.697 -61.118 -18.524 1.00 150.63 ? 35  LYS   A CD  1 
ATOM   56   C  CE  . LYS   A 1 15  ? -22.107 -61.308 -17.988 1.00 157.58 ? 35  LYS   A CE  1 
ATOM   57   N  NZ  . LYS   A 1 15  ? -22.240 -60.826 -16.585 1.00 147.58 ? 35  LYS   A NZ  1 
ATOM   58   N  N   . LEU   A 1 16  ? -20.978 -58.972 -22.076 1.00 132.86 ? 36  LEU   A N   1 
ATOM   59   C  CA  . LEU   A 1 16  ? -22.267 -58.330 -22.305 1.00 127.61 ? 36  LEU   A CA  1 
ATOM   60   C  C   . LEU   A 1 16  ? -22.502 -57.951 -23.760 1.00 136.86 ? 36  LEU   A C   1 
ATOM   61   O  O   . LEU   A 1 16  ? -23.591 -57.461 -24.078 1.00 145.14 ? 36  LEU   A O   1 
ATOM   62   C  CB  . LEU   A 1 16  ? -22.390 -57.084 -21.429 1.00 127.63 ? 36  LEU   A CB  1 
ATOM   63   C  CG  . LEU   A 1 16  ? -22.498 -57.314 -19.923 1.00 130.65 ? 36  LEU   A CG  1 
ATOM   64   C  CD1 . LEU   A 1 16  ? -22.377 -55.995 -19.180 1.00 128.02 ? 36  LEU   A CD1 1 
ATOM   65   C  CD2 . LEU   A 1 16  ? -23.811 -58.002 -19.586 1.00 127.52 ? 36  LEU   A CD2 1 
ATOM   66   N  N   . GLY   A 1 17  ? -21.532 -58.160 -24.646 1.00 129.99 ? 37  GLY   A N   1 
ATOM   67   C  CA  . GLY   A 1 17  ? -21.708 -57.753 -26.028 1.00 132.32 ? 37  GLY   A CA  1 
ATOM   68   C  C   . GLY   A 1 17  ? -21.759 -56.254 -26.207 1.00 143.44 ? 37  GLY   A C   1 
ATOM   69   O  O   . GLY   A 1 17  ? -22.464 -55.761 -27.095 1.00 146.69 ? 37  GLY   A O   1 
ATOM   70   N  N   . ILE   A 1 18  ? -21.036 -55.514 -25.376 1.00 143.58 ? 38  ILE   A N   1 
ATOM   71   C  CA  . ILE   A 1 18  ? -20.998 -54.056 -25.429 1.00 138.40 ? 38  ILE   A CA  1 
ATOM   72   C  C   . ILE   A 1 18  ? -19.675 -53.645 -26.064 1.00 130.26 ? 38  ILE   A C   1 
ATOM   73   O  O   . ILE   A 1 18  ? -18.611 -53.976 -25.518 1.00 134.07 ? 38  ILE   A O   1 
ATOM   74   C  CB  . ILE   A 1 18  ? -21.159 -53.437 -24.034 1.00 133.08 ? 38  ILE   A CB  1 
ATOM   75   C  CG1 . ILE   A 1 18  ? -22.570 -53.697 -23.502 1.00 129.76 ? 38  ILE   A CG1 1 
ATOM   76   C  CG2 . ILE   A 1 18  ? -20.857 -51.950 -24.078 1.00 126.35 ? 38  ILE   A CG2 1 
ATOM   77   C  CD1 . ILE   A 1 18  ? -22.771 -53.267 -22.071 1.00 129.35 ? 38  ILE   A CD1 1 
ATOM   78   N  N   . PRO   A 1 19  ? -19.687 -52.941 -27.192 1.00 120.36 ? 39  PRO   A N   1 
ATOM   79   C  CA  . PRO   A 1 19  ? -18.430 -52.602 -27.865 1.00 129.10 ? 39  PRO   A CA  1 
ATOM   80   C  C   . PRO   A 1 19  ? -17.622 -51.587 -27.071 1.00 135.28 ? 39  PRO   A C   1 
ATOM   81   O  O   . PRO   A 1 19  ? -18.121 -50.913 -26.167 1.00 131.30 ? 39  PRO   A O   1 
ATOM   82   C  CB  . PRO   A 1 19  ? -18.892 -52.020 -29.203 1.00 125.98 ? 39  PRO   A CB  1 
ATOM   83   C  CG  . PRO   A 1 19  ? -20.250 -51.471 -28.914 1.00 108.94 ? 39  PRO   A CG  1 
ATOM   84   C  CD  . PRO   A 1 19  ? -20.860 -52.399 -27.898 1.00 121.56 ? 39  PRO   A CD  1 
ATOM   85   N  N   . GLY   A 1 20  ? -16.344 -51.491 -27.427 1.00 125.09 ? 40  GLY   A N   1 
ATOM   86   C  CA  . GLY   A 1 20  ? -15.437 -50.576 -26.776 1.00 117.93 ? 40  GLY   A CA  1 
ATOM   87   C  C   . GLY   A 1 20  ? -13.988 -50.878 -27.096 1.00 126.30 ? 40  GLY   A C   1 
ATOM   88   O  O   . GLY   A 1 20  ? -13.650 -51.947 -27.612 1.00 126.48 ? 40  GLY   A O   1 
ATOM   89   N  N   . PRO   A 1 21  ? -13.099 -49.934 -26.792 1.00 127.88 ? 41  PRO   A N   1 
ATOM   90   C  CA  . PRO   A 1 21  ? -11.674 -50.146 -27.068 1.00 127.00 ? 41  PRO   A CA  1 
ATOM   91   C  C   . PRO   A 1 21  ? -11.097 -51.265 -26.217 1.00 120.49 ? 41  PRO   A C   1 
ATOM   92   O  O   . PRO   A 1 21  ? -11.549 -51.529 -25.100 1.00 115.69 ? 41  PRO   A O   1 
ATOM   93   C  CB  . PRO   A 1 21  ? -11.039 -48.795 -26.717 1.00 122.39 ? 41  PRO   A CB  1 
ATOM   94   C  CG  . PRO   A 1 21  ? -11.993 -48.169 -25.753 1.00 120.76 ? 41  PRO   A CG  1 
ATOM   95   C  CD  . PRO   A 1 21  ? -13.359 -48.618 -26.182 1.00 106.86 ? 41  PRO   A CD  1 
ATOM   96   N  N   . THR   A 1 22  ? -10.086 -51.927 -26.764 1.00 124.91 ? 42  THR   A N   1 
ATOM   97   C  CA  . THR   A 1 22  ? -9.457  -53.048 -26.076 1.00 113.00 ? 42  THR   A CA  1 
ATOM   98   C  C   . THR   A 1 22  ? -8.590  -52.533 -24.934 1.00 113.96 ? 42  THR   A C   1 
ATOM   99   O  O   . THR   A 1 22  ? -7.646  -51.771 -25.180 1.00 104.10 ? 42  THR   A O   1 
ATOM   100  C  CB  . THR   A 1 22  ? -8.618  -53.868 -27.050 1.00 122.74 ? 42  THR   A CB  1 
ATOM   101  O  OG1 . THR   A 1 22  ? -9.416  -54.222 -28.186 1.00 117.74 ? 42  THR   A OG1 1 
ATOM   102  C  CG2 . THR   A 1 22  ? -8.116  -55.136 -26.380 1.00 122.71 ? 42  THR   A CG2 1 
ATOM   103  N  N   . PRO   A 1 23  ? -8.867  -52.908 -23.689 1.00 105.34 ? 43  PRO   A N   1 
ATOM   104  C  CA  . PRO   A 1 23  ? -8.077  -52.394 -22.568 1.00 91.87  ? 43  PRO   A CA  1 
ATOM   105  C  C   . PRO   A 1 23  ? -6.760  -53.133 -22.402 1.00 122.93 ? 43  PRO   A C   1 
ATOM   106  O  O   . PRO   A 1 23  ? -6.632  -54.319 -22.715 1.00 126.56 ? 43  PRO   A O   1 
ATOM   107  C  CB  . PRO   A 1 23  ? -8.993  -52.632 -21.362 1.00 106.61 ? 43  PRO   A CB  1 
ATOM   108  C  CG  . PRO   A 1 23  ? -9.773  -53.845 -21.742 1.00 108.81 ? 43  PRO   A CG  1 
ATOM   109  C  CD  . PRO   A 1 23  ? -9.980  -53.762 -23.237 1.00 103.48 ? 43  PRO   A CD  1 
ATOM   110  N  N   . LEU   A 1 24  ? -5.771  -52.402 -21.901 1.00 116.14 ? 44  LEU   A N   1 
ATOM   111  C  CA  . LEU   A 1 24  ? -4.489  -52.968 -21.519 1.00 108.02 ? 44  LEU   A CA  1 
ATOM   112  C  C   . LEU   A 1 24  ? -4.544  -53.456 -20.078 1.00 114.93 ? 44  LEU   A C   1 
ATOM   113  O  O   . LEU   A 1 24  ? -5.375  -52.997 -19.288 1.00 104.75 ? 44  LEU   A O   1 
ATOM   114  C  CB  . LEU   A 1 24  ? -3.386  -51.924 -21.680 1.00 102.29 ? 44  LEU   A CB  1 
ATOM   115  C  CG  . LEU   A 1 24  ? -3.097  -51.441 -23.102 1.00 119.61 ? 44  LEU   A CG  1 
ATOM   116  C  CD1 . LEU   A 1 24  ? -2.031  -50.358 -23.086 1.00 112.19 ? 44  LEU   A CD1 1 
ATOM   117  C  CD2 . LEU   A 1 24  ? -2.672  -52.600 -23.991 1.00 122.27 ? 44  LEU   A CD2 1 
ATOM   118  N  N   . PRO   A 1 25  ? -3.685  -54.405 -19.706 1.00 110.75 ? 45  PRO   A N   1 
ATOM   119  C  CA  . PRO   A 1 25  ? -3.673  -54.875 -18.315 1.00 115.85 ? 45  PRO   A CA  1 
ATOM   120  C  C   . PRO   A 1 25  ? -3.349  -53.757 -17.333 1.00 118.99 ? 45  PRO   A C   1 
ATOM   121  O  O   . PRO   A 1 25  ? -2.496  -52.906 -17.593 1.00 115.79 ? 45  PRO   A O   1 
ATOM   122  C  CB  . PRO   A 1 25  ? -2.566  -55.935 -18.309 1.00 123.46 ? 45  PRO   A CB  1 
ATOM   123  C  CG  . PRO   A 1 25  ? -2.497  -56.409 -19.722 1.00 117.00 ? 45  PRO   A CG  1 
ATOM   124  C  CD  . PRO   A 1 25  ? -2.789  -55.200 -20.564 1.00 105.99 ? 45  PRO   A CD  1 
ATOM   125  N  N   . PHE   A 1 26  ? -4.064  -53.763 -16.204 1.00 119.17 ? 46  PHE   A N   1 
ATOM   126  C  CA  . PHE   A 1 26  ? -3.920  -52.777 -15.135 1.00 111.31 ? 46  PHE   A CA  1 
ATOM   127  C  C   . PHE   A 1 26  ? -4.358  -51.374 -15.542 1.00 106.84 ? 46  PHE   A C   1 
ATOM   128  O  O   . PHE   A 1 26  ? -5.190  -50.761 -14.866 1.00 122.92 ? 46  PHE   A O   1 
ATOM   129  C  CB  . PHE   A 1 26  ? -2.473  -52.720 -14.636 1.00 104.86 ? 46  PHE   A CB  1 
ATOM   130  C  CG  . PHE   A 1 26  ? -1.995  -54.002 -14.019 1.00 130.02 ? 46  PHE   A CG  1 
ATOM   131  C  CD1 . PHE   A 1 26  ? -2.239  -54.276 -12.684 1.00 139.48 ? 46  PHE   A CD1 1 
ATOM   132  C  CD2 . PHE   A 1 26  ? -1.300  -54.932 -14.774 1.00 143.11 ? 46  PHE   A CD2 1 
ATOM   133  C  CE1 . PHE   A 1 26  ? -1.800  -55.454 -12.113 1.00 161.85 ? 46  PHE   A CE1 1 
ATOM   134  C  CE2 . PHE   A 1 26  ? -0.858  -56.112 -14.209 1.00 144.41 ? 46  PHE   A CE2 1 
ATOM   135  C  CZ  . PHE   A 1 26  ? -1.109  -56.374 -12.876 1.00 159.14 ? 46  PHE   A CZ  1 
ATOM   136  N  N   . LEU   A 1 27  ? -3.802  -50.852 -16.638 1.00 114.53 ? 47  LEU   A N   1 
ATOM   137  C  CA  . LEU   A 1 27  ? -4.138  -49.499 -17.064 1.00 118.50 ? 47  LEU   A CA  1 
ATOM   138  C  C   . LEU   A 1 27  ? -5.561  -49.382 -17.594 1.00 116.50 ? 47  LEU   A C   1 
ATOM   139  O  O   . LEU   A 1 27  ? -6.121  -48.282 -17.585 1.00 104.80 ? 47  LEU   A O   1 
ATOM   140  C  CB  . LEU   A 1 27  ? -3.159  -49.022 -18.138 1.00 105.40 ? 47  LEU   A CB  1 
ATOM   141  C  CG  . LEU   A 1 27  ? -1.686  -48.931 -17.739 1.00 112.77 ? 47  LEU   A CG  1 
ATOM   142  C  CD1 . LEU   A 1 27  ? -0.881  -48.247 -18.835 1.00 117.89 ? 47  LEU   A CD1 1 
ATOM   143  C  CD2 . LEU   A 1 27  ? -1.532  -48.200 -16.416 1.00 115.20 ? 47  LEU   A CD2 1 
ATOM   144  N  N   . GLY   A 1 28  ? -6.162  -50.479 -18.045 1.00 119.45 ? 48  GLY   A N   1 
ATOM   145  C  CA  . GLY   A 1 28  ? -7.444  -50.383 -18.713 1.00 100.63 ? 48  GLY   A CA  1 
ATOM   146  C  C   . GLY   A 1 28  ? -7.332  -49.605 -20.006 1.00 95.75  ? 48  GLY   A C   1 
ATOM   147  O  O   . GLY   A 1 28  ? -6.589  -49.995 -20.912 1.00 110.03 ? 48  GLY   A O   1 
ATOM   148  N  N   . ASN   A 1 29  ? -8.051  -48.484 -20.098 1.00 102.51 ? 49  ASN   A N   1 
ATOM   149  C  CA  . ASN   A 1 29  ? -8.004  -47.629 -21.278 1.00 104.02 ? 49  ASN   A CA  1 
ATOM   150  C  C   . ASN   A 1 29  ? -7.496  -46.228 -20.955 1.00 99.05  ? 49  ASN   A C   1 
ATOM   151  O  O   . ASN   A 1 29  ? -7.738  -45.296 -21.728 1.00 104.61 ? 49  ASN   A O   1 
ATOM   152  C  CB  . ASN   A 1 29  ? -9.382  -47.545 -21.935 1.00 107.22 ? 49  ASN   A CB  1 
ATOM   153  C  CG  . ASN   A 1 29  ? -10.073 -48.889 -22.015 1.00 111.17 ? 49  ASN   A CG  1 
ATOM   154  O  OD1 . ASN   A 1 29  ? -10.661 -49.352 -21.039 1.00 103.61 ? 49  ASN   A OD1 1 
ATOM   155  N  ND2 . ASN   A 1 29  ? -10.016 -49.519 -23.183 1.00 117.07 ? 49  ASN   A ND2 1 
ATOM   156  N  N   . ILE   A 1 30  ? -6.785  -46.059 -19.835 1.00 94.08  ? 50  ILE   A N   1 
ATOM   157  C  CA  . ILE   A 1 30  ? -6.383  -44.723 -19.407 1.00 103.64 ? 50  ILE   A CA  1 
ATOM   158  C  C   . ILE   A 1 30  ? -5.356  -44.101 -20.342 1.00 111.97 ? 50  ILE   A C   1 
ATOM   159  O  O   . ILE   A 1 30  ? -5.223  -42.872 -20.371 1.00 116.59 ? 50  ILE   A O   1 
ATOM   160  C  CB  . ILE   A 1 30  ? -5.828  -44.739 -17.970 1.00 102.53 ? 50  ILE   A CB  1 
ATOM   161  C  CG1 . ILE   A 1 30  ? -4.529  -45.545 -17.903 1.00 111.31 ? 50  ILE   A CG1 1 
ATOM   162  C  CG2 . ILE   A 1 30  ? -6.870  -45.273 -16.997 1.00 114.77 ? 50  ILE   A CG2 1 
ATOM   163  C  CD1 . ILE   A 1 30  ? -3.670  -45.201 -16.712 1.00 108.72 ? 50  ILE   A CD1 1 
ATOM   164  N  N   . LEU   A 1 31  ? -4.613  -44.909 -21.104 1.00 113.36 ? 51  LEU   A N   1 
ATOM   165  C  CA  . LEU   A 1 31  ? -3.660  -44.339 -22.050 1.00 109.35 ? 51  LEU   A CA  1 
ATOM   166  C  C   . LEU   A 1 31  ? -4.364  -43.529 -23.129 1.00 116.40 ? 51  LEU   A C   1 
ATOM   167  O  O   . LEU   A 1 31  ? -3.766  -42.617 -23.711 1.00 126.83 ? 51  LEU   A O   1 
ATOM   168  C  CB  . LEU   A 1 31  ? -2.810  -45.439 -22.685 1.00 111.81 ? 51  LEU   A CB  1 
ATOM   169  C  CG  . LEU   A 1 31  ? -1.749  -46.093 -21.799 1.00 111.39 ? 51  LEU   A CG  1 
ATOM   170  C  CD1 . LEU   A 1 31  ? -0.801  -46.932 -22.641 1.00 103.61 ? 51  LEU   A CD1 1 
ATOM   171  C  CD2 . LEU   A 1 31  ? -0.984  -45.045 -21.006 1.00 99.77  ? 51  LEU   A CD2 1 
ATOM   172  N  N   . SER   A 1 32  ? -5.631  -43.842 -23.406 1.00 112.77 ? 52  SER   A N   1 
ATOM   173  C  CA  . SER   A 1 32  ? -6.402  -43.087 -24.384 1.00 122.22 ? 52  SER   A CA  1 
ATOM   174  C  C   . SER   A 1 32  ? -6.745  -41.683 -23.905 1.00 124.99 ? 52  SER   A C   1 
ATOM   175  O  O   . SER   A 1 32  ? -7.190  -40.863 -24.716 1.00 126.28 ? 52  SER   A O   1 
ATOM   176  C  CB  . SER   A 1 32  ? -7.684  -43.842 -24.732 1.00 121.74 ? 52  SER   A CB  1 
ATOM   177  O  OG  . SER   A 1 32  ? -7.395  -45.134 -25.235 1.00 113.46 ? 52  SER   A OG  1 
ATOM   178  N  N   . TYR   A 1 33  ? -6.550  -41.387 -22.621 1.00 121.02 ? 53  TYR   A N   1 
ATOM   179  C  CA  . TYR   A 1 33  ? -6.793  -40.058 -22.077 1.00 119.68 ? 53  TYR   A CA  1 
ATOM   180  C  C   . TYR   A 1 33  ? -5.688  -39.064 -22.418 1.00 141.91 ? 53  TYR   A C   1 
ATOM   181  O  O   . TYR   A 1 33  ? -5.630  -37.994 -21.801 1.00 144.33 ? 53  TYR   A O   1 
ATOM   182  C  CB  . TYR   A 1 33  ? -6.961  -40.132 -20.556 1.00 103.25 ? 53  TYR   A CB  1 
ATOM   183  C  CG  . TYR   A 1 33  ? -8.230  -40.813 -20.096 1.00 122.03 ? 53  TYR   A CG  1 
ATOM   184  C  CD1 . TYR   A 1 33  ? -9.377  -40.797 -20.878 1.00 112.95 ? 53  TYR   A CD1 1 
ATOM   185  C  CD2 . TYR   A 1 33  ? -8.281  -41.469 -18.873 1.00 116.43 ? 53  TYR   A CD2 1 
ATOM   186  C  CE1 . TYR   A 1 33  ? -10.539 -41.417 -20.455 1.00 103.99 ? 53  TYR   A CE1 1 
ATOM   187  C  CE2 . TYR   A 1 33  ? -9.436  -42.092 -18.442 1.00 109.84 ? 53  TYR   A CE2 1 
ATOM   188  C  CZ  . TYR   A 1 33  ? -10.562 -42.063 -19.237 1.00 116.86 ? 53  TYR   A CZ  1 
ATOM   189  O  OH  . TYR   A 1 33  ? -11.715 -42.682 -18.810 1.00 117.35 ? 53  TYR   A OH  1 
ATOM   190  N  N   . HIS   A 1 34  ? -4.812  -39.385 -23.373 1.00 160.89 ? 54  HIS   A N   1 
ATOM   191  C  CA  . HIS   A 1 34  ? -3.725  -38.476 -23.718 1.00 170.90 ? 54  HIS   A CA  1 
ATOM   192  C  C   . HIS   A 1 34  ? -4.220  -37.239 -24.456 1.00 166.28 ? 54  HIS   A C   1 
ATOM   193  O  O   . HIS   A 1 34  ? -3.527  -36.216 -24.458 1.00 175.19 ? 54  HIS   A O   1 
ATOM   194  C  CB  . HIS   A 1 34  ? -2.671  -39.204 -24.555 1.00 184.86 ? 54  HIS   A CB  1 
ATOM   195  C  CG  . HIS   A 1 34  ? -3.061  -39.399 -25.987 1.00 193.04 ? 54  HIS   A CG  1 
ATOM   196  N  ND1 . HIS   A 1 34  ? -4.179  -40.112 -26.365 1.00 188.29 ? 54  HIS   A ND1 1 
ATOM   197  C  CD2 . HIS   A 1 34  ? -2.477  -38.980 -27.134 1.00 192.25 ? 54  HIS   A CD2 1 
ATOM   198  C  CE1 . HIS   A 1 34  ? -4.269  -40.120 -27.683 1.00 189.11 ? 54  HIS   A CE1 1 
ATOM   199  N  NE2 . HIS   A 1 34  ? -3.248  -39.441 -28.174 1.00 190.38 ? 54  HIS   A NE2 1 
ATOM   200  N  N   . LYS   A 1 35  ? -5.395  -37.309 -25.081 1.00 155.64 ? 55  LYS   A N   1 
ATOM   201  C  CA  . LYS   A 1 35  ? -6.024  -36.155 -25.706 1.00 155.02 ? 55  LYS   A CA  1 
ATOM   202  C  C   . LYS   A 1 35  ? -7.101  -35.535 -24.825 1.00 142.35 ? 55  LYS   A C   1 
ATOM   203  O  O   . LYS   A 1 35  ? -7.811  -34.630 -25.274 1.00 154.54 ? 55  LYS   A O   1 
ATOM   204  C  CB  . LYS   A 1 35  ? -6.622  -36.542 -27.060 1.00 146.45 ? 55  LYS   A CB  1 
ATOM   205  C  CG  . LYS   A 1 35  ? -5.599  -36.765 -28.162 1.00 161.38 ? 55  LYS   A CG  1 
ATOM   206  C  CD  . LYS   A 1 35  ? -6.280  -37.149 -29.467 1.00 166.45 ? 55  LYS   A CD  1 
ATOM   207  C  CE  . LYS   A 1 35  ? -5.282  -37.262 -30.608 1.00 166.05 ? 55  LYS   A CE  1 
ATOM   208  N  NZ  . LYS   A 1 35  ? -4.646  -35.954 -30.925 1.00 163.02 ? 55  LYS   A NZ  1 
ATOM   209  N  N   . GLY   A 1 36  ? -7.237  -36.000 -23.590 1.00 126.85 ? 56  GLY   A N   1 
ATOM   210  C  CA  . GLY   A 1 36  ? -8.257  -35.503 -22.693 1.00 138.23 ? 56  GLY   A CA  1 
ATOM   211  C  C   . GLY   A 1 36  ? -9.544  -36.307 -22.776 1.00 136.61 ? 56  GLY   A C   1 
ATOM   212  O  O   . GLY   A 1 36  ? -9.805  -37.030 -23.737 1.00 133.85 ? 56  GLY   A O   1 
ATOM   213  N  N   . PHE   A 1 37  ? -10.357 -36.171 -21.725 1.00 108.31 ? 57  PHE   A N   1 
ATOM   214  C  CA  . PHE   A 1 37  ? -11.642 -36.863 -21.671 1.00 110.18 ? 57  PHE   A CA  1 
ATOM   215  C  C   . PHE   A 1 37  ? -12.493 -36.547 -22.892 1.00 115.65 ? 57  PHE   A C   1 
ATOM   216  O  O   . PHE   A 1 37  ? -13.152 -37.433 -23.449 1.00 115.69 ? 57  PHE   A O   1 
ATOM   217  C  CB  . PHE   A 1 37  ? -12.408 -36.471 -20.405 1.00 122.46 ? 57  PHE   A CB  1 
ATOM   218  C  CG  . PHE   A 1 37  ? -11.648 -36.690 -19.127 1.00 135.78 ? 57  PHE   A CG  1 
ATOM   219  C  CD1 . PHE   A 1 37  ? -10.678 -35.790 -18.715 1.00 157.41 ? 57  PHE   A CD1 1 
ATOM   220  C  CD2 . PHE   A 1 37  ? -11.933 -37.776 -18.316 1.00 116.78 ? 57  PHE   A CD2 1 
ATOM   221  C  CE1 . PHE   A 1 37  ? -9.988  -35.984 -17.536 1.00 169.42 ? 57  PHE   A CE1 1 
ATOM   222  C  CE2 . PHE   A 1 37  ? -11.249 -37.973 -17.133 1.00 131.90 ? 57  PHE   A CE2 1 
ATOM   223  C  CZ  . PHE   A 1 37  ? -10.275 -37.076 -16.743 1.00 169.00 ? 57  PHE   A CZ  1 
ATOM   224  N  N   . CYS   A 1 38  ? -12.487 -35.284 -23.323 1.00 117.42 ? 58  CYS   A N   1 
ATOM   225  C  CA  . CYS   A 1 38  ? -13.416 -34.840 -24.356 1.00 121.27 ? 58  CYS   A CA  1 
ATOM   226  C  C   . CYS   A 1 38  ? -13.140 -35.528 -25.687 1.00 118.76 ? 58  CYS   A C   1 
ATOM   227  O  O   . CYS   A 1 38  ? -14.039 -36.128 -26.286 1.00 119.54 ? 58  CYS   A O   1 
ATOM   228  C  CB  . CYS   A 1 38  ? -13.335 -33.321 -24.501 1.00 124.06 ? 58  CYS   A CB  1 
ATOM   229  S  SG  . CYS   A 1 38  ? -13.788 -32.411 -23.005 1.00 126.38 ? 58  CYS   A SG  1 
ATOM   230  N  N   . MET   A 1 39  ? -11.896 -35.453 -26.166 1.00 115.17 ? 59  MET   A N   1 
ATOM   231  C  CA  . MET   A 1 39  ? -11.563 -36.071 -27.445 1.00 121.76 ? 59  MET   A CA  1 
ATOM   232  C  C   . MET   A 1 39  ? -11.724 -37.584 -27.395 1.00 116.37 ? 59  MET   A C   1 
ATOM   233  O  O   . MET   A 1 39  ? -12.055 -38.206 -28.411 1.00 123.99 ? 59  MET   A O   1 
ATOM   234  C  CB  . MET   A 1 39  ? -10.137 -35.699 -27.852 1.00 129.11 ? 59  MET   A CB  1 
ATOM   235  C  CG  . MET   A 1 39  ? -9.843  -34.208 -27.785 1.00 132.13 ? 59  MET   A CG  1 
ATOM   236  S  SD  . MET   A 1 39  ? -11.075 -33.202 -28.636 1.00 170.40 ? 59  MET   A SD  1 
ATOM   237  C  CE  . MET   A 1 39  ? -10.940 -33.829 -30.308 1.00 154.10 ? 59  MET   A CE  1 
ATOM   238  N  N   . PHE   A 1 40  ? -11.503 -38.191 -26.228 1.00 104.47 ? 60  PHE   A N   1 
ATOM   239  C  CA  . PHE   A 1 40  ? -11.671 -39.634 -26.096 1.00 112.12 ? 60  PHE   A CA  1 
ATOM   240  C  C   . PHE   A 1 40  ? -13.132 -40.035 -26.264 1.00 119.98 ? 60  PHE   A C   1 
ATOM   241  O  O   . PHE   A 1 40  ? -13.448 -40.971 -27.009 1.00 117.11 ? 60  PHE   A O   1 
ATOM   242  C  CB  . PHE   A 1 40  ? -11.133 -40.097 -24.742 1.00 117.10 ? 60  PHE   A CB  1 
ATOM   243  C  CG  . PHE   A 1 40  ? -11.448 -41.529 -24.421 1.00 107.65 ? 60  PHE   A CG  1 
ATOM   244  C  CD1 . PHE   A 1 40  ? -10.892 -42.557 -25.162 1.00 103.07 ? 60  PHE   A CD1 1 
ATOM   245  C  CD2 . PHE   A 1 40  ? -12.292 -41.848 -23.370 1.00 108.24 ? 60  PHE   A CD2 1 
ATOM   246  C  CE1 . PHE   A 1 40  ? -11.176 -43.877 -24.866 1.00 106.39 ? 60  PHE   A CE1 1 
ATOM   247  C  CE2 . PHE   A 1 40  ? -12.579 -43.165 -23.068 1.00 113.76 ? 60  PHE   A CE2 1 
ATOM   248  C  CZ  . PHE   A 1 40  ? -12.021 -44.181 -23.818 1.00 113.70 ? 60  PHE   A CZ  1 
ATOM   249  N  N   . ASP   A 1 41  ? -14.039 -39.332 -25.582 1.00 120.96 ? 61  ASP   A N   1 
ATOM   250  C  CA  . ASP   A 1 41  ? -15.457 -39.663 -25.680 1.00 102.66 ? 61  ASP   A CA  1 
ATOM   251  C  C   . ASP   A 1 41  ? -16.008 -39.350 -27.066 1.00 110.35 ? 61  ASP   A C   1 
ATOM   252  O  O   . ASP   A 1 41  ? -16.830 -40.107 -27.595 1.00 115.01 ? 61  ASP   A O   1 
ATOM   253  C  CB  . ASP   A 1 41  ? -16.248 -38.918 -24.604 1.00 102.59 ? 61  ASP   A CB  1 
ATOM   254  C  CG  . ASP   A 1 41  ? -15.856 -39.336 -23.198 1.00 103.65 ? 61  ASP   A CG  1 
ATOM   255  O  OD1 . ASP   A 1 41  ? -15.429 -40.496 -23.018 1.00 98.37  ? 61  ASP   A OD1 1 
ATOM   256  O  OD2 . ASP   A 1 41  ? -15.976 -38.505 -22.274 1.00 99.42  ? 61  ASP   A OD2 1 
ATOM   257  N  N   . MET   A 1 42  ? -15.573 -38.238 -27.668 1.00 111.22 ? 62  MET   A N   1 
ATOM   258  C  CA  A MET   A 1 42  ? -16.019 -37.899 -29.017 0.44 116.16 ? 62  MET   A CA  1 
ATOM   259  C  CA  B MET   A 1 42  ? -16.032 -37.907 -29.013 0.56 117.96 ? 62  MET   A CA  1 
ATOM   260  C  C   . MET   A 1 42  ? -15.664 -39.002 -30.005 1.00 115.32 ? 62  MET   A C   1 
ATOM   261  O  O   . MET   A 1 42  ? -16.476 -39.367 -30.864 1.00 123.50 ? 62  MET   A O   1 
ATOM   262  C  CB  A MET   A 1 42  ? -15.403 -36.569 -29.454 0.44 119.18 ? 62  MET   A CB  1 
ATOM   263  C  CB  B MET   A 1 42  ? -15.456 -36.562 -29.456 0.56 116.74 ? 62  MET   A CB  1 
ATOM   264  C  CG  A MET   A 1 42  ? -15.964 -35.348 -28.741 0.44 117.41 ? 62  MET   A CG  1 
ATOM   265  C  CG  B MET   A 1 42  ? -16.057 -35.364 -28.739 0.56 115.98 ? 62  MET   A CG  1 
ATOM   266  S  SD  A MET   A 1 42  ? -17.501 -34.756 -29.474 0.44 114.74 ? 62  MET   A SD  1 
ATOM   267  S  SD  B MET   A 1 42  ? -15.772 -33.819 -29.624 0.56 128.81 ? 62  MET   A SD  1 
ATOM   268  C  CE  A MET   A 1 42  ? -16.929 -34.245 -31.092 0.44 109.53 ? 62  MET   A CE  1 
ATOM   269  C  CE  B MET   A 1 42  ? -16.711 -34.112 -31.121 0.56 109.74 ? 62  MET   A CE  1 
ATOM   270  N  N   . GLU   A 1 43  ? -14.449 -39.543 -29.901 1.00 123.33 ? 63  GLU   A N   1 
ATOM   271  C  CA  . GLU   A 1 43  ? -14.050 -40.637 -30.779 1.00 121.01 ? 63  GLU   A CA  1 
ATOM   272  C  C   . GLU   A 1 43  ? -14.832 -41.904 -30.461 1.00 124.15 ? 63  GLU   A C   1 
ATOM   273  O  O   . GLU   A 1 43  ? -15.341 -42.576 -31.366 1.00 132.46 ? 63  GLU   A O   1 
ATOM   274  C  CB  . GLU   A 1 43  ? -12.547 -40.893 -30.659 1.00 122.83 ? 63  GLU   A CB  1 
ATOM   275  C  CG  . GLU   A 1 43  ? -11.669 -39.768 -31.178 1.00 131.32 ? 63  GLU   A CG  1 
ATOM   276  C  CD  . GLU   A 1 43  ? -10.193 -40.087 -31.051 1.00 165.52 ? 63  GLU   A CD  1 
ATOM   277  O  OE1 . GLU   A 1 43  ? -9.864  -41.223 -30.647 1.00 172.45 ? 63  GLU   A OE1 1 
ATOM   278  O  OE2 . GLU   A 1 43  ? -9.361  -39.205 -31.352 1.00 166.88 ? 63  GLU   A OE2 1 
ATOM   279  N  N   . CYS   A 1 44  ? -14.936 -42.247 -29.173 1.00 125.81 ? 64  CYS   A N   1 
ATOM   280  C  CA  . CYS   A 1 44  ? -15.690 -43.433 -28.777 1.00 119.29 ? 64  CYS   A CA  1 
ATOM   281  C  C   . CYS   A 1 44  ? -17.145 -43.335 -29.212 1.00 116.65 ? 64  CYS   A C   1 
ATOM   282  O  O   . CYS   A 1 44  ? -17.745 -44.333 -29.629 1.00 121.05 ? 64  CYS   A O   1 
ATOM   283  C  CB  . CYS   A 1 44  ? -15.598 -43.634 -27.265 1.00 122.28 ? 64  CYS   A CB  1 
ATOM   284  S  SG  . CYS   A 1 44  ? -14.048 -44.362 -26.707 1.00 120.39 ? 64  CYS   A SG  1 
ATOM   285  N  N   . HIS   A 1 45  ? -17.732 -42.139 -29.119 1.00 124.04 ? 65  HIS   A N   1 
ATOM   286  C  CA  . HIS   A 1 45  ? -19.101 -41.952 -29.585 1.00 125.93 ? 65  HIS   A CA  1 
ATOM   287  C  C   . HIS   A 1 45  ? -19.218 -42.204 -31.081 1.00 125.99 ? 65  HIS   A C   1 
ATOM   288  O  O   . HIS   A 1 45  ? -20.255 -42.685 -31.551 1.00 127.55 ? 65  HIS   A O   1 
ATOM   289  C  CB  . HIS   A 1 45  ? -19.585 -40.544 -29.239 1.00 127.26 ? 65  HIS   A CB  1 
ATOM   290  C  CG  . HIS   A 1 45  ? -20.964 -40.240 -29.732 1.00 127.10 ? 65  HIS   A CG  1 
ATOM   291  N  ND1 . HIS   A 1 45  ? -21.993 -41.155 -29.675 1.00 129.38 ? 65  HIS   A ND1 1 
ATOM   292  C  CD2 . HIS   A 1 45  ? -21.486 -39.121 -30.289 1.00 129.46 ? 65  HIS   A CD2 1 
ATOM   293  C  CE1 . HIS   A 1 45  ? -23.089 -40.614 -30.178 1.00 134.51 ? 65  HIS   A CE1 1 
ATOM   294  N  NE2 . HIS   A 1 45  ? -22.808 -39.380 -30.557 1.00 138.02 ? 65  HIS   A NE2 1 
ATOM   295  N  N   . LYS   A 1 46  ? -18.166 -41.897 -31.841 1.00 122.71 ? 66  LYS   A N   1 
ATOM   296  C  CA  . LYS   A 1 46  ? -18.185 -42.146 -33.277 1.00 125.73 ? 66  LYS   A CA  1 
ATOM   297  C  C   . LYS   A 1 46  ? -17.766 -43.571 -33.614 1.00 135.11 ? 66  LYS   A C   1 
ATOM   298  O  O   . LYS   A 1 46  ? -18.175 -44.104 -34.651 1.00 146.62 ? 66  LYS   A O   1 
ATOM   299  C  CB  . LYS   A 1 46  ? -17.270 -41.152 -33.993 1.00 128.53 ? 66  LYS   A CB  1 
ATOM   300  C  CG  . LYS   A 1 46  ? -17.594 -40.957 -35.465 1.00 136.14 ? 66  LYS   A CG  1 
ATOM   301  C  CD  . LYS   A 1 46  ? -16.428 -40.331 -36.213 1.00 147.06 ? 66  LYS   A CD  1 
ATOM   302  C  CE  . LYS   A 1 46  ? -15.511 -41.397 -36.790 1.00 156.45 ? 66  LYS   A CE  1 
ATOM   303  N  NZ  . LYS   A 1 46  ? -16.218 -42.234 -37.801 1.00 173.43 ? 66  LYS   A NZ  1 
ATOM   304  N  N   . LYS   A 1 47  ? -16.963 -44.201 -32.754 1.00 134.11 ? 67  LYS   A N   1 
ATOM   305  C  CA  . LYS   A 1 47  ? -16.407 -45.511 -33.070 1.00 132.84 ? 67  LYS   A CA  1 
ATOM   306  C  C   . LYS   A 1 47  ? -17.402 -46.641 -32.837 1.00 130.58 ? 67  LYS   A C   1 
ATOM   307  O  O   . LYS   A 1 47  ? -17.380 -47.638 -33.568 1.00 137.91 ? 67  LYS   A O   1 
ATOM   308  C  CB  . LYS   A 1 47  ? -15.144 -45.756 -32.243 1.00 132.33 ? 67  LYS   A CB  1 
ATOM   309  C  CG  . LYS   A 1 47  ? -13.896 -46.014 -33.070 1.00 132.18 ? 67  LYS   A CG  1 
ATOM   310  C  CD  . LYS   A 1 47  ? -12.674 -46.222 -32.186 1.00 150.78 ? 67  LYS   A CD  1 
ATOM   311  C  CE  . LYS   A 1 47  ? -12.323 -44.961 -31.410 1.00 145.28 ? 67  LYS   A CE  1 
ATOM   312  N  NZ  . LYS   A 1 47  ? -11.069 -45.123 -30.621 1.00 124.13 ? 67  LYS   A NZ  1 
ATOM   313  N  N   . TYR   A 1 48  ? -18.276 -46.511 -31.838 1.00 130.62 ? 68  TYR   A N   1 
ATOM   314  C  CA  . TYR   A 1 48  ? -19.151 -47.609 -31.444 1.00 130.11 ? 68  TYR   A CA  1 
ATOM   315  C  C   . TYR   A 1 48  ? -20.634 -47.269 -31.436 1.00 130.69 ? 68  TYR   A C   1 
ATOM   316  O  O   . TYR   A 1 48  ? -21.451 -48.195 -31.498 1.00 118.57 ? 68  TYR   A O   1 
ATOM   317  C  CB  . TYR   A 1 48  ? -18.746 -48.131 -30.057 1.00 127.44 ? 68  TYR   A CB  1 
ATOM   318  C  CG  . TYR   A 1 48  ? -17.260 -48.381 -29.949 1.00 124.33 ? 68  TYR   A CG  1 
ATOM   319  C  CD1 . TYR   A 1 48  ? -16.685 -49.510 -30.515 1.00 128.82 ? 68  TYR   A CD1 1 
ATOM   320  C  CD2 . TYR   A 1 48  ? -16.428 -47.476 -29.303 1.00 132.29 ? 68  TYR   A CD2 1 
ATOM   321  C  CE1 . TYR   A 1 48  ? -15.326 -49.739 -30.430 1.00 128.77 ? 68  TYR   A CE1 1 
ATOM   322  C  CE2 . TYR   A 1 48  ? -15.066 -47.696 -29.213 1.00 128.61 ? 68  TYR   A CE2 1 
ATOM   323  C  CZ  . TYR   A 1 48  ? -14.522 -48.830 -29.779 1.00 127.23 ? 68  TYR   A CZ  1 
ATOM   324  O  OH  . TYR   A 1 48  ? -13.168 -49.061 -29.698 1.00 129.58 ? 68  TYR   A OH  1 
ATOM   325  N  N   . GLY   A 1 49  ? -21.016 -45.997 -31.362 1.00 134.28 ? 69  GLY   A N   1 
ATOM   326  C  CA  . GLY   A 1 49  ? -22.417 -45.644 -31.497 1.00 130.10 ? 69  GLY   A CA  1 
ATOM   327  C  C   . GLY   A 1 49  ? -23.114 -45.207 -30.224 1.00 123.50 ? 69  GLY   A C   1 
ATOM   328  O  O   . GLY   A 1 49  ? -22.612 -44.349 -29.491 1.00 120.71 ? 69  GLY   A O   1 
ATOM   329  N  N   . LYS   A 1 50  ? -24.280 -45.797 -29.954 1.00 124.44 ? 70  LYS   A N   1 
ATOM   330  C  CA  . LYS   A 1 50  ? -25.134 -45.317 -28.872 1.00 114.49 ? 70  LYS   A CA  1 
ATOM   331  C  C   . LYS   A 1 50  ? -24.631 -45.739 -27.497 1.00 105.02 ? 70  LYS   A C   1 
ATOM   332  O  O   . LYS   A 1 50  ? -24.891 -45.042 -26.510 1.00 99.73  ? 70  LYS   A O   1 
ATOM   333  C  CB  . LYS   A 1 50  ? -26.569 -45.811 -29.081 1.00 118.75 ? 70  LYS   A CB  1 
ATOM   334  C  CG  . LYS   A 1 50  ? -26.785 -47.274 -28.728 1.00 127.86 ? 70  LYS   A CG  1 
ATOM   335  C  CD  . LYS   A 1 50  ? -27.961 -47.871 -29.481 1.00 135.26 ? 70  LYS   A CD  1 
ATOM   336  C  CE  . LYS   A 1 50  ? -28.359 -49.214 -28.888 1.00 145.36 ? 70  LYS   A CE  1 
ATOM   337  N  NZ  . LYS   A 1 50  ? -27.182 -50.096 -28.651 1.00 145.52 ? 70  LYS   A NZ  1 
ATOM   338  N  N   . VAL   A 1 51  ? -23.915 -46.858 -27.407 1.00 115.13 ? 71  VAL   A N   1 
ATOM   339  C  CA  . VAL   A 1 51  ? -23.468 -47.395 -26.125 1.00 117.44 ? 71  VAL   A CA  1 
ATOM   340  C  C   . VAL   A 1 51  ? -22.108 -48.049 -26.319 1.00 121.07 ? 71  VAL   A C   1 
ATOM   341  O  O   . VAL   A 1 51  ? -21.916 -48.839 -27.248 1.00 110.36 ? 71  VAL   A O   1 
ATOM   342  C  CB  . VAL   A 1 51  ? -24.483 -48.403 -25.542 1.00 112.43 ? 71  VAL   A CB  1 
ATOM   343  C  CG1 . VAL   A 1 51  ? -23.802 -49.353 -24.567 1.00 110.09 ? 71  VAL   A CG1 1 
ATOM   344  C  CG2 . VAL   A 1 51  ? -25.623 -47.671 -24.851 1.00 114.32 ? 71  VAL   A CG2 1 
ATOM   345  N  N   . TRP   A 1 52  ? -21.162 -47.714 -25.443 1.00 114.36 ? 72  TRP   A N   1 
ATOM   346  C  CA  . TRP   A 1 52  ? -19.859 -48.359 -25.438 1.00 116.98 ? 72  TRP   A CA  1 
ATOM   347  C  C   . TRP   A 1 52  ? -19.371 -48.466 -24.000 1.00 109.58 ? 72  TRP   A C   1 
ATOM   348  O  O   . TRP   A 1 52  ? -19.984 -47.933 -23.071 1.00 112.27 ? 72  TRP   A O   1 
ATOM   349  C  CB  . TRP   A 1 52  ? -18.849 -47.603 -26.310 1.00 120.84 ? 72  TRP   A CB  1 
ATOM   350  C  CG  . TRP   A 1 52  ? -18.442 -46.269 -25.765 1.00 112.25 ? 72  TRP   A CG  1 
ATOM   351  C  CD1 . TRP   A 1 52  ? -17.372 -46.004 -24.961 1.00 117.46 ? 72  TRP   A CD1 1 
ATOM   352  C  CD2 . TRP   A 1 52  ? -19.094 -45.014 -25.993 1.00 103.68 ? 72  TRP   A CD2 1 
ATOM   353  N  NE1 . TRP   A 1 52  ? -17.320 -44.663 -24.670 1.00 117.51 ? 72  TRP   A NE1 1 
ATOM   354  C  CE2 . TRP   A 1 52  ? -18.364 -44.032 -25.294 1.00 105.94 ? 72  TRP   A CE2 1 
ATOM   355  C  CE3 . TRP   A 1 52  ? -20.223 -44.625 -26.719 1.00 111.16 ? 72  TRP   A CE3 1 
ATOM   356  C  CZ2 . TRP   A 1 52  ? -18.728 -42.687 -25.297 1.00 106.33 ? 72  TRP   A CZ2 1 
ATOM   357  C  CZ3 . TRP   A 1 52  ? -20.583 -43.289 -26.720 1.00 119.04 ? 72  TRP   A CZ3 1 
ATOM   358  C  CH2 . TRP   A 1 52  ? -19.837 -42.337 -26.015 1.00 118.66 ? 72  TRP   A CH2 1 
ATOM   359  N  N   . GLY   A 1 53  ? -18.252 -49.168 -23.824 1.00 98.33  ? 73  GLY   A N   1 
ATOM   360  C  CA  . GLY   A 1 53  ? -17.693 -49.371 -22.505 1.00 106.08 ? 73  GLY   A CA  1 
ATOM   361  C  C   . GLY   A 1 53  ? -16.179 -49.323 -22.538 1.00 103.20 ? 73  GLY   A C   1 
ATOM   362  O  O   . GLY   A 1 53  ? -15.547 -49.520 -23.579 1.00 115.46 ? 73  GLY   A O   1 
ATOM   363  N  N   . PHE   A 1 54  ? -15.606 -49.056 -21.369 1.00 101.12 ? 74  PHE   A N   1 
ATOM   364  C  CA  . PHE   A 1 54  ? -14.159 -49.007 -21.201 1.00 96.77  ? 74  PHE   A CA  1 
ATOM   365  C  C   . PHE   A 1 54  ? -13.847 -49.234 -19.726 1.00 97.15  ? 74  PHE   A C   1 
ATOM   366  O  O   . PHE   A 1 54  ? -14.742 -49.491 -18.916 1.00 96.25  ? 74  PHE   A O   1 
ATOM   367  C  CB  . PHE   A 1 54  ? -13.584 -47.685 -21.718 1.00 90.67  ? 74  PHE   A CB  1 
ATOM   368  C  CG  . PHE   A 1 54  ? -14.177 -46.467 -21.073 1.00 99.28  ? 74  PHE   A CG  1 
ATOM   369  C  CD1 . PHE   A 1 54  ? -15.371 -45.934 -21.531 1.00 95.71  ? 74  PHE   A CD1 1 
ATOM   370  C  CD2 . PHE   A 1 54  ? -13.535 -45.845 -20.015 1.00 96.99  ? 74  PHE   A CD2 1 
ATOM   371  C  CE1 . PHE   A 1 54  ? -15.917 -44.811 -20.943 1.00 99.44  ? 74  PHE   A CE1 1 
ATOM   372  C  CE2 . PHE   A 1 54  ? -14.077 -44.720 -19.423 1.00 112.08 ? 74  PHE   A CE2 1 
ATOM   373  C  CZ  . PHE   A 1 54  ? -15.268 -44.202 -19.889 1.00 96.86  ? 74  PHE   A CZ  1 
ATOM   374  N  N   . TYR   A 1 55  ? -12.565 -49.138 -19.380 1.00 104.10 ? 75  TYR   A N   1 
ATOM   375  C  CA  . TYR   A 1 55  ? -12.100 -49.488 -18.040 1.00 95.57  ? 75  TYR   A CA  1 
ATOM   376  C  C   . TYR   A 1 55  ? -11.153 -48.408 -17.540 1.00 94.19  ? 75  TYR   A C   1 
ATOM   377  O  O   . TYR   A 1 55  ? -10.040 -48.265 -18.057 1.00 101.90 ? 75  TYR   A O   1 
ATOM   378  C  CB  . TYR   A 1 55  ? -11.414 -50.855 -18.038 1.00 99.63  ? 75  TYR   A CB  1 
ATOM   379  C  CG  . TYR   A 1 55  ? -12.315 -51.988 -18.470 1.00 97.33  ? 75  TYR   A CG  1 
ATOM   380  C  CD1 . TYR   A 1 55  ? -12.477 -52.300 -19.815 1.00 95.77  ? 75  TYR   A CD1 1 
ATOM   381  C  CD2 . TYR   A 1 55  ? -13.004 -52.747 -17.535 1.00 93.42  ? 75  TYR   A CD2 1 
ATOM   382  C  CE1 . TYR   A 1 55  ? -13.302 -53.336 -20.214 1.00 97.53  ? 75  TYR   A CE1 1 
ATOM   383  C  CE2 . TYR   A 1 55  ? -13.829 -53.784 -17.923 1.00 105.07 ? 75  TYR   A CE2 1 
ATOM   384  C  CZ  . TYR   A 1 55  ? -13.975 -54.075 -19.263 1.00 108.97 ? 75  TYR   A CZ  1 
ATOM   385  O  OH  . TYR   A 1 55  ? -14.797 -55.108 -19.652 1.00 104.60 ? 75  TYR   A OH  1 
ATOM   386  N  N   . ASP   A 1 56  ? -11.594 -47.648 -16.540 1.00 104.61 ? 76  ASP   A N   1 
ATOM   387  C  CA  . ASP   A 1 56  ? -10.724 -46.715 -15.827 1.00 97.27  ? 76  ASP   A CA  1 
ATOM   388  C  C   . ASP   A 1 56  ? -9.916  -47.529 -14.825 1.00 103.77 ? 76  ASP   A C   1 
ATOM   389  O  O   . ASP   A 1 56  ? -10.332 -47.752 -13.687 1.00 102.37 ? 76  ASP   A O   1 
ATOM   390  C  CB  . ASP   A 1 56  ? -11.542 -45.624 -15.147 1.00 105.03 ? 76  ASP   A CB  1 
ATOM   391  C  CG  . ASP   A 1 56  ? -12.082 -44.603 -16.128 1.00 108.79 ? 76  ASP   A CG  1 
ATOM   392  O  OD1 . ASP   A 1 56  ? -11.749 -44.697 -17.328 1.00 111.52 ? 76  ASP   A OD1 1 
ATOM   393  O  OD2 . ASP   A 1 56  ? -12.837 -43.706 -15.699 1.00 105.79 ? 76  ASP   A OD2 1 
ATOM   394  N  N   . GLY   A 1 57  ? -8.744  -47.987 -15.257 1.00 117.75 ? 77  GLY   A N   1 
ATOM   395  C  CA  . GLY   A 1 57  ? -7.971  -48.925 -14.467 1.00 116.01 ? 77  GLY   A CA  1 
ATOM   396  C  C   . GLY   A 1 57  ? -8.618  -50.293 -14.478 1.00 106.38 ? 77  GLY   A C   1 
ATOM   397  O  O   . GLY   A 1 57  ? -8.648  -50.963 -15.514 1.00 112.74 ? 77  GLY   A O   1 
ATOM   398  N  N   . GLN   A 1 58  ? -9.145  -50.718 -13.332 1.00 104.56 ? 78  GLN   A N   1 
ATOM   399  C  CA  . GLN   A 1 58  ? -9.963  -51.920 -13.244 1.00 107.80 ? 78  GLN   A CA  1 
ATOM   400  C  C   . GLN   A 1 58  ? -11.447 -51.604 -13.126 1.00 107.89 ? 78  GLN   A C   1 
ATOM   401  O  O   . GLN   A 1 58  ? -12.259 -52.528 -13.015 1.00 110.63 ? 78  GLN   A O   1 
ATOM   402  C  CB  . GLN   A 1 58  ? -9.523  -52.777 -12.052 1.00 124.45 ? 78  GLN   A CB  1 
ATOM   403  C  CG  . GLN   A 1 58  ? -8.204  -53.503 -12.259 1.00 147.69 ? 78  GLN   A CG  1 
ATOM   404  C  CD  . GLN   A 1 58  ? -8.315  -54.640 -13.256 1.00 143.45 ? 78  GLN   A CD  1 
ATOM   405  O  OE1 . GLN   A 1 58  ? -9.405  -55.150 -13.515 1.00 144.51 ? 78  GLN   A OE1 1 
ATOM   406  N  NE2 . GLN   A 1 58  ? -7.183  -55.042 -13.823 1.00 145.29 ? 78  GLN   A NE2 1 
ATOM   407  N  N   . GLN   A 1 59  ? -11.817 -50.324 -13.156 1.00 112.16 ? 79  GLN   A N   1 
ATOM   408  C  CA  . GLN   A 1 59  ? -13.201 -49.911 -12.965 1.00 90.55  ? 79  GLN   A CA  1 
ATOM   409  C  C   . GLN   A 1 59  ? -13.934 -49.912 -14.299 1.00 93.93  ? 79  GLN   A C   1 
ATOM   410  O  O   . GLN   A 1 59  ? -13.586 -49.117 -15.183 1.00 92.81  ? 79  GLN   A O   1 
ATOM   411  C  CB  . GLN   A 1 59  ? -13.261 -48.526 -12.342 1.00 98.71  ? 79  GLN   A CB  1 
ATOM   412  C  CG  . GLN   A 1 59  ? -14.644 -47.897 -12.354 1.00 105.76 ? 79  GLN   A CG  1 
ATOM   413  C  CD  . GLN   A 1 59  ? -15.632 -48.642 -11.481 1.00 106.66 ? 79  GLN   A CD  1 
ATOM   414  O  OE1 . GLN   A 1 59  ? -15.400 -48.834 -10.287 1.00 85.43  ? 79  GLN   A OE1 1 
ATOM   415  N  NE2 . GLN   A 1 59  ? -16.741 -49.070 -12.073 1.00 95.60  ? 79  GLN   A NE2 1 
ATOM   416  N  N   . PRO   A 1 60  ? -14.936 -50.769 -14.494 1.00 86.38  ? 80  PRO   A N   1 
ATOM   417  C  CA  . PRO   A 1 60  ? -15.698 -50.736 -15.749 1.00 92.58  ? 80  PRO   A CA  1 
ATOM   418  C  C   . PRO   A 1 60  ? -16.628 -49.532 -15.788 1.00 102.84 ? 80  PRO   A C   1 
ATOM   419  O  O   . PRO   A 1 60  ? -17.363 -49.265 -14.834 1.00 100.04 ? 80  PRO   A O   1 
ATOM   420  C  CB  . PRO   A 1 60  ? -16.479 -52.055 -15.724 1.00 87.69  ? 80  PRO   A CB  1 
ATOM   421  C  CG  . PRO   A 1 60  ? -16.642 -52.352 -14.269 1.00 103.23 ? 80  PRO   A CG  1 
ATOM   422  C  CD  . PRO   A 1 60  ? -15.395 -51.841 -13.593 1.00 101.62 ? 80  PRO   A CD  1 
ATOM   423  N  N   . VAL   A 1 61  ? -16.586 -48.802 -16.899 1.00 93.38  ? 81  VAL   A N   1 
ATOM   424  C  CA  . VAL   A 1 61  ? -17.410 -47.616 -17.099 1.00 90.92  ? 81  VAL   A CA  1 
ATOM   425  C  C   . VAL   A 1 61  ? -18.225 -47.808 -18.369 1.00 97.64  ? 81  VAL   A C   1 
ATOM   426  O  O   . VAL   A 1 61  ? -17.666 -48.083 -19.437 1.00 108.44 ? 81  VAL   A O   1 
ATOM   427  C  CB  . VAL   A 1 61  ? -16.560 -46.336 -17.186 1.00 94.17  ? 81  VAL   A CB  1 
ATOM   428  C  CG1 . VAL   A 1 61  ? -17.458 -45.113 -17.284 1.00 95.59  ? 81  VAL   A CG1 1 
ATOM   429  C  CG2 . VAL   A 1 61  ? -15.631 -46.229 -15.986 1.00 94.59  ? 81  VAL   A CG2 1 
ATOM   430  N  N   . LEU   A 1 62  ? -19.542 -47.663 -18.251 1.00 99.67  ? 82  LEU   A N   1 
ATOM   431  C  CA  . LEU   A 1 62  ? -20.459 -47.777 -19.376 1.00 106.59 ? 82  LEU   A CA  1 
ATOM   432  C  C   . LEU   A 1 62  ? -20.945 -46.388 -19.767 1.00 104.97 ? 82  LEU   A C   1 
ATOM   433  O  O   . LEU   A 1 62  ? -21.418 -45.629 -18.915 1.00 95.91  ? 82  LEU   A O   1 
ATOM   434  C  CB  . LEU   A 1 62  ? -21.648 -48.675 -19.028 1.00 96.08  ? 82  LEU   A CB  1 
ATOM   435  C  CG  . LEU   A 1 62  ? -22.667 -48.910 -20.145 1.00 86.02  ? 82  LEU   A CG  1 
ATOM   436  C  CD1 . LEU   A 1 62  ? -22.061 -49.754 -21.254 1.00 102.20 ? 82  LEU   A CD1 1 
ATOM   437  C  CD2 . LEU   A 1 62  ? -23.932 -49.555 -19.600 1.00 96.92  ? 82  LEU   A CD2 1 
ATOM   438  N  N   . ALA   A 1 63  ? -20.829 -46.063 -21.050 1.00 97.17  ? 83  ALA   A N   1 
ATOM   439  C  CA  . ALA   A 1 63  ? -21.206 -44.756 -21.572 1.00 96.74  ? 83  ALA   A CA  1 
ATOM   440  C  C   . ALA   A 1 63  ? -22.482 -44.891 -22.390 1.00 106.67 ? 83  ALA   A C   1 
ATOM   441  O  O   . ALA   A 1 63  ? -22.494 -45.574 -23.420 1.00 114.72 ? 83  ALA   A O   1 
ATOM   442  C  CB  . ALA   A 1 63  ? -20.084 -44.164 -22.422 1.00 98.09  ? 83  ALA   A CB  1 
ATOM   443  N  N   . ILE   A 1 64  ? -23.548 -44.236 -21.936 1.00 107.16 ? 84  ILE   A N   1 
ATOM   444  C  CA  . ILE   A 1 64  ? -24.838 -44.258 -22.612 1.00 106.34 ? 84  ILE   A CA  1 
ATOM   445  C  C   . ILE   A 1 64  ? -25.071 -42.902 -23.264 1.00 96.63  ? 84  ILE   A C   1 
ATOM   446  O  O   . ILE   A 1 64  ? -24.668 -41.863 -22.728 1.00 103.13 ? 84  ILE   A O   1 
ATOM   447  C  CB  . ILE   A 1 64  ? -25.984 -44.608 -21.641 1.00 116.37 ? 84  ILE   A CB  1 
ATOM   448  C  CG1 . ILE   A 1 64  ? -26.120 -43.539 -20.556 1.00 108.82 ? 84  ILE   A CG1 1 
ATOM   449  C  CG2 . ILE   A 1 64  ? -25.746 -45.970 -21.009 1.00 104.95 ? 84  ILE   A CG2 1 
ATOM   450  C  CD1 . ILE   A 1 64  ? -27.343 -43.711 -19.685 1.00 96.93  ? 84  ILE   A CD1 1 
ATOM   451  N  N   . THR   A 1 65  ? -25.709 -42.918 -24.438 1.00 101.24 ? 85  THR   A N   1 
ATOM   452  C  CA  . THR   A 1 65  ? -26.055 -41.693 -25.149 1.00 107.89 ? 85  THR   A CA  1 
ATOM   453  C  C   . THR   A 1 65  ? -27.523 -41.660 -25.560 1.00 121.13 ? 85  THR   A C   1 
ATOM   454  O  O   . THR   A 1 65  ? -27.915 -40.785 -26.340 1.00 120.95 ? 85  THR   A O   1 
ATOM   455  C  CB  . THR   A 1 65  ? -25.175 -41.510 -26.393 1.00 113.75 ? 85  THR   A CB  1 
ATOM   456  O  OG1 . THR   A 1 65  ? -25.444 -42.558 -27.330 1.00 112.87 ? 85  THR   A OG1 1 
ATOM   457  C  CG2 . THR   A 1 65  ? -23.698 -41.534 -26.022 1.00 106.29 ? 85  THR   A CG2 1 
ATOM   458  N  N   . ASP   A 1 66  ? -28.340 -42.587 -25.063 1.00 128.97 ? 86  ASP   A N   1 
ATOM   459  C  CA  . ASP   A 1 66  ? -29.750 -42.637 -25.423 1.00 130.25 ? 86  ASP   A CA  1 
ATOM   460  C  C   . ASP   A 1 66  ? -30.543 -41.722 -24.501 1.00 129.24 ? 86  ASP   A C   1 
ATOM   461  O  O   . ASP   A 1 66  ? -30.491 -41.904 -23.277 1.00 127.64 ? 86  ASP   A O   1 
ATOM   462  C  CB  . ASP   A 1 66  ? -30.275 -44.059 -25.330 1.00 137.70 ? 86  ASP   A CB  1 
ATOM   463  C  CG  . ASP   A 1 66  ? -31.702 -44.189 -25.819 1.00 146.32 ? 86  ASP   A CG  1 
ATOM   464  O  OD1 . ASP   A 1 66  ? -31.916 -44.138 -27.048 1.00 158.11 ? 86  ASP   A OD1 1 
ATOM   465  O  OD2 . ASP   A 1 66  ? -32.610 -44.343 -24.975 1.00 146.73 ? 86  ASP   A OD2 1 
ATOM   466  N  N   . PRO   A 1 67  ? -31.279 -40.738 -25.031 1.00 124.26 ? 87  PRO   A N   1 
ATOM   467  C  CA  . PRO   A 1 67  ? -31.990 -39.797 -24.144 1.00 118.66 ? 87  PRO   A CA  1 
ATOM   468  C  C   . PRO   A 1 67  ? -32.959 -40.471 -23.189 1.00 121.14 ? 87  PRO   A C   1 
ATOM   469  O  O   . PRO   A 1 67  ? -33.061 -40.060 -22.027 1.00 114.89 ? 87  PRO   A O   1 
ATOM   470  C  CB  . PRO   A 1 67  ? -32.714 -38.872 -25.133 1.00 123.23 ? 87  PRO   A CB  1 
ATOM   471  C  CG  . PRO   A 1 67  ? -31.919 -38.965 -26.393 1.00 127.79 ? 87  PRO   A CG  1 
ATOM   472  C  CD  . PRO   A 1 67  ? -31.417 -40.377 -26.451 1.00 115.80 ? 87  PRO   A CD  1 
ATOM   473  N  N   . ASP   A 1 68  ? -33.682 -41.495 -23.648 1.00 113.76 ? 88  ASP   A N   1 
ATOM   474  C  CA  . ASP   A 1 68  ? -34.548 -42.247 -22.745 1.00 123.88 ? 88  ASP   A CA  1 
ATOM   475  C  C   . ASP   A 1 68  ? -33.730 -43.004 -21.707 1.00 115.93 ? 88  ASP   A C   1 
ATOM   476  O  O   . ASP   A 1 68  ? -34.110 -43.068 -20.532 1.00 112.99 ? 88  ASP   A O   1 
ATOM   477  C  CB  . ASP   A 1 68  ? -35.431 -43.208 -23.540 1.00 140.94 ? 88  ASP   A CB  1 
ATOM   478  C  CG  . ASP   A 1 68  ? -36.586 -42.506 -24.225 1.00 141.38 ? 88  ASP   A CG  1 
ATOM   479  O  OD1 . ASP   A 1 68  ? -37.288 -41.721 -23.553 1.00 134.29 ? 88  ASP   A OD1 1 
ATOM   480  O  OD2 . ASP   A 1 68  ? -36.790 -42.736 -25.436 1.00 135.28 ? 88  ASP   A OD2 1 
ATOM   481  N  N   . MET   A 1 69  ? -32.601 -43.582 -22.124 1.00 119.40 ? 89  MET   A N   1 
ATOM   482  C  CA  . MET   A 1 69  ? -31.738 -44.289 -21.184 1.00 112.68 ? 89  MET   A CA  1 
ATOM   483  C  C   . MET   A 1 69  ? -31.085 -43.321 -20.204 1.00 105.97 ? 89  MET   A C   1 
ATOM   484  O  O   . MET   A 1 69  ? -30.884 -43.657 -19.031 1.00 102.02 ? 89  MET   A O   1 
ATOM   485  C  CB  . MET   A 1 69  ? -30.682 -45.083 -21.951 1.00 116.76 ? 89  MET   A CB  1 
ATOM   486  C  CG  . MET   A 1 69  ? -30.143 -46.294 -21.216 1.00 112.78 ? 89  MET   A CG  1 
ATOM   487  S  SD  . MET   A 1 69  ? -29.066 -47.298 -22.257 1.00 121.61 ? 89  MET   A SD  1 
ATOM   488  C  CE  . MET   A 1 69  ? -30.175 -47.697 -23.607 1.00 131.18 ? 89  MET   A CE  1 
ATOM   489  N  N   . ILE   A 1 70  ? -30.751 -42.114 -20.666 1.00 98.82  ? 90  ILE   A N   1 
ATOM   490  C  CA  . ILE   A 1 70  ? -30.188 -41.103 -19.776 1.00 113.67 ? 90  ILE   A CA  1 
ATOM   491  C  C   . ILE   A 1 70  ? -31.244 -40.615 -18.793 1.00 110.56 ? 90  ILE   A C   1 
ATOM   492  O  O   . ILE   A 1 70  ? -30.990 -40.502 -17.588 1.00 96.48  ? 90  ILE   A O   1 
ATOM   493  C  CB  . ILE   A 1 70  ? -29.597 -39.938 -20.591 1.00 111.33 ? 90  ILE   A CB  1 
ATOM   494  C  CG1 . ILE   A 1 70  ? -28.413 -40.418 -21.434 1.00 105.72 ? 90  ILE   A CG1 1 
ATOM   495  C  CG2 . ILE   A 1 70  ? -29.178 -38.802 -19.671 1.00 92.61  ? 90  ILE   A CG2 1 
ATOM   496  C  CD1 . ILE   A 1 70  ? -27.871 -39.368 -22.379 1.00 97.44  ? 90  ILE   A CD1 1 
ATOM   497  N  N   . LYS   A 1 71  ? -32.446 -40.315 -19.296 1.00 114.69 ? 91  LYS   A N   1 
ATOM   498  C  CA  . LYS   A 1 71  ? -33.542 -39.911 -18.420 1.00 108.87 ? 91  LYS   A CA  1 
ATOM   499  C  C   . LYS   A 1 71  ? -33.864 -40.991 -17.397 1.00 101.42 ? 91  LYS   A C   1 
ATOM   500  O  O   . LYS   A 1 71  ? -34.259 -40.681 -16.267 1.00 97.80  ? 91  LYS   A O   1 
ATOM   501  C  CB  . LYS   A 1 71  ? -34.782 -39.581 -19.253 1.00 116.85 ? 91  LYS   A CB  1 
ATOM   502  C  CG  . LYS   A 1 71  ? -36.001 -39.185 -18.435 1.00 123.47 ? 91  LYS   A CG  1 
ATOM   503  C  CD  . LYS   A 1 71  ? -37.256 -39.148 -19.292 1.00 129.85 ? 91  LYS   A CD  1 
ATOM   504  C  CE  . LYS   A 1 71  ? -38.473 -38.757 -18.470 1.00 139.18 ? 91  LYS   A CE  1 
ATOM   505  N  NZ  . LYS   A 1 71  ? -39.743 -39.102 -19.168 1.00 157.30 ? 91  LYS   A NZ  1 
ATOM   506  N  N   . THR   A 1 72  ? -33.694 -42.261 -17.769 1.00 99.26  ? 92  THR   A N   1 
ATOM   507  C  CA  . THR   A 1 72  ? -33.943 -43.350 -16.831 1.00 101.03 ? 92  THR   A CA  1 
ATOM   508  C  C   . THR   A 1 72  ? -32.921 -43.350 -15.699 1.00 119.78 ? 92  THR   A C   1 
ATOM   509  O  O   . THR   A 1 72  ? -33.274 -43.574 -14.536 1.00 123.53 ? 92  THR   A O   1 
ATOM   510  C  CB  . THR   A 1 72  ? -33.925 -44.690 -17.568 1.00 104.02 ? 92  THR   A CB  1 
ATOM   511  O  OG1 . THR   A 1 72  ? -34.873 -44.660 -18.643 1.00 127.38 ? 92  THR   A OG1 1 
ATOM   512  C  CG2 . THR   A 1 72  ? -34.277 -45.826 -16.621 1.00 91.99  ? 92  THR   A CG2 1 
ATOM   513  N  N   . VAL   A 1 73  ? -31.652 -43.092 -16.019 1.00 105.29 ? 93  VAL   A N   1 
ATOM   514  C  CA  . VAL   A 1 73  ? -30.597 -43.144 -15.010 1.00 94.13  ? 93  VAL   A CA  1 
ATOM   515  C  C   . VAL   A 1 73  ? -30.624 -41.901 -14.129 1.00 99.16  ? 93  VAL   A C   1 
ATOM   516  O  O   . VAL   A 1 73  ? -30.613 -41.996 -12.897 1.00 102.37 ? 93  VAL   A O   1 
ATOM   517  C  CB  . VAL   A 1 73  ? -29.223 -43.326 -15.683 1.00 107.69 ? 93  VAL   A CB  1 
ATOM   518  C  CG1 . VAL   A 1 73  ? -28.107 -43.169 -14.663 1.00 92.02  ? 93  VAL   A CG1 1 
ATOM   519  C  CG2 . VAL   A 1 73  ? -29.138 -44.683 -16.355 1.00 105.34 ? 93  VAL   A CG2 1 
ATOM   520  N  N   . LEU   A 1 74  ? -30.657 -40.717 -14.743 1.00 92.07  ? 94  LEU   A N   1 
ATOM   521  C  CA  . LEU   A 1 74  ? -30.553 -39.484 -13.971 1.00 97.69  ? 94  LEU   A CA  1 
ATOM   522  C  C   . LEU   A 1 74  ? -31.826 -39.187 -13.185 1.00 106.71 ? 94  LEU   A C   1 
ATOM   523  O  O   . LEU   A 1 74  ? -31.753 -38.608 -12.094 1.00 98.02  ? 94  LEU   A O   1 
ATOM   524  C  CB  . LEU   A 1 74  ? -30.228 -38.308 -14.894 1.00 94.73  ? 94  LEU   A CB  1 
ATOM   525  C  CG  . LEU   A 1 74  ? -28.866 -38.315 -15.588 1.00 91.44  ? 94  LEU   A CG  1 
ATOM   526  C  CD1 . LEU   A 1 74  ? -28.710 -37.075 -16.453 1.00 86.69  ? 94  LEU   A CD1 1 
ATOM   527  C  CD2 . LEU   A 1 74  ? -27.745 -38.402 -14.566 1.00 91.11  ? 94  LEU   A CD2 1 
ATOM   528  N  N   . VAL   A 1 75  ? -32.991 -39.573 -13.709 1.00 106.81 ? 95  VAL   A N   1 
ATOM   529  C  CA  . VAL   A 1 75  ? -34.271 -39.164 -13.136 1.00 124.99 ? 95  VAL   A CA  1 
ATOM   530  C  C   . VAL   A 1 75  ? -35.067 -40.364 -12.632 1.00 112.51 ? 95  VAL   A C   1 
ATOM   531  O  O   . VAL   A 1 75  ? -35.366 -40.461 -11.437 1.00 108.40 ? 95  VAL   A O   1 
ATOM   532  C  CB  . VAL   A 1 75  ? -35.098 -38.362 -14.158 1.00 116.65 ? 95  VAL   A CB  1 
ATOM   533  C  CG1 . VAL   A 1 75  ? -36.404 -37.891 -13.531 1.00 105.42 ? 95  VAL   A CG1 1 
ATOM   534  C  CG2 . VAL   A 1 75  ? -34.293 -37.181 -14.687 1.00 118.45 ? 95  VAL   A CG2 1 
ATOM   535  N  N   . LYS   A 1 76  ? -35.420 -41.283 -13.535 1.00 111.65 ? 96  LYS   A N   1 
ATOM   536  C  CA  . LYS   A 1 76  ? -36.394 -42.318 -13.197 1.00 113.95 ? 96  LYS   A CA  1 
ATOM   537  C  C   . LYS   A 1 76  ? -35.870 -43.260 -12.119 1.00 117.20 ? 96  LYS   A C   1 
ATOM   538  O  O   . LYS   A 1 76  ? -36.601 -43.616 -11.187 1.00 115.10 ? 96  LYS   A O   1 
ATOM   539  C  CB  . LYS   A 1 76  ? -36.783 -43.100 -14.449 1.00 118.58 ? 96  LYS   A CB  1 
ATOM   540  C  CG  . LYS   A 1 76  ? -37.508 -42.271 -15.498 1.00 107.34 ? 96  LYS   A CG  1 
ATOM   541  C  CD  . LYS   A 1 76  ? -37.725 -43.062 -16.779 1.00 117.42 ? 96  LYS   A CD  1 
ATOM   542  C  CE  . LYS   A 1 76  ? -38.536 -42.265 -17.786 1.00 150.56 ? 96  LYS   A CE  1 
ATOM   543  N  NZ  . LYS   A 1 76  ? -38.634 -42.958 -19.099 1.00 161.98 ? 96  LYS   A NZ  1 
ATOM   544  N  N   . GLU   A 1 77  ? -34.613 -43.683 -12.229 1.00 129.47 ? 97  GLU   A N   1 
ATOM   545  C  CA  . GLU   A 1 77  ? -34.078 -44.660 -11.290 1.00 121.93 ? 97  GLU   A CA  1 
ATOM   546  C  C   . GLU   A 1 77  ? -32.925 -44.076 -10.484 1.00 115.04 ? 97  GLU   A C   1 
ATOM   547  O  O   . GLU   A 1 77  ? -31.885 -44.720 -10.317 1.00 117.63 ? 97  GLU   A O   1 
ATOM   548  C  CB  . GLU   A 1 77  ? -33.627 -45.921 -12.035 1.00 119.15 ? 97  GLU   A CB  1 
ATOM   549  C  CG  . GLU   A 1 77  ? -34.682 -46.491 -12.968 1.00 127.46 ? 97  GLU   A CG  1 
ATOM   550  C  CD  . GLU   A 1 77  ? -35.937 -46.917 -12.238 1.00 139.40 ? 97  GLU   A CD  1 
ATOM   551  O  OE1 . GLU   A 1 77  ? -35.820 -47.454 -11.115 1.00 142.55 ? 97  GLU   A OE1 1 
ATOM   552  O  OE2 . GLU   A 1 77  ? -37.041 -46.713 -12.784 1.00 146.21 ? 97  GLU   A OE2 1 
ATOM   553  N  N   . CYS   A 1 78  ? -33.105 -42.864 -9.963  1.00 111.34 ? 98  CYS   A N   1 
ATOM   554  C  CA  . CYS   A 1 78  ? -32.049 -42.214 -9.192  1.00 100.47 ? 98  CYS   A CA  1 
ATOM   555  C  C   . CYS   A 1 78  ? -32.058 -42.671 -7.738  1.00 112.70 ? 98  CYS   A C   1 
ATOM   556  O  O   . CYS   A 1 78  ? -31.048 -43.165 -7.225  1.00 112.77 ? 98  CYS   A O   1 
ATOM   557  C  CB  . CYS   A 1 78  ? -32.196 -40.692 -9.275  1.00 117.43 ? 98  CYS   A CB  1 
ATOM   558  S  SG  . CYS   A 1 78  ? -31.127 -39.778 -8.133  1.00 98.19  ? 98  CYS   A SG  1 
ATOM   559  N  N   . TYR   A 1 79  ? -33.194 -42.504 -7.056  1.00 127.84 ? 99  TYR   A N   1 
ATOM   560  C  CA  . TYR   A 1 79  ? -33.280 -42.849 -5.641  1.00 107.60 ? 99  TYR   A CA  1 
ATOM   561  C  C   . TYR   A 1 79  ? -33.066 -44.333 -5.382  1.00 113.06 ? 99  TYR   A C   1 
ATOM   562  O  O   . TYR   A 1 79  ? -32.780 -44.715 -4.243  1.00 124.40 ? 99  TYR   A O   1 
ATOM   563  C  CB  . TYR   A 1 79  ? -34.639 -42.426 -5.075  1.00 106.18 ? 99  TYR   A CB  1 
ATOM   564  C  CG  . TYR   A 1 79  ? -34.811 -40.934 -4.898  1.00 126.46 ? 99  TYR   A CG  1 
ATOM   565  C  CD1 . TYR   A 1 79  ? -34.193 -40.266 -3.850  1.00 127.32 ? 99  TYR   A CD1 1 
ATOM   566  C  CD2 . TYR   A 1 79  ? -35.603 -40.197 -5.768  1.00 122.91 ? 99  TYR   A CD2 1 
ATOM   567  C  CE1 . TYR   A 1 79  ? -34.349 -38.903 -3.679  1.00 125.63 ? 99  TYR   A CE1 1 
ATOM   568  C  CE2 . TYR   A 1 79  ? -35.766 -38.832 -5.604  1.00 129.91 ? 99  TYR   A CE2 1 
ATOM   569  C  CZ  . TYR   A 1 79  ? -35.136 -38.191 -4.558  1.00 141.21 ? 99  TYR   A CZ  1 
ATOM   570  O  OH  . TYR   A 1 79  ? -35.292 -36.834 -4.387  1.00 141.00 ? 99  TYR   A OH  1 
ATOM   571  N  N   . SER   A 1 80  ? -33.191 -45.176 -6.404  1.00 111.81 ? 100 SER   A N   1 
ATOM   572  C  CA  . SER   A 1 80  ? -33.144 -46.623 -6.227  1.00 121.18 ? 100 SER   A CA  1 
ATOM   573  C  C   . SER   A 1 80  ? -31.797 -47.226 -6.613  1.00 129.07 ? 100 SER   A C   1 
ATOM   574  O  O   . SER   A 1 80  ? -31.195 -47.955 -5.821  1.00 126.03 ? 100 SER   A O   1 
ATOM   575  C  CB  . SER   A 1 80  ? -34.265 -47.280 -7.042  1.00 122.43 ? 100 SER   A CB  1 
ATOM   576  O  OG  . SER   A 1 80  ? -34.181 -46.916 -8.411  1.00 123.29 ? 100 SER   A OG  1 
ATOM   577  N  N   . VAL   A 1 81  ? -31.305 -46.930 -7.818  1.00 124.69 ? 101 VAL   A N   1 
ATOM   578  C  CA  . VAL   A 1 81  ? -30.159 -47.620 -8.389  1.00 114.98 ? 101 VAL   A CA  1 
ATOM   579  C  C   . VAL   A 1 81  ? -28.966 -46.693 -8.578  1.00 108.39 ? 101 VAL   A C   1 
ATOM   580  O  O   . VAL   A 1 81  ? -27.829 -47.068 -8.271  1.00 112.78 ? 101 VAL   A O   1 
ATOM   581  C  CB  . VAL   A 1 81  ? -30.535 -48.296 -9.726  1.00 124.42 ? 101 VAL   A CB  1 
ATOM   582  C  CG1 . VAL   A 1 81  ? -29.380 -49.145 -10.245 1.00 112.95 ? 101 VAL   A CG1 1 
ATOM   583  C  CG2 . VAL   A 1 81  ? -31.793 -49.129 -9.560  1.00 107.28 ? 101 VAL   A CG2 1 
ATOM   584  N  N   . PHE   A 1 82  ? -29.190 -45.491 -9.097  1.00 104.69 ? 102 PHE   A N   1 
ATOM   585  C  CA  . PHE   A 1 82  ? -28.104 -44.577 -9.449  1.00 87.97  ? 102 PHE   A CA  1 
ATOM   586  C  C   . PHE   A 1 82  ? -28.170 -43.346 -8.550  1.00 104.73 ? 102 PHE   A C   1 
ATOM   587  O  O   . PHE   A 1 82  ? -28.451 -42.229 -8.995  1.00 115.88 ? 102 PHE   A O   1 
ATOM   588  C  CB  . PHE   A 1 82  ? -28.186 -44.203 -10.930 1.00 85.47  ? 102 PHE   A CB  1 
ATOM   589  C  CG  . PHE   A 1 82  ? -28.405 -45.379 -11.839 1.00 105.44 ? 102 PHE   A CG  1 
ATOM   590  C  CD1 . PHE   A 1 82  ? -27.350 -46.198 -12.208 1.00 106.35 ? 102 PHE   A CD1 1 
ATOM   591  C  CD2 . PHE   A 1 82  ? -29.670 -45.666 -12.326 1.00 114.79 ? 102 PHE   A CD2 1 
ATOM   592  C  CE1 . PHE   A 1 82  ? -27.554 -47.280 -13.046 1.00 109.73 ? 102 PHE   A CE1 1 
ATOM   593  C  CE2 . PHE   A 1 82  ? -29.880 -46.745 -13.163 1.00 114.75 ? 102 PHE   A CE2 1 
ATOM   594  C  CZ  . PHE   A 1 82  ? -28.821 -47.553 -13.524 1.00 105.89 ? 102 PHE   A CZ  1 
ATOM   595  N  N   . THR   A 1 83  ? -27.892 -43.558 -7.265  1.00 111.92 ? 103 THR   A N   1 
ATOM   596  C  CA  . THR   A 1 83  ? -27.941 -42.478 -6.289  1.00 100.26 ? 103 THR   A CA  1 
ATOM   597  C  C   . THR   A 1 83  ? -26.614 -41.740 -6.166  1.00 83.08  ? 103 THR   A C   1 
ATOM   598  O  O   . THR   A 1 83  ? -26.604 -40.518 -5.987  1.00 87.88  ? 103 THR   A O   1 
ATOM   599  C  CB  . THR   A 1 83  ? -28.350 -43.028 -4.920  1.00 109.07 ? 103 THR   A CB  1 
ATOM   600  O  OG1 . THR   A 1 83  ? -29.585 -43.746 -5.041  1.00 122.27 ? 103 THR   A OG1 1 
ATOM   601  C  CG2 . THR   A 1 83  ? -28.537 -41.892 -3.923  1.00 107.24 ? 103 THR   A CG2 1 
ATOM   602  N  N   . ASN   A 1 84  ? -25.493 -42.448 -6.272  1.00 97.55  ? 104 ASN   A N   1 
ATOM   603  C  CA  . ASN   A 1 84  ? -24.191 -41.888 -5.952  1.00 95.47  ? 104 ASN   A CA  1 
ATOM   604  C  C   . ASN   A 1 84  ? -23.292 -41.866 -7.182  1.00 93.65  ? 104 ASN   A C   1 
ATOM   605  O  O   . ASN   A 1 84  ? -23.487 -42.622 -8.139  1.00 104.82 ? 104 ASN   A O   1 
ATOM   606  C  CB  . ASN   A 1 84  ? -23.522 -42.684 -4.829  1.00 101.16 ? 104 ASN   A CB  1 
ATOM   607  C  CG  . ASN   A 1 84  ? -24.526 -43.246 -3.847  1.00 109.65 ? 104 ASN   A CG  1 
ATOM   608  O  OD1 . ASN   A 1 84  ? -25.167 -42.504 -3.105  1.00 113.96 ? 104 ASN   A OD1 1 
ATOM   609  N  ND2 . ASN   A 1 84  ? -24.677 -44.566 -3.846  1.00 112.70 ? 104 ASN   A ND2 1 
ATOM   610  N  N   . ARG   A 1 85  ? -22.296 -40.986 -7.138  1.00 84.79  ? 105 ARG   A N   1 
ATOM   611  C  CA  . ARG   A 1 85  ? -21.336 -40.839 -8.220  1.00 84.22  ? 105 ARG   A CA  1 
ATOM   612  C  C   . ARG   A 1 85  ? -20.154 -41.780 -7.989  1.00 105.38 ? 105 ARG   A C   1 
ATOM   613  O  O   . ARG   A 1 85  ? -20.153 -42.599 -7.065  1.00 101.89 ? 105 ARG   A O   1 
ATOM   614  C  CB  . ARG   A 1 85  ? -20.886 -39.384 -8.333  1.00 104.21 ? 105 ARG   A CB  1 
ATOM   615  C  CG  . ARG   A 1 85  ? -22.016 -38.392 -8.561  1.00 96.99  ? 105 ARG   A CG  1 
ATOM   616  C  CD  . ARG   A 1 85  ? -21.475 -36.982 -8.728  1.00 87.69  ? 105 ARG   A CD  1 
ATOM   617  N  NE  . ARG   A 1 85  ? -22.493 -36.048 -9.192  1.00 99.51  ? 105 ARG   A NE  1 
ATOM   618  C  CZ  . ARG   A 1 85  ? -23.139 -35.190 -8.414  1.00 93.48  ? 105 ARG   A CZ  1 
ATOM   619  N  NH1 . ARG   A 1 85  ? -22.892 -35.111 -7.117  1.00 108.04 ? 105 ARG   A NH1 1 
ATOM   620  N  NH2 . ARG   A 1 85  ? -24.053 -34.388 -8.952  1.00 78.94  ? 105 ARG   A NH2 1 
ATOM   621  N  N   . ARG   A 1 86  ? -19.132 -41.664 -8.830  1.00 109.28 ? 106 ARG   A N   1 
ATOM   622  C  CA  . ARG   A 1 86  ? -17.943 -42.492 -8.685  1.00 109.76 ? 106 ARG   A CA  1 
ATOM   623  C  C   . ARG   A 1 86  ? -17.251 -42.166 -7.365  1.00 116.84 ? 106 ARG   A C   1 
ATOM   624  O  O   . ARG   A 1 86  ? -17.098 -40.983 -7.028  1.00 130.23 ? 106 ARG   A O   1 
ATOM   625  C  CB  . ARG   A 1 86  ? -16.989 -42.259 -9.858  1.00 99.43  ? 106 ARG   A CB  1 
ATOM   626  C  CG  . ARG   A 1 86  ? -15.896 -43.307 -10.011 1.00 109.70 ? 106 ARG   A CG  1 
ATOM   627  C  CD  . ARG   A 1 86  ? -14.783 -42.813 -10.928 1.00 108.60 ? 106 ARG   A CD  1 
ATOM   628  N  NE  . ARG   A 1 86  ? -15.259 -42.503 -12.271 1.00 75.82  ? 106 ARG   A NE  1 
ATOM   629  C  CZ  . ARG   A 1 86  ? -14.892 -43.152 -13.368 1.00 89.78  ? 106 ARG   A CZ  1 
ATOM   630  N  NH1 . ARG   A 1 86  ? -14.027 -44.152 -13.322 1.00 110.88 ? 106 ARG   A NH1 1 
ATOM   631  N  NH2 . ARG   A 1 86  ? -15.400 -42.784 -14.541 1.00 82.43  ? 106 ARG   A NH2 1 
ATOM   632  N  N   . PRO   A 1 87  ? -16.838 -43.168 -6.587  1.00 118.04 ? 107 PRO   A N   1 
ATOM   633  C  CA  . PRO   A 1 87  ? -16.181 -42.880 -5.306  1.00 127.20 ? 107 PRO   A CA  1 
ATOM   634  C  C   . PRO   A 1 87  ? -14.898 -42.085 -5.504  1.00 136.37 ? 107 PRO   A C   1 
ATOM   635  O  O   . PRO   A 1 87  ? -14.136 -42.318 -6.444  1.00 131.98 ? 107 PRO   A O   1 
ATOM   636  C  CB  . PRO   A 1 87  ? -15.903 -44.272 -4.726  1.00 123.92 ? 107 PRO   A CB  1 
ATOM   637  C  CG  . PRO   A 1 87  ? -15.966 -45.202 -5.897  1.00 130.91 ? 107 PRO   A CG  1 
ATOM   638  C  CD  . PRO   A 1 87  ? -16.988 -44.613 -6.818  1.00 116.06 ? 107 PRO   A CD  1 
ATOM   639  N  N   . PHE   A 1 88  ? -14.670 -41.132 -4.602  1.00 142.10 ? 108 PHE   A N   1 
ATOM   640  C  CA  . PHE   A 1 88  ? -13.563 -40.190 -4.709  1.00 144.77 ? 108 PHE   A CA  1 
ATOM   641  C  C   . PHE   A 1 88  ? -12.800 -40.177 -3.394  1.00 156.56 ? 108 PHE   A C   1 
ATOM   642  O  O   . PHE   A 1 88  ? -13.391 -39.950 -2.333  1.00 152.98 ? 108 PHE   A O   1 
ATOM   643  C  CB  . PHE   A 1 88  ? -14.075 -38.788 -5.054  1.00 145.07 ? 108 PHE   A CB  1 
ATOM   644  C  CG  . PHE   A 1 88  ? -12.997 -37.828 -5.463  1.00 148.74 ? 108 PHE   A CG  1 
ATOM   645  C  CD1 . PHE   A 1 88  ? -12.422 -37.907 -6.721  1.00 156.63 ? 108 PHE   A CD1 1 
ATOM   646  C  CD2 . PHE   A 1 88  ? -12.568 -36.835 -4.598  1.00 153.69 ? 108 PHE   A CD2 1 
ATOM   647  C  CE1 . PHE   A 1 88  ? -11.433 -37.021 -7.104  1.00 170.99 ? 108 PHE   A CE1 1 
ATOM   648  C  CE2 . PHE   A 1 88  ? -11.579 -35.946 -4.975  1.00 165.79 ? 108 PHE   A CE2 1 
ATOM   649  C  CZ  . PHE   A 1 88  ? -11.011 -36.039 -6.230  1.00 170.94 ? 108 PHE   A CZ  1 
ATOM   650  N  N   . GLY   A 1 89  ? -11.494 -40.422 -3.465  1.00 161.78 ? 109 GLY   A N   1 
ATOM   651  C  CA  . GLY   A 1 89  ? -10.656 -40.442 -2.291  1.00 161.86 ? 109 GLY   A CA  1 
ATOM   652  C  C   . GLY   A 1 89  ? -9.188  -40.297 -2.635  1.00 159.91 ? 109 GLY   A C   1 
ATOM   653  O  O   . GLY   A 1 89  ? -8.778  -40.478 -3.785  1.00 155.17 ? 109 GLY   A O   1 
ATOM   654  N  N   . PRO   A 1 90  ? -8.359  -39.970 -1.635  1.00 164.98 ? 110 PRO   A N   1 
ATOM   655  C  CA  . PRO   A 1 90  ? -8.699  -39.740 -0.223  1.00 172.90 ? 110 PRO   A CA  1 
ATOM   656  C  C   . PRO   A 1 90  ? -9.353  -38.381 0.014   1.00 173.40 ? 110 PRO   A C   1 
ATOM   657  O  O   . PRO   A 1 90  ? -8.878  -37.355 -0.466  1.00 178.15 ? 110 PRO   A O   1 
ATOM   658  C  CB  . PRO   A 1 90  ? -7.336  -39.848 0.470   1.00 170.33 ? 110 PRO   A CB  1 
ATOM   659  C  CG  . PRO   A 1 90  ? -6.372  -39.337 -0.559  1.00 160.98 ? 110 PRO   A CG  1 
ATOM   660  C  CD  . PRO   A 1 90  ? -6.909  -39.849 -1.873  1.00 159.72 ? 110 PRO   A CD  1 
ATOM   661  N  N   . VAL   A 1 91  ? -10.455 -38.355 0.762   1.00 163.99 ? 111 VAL   A N   1 
ATOM   662  C  CA  . VAL   A 1 91  ? -11.186 -37.124 1.008   1.00 157.02 ? 111 VAL   A CA  1 
ATOM   663  C  C   . VAL   A 1 91  ? -11.149 -36.698 2.473   1.00 156.65 ? 111 VAL   A C   1 
ATOM   664  O  O   . VAL   A 1 91  ? -11.225 -35.496 2.753   1.00 166.76 ? 111 VAL   A O   1 
ATOM   665  C  CB  . VAL   A 1 91  ? -12.643 -37.250 0.516   1.00 151.51 ? 111 VAL   A CB  1 
ATOM   666  C  CG1 . VAL   A 1 91  ? -12.711 -37.050 -0.988  1.00 157.57 ? 111 VAL   A CG1 1 
ATOM   667  C  CG2 . VAL   A 1 91  ? -13.214 -38.606 0.900   1.00 153.02 ? 111 VAL   A CG2 1 
ATOM   668  N  N   . GLY   A 1 92  ? -11.039 -37.634 3.409   1.00 155.00 ? 112 GLY   A N   1 
ATOM   669  C  CA  . GLY   A 1 92  ? -10.997 -37.257 4.816   1.00 155.70 ? 112 GLY   A CA  1 
ATOM   670  C  C   . GLY   A 1 92  ? -12.368 -36.832 5.301   1.00 158.85 ? 112 GLY   A C   1 
ATOM   671  O  O   . GLY   A 1 92  ? -13.371 -37.515 5.067   1.00 159.92 ? 112 GLY   A O   1 
ATOM   672  N  N   . PHE   A 1 93  ? -12.422 -35.687 5.987   1.00 153.27 ? 113 PHE   A N   1 
ATOM   673  C  CA  . PHE   A 1 93  ? -13.700 -35.162 6.454   1.00 152.06 ? 113 PHE   A CA  1 
ATOM   674  C  C   . PHE   A 1 93  ? -14.581 -34.692 5.306   1.00 148.01 ? 113 PHE   A C   1 
ATOM   675  O  O   . PHE   A 1 93  ? -15.787 -34.503 5.500   1.00 146.12 ? 113 PHE   A O   1 
ATOM   676  C  CB  . PHE   A 1 93  ? -13.477 -34.017 7.446   1.00 146.89 ? 113 PHE   A CB  1 
ATOM   677  C  CG  . PHE   A 1 93  ? -12.988 -32.746 6.811   1.00 152.02 ? 113 PHE   A CG  1 
ATOM   678  C  CD1 . PHE   A 1 93  ? -11.647 -32.577 6.509   1.00 161.15 ? 113 PHE   A CD1 1 
ATOM   679  C  CD2 . PHE   A 1 93  ? -13.869 -31.716 6.525   1.00 156.58 ? 113 PHE   A CD2 1 
ATOM   680  C  CE1 . PHE   A 1 93  ? -11.195 -31.407 5.926   1.00 163.71 ? 113 PHE   A CE1 1 
ATOM   681  C  CE2 . PHE   A 1 93  ? -13.424 -30.545 5.942   1.00 155.08 ? 113 PHE   A CE2 1 
ATOM   682  C  CZ  . PHE   A 1 93  ? -12.085 -30.390 5.643   1.00 159.38 ? 113 PHE   A CZ  1 
ATOM   683  N  N   . MET   A 1 94  ? -14.007 -34.503 4.116   1.00 141.46 ? 114 MET   A N   1 
ATOM   684  C  CA  . MET   A 1 94  ? -14.774 -34.127 2.935   1.00 142.47 ? 114 MET   A CA  1 
ATOM   685  C  C   . MET   A 1 94  ? -15.660 -35.252 2.418   1.00 146.24 ? 114 MET   A C   1 
ATOM   686  O  O   . MET   A 1 94  ? -16.377 -35.041 1.434   1.00 144.26 ? 114 MET   A O   1 
ATOM   687  C  CB  . MET   A 1 94  ? -13.829 -33.660 1.826   1.00 149.16 ? 114 MET   A CB  1 
ATOM   688  C  CG  . MET   A 1 94  ? -13.172 -32.316 2.097   1.00 155.68 ? 114 MET   A CG  1 
ATOM   689  S  SD  . MET   A 1 94  ? -14.354 -30.957 2.048   1.00 146.43 ? 114 MET   A SD  1 
ATOM   690  C  CE  . MET   A 1 94  ? -14.957 -31.110 0.370   1.00 132.68 ? 114 MET   A CE  1 
ATOM   691  N  N   . LYS   A 1 95  ? -15.627 -36.434 3.040   1.00 162.72 ? 115 LYS   A N   1 
ATOM   692  C  CA  . LYS   A 1 95  ? -16.562 -37.490 2.665   1.00 160.45 ? 115 LYS   A CA  1 
ATOM   693  C  C   . LYS   A 1 95  ? -18.002 -37.065 2.917   1.00 155.64 ? 115 LYS   A C   1 
ATOM   694  O  O   . LYS   A 1 95  ? -18.920 -37.543 2.240   1.00 150.39 ? 115 LYS   A O   1 
ATOM   695  C  CB  . LYS   A 1 95  ? -16.251 -38.771 3.439   1.00 161.46 ? 115 LYS   A CB  1 
ATOM   696  C  CG  . LYS   A 1 95  ? -16.580 -38.673 4.919   1.00 165.14 ? 115 LYS   A CG  1 
ATOM   697  C  CD  . LYS   A 1 95  ? -16.551 -40.023 5.605   1.00 178.31 ? 115 LYS   A CD  1 
ATOM   698  C  CE  . LYS   A 1 95  ? -17.350 -39.978 6.896   1.00 178.06 ? 115 LYS   A CE  1 
ATOM   699  N  NZ  . LYS   A 1 95  ? -17.085 -38.728 7.664   1.00 171.78 ? 115 LYS   A NZ  1 
ATOM   700  N  N   . SER   A 1 96  ? -18.217 -36.172 3.882   1.00 150.92 ? 116 SER   A N   1 
ATOM   701  C  CA  A SER   A 1 96  ? -19.550 -35.682 4.203   0.39 146.55 ? 116 SER   A CA  1 
ATOM   702  C  CA  B SER   A 1 96  ? -19.550 -35.682 4.203   0.61 146.36 ? 116 SER   A CA  1 
ATOM   703  C  C   . SER   A 1 96  ? -20.014 -34.572 3.271   1.00 138.79 ? 116 SER   A C   1 
ATOM   704  O  O   . SER   A 1 96  ? -21.144 -34.096 3.420   1.00 139.12 ? 116 SER   A O   1 
ATOM   705  C  CB  A SER   A 1 96  ? -19.592 -35.192 5.653   0.39 148.34 ? 116 SER   A CB  1 
ATOM   706  C  CB  B SER   A 1 96  ? -19.592 -35.188 5.652   0.61 148.19 ? 116 SER   A CB  1 
ATOM   707  O  OG  A SER   A 1 96  ? -18.608 -34.198 5.884   0.39 144.98 ? 116 SER   A OG  1 
ATOM   708  O  OG  B SER   A 1 96  ? -19.237 -36.222 6.554   0.61 152.61 ? 116 SER   A OG  1 
ATOM   709  N  N   . ALA   A 1 97  ? -19.177 -34.147 2.327   1.00 126.31 ? 117 ALA   A N   1 
ATOM   710  C  CA  . ALA   A 1 97  ? -19.586 -33.127 1.372   1.00 125.13 ? 117 ALA   A CA  1 
ATOM   711  C  C   . ALA   A 1 97  ? -20.725 -33.649 0.507   1.00 124.57 ? 117 ALA   A C   1 
ATOM   712  O  O   . ALA   A 1 97  ? -20.760 -34.829 0.147   1.00 129.78 ? 117 ALA   A O   1 
ATOM   713  C  CB  . ALA   A 1 97  ? -18.402 -32.711 0.501   1.00 122.68 ? 117 ALA   A CB  1 
ATOM   714  N  N   . ILE   A 1 98  ? -21.660 -32.758 0.169   1.00 103.93 ? 118 ILE   A N   1 
ATOM   715  C  CA  . ILE   A 1 98  ? -22.879 -33.183 -0.515  1.00 110.82 ? 118 ILE   A CA  1 
ATOM   716  C  C   . ILE   A 1 98  ? -22.556 -33.765 -1.888  1.00 119.42 ? 118 ILE   A C   1 
ATOM   717  O  O   . ILE   A 1 98  ? -23.188 -34.732 -2.331  1.00 116.44 ? 118 ILE   A O   1 
ATOM   718  C  CB  . ILE   A 1 98  ? -23.878 -32.013 -0.604  1.00 105.96 ? 118 ILE   A CB  1 
ATOM   719  C  CG1 . ILE   A 1 98  ? -25.150 -32.449 -1.334  1.00 97.74  ? 118 ILE   A CG1 1 
ATOM   720  C  CG2 . ILE   A 1 98  ? -23.244 -30.803 -1.278  1.00 94.45  ? 118 ILE   A CG2 1 
ATOM   721  C  CD1 . ILE   A 1 98  ? -26.236 -31.398 -1.343  1.00 100.91 ? 118 ILE   A CD1 1 
ATOM   722  N  N   . SER   A 1 99  ? -21.537 -33.183 -2.580  1.00 110.24 ? 119 SER   A N   1 
ATOM   723  C  CA  . SER   A 1 99  ? -21.105 -33.724 -3.863  1.00 107.15 ? 119 SER   A CA  1 
ATOM   724  C  C   . SER   A 1 99  ? -20.318 -35.018 -3.720  1.00 110.25 ? 119 SER   A C   1 
ATOM   725  O  O   . SER   A 1 99  ? -19.946 -35.613 -4.738  1.00 105.14 ? 119 SER   A O   1 
ATOM   726  C  CB  . SER   A 1 99  ? -20.262 -32.692 -4.614  1.00 110.75 ? 119 SER   A CB  1 
ATOM   727  O  OG  . SER   A 1 99  ? -19.053 -32.424 -3.925  1.00 118.50 ? 119 SER   A OG  1 
ATOM   728  N  N   . ILE   A 1 100 ? -20.064 -35.469 -2.490  1.00 108.49 ? 120 ILE   A N   1 
ATOM   729  C  CA  . ILE   A 1 100 ? -19.235 -36.641 -2.238  1.00 114.79 ? 120 ILE   A CA  1 
ATOM   730  C  C   . ILE   A 1 100 ? -20.024 -37.641 -1.400  1.00 125.13 ? 120 ILE   A C   1 
ATOM   731  O  O   . ILE   A 1 100 ? -19.794 -38.853 -1.480  1.00 133.11 ? 120 ILE   A O   1 
ATOM   732  C  CB  . ILE   A 1 100 ? -17.916 -36.235 -1.551  1.00 127.10 ? 120 ILE   A CB  1 
ATOM   733  C  CG1 . ILE   A 1 100 ? -17.150 -35.238 -2.426  1.00 124.16 ? 120 ILE   A CG1 1 
ATOM   734  C  CG2 . ILE   A 1 100 ? -17.050 -37.451 -1.258  1.00 123.27 ? 120 ILE   A CG2 1 
ATOM   735  C  CD1 . ILE   A 1 100 ? -15.885 -34.702 -1.790  1.00 123.01 ? 120 ILE   A CD1 1 
ATOM   736  N  N   . ALA   A 1 101 ? -20.972 -37.141 -0.608  1.00 118.78 ? 121 ALA   A N   1 
ATOM   737  C  CA  . ALA   A 1 101 ? -21.771 -38.002 0.254   1.00 113.57 ? 121 ALA   A CA  1 
ATOM   738  C  C   . ALA   A 1 101 ? -22.613 -38.969 -0.576  1.00 106.67 ? 121 ALA   A C   1 
ATOM   739  O  O   . ALA   A 1 101 ? -22.849 -38.768 -1.770  1.00 103.37 ? 121 ALA   A O   1 
ATOM   740  C  CB  . ALA   A 1 101 ? -22.671 -37.166 1.163   1.00 117.04 ? 121 ALA   A CB  1 
ATOM   741  N  N   . GLU   A 1 102 ? -23.074 -40.033 0.080   1.00 98.02  ? 122 GLU   A N   1 
ATOM   742  C  CA  . GLU   A 1 102 ? -23.764 -41.119 -0.601  1.00 104.49 ? 122 GLU   A CA  1 
ATOM   743  C  C   . GLU   A 1 102 ? -25.001 -41.545 0.178   1.00 117.88 ? 122 GLU   A C   1 
ATOM   744  O  O   . GLU   A 1 102 ? -25.061 -41.417 1.404   1.00 118.07 ? 122 GLU   A O   1 
ATOM   745  C  CB  . GLU   A 1 102 ? -22.852 -42.341 -0.786  1.00 113.77 ? 122 GLU   A CB  1 
ATOM   746  C  CG  . GLU   A 1 102 ? -21.616 -42.100 -1.633  1.00 136.92 ? 122 GLU   A CG  1 
ATOM   747  C  CD  . GLU   A 1 102 ? -20.670 -43.287 -1.617  1.00 150.58 ? 122 GLU   A CD  1 
ATOM   748  O  OE1 . GLU   A 1 102 ? -20.684 -44.047 -0.624  1.00 155.64 ? 122 GLU   A OE1 1 
ATOM   749  O  OE2 . GLU   A 1 102 ? -19.918 -43.464 -2.597  1.00 157.23 ? 122 GLU   A OE2 1 
ATOM   750  N  N   . ASP   A 1 103 ? -25.984 -42.057 -0.561  1.00 121.47 ? 123 ASP   A N   1 
ATOM   751  C  CA  . ASP   A 1 103 ? -27.143 -42.786 -0.021  1.00 116.71 ? 123 ASP   A CA  1 
ATOM   752  C  C   . ASP   A 1 103 ? -27.899 -41.891 0.960   1.00 125.83 ? 123 ASP   A C   1 
ATOM   753  O  O   . ASP   A 1 103 ? -28.180 -40.729 0.626   1.00 122.04 ? 123 ASP   A O   1 
ATOM   754  C  CB  . ASP   A 1 103 ? -26.659 -44.114 0.544   1.00 131.82 ? 123 ASP   A CB  1 
ATOM   755  C  CG  . ASP   A 1 103 ? -26.630 -45.211 -0.497  1.00 143.68 ? 123 ASP   A CG  1 
ATOM   756  O  OD1 . ASP   A 1 103 ? -26.979 -44.932 -1.663  1.00 133.08 ? 123 ASP   A OD1 1 
ATOM   757  O  OD2 . ASP   A 1 103 ? -26.266 -46.354 -0.149  1.00 164.96 ? 123 ASP   A OD2 1 
ATOM   758  N  N   . GLU   A 1 104 ? -28.249 -42.378 2.154   1.00 133.95 ? 124 GLU   A N   1 
ATOM   759  C  CA  . GLU   A 1 104 ? -29.122 -41.626 3.048   1.00 138.20 ? 124 GLU   A CA  1 
ATOM   760  C  C   . GLU   A 1 104 ? -28.434 -40.390 3.609   1.00 133.03 ? 124 GLU   A C   1 
ATOM   761  O  O   . GLU   A 1 104 ? -29.111 -39.423 3.976   1.00 133.87 ? 124 GLU   A O   1 
ATOM   762  C  CB  . GLU   A 1 104 ? -29.606 -42.528 4.183   1.00 148.98 ? 124 GLU   A CB  1 
ATOM   763  C  CG  . GLU   A 1 104 ? -30.193 -43.849 3.710   1.00 148.82 ? 124 GLU   A CG  1 
ATOM   764  C  CD  . GLU   A 1 104 ? -31.361 -43.663 2.760   1.00 171.43 ? 124 GLU   A CD  1 
ATOM   765  O  OE1 . GLU   A 1 104 ? -32.175 -42.742 2.985   1.00 190.02 ? 124 GLU   A OE1 1 
ATOM   766  O  OE2 . GLU   A 1 104 ? -31.462 -44.436 1.784   1.00 169.84 ? 124 GLU   A OE2 1 
ATOM   767  N  N   . GLU   A 1 105 ? -27.102 -40.402 3.691   1.00 127.55 ? 125 GLU   A N   1 
ATOM   768  C  CA  . GLU   A 1 105 ? -26.389 -39.205 4.122   1.00 127.13 ? 125 GLU   A CA  1 
ATOM   769  C  C   . GLU   A 1 105 ? -26.567 -38.075 3.117   1.00 122.01 ? 125 GLU   A C   1 
ATOM   770  O  O   . GLU   A 1 105 ? -26.694 -36.906 3.500   1.00 121.37 ? 125 GLU   A O   1 
ATOM   771  C  CB  . GLU   A 1 105 ? -24.906 -39.516 4.322   1.00 137.33 ? 125 GLU   A CB  1 
ATOM   772  C  CG  . GLU   A 1 105 ? -24.108 -38.360 4.905   1.00 156.26 ? 125 GLU   A CG  1 
ATOM   773  C  CD  . GLU   A 1 105 ? -22.611 -38.562 4.781   1.00 160.69 ? 125 GLU   A CD  1 
ATOM   774  O  OE1 . GLU   A 1 105 ? -22.188 -39.352 3.911   1.00 156.16 ? 125 GLU   A OE1 1 
ATOM   775  O  OE2 . GLU   A 1 105 ? -21.858 -37.931 5.552   1.00 164.47 ? 125 GLU   A OE2 1 
ATOM   776  N  N   . TRP   A 1 106 ? -26.589 -38.406 1.824   1.00 117.13 ? 126 TRP   A N   1 
ATOM   777  C  CA  . TRP   A 1 106 ? -26.763 -37.381 0.799   1.00 109.28 ? 126 TRP   A CA  1 
ATOM   778  C  C   . TRP   A 1 106 ? -28.188 -36.843 0.788   1.00 114.03 ? 126 TRP   A C   1 
ATOM   779  O  O   . TRP   A 1 106 ? -28.398 -35.632 0.651   1.00 109.78 ? 126 TRP   A O   1 
ATOM   780  C  CB  . TRP   A 1 106 ? -26.396 -37.940 -0.573  1.00 98.15  ? 126 TRP   A CB  1 
ATOM   781  C  CG  . TRP   A 1 106 ? -26.939 -37.120 -1.702  1.00 100.55 ? 126 TRP   A CG  1 
ATOM   782  C  CD1 . TRP   A 1 106 ? -26.428 -35.952 -2.185  1.00 105.06 ? 126 TRP   A CD1 1 
ATOM   783  C  CD2 . TRP   A 1 106 ? -28.105 -37.403 -2.486  1.00 109.57 ? 126 TRP   A CD2 1 
ATOM   784  N  NE1 . TRP   A 1 106 ? -27.200 -35.490 -3.222  1.00 91.21  ? 126 TRP   A NE1 1 
ATOM   785  C  CE2 . TRP   A 1 106 ? -28.236 -36.363 -3.427  1.00 103.72 ? 126 TRP   A CE2 1 
ATOM   786  C  CE3 . TRP   A 1 106 ? -29.049 -38.435 -2.485  1.00 108.85 ? 126 TRP   A CE3 1 
ATOM   787  C  CZ2 . TRP   A 1 106 ? -29.273 -36.324 -4.357  1.00 106.69 ? 126 TRP   A CZ2 1 
ATOM   788  C  CZ3 . TRP   A 1 106 ? -30.077 -38.395 -3.409  1.00 102.44 ? 126 TRP   A CZ3 1 
ATOM   789  C  CH2 . TRP   A 1 106 ? -30.181 -37.347 -4.333  1.00 114.77 ? 126 TRP   A CH2 1 
ATOM   790  N  N   . LYS   A 1 107 ? -29.177 -37.731 0.920   1.00 120.52 ? 127 LYS   A N   1 
ATOM   791  C  CA  . LYS   A 1 107 ? -30.572 -37.299 0.896   1.00 115.65 ? 127 LYS   A CA  1 
ATOM   792  C  C   . LYS   A 1 107 ? -30.862 -36.309 2.016   1.00 115.23 ? 127 LYS   A C   1 
ATOM   793  O  O   . LYS   A 1 107 ? -31.654 -35.375 1.842   1.00 119.28 ? 127 LYS   A O   1 
ATOM   794  C  CB  . LYS   A 1 107 ? -31.494 -38.513 1.001   1.00 122.26 ? 127 LYS   A CB  1 
ATOM   795  C  CG  . LYS   A 1 107 ? -32.563 -38.574 -0.073  1.00 124.27 ? 127 LYS   A CG  1 
ATOM   796  C  CD  . LYS   A 1 107 ? -32.453 -39.858 -0.876  1.00 129.14 ? 127 LYS   A CD  1 
ATOM   797  C  CE  . LYS   A 1 107 ? -32.689 -41.081 -0.005  1.00 139.21 ? 127 LYS   A CE  1 
ATOM   798  N  NZ  . LYS   A 1 107 ? -32.594 -42.343 -0.790  1.00 111.03 ? 127 LYS   A NZ  1 
ATOM   799  N  N   . ARG   A 1 108 ? -30.227 -36.496 3.174   1.00 114.19 ? 128 ARG   A N   1 
ATOM   800  C  CA  . ARG   A 1 108 ? -30.410 -35.563 4.280   1.00 114.03 ? 128 ARG   A CA  1 
ATOM   801  C  C   . ARG   A 1 108 ? -29.753 -34.220 3.985   1.00 115.23 ? 128 ARG   A C   1 
ATOM   802  O  O   . ARG   A 1 108 ? -30.332 -33.163 4.264   1.00 132.71 ? 128 ARG   A O   1 
ATOM   803  C  CB  . ARG   A 1 108 ? -29.853 -36.176 5.564   1.00 117.82 ? 128 ARG   A CB  1 
ATOM   804  C  CG  . ARG   A 1 108 ? -29.740 -35.220 6.734   1.00 126.42 ? 128 ARG   A CG  1 
ATOM   805  C  CD  . ARG   A 1 108 ? -29.198 -35.944 7.954   1.00 159.44 ? 128 ARG   A CD  1 
ATOM   806  N  NE  . ARG   A 1 108 ? -28.327 -35.091 8.753   1.00 173.74 ? 128 ARG   A NE  1 
ATOM   807  C  CZ  . ARG   A 1 108 ? -27.035 -34.910 8.513   1.00 175.46 ? 128 ARG   A CZ  1 
ATOM   808  N  NH1 . ARG   A 1 108 ? -26.432 -35.501 7.495   1.00 164.15 ? 128 ARG   A NH1 1 
ATOM   809  N  NH2 . ARG   A 1 108 ? -26.332 -34.114 9.313   1.00 178.73 ? 128 ARG   A NH2 1 
ATOM   810  N  N   . LEU   A 1 109 ? -28.550 -34.238 3.407   1.00 109.94 ? 129 LEU   A N   1 
ATOM   811  C  CA  . LEU   A 1 109 ? -27.857 -32.990 3.101   1.00 108.28 ? 129 LEU   A CA  1 
ATOM   812  C  C   . LEU   A 1 109 ? -28.530 -32.247 1.954   1.00 112.18 ? 129 LEU   A C   1 
ATOM   813  O  O   . LEU   A 1 109 ? -28.633 -31.015 1.983   1.00 101.57 ? 129 LEU   A O   1 
ATOM   814  C  CB  . LEU   A 1 109 ? -26.394 -33.272 2.765   1.00 122.36 ? 129 LEU   A CB  1 
ATOM   815  C  CG  . LEU   A 1 109 ? -25.561 -33.930 3.864   1.00 112.72 ? 129 LEU   A CG  1 
ATOM   816  C  CD1 . LEU   A 1 109 ? -24.303 -34.541 3.276   1.00 122.39 ? 129 LEU   A CD1 1 
ATOM   817  C  CD2 . LEU   A 1 109 ? -25.212 -32.927 4.951   1.00 123.34 ? 129 LEU   A CD2 1 
ATOM   818  N  N   . ARG   A 1 110 ? -28.982 -32.977 0.930   1.00 117.01 ? 130 ARG   A N   1 
ATOM   819  C  CA  . ARG   A 1 110 ? -29.635 -32.334 -0.206  1.00 108.48 ? 130 ARG   A CA  1 
ATOM   820  C  C   . ARG   A 1 110 ? -30.918 -31.632 0.220   1.00 119.89 ? 130 ARG   A C   1 
ATOM   821  O  O   . ARG   A 1 110 ? -31.260 -30.570 -0.312  1.00 128.50 ? 130 ARG   A O   1 
ATOM   822  C  CB  . ARG   A 1 110 ? -29.923 -33.365 -1.300  1.00 95.85  ? 130 ARG   A CB  1 
ATOM   823  C  CG  . ARG   A 1 110 ? -30.571 -32.790 -2.554  1.00 94.18  ? 130 ARG   A CG  1 
ATOM   824  C  CD  . ARG   A 1 110 ? -29.535 -32.297 -3.553  1.00 94.58  ? 130 ARG   A CD  1 
ATOM   825  N  NE  . ARG   A 1 110 ? -30.148 -31.545 -4.643  1.00 112.44 ? 130 ARG   A NE  1 
ATOM   826  C  CZ  . ARG   A 1 110 ? -29.569 -31.308 -5.812  1.00 105.18 ? 130 ARG   A CZ  1 
ATOM   827  N  NH1 . ARG   A 1 110 ? -28.365 -31.778 -6.095  1.00 114.63 ? 130 ARG   A NH1 1 
ATOM   828  N  NH2 . ARG   A 1 110 ? -30.217 -30.587 -6.723  1.00 86.02  ? 130 ARG   A NH2 1 
ATOM   829  N  N   . SER   A 1 111 ? -31.643 -32.211 1.180   1.00 110.93 ? 131 SER   A N   1 
ATOM   830  C  CA  . SER   A 1 111 ? -32.849 -31.566 1.687   1.00 115.61 ? 131 SER   A CA  1 
ATOM   831  C  C   . SER   A 1 111 ? -32.507 -30.372 2.570   1.00 115.98 ? 131 SER   A C   1 
ATOM   832  O  O   . SER   A 1 111 ? -33.184 -29.338 2.519   1.00 130.30 ? 131 SER   A O   1 
ATOM   833  C  CB  . SER   A 1 111 ? -33.700 -32.576 2.456   1.00 128.20 ? 131 SER   A CB  1 
ATOM   834  O  OG  . SER   A 1 111 ? -34.940 -32.797 1.807   1.00 133.89 ? 131 SER   A OG  1 
ATOM   835  N  N   . LEU   A 1 112 ? -31.454 -30.494 3.381   1.00 113.66 ? 132 LEU   A N   1 
ATOM   836  C  CA  . LEU   A 1 112 ? -31.085 -29.418 4.294   1.00 122.67 ? 132 LEU   A CA  1 
ATOM   837  C  C   . LEU   A 1 112 ? -30.556 -28.197 3.551   1.00 116.19 ? 132 LEU   A C   1 
ATOM   838  O  O   . LEU   A 1 112 ? -30.757 -27.065 4.004   1.00 126.00 ? 132 LEU   A O   1 
ATOM   839  C  CB  . LEU   A 1 112 ? -30.046 -29.922 5.296   1.00 128.86 ? 132 LEU   A CB  1 
ATOM   840  C  CG  . LEU   A 1 112 ? -29.591 -28.958 6.392   1.00 139.62 ? 132 LEU   A CG  1 
ATOM   841  C  CD1 . LEU   A 1 112 ? -30.053 -29.450 7.752   1.00 153.69 ? 132 LEU   A CD1 1 
ATOM   842  C  CD2 . LEU   A 1 112 ? -28.081 -28.791 6.362   1.00 145.40 ? 132 LEU   A CD2 1 
ATOM   843  N  N   . LEU   A 1 113 ? -29.887 -28.400 2.417   1.00 126.04 ? 133 LEU   A N   1 
ATOM   844  C  CA  . LEU   A 1 113 ? -29.278 -27.310 1.668   1.00 125.76 ? 133 LEU   A CA  1 
ATOM   845  C  C   . LEU   A 1 113 ? -30.098 -26.875 0.461   1.00 120.82 ? 133 LEU   A C   1 
ATOM   846  O  O   . LEU   A 1 113 ? -29.705 -25.926 -0.224  1.00 126.37 ? 133 LEU   A O   1 
ATOM   847  C  CB  . LEU   A 1 113 ? -27.868 -27.705 1.216   1.00 123.85 ? 133 LEU   A CB  1 
ATOM   848  C  CG  . LEU   A 1 113 ? -26.900 -28.081 2.339   1.00 120.35 ? 133 LEU   A CG  1 
ATOM   849  C  CD1 . LEU   A 1 113 ? -25.527 -28.422 1.782   1.00 110.83 ? 133 LEU   A CD1 1 
ATOM   850  C  CD2 . LEU   A 1 113 ? -26.807 -26.958 3.360   1.00 126.71 ? 133 LEU   A CD2 1 
ATOM   851  N  N   . SER   A 1 114 ? -31.216 -27.545 0.178   1.00 120.19 ? 134 SER   A N   1 
ATOM   852  C  CA  . SER   A 1 114 ? -32.069 -27.126 -0.933  1.00 120.38 ? 134 SER   A CA  1 
ATOM   853  C  C   . SER   A 1 114 ? -32.793 -25.795 -0.769  1.00 127.02 ? 134 SER   A C   1 
ATOM   854  O  O   . SER   A 1 114 ? -32.999 -25.105 -1.783  1.00 134.23 ? 134 SER   A O   1 
ATOM   855  C  CB  . SER   A 1 114 ? -33.166 -28.170 -1.169  1.00 129.12 ? 134 SER   A CB  1 
ATOM   856  O  OG  . SER   A 1 114 ? -32.623 -29.385 -1.657  1.00 132.94 ? 134 SER   A OG  1 
ATOM   857  N  N   . PRO   A 1 115 ? -33.206 -25.364 0.444   1.00 124.09 ? 135 PRO   A N   1 
ATOM   858  C  CA  . PRO   A 1 115 ? -33.826 -24.035 0.567   1.00 122.00 ? 135 PRO   A CA  1 
ATOM   859  C  C   . PRO   A 1 115 ? -32.865 -22.856 0.534   1.00 127.73 ? 135 PRO   A C   1 
ATOM   860  O  O   . PRO   A 1 115 ? -33.242 -21.739 0.900   1.00 138.08 ? 135 PRO   A O   1 
ATOM   861  C  CB  . PRO   A 1 115 ? -34.628 -24.140 1.874   1.00 138.40 ? 135 PRO   A CB  1 
ATOM   862  C  CG  . PRO   A 1 115 ? -34.726 -25.601 2.167   1.00 126.56 ? 135 PRO   A CG  1 
ATOM   863  C  CD  . PRO   A 1 115 ? -33.457 -26.176 1.647   1.00 117.48 ? 135 PRO   A CD  1 
ATOM   864  N  N   . THR   A 1 116 ? -31.625 -23.081 0.100   1.00 130.45 ? 136 THR   A N   1 
ATOM   865  C  CA  . THR   A 1 116 ? -30.653 -21.999 0.017   1.00 134.45 ? 136 THR   A CA  1 
ATOM   866  C  C   . THR   A 1 116 ? -30.726 -21.237 -1.299  1.00 134.29 ? 136 THR   A C   1 
ATOM   867  O  O   . THR   A 1 116 ? -30.405 -20.043 -1.335  1.00 134.80 ? 136 THR   A O   1 
ATOM   868  C  CB  . THR   A 1 116 ? -29.237 -22.553 0.218   1.00 133.18 ? 136 THR   A CB  1 
ATOM   869  O  OG1 . THR   A 1 116 ? -29.212 -23.388 1.382   1.00 134.74 ? 136 THR   A OG1 1 
ATOM   870  C  CG2 . THR   A 1 116 ? -28.234 -21.420 0.403   1.00 134.17 ? 136 THR   A CG2 1 
ATOM   871  N  N   . PHE   A 1 117 ? -31.159 -21.891 -2.373  1.00 125.72 ? 137 PHE   A N   1 
ATOM   872  C  CA  . PHE   A 1 117 ? -31.245 -21.281 -3.693  1.00 128.16 ? 137 PHE   A CA  1 
ATOM   873  C  C   . PHE   A 1 117 ? -32.686 -21.227 -4.184  1.00 125.75 ? 137 PHE   A C   1 
ATOM   874  O  O   . PHE   A 1 117 ? -32.967 -21.442 -5.365  1.00 127.84 ? 137 PHE   A O   1 
ATOM   875  C  CB  . PHE   A 1 117 ? -30.369 -22.024 -4.697  1.00 139.61 ? 137 PHE   A CB  1 
ATOM   876  C  CG  . PHE   A 1 117 ? -28.955 -22.213 -4.240  1.00 143.06 ? 137 PHE   A CG  1 
ATOM   877  C  CD1 . PHE   A 1 117 ? -28.108 -21.127 -4.099  1.00 128.51 ? 137 PHE   A CD1 1 
ATOM   878  C  CD2 . PHE   A 1 117 ? -28.470 -23.478 -3.956  1.00 134.87 ? 137 PHE   A CD2 1 
ATOM   879  C  CE1 . PHE   A 1 117 ? -26.805 -21.298 -3.680  1.00 128.77 ? 137 PHE   A CE1 1 
ATOM   880  C  CE2 . PHE   A 1 117 ? -27.168 -23.656 -3.537  1.00 127.24 ? 137 PHE   A CE2 1 
ATOM   881  C  CZ  . PHE   A 1 117 ? -26.334 -22.564 -3.400  1.00 133.01 ? 137 PHE   A CZ  1 
ATOM   882  N  N   . THR   A 1 118 ? -33.621 -20.945 -3.282  1.00 145.30 ? 138 THR   A N   1 
ATOM   883  C  CA  . THR   A 1 118 ? -34.994 -20.731 -3.706  1.00 151.11 ? 138 THR   A CA  1 
ATOM   884  C  C   . THR   A 1 118 ? -35.108 -19.403 -4.452  1.00 159.80 ? 138 THR   A C   1 
ATOM   885  O  O   . THR   A 1 118 ? -34.201 -18.565 -4.433  1.00 155.29 ? 138 THR   A O   1 
ATOM   886  C  CB  . THR   A 1 118 ? -35.944 -20.748 -2.508  1.00 145.79 ? 138 THR   A CB  1 
ATOM   887  O  OG1 . THR   A 1 118 ? -35.629 -19.662 -1.629  1.00 142.01 ? 138 THR   A OG1 1 
ATOM   888  C  CG2 . THR   A 1 118 ? -35.826 -22.059 -1.751  1.00 104.18 ? 138 THR   A CG2 1 
ATOM   889  N  N   . SER   A 1 119 ? -36.248 -19.214 -5.120  1.00 157.11 ? 139 SER   A N   1 
ATOM   890  C  CA  . SER   A 1 119 ? -36.476 -17.976 -5.857  1.00 154.75 ? 139 SER   A CA  1 
ATOM   891  C  C   . SER   A 1 119 ? -36.508 -16.757 -4.943  1.00 159.49 ? 139 SER   A C   1 
ATOM   892  O  O   . SER   A 1 119 ? -36.246 -15.641 -5.405  1.00 159.80 ? 139 SER   A O   1 
ATOM   893  C  CB  . SER   A 1 119 ? -37.778 -18.078 -6.653  1.00 162.75 ? 139 SER   A CB  1 
ATOM   894  O  OG  . SER   A 1 119 ? -38.747 -18.845 -5.958  1.00 166.93 ? 139 SER   A OG  1 
ATOM   895  N  N   . GLY   A 1 120 ? -36.812 -16.942 -3.660  1.00 183.61 ? 140 GLY   A N   1 
ATOM   896  C  CA  . GLY   A 1 120 ? -36.807 -15.842 -2.716  1.00 180.84 ? 140 GLY   A CA  1 
ATOM   897  C  C   . GLY   A 1 120 ? -35.436 -15.553 -2.138  1.00 176.05 ? 140 GLY   A C   1 
ATOM   898  O  O   . GLY   A 1 120 ? -35.052 -14.390 -1.986  1.00 179.71 ? 140 GLY   A O   1 
ATOM   899  N  N   . LYS   A 1 121 ? -34.690 -16.611 -1.804  1.00 163.54 ? 141 LYS   A N   1 
ATOM   900  C  CA  . LYS   A 1 121 ? -33.344 -16.428 -1.272  1.00 150.62 ? 141 LYS   A CA  1 
ATOM   901  C  C   . LYS   A 1 121 ? -32.410 -15.809 -2.304  1.00 148.74 ? 141 LYS   A C   1 
ATOM   902  O  O   . LYS   A 1 121 ? -31.493 -15.064 -1.939  1.00 145.26 ? 141 LYS   A O   1 
ATOM   903  C  CB  . LYS   A 1 121 ? -32.784 -17.766 -0.787  1.00 143.45 ? 141 LYS   A CB  1 
ATOM   904  C  CG  . LYS   A 1 121 ? -33.533 -18.377 0.388   1.00 141.76 ? 141 LYS   A CG  1 
ATOM   905  C  CD  . LYS   A 1 121 ? -33.258 -17.633 1.684   1.00 144.58 ? 141 LYS   A CD  1 
ATOM   906  C  CE  . LYS   A 1 121 ? -34.033 -18.245 2.841   1.00 143.30 ? 141 LYS   A CE  1 
ATOM   907  N  NZ  . LYS   A 1 121 ? -33.789 -19.709 2.963   1.00 135.77 ? 141 LYS   A NZ  1 
ATOM   908  N  N   . LEU   A 1 122 ? -32.622 -16.105 -3.588  1.00 143.99 ? 142 LEU   A N   1 
ATOM   909  C  CA  . LEU   A 1 122 ? -31.813 -15.488 -4.633  1.00 143.46 ? 142 LEU   A CA  1 
ATOM   910  C  C   . LEU   A 1 122 ? -32.178 -14.022 -4.821  1.00 144.29 ? 142 LEU   A C   1 
ATOM   911  O  O   . LEU   A 1 122 ? -31.309 -13.191 -5.111  1.00 144.28 ? 142 LEU   A O   1 
ATOM   912  C  CB  . LEU   A 1 122 ? -31.980 -16.254 -5.945  1.00 131.28 ? 142 LEU   A CB  1 
ATOM   913  C  CG  . LEU   A 1 122 ? -30.831 -17.171 -6.366  1.00 127.58 ? 142 LEU   A CG  1 
ATOM   914  C  CD1 . LEU   A 1 122 ? -30.378 -18.041 -5.206  1.00 135.14 ? 142 LEU   A CD1 1 
ATOM   915  C  CD2 . LEU   A 1 122 ? -31.253 -18.029 -7.548  1.00 134.89 ? 142 LEU   A CD2 1 
ATOM   916  N  N   . LYS   A 1 123 ? -33.461 -13.685 -4.661  1.00 149.27 ? 143 LYS   A N   1 
ATOM   917  C  CA  . LYS   A 1 123 ? -33.894 -12.303 -4.831  1.00 149.91 ? 143 LYS   A CA  1 
ATOM   918  C  C   . LYS   A 1 123 ? -33.305 -11.395 -3.759  1.00 154.70 ? 143 LYS   A C   1 
ATOM   919  O  O   . LYS   A 1 123 ? -33.093 -10.202 -4.007  1.00 149.85 ? 143 LYS   A O   1 
ATOM   920  C  CB  . LYS   A 1 123 ? -35.421 -12.232 -4.816  1.00 148.20 ? 143 LYS   A CB  1 
ATOM   921  C  CG  . LYS   A 1 123 ? -35.997 -10.922 -5.326  1.00 160.49 ? 143 LYS   A CG  1 
ATOM   922  C  CD  . LYS   A 1 123 ? -37.048 -11.176 -6.395  1.00 160.80 ? 143 LYS   A CD  1 
ATOM   923  C  CE  . LYS   A 1 123 ? -38.106 -12.153 -5.908  1.00 150.70 ? 143 LYS   A CE  1 
ATOM   924  N  NZ  . LYS   A 1 123 ? -39.085 -12.495 -6.977  1.00 142.93 ? 143 LYS   A NZ  1 
ATOM   925  N  N   . GLU   A 1 124 ? -33.035 -11.936 -2.569  1.00 151.48 ? 144 GLU   A N   1 
ATOM   926  C  CA  . GLU   A 1 124 ? -32.378 -11.158 -1.526  1.00 145.60 ? 144 GLU   A CA  1 
ATOM   927  C  C   . GLU   A 1 124 ? -30.902 -10.936 -1.820  1.00 147.43 ? 144 GLU   A C   1 
ATOM   928  O  O   . GLU   A 1 124 ? -30.295 -10.032 -1.236  1.00 135.53 ? 144 GLU   A O   1 
ATOM   929  C  CB  . GLU   A 1 124 ? -32.534 -11.851 -0.172  1.00 146.25 ? 144 GLU   A CB  1 
ATOM   930  C  CG  . GLU   A 1 124 ? -33.970 -12.171 0.205   1.00 161.63 ? 144 GLU   A CG  1 
ATOM   931  C  CD  . GLU   A 1 124 ? -34.070 -12.968 1.491   1.00 175.71 ? 144 GLU   A CD  1 
ATOM   932  O  OE1 . GLU   A 1 124 ? -33.090 -12.977 2.266   1.00 177.32 ? 144 GLU   A OE1 1 
ATOM   933  O  OE2 . GLU   A 1 124 ? -35.127 -13.591 1.725   1.00 190.16 ? 144 GLU   A OE2 1 
ATOM   934  N  N   . MET   A 1 125 ? -30.313 -11.737 -2.708  1.00 149.14 ? 145 MET   A N   1 
ATOM   935  C  CA  . MET   A 1 125 ? -28.898 -11.620 -3.031  1.00 150.68 ? 145 MET   A CA  1 
ATOM   936  C  C   . MET   A 1 125 ? -28.614 -10.593 -4.117  1.00 151.52 ? 145 MET   A C   1 
ATOM   937  O  O   . MET   A 1 125 ? -27.476 -10.119 -4.214  1.00 144.03 ? 145 MET   A O   1 
ATOM   938  C  CB  . MET   A 1 125 ? -28.343 -12.981 -3.463  1.00 137.65 ? 145 MET   A CB  1 
ATOM   939  C  CG  . MET   A 1 125 ? -28.395 -14.045 -2.377  1.00 145.26 ? 145 MET   A CG  1 
ATOM   940  S  SD  . MET   A 1 125 ? -27.848 -15.665 -2.948  1.00 140.24 ? 145 MET   A SD  1 
ATOM   941  C  CE  . MET   A 1 125 ? -27.957 -16.614 -1.433  1.00 125.35 ? 145 MET   A CE  1 
ATOM   942  N  N   . VAL   A 1 126 ? -29.611 -10.238 -4.931  1.00 153.34 ? 146 VAL   A N   1 
ATOM   943  C  CA  . VAL   A 1 126 ? -29.386 -9.256  -5.995  1.00 155.90 ? 146 VAL   A CA  1 
ATOM   944  C  C   . VAL   A 1 126 ? -28.941 -7.905  -5.445  1.00 147.88 ? 146 VAL   A C   1 
ATOM   945  O  O   . VAL   A 1 126 ? -27.981 -7.331  -5.987  1.00 143.53 ? 146 VAL   A O   1 
ATOM   946  C  CB  . VAL   A 1 126 ? -30.632 -9.154  -6.894  1.00 155.27 ? 146 VAL   A CB  1 
ATOM   947  C  CG1 . VAL   A 1 126 ? -30.422 -8.107  -7.978  1.00 138.22 ? 146 VAL   A CG1 1 
ATOM   948  C  CG2 . VAL   A 1 126 ? -30.952 -10.505 -7.509  1.00 145.88 ? 146 VAL   A CG2 1 
ATOM   949  N  N   . PRO   A 1 127 ? -29.566 -7.341  -4.403  1.00 149.38 ? 147 PRO   A N   1 
ATOM   950  C  CA  . PRO   A 1 127 ? -29.026 -6.091  -3.840  1.00 157.51 ? 147 PRO   A CA  1 
ATOM   951  C  C   . PRO   A 1 127 ? -27.632 -6.245  -3.257  1.00 159.13 ? 147 PRO   A C   1 
ATOM   952  O  O   . PRO   A 1 127 ? -26.861 -5.278  -3.257  1.00 161.02 ? 147 PRO   A O   1 
ATOM   953  C  CB  . PRO   A 1 127 ? -30.052 -5.721  -2.760  1.00 145.43 ? 147 PRO   A CB  1 
ATOM   954  C  CG  . PRO   A 1 127 ? -31.304 -6.394  -3.183  1.00 150.95 ? 147 PRO   A CG  1 
ATOM   955  C  CD  . PRO   A 1 127 ? -30.859 -7.689  -3.785  1.00 145.58 ? 147 PRO   A CD  1 
ATOM   956  N  N   . ILE   A 1 128 ? -27.284 -7.434  -2.763  1.00 156.37 ? 148 ILE   A N   1 
ATOM   957  C  CA  . ILE   A 1 128 ? -25.959 -7.643  -2.190  1.00 150.73 ? 148 ILE   A CA  1 
ATOM   958  C  C   . ILE   A 1 128 ? -24.924 -7.856  -3.288  1.00 156.81 ? 148 ILE   A C   1 
ATOM   959  O  O   . ILE   A 1 128 ? -23.824 -7.295  -3.236  1.00 163.94 ? 148 ILE   A O   1 
ATOM   960  C  CB  . ILE   A 1 128 ? -25.987 -8.818  -1.194  1.00 154.14 ? 148 ILE   A CB  1 
ATOM   961  C  CG1 . ILE   A 1 128 ? -26.524 -8.367  0.168   1.00 158.78 ? 148 ILE   A CG1 1 
ATOM   962  C  CG2 . ILE   A 1 128 ? -24.602 -9.430  -1.037  1.00 163.35 ? 148 ILE   A CG2 1 
ATOM   963  C  CD1 . ILE   A 1 128 ? -28.031 -8.225  0.238   1.00 157.38 ? 148 ILE   A CD1 1 
ATOM   964  N  N   . ILE   A 1 129 ? -25.259 -8.658  -4.302  1.00 160.69 ? 149 ILE   A N   1 
ATOM   965  C  CA  . ILE   A 1 129 ? -24.328 -8.901  -5.402  1.00 161.81 ? 149 ILE   A CA  1 
ATOM   966  C  C   . ILE   A 1 129 ? -24.039 -7.613  -6.165  1.00 177.96 ? 149 ILE   A C   1 
ATOM   967  O  O   . ILE   A 1 129 ? -22.949 -7.444  -6.729  1.00 176.24 ? 149 ILE   A O   1 
ATOM   968  C  CB  . ILE   A 1 129 ? -24.887 -10.009 -6.323  1.00 145.00 ? 149 ILE   A CB  1 
ATOM   969  C  CG1 . ILE   A 1 129 ? -24.921 -11.348 -5.583  1.00 150.42 ? 149 ILE   A CG1 1 
ATOM   970  C  CG2 . ILE   A 1 129 ? -24.062 -10.141 -7.598  1.00 146.55 ? 149 ILE   A CG2 1 
ATOM   971  C  CD1 . ILE   A 1 129 ? -25.435 -12.502 -6.417  1.00 144.31 ? 149 ILE   A CD1 1 
ATOM   972  N  N   . ALA   A 1 130 ? -24.979 -6.665  -6.153  1.00 181.36 ? 150 ALA   A N   1 
ATOM   973  C  CA  . ALA   A 1 130 ? -24.894 -5.464  -6.981  1.00 179.66 ? 150 ALA   A CA  1 
ATOM   974  C  C   . ALA   A 1 130 ? -23.783 -4.523  -6.529  1.00 182.43 ? 150 ALA   A C   1 
ATOM   975  O  O   . ALA   A 1 130 ? -23.587 -3.459  -7.127  1.00 189.85 ? 150 ALA   A O   1 
ATOM   976  C  CB  . ALA   A 1 130 ? -26.230 -4.718  -6.980  1.00 181.76 ? 150 ALA   A CB  1 
ATOM   977  N  N   . GLN   A 1 131 ? -23.054 -4.896  -5.480  1.00 172.34 ? 151 GLN   A N   1 
ATOM   978  C  CA  . GLN   A 1 131 ? -21.963 -4.066  -4.991  1.00 171.11 ? 151 GLN   A CA  1 
ATOM   979  C  C   . GLN   A 1 131 ? -20.645 -4.381  -5.692  1.00 167.97 ? 151 GLN   A C   1 
ATOM   980  O  O   . GLN   A 1 131 ? -19.985 -3.479  -6.217  1.00 174.28 ? 151 GLN   A O   1 
ATOM   981  C  CB  . GLN   A 1 131 ? -21.802 -4.237  -3.478  1.00 182.28 ? 151 GLN   A CB  1 
ATOM   982  C  CG  . GLN   A 1 131 ? -20.508 -3.645  -2.955  1.00 176.94 ? 151 GLN   A CG  1 
ATOM   983  C  CD  . GLN   A 1 131 ? -20.252 -3.960  -1.494  1.00 180.75 ? 151 GLN   A CD  1 
ATOM   984  O  OE1 . GLN   A 1 131 ? -21.160 -3.912  -0.662  1.00 188.54 ? 151 GLN   A OE1 1 
ATOM   985  N  NE2 . GLN   A 1 131 ? -19.004 -4.277  -1.173  1.00 169.49 ? 151 GLN   A NE2 1 
ATOM   986  N  N   . TYR   A 1 132 ? -20.256 -5.657  -5.719  1.00 168.98 ? 152 TYR   A N   1 
ATOM   987  C  CA  . TYR   A 1 132 ? -18.958 -6.021  -6.272  1.00 165.45 ? 152 TYR   A CA  1 
ATOM   988  C  C   . TYR   A 1 132 ? -18.928 -5.939  -7.791  1.00 167.66 ? 152 TYR   A C   1 
ATOM   989  O  O   . TYR   A 1 132 ? -17.839 -5.935  -8.374  1.00 167.63 ? 152 TYR   A O   1 
ATOM   990  C  CB  . TYR   A 1 132 ? -18.569 -7.421  -5.803  1.00 161.39 ? 152 TYR   A CB  1 
ATOM   991  C  CG  . TYR   A 1 132 ? -18.615 -7.563  -4.301  1.00 166.83 ? 152 TYR   A CG  1 
ATOM   992  C  CD1 . TYR   A 1 132 ? -17.593 -7.062  -3.506  1.00 165.61 ? 152 TYR   A CD1 1 
ATOM   993  C  CD2 . TYR   A 1 132 ? -19.689 -8.181  -3.678  1.00 160.43 ? 152 TYR   A CD2 1 
ATOM   994  C  CE1 . TYR   A 1 132 ? -17.634 -7.184  -2.132  1.00 168.05 ? 152 TYR   A CE1 1 
ATOM   995  C  CE2 . TYR   A 1 132 ? -19.740 -8.307  -2.305  1.00 169.01 ? 152 TYR   A CE2 1 
ATOM   996  C  CZ  . TYR   A 1 132 ? -18.710 -7.807  -1.538  1.00 169.27 ? 152 TYR   A CZ  1 
ATOM   997  O  OH  . TYR   A 1 132 ? -18.759 -7.932  -0.171  1.00 170.34 ? 152 TYR   A OH  1 
ATOM   998  N  N   . GLY   A 1 133 ? -20.091 -5.877  -8.442  1.00 163.10 ? 153 GLY   A N   1 
ATOM   999  C  CA  . GLY   A 1 133 ? -20.108 -5.583  -9.864  1.00 154.41 ? 153 GLY   A CA  1 
ATOM   1000 C  C   . GLY   A 1 133 ? -19.552 -4.205  -10.165 1.00 167.10 ? 153 GLY   A C   1 
ATOM   1001 O  O   . GLY   A 1 133 ? -18.866 -4.006  -11.171 1.00 174.77 ? 153 GLY   A O   1 
ATOM   1002 N  N   . ASP   A 1 134 ? -19.838 -3.234  -9.293  1.00 183.62 ? 154 ASP   A N   1 
ATOM   1003 C  CA  . ASP   A 1 134 ? -19.215 -1.921  -9.420  1.00 189.70 ? 154 ASP   A CA  1 
ATOM   1004 C  C   . ASP   A 1 134 ? -17.735 -1.983  -9.065  1.00 187.85 ? 154 ASP   A C   1 
ATOM   1005 O  O   . ASP   A 1 134 ? -16.918 -1.271  -9.659  1.00 196.64 ? 154 ASP   A O   1 
ATOM   1006 C  CB  . ASP   A 1 134 ? -19.943 -0.906  -8.539  1.00 195.00 ? 154 ASP   A CB  1 
ATOM   1007 C  CG  . ASP   A 1 134 ? -21.355 -0.630  -9.015  1.00 203.45 ? 154 ASP   A CG  1 
ATOM   1008 O  OD1 . ASP   A 1 134 ? -21.614 -0.784  -10.228 1.00 207.69 ? 154 ASP   A OD1 1 
ATOM   1009 O  OD2 . ASP   A 1 134 ? -22.206 -0.258  -8.180  1.00 207.29 ? 154 ASP   A OD2 1 
ATOM   1010 N  N   . VAL   A 1 135 ? -17.373 -2.826  -8.094  1.00 174.91 ? 155 VAL   A N   1 
ATOM   1011 C  CA  . VAL   A 1 135 ? -15.963 -3.109  -7.850  1.00 167.90 ? 155 VAL   A CA  1 
ATOM   1012 C  C   . VAL   A 1 135 ? -15.357 -3.811  -9.056  1.00 176.74 ? 155 VAL   A C   1 
ATOM   1013 O  O   . VAL   A 1 135 ? -14.173 -3.630  -9.365  1.00 175.69 ? 155 VAL   A O   1 
ATOM   1014 C  CB  . VAL   A 1 135 ? -15.799 -3.943  -6.563  1.00 162.57 ? 155 VAL   A CB  1 
ATOM   1015 C  CG1 . VAL   A 1 135 ? -14.327 -4.178  -6.256  1.00 158.45 ? 155 VAL   A CG1 1 
ATOM   1016 C  CG2 . VAL   A 1 135 ? -16.489 -3.258  -5.393  1.00 154.65 ? 155 VAL   A CG2 1 
ATOM   1017 N  N   . LEU   A 1 136 ? -16.159 -4.610  -9.765  1.00 169.16 ? 156 LEU   A N   1 
ATOM   1018 C  CA  . LEU   A 1 136 ? -15.677 -5.282  -10.967 1.00 154.90 ? 156 LEU   A CA  1 
ATOM   1019 C  C   . LEU   A 1 136 ? -15.475 -4.296  -12.111 1.00 160.62 ? 156 LEU   A C   1 
ATOM   1020 O  O   . LEU   A 1 136 ? -14.471 -4.368  -12.830 1.00 163.40 ? 156 LEU   A O   1 
ATOM   1021 C  CB  . LEU   A 1 136 ? -16.657 -6.385  -11.368 1.00 145.33 ? 156 LEU   A CB  1 
ATOM   1022 C  CG  . LEU   A 1 136 ? -16.416 -7.144  -12.672 1.00 149.57 ? 156 LEU   A CG  1 
ATOM   1023 C  CD1 . LEU   A 1 136 ? -15.039 -7.776  -12.679 1.00 138.77 ? 156 LEU   A CD1 1 
ATOM   1024 C  CD2 . LEU   A 1 136 ? -17.488 -8.204  -12.859 1.00 152.30 ? 156 LEU   A CD2 1 
ATOM   1025 N  N   . VAL   A 1 137 ? -16.418 -3.369  -12.296 1.00 161.34 ? 157 VAL   A N   1 
ATOM   1026 C  CA  . VAL   A 1 137 ? -16.274 -2.365  -13.346 1.00 168.17 ? 157 VAL   A CA  1 
ATOM   1027 C  C   . VAL   A 1 137 ? -15.115 -1.427  -13.034 1.00 180.17 ? 157 VAL   A C   1 
ATOM   1028 O  O   . VAL   A 1 137 ? -14.308 -1.101  -13.913 1.00 171.91 ? 157 VAL   A O   1 
ATOM   1029 C  CB  . VAL   A 1 137 ? -17.594 -1.593  -13.533 1.00 162.72 ? 157 VAL   A CB  1 
ATOM   1030 C  CG1 . VAL   A 1 137 ? -17.401 -0.432  -14.496 1.00 172.81 ? 157 VAL   A CG1 1 
ATOM   1031 C  CG2 . VAL   A 1 137 ? -18.686 -2.524  -14.032 1.00 160.72 ? 157 VAL   A CG2 1 
ATOM   1032 N  N   . ARG   A 1 138 ? -15.007 -0.984  -11.779 1.00 185.46 ? 158 ARG   A N   1 
ATOM   1033 C  CA  . ARG   A 1 138 ? -13.930 -0.072  -11.410 1.00 184.68 ? 158 ARG   A CA  1 
ATOM   1034 C  C   . ARG   A 1 138 ? -12.569 -0.755  -11.461 1.00 183.53 ? 158 ARG   A C   1 
ATOM   1035 O  O   . ARG   A 1 138 ? -11.566 -0.106  -11.779 1.00 195.20 ? 158 ARG   A O   1 
ATOM   1036 C  CB  . ARG   A 1 138 ? -14.189 0.510   -10.021 1.00 190.62 ? 158 ARG   A CB  1 
ATOM   1037 C  CG  . ARG   A 1 138 ? -14.253 2.030   -9.989  1.00 201.95 ? 158 ARG   A CG  1 
ATOM   1038 C  CD  . ARG   A 1 138 ? -14.593 2.550   -8.599  1.00 203.59 ? 158 ARG   A CD  1 
ATOM   1039 N  NE  . ARG   A 1 138 ? -13.769 1.935   -7.565  1.00 208.79 ? 158 ARG   A NE  1 
ATOM   1040 C  CZ  . ARG   A 1 138 ? -14.205 1.031   -6.698  1.00 207.13 ? 158 ARG   A CZ  1 
ATOM   1041 N  NH1 . ARG   A 1 138 ? -15.466 0.631   -6.693  1.00 204.11 ? 158 ARG   A NH1 1 
ATOM   1042 N  NH2 . ARG   A 1 138 ? -13.355 0.516   -5.815  1.00 205.51 ? 158 ARG   A NH2 1 
ATOM   1043 N  N   . ASN   A 1 139 ? -12.508 -2.053  -11.150 1.00 172.20 ? 159 ASN   A N   1 
ATOM   1044 C  CA  . ASN   A 1 139 ? -11.261 -2.788  -11.338 1.00 175.19 ? 159 ASN   A CA  1 
ATOM   1045 C  C   . ASN   A 1 139 ? -10.948 -2.980  -12.816 1.00 168.47 ? 159 ASN   A C   1 
ATOM   1046 O  O   . ASN   A 1 139 ? -9.774  -3.047  -13.196 1.00 176.10 ? 159 ASN   A O   1 
ATOM   1047 C  CB  . ASN   A 1 139 ? -11.323 -4.143  -10.629 1.00 175.08 ? 159 ASN   A CB  1 
ATOM   1048 C  CG  . ASN   A 1 139 ? -11.047 -4.037  -9.139  1.00 180.33 ? 159 ASN   A CG  1 
ATOM   1049 O  OD1 . ASN   A 1 139 ? -10.353 -3.127  -8.687  1.00 187.49 ? 159 ASN   A OD1 1 
ATOM   1050 N  ND2 . ASN   A 1 139 ? -11.585 -4.977  -8.369  1.00 161.67 ? 159 ASN   A ND2 1 
ATOM   1051 N  N   . LEU   A 1 140 ? -11.978 -3.072  -13.660 1.00 170.08 ? 160 LEU   A N   1 
ATOM   1052 C  CA  . LEU   A 1 140 ? -11.771 -3.153  -15.100 1.00 166.49 ? 160 LEU   A CA  1 
ATOM   1053 C  C   . LEU   A 1 140 ? -11.582 -1.785  -15.740 1.00 179.48 ? 160 LEU   A C   1 
ATOM   1054 O  O   . LEU   A 1 140 ? -11.038 -1.704  -16.847 1.00 185.94 ? 160 LEU   A O   1 
ATOM   1055 C  CB  . LEU   A 1 140 ? -12.947 -3.875  -15.764 1.00 156.36 ? 160 LEU   A CB  1 
ATOM   1056 C  CG  . LEU   A 1 140 ? -12.921 -5.402  -15.697 1.00 153.29 ? 160 LEU   A CG  1 
ATOM   1057 C  CD1 . LEU   A 1 140 ? -14.160 -5.991  -16.351 1.00 150.90 ? 160 LEU   A CD1 1 
ATOM   1058 C  CD2 . LEU   A 1 140 ? -11.660 -5.932  -16.360 1.00 145.68 ? 160 LEU   A CD2 1 
ATOM   1059 N  N   . ARG   A 1 141 ? -12.015 -0.715  -15.071 1.00 181.54 ? 161 ARG   A N   1 
ATOM   1060 C  CA  . ARG   A 1 141 ? -11.840 0.628   -15.609 1.00 180.43 ? 161 ARG   A CA  1 
ATOM   1061 C  C   . ARG   A 1 141 ? -10.396 1.108   -15.497 1.00 195.31 ? 161 ARG   A C   1 
ATOM   1062 O  O   . ARG   A 1 141 ? -9.995  2.012   -16.240 1.00 214.19 ? 161 ARG   A O   1 
ATOM   1063 C  CB  . ARG   A 1 141 ? -12.786 1.596   -14.892 1.00 174.00 ? 161 ARG   A CB  1 
ATOM   1064 C  CG  . ARG   A 1 141 ? -12.788 3.015   -15.435 1.00 178.97 ? 161 ARG   A CG  1 
ATOM   1065 C  CD  . ARG   A 1 141 ? -14.150 3.660   -15.269 1.00 173.60 ? 161 ARG   A CD  1 
ATOM   1066 N  NE  . ARG   A 1 141 ? -15.072 3.245   -16.319 1.00 174.43 ? 161 ARG   A NE  1 
ATOM   1067 C  CZ  . ARG   A 1 141 ? -16.381 3.451   -16.291 1.00 186.71 ? 161 ARG   A CZ  1 
ATOM   1068 N  NH1 . ARG   A 1 141 ? -16.966 4.040   -15.261 1.00 183.53 ? 161 ARG   A NH1 1 
ATOM   1069 N  NH2 . ARG   A 1 141 ? -17.123 3.053   -17.321 1.00 196.43 ? 161 ARG   A NH2 1 
ATOM   1070 N  N   . ARG   A 1 142 ? -9.601  0.509   -14.607 1.00 200.76 ? 162 ARG   A N   1 
ATOM   1071 C  CA  . ARG   A 1 142 ? -8.207  0.897   -14.425 1.00 213.39 ? 162 ARG   A CA  1 
ATOM   1072 C  C   . ARG   A 1 142 ? -7.281  0.268   -15.463 1.00 222.17 ? 162 ARG   A C   1 
ATOM   1073 O  O   . ARG   A 1 142 ? -6.352  0.929   -15.941 1.00 224.72 ? 162 ARG   A O   1 
ATOM   1074 C  CB  . ARG   A 1 142 ? -7.745  0.520   -13.018 1.00 211.77 ? 162 ARG   A CB  1 
ATOM   1075 C  CG  . ARG   A 1 142 ? -8.482  1.269   -11.919 1.00 199.75 ? 162 ARG   A CG  1 
ATOM   1076 C  CD  . ARG   A 1 142 ? -8.167  0.701   -10.549 1.00 200.51 ? 162 ARG   A CD  1 
ATOM   1077 N  NE  . ARG   A 1 142 ? -8.772  1.488   -9.481  1.00 203.33 ? 162 ARG   A NE  1 
ATOM   1078 C  CZ  . ARG   A 1 142 ? -8.763  1.141   -8.202  1.00 206.22 ? 162 ARG   A CZ  1 
ATOM   1079 N  NH1 . ARG   A 1 142 ? -8.205  0.013   -7.796  1.00 212.34 ? 162 ARG   A NH1 1 
ATOM   1080 N  NH2 . ARG   A 1 142 ? -9.328  1.947   -7.307  1.00 198.96 ? 162 ARG   A NH2 1 
ATOM   1081 N  N   . GLU   A 1 143 ? -7.555  -0.988  -15.813 1.00 216.20 ? 163 GLU   A N   1 
ATOM   1082 C  CA  . GLU   A 1 143 ? -6.768  -1.645  -16.886 1.00 216.08 ? 163 GLU   A CA  1 
ATOM   1083 C  C   . GLU   A 1 143 ? -7.207  -1.017  -18.204 1.00 215.37 ? 163 GLU   A C   1 
ATOM   1084 O  O   . GLU   A 1 143 ? -6.388  -0.954  -19.136 1.00 215.72 ? 163 GLU   A O   1 
ATOM   1085 C  CB  . GLU   A 1 143 ? -7.023  -3.150  -16.887 1.00 213.22 ? 163 GLU   A CB  1 
ATOM   1086 C  CG  . GLU   A 1 143 ? -7.949  -3.602  -15.773 1.00 219.15 ? 163 GLU   A CG  1 
ATOM   1087 C  CD  . GLU   A 1 143 ? -7.289  -3.743  -14.412 1.00 215.55 ? 163 GLU   A CD  1 
ATOM   1088 O  OE1 . GLU   A 1 143 ? -7.331  -4.855  -13.851 1.00 211.33 ? 163 GLU   A OE1 1 
ATOM   1089 O  OE2 . GLU   A 1 143 ? -6.745  -2.739  -13.910 1.00 216.20 ? 163 GLU   A OE2 1 
ATOM   1090 N  N   . ALA   A 1 144 ? -8.460  -0.565  -18.261 1.00 226.46 ? 164 ALA   A N   1 
ATOM   1091 C  CA  . ALA   A 1 144 ? -8.958  0.117   -19.475 1.00 218.96 ? 164 ALA   A CA  1 
ATOM   1092 C  C   . ALA   A 1 144 ? -7.976  1.226   -19.850 1.00 229.63 ? 164 ALA   A C   1 
ATOM   1093 O  O   . ALA   A 1 144 ? -7.421  1.176   -20.963 1.00 222.28 ? 164 ALA   A O   1 
ATOM   1094 C  CB  . ALA   A 1 144 ? -10.331 0.671   -19.207 1.00 197.83 ? 164 ALA   A CB  1 
ATOM   1095 N  N   . GLU   A 1 145 ? -7.774  2.185   -18.943 1.00 255.82 ? 165 GLU   A N   1 
ATOM   1096 C  CA  . GLU   A 1 145 ? -6.820  3.294   -19.199 1.00 263.81 ? 165 GLU   A CA  1 
ATOM   1097 C  C   . GLU   A 1 145 ? -5.458  2.696   -19.555 1.00 255.33 ? 165 GLU   A C   1 
ATOM   1098 O  O   . GLU   A 1 145 ? -4.836  3.182   -20.516 1.00 263.01 ? 165 GLU   A O   1 
ATOM   1099 C  CB  . GLU   A 1 145 ? -6.715  4.199   -17.972 1.00 269.97 ? 165 GLU   A CB  1 
ATOM   1100 C  CG  . GLU   A 1 145 ? -7.943  4.161   -17.084 1.00 281.01 ? 165 GLU   A CG  1 
ATOM   1101 C  CD  . GLU   A 1 145 ? -7.643  3.996   -15.605 1.00 280.85 ? 165 GLU   A CD  1 
ATOM   1102 O  OE1 . GLU   A 1 145 ? -6.475  3.719   -15.267 1.00 287.00 ? 165 GLU   A OE1 1 
ATOM   1103 O  OE2 . GLU   A 1 145 ? -8.578  4.144   -14.794 1.00 280.26 ? 165 GLU   A OE2 1 
ATOM   1104 N  N   . THR   A 1 146 ? -5.029  1.669   -18.818 1.00 234.78 ? 166 THR   A N   1 
ATOM   1105 C  CA  . THR   A 1 146 ? -3.718  1.023   -19.086 1.00 226.43 ? 166 THR   A CA  1 
ATOM   1106 C  C   . THR   A 1 146 ? -3.641  0.637   -20.565 1.00 224.66 ? 166 THR   A C   1 
ATOM   1107 O  O   . THR   A 1 146 ? -2.519  0.396   -21.043 1.00 220.81 ? 166 THR   A O   1 
ATOM   1108 C  CB  . THR   A 1 146 ? -3.492  -0.175  -18.159 1.00 218.14 ? 166 THR   A CB  1 
ATOM   1109 O  OG1 . THR   A 1 146 ? -4.108  0.116   -16.905 1.00 193.33 ? 166 THR   A OG1 1 
ATOM   1110 C  CG2 . THR   A 1 146 ? -2.027  -0.480  -17.941 1.00 223.64 ? 166 THR   A CG2 1 
ATOM   1111 N  N   . GLY   A 1 147 ? -4.786  0.597   -21.254 1.00 231.09 ? 167 GLY   A N   1 
ATOM   1112 C  CA  . GLY   A 1 147 ? -4.801  0.287   -22.697 1.00 231.62 ? 167 GLY   A CA  1 
ATOM   1113 C  C   . GLY   A 1 147 ? -3.983  -0.911  -23.143 1.00 219.12 ? 167 GLY   A C   1 
ATOM   1114 O  O   . GLY   A 1 147 ? -3.153  -0.749  -24.059 1.00 214.61 ? 167 GLY   A O   1 
ATOM   1115 N  N   . LYS   A 1 148 ? -4.209  -2.070  -22.520 1.00 204.57 ? 168 LYS   A N   1 
ATOM   1116 C  CA  . LYS   A 1 148 ? -3.401  -3.281  -22.809 1.00 197.60 ? 168 LYS   A CA  1 
ATOM   1117 C  C   . LYS   A 1 148 ? -4.271  -4.528  -22.659 1.00 187.27 ? 168 LYS   A C   1 
ATOM   1118 O  O   . LYS   A 1 148 ? -5.421  -4.394  -22.206 1.00 189.56 ? 168 LYS   A O   1 
ATOM   1119 C  CB  . LYS   A 1 148 ? -2.233  -3.311  -21.821 1.00 199.97 ? 168 LYS   A CB  1 
ATOM   1120 C  CG  . LYS   A 1 148 ? -2.559  -2.808  -20.423 1.00 210.73 ? 168 LYS   A CG  1 
ATOM   1121 C  CD  . LYS   A 1 148 ? -2.871  -3.916  -19.445 1.00 208.79 ? 168 LYS   A CD  1 
ATOM   1122 C  CE  . LYS   A 1 148 ? -4.233  -3.768  -18.804 1.00 210.64 ? 168 LYS   A CE  1 
ATOM   1123 N  NZ  . LYS   A 1 148 ? -5.239  -3.264  -19.768 1.00 189.40 ? 168 LYS   A NZ  1 
ATOM   1124 N  N   . PRO   A 1 149 ? -3.781  -5.731  -23.022 1.00 183.50 ? 169 PRO   A N   1 
ATOM   1125 C  CA  . PRO   A 1 149 ? -4.542  -6.968  -22.830 1.00 188.88 ? 169 PRO   A CA  1 
ATOM   1126 C  C   . PRO   A 1 149 ? -4.984  -7.141  -21.369 1.00 195.84 ? 169 PRO   A C   1 
ATOM   1127 O  O   . PRO   A 1 149 ? -4.396  -6.515  -20.510 1.00 202.14 ? 169 PRO   A O   1 
ATOM   1128 C  CB  . PRO   A 1 149 ? -3.523  -8.055  -23.192 1.00 175.99 ? 169 PRO   A CB  1 
ATOM   1129 C  CG  . PRO   A 1 149 ? -2.190  -7.353  -23.087 1.00 168.92 ? 169 PRO   A CG  1 
ATOM   1130 C  CD  . PRO   A 1 149 ? -2.477  -5.974  -23.630 1.00 179.48 ? 169 PRO   A CD  1 
ATOM   1131 N  N   . VAL   A 1 150 ? -5.992  -7.986  -21.124 1.00 184.97 ? 170 VAL   A N   1 
ATOM   1132 C  CA  . VAL   A 1 150 ? -6.521  -8.190  -19.741 1.00 188.75 ? 170 VAL   A CA  1 
ATOM   1133 C  C   . VAL   A 1 150 ? -6.769  -9.682  -19.512 1.00 191.98 ? 170 VAL   A C   1 
ATOM   1134 O  O   . VAL   A 1 150 ? -7.286  -10.336 -20.437 1.00 183.76 ? 170 VAL   A O   1 
ATOM   1135 C  CB  . VAL   A 1 150 ? -7.813  -7.382  -19.521 1.00 175.68 ? 170 VAL   A CB  1 
ATOM   1136 C  CG1 . VAL   A 1 150 ? -8.643  -7.937  -18.374 1.00 172.59 ? 170 VAL   A CG1 1 
ATOM   1137 C  CG2 . VAL   A 1 150 ? -7.525  -5.904  -19.312 1.00 190.23 ? 170 VAL   A CG2 1 
ATOM   1138 N  N   . THR   A 1 151 ? -6.407  -10.206 -18.336 1.00 213.50 ? 171 THR   A N   1 
ATOM   1139 C  CA  . THR   A 1 151 ? -6.741  -11.600 -18.060 1.00 208.55 ? 171 THR   A CA  1 
ATOM   1140 C  C   . THR   A 1 151 ? -8.123  -11.638 -17.421 1.00 203.07 ? 171 THR   A C   1 
ATOM   1141 O  O   . THR   A 1 151 ? -8.311  -11.132 -16.309 1.00 205.08 ? 171 THR   A O   1 
ATOM   1142 C  CB  . THR   A 1 151 ? -5.694  -12.238 -17.149 1.00 210.70 ? 171 THR   A CB  1 
ATOM   1143 O  OG1 . THR   A 1 151 ? -5.658  -11.546 -15.895 1.00 212.98 ? 171 THR   A OG1 1 
ATOM   1144 C  CG2 . THR   A 1 151 ? -4.318  -12.171 -17.795 1.00 213.08 ? 171 THR   A CG2 1 
ATOM   1145 N  N   . LEU   A 1 152 ? -9.093  -12.224 -18.123 1.00 176.15 ? 172 LEU   A N   1 
ATOM   1146 C  CA  . LEU   A 1 152 ? -10.476 -12.169 -17.663 1.00 161.52 ? 172 LEU   A CA  1 
ATOM   1147 C  C   . LEU   A 1 152 ? -10.684 -12.984 -16.394 1.00 157.47 ? 172 LEU   A C   1 
ATOM   1148 O  O   . LEU   A 1 152 ? -11.340 -12.519 -15.455 1.00 153.28 ? 172 LEU   A O   1 
ATOM   1149 C  CB  . LEU   A 1 152 ? -11.406 -12.646 -18.774 1.00 156.78 ? 172 LEU   A CB  1 
ATOM   1150 C  CG  . LEU   A 1 152 ? -11.336 -11.782 -20.032 1.00 155.83 ? 172 LEU   A CG  1 
ATOM   1151 C  CD1 . LEU   A 1 152 ? -12.064 -12.452 -21.176 1.00 150.24 ? 172 LEU   A CD1 1 
ATOM   1152 C  CD2 . LEU   A 1 152 ? -11.910 -10.399 -19.757 1.00 148.12 ? 172 LEU   A CD2 1 
ATOM   1153 N  N   . LYS   A 1 153 ? -10.120 -14.192 -16.340 1.00 159.58 ? 173 LYS   A N   1 
ATOM   1154 C  CA  . LYS   A 1 153 ? -10.397 -15.083 -15.219 1.00 150.97 ? 173 LYS   A CA  1 
ATOM   1155 C  C   . LYS   A 1 153 ? -9.879  -14.518 -13.902 1.00 158.41 ? 173 LYS   A C   1 
ATOM   1156 O  O   . LYS   A 1 153 ? -10.404 -14.854 -12.835 1.00 150.16 ? 173 LYS   A O   1 
ATOM   1157 C  CB  . LYS   A 1 153 ? -9.794  -16.461 -15.491 1.00 148.25 ? 173 LYS   A CB  1 
ATOM   1158 C  CG  . LYS   A 1 153 ? -10.508 -17.604 -14.789 1.00 115.84 ? 173 LYS   A CG  1 
ATOM   1159 C  CD  . LYS   A 1 153 ? -10.243 -18.920 -15.502 1.00 126.97 ? 173 LYS   A CD  1 
ATOM   1160 C  CE  . LYS   A 1 153 ? -10.933 -20.080 -14.809 1.00 128.43 ? 173 LYS   A CE  1 
ATOM   1161 N  NZ  . LYS   A 1 153 ? -10.820 -21.336 -15.601 1.00 147.59 ? 173 LYS   A NZ  1 
ATOM   1162 N  N   . ASP   A 1 154 ? -8.861  -13.656 -13.953 1.00 156.89 ? 174 ASP   A N   1 
ATOM   1163 C  CA  . ASP   A 1 154 ? -8.375  -13.010 -12.738 1.00 159.26 ? 174 ASP   A CA  1 
ATOM   1164 C  C   . ASP   A 1 154 ? -9.401  -12.020 -12.200 1.00 150.27 ? 174 ASP   A C   1 
ATOM   1165 O  O   . ASP   A 1 154 ? -9.815  -12.103 -11.038 1.00 140.50 ? 174 ASP   A O   1 
ATOM   1166 C  CB  . ASP   A 1 154 ? -7.042  -12.309 -13.012 1.00 181.31 ? 174 ASP   A CB  1 
ATOM   1167 C  CG  . ASP   A 1 154 ? -5.915  -13.285 -13.276 1.00 188.76 ? 174 ASP   A CG  1 
ATOM   1168 O  OD1 . ASP   A 1 154 ? -6.145  -14.507 -13.161 1.00 178.20 ? 174 ASP   A OD1 1 
ATOM   1169 O  OD2 . ASP   A 1 154 ? -4.798  -12.830 -13.599 1.00 197.08 ? 174 ASP   A OD2 1 
ATOM   1170 N  N   . VAL   A 1 155 ? -9.826  -11.071 -13.038 1.00 162.22 ? 175 VAL   A N   1 
ATOM   1171 C  CA  . VAL   A 1 155 ? -10.801 -10.079 -12.604 1.00 150.98 ? 175 VAL   A CA  1 
ATOM   1172 C  C   . VAL   A 1 155 ? -12.187 -10.694 -12.442 1.00 148.20 ? 175 VAL   A C   1 
ATOM   1173 O  O   . VAL   A 1 155 ? -13.005 -10.173 -11.673 1.00 143.10 ? 175 VAL   A O   1 
ATOM   1174 C  CB  . VAL   A 1 155 ? -10.821 -8.891  -13.587 1.00 148.21 ? 175 VAL   A CB  1 
ATOM   1175 C  CG1 . VAL   A 1 155 ? -11.526 -9.268  -14.883 1.00 147.18 ? 175 VAL   A CG1 1 
ATOM   1176 C  CG2 . VAL   A 1 155 ? -11.458 -7.667  -12.944 1.00 144.20 ? 175 VAL   A CG2 1 
ATOM   1177 N  N   . PHE   A 1 156 ? -12.473 -11.797 -13.139 1.00 155.22 ? 176 PHE   A N   1 
ATOM   1178 C  CA  . PHE   A 1 156 ? -13.725 -12.514 -12.916 1.00 139.30 ? 176 PHE   A CA  1 
ATOM   1179 C  C   . PHE   A 1 156 ? -13.667 -13.342 -11.639 1.00 137.78 ? 176 PHE   A C   1 
ATOM   1180 O  O   . PHE   A 1 156 ? -14.625 -13.350 -10.857 1.00 145.14 ? 176 PHE   A O   1 
ATOM   1181 C  CB  . PHE   A 1 156 ? -14.045 -13.412 -14.112 1.00 136.53 ? 176 PHE   A CB  1 
ATOM   1182 C  CG  . PHE   A 1 156 ? -14.591 -12.672 -15.298 1.00 144.48 ? 176 PHE   A CG  1 
ATOM   1183 C  CD1 . PHE   A 1 156 ? -15.429 -11.583 -15.125 1.00 145.45 ? 176 PHE   A CD1 1 
ATOM   1184 C  CD2 . PHE   A 1 156 ? -14.265 -13.064 -16.586 1.00 137.43 ? 176 PHE   A CD2 1 
ATOM   1185 C  CE1 . PHE   A 1 156 ? -15.934 -10.900 -16.214 1.00 141.95 ? 176 PHE   A CE1 1 
ATOM   1186 C  CE2 . PHE   A 1 156 ? -14.766 -12.384 -17.678 1.00 133.14 ? 176 PHE   A CE2 1 
ATOM   1187 C  CZ  . PHE   A 1 156 ? -15.601 -11.300 -17.492 1.00 135.03 ? 176 PHE   A CZ  1 
ATOM   1188 N  N   . GLY   A 1 157 ? -12.556 -14.047 -11.416 1.00 146.81 ? 177 GLY   A N   1 
ATOM   1189 C  CA  . GLY   A 1 157 ? -12.414 -14.815 -10.191 1.00 141.75 ? 177 GLY   A CA  1 
ATOM   1190 C  C   . GLY   A 1 157 ? -12.366 -13.934 -8.958  1.00 152.28 ? 177 GLY   A C   1 
ATOM   1191 O  O   . GLY   A 1 157 ? -12.912 -14.289 -7.909  1.00 143.69 ? 177 GLY   A O   1 
ATOM   1192 N  N   . ALA   A 1 158 ? -11.706 -12.778 -9.063  1.00 152.51 ? 178 ALA   A N   1 
ATOM   1193 C  CA  . ALA   A 1 158 ? -11.731 -11.811 -7.972  1.00 148.38 ? 178 ALA   A CA  1 
ATOM   1194 C  C   . ALA   A 1 158 ? -13.152 -11.339 -7.695  1.00 146.01 ? 178 ALA   A C   1 
ATOM   1195 O  O   . ALA   A 1 158 ? -13.549 -11.178 -6.535  1.00 149.23 ? 178 ALA   A O   1 
ATOM   1196 C  CB  . ALA   A 1 158 ? -10.824 -10.625 -8.300  1.00 154.39 ? 178 ALA   A CB  1 
ATOM   1197 N  N   . TYR   A 1 159 ? -13.934 -11.116 -8.752  1.00 142.78 ? 179 TYR   A N   1 
ATOM   1198 C  CA  . TYR   A 1 159 ? -15.344 -10.786 -8.579  1.00 139.57 ? 179 TYR   A CA  1 
ATOM   1199 C  C   . TYR   A 1 159 ? -16.117 -11.970 -8.012  1.00 143.85 ? 179 TYR   A C   1 
ATOM   1200 O  O   . TYR   A 1 159 ? -16.898 -11.820 -7.066  1.00 140.45 ? 179 TYR   A O   1 
ATOM   1201 C  CB  . TYR   A 1 159 ? -15.943 -10.340 -9.915  1.00 138.84 ? 179 TYR   A CB  1 
ATOM   1202 C  CG  . TYR   A 1 159 ? -17.434 -10.578 -10.031 1.00 147.64 ? 179 TYR   A CG  1 
ATOM   1203 C  CD1 . TYR   A 1 159 ? -18.344 -9.673  -9.503  1.00 153.95 ? 179 TYR   A CD1 1 
ATOM   1204 C  CD2 . TYR   A 1 159 ? -17.930 -11.707 -10.675 1.00 147.73 ? 179 TYR   A CD2 1 
ATOM   1205 C  CE1 . TYR   A 1 159 ? -19.706 -9.886  -9.607  1.00 146.77 ? 179 TYR   A CE1 1 
ATOM   1206 C  CE2 . TYR   A 1 159 ? -19.289 -11.930 -10.780 1.00 139.68 ? 179 TYR   A CE2 1 
ATOM   1207 C  CZ  . TYR   A 1 159 ? -20.173 -11.016 -10.246 1.00 139.56 ? 179 TYR   A CZ  1 
ATOM   1208 O  OH  . TYR   A 1 159 ? -21.528 -11.231 -10.351 1.00 120.36 ? 179 TYR   A OH  1 
ATOM   1209 N  N   . SER   A 1 160 ? -15.908 -13.160 -8.583  1.00 158.16 ? 180 SER   A N   1 
ATOM   1210 C  CA  . SER   A 1 160 ? -16.675 -14.331 -8.170  1.00 140.24 ? 180 SER   A CA  1 
ATOM   1211 C  C   . SER   A 1 160 ? -16.397 -14.695 -6.717  1.00 143.31 ? 180 SER   A C   1 
ATOM   1212 O  O   . SER   A 1 160 ? -17.301 -15.134 -5.996  1.00 137.80 ? 180 SER   A O   1 
ATOM   1213 C  CB  . SER   A 1 160 ? -16.362 -15.512 -9.089  1.00 138.88 ? 180 SER   A CB  1 
ATOM   1214 O  OG  . SER   A 1 160 ? -16.564 -15.169 -10.449 1.00 142.50 ? 180 SER   A OG  1 
ATOM   1215 N  N   . MET   A 1 161 ? -15.151 -14.522 -6.268  1.00 148.82 ? 181 MET   A N   1 
ATOM   1216 C  CA  . MET   A 1 161 ? -14.831 -14.787 -4.869  1.00 149.30 ? 181 MET   A CA  1 
ATOM   1217 C  C   . MET   A 1 161 ? -15.492 -13.772 -3.944  1.00 151.22 ? 181 MET   A C   1 
ATOM   1218 O  O   . MET   A 1 161 ? -15.898 -14.123 -2.830  1.00 143.12 ? 181 MET   A O   1 
ATOM   1219 C  CB  . MET   A 1 161 ? -13.316 -14.791 -4.665  1.00 156.07 ? 181 MET   A CB  1 
ATOM   1220 C  CG  . MET   A 1 161 ? -12.884 -15.097 -3.239  1.00 155.98 ? 181 MET   A CG  1 
ATOM   1221 S  SD  . MET   A 1 161 ? -13.475 -16.698 -2.653  1.00 168.93 ? 181 MET   A SD  1 
ATOM   1222 C  CE  . MET   A 1 161 ? -12.554 -17.810 -3.712  1.00 139.72 ? 181 MET   A CE  1 
ATOM   1223 N  N   . ASP   A 1 162 ? -15.616 -12.518 -4.387  1.00 159.33 ? 182 ASP   A N   1 
ATOM   1224 C  CA  . ASP   A 1 162 ? -16.320 -11.517 -3.591  1.00 162.03 ? 182 ASP   A CA  1 
ATOM   1225 C  C   . ASP   A 1 162 ? -17.789 -11.873 -3.417  1.00 156.68 ? 182 ASP   A C   1 
ATOM   1226 O  O   . ASP   A 1 162 ? -18.380 -11.587 -2.370  1.00 160.14 ? 182 ASP   A O   1 
ATOM   1227 C  CB  . ASP   A 1 162 ? -16.191 -10.141 -4.242  1.00 166.57 ? 182 ASP   A CB  1 
ATOM   1228 C  CG  . ASP   A 1 162 ? -14.779 -9.603  -4.195  1.00 173.69 ? 182 ASP   A CG  1 
ATOM   1229 O  OD1 . ASP   A 1 162 ? -13.909 -10.291 -3.622  1.00 179.82 ? 182 ASP   A OD1 1 
ATOM   1230 O  OD2 . ASP   A 1 162 ? -14.539 -8.495  -4.724  1.00 174.16 ? 182 ASP   A OD2 1 
ATOM   1231 N  N   . VAL   A 1 163 ? -18.394 -12.493 -4.430  1.00 152.46 ? 183 VAL   A N   1 
ATOM   1232 C  CA  . VAL   A 1 163 ? -19.813 -12.823 -4.364  1.00 153.45 ? 183 VAL   A CA  1 
ATOM   1233 C  C   . VAL   A 1 163 ? -20.049 -14.039 -3.476  1.00 158.64 ? 183 VAL   A C   1 
ATOM   1234 O  O   . VAL   A 1 163 ? -20.996 -14.068 -2.684  1.00 163.89 ? 183 VAL   A O   1 
ATOM   1235 C  CB  . VAL   A 1 163 ? -20.371 -13.039 -5.783  1.00 145.85 ? 183 VAL   A CB  1 
ATOM   1236 C  CG1 . VAL   A 1 163 ? -21.860 -13.350 -5.737  1.00 135.63 ? 183 VAL   A CG1 1 
ATOM   1237 C  CG2 . VAL   A 1 163 ? -20.107 -11.819 -6.652  1.00 145.10 ? 183 VAL   A CG2 1 
ATOM   1238 N  N   . ILE   A 1 164 ? -19.190 -15.057 -3.580  1.00 148.37 ? 184 ILE   A N   1 
ATOM   1239 C  CA  . ILE   A 1 164 ? -19.443 -16.314 -2.878  1.00 148.27 ? 184 ILE   A CA  1 
ATOM   1240 C  C   . ILE   A 1 164 ? -19.217 -16.168 -1.376  1.00 147.36 ? 184 ILE   A C   1 
ATOM   1241 O  O   . ILE   A 1 164 ? -19.914 -16.803 -0.575  1.00 141.76 ? 184 ILE   A O   1 
ATOM   1242 C  CB  . ILE   A 1 164 ? -18.590 -17.445 -3.487  1.00 149.11 ? 184 ILE   A CB  1 
ATOM   1243 C  CG1 . ILE   A 1 164 ? -19.494 -18.569 -3.981  1.00 132.24 ? 184 ILE   A CG1 1 
ATOM   1244 C  CG2 . ILE   A 1 164 ? -17.583 -17.997 -2.484  1.00 146.25 ? 184 ILE   A CG2 1 
ATOM   1245 C  CD1 . ILE   A 1 164 ? -20.318 -19.216 -2.893  1.00 134.68 ? 184 ILE   A CD1 1 
ATOM   1246 N  N   . THR   A 1 165 ? -18.260 -15.332 -0.963  1.00 154.67 ? 185 THR   A N   1 
ATOM   1247 C  CA  . THR   A 1 165 ? -18.007 -15.152 0.461   1.00 149.64 ? 185 THR   A CA  1 
ATOM   1248 C  C   . THR   A 1 165 ? -19.092 -14.328 1.144   1.00 166.24 ? 185 THR   A C   1 
ATOM   1249 O  O   . THR   A 1 165 ? -19.287 -14.469 2.356   1.00 172.26 ? 185 THR   A O   1 
ATOM   1250 C  CB  . THR   A 1 165 ? -16.644 -14.493 0.675   1.00 156.55 ? 185 THR   A CB  1 
ATOM   1251 O  OG1 . THR   A 1 165 ? -16.568 -13.285 -0.092  1.00 165.51 ? 185 THR   A OG1 1 
ATOM   1252 C  CG2 . THR   A 1 165 ? -15.519 -15.432 0.251   1.00 157.09 ? 185 THR   A CG2 1 
ATOM   1253 N  N   . SER   A 1 166 ? -19.801 -13.480 0.398   1.00 174.87 ? 186 SER   A N   1 
ATOM   1254 C  CA  . SER   A 1 166 ? -20.854 -12.635 0.948   1.00 178.10 ? 186 SER   A CA  1 
ATOM   1255 C  C   . SER   A 1 166 ? -22.251 -13.217 0.786   1.00 175.97 ? 186 SER   A C   1 
ATOM   1256 O  O   . SER   A 1 166 ? -23.097 -13.011 1.662   1.00 179.91 ? 186 SER   A O   1 
ATOM   1257 C  CB  . SER   A 1 166 ? -20.812 -11.246 0.298   1.00 174.90 ? 186 SER   A CB  1 
ATOM   1258 O  OG  . SER   A 1 166 ? -20.597 -11.341 -1.100  1.00 175.93 ? 186 SER   A OG  1 
ATOM   1259 N  N   . THR   A 1 167 ? -22.521 -13.925 -0.313  1.00 156.35 ? 187 THR   A N   1 
ATOM   1260 C  CA  . THR   A 1 167 ? -23.836 -14.527 -0.503  1.00 156.37 ? 187 THR   A CA  1 
ATOM   1261 C  C   . THR   A 1 167 ? -24.082 -15.695 0.442   1.00 164.26 ? 187 THR   A C   1 
ATOM   1262 O  O   . THR   A 1 167 ? -25.240 -16.072 0.653   1.00 168.74 ? 187 THR   A O   1 
ATOM   1263 C  CB  . THR   A 1 167 ? -24.005 -15.001 -1.949  1.00 158.36 ? 187 THR   A CB  1 
ATOM   1264 O  OG1 . THR   A 1 167 ? -22.828 -15.705 -2.365  1.00 158.70 ? 187 THR   A OG1 1 
ATOM   1265 C  CG2 . THR   A 1 167 ? -24.250 -13.821 -2.878  1.00 157.18 ? 187 THR   A CG2 1 
ATOM   1266 N  N   . SER   A 1 168 ? -23.028 -16.272 1.013   1.00 166.47 ? 188 SER   A N   1 
ATOM   1267 C  CA  . SER   A 1 168 ? -23.154 -17.425 1.891   1.00 157.43 ? 188 SER   A CA  1 
ATOM   1268 C  C   . SER   A 1 168 ? -22.747 -17.154 3.330   1.00 161.73 ? 188 SER   A C   1 
ATOM   1269 O  O   . SER   A 1 168 ? -23.310 -17.770 4.236   1.00 166.54 ? 188 SER   A O   1 
ATOM   1270 C  CB  . SER   A 1 168 ? -22.318 -18.597 1.354   1.00 156.56 ? 188 SER   A CB  1 
ATOM   1271 O  OG  . SER   A 1 168 ? -22.784 -19.013 0.083   1.00 159.44 ? 188 SER   A OG  1 
ATOM   1272 N  N   . PHE   A 1 169 ? -21.818 -16.214 3.524   1.00 166.34 ? 189 PHE   A N   1 
ATOM   1273 C  CA  . PHE   A 1 169 ? -21.323 -15.889 4.887   1.00 153.67 ? 189 PHE   A CA  1 
ATOM   1274 C  C   . PHE   A 1 169 ? -21.400 -14.374 5.100   1.00 161.43 ? 189 PHE   A C   1 
ATOM   1275 O  O   . PHE   A 1 169 ? -21.626 -13.946 6.248   1.00 179.37 ? 189 PHE   A O   1 
ATOM   1276 C  CB  . PHE   A 1 169 ? -19.909 -16.446 5.062   1.00 152.60 ? 189 PHE   A CB  1 
ATOM   1277 C  CG  . PHE   A 1 169 ? -19.637 -17.657 4.206   1.00 145.11 ? 189 PHE   A CG  1 
ATOM   1278 C  CD1 . PHE   A 1 169 ? -20.080 -18.912 4.594   1.00 142.48 ? 189 PHE   A CD1 1 
ATOM   1279 C  CD2 . PHE   A 1 169 ? -18.969 -17.539 2.998   1.00 133.16 ? 189 PHE   A CD2 1 
ATOM   1280 C  CE1 . PHE   A 1 169 ? -19.843 -20.024 3.802   1.00 146.98 ? 189 PHE   A CE1 1 
ATOM   1281 C  CE2 . PHE   A 1 169 ? -18.733 -18.652 2.207   1.00 134.78 ? 189 PHE   A CE2 1 
ATOM   1282 C  CZ  . PHE   A 1 169 ? -19.170 -19.892 2.611   1.00 142.31 ? 189 PHE   A CZ  1 
ATOM   1283 N  N   . GLY   A 1 170 ? -21.220 -13.592 4.031   1.00 181.95 ? 190 GLY   A N   1 
ATOM   1284 C  CA  . GLY   A 1 170 ? -21.350 -12.125 4.134   1.00 177.11 ? 190 GLY   A CA  1 
ATOM   1285 C  C   . GLY   A 1 170 ? -20.052 -11.444 4.528   1.00 181.69 ? 190 GLY   A C   1 
ATOM   1286 O  O   . GLY   A 1 170 ? -20.118 -10.439 5.261   1.00 178.86 ? 190 GLY   A O   1 
ATOM   1287 N  N   . VAL   A 1 171 ? -18.912 -11.960 4.061   1.00 177.88 ? 191 VAL   A N   1 
ATOM   1288 C  CA  . VAL   A 1 171 ? -17.600 -11.301 4.339   1.00 187.47 ? 191 VAL   A CA  1 
ATOM   1289 C  C   . VAL   A 1 171 ? -17.293 -10.352 3.178   1.00 187.53 ? 191 VAL   A C   1 
ATOM   1290 O  O   . VAL   A 1 171 ? -17.344 -10.817 2.022   1.00 181.02 ? 191 VAL   A O   1 
ATOM   1291 C  CB  . VAL   A 1 171 ? -16.479 -12.341 4.523   1.00 188.57 ? 191 VAL   A CB  1 
ATOM   1292 C  CG1 . VAL   A 1 171 ? -15.696 -12.102 5.803   1.00 196.40 ? 191 VAL   A CG1 1 
ATOM   1293 C  CG2 . VAL   A 1 171 ? -17.016 -13.764 4.478   1.00 188.34 ? 191 VAL   A CG2 1 
ATOM   1294 N  N   . ASN   A 1 172 ? -17.012 -9.080  3.474   1.00 193.29 ? 192 ASN   A N   1 
ATOM   1295 C  CA  . ASN   A 1 172 ? -16.776 -8.075  2.402   1.00 195.71 ? 192 ASN   A CA  1 
ATOM   1296 C  C   . ASN   A 1 172 ? -15.272 -7.891  2.195   1.00 195.05 ? 192 ASN   A C   1 
ATOM   1297 O  O   . ASN   A 1 172 ? -14.603 -7.428  3.140   1.00 194.65 ? 192 ASN   A O   1 
ATOM   1298 C  CB  . ASN   A 1 172 ? -17.459 -6.745  2.721   1.00 199.70 ? 192 ASN   A CB  1 
ATOM   1299 C  CG  . ASN   A 1 172 ? -17.691 -6.555  4.205   1.00 207.59 ? 192 ASN   A CG  1 
ATOM   1300 O  OD1 . ASN   A 1 172 ? -18.657 -7.074  4.758   1.00 207.31 ? 192 ASN   A OD1 1 
ATOM   1301 N  ND2 . ASN   A 1 172 ? -16.803 -5.823  4.858   1.00 205.88 ? 192 ASN   A ND2 1 
ATOM   1302 N  N   . ILE   A 1 173 ? -14.769 -8.233  1.006   1.00 192.01 ? 193 ILE   A N   1 
ATOM   1303 C  CA  . ILE   A 1 173 ? -13.346 -8.096  0.710   1.00 189.65 ? 193 ILE   A CA  1 
ATOM   1304 C  C   . ILE   A 1 173 ? -13.186 -7.688  -0.748  1.00 193.69 ? 193 ILE   A C   1 
ATOM   1305 O  O   . ILE   A 1 173 ? -13.774 -8.308  -1.640  1.00 178.10 ? 193 ILE   A O   1 
ATOM   1306 C  CB  . ILE   A 1 173 ? -12.572 -9.401  0.992   1.00 187.01 ? 193 ILE   A CB  1 
ATOM   1307 C  CG1 . ILE   A 1 173 ? -12.382 -9.604  2.497   1.00 180.05 ? 193 ILE   A CG1 1 
ATOM   1308 C  CG2 . ILE   A 1 173 ? -11.230 -9.401  0.269   1.00 198.52 ? 193 ILE   A CG2 1 
ATOM   1309 C  CD1 . ILE   A 1 173 ? -11.646 -10.874 2.860   1.00 174.27 ? 193 ILE   A CD1 1 
ATOM   1310 N  N   . ASP   A 1 174 ? -12.397 -6.642  -0.987  1.00 206.40 ? 194 ASP   A N   1 
ATOM   1311 C  CA  . ASP   A 1 174 ? -12.031 -6.226  -2.340  1.00 208.03 ? 194 ASP   A CA  1 
ATOM   1312 C  C   . ASP   A 1 174 ? -10.941 -7.227  -2.703  1.00 211.59 ? 194 ASP   A C   1 
ATOM   1313 O  O   . ASP   A 1 174 ? -9.849  -7.212  -2.130  1.00 216.34 ? 194 ASP   A O   1 
ATOM   1314 C  CB  . ASP   A 1 174 ? -11.620 -4.757  -2.353  1.00 197.78 ? 194 ASP   A CB  1 
ATOM   1315 C  CG  . ASP   A 1 174 ? -11.290 -4.248  -3.745  1.00 195.33 ? 194 ASP   A CG  1 
ATOM   1316 O  OD1 . ASP   A 1 174 ? -11.550 -4.970  -4.731  1.00 196.65 ? 194 ASP   A OD1 1 
ATOM   1317 O  OD2 . ASP   A 1 174 ? -10.766 -3.119  -3.853  1.00 203.05 ? 194 ASP   A OD2 1 
ATOM   1318 N  N   . SER   A 1 175 ? -11.228 -8.099  -3.671  1.00 195.71 ? 195 SER   A N   1 
ATOM   1319 C  CA  . SER   A 1 175 ? -10.277 -9.144  -4.036  1.00 193.00 ? 195 SER   A CA  1 
ATOM   1320 C  C   . SER   A 1 175 ? -9.185  -8.659  -4.981  1.00 205.49 ? 195 SER   A C   1 
ATOM   1321 O  O   . SER   A 1 175 ? -8.966  -9.252  -6.042  1.00 197.66 ? 195 SER   A O   1 
ATOM   1322 C  CB  . SER   A 1 175 ? -11.004 -10.334 -4.664  1.00 185.47 ? 195 SER   A CB  1 
ATOM   1323 O  OG  . SER   A 1 175 ? -11.690 -11.086 -3.678  1.00 186.38 ? 195 SER   A OG  1 
ATOM   1324 N  N   . LEU   A 1 176 ? -8.495  -7.584  -4.608  1.00 214.08 ? 196 LEU   A N   1 
ATOM   1325 C  CA  . LEU   A 1 176 ? -7.211  -7.256  -5.202  1.00 214.92 ? 196 LEU   A CA  1 
ATOM   1326 C  C   . LEU   A 1 176 ? -6.091  -7.229  -4.176  1.00 219.90 ? 196 LEU   A C   1 
ATOM   1327 O  O   . LEU   A 1 176 ? -4.923  -7.105  -4.562  1.00 212.55 ? 196 LEU   A O   1 
ATOM   1328 C  CB  . LEU   A 1 176 ? -7.270  -5.910  -5.941  1.00 209.52 ? 196 LEU   A CB  1 
ATOM   1329 C  CG  . LEU   A 1 176 ? -6.726  -5.996  -7.370  1.00 205.25 ? 196 LEU   A CG  1 
ATOM   1330 C  CD1 . LEU   A 1 176 ? -7.507  -7.025  -8.178  1.00 193.52 ? 196 LEU   A CD1 1 
ATOM   1331 C  CD2 . LEU   A 1 176 ? -6.751  -4.640  -8.057  1.00 197.14 ? 196 LEU   A CD2 1 
ATOM   1332 N  N   . ASP   A 1 197 ? -2.924  -34.290 -15.128 1.00 211.76 ? 217 ASP   A N   1 
ATOM   1333 C  CA  . ASP   A 1 197 ? -2.815  -34.384 -13.648 1.00 208.62 ? 217 ASP   A CA  1 
ATOM   1334 C  C   . ASP   A 1 197 ? -1.494  -35.067 -13.278 1.00 221.39 ? 217 ASP   A C   1 
ATOM   1335 O  O   . ASP   A 1 197 ? -0.979  -35.846 -14.103 1.00 221.49 ? 217 ASP   A O   1 
ATOM   1336 C  CB  . ASP   A 1 197 ? -4.012  -35.124 -13.047 1.00 201.49 ? 217 ASP   A CB  1 
ATOM   1337 C  CG  . ASP   A 1 197 ? -5.300  -34.322 -13.109 1.00 197.79 ? 217 ASP   A CG  1 
ATOM   1338 O  OD1 . ASP   A 1 197 ? -5.215  -33.104 -13.351 1.00 203.24 ? 217 ASP   A OD1 1 
ATOM   1339 O  OD2 . ASP   A 1 197 ? -6.375  -34.923 -12.923 1.00 189.50 ? 217 ASP   A OD2 1 
ATOM   1340 N  N   . PRO   A 1 198 ? -0.931  -34.822 -12.074 1.00 222.56 ? 218 PRO   A N   1 
ATOM   1341 C  CA  . PRO   A 1 198 ? 0.316   -35.459 -11.634 1.00 221.01 ? 218 PRO   A CA  1 
ATOM   1342 C  C   . PRO   A 1 198 ? 0.126   -36.701 -10.771 1.00 210.11 ? 218 PRO   A C   1 
ATOM   1343 O  O   . PRO   A 1 198 ? 0.958   -37.614 -10.799 1.00 204.37 ? 218 PRO   A O   1 
ATOM   1344 C  CB  . PRO   A 1 198 ? 0.993   -34.340 -10.836 1.00 219.54 ? 218 PRO   A CB  1 
ATOM   1345 C  CG  . PRO   A 1 198 ? -0.181  -33.488 -10.306 1.00 220.81 ? 218 PRO   A CG  1 
ATOM   1346 C  CD  . PRO   A 1 198 ? -1.449  -33.928 -11.024 1.00 224.33 ? 218 PRO   A CD  1 
ATOM   1347 N  N   . PHE   A 1 199 ? -0.956  -36.746 -10.006 1.00 216.30 ? 219 PHE   A N   1 
ATOM   1348 C  CA  . PHE   A 1 199 ? -1.135  -37.696 -8.914  1.00 210.80 ? 219 PHE   A CA  1 
ATOM   1349 C  C   . PHE   A 1 199 ? -2.437  -38.478 -9.000  1.00 204.08 ? 219 PHE   A C   1 
ATOM   1350 O  O   . PHE   A 1 199 ? -2.464  -39.653 -8.622  1.00 192.06 ? 219 PHE   A O   1 
ATOM   1351 C  CB  . PHE   A 1 199 ? -1.041  -36.918 -7.583  1.00 214.67 ? 219 PHE   A CB  1 
ATOM   1352 C  CG  . PHE   A 1 199 ? -1.902  -37.467 -6.482  1.00 205.95 ? 219 PHE   A CG  1 
ATOM   1353 C  CD1 . PHE   A 1 199 ? -1.438  -38.481 -5.661  1.00 194.48 ? 219 PHE   A CD1 1 
ATOM   1354 C  CD2 . PHE   A 1 199 ? -3.163  -36.943 -6.247  1.00 210.74 ? 219 PHE   A CD2 1 
ATOM   1355 C  CE1 . PHE   A 1 199 ? -2.225  -38.977 -4.639  1.00 185.77 ? 219 PHE   A CE1 1 
ATOM   1356 C  CE2 . PHE   A 1 199 ? -3.955  -37.436 -5.229  1.00 208.73 ? 219 PHE   A CE2 1 
ATOM   1357 C  CZ  . PHE   A 1 199 ? -3.485  -38.454 -4.423  1.00 194.02 ? 219 PHE   A CZ  1 
ATOM   1358 N  N   . PHE   A 1 200 ? -3.517  -37.860 -9.486  1.00 217.99 ? 220 PHE   A N   1 
ATOM   1359 C  CA  . PHE   A 1 200 ? -4.759  -38.595 -9.698  1.00 219.33 ? 220 PHE   A CA  1 
ATOM   1360 C  C   . PHE   A 1 200 ? -4.608  -39.667 -10.767 1.00 212.54 ? 220 PHE   A C   1 
ATOM   1361 O  O   . PHE   A 1 200 ? -5.451  -40.568 -10.853 1.00 210.35 ? 220 PHE   A O   1 
ATOM   1362 C  CB  . PHE   A 1 200 ? -5.887  -37.632 -10.078 1.00 219.99 ? 220 PHE   A CB  1 
ATOM   1363 C  CG  . PHE   A 1 200 ? -6.101  -36.525 -9.086  1.00 226.93 ? 220 PHE   A CG  1 
ATOM   1364 C  CD1 . PHE   A 1 200 ? -5.398  -35.336 -9.193  1.00 227.67 ? 220 PHE   A CD1 1 
ATOM   1365 C  CD2 . PHE   A 1 200 ? -7.009  -36.670 -8.050  1.00 225.57 ? 220 PHE   A CD2 1 
ATOM   1366 C  CE1 . PHE   A 1 200 ? -5.592  -34.316 -8.283  1.00 228.88 ? 220 PHE   A CE1 1 
ATOM   1367 C  CE2 . PHE   A 1 200 ? -7.208  -35.652 -7.137  1.00 227.92 ? 220 PHE   A CE2 1 
ATOM   1368 C  CZ  . PHE   A 1 200 ? -6.498  -34.473 -7.254  1.00 231.77 ? 220 PHE   A CZ  1 
ATOM   1369 N  N   . LEU   A 1 201 ? -3.558  -39.579 -11.588 1.00 194.02 ? 221 LEU   A N   1 
ATOM   1370 C  CA  . LEU   A 1 201 ? -3.244  -40.647 -12.531 1.00 189.12 ? 221 LEU   A CA  1 
ATOM   1371 C  C   . LEU   A 1 201 ? -3.036  -41.975 -11.814 1.00 173.99 ? 221 LEU   A C   1 
ATOM   1372 O  O   . LEU   A 1 201 ? -3.385  -43.034 -12.349 1.00 168.23 ? 221 LEU   A O   1 
ATOM   1373 C  CB  . LEU   A 1 201 ? -1.999  -40.270 -13.334 1.00 187.22 ? 221 LEU   A CB  1 
ATOM   1374 C  CG  . LEU   A 1 201 ? -2.048  -40.398 -14.858 1.00 184.25 ? 221 LEU   A CG  1 
ATOM   1375 C  CD1 . LEU   A 1 201 ? -1.887  -41.846 -15.291 1.00 168.76 ? 221 LEU   A CD1 1 
ATOM   1376 C  CD2 . LEU   A 1 201 ? -3.346  -39.817 -15.398 1.00 186.36 ? 221 LEU   A CD2 1 
ATOM   1377 N  N   . SER   A 1 202 ? -2.478  -41.939 -10.603 1.00 194.19 ? 222 SER   A N   1 
ATOM   1378 C  CA  . SER   A 1 202 ? -2.283  -43.148 -9.816  1.00 190.42 ? 222 SER   A CA  1 
ATOM   1379 C  C   . SER   A 1 202 ? -3.540  -43.567 -9.067  1.00 189.93 ? 222 SER   A C   1 
ATOM   1380 O  O   . SER   A 1 202 ? -3.631  -44.723 -8.644  1.00 186.24 ? 222 SER   A O   1 
ATOM   1381 C  CB  . SER   A 1 202 ? -1.138  -42.946 -8.822  1.00 182.65 ? 222 SER   A CB  1 
ATOM   1382 O  OG  . SER   A 1 202 ? 0.029   -42.471 -9.471  1.00 170.46 ? 222 SER   A OG  1 
ATOM   1383 N  N   . ILE   A 1 203 ? -4.503  -42.659 -8.895  1.00 173.00 ? 223 ILE   A N   1 
ATOM   1384 C  CA  . ILE   A 1 203 ? -5.733  -42.996 -8.182  1.00 170.25 ? 223 ILE   A CA  1 
ATOM   1385 C  C   . ILE   A 1 203 ? -6.510  -44.071 -8.929  1.00 179.18 ? 223 ILE   A C   1 
ATOM   1386 O  O   . ILE   A 1 203 ? -7.034  -45.015 -8.324  1.00 182.42 ? 223 ILE   A O   1 
ATOM   1387 C  CB  . ILE   A 1 203 ? -6.586  -41.730 -7.967  1.00 162.23 ? 223 ILE   A CB  1 
ATOM   1388 C  CG1 . ILE   A 1 203 ? -6.176  -41.015 -6.679  1.00 171.79 ? 223 ILE   A CG1 1 
ATOM   1389 C  CG2 . ILE   A 1 203 ? -8.075  -42.065 -7.951  1.00 152.68 ? 223 ILE   A CG2 1 
ATOM   1390 C  CD1 . ILE   A 1 203 ? -7.011  -39.789 -6.375  1.00 188.98 ? 223 ILE   A CD1 1 
ATOM   1391 N  N   . THR   A 1 204 ? -6.588  -43.955 -10.255 1.00 166.43 ? 224 THR   A N   1 
ATOM   1392 C  CA  . THR   A 1 204 ? -7.474  -44.823 -11.019 1.00 156.57 ? 224 THR   A CA  1 
ATOM   1393 C  C   . THR   A 1 204 ? -6.883  -46.213 -11.215 1.00 153.12 ? 224 THR   A C   1 
ATOM   1394 O  O   . THR   A 1 204 ? -7.618  -47.207 -11.191 1.00 161.70 ? 224 THR   A O   1 
ATOM   1395 C  CB  . THR   A 1 204 ? -7.795  -44.183 -12.367 1.00 144.25 ? 224 THR   A CB  1 
ATOM   1396 O  OG1 . THR   A 1 204 ? -7.686  -42.760 -12.249 1.00 160.06 ? 224 THR   A OG1 1 
ATOM   1397 C  CG2 . THR   A 1 204 ? -9.211  -44.526 -12.776 1.00 145.75 ? 224 THR   A CG2 1 
ATOM   1398 N  N   . VAL   A 1 205 ? -5.568  -46.307 -11.419 1.00 161.36 ? 225 VAL   A N   1 
ATOM   1399 C  CA  . VAL   A 1 205 ? -4.936  -47.619 -11.492 1.00 171.35 ? 225 VAL   A CA  1 
ATOM   1400 C  C   . VAL   A 1 205 ? -4.732  -48.215 -10.107 1.00 185.73 ? 225 VAL   A C   1 
ATOM   1401 O  O   . VAL   A 1 205 ? -4.648  -49.443 -9.972  1.00 181.01 ? 225 VAL   A O   1 
ATOM   1402 C  CB  . VAL   A 1 205 ? -3.594  -47.549 -12.239 1.00 173.90 ? 225 VAL   A CB  1 
ATOM   1403 C  CG1 . VAL   A 1 205 ? -3.165  -48.938 -12.693 1.00 162.14 ? 225 VAL   A CG1 1 
ATOM   1404 C  CG2 . VAL   A 1 205 ? -3.704  -46.609 -13.422 1.00 158.30 ? 225 VAL   A CG2 1 
ATOM   1405 N  N   . PHE   A 1 206 ? -4.669  -47.383 -9.069  1.00 207.12 ? 226 PHE   A N   1 
ATOM   1406 C  CA  . PHE   A 1 206 ? -4.580  -47.842 -7.684  1.00 212.25 ? 226 PHE   A CA  1 
ATOM   1407 C  C   . PHE   A 1 206 ? -5.779  -47.346 -6.878  1.00 209.89 ? 226 PHE   A C   1 
ATOM   1408 O  O   . PHE   A 1 206 ? -5.616  -46.574 -5.926  1.00 210.30 ? 226 PHE   A O   1 
ATOM   1409 C  CB  . PHE   A 1 206 ? -3.283  -47.374 -7.026  1.00 218.07 ? 226 PHE   A CB  1 
ATOM   1410 C  CG  . PHE   A 1 206 ? -2.046  -47.584 -7.859  1.00 221.98 ? 226 PHE   A CG  1 
ATOM   1411 C  CD1 . PHE   A 1 206 ? -1.892  -48.714 -8.643  1.00 223.20 ? 226 PHE   A CD1 1 
ATOM   1412 C  CD2 . PHE   A 1 206 ? -1.027  -46.645 -7.841  1.00 224.15 ? 226 PHE   A CD2 1 
ATOM   1413 C  CE1 . PHE   A 1 206 ? -0.753  -48.897 -9.402  1.00 227.18 ? 226 PHE   A CE1 1 
ATOM   1414 C  CE2 . PHE   A 1 206 ? 0.116   -46.825 -8.596  1.00 224.60 ? 226 PHE   A CE2 1 
ATOM   1415 C  CZ  . PHE   A 1 206 ? 0.253   -47.953 -9.377  1.00 223.75 ? 226 PHE   A CZ  1 
ATOM   1416 N  N   . PRO   A 1 207 ? -7.002  -47.767 -7.224  1.00 183.47 ? 227 PRO   A N   1 
ATOM   1417 C  CA  . PRO   A 1 207 ? -8.139  -47.439 -6.353  1.00 176.96 ? 227 PRO   A CA  1 
ATOM   1418 C  C   . PRO   A 1 207 ? -8.095  -48.205 -5.051  1.00 175.08 ? 227 PRO   A C   1 
ATOM   1419 O  O   . PRO   A 1 207 ? -8.738  -47.794 -4.078  1.00 168.66 ? 227 PRO   A O   1 
ATOM   1420 C  CB  . PRO   A 1 207 ? -9.355  -47.829 -7.199  1.00 174.51 ? 227 PRO   A CB  1 
ATOM   1421 C  CG  . PRO   A 1 207 ? -8.864  -48.960 -8.017  1.00 184.47 ? 227 PRO   A CG  1 
ATOM   1422 C  CD  . PRO   A 1 207 ? -7.408  -48.675 -8.314  1.00 187.09 ? 227 PRO   A CD  1 
ATOM   1423 N  N   . PHE   A 1 208 ? -7.349  -49.310 -5.013  1.00 169.98 ? 228 PHE   A N   1 
ATOM   1424 C  CA  . PHE   A 1 208 ? -7.085  -50.016 -3.770  1.00 175.40 ? 228 PHE   A CA  1 
ATOM   1425 C  C   . PHE   A 1 208 ? -6.206  -49.208 -2.827  1.00 173.53 ? 228 PHE   A C   1 
ATOM   1426 O  O   . PHE   A 1 208 ? -6.205  -49.473 -1.620  1.00 172.48 ? 228 PHE   A O   1 
ATOM   1427 C  CB  . PHE   A 1 208 ? -6.430  -51.364 -4.075  1.00 183.10 ? 228 PHE   A CB  1 
ATOM   1428 C  CG  . PHE   A 1 208 ? -5.211  -51.269 -4.952  1.00 187.91 ? 228 PHE   A CG  1 
ATOM   1429 C  CD1 . PHE   A 1 208 ? -3.965  -51.022 -4.404  1.00 187.12 ? 228 PHE   A CD1 1 
ATOM   1430 C  CD2 . PHE   A 1 208 ? -5.310  -51.440 -6.323  1.00 184.83 ? 228 PHE   A CD2 1 
ATOM   1431 C  CE1 . PHE   A 1 208 ? -2.842  -50.940 -5.201  1.00 187.74 ? 228 PHE   A CE1 1 
ATOM   1432 C  CE2 . PHE   A 1 208 ? -4.189  -51.358 -7.128  1.00 191.58 ? 228 PHE   A CE2 1 
ATOM   1433 C  CZ  . PHE   A 1 208 ? -2.954  -51.109 -6.563  1.00 196.56 ? 228 PHE   A CZ  1 
ATOM   1434 N  N   . LEU   A 1 209 ? -5.454  -48.238 -3.350  1.00 177.93 ? 229 LEU   A N   1 
ATOM   1435 C  CA  . LEU   A 1 209 ? -4.630  -47.372 -2.518  1.00 173.09 ? 229 LEU   A CA  1 
ATOM   1436 C  C   . LEU   A 1 209 ? -5.417  -46.235 -1.883  1.00 173.05 ? 229 LEU   A C   1 
ATOM   1437 O  O   . LEU   A 1 209 ? -4.887  -45.565 -0.991  1.00 172.12 ? 229 LEU   A O   1 
ATOM   1438 C  CB  . LEU   A 1 209 ? -3.471  -46.793 -3.336  1.00 180.84 ? 229 LEU   A CB  1 
ATOM   1439 C  CG  . LEU   A 1 209 ? -2.224  -47.667 -3.474  1.00 180.43 ? 229 LEU   A CG  1 
ATOM   1440 C  CD1 . LEU   A 1 209 ? -1.125  -46.925 -4.215  1.00 182.56 ? 229 LEU   A CD1 1 
ATOM   1441 C  CD2 . LEU   A 1 209 ? -1.736  -48.100 -2.108  1.00 180.00 ? 229 LEU   A CD2 1 
ATOM   1442 N  N   . ILE   A 1 210 ? -6.654  -45.994 -2.323  1.00 173.78 ? 230 ILE   A N   1 
ATOM   1443 C  CA  . ILE   A 1 210 ? -7.475  -44.963 -1.687  1.00 166.71 ? 230 ILE   A CA  1 
ATOM   1444 C  C   . ILE   A 1 210 ? -7.727  -45.268 -0.214  1.00 171.69 ? 230 ILE   A C   1 
ATOM   1445 O  O   . ILE   A 1 210 ? -7.540  -44.366 0.619   1.00 173.70 ? 230 ILE   A O   1 
ATOM   1446 C  CB  . ILE   A 1 210 ? -8.773  -44.749 -2.486  1.00 155.71 ? 230 ILE   A CB  1 
ATOM   1447 C  CG1 . ILE   A 1 210 ? -8.473  -44.055 -3.817  1.00 150.23 ? 230 ILE   A CG1 1 
ATOM   1448 C  CG2 . ILE   A 1 210 ? -9.777  -43.945 -1.673  1.00 164.20 ? 230 ILE   A CG2 1 
ATOM   1449 C  CD1 . ILE   A 1 210 ? -9.711  -43.710 -4.618  1.00 148.46 ? 230 ILE   A CD1 1 
ATOM   1450 N  N   . PRO   A 1 211 ? -8.133  -46.483 0.181   1.00 169.77 ? 231 PRO   A N   1 
ATOM   1451 C  CA  . PRO   A 1 211 ? -8.240  -46.761 1.623   1.00 169.99 ? 231 PRO   A CA  1 
ATOM   1452 C  C   . PRO   A 1 211 ? -6.926  -46.598 2.365   1.00 171.60 ? 231 PRO   A C   1 
ATOM   1453 O  O   . PRO   A 1 211 ? -6.938  -46.269 3.559   1.00 167.78 ? 231 PRO   A O   1 
ATOM   1454 C  CB  . PRO   A 1 211 ? -8.738  -48.213 1.664   1.00 161.99 ? 231 PRO   A CB  1 
ATOM   1455 C  CG  . PRO   A 1 211 ? -9.431  -48.407 0.373   1.00 164.01 ? 231 PRO   A CG  1 
ATOM   1456 C  CD  . PRO   A 1 211 ? -8.638  -47.614 -0.620  1.00 168.71 ? 231 PRO   A CD  1 
ATOM   1457 N  N   . ILE   A 1 212 ? -5.791  -46.824 1.698   1.00 178.22 ? 232 ILE   A N   1 
ATOM   1458 C  CA  . ILE   A 1 212 ? -4.494  -46.600 2.335   1.00 176.81 ? 232 ILE   A CA  1 
ATOM   1459 C  C   . ILE   A 1 212 ? -4.341  -45.135 2.720   1.00 175.08 ? 232 ILE   A C   1 
ATOM   1460 O  O   . ILE   A 1 212 ? -3.996  -44.805 3.860   1.00 179.09 ? 232 ILE   A O   1 
ATOM   1461 C  CB  . ILE   A 1 212 ? -3.349  -47.053 1.411   1.00 179.25 ? 232 ILE   A CB  1 
ATOM   1462 C  CG1 . ILE   A 1 212 ? -3.304  -48.580 1.308   1.00 178.78 ? 232 ILE   A CG1 1 
ATOM   1463 C  CG2 . ILE   A 1 212 ? -2.019  -46.470 1.888   1.00 177.00 ? 232 ILE   A CG2 1 
ATOM   1464 C  CD1 . ILE   A 1 212 ? -1.906  -49.156 1.331   1.00 180.96 ? 232 ILE   A CD1 1 
ATOM   1465 N  N   . LEU   A 1 213 ? -4.599  -44.233 1.773   1.00 170.74 ? 233 LEU   A N   1 
ATOM   1466 C  CA  . LEU   A 1 213 ? -4.366  -42.814 2.012   1.00 169.66 ? 233 LEU   A CA  1 
ATOM   1467 C  C   . LEU   A 1 213 ? -5.368  -42.214 2.988   1.00 183.22 ? 233 LEU   A C   1 
ATOM   1468 O  O   . LEU   A 1 213 ? -5.070  -41.189 3.609   1.00 182.53 ? 233 LEU   A O   1 
ATOM   1469 C  CB  . LEU   A 1 213 ? -4.399  -42.056 0.686   1.00 170.57 ? 233 LEU   A CB  1 
ATOM   1470 C  CG  . LEU   A 1 213 ? -3.545  -42.653 -0.433  1.00 166.83 ? 233 LEU   A CG  1 
ATOM   1471 C  CD1 . LEU   A 1 213 ? -3.706  -41.860 -1.722  1.00 170.67 ? 233 LEU   A CD1 1 
ATOM   1472 C  CD2 . LEU   A 1 213 ? -2.083  -42.722 -0.019  1.00 162.02 ? 233 LEU   A CD2 1 
ATOM   1473 N  N   . GLU   A 1 214 ? -6.545  -42.827 3.139   1.00 186.79 ? 234 GLU   A N   1 
ATOM   1474 C  CA  . GLU   A 1 214 ? -7.530  -42.312 4.084   1.00 188.21 ? 234 GLU   A CA  1 
ATOM   1475 C  C   . GLU   A 1 214 ? -7.061  -42.463 5.526   1.00 191.12 ? 234 GLU   A C   1 
ATOM   1476 O  O   . GLU   A 1 214 ? -7.452  -41.669 6.388   1.00 194.54 ? 234 GLU   A O   1 
ATOM   1477 C  CB  . GLU   A 1 214 ? -8.872  -43.022 3.891   1.00 187.20 ? 234 GLU   A CB  1 
ATOM   1478 C  CG  . GLU   A 1 214 ? -9.509  -42.835 2.519   1.00 188.53 ? 234 GLU   A CG  1 
ATOM   1479 C  CD  . GLU   A 1 214 ? -10.432 -41.631 2.447   1.00 184.08 ? 234 GLU   A CD  1 
ATOM   1480 O  OE1 . GLU   A 1 214 ? -10.232 -40.672 3.221   1.00 186.04 ? 234 GLU   A OE1 1 
ATOM   1481 O  OE2 . GLU   A 1 214 ? -11.364 -41.649 1.615   1.00 180.52 ? 234 GLU   A OE2 1 
ATOM   1482 N  N   . VAL   A 1 215 ? -6.228  -43.471 5.808   1.00 174.49 ? 235 VAL   A N   1 
ATOM   1483 C  CA  . VAL   A 1 215 ? -5.738  -43.694 7.166   1.00 170.52 ? 235 VAL   A CA  1 
ATOM   1484 C  C   . VAL   A 1 215 ? -4.454  -42.927 7.456   1.00 174.94 ? 235 VAL   A C   1 
ATOM   1485 O  O   . VAL   A 1 215 ? -3.988  -42.928 8.606   1.00 171.96 ? 235 VAL   A O   1 
ATOM   1486 C  CB  . VAL   A 1 215 ? -5.533  -45.203 7.422   1.00 161.05 ? 235 VAL   A CB  1 
ATOM   1487 C  CG1 . VAL   A 1 215 ? -4.175  -45.662 6.913   1.00 164.28 ? 235 VAL   A CG1 1 
ATOM   1488 C  CG2 . VAL   A 1 215 ? -5.712  -45.532 8.900   1.00 156.86 ? 235 VAL   A CG2 1 
ATOM   1489 N  N   . LEU   A 1 216 ? -3.872  -42.262 6.459   1.00 162.04 ? 236 LEU   A N   1 
ATOM   1490 C  CA  . LEU   A 1 216 ? -2.675  -41.453 6.644   1.00 164.38 ? 236 LEU   A CA  1 
ATOM   1491 C  C   . LEU   A 1 216 ? -2.985  -39.965 6.738   1.00 172.55 ? 236 LEU   A C   1 
ATOM   1492 O  O   . LEU   A 1 216 ? -2.055  -39.150 6.748   1.00 177.83 ? 236 LEU   A O   1 
ATOM   1493 C  CB  . LEU   A 1 216 ? -1.688  -41.693 5.498   1.00 155.20 ? 236 LEU   A CB  1 
ATOM   1494 C  CG  . LEU   A 1 216 ? -1.470  -43.124 5.004   1.00 147.17 ? 236 LEU   A CG  1 
ATOM   1495 C  CD1 . LEU   A 1 216 ? -0.482  -43.139 3.847   1.00 141.40 ? 236 LEU   A CD1 1 
ATOM   1496 C  CD2 . LEU   A 1 216 ? -0.993  -44.025 6.128   1.00 157.41 ? 236 LEU   A CD2 1 
ATOM   1497 N  N   . ASN   A 1 217 ? -4.264  -39.594 6.797   1.00 163.20 ? 237 ASN   A N   1 
ATOM   1498 C  CA  . ASN   A 1 217 ? -4.740  -38.217 6.692   1.00 169.22 ? 237 ASN   A CA  1 
ATOM   1499 C  C   . ASN   A 1 217 ? -4.321  -37.553 5.384   1.00 173.86 ? 237 ASN   A C   1 
ATOM   1500 O  O   . ASN   A 1 217 ? -4.450  -36.330 5.245   1.00 189.77 ? 237 ASN   A O   1 
ATOM   1501 C  CB  . ASN   A 1 217 ? -4.282  -37.359 7.882   1.00 176.91 ? 237 ASN   A CB  1 
ATOM   1502 C  CG  . ASN   A 1 217 ? -5.222  -36.194 8.165   1.00 183.65 ? 237 ASN   A CG  1 
ATOM   1503 O  OD1 . ASN   A 1 217 ? -5.246  -35.659 9.273   1.00 199.03 ? 237 ASN   A OD1 1 
ATOM   1504 N  ND2 . ASN   A 1 217 ? -6.009  -35.805 7.166   1.00 174.72 ? 237 ASN   A ND2 1 
ATOM   1505 N  N   . ILE   A 1 218 ? -3.817  -38.327 4.421   1.00 182.16 ? 238 ILE   A N   1 
ATOM   1506 C  CA  . ILE   A 1 218 ? -3.509  -37.784 3.105   1.00 178.16 ? 238 ILE   A CA  1 
ATOM   1507 C  C   . ILE   A 1 218 ? -4.802  -37.345 2.435   1.00 189.23 ? 238 ILE   A C   1 
ATOM   1508 O  O   . ILE   A 1 218 ? -5.829  -38.034 2.511   1.00 188.96 ? 238 ILE   A O   1 
ATOM   1509 C  CB  . ILE   A 1 218 ? -2.755  -38.824 2.257   1.00 161.85 ? 238 ILE   A CB  1 
ATOM   1510 C  CG1 . ILE   A 1 218 ? -1.354  -39.058 2.826   1.00 166.72 ? 238 ILE   A CG1 1 
ATOM   1511 C  CG2 . ILE   A 1 218 ? -2.674  -38.386 0.801   1.00 163.43 ? 238 ILE   A CG2 1 
ATOM   1512 C  CD1 . ILE   A 1 218 ? -0.477  -39.928 1.951   1.00 160.92 ? 238 ILE   A CD1 1 
ATOM   1513 N  N   . CYS   A 1 219 ? -4.767  -36.182 1.792   1.00 210.15 ? 239 CYS   A N   1 
ATOM   1514 C  CA  . CYS   A 1 219 ? -5.959  -35.606 1.193   1.00 212.33 ? 239 CYS   A CA  1 
ATOM   1515 C  C   . CYS   A 1 219 ? -5.612  -35.029 -0.170  1.00 212.82 ? 239 CYS   A C   1 
ATOM   1516 O  O   . CYS   A 1 219 ? -4.576  -34.377 -0.330  1.00 218.54 ? 239 CYS   A O   1 
ATOM   1517 C  CB  . CYS   A 1 219 ? -6.554  -34.518 2.096   1.00 214.60 ? 239 CYS   A CB  1 
ATOM   1518 S  SG  . CYS   A 1 219 ? -8.339  -34.300 1.938   1.00 219.71 ? 239 CYS   A SG  1 
ATOM   1519 N  N   . VAL   A 1 220 ? -6.481  -35.280 -1.154  1.00 196.02 ? 240 VAL   A N   1 
ATOM   1520 C  CA  . VAL   A 1 220 ? -6.319  -34.668 -2.467  1.00 196.22 ? 240 VAL   A CA  1 
ATOM   1521 C  C   . VAL   A 1 220 ? -6.400  -33.154 -2.371  1.00 196.43 ? 240 VAL   A C   1 
ATOM   1522 O  O   . VAL   A 1 220 ? -5.868  -32.445 -3.233  1.00 195.01 ? 240 VAL   A O   1 
ATOM   1523 C  CB  . VAL   A 1 220 ? -7.368  -35.217 -3.455  1.00 187.22 ? 240 VAL   A CB  1 
ATOM   1524 C  CG1 . VAL   A 1 220 ? -7.155  -36.703 -3.680  1.00 184.91 ? 240 VAL   A CG1 1 
ATOM   1525 C  CG2 . VAL   A 1 220 ? -8.774  -34.949 -2.942  1.00 184.60 ? 240 VAL   A CG2 1 
ATOM   1526 N  N   . PHE   A 1 221 ? -7.063  -32.639 -1.338  1.00 182.14 ? 241 PHE   A N   1 
ATOM   1527 C  CA  . PHE   A 1 221 ? -7.047  -31.221 -1.030  1.00 185.10 ? 241 PHE   A CA  1 
ATOM   1528 C  C   . PHE   A 1 221 ? -5.966  -30.989 0.013   1.00 188.95 ? 241 PHE   A C   1 
ATOM   1529 O  O   . PHE   A 1 221 ? -6.088  -31.504 1.136   1.00 199.15 ? 241 PHE   A O   1 
ATOM   1530 C  CB  . PHE   A 1 221 ? -8.409  -30.771 -0.507  1.00 189.09 ? 241 PHE   A CB  1 
ATOM   1531 C  CG  . PHE   A 1 221 ? -9.562  -31.531 -1.103  1.00 185.05 ? 241 PHE   A CG  1 
ATOM   1532 C  CD1 . PHE   A 1 221 ? -9.959  -31.301 -2.410  1.00 181.78 ? 241 PHE   A CD1 1 
ATOM   1533 C  CD2 . PHE   A 1 221 ? -10.244 -32.480 -0.359  1.00 183.71 ? 241 PHE   A CD2 1 
ATOM   1534 C  CE1 . PHE   A 1 221 ? -11.016 -32.002 -2.963  1.00 169.82 ? 241 PHE   A CE1 1 
ATOM   1535 C  CE2 . PHE   A 1 221 ? -11.302 -33.183 -0.905  1.00 168.78 ? 241 PHE   A CE2 1 
ATOM   1536 C  CZ  . PHE   A 1 221 ? -11.689 -32.943 -2.209  1.00 159.04 ? 241 PHE   A CZ  1 
ATOM   1537 N  N   . PRO   A 1 222 ? -4.901  -30.251 -0.301  1.00 187.63 ? 242 PRO   A N   1 
ATOM   1538 C  CA  . PRO   A 1 222 ? -3.758  -30.158 0.619   1.00 200.58 ? 242 PRO   A CA  1 
ATOM   1539 C  C   . PRO   A 1 222 ? -4.176  -29.720 2.015   1.00 199.92 ? 242 PRO   A C   1 
ATOM   1540 O  O   . PRO   A 1 222 ? -4.955  -28.778 2.186   1.00 198.64 ? 242 PRO   A O   1 
ATOM   1541 C  CB  . PRO   A 1 222 ? -2.845  -29.124 -0.054  1.00 203.97 ? 242 PRO   A CB  1 
ATOM   1542 C  CG  . PRO   A 1 222 ? -3.698  -28.439 -1.082  1.00 193.77 ? 242 PRO   A CG  1 
ATOM   1543 C  CD  . PRO   A 1 222 ? -4.702  -29.451 -1.518  1.00 175.58 ? 242 PRO   A CD  1 
ATOM   1544 N  N   . ARG   A 1 223 ? -3.647  -30.421 3.021   1.00 203.68 ? 243 ARG   A N   1 
ATOM   1545 C  CA  . ARG   A 1 223 ? -4.121  -30.278 4.392   1.00 206.48 ? 243 ARG   A CA  1 
ATOM   1546 C  C   . ARG   A 1 223 ? -3.893  -28.887 4.965   1.00 207.01 ? 243 ARG   A C   1 
ATOM   1547 O  O   . ARG   A 1 223 ? -4.447  -28.579 6.025   1.00 205.99 ? 243 ARG   A O   1 
ATOM   1548 C  CB  . ARG   A 1 223 ? -3.453  -31.323 5.287   1.00 204.68 ? 243 ARG   A CB  1 
ATOM   1549 C  CG  . ARG   A 1 223 ? -2.025  -30.994 5.687   1.00 209.50 ? 243 ARG   A CG  1 
ATOM   1550 C  CD  . ARG   A 1 223 ? -1.446  -32.096 6.559   1.00 215.18 ? 243 ARG   A CD  1 
ATOM   1551 N  NE  . ARG   A 1 223 ? -2.468  -32.705 7.402   1.00 215.38 ? 243 ARG   A NE  1 
ATOM   1552 C  CZ  . ARG   A 1 223 ? -2.857  -32.228 8.576   1.00 217.73 ? 243 ARG   A CZ  1 
ATOM   1553 N  NH1 . ARG   A 1 223 ? -2.322  -31.132 9.088   1.00 216.60 ? 243 ARG   A NH1 1 
ATOM   1554 N  NH2 . ARG   A 1 223 ? -3.809  -32.865 9.252   1.00 217.25 ? 243 ARG   A NH2 1 
ATOM   1555 N  N   . GLU   A 1 224 ? -3.097  -28.046 4.307   1.00 220.87 ? 244 GLU   A N   1 
ATOM   1556 C  CA  . GLU   A 1 224 ? -2.941  -26.663 4.735   1.00 223.39 ? 244 GLU   A CA  1 
ATOM   1557 C  C   . GLU   A 1 224 ? -4.008  -25.745 4.156   1.00 219.60 ? 244 GLU   A C   1 
ATOM   1558 O  O   . GLU   A 1 224 ? -4.284  -24.691 4.741   1.00 221.34 ? 244 GLU   A O   1 
ATOM   1559 C  CB  . GLU   A 1 224 ? -1.551  -26.145 4.355   1.00 235.67 ? 244 GLU   A CB  1 
ATOM   1560 C  CG  . GLU   A 1 224 ? -1.200  -26.317 2.889   1.00 236.64 ? 244 GLU   A CG  1 
ATOM   1561 C  CD  . GLU   A 1 224 ? 0.285   -26.167 2.630   1.00 253.00 ? 244 GLU   A CD  1 
ATOM   1562 O  OE1 . GLU   A 1 224 ? 1.059   -26.137 3.610   1.00 247.89 ? 244 GLU   A OE1 1 
ATOM   1563 O  OE2 . GLU   A 1 224 ? 0.680   -26.080 1.449   1.00 256.03 ? 244 GLU   A OE2 1 
ATOM   1564 N  N   . VAL   A 1 225 ? -4.611  -26.118 3.025   1.00 210.09 ? 245 VAL   A N   1 
ATOM   1565 C  CA  . VAL   A 1 225 ? -5.740  -25.356 2.502   1.00 202.61 ? 245 VAL   A CA  1 
ATOM   1566 C  C   . VAL   A 1 225 ? -6.984  -25.610 3.343   1.00 198.39 ? 245 VAL   A C   1 
ATOM   1567 O  O   . VAL   A 1 225 ? -7.751  -24.685 3.639   1.00 186.74 ? 245 VAL   A O   1 
ATOM   1568 C  CB  . VAL   A 1 225 ? -5.974  -25.700 1.019   1.00 188.75 ? 245 VAL   A CB  1 
ATOM   1569 C  CG1 . VAL   A 1 225 ? -7.263  -25.069 0.522   1.00 169.51 ? 245 VAL   A CG1 1 
ATOM   1570 C  CG2 . VAL   A 1 225 ? -4.794  -25.238 0.179   1.00 191.05 ? 245 VAL   A CG2 1 
ATOM   1571 N  N   . THR   A 1 226 ? -7.200  -26.863 3.751   1.00 199.39 ? 246 THR   A N   1 
ATOM   1572 C  CA  . THR   A 1 226 ? -8.352  -27.177 4.589   1.00 195.07 ? 246 THR   A CA  1 
ATOM   1573 C  C   . THR   A 1 226 ? -8.155  -26.669 6.013   1.00 210.05 ? 246 THR   A C   1 
ATOM   1574 O  O   . THR   A 1 226 ? -9.090  -26.133 6.617   1.00 209.81 ? 246 THR   A O   1 
ATOM   1575 C  CB  . THR   A 1 226 ? -8.614  -28.683 4.587   1.00 191.30 ? 246 THR   A CB  1 
ATOM   1576 O  OG1 . THR   A 1 226 ? -7.433  -29.377 5.008   1.00 210.76 ? 246 THR   A OG1 1 
ATOM   1577 C  CG2 . THR   A 1 226 ? -9.007  -29.153 3.194   1.00 166.92 ? 246 THR   A CG2 1 
ATOM   1578 N  N   . ASN   A 1 227 ? -6.948  -26.830 6.567   1.00 231.79 ? 247 ASN   A N   1 
ATOM   1579 C  CA  . ASN   A 1 227 ? -6.675  -26.293 7.898   1.00 235.98 ? 247 ASN   A CA  1 
ATOM   1580 C  C   . ASN   A 1 227 ? -6.825  -24.780 7.929   1.00 239.15 ? 247 ASN   A C   1 
ATOM   1581 O  O   . ASN   A 1 227 ? -7.179  -24.213 8.969   1.00 245.70 ? 247 ASN   A O   1 
ATOM   1582 C  CB  . ASN   A 1 227 ? -5.276  -26.692 8.364   1.00 240.85 ? 247 ASN   A CB  1 
ATOM   1583 C  CG  . ASN   A 1 227 ? -5.242  -28.072 8.989   1.00 243.06 ? 247 ASN   A CG  1 
ATOM   1584 O  OD1 . ASN   A 1 227 ? -6.240  -28.544 9.532   1.00 241.91 ? 247 ASN   A OD1 1 
ATOM   1585 N  ND2 . ASN   A 1 227 ? -4.088  -28.724 8.921   1.00 246.24 ? 247 ASN   A ND2 1 
ATOM   1586 N  N   . PHE   A 1 228 ? -6.560  -24.110 6.806   1.00 216.47 ? 248 PHE   A N   1 
ATOM   1587 C  CA  . PHE   A 1 228 ? -6.883  -22.694 6.698   1.00 206.90 ? 248 PHE   A CA  1 
ATOM   1588 C  C   . PHE   A 1 228 ? -8.381  -22.448 6.828   1.00 195.58 ? 248 PHE   A C   1 
ATOM   1589 O  O   . PHE   A 1 228 ? -8.789  -21.328 7.146   1.00 192.88 ? 248 PHE   A O   1 
ATOM   1590 C  CB  . PHE   A 1 228 ? -6.361  -22.138 5.369   1.00 194.63 ? 248 PHE   A CB  1 
ATOM   1591 C  CG  . PHE   A 1 228 ? -6.793  -20.728 5.090   1.00 184.92 ? 248 PHE   A CG  1 
ATOM   1592 C  CD1 . PHE   A 1 228 ? -6.428  -19.697 5.939   1.00 189.45 ? 248 PHE   A CD1 1 
ATOM   1593 C  CD2 . PHE   A 1 228 ? -7.563  -20.433 3.977   1.00 161.91 ? 248 PHE   A CD2 1 
ATOM   1594 C  CE1 . PHE   A 1 228 ? -6.826  -18.399 5.687   1.00 179.71 ? 248 PHE   A CE1 1 
ATOM   1595 C  CE2 . PHE   A 1 228 ? -7.963  -19.139 3.720   1.00 170.16 ? 248 PHE   A CE2 1 
ATOM   1596 C  CZ  . PHE   A 1 228 ? -7.593  -18.120 4.576   1.00 177.40 ? 248 PHE   A CZ  1 
ATOM   1597 N  N   . LEU   A 1 229 ? -9.204  -23.478 6.609   1.00 207.27 ? 249 LEU   A N   1 
ATOM   1598 C  CA  . LEU   A 1 229 ? -10.650 -23.365 6.702   1.00 202.20 ? 249 LEU   A CA  1 
ATOM   1599 C  C   . LEU   A 1 229 ? -11.272 -24.217 7.799   1.00 216.49 ? 249 LEU   A C   1 
ATOM   1600 O  O   . LEU   A 1 229 ? -12.391 -23.913 8.225   1.00 213.85 ? 249 LEU   A O   1 
ATOM   1601 C  CB  . LEU   A 1 229 ? -11.300 -23.740 5.361   1.00 191.20 ? 249 LEU   A CB  1 
ATOM   1602 C  CG  . LEU   A 1 229 ? -10.675 -23.050 4.148   1.00 183.44 ? 249 LEU   A CG  1 
ATOM   1603 C  CD1 . LEU   A 1 229 ? -11.211 -23.638 2.853   1.00 163.69 ? 249 LEU   A CD1 1 
ATOM   1604 C  CD2 . LEU   A 1 229 ? -10.919 -21.550 4.204   1.00 169.84 ? 249 LEU   A CD2 1 
ATOM   1605 N  N   . ARG   A 1 230 ? -10.590 -25.268 8.269   1.00 220.93 ? 250 ARG   A N   1 
ATOM   1606 C  CA  . ARG   A 1 230 ? -11.093 -26.037 9.404   1.00 228.83 ? 250 ARG   A CA  1 
ATOM   1607 C  C   . ARG   A 1 230 ? -11.235 -25.188 10.659  1.00 233.99 ? 250 ARG   A C   1 
ATOM   1608 O  O   . ARG   A 1 230 ? -11.878 -25.629 11.619  1.00 231.43 ? 250 ARG   A O   1 
ATOM   1609 C  CB  . ARG   A 1 230 ? -10.182 -27.237 9.683   1.00 227.39 ? 250 ARG   A CB  1 
ATOM   1610 C  CG  . ARG   A 1 230 ? -10.208 -28.297 8.590   1.00 222.62 ? 250 ARG   A CG  1 
ATOM   1611 C  CD  . ARG   A 1 230 ? -9.370  -29.517 8.945   1.00 219.55 ? 250 ARG   A CD  1 
ATOM   1612 N  NE  . ARG   A 1 230 ? -9.962  -30.302 10.022  1.00 221.64 ? 250 ARG   A NE  1 
ATOM   1613 C  CZ  . ARG   A 1 230 ? -9.600  -31.540 10.331  1.00 219.68 ? 250 ARG   A CZ  1 
ATOM   1614 N  NH1 . ARG   A 1 230 ? -8.657  -32.175 9.655   1.00 213.88 ? 250 ARG   A NH1 1 
ATOM   1615 N  NH2 . ARG   A 1 230 ? -10.204 -32.158 11.342  1.00 221.59 ? 250 ARG   A NH2 1 
ATOM   1616 N  N   . LYS   A 1 231 ? -10.647 -23.996 10.676  1.00 257.38 ? 251 LYS   A N   1 
ATOM   1617 C  CA  . LYS   A 1 231 ? -10.873 -23.007 11.717  1.00 261.06 ? 251 LYS   A CA  1 
ATOM   1618 C  C   . LYS   A 1 231 ? -11.524 -21.731 11.208  1.00 257.92 ? 251 LYS   A C   1 
ATOM   1619 O  O   . LYS   A 1 231 ? -12.235 -21.077 11.972  1.00 262.21 ? 251 LYS   A O   1 
ATOM   1620 C  CB  . LYS   A 1 231 ? -9.549  -22.648 12.410  1.00 267.98 ? 251 LYS   A CB  1 
ATOM   1621 C  CG  . LYS   A 1 231 ? -8.370  -22.542 11.457  1.00 269.34 ? 251 LYS   A CG  1 
ATOM   1622 C  CD  . LYS   A 1 231 ? -7.099  -22.127 12.179  1.00 274.99 ? 251 LYS   A CD  1 
ATOM   1623 C  CE  . LYS   A 1 231 ? -5.868  -22.433 11.340  1.00 274.32 ? 251 LYS   A CE  1 
ATOM   1624 N  NZ  . LYS   A 1 231 ? -5.993  -21.915 9.949   1.00 273.53 ? 251 LYS   A NZ  1 
ATOM   1625 N  N   . SER   A 1 232 ? -11.316 -21.370 9.936   1.00 225.16 ? 252 SER   A N   1 
ATOM   1626 C  CA  . SER   A 1 232 ? -11.874 -20.127 9.412   1.00 223.76 ? 252 SER   A CA  1 
ATOM   1627 C  C   . SER   A 1 232 ? -13.395 -20.160 9.359   1.00 224.34 ? 252 SER   A C   1 
ATOM   1628 O  O   . SER   A 1 232 ? -14.040 -19.116 9.509   1.00 221.58 ? 252 SER   A O   1 
ATOM   1629 C  CB  . SER   A 1 232 ? -11.310 -19.835 8.023   1.00 210.01 ? 252 SER   A CB  1 
ATOM   1630 O  OG  . SER   A 1 232 ? -9.914  -19.596 8.078   1.00 204.54 ? 252 SER   A OG  1 
ATOM   1631 N  N   . VAL   A 1 233 ? -13.988 -21.334 9.135   1.00 216.87 ? 253 VAL   A N   1 
ATOM   1632 C  CA  . VAL   A 1 233 ? -15.443 -21.428 9.166   1.00 208.88 ? 253 VAL   A CA  1 
ATOM   1633 C  C   . VAL   A 1 233 ? -15.946 -21.332 10.600  1.00 209.52 ? 253 VAL   A C   1 
ATOM   1634 O  O   . VAL   A 1 233 ? -16.965 -20.687 10.874  1.00 201.92 ? 253 VAL   A O   1 
ATOM   1635 C  CB  . VAL   A 1 233 ? -15.912 -22.722 8.478   1.00 196.73 ? 253 VAL   A CB  1 
ATOM   1636 C  CG1 . VAL   A 1 233 ? -17.427 -22.738 8.354   1.00 186.92 ? 253 VAL   A CG1 1 
ATOM   1637 C  CG2 . VAL   A 1 233 ? -15.264 -22.855 7.109   1.00 186.64 ? 253 VAL   A CG2 1 
ATOM   1638 N  N   . LYS   A 1 234 ? -15.239 -21.968 11.539  1.00 216.32 ? 254 LYS   A N   1 
ATOM   1639 C  CA  . LYS   A 1 234 ? -15.483 -21.708 12.952  1.00 215.07 ? 254 LYS   A CA  1 
ATOM   1640 C  C   . LYS   A 1 234 ? -15.133 -20.273 13.322  1.00 212.98 ? 254 LYS   A C   1 
ATOM   1641 O  O   . LYS   A 1 234 ? -15.666 -19.747 14.307  1.00 209.50 ? 254 LYS   A O   1 
ATOM   1642 C  CB  . LYS   A 1 234 ? -14.679 -22.683 13.814  1.00 206.47 ? 254 LYS   A CB  1 
ATOM   1643 C  CG  . LYS   A 1 234 ? -14.911 -24.149 13.482  1.00 197.65 ? 254 LYS   A CG  1 
ATOM   1644 C  CD  . LYS   A 1 234 ? -13.976 -25.046 14.277  1.00 198.99 ? 254 LYS   A CD  1 
ATOM   1645 C  CE  . LYS   A 1 234 ? -14.143 -26.506 13.887  1.00 177.46 ? 254 LYS   A CE  1 
ATOM   1646 N  NZ  . LYS   A 1 234 ? -13.183 -27.386 14.608  1.00 176.60 ? 254 LYS   A NZ  1 
ATOM   1647 N  N   . ARG   A 1 235 ? -14.252 -19.633 12.553  1.00 215.73 ? 255 ARG   A N   1 
ATOM   1648 C  CA  . ARG   A 1 235 ? -13.903 -18.227 12.705  1.00 220.91 ? 255 ARG   A CA  1 
ATOM   1649 C  C   . ARG   A 1 235 ? -14.926 -17.297 12.058  1.00 215.73 ? 255 ARG   A C   1 
ATOM   1650 O  O   . ARG   A 1 235 ? -14.641 -16.108 11.879  1.00 217.41 ? 255 ARG   A O   1 
ATOM   1651 C  CB  . ARG   A 1 235 ? -12.516 -17.971 12.105  1.00 229.14 ? 255 ARG   A CB  1 
ATOM   1652 C  CG  . ARG   A 1 235 ? -11.749 -16.787 12.667  1.00 230.52 ? 255 ARG   A CG  1 
ATOM   1653 C  CD  . ARG   A 1 235 ? -10.576 -16.450 11.756  1.00 233.48 ? 255 ARG   A CD  1 
ATOM   1654 N  NE  . ARG   A 1 235 ? -9.789  -17.633 11.424  1.00 239.62 ? 255 ARG   A NE  1 
ATOM   1655 C  CZ  . ARG   A 1 235 ? -8.844  -17.669 10.494  1.00 236.00 ? 255 ARG   A CZ  1 
ATOM   1656 N  NH1 . ARG   A 1 235 ? -8.547  -16.603 9.768   1.00 233.83 ? 255 ARG   A NH1 1 
ATOM   1657 N  NH2 . ARG   A 1 235 ? -8.183  -18.804 10.285  1.00 232.06 ? 255 ARG   A NH2 1 
ATOM   1658 N  N   . MET   A 1 236 ? -16.103 -17.807 11.693  1.00 218.25 ? 256 MET   A N   1 
ATOM   1659 C  CA  . MET   A 1 236 ? -17.158 -16.990 11.103  1.00 210.32 ? 256 MET   A CA  1 
ATOM   1660 C  C   . MET   A 1 236 ? -18.526 -17.366 11.680  1.00 199.07 ? 256 MET   A C   1 
ATOM   1661 O  O   . MET   A 1 236 ? -19.435 -17.772 10.964  1.00 196.41 ? 256 MET   A O   1 
ATOM   1662 C  CB  . MET   A 1 236 ? -17.180 -17.135 9.581   1.00 208.59 ? 256 MET   A CB  1 
ATOM   1663 C  CG  . MET   A 1 236 ? -15.988 -16.547 8.848   1.00 208.94 ? 256 MET   A CG  1 
ATOM   1664 S  SD  . MET   A 1 236 ? -16.196 -16.680 7.060   1.00 188.36 ? 256 MET   A SD  1 
ATOM   1665 C  CE  . MET   A 1 236 ? -14.644 -16.002 6.479   1.00 201.07 ? 256 MET   A CE  1 
ATOM   1666 N  N   . ASP   A 1 250 ? -28.317 -16.218 5.099   1.00 204.81 ? 270 ASP   A N   1 
ATOM   1667 C  CA  . ASP   A 1 250 ? -27.252 -16.699 4.227   1.00 198.69 ? 270 ASP   A CA  1 
ATOM   1668 C  C   . ASP   A 1 250 ? -27.047 -18.201 4.386   1.00 189.60 ? 270 ASP   A C   1 
ATOM   1669 O  O   . ASP   A 1 250 ? -27.549 -18.804 5.331   1.00 189.01 ? 270 ASP   A O   1 
ATOM   1670 C  CB  . ASP   A 1 250 ? -25.945 -15.958 4.516   1.00 205.45 ? 270 ASP   A CB  1 
ATOM   1671 C  CG  . ASP   A 1 250 ? -26.015 -14.488 4.153   1.00 211.80 ? 270 ASP   A CG  1 
ATOM   1672 O  OD1 . ASP   A 1 250 ? -26.852 -14.126 3.299   1.00 211.39 ? 270 ASP   A OD1 1 
ATOM   1673 O  OD2 . ASP   A 1 250 ? -25.231 -13.697 4.716   1.00 216.59 ? 270 ASP   A OD2 1 
ATOM   1674 N  N   . PHE   A 1 251 ? -26.300 -18.791 3.448   1.00 177.44 ? 271 PHE   A N   1 
ATOM   1675 C  CA  . PHE   A 1 251 ? -26.024 -20.225 3.490   1.00 162.01 ? 271 PHE   A CA  1 
ATOM   1676 C  C   . PHE   A 1 251 ? -25.431 -20.642 4.830   1.00 157.37 ? 271 PHE   A C   1 
ATOM   1677 O  O   . PHE   A 1 251 ? -25.812 -21.674 5.393   1.00 155.64 ? 271 PHE   A O   1 
ATOM   1678 C  CB  . PHE   A 1 251 ? -25.091 -20.596 2.335   1.00 157.67 ? 271 PHE   A CB  1 
ATOM   1679 C  CG  . PHE   A 1 251 ? -24.358 -21.895 2.524   1.00 157.81 ? 271 PHE   A CG  1 
ATOM   1680 C  CD1 . PHE   A 1 251 ? -24.973 -23.103 2.244   1.00 155.45 ? 271 PHE   A CD1 1 
ATOM   1681 C  CD2 . PHE   A 1 251 ? -23.039 -21.903 2.950   1.00 157.15 ? 271 PHE   A CD2 1 
ATOM   1682 C  CE1 . PHE   A 1 251 ? -24.293 -24.297 2.405   1.00 141.92 ? 271 PHE   A CE1 1 
ATOM   1683 C  CE2 . PHE   A 1 251 ? -22.355 -23.092 3.114   1.00 148.81 ? 271 PHE   A CE2 1 
ATOM   1684 C  CZ  . PHE   A 1 251 ? -22.981 -24.289 2.837   1.00 132.54 ? 271 PHE   A CZ  1 
ATOM   1685 N  N   . LEU   A 1 252 ? -24.502 -19.845 5.362   1.00 174.89 ? 272 LEU   A N   1 
ATOM   1686 C  CA  . LEU   A 1 252 ? -23.973 -20.117 6.695   1.00 164.09 ? 272 LEU   A CA  1 
ATOM   1687 C  C   . LEU   A 1 252 ? -25.063 -19.996 7.751   1.00 171.38 ? 272 LEU   A C   1 
ATOM   1688 O  O   . LEU   A 1 252 ? -25.115 -20.791 8.698   1.00 169.30 ? 272 LEU   A O   1 
ATOM   1689 C  CB  . LEU   A 1 252 ? -22.820 -19.162 6.999   1.00 157.44 ? 272 LEU   A CB  1 
ATOM   1690 C  CG  . LEU   A 1 252 ? -22.303 -19.098 8.434   1.00 152.13 ? 272 LEU   A CG  1 
ATOM   1691 C  CD1 . LEU   A 1 252 ? -21.458 -20.318 8.761   1.00 154.19 ? 272 LEU   A CD1 1 
ATOM   1692 C  CD2 . LEU   A 1 252 ? -21.519 -17.815 8.637   1.00 168.38 ? 272 LEU   A CD2 1 
ATOM   1693 N  N   . GLN   A 1 253 ? -25.947 -19.008 7.603   1.00 174.64 ? 273 GLN   A N   1 
ATOM   1694 C  CA  . GLN   A 1 253 ? -27.059 -18.856 8.535   1.00 185.36 ? 273 GLN   A CA  1 
ATOM   1695 C  C   . GLN   A 1 253 ? -28.021 -20.035 8.435   1.00 189.08 ? 273 GLN   A C   1 
ATOM   1696 O  O   . GLN   A 1 253 ? -28.402 -20.627 9.451   1.00 185.97 ? 273 GLN   A O   1 
ATOM   1697 C  CB  . GLN   A 1 253 ? -27.788 -17.540 8.262   1.00 192.03 ? 273 GLN   A CB  1 
ATOM   1698 C  CG  . GLN   A 1 253 ? -28.932 -17.243 9.214   1.00 199.02 ? 273 GLN   A CG  1 
ATOM   1699 C  CD  . GLN   A 1 253 ? -28.511 -16.368 10.377  1.00 205.07 ? 273 GLN   A CD  1 
ATOM   1700 O  OE1 . GLN   A 1 253 ? -28.497 -15.141 10.272  1.00 214.32 ? 273 GLN   A OE1 1 
ATOM   1701 N  NE2 . GLN   A 1 253 ? -28.165 -16.994 11.495  1.00 200.95 ? 273 GLN   A NE2 1 
ATOM   1702 N  N   . LEU   A 1 254 ? -28.408 -20.402 7.211   1.00 185.38 ? 274 LEU   A N   1 
ATOM   1703 C  CA  . LEU   A 1 254 ? -29.402 -21.446 6.974   1.00 188.06 ? 274 LEU   A CA  1 
ATOM   1704 C  C   . LEU   A 1 254 ? -28.927 -22.843 7.365   1.00 183.90 ? 274 LEU   A C   1 
ATOM   1705 O  O   . LEU   A 1 254 ? -29.688 -23.799 7.176   1.00 184.30 ? 274 LEU   A O   1 
ATOM   1706 C  CB  . LEU   A 1 254 ? -29.821 -21.447 5.503   1.00 182.09 ? 274 LEU   A CB  1 
ATOM   1707 C  CG  . LEU   A 1 254 ? -30.327 -20.124 4.923   1.00 181.37 ? 274 LEU   A CG  1 
ATOM   1708 C  CD1 . LEU   A 1 254 ? -30.555 -20.258 3.427   1.00 167.20 ? 274 LEU   A CD1 1 
ATOM   1709 C  CD2 . LEU   A 1 254 ? -31.590 -19.654 5.630   1.00 184.27 ? 274 LEU   A CD2 1 
ATOM   1710 N  N   . MET   A 1 255 ? -27.711 -22.999 7.893   1.00 179.03 ? 275 MET   A N   1 
ATOM   1711 C  CA  . MET   A 1 255 ? -27.207 -24.300 8.320   1.00 186.84 ? 275 MET   A CA  1 
ATOM   1712 C  C   . MET   A 1 255 ? -27.366 -24.527 9.817   1.00 202.19 ? 275 MET   A C   1 
ATOM   1713 O  O   . MET   A 1 255 ? -27.915 -25.552 10.233  1.00 216.63 ? 275 MET   A O   1 
ATOM   1714 C  CB  . MET   A 1 255 ? -25.732 -24.454 7.926   1.00 175.97 ? 275 MET   A CB  1 
ATOM   1715 C  CG  . MET   A 1 255 ? -25.505 -24.594 6.433   1.00 172.85 ? 275 MET   A CG  1 
ATOM   1716 S  SD  . MET   A 1 255 ? -23.784 -24.919 6.011   1.00 167.17 ? 275 MET   A SD  1 
ATOM   1717 C  CE  . MET   A 1 255 ? -23.753 -26.708 6.032   1.00 155.32 ? 275 MET   A CE  1 
ATOM   1718 N  N   . ILE   A 1 256 ? -26.891 -23.590 10.640  1.00 205.10 ? 276 ILE   A N   1 
ATOM   1719 C  CA  . ILE   A 1 256 ? -27.061 -23.729 12.082  1.00 205.85 ? 276 ILE   A CA  1 
ATOM   1720 C  C   . ILE   A 1 256 ? -28.527 -23.583 12.461  1.00 224.07 ? 276 ILE   A C   1 
ATOM   1721 O  O   . ILE   A 1 256 ? -28.984 -24.179 13.444  1.00 224.81 ? 276 ILE   A O   1 
ATOM   1722 C  CB  . ILE   A 1 256 ? -26.185 -22.708 12.830  1.00 201.90 ? 276 ILE   A CB  1 
ATOM   1723 C  CG1 . ILE   A 1 256 ? -24.885 -22.458 12.066  1.00 191.04 ? 276 ILE   A CG1 1 
ATOM   1724 C  CG2 . ILE   A 1 256 ? -25.883 -23.202 14.238  1.00 189.49 ? 276 ILE   A CG2 1 
ATOM   1725 C  CD1 . ILE   A 1 256 ? -24.041 -21.345 12.648  1.00 169.30 ? 276 ILE   A CD1 1 
ATOM   1726 N  N   . ASP   A 1 257 ? -29.288 -22.794 11.697  1.00 240.80 ? 277 ASP   A N   1 
ATOM   1727 C  CA  . ASP   A 1 257 ? -30.712 -22.643 11.977  1.00 248.04 ? 277 ASP   A CA  1 
ATOM   1728 C  C   . ASP   A 1 257 ? -31.470 -23.940 11.731  1.00 248.03 ? 277 ASP   A C   1 
ATOM   1729 O  O   . ASP   A 1 257 ? -32.468 -24.211 12.409  1.00 239.63 ? 277 ASP   A O   1 
ATOM   1730 C  CB  . ASP   A 1 257 ? -31.298 -21.514 11.130  1.00 242.51 ? 277 ASP   A CB  1 
ATOM   1731 C  CG  . ASP   A 1 257 ? -30.607 -20.188 11.372  1.00 246.20 ? 277 ASP   A CG  1 
ATOM   1732 O  OD1 . ASP   A 1 257 ? -29.621 -20.161 12.138  1.00 247.72 ? 277 ASP   A OD1 1 
ATOM   1733 O  OD2 . ASP   A 1 257 ? -31.047 -19.172 10.793  1.00 255.94 ? 277 ASP   A OD2 1 
ATOM   1734 N  N   . SER   A 1 258 ? -31.021 -24.745 10.772  1.00 241.64 ? 278 SER   A N   1 
ATOM   1735 C  CA  . SER   A 1 258 ? -31.568 -26.074 10.547  1.00 242.59 ? 278 SER   A CA  1 
ATOM   1736 C  C   . SER   A 1 258 ? -30.834 -27.146 11.344  1.00 246.74 ? 278 SER   A C   1 
ATOM   1737 O  O   . SER   A 1 258 ? -31.113 -28.337 11.168  1.00 247.02 ? 278 SER   A O   1 
ATOM   1738 C  CB  . SER   A 1 258 ? -31.546 -26.409 9.053   1.00 226.94 ? 278 SER   A CB  1 
ATOM   1739 O  OG  . SER   A 1 258 ? -30.336 -25.985 8.450   1.00 220.48 ? 278 SER   A OG  1 
ATOM   1740 N  N   . GLN   A 1 259 ? -29.898 -26.749 12.207  1.00 236.02 ? 279 GLN   A N   1 
ATOM   1741 C  CA  . GLN   A 1 259 ? -29.270 -27.661 13.157  1.00 231.99 ? 279 GLN   A CA  1 
ATOM   1742 C  C   . GLN   A 1 259 ? -30.005 -27.642 14.494  1.00 234.18 ? 279 GLN   A C   1 
ATOM   1743 O  O   . GLN   A 1 259 ? -30.479 -28.682 14.964  1.00 233.74 ? 279 GLN   A O   1 
ATOM   1744 C  CB  . GLN   A 1 259 ? -27.793 -27.295 13.350  1.00 217.29 ? 279 GLN   A CB  1 
ATOM   1745 C  CG  . GLN   A 1 259 ? -27.152 -27.945 14.568  1.00 215.35 ? 279 GLN   A CG  1 
ATOM   1746 C  CD  . GLN   A 1 259 ? -25.746 -27.440 14.832  1.00 213.93 ? 279 GLN   A CD  1 
ATOM   1747 O  OE1 . GLN   A 1 259 ? -25.003 -27.122 13.904  1.00 206.46 ? 279 GLN   A OE1 1 
ATOM   1748 N  NE2 . GLN   A 1 259 ? -25.377 -27.358 16.105  1.00 206.23 ? 279 GLN   A NE2 1 
ATOM   1749 N  N   . ASN   A 1 260 ? -30.107 -26.464 15.108  1.00 237.41 ? 280 ASN   A N   1 
ATOM   1750 C  CA  . ASN   A 1 260 ? -30.817 -26.275 16.373  1.00 229.80 ? 280 ASN   A CA  1 
ATOM   1751 C  C   . ASN   A 1 260 ? -30.331 -27.228 17.462  1.00 225.18 ? 280 ASN   A C   1 
ATOM   1752 O  O   . ASN   A 1 260 ? -30.466 -26.946 18.652  1.00 223.59 ? 280 ASN   A O   1 
ATOM   1753 C  CB  . ASN   A 1 260 ? -32.326 -26.438 16.168  1.00 226.17 ? 280 ASN   A CB  1 
ATOM   1754 C  CG  . ASN   A 1 260 ? -32.932 -25.299 15.370  1.00 223.19 ? 280 ASN   A CG  1 
ATOM   1755 O  OD1 . ASN   A 1 260 ? -32.573 -24.136 15.555  1.00 216.01 ? 280 ASN   A OD1 1 
ATOM   1756 N  ND2 . ASN   A 1 260 ? -33.854 -25.630 14.473  1.00 223.26 ? 280 ASN   A ND2 1 
ATOM   1757 N  N   . LYS   A 1 268 ? -30.007 -36.672 13.498  1.00 216.43 ? 288 LYS   A N   1 
ATOM   1758 C  CA  . LYS   A 1 268 ? -30.775 -36.521 12.268  1.00 208.55 ? 288 LYS   A CA  1 
ATOM   1759 C  C   . LYS   A 1 268 ? -30.763 -35.063 11.809  1.00 212.73 ? 288 LYS   A C   1 
ATOM   1760 O  O   . LYS   A 1 268 ? -31.523 -34.664 10.920  1.00 208.00 ? 288 LYS   A O   1 
ATOM   1761 C  CB  . LYS   A 1 268 ? -32.212 -37.008 12.470  1.00 209.12 ? 288 LYS   A CB  1 
ATOM   1762 C  CG  . LYS   A 1 268 ? -32.882 -37.522 11.205  1.00 203.39 ? 288 LYS   A CG  1 
ATOM   1763 C  CD  . LYS   A 1 268 ? -34.289 -38.025 11.498  1.00 204.43 ? 288 LYS   A CD  1 
ATOM   1764 C  CE  . LYS   A 1 268 ? -34.999 -38.476 10.230  1.00 197.75 ? 288 LYS   A CE  1 
ATOM   1765 N  NZ  . LYS   A 1 268 ? -36.422 -38.837 10.489  1.00 190.82 ? 288 LYS   A NZ  1 
ATOM   1766 N  N   . ALA   A 1 269 ? -29.894 -34.268 12.433  1.00 217.94 ? 289 ALA   A N   1 
ATOM   1767 C  CA  . ALA   A 1 269 ? -29.706 -32.867 12.096  1.00 212.89 ? 289 ALA   A CA  1 
ATOM   1768 C  C   . ALA   A 1 269 ? -28.285 -32.669 11.564  1.00 206.87 ? 289 ALA   A C   1 
ATOM   1769 O  O   . ALA   A 1 269 ? -27.608 -33.638 11.198  1.00 211.11 ? 289 ALA   A O   1 
ATOM   1770 C  CB  . ALA   A 1 269 ? -30.008 -31.996 13.316  1.00 214.89 ? 289 ALA   A CB  1 
ATOM   1771 N  N   . LEU   A 1 270 ? -27.825 -31.420 11.536  1.00 205.88 ? 290 LEU   A N   1 
ATOM   1772 C  CA  . LEU   A 1 270 ? -26.545 -31.076 10.925  1.00 207.29 ? 290 LEU   A CA  1 
ATOM   1773 C  C   . LEU   A 1 270 ? -25.446 -30.977 11.978  1.00 207.67 ? 290 LEU   A C   1 
ATOM   1774 O  O   . LEU   A 1 270 ? -25.686 -30.554 13.110  1.00 218.77 ? 290 LEU   A O   1 
ATOM   1775 C  CB  . LEU   A 1 270 ? -26.643 -29.753 10.160  1.00 196.09 ? 290 LEU   A CB  1 
ATOM   1776 C  CG  . LEU   A 1 270 ? -25.381 -29.284 9.432   1.00 197.77 ? 290 LEU   A CG  1 
ATOM   1777 C  CD1 . LEU   A 1 270 ? -25.002 -30.254 8.319   1.00 190.38 ? 290 LEU   A CD1 1 
ATOM   1778 C  CD2 . LEU   A 1 270 ? -25.583 -27.885 8.893   1.00 195.63 ? 290 LEU   A CD2 1 
ATOM   1779 N  N   . SER   A 1 271 ? -24.229 -31.365 11.590  1.00 187.70 ? 291 SER   A N   1 
ATOM   1780 C  CA  . SER   A 1 271 ? -23.078 -31.331 12.483  1.00 174.99 ? 291 SER   A CA  1 
ATOM   1781 C  C   . SER   A 1 271 ? -22.296 -30.033 12.257  1.00 178.93 ? 291 SER   A C   1 
ATOM   1782 O  O   . SER   A 1 271 ? -22.823 -29.075 11.686  1.00 186.76 ? 291 SER   A O   1 
ATOM   1783 C  CB  . SER   A 1 271 ? -22.224 -32.586 12.274  1.00 169.64 ? 291 SER   A CB  1 
ATOM   1784 O  OG  . SER   A 1 271 ? -20.953 -32.437 12.884  1.00 165.46 ? 291 SER   A OG  1 
ATOM   1785 N  N   . ASP   A 1 272 ? -21.036 -29.986 12.694  1.00 156.36 ? 292 ASP   A N   1 
ATOM   1786 C  CA  . ASP   A 1 272 ? -20.211 -28.790 12.563  1.00 159.77 ? 292 ASP   A CA  1 
ATOM   1787 C  C   . ASP   A 1 272 ? -19.024 -28.991 11.637  1.00 153.77 ? 292 ASP   A C   1 
ATOM   1788 O  O   . ASP   A 1 272 ? -18.766 -28.140 10.777  1.00 150.97 ? 292 ASP   A O   1 
ATOM   1789 C  CB  . ASP   A 1 272 ? -19.723 -28.331 13.943  1.00 161.55 ? 292 ASP   A CB  1 
ATOM   1790 C  CG  . ASP   A 1 272 ? -20.823 -27.699 14.767  1.00 176.30 ? 292 ASP   A CG  1 
ATOM   1791 O  OD1 . ASP   A 1 272 ? -21.972 -27.631 14.280  1.00 163.27 ? 292 ASP   A OD1 1 
ATOM   1792 O  OD2 . ASP   A 1 272 ? -20.537 -27.268 15.903  1.00 194.95 ? 292 ASP   A OD2 1 
ATOM   1793 N  N   . LEU   A 1 273 ? -18.272 -30.085 11.797  1.00 147.53 ? 293 LEU   A N   1 
ATOM   1794 C  CA  . LEU   A 1 273 ? -17.213 -30.385 10.839  1.00 154.52 ? 293 LEU   A CA  1 
ATOM   1795 C  C   . LEU   A 1 273 ? -17.786 -30.625 9.451   1.00 155.75 ? 293 LEU   A C   1 
ATOM   1796 O  O   . LEU   A 1 273 ? -17.119 -30.358 8.445   1.00 151.20 ? 293 LEU   A O   1 
ATOM   1797 C  CB  . LEU   A 1 273 ? -16.400 -31.598 11.300  1.00 146.24 ? 293 LEU   A CB  1 
ATOM   1798 C  CG  . LEU   A 1 273 ? -15.231 -32.025 10.408  1.00 144.81 ? 293 LEU   A CG  1 
ATOM   1799 C  CD1 . LEU   A 1 273 ? -14.266 -30.869 10.192  1.00 151.01 ? 293 LEU   A CD1 1 
ATOM   1800 C  CD2 . LEU   A 1 273 ? -14.505 -33.227 10.996  1.00 160.30 ? 293 LEU   A CD2 1 
ATOM   1801 N  N   . GLU   A 1 274 ? -19.021 -31.122 9.377   1.00 158.39 ? 294 GLU   A N   1 
ATOM   1802 C  CA  . GLU   A 1 274 ? -19.680 -31.261 8.085   1.00 149.98 ? 294 GLU   A CA  1 
ATOM   1803 C  C   . GLU   A 1 274 ? -20.126 -29.910 7.545   1.00 145.78 ? 294 GLU   A C   1 
ATOM   1804 O  O   . GLU   A 1 274 ? -20.225 -29.735 6.325   1.00 136.97 ? 294 GLU   A O   1 
ATOM   1805 C  CB  . GLU   A 1 274 ? -20.866 -32.218 8.206   1.00 159.45 ? 294 GLU   A CB  1 
ATOM   1806 C  CG  . GLU   A 1 274 ? -20.494 -33.577 8.777   1.00 173.29 ? 294 GLU   A CG  1 
ATOM   1807 C  CD  . GLU   A 1 274 ? -21.689 -34.495 8.937   1.00 182.70 ? 294 GLU   A CD  1 
ATOM   1808 O  OE1 . GLU   A 1 274 ? -22.788 -33.992 9.255   1.00 177.45 ? 294 GLU   A OE1 1 
ATOM   1809 O  OE2 . GLU   A 1 274 ? -21.533 -35.718 8.738   1.00 187.30 ? 294 GLU   A OE2 1 
ATOM   1810 N  N   . LEU   A 1 275 ? -20.392 -28.946 8.430   1.00 154.66 ? 295 LEU   A N   1 
ATOM   1811 C  CA  . LEU   A 1 275 ? -20.722 -27.597 7.980   1.00 148.36 ? 295 LEU   A CA  1 
ATOM   1812 C  C   . LEU   A 1 275 ? -19.544 -26.965 7.250   1.00 141.69 ? 295 LEU   A C   1 
ATOM   1813 O  O   . LEU   A 1 275 ? -19.729 -26.235 6.268   1.00 136.59 ? 295 LEU   A O   1 
ATOM   1814 C  CB  . LEU   A 1 275 ? -21.150 -26.739 9.174   1.00 145.23 ? 295 LEU   A CB  1 
ATOM   1815 C  CG  . LEU   A 1 275 ? -21.775 -25.360 8.937   1.00 154.42 ? 295 LEU   A CG  1 
ATOM   1816 C  CD1 . LEU   A 1 275 ? -22.706 -25.005 10.085  1.00 164.29 ? 295 LEU   A CD1 1 
ATOM   1817 C  CD2 . LEU   A 1 275 ? -20.719 -24.276 8.771   1.00 156.95 ? 295 LEU   A CD2 1 
ATOM   1818 N  N   . VAL   A 1 276 ? -18.324 -27.237 7.715   1.00 141.01 ? 296 VAL   A N   1 
ATOM   1819 C  CA  . VAL   A 1 276 ? -17.135 -26.732 7.037   1.00 143.33 ? 296 VAL   A CA  1 
ATOM   1820 C  C   . VAL   A 1 276 ? -16.989 -27.377 5.665   1.00 137.72 ? 296 VAL   A C   1 
ATOM   1821 O  O   . VAL   A 1 276 ? -16.646 -26.708 4.683   1.00 132.87 ? 296 VAL   A O   1 
ATOM   1822 C  CB  . VAL   A 1 276 ? -15.888 -26.967 7.908   1.00 148.33 ? 296 VAL   A CB  1 
ATOM   1823 C  CG1 . VAL   A 1 276 ? -14.637 -26.464 7.201   1.00 150.27 ? 296 VAL   A CG1 1 
ATOM   1824 C  CG2 . VAL   A 1 276 ? -16.052 -26.297 9.264   1.00 154.82 ? 296 VAL   A CG2 1 
ATOM   1825 N  N   . ALA   A 1 277 ? -17.256 -28.683 5.572   1.00 129.90 ? 297 ALA   A N   1 
ATOM   1826 C  CA  . ALA   A 1 277 ? -17.086 -29.389 4.305   1.00 132.37 ? 297 ALA   A CA  1 
ATOM   1827 C  C   . ALA   A 1 277 ? -18.030 -28.852 3.237   1.00 127.12 ? 297 ALA   A C   1 
ATOM   1828 O  O   . ALA   A 1 277 ? -17.655 -28.746 2.064   1.00 120.99 ? 297 ALA   A O   1 
ATOM   1829 C  CB  . ALA   A 1 277 ? -17.301 -30.889 4.507   1.00 141.64 ? 297 ALA   A CB  1 
ATOM   1830 N  N   . GLN   A 1 278 ? -19.263 -28.509 3.621   1.00 129.16 ? 298 GLN   A N   1 
ATOM   1831 C  CA  . GLN   A 1 278 ? -20.187 -27.929 2.653   1.00 123.72 ? 298 GLN   A CA  1 
ATOM   1832 C  C   . GLN   A 1 278 ? -19.759 -26.525 2.250   1.00 117.45 ? 298 GLN   A C   1 
ATOM   1833 O  O   . GLN   A 1 278 ? -19.989 -26.113 1.108   1.00 127.13 ? 298 GLN   A O   1 
ATOM   1834 C  CB  . GLN   A 1 278 ? -21.609 -27.908 3.216   1.00 117.47 ? 298 GLN   A CB  1 
ATOM   1835 C  CG  . GLN   A 1 278 ? -22.058 -29.213 3.858   1.00 119.65 ? 298 GLN   A CG  1 
ATOM   1836 C  CD  . GLN   A 1 278 ? -21.956 -30.408 2.927   1.00 121.79 ? 298 GLN   A CD  1 
ATOM   1837 O  OE1 . GLN   A 1 278 ? -22.044 -30.274 1.706   1.00 132.21 ? 298 GLN   A OE1 1 
ATOM   1838 N  NE2 . GLN   A 1 278 ? -21.770 -31.589 3.505   1.00 118.68 ? 298 GLN   A NE2 1 
ATOM   1839 N  N   . SER   A 1 279 ? -19.140 -25.779 3.168   1.00 108.37 ? 299 SER   A N   1 
ATOM   1840 C  CA  . SER   A 1 279 ? -18.624 -24.460 2.820   1.00 119.01 ? 299 SER   A CA  1 
ATOM   1841 C  C   . SER   A 1 279 ? -17.530 -24.563 1.766   1.00 120.50 ? 299 SER   A C   1 
ATOM   1842 O  O   . SER   A 1 279 ? -17.491 -23.768 0.821   1.00 124.07 ? 299 SER   A O   1 
ATOM   1843 C  CB  . SER   A 1 279 ? -18.102 -23.753 4.070   1.00 128.09 ? 299 SER   A CB  1 
ATOM   1844 O  OG  . SER   A 1 279 ? -19.127 -23.600 5.037   1.00 140.14 ? 299 SER   A OG  1 
ATOM   1845 N  N   . ILE   A 1 280 ? -16.637 -25.546 1.907   1.00 113.48 ? 300 ILE   A N   1 
ATOM   1846 C  CA  . ILE   A 1 280 ? -15.560 -25.724 0.937   1.00 107.76 ? 300 ILE   A CA  1 
ATOM   1847 C  C   . ILE   A 1 280 ? -16.128 -26.031 -0.442  1.00 115.36 ? 300 ILE   A C   1 
ATOM   1848 O  O   . ILE   A 1 280 ? -15.637 -25.528 -1.460  1.00 119.70 ? 300 ILE   A O   1 
ATOM   1849 C  CB  . ILE   A 1 280 ? -14.597 -26.829 1.409   1.00 112.26 ? 300 ILE   A CB  1 
ATOM   1850 C  CG1 . ILE   A 1 280 ? -14.087 -26.523 2.818   1.00 121.32 ? 300 ILE   A CG1 1 
ATOM   1851 C  CG2 . ILE   A 1 280 ? -13.437 -26.975 0.436   1.00 116.58 ? 300 ILE   A CG2 1 
ATOM   1852 C  CD1 . ILE   A 1 280 ? -13.334 -27.667 3.456   1.00 134.38 ? 300 ILE   A CD1 1 
ATOM   1853 N  N   . ILE   A 1 281 ? -17.171 -26.862 -0.497  1.00 113.85 ? 301 ILE   A N   1 
ATOM   1854 C  CA  . ILE   A 1 281 ? -17.797 -27.194 -1.774  1.00 114.86 ? 301 ILE   A CA  1 
ATOM   1855 C  C   . ILE   A 1 281 ? -18.387 -25.946 -2.416  1.00 113.57 ? 301 ILE   A C   1 
ATOM   1856 O  O   . ILE   A 1 281 ? -18.179 -25.679 -3.606  1.00 125.68 ? 301 ILE   A O   1 
ATOM   1857 C  CB  . ILE   A 1 281 ? -18.868 -28.282 -1.578  1.00 114.86 ? 301 ILE   A CB  1 
ATOM   1858 C  CG1 . ILE   A 1 281 ? -18.212 -29.599 -1.170  1.00 124.72 ? 301 ILE   A CG1 1 
ATOM   1859 C  CG2 . ILE   A 1 281 ? -19.689 -28.460 -2.846  1.00 116.51 ? 301 ILE   A CG2 1 
ATOM   1860 C  CD1 . ILE   A 1 281 ? -17.271 -30.148 -2.211  1.00 131.49 ? 301 ILE   A CD1 1 
ATOM   1861 N  N   . PHE   A 1 282 ? -19.127 -25.161 -1.633  1.00 113.04 ? 302 PHE   A N   1 
ATOM   1862 C  CA  . PHE   A 1 282 ? -19.776 -23.970 -2.172  1.00 122.10 ? 302 PHE   A CA  1 
ATOM   1863 C  C   . PHE   A 1 282 ? -18.754 -22.910 -2.565  1.00 122.74 ? 302 PHE   A C   1 
ATOM   1864 O  O   . PHE   A 1 282 ? -18.896 -22.262 -3.609  1.00 125.77 ? 302 PHE   A O   1 
ATOM   1865 C  CB  . PHE   A 1 282 ? -20.765 -23.407 -1.151  1.00 128.13 ? 302 PHE   A CB  1 
ATOM   1866 C  CG  . PHE   A 1 282 ? -22.083 -24.134 -1.107  1.00 129.33 ? 302 PHE   A CG  1 
ATOM   1867 C  CD1 . PHE   A 1 282 ? -22.134 -25.518 -1.045  1.00 130.55 ? 302 PHE   A CD1 1 
ATOM   1868 C  CD2 . PHE   A 1 282 ? -23.273 -23.428 -1.109  1.00 134.46 ? 302 PHE   A CD2 1 
ATOM   1869 C  CE1 . PHE   A 1 282 ? -23.345 -26.181 -0.999  1.00 122.05 ? 302 PHE   A CE1 1 
ATOM   1870 C  CE2 . PHE   A 1 282 ? -24.487 -24.086 -1.061  1.00 126.51 ? 302 PHE   A CE2 1 
ATOM   1871 C  CZ  . PHE   A 1 282 ? -24.523 -25.463 -1.007  1.00 122.60 ? 302 PHE   A CZ  1 
ATOM   1872 N  N   . ILE   A 1 283 ? -17.719 -22.720 -1.743  1.00 120.65 ? 303 ILE   A N   1 
ATOM   1873 C  CA  . ILE   A 1 283 ? -16.732 -21.678 -2.014  1.00 114.83 ? 303 ILE   A CA  1 
ATOM   1874 C  C   . ILE   A 1 283 ? -15.976 -21.977 -3.303  1.00 116.59 ? 303 ILE   A C   1 
ATOM   1875 O  O   . ILE   A 1 283 ? -15.706 -21.074 -4.105  1.00 130.62 ? 303 ILE   A O   1 
ATOM   1876 C  CB  . ILE   A 1 283 ? -15.782 -21.520 -0.811  1.00 113.64 ? 303 ILE   A CB  1 
ATOM   1877 C  CG1 . ILE   A 1 283 ? -16.517 -20.854 0.354   1.00 121.90 ? 303 ILE   A CG1 1 
ATOM   1878 C  CG2 . ILE   A 1 283 ? -14.551 -20.713 -1.193  1.00 116.12 ? 303 ILE   A CG2 1 
ATOM   1879 C  CD1 . ILE   A 1 283 ? -15.767 -20.912 1.664   1.00 122.50 ? 303 ILE   A CD1 1 
ATOM   1880 N  N   . PHE   A 1 284 ? -15.632 -23.246 -3.532  1.00 108.57 ? 304 PHE   A N   1 
ATOM   1881 C  CA  . PHE   A 1 284 ? -14.993 -23.613 -4.792  1.00 116.06 ? 304 PHE   A CA  1 
ATOM   1882 C  C   . PHE   A 1 284 ? -15.969 -23.492 -5.955  1.00 122.36 ? 304 PHE   A C   1 
ATOM   1883 O  O   . PHE   A 1 284 ? -15.629 -22.944 -7.010  1.00 134.69 ? 304 PHE   A O   1 
ATOM   1884 C  CB  . PHE   A 1 284 ? -14.435 -25.034 -4.715  1.00 111.16 ? 304 PHE   A CB  1 
ATOM   1885 C  CG  . PHE   A 1 284 ? -13.980 -25.578 -6.044  1.00 119.43 ? 304 PHE   A CG  1 
ATOM   1886 C  CD1 . PHE   A 1 284 ? -12.713 -25.292 -6.527  1.00 122.96 ? 304 PHE   A CD1 1 
ATOM   1887 C  CD2 . PHE   A 1 284 ? -14.819 -26.373 -6.811  1.00 117.30 ? 304 PHE   A CD2 1 
ATOM   1888 C  CE1 . PHE   A 1 284 ? -12.292 -25.788 -7.748  1.00 121.29 ? 304 PHE   A CE1 1 
ATOM   1889 C  CE2 . PHE   A 1 284 ? -14.404 -26.870 -8.033  1.00 124.21 ? 304 PHE   A CE2 1 
ATOM   1890 C  CZ  . PHE   A 1 284 ? -13.139 -26.577 -8.501  1.00 124.03 ? 304 PHE   A CZ  1 
ATOM   1891 N  N   . ALA   A 1 285 ? -17.187 -24.012 -5.779  1.00 121.71 ? 305 ALA   A N   1 
ATOM   1892 C  CA  . ALA   A 1 285 ? -18.159 -24.038 -6.868  1.00 127.13 ? 305 ALA   A CA  1 
ATOM   1893 C  C   . ALA   A 1 285 ? -18.466 -22.634 -7.371  1.00 127.87 ? 305 ALA   A C   1 
ATOM   1894 O  O   . ALA   A 1 285 ? -18.443 -22.376 -8.580  1.00 128.05 ? 305 ALA   A O   1 
ATOM   1895 C  CB  . ALA   A 1 285 ? -19.437 -24.738 -6.408  1.00 109.48 ? 305 ALA   A CB  1 
ATOM   1896 N  N   . GLY   A 1 286 ? -18.745 -21.706 -6.455  1.00 143.28 ? 306 GLY   A N   1 
ATOM   1897 C  CA  . GLY   A 1 286 ? -19.056 -20.348 -6.860  1.00 148.54 ? 306 GLY   A CA  1 
ATOM   1898 C  C   . GLY   A 1 286 ? -17.875 -19.581 -7.413  1.00 150.82 ? 306 GLY   A C   1 
ATOM   1899 O  O   . GLY   A 1 286 ? -18.071 -18.628 -8.173  1.00 150.81 ? 306 GLY   A O   1 
ATOM   1900 N  N   . TYR   A 1 287 ? -16.651 -19.971 -7.055  1.00 133.70 ? 307 TYR   A N   1 
ATOM   1901 C  CA  . TYR   A 1 287 ? -15.472 -19.281 -7.580  1.00 130.53 ? 307 TYR   A CA  1 
ATOM   1902 C  C   . TYR   A 1 287 ? -15.102 -19.802 -8.966  1.00 133.67 ? 307 TYR   A C   1 
ATOM   1903 O  O   . TYR   A 1 287 ? -15.187 -19.074 -9.960  1.00 135.59 ? 307 TYR   A O   1 
ATOM   1904 C  CB  . TYR   A 1 287 ? -14.289 -19.429 -6.618  1.00 136.63 ? 307 TYR   A CB  1 
ATOM   1905 C  CG  . TYR   A 1 287 ? -12.978 -18.954 -7.217  1.00 145.89 ? 307 TYR   A CG  1 
ATOM   1906 C  CD1 . TYR   A 1 287 ? -12.663 -17.602 -7.257  1.00 152.88 ? 307 TYR   A CD1 1 
ATOM   1907 C  CD2 . TYR   A 1 287 ? -12.062 -19.855 -7.750  1.00 147.15 ? 307 TYR   A CD2 1 
ATOM   1908 C  CE1 . TYR   A 1 287 ? -11.474 -17.162 -7.806  1.00 152.48 ? 307 TYR   A CE1 1 
ATOM   1909 C  CE2 . TYR   A 1 287 ? -10.872 -19.422 -8.304  1.00 145.33 ? 307 TYR   A CE2 1 
ATOM   1910 C  CZ  . TYR   A 1 287 ? -10.584 -18.075 -8.328  1.00 154.96 ? 307 TYR   A CZ  1 
ATOM   1911 O  OH  . TYR   A 1 287 ? -9.402  -17.637 -8.876  1.00 174.95 ? 307 TYR   A OH  1 
ATOM   1912 N  N   . GLU   A 1 288 ? -14.681 -21.067 -9.041  1.00 128.42 ? 308 GLU   A N   1 
ATOM   1913 C  CA  . GLU   A 1 288 ? -14.066 -21.577 -10.263 1.00 130.40 ? 308 GLU   A CA  1 
ATOM   1914 C  C   . GLU   A 1 288 ? -15.078 -21.677 -11.398 1.00 126.77 ? 308 GLU   A C   1 
ATOM   1915 O  O   . GLU   A 1 288 ? -14.799 -21.257 -12.526 1.00 126.78 ? 308 GLU   A O   1 
ATOM   1916 C  CB  . GLU   A 1 288 ? -13.417 -22.935 -9.990  1.00 132.54 ? 308 GLU   A CB  1 
ATOM   1917 C  CG  . GLU   A 1 288 ? -12.131 -23.178 -10.767 1.00 132.87 ? 308 GLU   A CG  1 
ATOM   1918 C  CD  . GLU   A 1 288 ? -12.352 -23.250 -12.265 1.00 143.48 ? 308 GLU   A CD  1 
ATOM   1919 O  OE1 . GLU   A 1 288 ? -13.359 -23.853 -12.691 1.00 142.49 ? 308 GLU   A OE1 1 
ATOM   1920 O  OE2 . GLU   A 1 288 ? -11.520 -22.700 -13.016 1.00 131.50 ? 308 GLU   A OE2 1 
ATOM   1921 N  N   . THR   A 1 289 ? -16.260 -22.229 -11.119 1.00 127.75 ? 309 THR   A N   1 
ATOM   1922 C  CA  . THR   A 1 289 ? -17.252 -22.428 -12.172 1.00 124.55 ? 309 THR   A CA  1 
ATOM   1923 C  C   . THR   A 1 289 ? -17.710 -21.098 -12.757 1.00 130.08 ? 309 THR   A C   1 
ATOM   1924 O  O   . THR   A 1 289 ? -17.802 -20.943 -13.981 1.00 119.23 ? 309 THR   A O   1 
ATOM   1925 C  CB  . THR   A 1 289 ? -18.447 -23.213 -11.632 1.00 118.23 ? 309 THR   A CB  1 
ATOM   1926 O  OG1 . THR   A 1 289 ? -19.155 -22.411 -10.679 1.00 122.70 ? 309 THR   A OG1 1 
ATOM   1927 C  CG2 . THR   A 1 289 ? -17.978 -24.492 -10.960 1.00 117.17 ? 309 THR   A CG2 1 
ATOM   1928 N  N   . THR   A 1 290 ? -18.000 -20.121 -11.895 1.00 138.18 ? 310 THR   A N   1 
ATOM   1929 C  CA  . THR   A 1 290 ? -18.470 -18.825 -12.375 1.00 130.76 ? 310 THR   A CA  1 
ATOM   1930 C  C   . THR   A 1 290 ? -17.388 -18.110 -13.176 1.00 123.17 ? 310 THR   A C   1 
ATOM   1931 O  O   . THR   A 1 290 ? -17.656 -17.570 -14.255 1.00 124.78 ? 310 THR   A O   1 
ATOM   1932 C  CB  . THR   A 1 290 ? -18.927 -17.962 -11.198 1.00 126.76 ? 310 THR   A CB  1 
ATOM   1933 O  OG1 . THR   A 1 290 ? -19.899 -18.678 -10.426 1.00 134.51 ? 310 THR   A OG1 1 
ATOM   1934 C  CG2 . THR   A 1 290 ? -19.544 -16.664 -11.698 1.00 125.07 ? 310 THR   A CG2 1 
ATOM   1935 N  N   . SER   A 1 291 ? -16.154 -18.103 -12.667 1.00 130.65 ? 311 SER   A N   1 
ATOM   1936 C  CA  . SER   A 1 291 ? -15.074 -17.408 -13.360 1.00 120.65 ? 311 SER   A CA  1 
ATOM   1937 C  C   . SER   A 1 291 ? -14.720 -18.096 -14.673 1.00 112.14 ? 311 SER   A C   1 
ATOM   1938 O  O   . SER   A 1 291 ? -14.406 -17.426 -15.665 1.00 114.33 ? 311 SER   A O   1 
ATOM   1939 C  CB  . SER   A 1 291 ? -13.845 -17.317 -12.456 1.00 124.43 ? 311 SER   A CB  1 
ATOM   1940 O  OG  . SER   A 1 291 ? -13.399 -18.606 -12.070 1.00 122.84 ? 311 SER   A OG  1 
ATOM   1941 N  N   . SER   A 1 292 ? -14.767 -19.429 -14.701 1.00 109.15 ? 312 SER   A N   1 
ATOM   1942 C  CA  . SER   A 1 292 ? -14.366 -20.158 -15.901 1.00 115.05 ? 312 SER   A CA  1 
ATOM   1943 C  C   . SER   A 1 292 ? -15.364 -19.951 -17.033 1.00 109.74 ? 312 SER   A C   1 
ATOM   1944 O  O   . SER   A 1 292 ? -14.974 -19.704 -18.180 1.00 111.24 ? 312 SER   A O   1 
ATOM   1945 C  CB  . SER   A 1 292 ? -14.211 -21.646 -15.586 1.00 121.14 ? 312 SER   A CB  1 
ATOM   1946 O  OG  . SER   A 1 292 ? -13.736 -22.361 -16.713 1.00 126.07 ? 312 SER   A OG  1 
ATOM   1947 N  N   . VAL   A 1 293 ? -16.660 -20.050 -16.732 1.00 117.94 ? 313 VAL   A N   1 
ATOM   1948 C  CA  . VAL   A 1 293 ? -17.671 -19.882 -17.770 1.00 116.81 ? 313 VAL   A CA  1 
ATOM   1949 C  C   . VAL   A 1 293 ? -17.708 -18.436 -18.249 1.00 106.45 ? 313 VAL   A C   1 
ATOM   1950 O  O   . VAL   A 1 293 ? -17.909 -18.169 -19.440 1.00 101.82 ? 313 VAL   A O   1 
ATOM   1951 C  CB  . VAL   A 1 293 ? -19.044 -20.353 -17.260 1.00 111.80 ? 313 VAL   A CB  1 
ATOM   1952 C  CG1 . VAL   A 1 293 ? -20.099 -20.186 -18.341 1.00 114.77 ? 313 VAL   A CG1 1 
ATOM   1953 C  CG2 . VAL   A 1 293 ? -18.968 -21.804 -16.814 1.00 101.71 ? 313 VAL   A CG2 1 
ATOM   1954 N  N   . LEU   A 1 294 ? -17.507 -17.481 -17.337 1.00 111.33 ? 314 LEU   A N   1 
ATOM   1955 C  CA  . LEU   A 1 294 ? -17.442 -16.080 -17.741 1.00 119.63 ? 314 LEU   A CA  1 
ATOM   1956 C  C   . LEU   A 1 294 ? -16.256 -15.829 -18.664 1.00 116.22 ? 314 LEU   A C   1 
ATOM   1957 O  O   . LEU   A 1 294 ? -16.339 -15.005 -19.582 1.00 114.29 ? 314 LEU   A O   1 
ATOM   1958 C  CB  . LEU   A 1 294 ? -17.368 -15.177 -16.509 1.00 115.72 ? 314 LEU   A CB  1 
ATOM   1959 C  CG  . LEU   A 1 294 ? -18.680 -14.943 -15.758 1.00 120.80 ? 314 LEU   A CG  1 
ATOM   1960 C  CD1 . LEU   A 1 294 ? -18.435 -14.158 -14.479 1.00 118.19 ? 314 LEU   A CD1 1 
ATOM   1961 C  CD2 . LEU   A 1 294 ? -19.680 -14.222 -16.646 1.00 114.70 ? 314 LEU   A CD2 1 
ATOM   1962 N  N   . SER   A 1 295 ? -15.143 -16.530 -18.436 1.00 108.65 ? 315 SER   A N   1 
ATOM   1963 C  CA  . SER   A 1 295 ? -14.011 -16.430 -19.350 1.00 104.90 ? 315 SER   A CA  1 
ATOM   1964 C  C   . SER   A 1 295 ? -14.370 -16.980 -20.724 1.00 109.63 ? 315 SER   A C   1 
ATOM   1965 O  O   . SER   A 1 295 ? -13.989 -16.406 -21.752 1.00 115.76 ? 315 SER   A O   1 
ATOM   1966 C  CB  . SER   A 1 295 ? -12.803 -17.170 -18.774 1.00 109.42 ? 315 SER   A CB  1 
ATOM   1967 O  OG  . SER   A 1 295 ? -12.482 -16.697 -17.478 1.00 122.97 ? 315 SER   A OG  1 
ATOM   1968 N  N   . PHE   A 1 296 ? -15.108 -18.092 -20.761 1.00 106.21 ? 316 PHE   A N   1 
ATOM   1969 C  CA  . PHE   A 1 296 ? -15.540 -18.659 -22.034 1.00 98.22  ? 316 PHE   A CA  1 
ATOM   1970 C  C   . PHE   A 1 296 ? -16.513 -17.735 -22.754 1.00 100.53 ? 316 PHE   A C   1 
ATOM   1971 O  O   . PHE   A 1 296 ? -16.480 -17.628 -23.986 1.00 90.25  ? 316 PHE   A O   1 
ATOM   1972 C  CB  . PHE   A 1 296 ? -16.181 -20.028 -21.806 1.00 107.54 ? 316 PHE   A CB  1 
ATOM   1973 C  CG  . PHE   A 1 296 ? -15.193 -21.133 -21.564 1.00 99.84  ? 316 PHE   A CG  1 
ATOM   1974 C  CD1 . PHE   A 1 296 ? -14.077 -21.272 -22.371 1.00 106.57 ? 316 PHE   A CD1 1 
ATOM   1975 C  CD2 . PHE   A 1 296 ? -15.382 -22.033 -20.528 1.00 104.98 ? 316 PHE   A CD2 1 
ATOM   1976 C  CE1 . PHE   A 1 296 ? -13.168 -22.290 -22.151 1.00 105.30 ? 316 PHE   A CE1 1 
ATOM   1977 C  CE2 . PHE   A 1 296 ? -14.476 -23.052 -20.302 1.00 108.21 ? 316 PHE   A CE2 1 
ATOM   1978 C  CZ  . PHE   A 1 296 ? -13.368 -23.181 -21.115 1.00 109.29 ? 316 PHE   A CZ  1 
ATOM   1979 N  N   . ILE   A 1 297 ? -17.388 -17.062 -22.006 1.00 103.04 ? 317 ILE   A N   1 
ATOM   1980 C  CA  . ILE   A 1 297 ? -18.411 -16.225 -22.627 1.00 110.41 ? 317 ILE   A CA  1 
ATOM   1981 C  C   . ILE   A 1 297 ? -17.780 -15.001 -23.279 1.00 111.51 ? 317 ILE   A C   1 
ATOM   1982 O  O   . ILE   A 1 297 ? -18.103 -14.651 -24.420 1.00 112.03 ? 317 ILE   A O   1 
ATOM   1983 C  CB  . ILE   A 1 297 ? -19.481 -15.828 -21.594 1.00 114.06 ? 317 ILE   A CB  1 
ATOM   1984 C  CG1 . ILE   A 1 297 ? -20.322 -17.045 -21.207 1.00 112.76 ? 317 ILE   A CG1 1 
ATOM   1985 C  CG2 . ILE   A 1 297 ? -20.369 -14.717 -22.137 1.00 115.02 ? 317 ILE   A CG2 1 
ATOM   1986 C  CD1 . ILE   A 1 297 ? -21.446 -16.733 -20.247 1.00 117.70 ? 317 ILE   A CD1 1 
ATOM   1987 N  N   . MET   A 1 298 ? -16.867 -14.334 -22.569 1.00 109.98 ? 318 MET   A N   1 
ATOM   1988 C  CA  . MET   A 1 298 ? -16.258 -13.127 -23.116 1.00 120.66 ? 318 MET   A CA  1 
ATOM   1989 C  C   . MET   A 1 298 ? -15.343 -13.438 -24.294 1.00 112.50 ? 318 MET   A C   1 
ATOM   1990 O  O   . MET   A 1 298 ? -15.163 -12.589 -25.175 1.00 109.13 ? 318 MET   A O   1 
ATOM   1991 C  CB  . MET   A 1 298 ? -15.494 -12.380 -22.025 1.00 114.92 ? 318 MET   A CB  1 
ATOM   1992 C  CG  . MET   A 1 298 ? -16.348 -12.009 -20.828 1.00 127.34 ? 318 MET   A CG  1 
ATOM   1993 S  SD  . MET   A 1 298 ? -17.964 -11.359 -21.293 1.00 144.78 ? 318 MET   A SD  1 
ATOM   1994 C  CE  . MET   A 1 298 ? -17.508 -9.867  -22.168 1.00 137.94 ? 318 MET   A CE  1 
ATOM   1995 N  N   . TYR   A 1 299 ? -14.759 -14.638 -24.330 1.00 105.66 ? 319 TYR   A N   1 
ATOM   1996 C  CA  . TYR   A 1 299 ? -13.991 -15.041 -25.503 1.00 107.71 ? 319 TYR   A CA  1 
ATOM   1997 C  C   . TYR   A 1 299 ? -14.895 -15.172 -26.722 1.00 106.51 ? 319 TYR   A C   1 
ATOM   1998 O  O   . TYR   A 1 299 ? -14.564 -14.688 -27.811 1.00 124.51 ? 319 TYR   A O   1 
ATOM   1999 C  CB  . TYR   A 1 299 ? -13.260 -16.358 -25.236 1.00 114.69 ? 319 TYR   A CB  1 
ATOM   2000 C  CG  . TYR   A 1 299 ? -12.685 -16.988 -26.489 1.00 123.34 ? 319 TYR   A CG  1 
ATOM   2001 C  CD1 . TYR   A 1 299 ? -11.464 -16.571 -27.001 1.00 130.53 ? 319 TYR   A CD1 1 
ATOM   2002 C  CD2 . TYR   A 1 299 ? -13.368 -17.995 -27.162 1.00 110.54 ? 319 TYR   A CD2 1 
ATOM   2003 C  CE1 . TYR   A 1 299 ? -10.937 -17.139 -28.146 1.00 126.81 ? 319 TYR   A CE1 1 
ATOM   2004 C  CE2 . TYR   A 1 299 ? -12.849 -18.568 -28.308 1.00 119.56 ? 319 TYR   A CE2 1 
ATOM   2005 C  CZ  . TYR   A 1 299 ? -11.634 -18.136 -28.795 1.00 137.31 ? 319 TYR   A CZ  1 
ATOM   2006 O  OH  . TYR   A 1 299 ? -11.113 -18.705 -29.934 1.00 152.44 ? 319 TYR   A OH  1 
ATOM   2007 N  N   . GLU   A 1 300 ? -16.045 -15.828 -26.555 1.00 112.94 ? 320 GLU   A N   1 
ATOM   2008 C  CA  . GLU   A 1 300 ? -16.949 -16.033 -27.682 1.00 117.82 ? 320 GLU   A CA  1 
ATOM   2009 C  C   . GLU   A 1 300 ? -17.543 -14.717 -28.167 1.00 122.41 ? 320 GLU   A C   1 
ATOM   2010 O  O   . GLU   A 1 300 ? -17.771 -14.541 -29.370 1.00 124.30 ? 320 GLU   A O   1 
ATOM   2011 C  CB  . GLU   A 1 300 ? -18.055 -17.017 -27.298 1.00 109.90 ? 320 GLU   A CB  1 
ATOM   2012 C  CG  . GLU   A 1 300 ? -17.589 -18.463 -27.182 1.00 110.58 ? 320 GLU   A CG  1 
ATOM   2013 C  CD  . GLU   A 1 300 ? -17.160 -19.051 -28.514 1.00 125.51 ? 320 GLU   A CD  1 
ATOM   2014 O  OE1 . GLU   A 1 300 ? -17.497 -18.468 -29.566 1.00 126.15 ? 320 GLU   A OE1 1 
ATOM   2015 O  OE2 . GLU   A 1 300 ? -16.482 -20.100 -28.510 1.00 127.05 ? 320 GLU   A OE2 1 
ATOM   2016 N  N   . LEU   A 1 301 ? -17.803 -13.780 -27.252 1.00 118.72 ? 321 LEU   A N   1 
ATOM   2017 C  CA  . LEU   A 1 301 ? -18.305 -12.474 -27.667 1.00 117.71 ? 321 LEU   A CA  1 
ATOM   2018 C  C   . LEU   A 1 301 ? -17.254 -11.695 -28.446 1.00 134.05 ? 321 LEU   A C   1 
ATOM   2019 O  O   . LEU   A 1 301 ? -17.596 -10.938 -29.362 1.00 150.03 ? 321 LEU   A O   1 
ATOM   2020 C  CB  . LEU   A 1 301 ? -18.766 -11.671 -26.451 1.00 119.85 ? 321 LEU   A CB  1 
ATOM   2021 C  CG  . LEU   A 1 301 ? -19.918 -12.246 -25.625 1.00 122.33 ? 321 LEU   A CG  1 
ATOM   2022 C  CD1 . LEU   A 1 301 ? -20.364 -11.253 -24.560 1.00 120.77 ? 321 LEU   A CD1 1 
ATOM   2023 C  CD2 . LEU   A 1 301 ? -21.084 -12.642 -26.518 1.00 121.33 ? 321 LEU   A CD2 1 
ATOM   2024 N  N   . ALA   A 1 302 ? -15.976 -11.870 -28.103 1.00 137.08 ? 322 ALA   A N   1 
ATOM   2025 C  CA  . ALA   A 1 302 ? -14.918 -11.150 -28.802 1.00 135.72 ? 322 ALA   A CA  1 
ATOM   2026 C  C   . ALA   A 1 302 ? -14.692 -11.714 -30.200 1.00 137.66 ? 322 ALA   A C   1 
ATOM   2027 O  O   . ALA   A 1 302 ? -14.524 -10.954 -31.160 1.00 144.85 ? 322 ALA   A O   1 
ATOM   2028 C  CB  . ALA   A 1 302 ? -13.625 -11.197 -27.990 1.00 140.12 ? 322 ALA   A CB  1 
ATOM   2029 N  N   . THR   A 1 303 ? -14.680 -13.041 -30.334 1.00 137.11 ? 323 THR   A N   1 
ATOM   2030 C  CA  . THR   A 1 303 ? -14.494 -13.672 -31.634 1.00 138.99 ? 323 THR   A CA  1 
ATOM   2031 C  C   . THR   A 1 303 ? -15.750 -13.637 -32.496 1.00 142.77 ? 323 THR   A C   1 
ATOM   2032 O  O   . THR   A 1 303 ? -15.672 -13.950 -33.688 1.00 131.70 ? 323 THR   A O   1 
ATOM   2033 C  CB  . THR   A 1 303 ? -14.032 -15.123 -31.458 1.00 133.74 ? 323 THR   A CB  1 
ATOM   2034 O  OG1 . THR   A 1 303 ? -15.056 -15.879 -30.800 1.00 129.07 ? 323 THR   A OG1 1 
ATOM   2035 C  CG2 . THR   A 1 303 ? -12.757 -15.177 -30.629 1.00 129.00 ? 323 THR   A CG2 1 
ATOM   2036 N  N   . HIS   A 1 304 ? -16.896 -13.268 -31.924 1.00 143.58 ? 324 HIS   A N   1 
ATOM   2037 C  CA  . HIS   A 1 304 ? -18.145 -13.094 -32.665 1.00 135.88 ? 324 HIS   A CA  1 
ATOM   2038 C  C   . HIS   A 1 304 ? -18.715 -11.737 -32.275 1.00 134.39 ? 324 HIS   A C   1 
ATOM   2039 O  O   . HIS   A 1 304 ? -19.602 -11.643 -31.415 1.00 136.44 ? 324 HIS   A O   1 
ATOM   2040 C  CB  . HIS   A 1 304 ? -19.129 -14.229 -32.377 1.00 133.52 ? 324 HIS   A CB  1 
ATOM   2041 C  CG  . HIS   A 1 304 ? -18.629 -15.581 -32.785 1.00 126.42 ? 324 HIS   A CG  1 
ATOM   2042 N  ND1 . HIS   A 1 304 ? -17.601 -16.224 -32.129 1.00 128.13 ? 324 HIS   A ND1 1 
ATOM   2043 C  CD2 . HIS   A 1 304 ? -19.015 -16.411 -33.782 1.00 126.55 ? 324 HIS   A CD2 1 
ATOM   2044 C  CE1 . HIS   A 1 304 ? -17.376 -17.391 -32.705 1.00 124.40 ? 324 HIS   A CE1 1 
ATOM   2045 N  NE2 . HIS   A 1 304 ? -18.220 -17.529 -33.711 1.00 128.38 ? 324 HIS   A NE2 1 
ATOM   2046 N  N   . PRO   A 1 305 ? -18.221 -10.657 -32.889 1.00 137.45 ? 325 PRO   A N   1 
ATOM   2047 C  CA  . PRO   A 1 305 ? -18.615 -9.313  -32.434 1.00 138.47 ? 325 PRO   A CA  1 
ATOM   2048 C  C   . PRO   A 1 305 ? -20.079 -8.990  -32.672 1.00 146.62 ? 325 PRO   A C   1 
ATOM   2049 O  O   . PRO   A 1 305 ? -20.653 -8.199  -31.913 1.00 141.65 ? 325 PRO   A O   1 
ATOM   2050 C  CB  . PRO   A 1 305 ? -17.698 -8.383  -33.246 1.00 137.99 ? 325 PRO   A CB  1 
ATOM   2051 C  CG  . PRO   A 1 305 ? -16.590 -9.264  -33.755 1.00 140.60 ? 325 PRO   A CG  1 
ATOM   2052 C  CD  . PRO   A 1 305 ? -17.212 -10.606 -33.958 1.00 142.79 ? 325 PRO   A CD  1 
ATOM   2053 N  N   . ASP   A 1 306 ? -20.697 -9.568  -33.705 1.00 153.12 ? 326 ASP   A N   1 
ATOM   2054 C  CA  . ASP   A 1 306 ? -22.104 -9.288  -33.978 1.00 142.84 ? 326 ASP   A CA  1 
ATOM   2055 C  C   . ASP   A 1 306 ? -22.990 -9.729  -32.819 1.00 136.99 ? 326 ASP   A C   1 
ATOM   2056 O  O   . ASP   A 1 306 ? -23.973 -9.056  -32.488 1.00 133.75 ? 326 ASP   A O   1 
ATOM   2057 C  CB  . ASP   A 1 306 ? -22.530 -9.974  -35.276 1.00 151.82 ? 326 ASP   A CB  1 
ATOM   2058 C  CG  . ASP   A 1 306 ? -22.174 -11.447 -35.299 1.00 163.03 ? 326 ASP   A CG  1 
ATOM   2059 O  OD1 . ASP   A 1 306 ? -21.205 -11.837 -34.613 1.00 157.03 ? 326 ASP   A OD1 1 
ATOM   2060 O  OD2 . ASP   A 1 306 ? -22.860 -12.217 -36.004 1.00 178.94 ? 326 ASP   A OD2 1 
ATOM   2061 N  N   . VAL   A 1 307 ? -22.653 -10.855 -32.187 1.00 146.05 ? 327 VAL   A N   1 
ATOM   2062 C  CA  . VAL   A 1 307 ? -23.405 -11.305 -31.021 1.00 143.38 ? 327 VAL   A CA  1 
ATOM   2063 C  C   . VAL   A 1 307 ? -23.202 -10.353 -29.850 1.00 133.16 ? 327 VAL   A C   1 
ATOM   2064 O  O   . VAL   A 1 307 ? -24.124 -10.124 -29.058 1.00 125.35 ? 327 VAL   A O   1 
ATOM   2065 C  CB  . VAL   A 1 307 ? -23.002 -12.745 -30.655 1.00 129.04 ? 327 VAL   A CB  1 
ATOM   2066 C  CG1 . VAL   A 1 307 ? -23.838 -13.259 -29.493 1.00 121.02 ? 327 VAL   A CG1 1 
ATOM   2067 C  CG2 . VAL   A 1 307 ? -23.138 -13.659 -31.865 1.00 134.97 ? 327 VAL   A CG2 1 
ATOM   2068 N  N   . GLN   A 1 308 ? -22.006 -9.774  -29.725 1.00 133.90 ? 328 GLN   A N   1 
ATOM   2069 C  CA  . GLN   A 1 308 ? -21.728 -8.887  -28.601 1.00 131.94 ? 328 GLN   A CA  1 
ATOM   2070 C  C   . GLN   A 1 308 ? -22.523 -7.591  -28.703 1.00 132.05 ? 328 GLN   A C   1 
ATOM   2071 O  O   . GLN   A 1 308 ? -23.060 -7.108  -27.700 1.00 129.44 ? 328 GLN   A O   1 
ATOM   2072 C  CB  . GLN   A 1 308 ? -20.230 -8.597  -28.519 1.00 133.72 ? 328 GLN   A CB  1 
ATOM   2073 C  CG  . GLN   A 1 308 ? -19.828 -7.731  -27.335 1.00 134.98 ? 328 GLN   A CG  1 
ATOM   2074 C  CD  . GLN   A 1 308 ? -18.329 -7.719  -27.105 1.00 132.50 ? 328 GLN   A CD  1 
ATOM   2075 O  OE1 . GLN   A 1 308 ? -17.840 -7.108  -26.154 1.00 133.63 ? 328 GLN   A OE1 1 
ATOM   2076 N  NE2 . GLN   A 1 308 ? -17.591 -8.399  -27.975 1.00 130.12 ? 328 GLN   A NE2 1 
ATOM   2077 N  N   . GLN   A 1 309 ? -22.611 -7.012  -29.903 1.00 136.67 ? 329 GLN   A N   1 
ATOM   2078 C  CA  . GLN   A 1 309 ? -23.375 -5.779  -30.067 1.00 138.13 ? 329 GLN   A CA  1 
ATOM   2079 C  C   . GLN   A 1 309 ? -24.864 -6.025  -29.860 1.00 136.34 ? 329 GLN   A C   1 
ATOM   2080 O  O   . GLN   A 1 309 ? -25.529 -5.283  -29.128 1.00 134.56 ? 329 GLN   A O   1 
ATOM   2081 C  CB  . GLN   A 1 309 ? -23.120 -5.171  -31.446 1.00 137.95 ? 329 GLN   A CB  1 
ATOM   2082 C  CG  . GLN   A 1 309 ? -23.954 -3.928  -31.716 1.00 138.07 ? 329 GLN   A CG  1 
ATOM   2083 C  CD  . GLN   A 1 309 ? -23.669 -3.308  -33.068 1.00 141.01 ? 329 GLN   A CD  1 
ATOM   2084 O  OE1 . GLN   A 1 309 ? -22.518 -3.227  -33.497 1.00 135.57 ? 329 GLN   A OE1 1 
ATOM   2085 N  NE2 . GLN   A 1 309 ? -24.720 -2.870  -33.750 1.00 126.68 ? 329 GLN   A NE2 1 
ATOM   2086 N  N   . LYS   A 1 310 ? -25.406 -7.067  -30.499 1.00 138.32 ? 330 LYS   A N   1 
ATOM   2087 C  CA  . LYS   A 1 310 ? -26.812 -7.406  -30.301 1.00 123.94 ? 330 LYS   A CA  1 
ATOM   2088 C  C   . LYS   A 1 310 ? -27.108 -7.708  -28.838 1.00 129.36 ? 330 LYS   A C   1 
ATOM   2089 O  O   . LYS   A 1 310 ? -28.240 -7.515  -28.379 1.00 132.64 ? 330 LYS   A O   1 
ATOM   2090 C  CB  . LYS   A 1 310 ? -27.196 -8.596  -31.182 1.00 123.04 ? 330 LYS   A CB  1 
ATOM   2091 C  CG  . LYS   A 1 310 ? -28.688 -8.900  -31.205 1.00 133.14 ? 330 LYS   A CG  1 
ATOM   2092 C  CD  . LYS   A 1 310 ? -28.991 -10.131 -32.044 1.00 137.80 ? 330 LYS   A CD  1 
ATOM   2093 C  CE  . LYS   A 1 310 ? -30.479 -10.445 -32.044 1.00 139.41 ? 330 LYS   A CE  1 
ATOM   2094 N  NZ  . LYS   A 1 310 ? -30.797 -11.680 -32.812 1.00 138.64 ? 330 LYS   A NZ  1 
ATOM   2095 N  N   . LEU   A 1 311 ? -26.108 -8.177  -28.090 1.00 125.06 ? 331 LEU   A N   1 
ATOM   2096 C  CA  . LEU   A 1 311 ? -26.291 -8.373  -26.657 1.00 118.04 ? 331 LEU   A CA  1 
ATOM   2097 C  C   . LEU   A 1 311 ? -26.279 -7.041  -25.918 1.00 132.98 ? 331 LEU   A C   1 
ATOM   2098 O  O   . LEU   A 1 311 ? -27.099 -6.813  -25.021 1.00 133.50 ? 331 LEU   A O   1 
ATOM   2099 C  CB  . LEU   A 1 311 ? -25.207 -9.308  -26.119 1.00 123.68 ? 331 LEU   A CB  1 
ATOM   2100 C  CG  . LEU   A 1 311 ? -25.338 -9.760  -24.666 1.00 124.63 ? 331 LEU   A CG  1 
ATOM   2101 C  CD1 . LEU   A 1 311 ? -26.740 -10.268 -24.400 1.00 122.23 ? 331 LEU   A CD1 1 
ATOM   2102 C  CD2 . LEU   A 1 311 ? -24.313 -10.838 -24.363 1.00 112.80 ? 331 LEU   A CD2 1 
ATOM   2103 N  N   . GLN   A 1 312 ? -25.363 -6.143  -26.293 1.00 141.84 ? 332 GLN   A N   1 
ATOM   2104 C  CA  . GLN   A 1 312 ? -25.322 -4.820  -25.677 1.00 132.20 ? 332 GLN   A CA  1 
ATOM   2105 C  C   . GLN   A 1 312 ? -26.578 -4.015  -25.988 1.00 142.46 ? 332 GLN   A C   1 
ATOM   2106 O  O   . GLN   A 1 312 ? -26.983 -3.164  -25.188 1.00 147.18 ? 332 GLN   A O   1 
ATOM   2107 C  CB  . GLN   A 1 312 ? -24.081 -4.061  -26.146 1.00 126.89 ? 332 GLN   A CB  1 
ATOM   2108 C  CG  . GLN   A 1 312 ? -22.766 -4.632  -25.644 1.00 129.17 ? 332 GLN   A CG  1 
ATOM   2109 C  CD  . GLN   A 1 312 ? -21.564 -3.963  -26.282 1.00 141.97 ? 332 GLN   A CD  1 
ATOM   2110 O  OE1 . GLN   A 1 312 ? -21.592 -3.606  -27.460 1.00 140.85 ? 332 GLN   A OE1 1 
ATOM   2111 N  NE2 . GLN   A 1 312 ? -20.503 -3.781  -25.504 1.00 140.66 ? 332 GLN   A NE2 1 
ATOM   2112 N  N   . GLU   A 1 313 ? -27.203 -4.265  -27.141 1.00 141.59 ? 333 GLU   A N   1 
ATOM   2113 C  CA  . GLU   A 1 313 ? -28.425 -3.550  -27.493 1.00 135.64 ? 333 GLU   A CA  1 
ATOM   2114 C  C   . GLU   A 1 313 ? -29.583 -3.956  -26.590 1.00 140.48 ? 333 GLU   A C   1 
ATOM   2115 O  O   . GLU   A 1 313 ? -30.379 -3.107  -26.173 1.00 150.58 ? 333 GLU   A O   1 
ATOM   2116 C  CB  . GLU   A 1 313 ? -28.773 -3.801  -28.960 1.00 142.41 ? 333 GLU   A CB  1 
ATOM   2117 C  CG  . GLU   A 1 313 ? -27.769 -3.224  -29.945 1.00 138.50 ? 333 GLU   A CG  1 
ATOM   2118 C  CD  . GLU   A 1 313 ? -27.901 -3.819  -31.333 1.00 151.28 ? 333 GLU   A CD  1 
ATOM   2119 O  OE1 . GLU   A 1 313 ? -28.721 -4.745  -31.510 1.00 154.27 ? 333 GLU   A OE1 1 
ATOM   2120 O  OE2 . GLU   A 1 313 ? -27.183 -3.363  -32.248 1.00 167.94 ? 333 GLU   A OE2 1 
ATOM   2121 N  N   . GLU   A 1 314 ? -29.695 -5.249  -26.278 1.00 133.60 ? 334 GLU   A N   1 
ATOM   2122 C  CA  . GLU   A 1 314 ? -30.765 -5.703  -25.396 1.00 139.95 ? 334 GLU   A CA  1 
ATOM   2123 C  C   . GLU   A 1 314 ? -30.528 -5.268  -23.956 1.00 146.33 ? 334 GLU   A C   1 
ATOM   2124 O  O   . GLU   A 1 314 ? -31.490 -5.015  -23.221 1.00 137.81 ? 334 GLU   A O   1 
ATOM   2125 C  CB  . GLU   A 1 314 ? -30.902 -7.223  -25.471 1.00 139.89 ? 334 GLU   A CB  1 
ATOM   2126 C  CG  . GLU   A 1 314 ? -32.127 -7.772  -24.758 1.00 138.13 ? 334 GLU   A CG  1 
ATOM   2127 C  CD  . GLU   A 1 314 ? -31.945 -9.209  -24.312 1.00 138.01 ? 334 GLU   A CD  1 
ATOM   2128 O  OE1 . GLU   A 1 314 ? -30.841 -9.548  -23.836 1.00 140.23 ? 334 GLU   A OE1 1 
ATOM   2129 O  OE2 . GLU   A 1 314 ? -32.903 -9.999  -24.441 1.00 141.84 ? 334 GLU   A OE2 1 
ATOM   2130 N  N   . ILE   A 1 315 ? -29.264 -5.177  -23.536 1.00 147.66 ? 335 ILE   A N   1 
ATOM   2131 C  CA  . ILE   A 1 315 ? -28.964 -4.758  -22.171 1.00 152.28 ? 335 ILE   A CA  1 
ATOM   2132 C  C   . ILE   A 1 315 ? -29.374 -3.307  -21.954 1.00 156.83 ? 335 ILE   A C   1 
ATOM   2133 O  O   . ILE   A 1 315 ? -29.929 -2.953  -20.907 1.00 156.75 ? 335 ILE   A O   1 
ATOM   2134 C  CB  . ILE   A 1 315 ? -27.472 -4.984  -21.861 1.00 140.79 ? 335 ILE   A CB  1 
ATOM   2135 C  CG1 . ILE   A 1 315 ? -27.152 -6.479  -21.853 1.00 129.50 ? 335 ILE   A CG1 1 
ATOM   2136 C  CG2 . ILE   A 1 315 ? -27.100 -4.362  -20.527 1.00 144.42 ? 335 ILE   A CG2 1 
ATOM   2137 C  CD1 . ILE   A 1 315 ? -25.716 -6.793  -21.499 1.00 135.03 ? 335 ILE   A CD1 1 
ATOM   2138 N  N   . ASP   A 1 316 ? -29.119 -2.446  -22.939 1.00 166.42 ? 336 ASP   A N   1 
ATOM   2139 C  CA  . ASP   A 1 316 ? -29.530 -1.051  -22.853 1.00 167.08 ? 336 ASP   A CA  1 
ATOM   2140 C  C   . ASP   A 1 316 ? -31.017 -0.856  -23.115 1.00 168.83 ? 336 ASP   A C   1 
ATOM   2141 O  O   . ASP   A 1 316 ? -31.548 0.216   -22.806 1.00 172.52 ? 336 ASP   A O   1 
ATOM   2142 C  CB  . ASP   A 1 316 ? -28.717 -0.204  -23.834 1.00 171.13 ? 336 ASP   A CB  1 
ATOM   2143 C  CG  . ASP   A 1 316 ? -27.223 -0.323  -23.605 1.00 174.57 ? 336 ASP   A CG  1 
ATOM   2144 O  OD1 . ASP   A 1 316 ? -26.811 -0.498  -22.439 1.00 175.18 ? 336 ASP   A OD1 1 
ATOM   2145 O  OD2 . ASP   A 1 316 ? -26.461 -0.244  -24.591 1.00 170.85 ? 336 ASP   A OD2 1 
ATOM   2146 N  N   . ALA   A 1 317 ? -31.698 -1.857  -23.676 1.00 158.62 ? 337 ALA   A N   1 
ATOM   2147 C  CA  . ALA   A 1 317 ? -33.138 -1.754  -23.890 1.00 144.18 ? 337 ALA   A CA  1 
ATOM   2148 C  C   . ALA   A 1 317 ? -33.906 -2.055  -22.609 1.00 145.89 ? 337 ALA   A C   1 
ATOM   2149 O  O   . ALA   A 1 317 ? -34.792 -1.290  -22.212 1.00 157.84 ? 337 ALA   A O   1 
ATOM   2150 C  CB  . ALA   A 1 317 ? -33.572 -2.696  -25.014 1.00 136.86 ? 337 ALA   A CB  1 
ATOM   2151 N  N   . VAL   A 1 318 ? -33.580 -3.170  -21.950 1.00 142.35 ? 338 VAL   A N   1 
ATOM   2152 C  CA  . VAL   A 1 318 ? -34.225 -3.497  -20.684 1.00 142.62 ? 338 VAL   A CA  1 
ATOM   2153 C  C   . VAL   A 1 318 ? -33.746 -2.564  -19.579 1.00 146.83 ? 338 VAL   A C   1 
ATOM   2154 O  O   . VAL   A 1 318 ? -34.518 -2.204  -18.682 1.00 151.45 ? 338 VAL   A O   1 
ATOM   2155 C  CB  . VAL   A 1 318 ? -33.975 -4.975  -20.328 1.00 140.70 ? 338 VAL   A CB  1 
ATOM   2156 C  CG1 . VAL   A 1 318 ? -34.635 -5.333  -19.004 1.00 142.19 ? 338 VAL   A CG1 1 
ATOM   2157 C  CG2 . VAL   A 1 318 ? -34.481 -5.881  -21.441 1.00 137.78 ? 338 VAL   A CG2 1 
ATOM   2158 N  N   . LEU   A 1 319 ? -32.480 -2.144  -19.629 1.00 153.04 ? 339 LEU   A N   1 
ATOM   2159 C  CA  . LEU   A 1 319 ? -31.883 -1.269  -18.622 1.00 151.99 ? 339 LEU   A CA  1 
ATOM   2160 C  C   . LEU   A 1 319 ? -31.348 -0.016  -19.309 1.00 167.80 ? 339 LEU   A C   1 
ATOM   2161 O  O   . LEU   A 1 319 ? -30.145 0.084   -19.592 1.00 174.51 ? 339 LEU   A O   1 
ATOM   2162 C  CB  . LEU   A 1 319 ? -30.773 -1.984  -17.856 1.00 154.00 ? 339 LEU   A CB  1 
ATOM   2163 C  CG  . LEU   A 1 319 ? -31.183 -3.234  -17.079 1.00 144.70 ? 339 LEU   A CG  1 
ATOM   2164 C  CD1 . LEU   A 1 319 ? -29.966 -3.860  -16.433 1.00 148.21 ? 339 LEU   A CD1 1 
ATOM   2165 C  CD2 . LEU   A 1 319 ? -32.238 -2.903  -16.036 1.00 145.70 ? 339 LEU   A CD2 1 
ATOM   2166 N  N   . PRO   A 1 320 ? -32.209 0.958   -19.592 1.00 165.56 ? 340 PRO   A N   1 
ATOM   2167 C  CA  . PRO   A 1 320 ? -31.733 2.211   -20.182 1.00 165.99 ? 340 PRO   A CA  1 
ATOM   2168 C  C   . PRO   A 1 320 ? -30.986 3.055   -19.160 1.00 181.17 ? 340 PRO   A C   1 
ATOM   2169 O  O   . PRO   A 1 320 ? -31.148 2.904   -17.947 1.00 185.88 ? 340 PRO   A O   1 
ATOM   2170 C  CB  . PRO   A 1 320 ? -33.022 2.901   -20.640 1.00 152.95 ? 340 PRO   A CB  1 
ATOM   2171 C  CG  . PRO   A 1 320 ? -34.068 2.367   -19.721 1.00 155.53 ? 340 PRO   A CG  1 
ATOM   2172 C  CD  . PRO   A 1 320 ? -33.673 0.944   -19.423 1.00 161.02 ? 340 PRO   A CD  1 
ATOM   2173 N  N   . ASN   A 1 321 ? -30.149 3.955   -19.681 1.00 200.00 ? 341 ASN   A N   1 
ATOM   2174 C  CA  . ASN   A 1 321 ? -29.315 4.839   -18.863 1.00 202.11 ? 341 ASN   A CA  1 
ATOM   2175 C  C   . ASN   A 1 321 ? -28.389 4.052   -17.938 1.00 198.77 ? 341 ASN   A C   1 
ATOM   2176 O  O   . ASN   A 1 321 ? -28.040 4.521   -16.851 1.00 204.00 ? 341 ASN   A O   1 
ATOM   2177 C  CB  . ASN   A 1 321 ? -30.167 5.821   -18.050 1.00 204.29 ? 341 ASN   A CB  1 
ATOM   2178 C  CG  . ASN   A 1 321 ? -31.017 6.723   -18.925 1.00 204.45 ? 341 ASN   A CG  1 
ATOM   2179 O  OD1 . ASN   A 1 321 ? -30.639 7.056   -20.048 1.00 204.78 ? 341 ASN   A OD1 1 
ATOM   2180 N  ND2 . ASN   A 1 321 ? -32.173 7.128   -18.410 1.00 204.76 ? 341 ASN   A ND2 1 
ATOM   2181 N  N   . LYS   A 1 322 ? -27.981 2.855   -18.367 1.00 176.08 ? 342 LYS   A N   1 
ATOM   2182 C  CA  . LYS   A 1 322 ? -27.148 1.955   -17.566 1.00 171.24 ? 342 LYS   A CA  1 
ATOM   2183 C  C   . LYS   A 1 322 ? -27.799 1.678   -16.209 1.00 170.52 ? 342 LYS   A C   1 
ATOM   2184 O  O   . LYS   A 1 322 ? -27.235 1.947   -15.146 1.00 174.01 ? 342 LYS   A O   1 
ATOM   2185 C  CB  . LYS   A 1 322 ? -25.732 2.516   -17.396 1.00 167.42 ? 342 LYS   A CB  1 
ATOM   2186 C  CG  . LYS   A 1 322 ? -24.957 2.688   -18.692 1.00 173.60 ? 342 LYS   A CG  1 
ATOM   2187 C  CD  . LYS   A 1 322 ? -23.527 3.125   -18.411 1.00 182.47 ? 342 LYS   A CD  1 
ATOM   2188 C  CE  . LYS   A 1 322 ? -22.722 3.269   -19.692 1.00 178.84 ? 342 LYS   A CE  1 
ATOM   2189 N  NZ  . LYS   A 1 322 ? -21.292 3.578   -19.412 1.00 177.25 ? 342 LYS   A NZ  1 
ATOM   2190 N  N   . ALA   A 1 323 ? -29.010 1.131   -16.267 1.00 157.97 ? 343 ALA   A N   1 
ATOM   2191 C  CA  . ALA   A 1 323 ? -29.779 0.893   -15.059 1.00 157.30 ? 343 ALA   A CA  1 
ATOM   2192 C  C   . ALA   A 1 323 ? -29.212 -0.297  -14.284 1.00 155.75 ? 343 ALA   A C   1 
ATOM   2193 O  O   . ALA   A 1 323 ? -28.630 -1.212  -14.873 1.00 146.12 ? 343 ALA   A O   1 
ATOM   2194 C  CB  . ALA   A 1 323 ? -31.245 0.643   -15.401 1.00 158.04 ? 343 ALA   A CB  1 
ATOM   2195 N  N   . PRO   A 1 324 ? -29.358 -0.300  -12.962 1.00 154.07 ? 344 PRO   A N   1 
ATOM   2196 C  CA  . PRO   A 1 324 ? -28.883 -1.434  -12.163 1.00 149.75 ? 344 PRO   A CA  1 
ATOM   2197 C  C   . PRO   A 1 324 ? -29.723 -2.670  -12.424 1.00 147.46 ? 344 PRO   A C   1 
ATOM   2198 O  O   . PRO   A 1 324 ? -30.959 -2.623  -12.330 1.00 145.01 ? 344 PRO   A O   1 
ATOM   2199 C  CB  . PRO   A 1 324 ? -29.048 -0.945  -10.714 1.00 149.50 ? 344 PRO   A CB  1 
ATOM   2200 C  CG  . PRO   A 1 324 ? -29.176 0.543   -10.813 1.00 149.91 ? 344 PRO   A CG  1 
ATOM   2201 C  CD  . PRO   A 1 324 ? -29.856 0.798   -12.118 1.00 150.09 ? 344 PRO   A CD  1 
ATOM   2202 N  N   . PRO   A 1 325 ? -29.091 -3.797  -12.756 1.00 149.21 ? 345 PRO   A N   1 
ATOM   2203 C  CA  . PRO   A 1 325 ? -29.854 -5.022  -13.044 1.00 138.24 ? 345 PRO   A CA  1 
ATOM   2204 C  C   . PRO   A 1 325 ? -30.492 -5.583  -11.781 1.00 140.20 ? 345 PRO   A C   1 
ATOM   2205 O  O   . PRO   A 1 325 ? -29.807 -5.884  -10.802 1.00 148.10 ? 345 PRO   A O   1 
ATOM   2206 C  CB  . PRO   A 1 325 ? -28.795 -5.972  -13.616 1.00 134.97 ? 345 PRO   A CB  1 
ATOM   2207 C  CG  . PRO   A 1 325 ? -27.502 -5.475  -13.055 1.00 135.80 ? 345 PRO   A CG  1 
ATOM   2208 C  CD  . PRO   A 1 325 ? -27.644 -3.983  -12.954 1.00 148.51 ? 345 PRO   A CD  1 
ATOM   2209 N  N   . THR   A 1 326 ? -31.815 -5.717  -11.810 1.00 140.80 ? 346 THR   A N   1 
ATOM   2210 C  CA  . THR   A 1 326 ? -32.573 -6.319  -10.727 1.00 144.84 ? 346 THR   A CA  1 
ATOM   2211 C  C   . THR   A 1 326 ? -32.910 -7.765  -11.084 1.00 147.29 ? 346 THR   A C   1 
ATOM   2212 O  O   . THR   A 1 326 ? -32.596 -8.254  -12.171 1.00 147.62 ? 346 THR   A O   1 
ATOM   2213 C  CB  . THR   A 1 326 ? -33.838 -5.507  -10.439 1.00 141.73 ? 346 THR   A CB  1 
ATOM   2214 O  OG1 . THR   A 1 326 ? -34.625 -5.404  -11.632 1.00 141.25 ? 346 THR   A OG1 1 
ATOM   2215 C  CG2 . THR   A 1 326 ? -33.476 -4.111  -9.953  1.00 142.89 ? 346 THR   A CG2 1 
ATOM   2216 N  N   . TYR   A 1 327 ? -33.563 -8.459  -10.148 1.00 145.71 ? 347 TYR   A N   1 
ATOM   2217 C  CA  . TYR   A 1 327 ? -33.902 -9.863  -10.367 1.00 147.43 ? 347 TYR   A CA  1 
ATOM   2218 C  C   . TYR   A 1 327 ? -34.826 -10.026 -11.568 1.00 156.38 ? 347 TYR   A C   1 
ATOM   2219 O  O   . TYR   A 1 327 ? -34.610 -10.895 -12.421 1.00 153.19 ? 347 TYR   A O   1 
ATOM   2220 C  CB  . TYR   A 1 327 ? -34.549 -10.449 -9.110  1.00 152.77 ? 347 TYR   A CB  1 
ATOM   2221 C  CG  . TYR   A 1 327 ? -34.852 -11.933 -9.198  1.00 147.93 ? 347 TYR   A CG  1 
ATOM   2222 C  CD1 . TYR   A 1 327 ? -36.017 -12.393 -9.803  1.00 146.54 ? 347 TYR   A CD1 1 
ATOM   2223 C  CD2 . TYR   A 1 327 ? -33.979 -12.871 -8.665  1.00 141.42 ? 347 TYR   A CD2 1 
ATOM   2224 C  CE1 . TYR   A 1 327 ? -36.295 -13.743 -9.885  1.00 143.79 ? 347 TYR   A CE1 1 
ATOM   2225 C  CE2 . TYR   A 1 327 ? -34.250 -14.225 -8.743  1.00 137.74 ? 347 TYR   A CE2 1 
ATOM   2226 C  CZ  . TYR   A 1 327 ? -35.409 -14.655 -9.353  1.00 138.22 ? 347 TYR   A CZ  1 
ATOM   2227 O  OH  . TYR   A 1 327 ? -35.684 -16.001 -9.431  1.00 135.90 ? 347 TYR   A OH  1 
ATOM   2228 N  N   . ASP   A 1 328 ? -35.865 -9.195  -11.651 1.00 163.95 ? 348 ASP   A N   1 
ATOM   2229 C  CA  . ASP   A 1 328 ? -36.883 -9.384  -12.678 1.00 163.27 ? 348 ASP   A CA  1 
ATOM   2230 C  C   . ASP   A 1 328 ? -36.392 -8.958  -14.057 1.00 159.82 ? 348 ASP   A C   1 
ATOM   2231 O  O   . ASP   A 1 328 ? -36.856 -9.497  -15.069 1.00 156.58 ? 348 ASP   A O   1 
ATOM   2232 C  CB  . ASP   A 1 328 ? -38.151 -8.620  -12.295 1.00 168.81 ? 348 ASP   A CB  1 
ATOM   2233 C  CG  . ASP   A 1 328 ? -38.805 -9.175  -11.042 1.00 170.92 ? 348 ASP   A CG  1 
ATOM   2234 O  OD1 . ASP   A 1 328 ? -39.280 -10.329 -11.078 1.00 157.03 ? 348 ASP   A OD1 1 
ATOM   2235 O  OD2 . ASP   A 1 328 ? -38.828 -8.464  -10.016 1.00 172.93 ? 348 ASP   A OD2 1 
ATOM   2236 N  N   . THR   A 1 329 ? -35.463 -8.002  -14.123 1.00 156.83 ? 349 THR   A N   1 
ATOM   2237 C  CA  . THR   A 1 329 ? -34.918 -7.580  -15.408 1.00 149.33 ? 349 THR   A CA  1 
ATOM   2238 C  C   . THR   A 1 329 ? -33.899 -8.566  -15.965 1.00 148.29 ? 349 THR   A C   1 
ATOM   2239 O  O   . THR   A 1 329 ? -33.656 -8.566  -17.177 1.00 144.81 ? 349 THR   A O   1 
ATOM   2240 C  CB  . THR   A 1 329 ? -34.276 -6.195  -15.289 1.00 137.80 ? 349 THR   A CB  1 
ATOM   2241 O  OG1 . THR   A 1 329 ? -33.313 -6.198  -14.227 1.00 145.07 ? 349 THR   A OG1 1 
ATOM   2242 C  CG2 . THR   A 1 329 ? -35.336 -5.138  -15.009 1.00 126.17 ? 349 THR   A CG2 1 
ATOM   2243 N  N   . VAL   A 1 330 ? -33.306 -9.405  -15.115 1.00 150.43 ? 350 VAL   A N   1 
ATOM   2244 C  CA  . VAL   A 1 330 ? -32.339 -10.389 -15.590 1.00 145.19 ? 350 VAL   A CA  1 
ATOM   2245 C  C   . VAL   A 1 330 ? -33.041 -11.535 -16.312 1.00 149.30 ? 350 VAL   A C   1 
ATOM   2246 O  O   . VAL   A 1 330 ? -32.587 -11.986 -17.369 1.00 154.93 ? 350 VAL   A O   1 
ATOM   2247 C  CB  . VAL   A 1 330 ? -31.477 -10.893 -14.418 1.00 130.81 ? 350 VAL   A CB  1 
ATOM   2248 C  CG1 . VAL   A 1 330 ? -30.705 -12.137 -14.818 1.00 125.21 ? 350 VAL   A CG1 1 
ATOM   2249 C  CG2 . VAL   A 1 330 ? -30.520 -9.804  -13.967 1.00 123.64 ? 350 VAL   A CG2 1 
ATOM   2250 N  N   . LEU   A 1 331 ? -34.159 -12.018 -15.765 1.00 152.22 ? 351 LEU   A N   1 
ATOM   2251 C  CA  . LEU   A 1 331 ? -34.905 -13.093 -16.407 1.00 152.43 ? 351 LEU   A CA  1 
ATOM   2252 C  C   . LEU   A 1 331 ? -35.618 -12.644 -17.676 1.00 152.88 ? 351 LEU   A C   1 
ATOM   2253 O  O   . LEU   A 1 331 ? -36.115 -13.497 -18.419 1.00 139.25 ? 351 LEU   A O   1 
ATOM   2254 C  CB  . LEU   A 1 331 ? -35.922 -13.687 -15.430 1.00 127.95 ? 351 LEU   A CB  1 
ATOM   2255 C  CG  . LEU   A 1 331 ? -35.346 -14.464 -14.244 1.00 137.01 ? 351 LEU   A CG  1 
ATOM   2256 C  CD1 . LEU   A 1 331 ? -36.456 -14.974 -13.338 1.00 132.97 ? 351 LEU   A CD1 1 
ATOM   2257 C  CD2 . LEU   A 1 331 ? -34.480 -15.613 -14.735 1.00 152.71 ? 351 LEU   A CD2 1 
ATOM   2258 N  N   . GLN   A 1 332 ? -35.682 -11.338 -17.940 1.00 153.68 ? 352 GLN   A N   1 
ATOM   2259 C  CA  . GLN   A 1 332 ? -36.333 -10.850 -19.149 1.00 153.46 ? 352 GLN   A CA  1 
ATOM   2260 C  C   . GLN   A 1 332 ? -35.406 -10.895 -20.358 1.00 158.48 ? 352 GLN   A C   1 
ATOM   2261 O  O   . GLN   A 1 332 ? -35.870 -11.118 -21.482 1.00 173.03 ? 352 GLN   A O   1 
ATOM   2262 C  CB  . GLN   A 1 332 ? -36.843 -9.423  -18.927 1.00 158.03 ? 352 GLN   A CB  1 
ATOM   2263 C  CG  . GLN   A 1 332 ? -37.515 -8.798  -20.140 1.00 161.51 ? 352 GLN   A CG  1 
ATOM   2264 C  CD  . GLN   A 1 332 ? -37.962 -7.371  -19.888 1.00 163.66 ? 352 GLN   A CD  1 
ATOM   2265 O  OE1 . GLN   A 1 332 ? -38.061 -6.932  -18.743 1.00 166.34 ? 352 GLN   A OE1 1 
ATOM   2266 N  NE2 . GLN   A 1 332 ? -38.232 -6.638  -20.962 1.00 173.63 ? 352 GLN   A NE2 1 
ATOM   2267 N  N   . MET   A 1 333 ? -34.106 -10.700 -20.150 1.00 140.31 ? 353 MET   A N   1 
ATOM   2268 C  CA  . MET   A 1 333 ? -33.139 -10.661 -21.245 1.00 140.99 ? 353 MET   A CA  1 
ATOM   2269 C  C   . MET   A 1 333 ? -32.970 -12.063 -21.814 1.00 137.93 ? 353 MET   A C   1 
ATOM   2270 O  O   . MET   A 1 333 ? -32.236 -12.889 -21.266 1.00 132.24 ? 353 MET   A O   1 
ATOM   2271 C  CB  . MET   A 1 333 ? -31.812 -10.094 -20.756 1.00 131.08 ? 353 MET   A CB  1 
ATOM   2272 C  CG  . MET   A 1 333 ? -31.951 -8.750  -20.062 1.00 140.23 ? 353 MET   A CG  1 
ATOM   2273 S  SD  . MET   A 1 333 ? -30.371 -7.956  -19.726 1.00 153.48 ? 353 MET   A SD  1 
ATOM   2274 C  CE  . MET   A 1 333 ? -30.918 -6.493  -18.850 1.00 138.41 ? 353 MET   A CE  1 
ATOM   2275 N  N   . GLU   A 1 334 ? -33.652 -12.335 -22.928 1.00 126.70 ? 354 GLU   A N   1 
ATOM   2276 C  CA  . GLU   A 1 334 ? -33.624 -13.672 -23.509 1.00 126.81 ? 354 GLU   A CA  1 
ATOM   2277 C  C   . GLU   A 1 334 ? -32.368 -13.903 -24.339 1.00 121.44 ? 354 GLU   A C   1 
ATOM   2278 O  O   . GLU   A 1 334 ? -31.833 -15.017 -24.354 1.00 126.65 ? 354 GLU   A O   1 
ATOM   2279 C  CB  . GLU   A 1 334 ? -34.876 -13.905 -24.356 1.00 139.27 ? 354 GLU   A CB  1 
ATOM   2280 C  CG  . GLU   A 1 334 ? -36.169 -13.884 -23.556 1.00 159.72 ? 354 GLU   A CG  1 
ATOM   2281 C  CD  . GLU   A 1 334 ? -37.392 -14.152 -24.414 1.00 188.37 ? 354 GLU   A CD  1 
ATOM   2282 O  OE1 . GLU   A 1 334 ? -37.221 -14.588 -25.571 1.00 196.92 ? 354 GLU   A OE1 1 
ATOM   2283 O  OE2 . GLU   A 1 334 ? -38.523 -13.923 -23.933 1.00 186.50 ? 354 GLU   A OE2 1 
ATOM   2284 N  N   . TYR   A 1 335 ? -31.885 -12.874 -25.042 1.00 127.69 ? 355 TYR   A N   1 
ATOM   2285 C  CA  . TYR   A 1 335 ? -30.649 -13.035 -25.799 1.00 120.26 ? 355 TYR   A CA  1 
ATOM   2286 C  C   . TYR   A 1 335 ? -29.454 -13.230 -24.876 1.00 116.86 ? 355 TYR   A C   1 
ATOM   2287 O  O   . TYR   A 1 335 ? -28.491 -13.911 -25.244 1.00 118.87 ? 355 TYR   A O   1 
ATOM   2288 C  CB  . TYR   A 1 335 ? -30.423 -11.836 -26.720 1.00 117.16 ? 355 TYR   A CB  1 
ATOM   2289 C  CG  . TYR   A 1 335 ? -29.439 -12.115 -27.833 1.00 123.63 ? 355 TYR   A CG  1 
ATOM   2290 C  CD1 . TYR   A 1 335 ? -29.807 -12.879 -28.933 1.00 126.13 ? 355 TYR   A CD1 1 
ATOM   2291 C  CD2 . TYR   A 1 335 ? -28.142 -11.619 -27.785 1.00 120.75 ? 355 TYR   A CD2 1 
ATOM   2292 C  CE1 . TYR   A 1 335 ? -28.914 -13.141 -29.954 1.00 126.16 ? 355 TYR   A CE1 1 
ATOM   2293 C  CE2 . TYR   A 1 335 ? -27.240 -11.875 -28.804 1.00 115.51 ? 355 TYR   A CE2 1 
ATOM   2294 C  CZ  . TYR   A 1 335 ? -27.633 -12.637 -29.886 1.00 122.87 ? 355 TYR   A CZ  1 
ATOM   2295 O  OH  . TYR   A 1 335 ? -26.745 -12.898 -30.905 1.00 129.74 ? 355 TYR   A OH  1 
ATOM   2296 N  N   . LEU   A 1 336 ? -29.500 -12.646 -23.676 1.00 114.45 ? 356 LEU   A N   1 
ATOM   2297 C  CA  . LEU   A 1 336 ? -28.484 -12.944 -22.673 1.00 111.72 ? 356 LEU   A CA  1 
ATOM   2298 C  C   . LEU   A 1 336 ? -28.533 -14.412 -22.275 1.00 115.62 ? 356 LEU   A C   1 
ATOM   2299 O  O   . LEU   A 1 336 ? -27.491 -15.064 -22.141 1.00 109.77 ? 356 LEU   A O   1 
ATOM   2300 C  CB  . LEU   A 1 336 ? -28.676 -12.044 -21.452 1.00 105.01 ? 356 LEU   A CB  1 
ATOM   2301 C  CG  . LEU   A 1 336 ? -27.635 -12.150 -20.338 1.00 117.31 ? 356 LEU   A CG  1 
ATOM   2302 C  CD1 . LEU   A 1 336 ? -26.252 -11.792 -20.859 1.00 106.75 ? 356 LEU   A CD1 1 
ATOM   2303 C  CD2 . LEU   A 1 336 ? -28.020 -11.254 -19.174 1.00 126.24 ? 356 LEU   A CD2 1 
ATOM   2304 N  N   . ASP   A 1 337 ? -29.740 -14.954 -22.099 1.00 113.31 ? 357 ASP   A N   1 
ATOM   2305 C  CA  . ASP   A 1 337 ? -29.884 -16.373 -21.789 1.00 103.01 ? 357 ASP   A CA  1 
ATOM   2306 C  C   . ASP   A 1 337 ? -29.419 -17.242 -22.952 1.00 106.66 ? 357 ASP   A C   1 
ATOM   2307 O  O   . ASP   A 1 337 ? -28.859 -18.324 -22.740 1.00 103.87 ? 357 ASP   A O   1 
ATOM   2308 C  CB  . ASP   A 1 337 ? -31.338 -16.681 -21.431 1.00 114.07 ? 357 ASP   A CB  1 
ATOM   2309 C  CG  . ASP   A 1 337 ? -31.573 -18.153 -21.152 1.00 121.38 ? 357 ASP   A CG  1 
ATOM   2310 O  OD1 . ASP   A 1 337 ? -31.151 -18.633 -20.078 1.00 123.11 ? 357 ASP   A OD1 1 
ATOM   2311 O  OD2 . ASP   A 1 337 ? -32.182 -18.831 -22.007 1.00 119.66 ? 357 ASP   A OD2 1 
ATOM   2312 N  N   . MET   A 1 338 ? -29.639 -16.785 -24.187 1.00 108.07 ? 358 MET   A N   1 
ATOM   2313 C  CA  . MET   A 1 338 ? -29.214 -17.558 -25.350 1.00 106.02 ? 358 MET   A CA  1 
ATOM   2314 C  C   . MET   A 1 338 ? -27.695 -17.604 -25.459 1.00 112.54 ? 358 MET   A C   1 
ATOM   2315 O  O   . MET   A 1 338 ? -27.125 -18.635 -25.837 1.00 110.83 ? 358 MET   A O   1 
ATOM   2316 C  CB  . MET   A 1 338 ? -29.829 -16.971 -26.620 1.00 104.05 ? 358 MET   A CB  1 
ATOM   2317 C  CG  . MET   A 1 338 ? -31.335 -17.147 -26.710 1.00 118.77 ? 358 MET   A CG  1 
ATOM   2318 S  SD  . MET   A 1 338 ? -32.112 -16.032 -27.895 1.00 110.79 ? 358 MET   A SD  1 
ATOM   2319 C  CE  . MET   A 1 338 ? -31.190 -16.411 -29.381 1.00 124.44 ? 358 MET   A CE  1 
ATOM   2320 N  N   . VAL   A 1 339 ? -27.022 -16.497 -25.138 1.00 114.68 ? 359 VAL   A N   1 
ATOM   2321 C  CA  . VAL   A 1 339 ? -25.563 -16.489 -25.145 1.00 100.30 ? 359 VAL   A CA  1 
ATOM   2322 C  C   . VAL   A 1 339 ? -25.020 -17.390 -24.042 1.00 85.77  ? 359 VAL   A C   1 
ATOM   2323 O  O   . VAL   A 1 339 ? -24.016 -18.088 -24.229 1.00 92.92  ? 359 VAL   A O   1 
ATOM   2324 C  CB  . VAL   A 1 339 ? -25.038 -15.048 -25.015 1.00 103.87 ? 359 VAL   A CB  1 
ATOM   2325 C  CG1 . VAL   A 1 339 ? -23.532 -15.039 -24.809 1.00 103.26 ? 359 VAL   A CG1 1 
ATOM   2326 C  CG2 . VAL   A 1 339 ? -25.411 -14.238 -26.247 1.00 99.40  ? 359 VAL   A CG2 1 
ATOM   2327 N  N   . VAL   A 1 340 ? -25.682 -17.403 -22.884 1.00 100.13 ? 360 VAL   A N   1 
ATOM   2328 C  CA  . VAL   A 1 340 ? -25.222 -18.230 -21.772 1.00 110.09 ? 360 VAL   A CA  1 
ATOM   2329 C  C   . VAL   A 1 340 ? -25.393 -19.709 -22.098 1.00 112.42 ? 360 VAL   A C   1 
ATOM   2330 O  O   . VAL   A 1 340 ? -24.485 -20.519 -21.873 1.00 97.03  ? 360 VAL   A O   1 
ATOM   2331 C  CB  . VAL   A 1 340 ? -25.964 -17.849 -20.478 1.00 98.34  ? 360 VAL   A CB  1 
ATOM   2332 C  CG1 . VAL   A 1 340 ? -25.664 -18.855 -19.380 1.00 110.27 ? 360 VAL   A CG1 1 
ATOM   2333 C  CG2 . VAL   A 1 340 ? -25.570 -16.449 -20.035 1.00 91.84  ? 360 VAL   A CG2 1 
ATOM   2334 N  N   . ASN   A 1 341 ? -26.556 -20.083 -22.637 1.00 111.84 ? 361 ASN   A N   1 
ATOM   2335 C  CA  . ASN   A 1 341 ? -26.813 -21.489 -22.937 1.00 104.45 ? 361 ASN   A CA  1 
ATOM   2336 C  C   . ASN   A 1 341 ? -25.862 -22.014 -24.006 1.00 100.35 ? 361 ASN   A C   1 
ATOM   2337 O  O   . ASN   A 1 341 ? -25.344 -23.131 -23.891 1.00 112.28 ? 361 ASN   A O   1 
ATOM   2338 C  CB  . ASN   A 1 341 ? -28.264 -21.681 -23.378 1.00 103.09 ? 361 ASN   A CB  1 
ATOM   2339 C  CG  . ASN   A 1 341 ? -29.255 -21.394 -22.268 1.00 104.00 ? 361 ASN   A CG  1 
ATOM   2340 O  OD1 . ASN   A 1 341 ? -28.893 -21.352 -21.092 1.00 103.34 ? 361 ASN   A OD1 1 
ATOM   2341 N  ND2 . ASN   A 1 341 ? -30.516 -21.203 -22.636 1.00 112.67 ? 361 ASN   A ND2 1 
ATOM   2342 N  N   . GLU   A 1 342 ? -25.619 -21.221 -25.053 1.00 102.06 ? 362 GLU   A N   1 
ATOM   2343 C  CA  . GLU   A 1 342 ? -24.777 -21.686 -26.151 1.00 97.05  ? 362 GLU   A CA  1 
ATOM   2344 C  C   . GLU   A 1 342 ? -23.332 -21.868 -25.708 1.00 110.69 ? 362 GLU   A C   1 
ATOM   2345 O  O   . GLU   A 1 342 ? -22.672 -22.834 -26.109 1.00 117.82 ? 362 GLU   A O   1 
ATOM   2346 C  CB  . GLU   A 1 342 ? -24.866 -20.714 -27.328 1.00 97.37  ? 362 GLU   A CB  1 
ATOM   2347 C  CG  . GLU   A 1 342 ? -23.893 -21.002 -28.469 1.00 104.23 ? 362 GLU   A CG  1 
ATOM   2348 C  CD  . GLU   A 1 342 ? -24.263 -22.229 -29.290 1.00 106.08 ? 362 GLU   A CD  1 
ATOM   2349 O  OE1 . GLU   A 1 342 ? -25.239 -22.927 -28.940 1.00 112.64 ? 362 GLU   A OE1 1 
ATOM   2350 O  OE2 . GLU   A 1 342 ? -23.573 -22.493 -30.297 1.00 110.82 ? 362 GLU   A OE2 1 
ATOM   2351 N  N   . THR   A 1 343 ? -22.820 -20.952 -24.882 1.00 105.10 ? 363 THR   A N   1 
ATOM   2352 C  CA  . THR   A 1 343 ? -21.461 -21.106 -24.374 1.00 100.75 ? 363 THR   A CA  1 
ATOM   2353 C  C   . THR   A 1 343 ? -21.349 -22.336 -23.482 1.00 103.89 ? 363 THR   A C   1 
ATOM   2354 O  O   . THR   A 1 343 ? -20.342 -23.053 -23.523 1.00 98.77  ? 363 THR   A O   1 
ATOM   2355 C  CB  . THR   A 1 343 ? -21.035 -19.850 -23.615 1.00 100.02 ? 363 THR   A CB  1 
ATOM   2356 O  OG1 . THR   A 1 343 ? -21.229 -18.699 -24.446 1.00 102.61 ? 363 THR   A OG1 1 
ATOM   2357 C  CG2 . THR   A 1 343 ? -19.567 -19.941 -23.229 1.00 108.59 ? 363 THR   A CG2 1 
ATOM   2358 N  N   . LEU   A 1 344 ? -22.379 -22.602 -22.675 1.00 106.65 ? 364 LEU   A N   1 
ATOM   2359 C  CA  . LEU   A 1 344 ? -22.388 -23.811 -21.861 1.00 94.92  ? 364 LEU   A CA  1 
ATOM   2360 C  C   . LEU   A 1 344 ? -22.516 -25.073 -22.704 1.00 95.33  ? 364 LEU   A C   1 
ATOM   2361 O  O   . LEU   A 1 344 ? -22.122 -26.150 -22.245 1.00 98.62  ? 364 LEU   A O   1 
ATOM   2362 C  CB  . LEU   A 1 344 ? -23.518 -23.750 -20.834 1.00 88.58  ? 364 LEU   A CB  1 
ATOM   2363 C  CG  . LEU   A 1 344 ? -23.233 -22.888 -19.604 1.00 88.94  ? 364 LEU   A CG  1 
ATOM   2364 C  CD1 . LEU   A 1 344 ? -24.417 -22.907 -18.654 1.00 105.49 ? 364 LEU   A CD1 1 
ATOM   2365 C  CD2 . LEU   A 1 344 ? -21.971 -23.368 -18.903 1.00 80.44  ? 364 LEU   A CD2 1 
ATOM   2366 N  N   . ARG   A 1 345 ? -23.060 -24.968 -23.918 1.00 86.81  ? 365 ARG   A N   1 
ATOM   2367 C  CA  . ARG   A 1 345 ? -23.068 -26.116 -24.817 1.00 94.96  ? 365 ARG   A CA  1 
ATOM   2368 C  C   . ARG   A 1 345 ? -21.657 -26.440 -25.290 1.00 94.77  ? 365 ARG   A C   1 
ATOM   2369 O  O   . ARG   A 1 345 ? -21.221 -27.595 -25.234 1.00 90.58  ? 365 ARG   A O   1 
ATOM   2370 C  CB  . ARG   A 1 345 ? -23.986 -25.851 -26.012 1.00 86.79  ? 365 ARG   A CB  1 
ATOM   2371 C  CG  . ARG   A 1 345 ? -24.128 -27.042 -26.949 1.00 94.90  ? 365 ARG   A CG  1 
ATOM   2372 C  CD  . ARG   A 1 345 ? -24.872 -26.676 -28.223 1.00 91.28  ? 365 ARG   A CD  1 
ATOM   2373 N  NE  . ARG   A 1 345 ? -24.101 -25.774 -29.071 1.00 97.82  ? 365 ARG   A NE  1 
ATOM   2374 C  CZ  . ARG   A 1 345 ? -23.185 -26.169 -29.945 1.00 103.08 ? 365 ARG   A CZ  1 
ATOM   2375 N  NH1 . ARG   A 1 345 ? -22.887 -27.448 -30.105 1.00 109.14 ? 365 ARG   A NH1 1 
ATOM   2376 N  NH2 . ARG   A 1 345 ? -22.550 -25.257 -30.676 1.00 111.87 ? 365 ARG   A NH2 1 
ATOM   2377 N  N   . LEU   A 1 346 ? -20.923 -25.425 -25.749 1.00 101.85 ? 366 LEU   A N   1 
ATOM   2378 C  CA  . LEU   A 1 346 ? -19.563 -25.655 -26.221 1.00 105.17 ? 366 LEU   A CA  1 
ATOM   2379 C  C   . LEU   A 1 346 ? -18.616 -25.999 -25.080 1.00 92.41  ? 366 LEU   A C   1 
ATOM   2380 O  O   . LEU   A 1 346 ? -17.652 -26.747 -25.284 1.00 82.36  ? 366 LEU   A O   1 
ATOM   2381 C  CB  . LEU   A 1 346 ? -19.052 -24.428 -26.977 1.00 93.51  ? 366 LEU   A CB  1 
ATOM   2382 C  CG  . LEU   A 1 346 ? -19.658 -24.182 -28.358 1.00 95.51  ? 366 LEU   A CG  1 
ATOM   2383 C  CD1 . LEU   A 1 346 ? -19.099 -22.907 -28.968 1.00 115.93 ? 366 LEU   A CD1 1 
ATOM   2384 C  CD2 . LEU   A 1 346 ? -19.401 -25.372 -29.269 1.00 76.43  ? 366 LEU   A CD2 1 
ATOM   2385 N  N   . PHE   A 1 347 ? -18.866 -25.478 -23.881 1.00 84.09  ? 367 PHE   A N   1 
ATOM   2386 C  CA  . PHE   A 1 347 ? -17.975 -25.671 -22.738 1.00 88.15  ? 367 PHE   A CA  1 
ATOM   2387 C  C   . PHE   A 1 347 ? -18.770 -26.088 -21.506 1.00 94.28  ? 367 PHE   A C   1 
ATOM   2388 O  O   . PHE   A 1 347 ? -18.944 -25.302 -20.566 1.00 98.48  ? 367 PHE   A O   1 
ATOM   2389 C  CB  . PHE   A 1 347 ? -17.170 -24.400 -22.462 1.00 89.47  ? 367 PHE   A CB  1 
ATOM   2390 C  CG  . PHE   A 1 347 ? -16.610 -23.761 -23.699 1.00 100.25 ? 367 PHE   A CG  1 
ATOM   2391 C  CD1 . PHE   A 1 347 ? -15.606 -24.382 -24.422 1.00 99.09  ? 367 PHE   A CD1 1 
ATOM   2392 C  CD2 . PHE   A 1 347 ? -17.088 -22.538 -24.139 1.00 96.71  ? 367 PHE   A CD2 1 
ATOM   2393 C  CE1 . PHE   A 1 347 ? -15.090 -23.797 -25.562 1.00 92.30  ? 367 PHE   A CE1 1 
ATOM   2394 C  CE2 . PHE   A 1 347 ? -16.575 -21.946 -25.277 1.00 105.13 ? 367 PHE   A CE2 1 
ATOM   2395 C  CZ  . PHE   A 1 347 ? -15.574 -22.577 -25.990 1.00 101.71 ? 367 PHE   A CZ  1 
ATOM   2396 N  N   . PRO   A 1 348 ? -19.268 -27.331 -21.473 1.00 81.72  ? 368 PRO   A N   1 
ATOM   2397 C  CA  . PRO   A 1 348 ? -19.825 -27.856 -20.220 1.00 94.81  ? 368 PRO   A CA  1 
ATOM   2398 C  C   . PRO   A 1 348 ? -18.713 -28.254 -19.263 1.00 107.14 ? 368 PRO   A C   1 
ATOM   2399 O  O   . PRO   A 1 348 ? -18.128 -29.334 -19.396 1.00 108.62 ? 368 PRO   A O   1 
ATOM   2400 C  CB  . PRO   A 1 348 ? -20.651 -29.063 -20.679 1.00 104.55 ? 368 PRO   A CB  1 
ATOM   2401 C  CG  . PRO   A 1 348 ? -19.974 -29.520 -21.924 1.00 100.50 ? 368 PRO   A CG  1 
ATOM   2402 C  CD  . PRO   A 1 348 ? -19.406 -28.290 -22.585 1.00 91.16  ? 368 PRO   A CD  1 
ATOM   2403 N  N   . ILE   A 1 349 ? -18.422 -27.385 -18.294 1.00 97.10  ? 369 ILE   A N   1 
ATOM   2404 C  CA  . ILE   A 1 349 ? -17.249 -27.492 -17.429 1.00 97.81  ? 369 ILE   A CA  1 
ATOM   2405 C  C   . ILE   A 1 349 ? -17.143 -28.865 -16.774 1.00 97.22  ? 369 ILE   A C   1 
ATOM   2406 O  O   . ILE   A 1 349 ? -16.049 -29.300 -16.400 1.00 106.18 ? 369 ILE   A O   1 
ATOM   2407 C  CB  . ILE   A 1 349 ? -17.264 -26.387 -16.359 1.00 102.30 ? 369 ILE   A CB  1 
ATOM   2408 C  CG1 . ILE   A 1 349 ? -18.587 -26.416 -15.592 1.00 103.06 ? 369 ILE   A CG1 1 
ATOM   2409 C  CG2 . ILE   A 1 349 ? -17.033 -25.024 -16.997 1.00 92.62  ? 369 ILE   A CG2 1 
ATOM   2410 C  CD1 . ILE   A 1 349 ? -18.670 -25.407 -14.478 1.00 101.78 ? 369 ILE   A CD1 1 
ATOM   2411 N  N   . ALA   A 1 350 ? -18.273 -29.557 -16.628 1.00 106.67 ? 370 ALA   A N   1 
ATOM   2412 C  CA  . ALA   A 1 350 ? -18.260 -30.884 -16.028 1.00 97.93  ? 370 ALA   A CA  1 
ATOM   2413 C  C   . ALA   A 1 350 ? -17.900 -31.980 -17.021 1.00 93.68  ? 370 ALA   A C   1 
ATOM   2414 O  O   . ALA   A 1 350 ? -17.431 -33.044 -16.598 1.00 86.50  ? 370 ALA   A O   1 
ATOM   2415 C  CB  . ALA   A 1 350 ? -19.619 -31.193 -15.396 1.00 81.85  ? 370 ALA   A CB  1 
ATOM   2416 N  N   . MET   A 1 351 ? -18.133 -31.758 -18.317 1.00 90.33  ? 371 MET   A N   1 
ATOM   2417 C  CA  . MET   A 1 351 ? -17.767 -32.692 -19.382 1.00 89.41  ? 371 MET   A CA  1 
ATOM   2418 C  C   . MET   A 1 351 ? -18.640 -33.938 -19.267 1.00 86.97  ? 371 MET   A C   1 
ATOM   2419 O  O   . MET   A 1 351 ? -19.280 -34.340 -20.244 1.00 84.23  ? 371 MET   A O   1 
ATOM   2420 C  CB  . MET   A 1 351 ? -16.257 -32.947 -19.377 1.00 100.95 ? 371 MET   A CB  1 
ATOM   2421 C  CG  . MET   A 1 351 ? -15.422 -31.725 -19.715 1.00 114.79 ? 371 MET   A CG  1 
ATOM   2422 S  SD  . MET   A 1 351 ? -13.666 -31.987 -19.413 1.00 130.90 ? 371 MET   A SD  1 
ATOM   2423 C  CE  . MET   A 1 351 ? -13.662 -32.190 -17.633 1.00 137.97 ? 371 MET   A CE  1 
ATOM   2424 N  N   . ARG   A 1 352 ? -18.674 -34.561 -18.089 1.00 90.21  ? 372 ARG   A N   1 
ATOM   2425 C  CA  . ARG   A 1 352 ? -19.286 -35.868 -17.900 1.00 88.40  ? 372 ARG   A CA  1 
ATOM   2426 C  C   . ARG   A 1 352 ? -20.250 -35.833 -16.724 1.00 84.19  ? 372 ARG   A C   1 
ATOM   2427 O  O   . ARG   A 1 352 ? -20.083 -35.055 -15.781 1.00 90.47  ? 372 ARG   A O   1 
ATOM   2428 C  CB  . ARG   A 1 352 ? -18.232 -36.954 -17.648 1.00 79.95  ? 372 ARG   A CB  1 
ATOM   2429 C  CG  . ARG   A 1 352 ? -17.283 -37.214 -18.801 1.00 85.87  ? 372 ARG   A CG  1 
ATOM   2430 C  CD  . ARG   A 1 352 ? -16.147 -38.110 -18.340 1.00 98.97  ? 372 ARG   A CD  1 
ATOM   2431 N  NE  . ARG   A 1 352 ? -15.475 -38.780 -19.446 1.00 88.81  ? 372 ARG   A NE  1 
ATOM   2432 C  CZ  . ARG   A 1 352 ? -14.614 -39.777 -19.299 1.00 88.90  ? 372 ARG   A CZ  1 
ATOM   2433 N  NH1 . ARG   A 1 352 ? -14.305 -40.252 -18.103 1.00 107.37 ? 372 ARG   A NH1 1 
ATOM   2434 N  NH2 . ARG   A 1 352 ? -14.057 -40.318 -20.378 1.00 98.90  ? 372 ARG   A NH2 1 
ATOM   2435 N  N   . LEU   A 1 353 ? -21.261 -36.695 -16.794 1.00 79.72  ? 373 LEU   A N   1 
ATOM   2436 C  CA  . LEU   A 1 353 ? -22.155 -36.984 -15.680 1.00 84.39  ? 373 LEU   A CA  1 
ATOM   2437 C  C   . LEU   A 1 353 ? -22.040 -38.468 -15.368 1.00 88.93  ? 373 LEU   A C   1 
ATOM   2438 O  O   . LEU   A 1 353 ? -22.136 -39.301 -16.275 1.00 85.84  ? 373 LEU   A O   1 
ATOM   2439 C  CB  . LEU   A 1 353 ? -23.603 -36.620 -16.017 1.00 90.73  ? 373 LEU   A CB  1 
ATOM   2440 C  CG  . LEU   A 1 353 ? -23.861 -35.181 -16.464 1.00 95.78  ? 373 LEU   A CG  1 
ATOM   2441 C  CD1 . LEU   A 1 353 ? -25.275 -35.030 -17.006 1.00 94.14  ? 373 LEU   A CD1 1 
ATOM   2442 C  CD2 . LEU   A 1 353 ? -23.624 -34.223 -15.313 1.00 85.46  ? 373 LEU   A CD2 1 
ATOM   2443 N  N   . GLU   A 1 354 ? -21.827 -38.801 -14.096 1.00 87.76  ? 374 GLU   A N   1 
ATOM   2444 C  CA  . GLU   A 1 354 ? -21.535 -40.174 -13.711 1.00 74.27  ? 374 GLU   A CA  1 
ATOM   2445 C  C   . GLU   A 1 354 ? -22.417 -40.616 -12.552 1.00 76.30  ? 374 GLU   A C   1 
ATOM   2446 O  O   . GLU   A 1 354 ? -22.713 -39.833 -11.645 1.00 90.25  ? 374 GLU   A O   1 
ATOM   2447 C  CB  . GLU   A 1 354 ? -20.058 -40.339 -13.334 1.00 102.83 ? 374 GLU   A CB  1 
ATOM   2448 C  CG  . GLU   A 1 354 ? -19.102 -40.102 -14.492 1.00 103.15 ? 374 GLU   A CG  1 
ATOM   2449 C  CD  . GLU   A 1 354 ? -17.677 -40.501 -14.167 1.00 111.78 ? 374 GLU   A CD  1 
ATOM   2450 O  OE1 . GLU   A 1 354 ? -17.405 -40.833 -12.995 1.00 113.49 ? 374 GLU   A OE1 1 
ATOM   2451 O  OE2 . GLU   A 1 354 ? -16.831 -40.486 -15.086 1.00 121.98 ? 374 GLU   A OE2 1 
ATOM   2452 N  N   . ARG   A 1 355 ? -22.832 -41.882 -12.599 1.00 99.78  ? 375 ARG   A N   1 
ATOM   2453 C  CA  . ARG   A 1 355 ? -23.603 -42.521 -11.543 1.00 91.65  ? 375 ARG   A CA  1 
ATOM   2454 C  C   . ARG   A 1 355 ? -23.091 -43.941 -11.360 1.00 91.18  ? 375 ARG   A C   1 
ATOM   2455 O  O   . ARG   A 1 355 ? -22.738 -44.608 -12.336 1.00 90.45  ? 375 ARG   A O   1 
ATOM   2456 C  CB  . ARG   A 1 355 ? -25.103 -42.556 -11.871 1.00 83.61  ? 375 ARG   A CB  1 
ATOM   2457 C  CG  . ARG   A 1 355 ? -25.753 -41.198 -12.075 1.00 100.25 ? 375 ARG   A CG  1 
ATOM   2458 C  CD  . ARG   A 1 355 ? -25.933 -40.457 -10.763 1.00 94.09  ? 375 ARG   A CD  1 
ATOM   2459 N  NE  . ARG   A 1 355 ? -26.695 -39.227 -10.946 1.00 92.30  ? 375 ARG   A NE  1 
ATOM   2460 C  CZ  . ARG   A 1 355 ? -26.163 -38.062 -11.286 1.00 76.69  ? 375 ARG   A CZ  1 
ATOM   2461 N  NH1 . ARG   A 1 355 ? -24.862 -37.926 -11.481 1.00 85.40  ? 375 ARG   A NH1 1 
ATOM   2462 N  NH2 . ARG   A 1 355 ? -26.957 -37.005 -11.437 1.00 88.55  ? 375 ARG   A NH2 1 
ATOM   2463 N  N   . VAL   A 1 356 ? -23.053 -44.401 -10.114 1.00 103.06 ? 376 VAL   A N   1 
ATOM   2464 C  CA  . VAL   A 1 356 ? -22.632 -45.763 -9.806  1.00 85.15  ? 376 VAL   A CA  1 
ATOM   2465 C  C   . VAL   A 1 356 ? -23.867 -46.649 -9.726  1.00 103.27 ? 376 VAL   A C   1 
ATOM   2466 O  O   . VAL   A 1 356 ? -24.755 -46.421 -8.896  1.00 101.93 ? 376 VAL   A O   1 
ATOM   2467 C  CB  . VAL   A 1 356 ? -21.826 -45.820 -8.500  1.00 88.06  ? 376 VAL   A CB  1 
ATOM   2468 C  CG1 . VAL   A 1 356 ? -21.768 -47.248 -7.976  1.00 90.46  ? 376 VAL   A CG1 1 
ATOM   2469 C  CG2 . VAL   A 1 356 ? -20.422 -45.291 -8.727  1.00 106.82 ? 376 VAL   A CG2 1 
ATOM   2470 N  N   . CYS   A 1 357 ? -23.929 -47.652 -10.597 1.00 110.35 ? 377 CYS   A N   1 
ATOM   2471 C  CA  . CYS   A 1 357 ? -24.988 -48.649 -10.528 1.00 113.67 ? 377 CYS   A CA  1 
ATOM   2472 C  C   . CYS   A 1 357 ? -24.825 -49.469 -9.253  1.00 108.00 ? 377 CYS   A C   1 
ATOM   2473 O  O   . CYS   A 1 357 ? -23.809 -50.148 -9.071  1.00 115.99 ? 377 CYS   A O   1 
ATOM   2474 C  CB  . CYS   A 1 357 ? -24.939 -49.544 -11.765 1.00 104.17 ? 377 CYS   A CB  1 
ATOM   2475 S  SG  . CYS   A 1 357 ? -26.133 -50.892 -11.778 1.00 124.01 ? 377 CYS   A SG  1 
ATOM   2476 N  N   . LYS   A 1 358 ? -25.818 -49.404 -8.367  1.00 94.28  ? 378 LYS   A N   1 
ATOM   2477 C  CA  . LYS   A 1 358 ? -25.707 -50.014 -7.048  1.00 116.92 ? 378 LYS   A CA  1 
ATOM   2478 C  C   . LYS   A 1 358 ? -26.382 -51.378 -6.950  1.00 124.16 ? 378 LYS   A C   1 
ATOM   2479 O  O   . LYS   A 1 358 ? -26.290 -52.017 -5.898  1.00 120.08 ? 378 LYS   A O   1 
ATOM   2480 C  CB  . LYS   A 1 358 ? -26.278 -49.076 -5.976  1.00 101.38 ? 378 LYS   A CB  1 
ATOM   2481 C  CG  . LYS   A 1 358 ? -27.787 -49.144 -5.814  1.00 118.90 ? 378 LYS   A CG  1 
ATOM   2482 C  CD  . LYS   A 1 358 ? -28.254 -48.441 -4.544  1.00 125.62 ? 378 LYS   A CD  1 
ATOM   2483 C  CE  . LYS   A 1 358 ? -28.284 -46.929 -4.706  1.00 119.58 ? 378 LYS   A CE  1 
ATOM   2484 N  NZ  . LYS   A 1 358 ? -29.025 -46.280 -3.586  1.00 128.02 ? 378 LYS   A NZ  1 
ATOM   2485 N  N   . LYS   A 1 359 ? -27.052 -51.837 -8.006  1.00 113.58 ? 379 LYS   A N   1 
ATOM   2486 C  CA  . LYS   A 1 359 ? -27.597 -53.191 -8.050  1.00 123.99 ? 379 LYS   A CA  1 
ATOM   2487 C  C   . LYS   A 1 359 ? -28.011 -53.504 -9.480  1.00 135.67 ? 379 LYS   A C   1 
ATOM   2488 O  O   . LYS   A 1 359 ? -28.218 -52.600 -10.296 1.00 144.39 ? 379 LYS   A O   1 
ATOM   2489 C  CB  . LYS   A 1 359 ? -28.783 -53.370 -7.093  1.00 126.27 ? 379 LYS   A CB  1 
ATOM   2490 C  CG  . LYS   A 1 359 ? -30.005 -52.526 -7.406  1.00 116.71 ? 379 LYS   A CG  1 
ATOM   2491 C  CD  . LYS   A 1 359 ? -31.090 -52.768 -6.365  1.00 108.62 ? 379 LYS   A CD  1 
ATOM   2492 C  CE  . LYS   A 1 359 ? -32.337 -51.946 -6.640  1.00 115.20 ? 379 LYS   A CE  1 
ATOM   2493 N  NZ  . LYS   A 1 359 ? -33.361 -52.138 -5.575  1.00 134.52 ? 379 LYS   A NZ  1 
ATOM   2494 N  N   . ASP   A 1 360 ? -28.130 -54.801 -9.768  1.00 128.50 ? 380 ASP   A N   1 
ATOM   2495 C  CA  . ASP   A 1 360 ? -28.447 -55.258 -11.117 1.00 130.62 ? 380 ASP   A CA  1 
ATOM   2496 C  C   . ASP   A 1 360 ? -29.755 -54.653 -11.608 1.00 136.15 ? 380 ASP   A C   1 
ATOM   2497 O  O   . ASP   A 1 360 ? -30.752 -54.609 -10.881 1.00 152.37 ? 380 ASP   A O   1 
ATOM   2498 C  CB  . ASP   A 1 360 ? -28.538 -56.784 -11.153 1.00 137.92 ? 380 ASP   A CB  1 
ATOM   2499 C  CG  . ASP   A 1 360 ? -27.202 -57.457 -10.914 1.00 145.12 ? 380 ASP   A CG  1 
ATOM   2500 O  OD1 . ASP   A 1 360 ? -26.214 -56.745 -10.640 1.00 146.64 ? 380 ASP   A OD1 1 
ATOM   2501 O  OD2 . ASP   A 1 360 ? -27.140 -58.701 -11.003 1.00 159.79 ? 380 ASP   A OD2 1 
ATOM   2502 N  N   . VAL   A 1 361 ? -29.743 -54.184 -12.858 1.00 116.07 ? 381 VAL   A N   1 
ATOM   2503 C  CA  . VAL   A 1 361 ? -30.914 -53.588 -13.488 1.00 128.55 ? 381 VAL   A CA  1 
ATOM   2504 C  C   . VAL   A 1 361 ? -30.900 -53.917 -14.973 1.00 130.15 ? 381 VAL   A C   1 
ATOM   2505 O  O   . VAL   A 1 361 ? -29.875 -54.301 -15.541 1.00 127.05 ? 381 VAL   A O   1 
ATOM   2506 C  CB  . VAL   A 1 361 ? -30.978 -52.056 -13.284 1.00 132.50 ? 381 VAL   A CB  1 
ATOM   2507 C  CG1 . VAL   A 1 361 ? -31.682 -51.727 -11.983 1.00 134.57 ? 381 VAL   A CG1 1 
ATOM   2508 C  CG2 . VAL   A 1 361 ? -29.579 -51.462 -13.306 1.00 131.55 ? 381 VAL   A CG2 1 
ATOM   2509 N  N   . GLU   A 1 362 ? -32.066 -53.761 -15.602 1.00 162.49 ? 382 GLU   A N   1 
ATOM   2510 C  CA  . GLU   A 1 362 ? -32.247 -53.943 -17.043 1.00 164.20 ? 382 GLU   A CA  1 
ATOM   2511 C  C   . GLU   A 1 362 ? -33.009 -52.718 -17.543 1.00 163.14 ? 382 GLU   A C   1 
ATOM   2512 O  O   . GLU   A 1 362 ? -34.218 -52.770 -17.780 1.00 172.29 ? 382 GLU   A O   1 
ATOM   2513 C  CB  . GLU   A 1 362 ? -32.982 -55.253 -17.351 1.00 177.83 ? 382 GLU   A CB  1 
ATOM   2514 C  CG  . GLU   A 1 362 ? -33.198 -55.522 -18.834 1.00 179.59 ? 382 GLU   A CG  1 
ATOM   2515 C  CD  . GLU   A 1 362 ? -34.070 -56.737 -19.085 1.00 206.36 ? 382 GLU   A CD  1 
ATOM   2516 O  OE1 . GLU   A 1 362 ? -34.014 -57.690 -18.279 1.00 223.11 ? 382 GLU   A OE1 1 
ATOM   2517 O  OE2 . GLU   A 1 362 ? -34.821 -56.734 -20.084 1.00 199.38 ? 382 GLU   A OE2 1 
ATOM   2518 N  N   . ILE   A 1 363 ? -32.298 -51.608 -17.691 1.00 143.94 ? 383 ILE   A N   1 
ATOM   2519 C  CA  . ILE   A 1 363 ? -32.923 -50.357 -18.104 1.00 152.49 ? 383 ILE   A CA  1 
ATOM   2520 C  C   . ILE   A 1 363 ? -33.043 -50.327 -19.622 1.00 161.96 ? 383 ILE   A C   1 
ATOM   2521 O  O   . ILE   A 1 363 ? -32.103 -50.679 -20.346 1.00 155.39 ? 383 ILE   A O   1 
ATOM   2522 C  CB  . ILE   A 1 363 ? -32.131 -49.149 -17.567 1.00 139.13 ? 383 ILE   A CB  1 
ATOM   2523 C  CG1 . ILE   A 1 363 ? -30.780 -49.009 -18.271 1.00 134.62 ? 383 ILE   A CG1 1 
ATOM   2524 C  CG2 . ILE   A 1 363 ? -31.907 -49.289 -16.071 1.00 133.59 ? 383 ILE   A CG2 1 
ATOM   2525 C  CD1 . ILE   A 1 363 ? -30.052 -47.740 -17.927 1.00 131.33 ? 383 ILE   A CD1 1 
ATOM   2526 N  N   . ASN   A 1 364 ? -34.224 -49.927 -20.101 1.00 167.73 ? 384 ASN   A N   1 
ATOM   2527 C  CA  . ASN   A 1 364 ? -34.520 -49.742 -21.522 1.00 167.07 ? 384 ASN   A CA  1 
ATOM   2528 C  C   . ASN   A 1 364 ? -33.995 -50.882 -22.388 1.00 162.93 ? 384 ASN   A C   1 
ATOM   2529 O  O   . ASN   A 1 364 ? -33.435 -50.649 -23.463 1.00 158.95 ? 384 ASN   A O   1 
ATOM   2530 C  CB  . ASN   A 1 364 ? -33.956 -48.401 -22.004 1.00 158.81 ? 384 ASN   A CB  1 
ATOM   2531 C  CG  . ASN   A 1 364 ? -34.692 -47.208 -21.414 1.00 148.48 ? 384 ASN   A CG  1 
ATOM   2532 O  OD1 . ASN   A 1 364 ? -35.587 -46.640 -22.043 1.00 150.64 ? 384 ASN   A OD1 1 
ATOM   2533 N  ND2 . ASN   A 1 364 ? -34.317 -46.824 -20.201 1.00 139.42 ? 384 ASN   A ND2 1 
ATOM   2534 N  N   . GLY   A 1 365 ? -34.164 -52.114 -21.917 1.00 157.52 ? 385 GLY   A N   1 
ATOM   2535 C  CA  . GLY   A 1 365 ? -33.784 -53.285 -22.676 1.00 162.73 ? 385 GLY   A CA  1 
ATOM   2536 C  C   . GLY   A 1 365 ? -32.326 -53.681 -22.603 1.00 163.14 ? 385 GLY   A C   1 
ATOM   2537 O  O   . GLY   A 1 365 ? -31.905 -54.556 -23.369 1.00 157.70 ? 385 GLY   A O   1 
ATOM   2538 N  N   . MET   A 1 366 ? -31.541 -53.078 -21.713 1.00 154.59 ? 386 MET   A N   1 
ATOM   2539 C  CA  . MET   A 1 366 ? -30.122 -53.391 -21.586 1.00 142.54 ? 386 MET   A CA  1 
ATOM   2540 C  C   . MET   A 1 366 ? -29.813 -53.718 -20.134 1.00 139.52 ? 386 MET   A C   1 
ATOM   2541 O  O   . MET   A 1 366 ? -30.091 -52.911 -19.241 1.00 131.23 ? 386 MET   A O   1 
ATOM   2542 C  CB  . MET   A 1 366 ? -29.249 -52.229 -22.064 1.00 143.79 ? 386 MET   A CB  1 
ATOM   2543 C  CG  . MET   A 1 366 ? -27.758 -52.473 -21.891 1.00 139.47 ? 386 MET   A CG  1 
ATOM   2544 S  SD  . MET   A 1 366 ? -26.765 -51.043 -22.353 1.00 136.43 ? 386 MET   A SD  1 
ATOM   2545 C  CE  . MET   A 1 366 ? -27.377 -50.741 -24.008 1.00 126.61 ? 386 MET   A CE  1 
ATOM   2546 N  N   . PHE   A 1 367 ? -29.234 -54.894 -19.902 1.00 139.25 ? 387 PHE   A N   1 
ATOM   2547 C  CA  . PHE   A 1 367 ? -28.797 -55.262 -18.563 1.00 130.98 ? 387 PHE   A CA  1 
ATOM   2548 C  C   . PHE   A 1 367 ? -27.531 -54.501 -18.191 1.00 128.97 ? 387 PHE   A C   1 
ATOM   2549 O  O   . PHE   A 1 367 ? -26.626 -54.326 -19.012 1.00 131.09 ? 387 PHE   A O   1 
ATOM   2550 C  CB  . PHE   A 1 367 ? -28.549 -56.767 -18.476 1.00 130.13 ? 387 PHE   A CB  1 
ATOM   2551 C  CG  . PHE   A 1 367 ? -27.841 -57.193 -17.220 1.00 136.52 ? 387 PHE   A CG  1 
ATOM   2552 C  CD1 . PHE   A 1 367 ? -28.521 -57.264 -16.015 1.00 142.61 ? 387 PHE   A CD1 1 
ATOM   2553 C  CD2 . PHE   A 1 367 ? -26.495 -57.524 -17.243 1.00 130.57 ? 387 PHE   A CD2 1 
ATOM   2554 C  CE1 . PHE   A 1 367 ? -27.873 -57.653 -14.857 1.00 137.54 ? 387 PHE   A CE1 1 
ATOM   2555 C  CE2 . PHE   A 1 367 ? -25.841 -57.915 -16.088 1.00 132.69 ? 387 PHE   A CE2 1 
ATOM   2556 C  CZ  . PHE   A 1 367 ? -26.531 -57.980 -14.894 1.00 129.61 ? 387 PHE   A CZ  1 
ATOM   2557 N  N   . ILE   A 1 368 ? -27.472 -54.045 -16.939 1.00 135.29 ? 388 ILE   A N   1 
ATOM   2558 C  CA  . ILE   A 1 368 ? -26.313 -53.345 -16.408 1.00 118.52 ? 388 ILE   A CA  1 
ATOM   2559 C  C   . ILE   A 1 368 ? -25.932 -54.000 -15.085 1.00 132.66 ? 388 ILE   A C   1 
ATOM   2560 O  O   . ILE   A 1 368 ? -26.739 -54.016 -14.151 1.00 126.52 ? 388 ILE   A O   1 
ATOM   2561 C  CB  . ILE   A 1 368 ? -26.573 -51.842 -16.206 1.00 125.65 ? 388 ILE   A CB  1 
ATOM   2562 C  CG1 . ILE   A 1 368 ? -26.873 -51.171 -17.549 1.00 122.50 ? 388 ILE   A CG1 1 
ATOM   2563 C  CG2 . ILE   A 1 368 ? -25.382 -51.180 -15.528 1.00 114.08 ? 388 ILE   A CG2 1 
ATOM   2564 C  CD1 . ILE   A 1 368 ? -27.060 -49.677 -17.455 1.00 104.83 ? 388 ILE   A CD1 1 
ATOM   2565 N  N   . PRO   A 1 369 ? -24.728 -54.545 -14.949 1.00 127.25 ? 389 PRO   A N   1 
ATOM   2566 C  CA  . PRO   A 1 369 ? -24.372 -55.270 -13.727 1.00 115.45 ? 389 PRO   A CA  1 
ATOM   2567 C  C   . PRO   A 1 369 ? -24.090 -54.325 -12.568 1.00 117.87 ? 389 PRO   A C   1 
ATOM   2568 O  O   . PRO   A 1 369 ? -23.883 -53.122 -12.738 1.00 122.79 ? 389 PRO   A O   1 
ATOM   2569 C  CB  . PRO   A 1 369 ? -23.104 -56.043 -14.120 1.00 116.09 ? 389 PRO   A CB  1 
ATOM   2570 C  CG  . PRO   A 1 369 ? -22.908 -55.798 -15.599 1.00 121.39 ? 389 PRO   A CG  1 
ATOM   2571 C  CD  . PRO   A 1 369 ? -23.616 -54.524 -15.909 1.00 120.37 ? 389 PRO   A CD  1 
ATOM   2572 N  N   . LYS   A 1 370 ? -24.077 -54.906 -11.372 1.00 114.68 ? 390 LYS   A N   1 
ATOM   2573 C  CA  . LYS   A 1 370 ? -23.835 -54.132 -10.163 1.00 121.36 ? 390 LYS   A CA  1 
ATOM   2574 C  C   . LYS   A 1 370 ? -22.393 -53.640 -10.124 1.00 115.37 ? 390 LYS   A C   1 
ATOM   2575 O  O   . LYS   A 1 370 ? -21.458 -54.401 -10.389 1.00 124.41 ? 390 LYS   A O   1 
ATOM   2576 C  CB  . LYS   A 1 370 ? -24.142 -54.978 -8.929  1.00 117.62 ? 390 LYS   A CB  1 
ATOM   2577 C  CG  . LYS   A 1 370 ? -23.957 -54.254 -7.608  1.00 99.65  ? 390 LYS   A CG  1 
ATOM   2578 C  CD  . LYS   A 1 370 ? -24.377 -55.137 -6.444  1.00 130.49 ? 390 LYS   A CD  1 
ATOM   2579 C  CE  . LYS   A 1 370 ? -24.251 -54.409 -5.117  1.00 144.55 ? 390 LYS   A CE  1 
ATOM   2580 N  NZ  . LYS   A 1 370 ? -24.742 -55.237 -3.981  1.00 158.26 ? 390 LYS   A NZ  1 
ATOM   2581 N  N   . GLY   A 1 371 ? -22.217 -52.359 -9.795  1.00 106.88 ? 391 GLY   A N   1 
ATOM   2582 C  CA  . GLY   A 1 371 ? -20.912 -51.758 -9.648  1.00 101.55 ? 391 GLY   A CA  1 
ATOM   2583 C  C   . GLY   A 1 371 ? -20.450 -50.937 -10.836 1.00 107.94 ? 391 GLY   A C   1 
ATOM   2584 O  O   . GLY   A 1 371 ? -19.493 -50.166 -10.700 1.00 106.61 ? 391 GLY   A O   1 
ATOM   2585 N  N   . VAL   A 1 372 ? -21.102 -51.079 -11.990 1.00 103.92 ? 392 VAL   A N   1 
ATOM   2586 C  CA  . VAL   A 1 372 ? -20.676 -50.368 -13.189 1.00 93.70  ? 392 VAL   A CA  1 
ATOM   2587 C  C   . VAL   A 1 372 ? -20.942 -48.878 -13.028 1.00 100.69 ? 392 VAL   A C   1 
ATOM   2588 O  O   . VAL   A 1 372 ? -22.027 -48.466 -12.598 1.00 112.95 ? 392 VAL   A O   1 
ATOM   2589 C  CB  . VAL   A 1 372 ? -21.390 -50.930 -14.428 1.00 97.31  ? 392 VAL   A CB  1 
ATOM   2590 C  CG1 . VAL   A 1 372 ? -21.143 -50.042 -15.638 1.00 100.54 ? 392 VAL   A CG1 1 
ATOM   2591 C  CG2 . VAL   A 1 372 ? -20.925 -52.350 -14.706 1.00 111.56 ? 392 VAL   A CG2 1 
ATOM   2592 N  N   . VAL   A 1 373 ? -19.948 -48.063 -13.368 1.00 105.64 ? 393 VAL   A N   1 
ATOM   2593 C  CA  . VAL   A 1 373 ? -20.102 -46.612 -13.370 1.00 98.34  ? 393 VAL   A CA  1 
ATOM   2594 C  C   . VAL   A 1 373 ? -20.746 -46.210 -14.693 1.00 99.24  ? 393 VAL   A C   1 
ATOM   2595 O  O   . VAL   A 1 373 ? -20.143 -46.357 -15.758 1.00 102.54 ? 393 VAL   A O   1 
ATOM   2596 C  CB  . VAL   A 1 373 ? -18.760 -45.900 -13.166 1.00 85.99  ? 393 VAL   A CB  1 
ATOM   2597 C  CG1 . VAL   A 1 373 ? -18.891 -44.416 -13.479 1.00 76.59  ? 393 VAL   A CG1 1 
ATOM   2598 C  CG2 . VAL   A 1 373 ? -18.265 -46.102 -11.743 1.00 79.85  ? 393 VAL   A CG2 1 
ATOM   2599 N  N   . VAL   A 1 374 ? -21.976 -45.711 -14.628 1.00 93.15  ? 394 VAL   A N   1 
ATOM   2600 C  CA  . VAL   A 1 374 ? -22.686 -45.233 -15.809 1.00 95.29  ? 394 VAL   A CA  1 
ATOM   2601 C  C   . VAL   A 1 374 ? -22.289 -43.784 -16.050 1.00 88.07  ? 394 VAL   A C   1 
ATOM   2602 O  O   . VAL   A 1 374 ? -22.395 -42.943 -15.150 1.00 91.96  ? 394 VAL   A O   1 
ATOM   2603 C  CB  . VAL   A 1 374 ? -24.206 -45.374 -15.634 1.00 84.11  ? 394 VAL   A CB  1 
ATOM   2604 C  CG1 . VAL   A 1 374 ? -24.920 -45.075 -16.943 1.00 86.42  ? 394 VAL   A CG1 1 
ATOM   2605 C  CG2 . VAL   A 1 374 ? -24.551 -46.768 -15.135 1.00 80.73  ? 394 VAL   A CG2 1 
ATOM   2606 N  N   . MET   A 1 375 ? -21.836 -43.489 -17.265 1.00 90.60  ? 395 MET   A N   1 
ATOM   2607 C  CA  A MET   A 1 375 ? -21.317 -42.173 -17.606 0.57 102.65 ? 395 MET   A CA  1 
ATOM   2608 C  CA  B MET   A 1 375 ? -21.312 -42.177 -17.611 0.43 97.36  ? 395 MET   A CA  1 
ATOM   2609 C  C   . MET   A 1 375 ? -22.049 -41.628 -18.823 1.00 90.48  ? 395 MET   A C   1 
ATOM   2610 O  O   . MET   A 1 375 ? -22.335 -42.365 -19.771 1.00 99.64  ? 395 MET   A O   1 
ATOM   2611 C  CB  A MET   A 1 375 ? -19.803 -42.232 -17.871 0.57 96.46  ? 395 MET   A CB  1 
ATOM   2612 C  CB  B MET   A 1 375 ? -19.811 -42.250 -17.906 0.43 91.52  ? 395 MET   A CB  1 
ATOM   2613 C  CG  A MET   A 1 375 ? -19.129 -40.879 -18.048 0.57 89.28  ? 395 MET   A CG  1 
ATOM   2614 C  CG  B MET   A 1 375 ? -19.160 -40.912 -18.180 0.43 88.99  ? 395 MET   A CG  1 
ATOM   2615 S  SD  A MET   A 1 375 ? -19.122 -40.295 -19.754 0.57 75.31  ? 395 MET   A SD  1 
ATOM   2616 S  SD  B MET   A 1 375 ? -17.689 -41.098 -19.200 0.43 102.09 ? 395 MET   A SD  1 
ATOM   2617 C  CE  A MET   A 1 375 ? -18.187 -41.595 -20.556 0.57 85.06  ? 395 MET   A CE  1 
ATOM   2618 C  CE  B MET   A 1 375 ? -18.426 -41.395 -20.804 0.43 86.30  ? 395 MET   A CE  1 
ATOM   2619 N  N   . ILE   A 1 376 ? -22.353 -40.335 -18.787 1.00 83.79  ? 396 ILE   A N   1 
ATOM   2620 C  CA  . ILE   A 1 376 ? -22.996 -39.630 -19.889 1.00 93.39  ? 396 ILE   A CA  1 
ATOM   2621 C  C   . ILE   A 1 376 ? -21.983 -38.633 -20.449 1.00 85.20  ? 396 ILE   A C   1 
ATOM   2622 O  O   . ILE   A 1 376 ? -21.660 -37.640 -19.780 1.00 84.76  ? 396 ILE   A O   1 
ATOM   2623 C  CB  . ILE   A 1 376 ? -24.284 -38.921 -19.446 1.00 95.19  ? 396 ILE   A CB  1 
ATOM   2624 C  CG1 . ILE   A 1 376 ? -25.324 -39.934 -18.958 1.00 90.25  ? 396 ILE   A CG1 1 
ATOM   2625 C  CG2 . ILE   A 1 376 ? -24.846 -38.081 -20.583 1.00 83.85  ? 396 ILE   A CG2 1 
ATOM   2626 C  CD1 . ILE   A 1 376 ? -25.329 -40.135 -17.458 1.00 88.44  ? 396 ILE   A CD1 1 
ATOM   2627 N  N   . PRO   A 1 377 ? -21.452 -38.851 -21.654 1.00 80.97  ? 397 PRO   A N   1 
ATOM   2628 C  CA  . PRO   A 1 377 ? -20.461 -37.916 -22.204 1.00 89.93  ? 397 PRO   A CA  1 
ATOM   2629 C  C   . PRO   A 1 377 ? -21.088 -36.595 -22.622 1.00 90.18  ? 397 PRO   A C   1 
ATOM   2630 O  O   . PRO   A 1 377 ? -21.445 -36.411 -23.790 1.00 88.49  ? 397 PRO   A O   1 
ATOM   2631 C  CB  . PRO   A 1 377 ? -19.893 -38.679 -23.406 1.00 104.58 ? 397 PRO   A CB  1 
ATOM   2632 C  CG  . PRO   A 1 377 ? -21.006 -39.580 -23.828 1.00 99.92  ? 397 PRO   A CG  1 
ATOM   2633 C  CD  . PRO   A 1 377 ? -21.722 -39.977 -22.565 1.00 90.50  ? 397 PRO   A CD  1 
ATOM   2634 N  N   . SER   A 1 378 ? -21.215 -35.667 -21.670 1.00 97.29  ? 398 SER   A N   1 
ATOM   2635 C  CA  . SER   A 1 378 ? -21.903 -34.408 -21.941 1.00 70.41  ? 398 SER   A CA  1 
ATOM   2636 C  C   . SER   A 1 378 ? -21.200 -33.608 -23.030 1.00 84.02  ? 398 SER   A C   1 
ATOM   2637 O  O   . SER   A 1 378 ? -21.855 -33.054 -23.920 1.00 85.34  ? 398 SER   A O   1 
ATOM   2638 C  CB  . SER   A 1 378 ? -22.017 -33.586 -20.658 1.00 81.32  ? 398 SER   A CB  1 
ATOM   2639 O  OG  . SER   A 1 378 ? -22.872 -34.220 -19.723 1.00 99.55  ? 398 SER   A OG  1 
ATOM   2640 N  N   . TYR   A 1 379 ? -19.868 -33.531 -22.978 1.00 83.27  ? 399 TYR   A N   1 
ATOM   2641 C  CA  . TYR   A 1 379 ? -19.139 -32.810 -24.017 1.00 89.67  ? 399 TYR   A CA  1 
ATOM   2642 C  C   . TYR   A 1 379 ? -19.364 -33.442 -25.384 1.00 88.21  ? 399 TYR   A C   1 
ATOM   2643 O  O   . TYR   A 1 379 ? -19.487 -32.735 -26.391 1.00 86.39  ? 399 TYR   A O   1 
ATOM   2644 C  CB  . TYR   A 1 379 ? -17.646 -32.767 -23.687 1.00 96.44  ? 399 TYR   A CB  1 
ATOM   2645 C  CG  . TYR   A 1 379 ? -16.820 -31.972 -24.678 1.00 86.94  ? 399 TYR   A CG  1 
ATOM   2646 C  CD1 . TYR   A 1 379 ? -16.345 -32.555 -25.848 1.00 95.04  ? 399 TYR   A CD1 1 
ATOM   2647 C  CD2 . TYR   A 1 379 ? -16.513 -30.638 -24.443 1.00 95.00  ? 399 TYR   A CD2 1 
ATOM   2648 C  CE1 . TYR   A 1 379 ? -15.592 -31.834 -26.753 1.00 102.02 ? 399 TYR   A CE1 1 
ATOM   2649 C  CE2 . TYR   A 1 379 ? -15.758 -29.909 -25.344 1.00 103.50 ? 399 TYR   A CE2 1 
ATOM   2650 C  CZ  . TYR   A 1 379 ? -15.300 -30.513 -26.497 1.00 105.49 ? 399 TYR   A CZ  1 
ATOM   2651 O  OH  . TYR   A 1 379 ? -14.548 -29.795 -27.398 1.00 104.06 ? 399 TYR   A OH  1 
ATOM   2652 N  N   . ALA   A 1 380 ? -19.421 -34.774 -25.440 1.00 91.68  ? 400 ALA   A N   1 
ATOM   2653 C  CA  . ALA   A 1 380 ? -19.621 -35.448 -26.718 1.00 102.43 ? 400 ALA   A CA  1 
ATOM   2654 C  C   . ALA   A 1 380 ? -21.025 -35.208 -27.257 1.00 103.14 ? 400 ALA   A C   1 
ATOM   2655 O  O   . ALA   A 1 380 ? -21.205 -35.005 -28.464 1.00 107.89 ? 400 ALA   A O   1 
ATOM   2656 C  CB  . ALA   A 1 380 ? -19.348 -36.944 -26.572 1.00 99.84  ? 400 ALA   A CB  1 
ATOM   2657 N  N   . LEU   A 1 381 ? -22.031 -35.220 -26.380 1.00 84.42  ? 401 LEU   A N   1 
ATOM   2658 C  CA  . LEU   A 1 381 ? -23.406 -35.029 -26.829 1.00 94.88  ? 401 LEU   A CA  1 
ATOM   2659 C  C   . LEU   A 1 381 ? -23.649 -33.595 -27.279 1.00 97.26  ? 401 LEU   A C   1 
ATOM   2660 O  O   . LEU   A 1 381 ? -24.389 -33.358 -28.242 1.00 110.91 ? 401 LEU   A O   1 
ATOM   2661 C  CB  . LEU   A 1 381 ? -24.379 -35.415 -25.717 1.00 100.54 ? 401 LEU   A CB  1 
ATOM   2662 C  CG  . LEU   A 1 381 ? -24.276 -36.854 -25.209 1.00 98.89  ? 401 LEU   A CG  1 
ATOM   2663 C  CD1 . LEU   A 1 381 ? -25.306 -37.114 -24.123 1.00 90.49  ? 401 LEU   A CD1 1 
ATOM   2664 C  CD2 . LEU   A 1 381 ? -24.431 -37.841 -26.355 1.00 100.75 ? 401 LEU   A CD2 1 
ATOM   2665 N  N   . HIS   A 1 382 ? -23.035 -32.624 -26.599 1.00 93.11  ? 402 HIS   A N   1 
ATOM   2666 C  CA  . HIS   A 1 382 ? -23.194 -31.223 -26.969 1.00 93.71  ? 402 HIS   A CA  1 
ATOM   2667 C  C   . HIS   A 1 382 ? -22.594 -30.898 -28.330 1.00 103.93 ? 402 HIS   A C   1 
ATOM   2668 O  O   . HIS   A 1 382 ? -22.843 -29.805 -28.851 1.00 105.17 ? 402 HIS   A O   1 
ATOM   2669 C  CB  . HIS   A 1 382 ? -22.560 -30.321 -25.909 1.00 93.95  ? 402 HIS   A CB  1 
ATOM   2670 C  CG  . HIS   A 1 382 ? -23.265 -30.343 -24.588 1.00 94.24  ? 402 HIS   A CG  1 
ATOM   2671 N  ND1 . HIS   A 1 382 ? -23.029 -29.405 -23.606 1.00 94.33  ? 402 HIS   A ND1 1 
ATOM   2672 C  CD2 . HIS   A 1 382 ? -24.197 -31.187 -24.085 1.00 103.69 ? 402 HIS   A CD2 1 
ATOM   2673 C  CE1 . HIS   A 1 382 ? -23.785 -29.670 -22.556 1.00 95.67  ? 402 HIS   A CE1 1 
ATOM   2674 N  NE2 . HIS   A 1 382 ? -24.502 -30.746 -22.820 1.00 99.32  ? 402 HIS   A NE2 1 
ATOM   2675 N  N   . ARG   A 1 383 ? -21.810 -31.810 -28.914 1.00 105.99 ? 403 ARG   A N   1 
ATOM   2676 C  CA  . ARG   A 1 383 ? -21.170 -31.575 -30.203 1.00 118.29 ? 403 ARG   A CA  1 
ATOM   2677 C  C   . ARG   A 1 383 ? -21.490 -32.674 -31.211 1.00 121.56 ? 403 ARG   A C   1 
ATOM   2678 O  O   . ARG   A 1 383 ? -20.738 -32.862 -32.172 1.00 114.10 ? 403 ARG   A O   1 
ATOM   2679 C  CB  . ARG   A 1 383 ? -19.654 -31.441 -30.034 1.00 105.61 ? 403 ARG   A CB  1 
ATOM   2680 C  CG  . ARG   A 1 383 ? -19.249 -30.492 -28.922 1.00 100.18 ? 403 ARG   A CG  1 
ATOM   2681 C  CD  . ARG   A 1 383 ? -17.860 -29.934 -29.146 1.00 112.02 ? 403 ARG   A CD  1 
ATOM   2682 N  NE  . ARG   A 1 383 ? -17.574 -28.829 -28.240 1.00 106.19 ? 403 ARG   A NE  1 
ATOM   2683 C  CZ  . ARG   A 1 383 ? -16.698 -27.867 -28.490 1.00 93.86  ? 403 ARG   A CZ  1 
ATOM   2684 N  NH1 . ARG   A 1 383 ? -16.010 -27.835 -29.619 1.00 98.76  ? 403 ARG   A NH1 1 
ATOM   2685 N  NH2 . ARG   A 1 383 ? -16.513 -26.908 -27.587 1.00 98.95  ? 403 ARG   A NH2 1 
ATOM   2686 N  N   . ASP   A 1 384 ? -22.588 -33.397 -31.017 1.00 122.48 ? 404 ASP   A N   1 
ATOM   2687 C  CA  . ASP   A 1 384 ? -22.951 -34.483 -31.921 1.00 137.08 ? 404 ASP   A CA  1 
ATOM   2688 C  C   . ASP   A 1 384 ? -23.671 -33.925 -33.143 1.00 145.19 ? 404 ASP   A C   1 
ATOM   2689 O  O   . ASP   A 1 384 ? -24.722 -33.289 -32.992 1.00 149.59 ? 404 ASP   A O   1 
ATOM   2690 C  CB  . ASP   A 1 384 ? -23.834 -35.496 -31.201 1.00 143.10 ? 404 ASP   A CB  1 
ATOM   2691 C  CG  . ASP   A 1 384 ? -24.094 -36.743 -32.028 1.00 152.03 ? 404 ASP   A CG  1 
ATOM   2692 O  OD1 . ASP   A 1 384 ? -23.492 -36.884 -33.113 1.00 157.10 ? 404 ASP   A OD1 1 
ATOM   2693 O  OD2 . ASP   A 1 384 ? -24.904 -37.587 -31.591 1.00 155.09 ? 404 ASP   A OD2 1 
ATOM   2694 N  N   . PRO   A 1 385 ? -23.146 -34.124 -34.357 1.00 155.34 ? 405 PRO   A N   1 
ATOM   2695 C  CA  . PRO   A 1 385 ? -23.849 -33.631 -35.554 1.00 151.06 ? 405 PRO   A CA  1 
ATOM   2696 C  C   . PRO   A 1 385 ? -25.204 -34.277 -35.772 1.00 150.20 ? 405 PRO   A C   1 
ATOM   2697 O  O   . PRO   A 1 385 ? -26.029 -33.712 -36.498 1.00 149.92 ? 405 PRO   A O   1 
ATOM   2698 C  CB  . PRO   A 1 385 ? -22.881 -33.971 -36.696 1.00 146.89 ? 405 PRO   A CB  1 
ATOM   2699 C  CG  . PRO   A 1 385 ? -21.549 -34.054 -36.044 1.00 134.99 ? 405 PRO   A CG  1 
ATOM   2700 C  CD  . PRO   A 1 385 ? -21.800 -34.625 -34.677 1.00 140.41 ? 405 PRO   A CD  1 
ATOM   2701 N  N   . LYS   A 1 386 ? -25.462 -35.438 -35.173 1.00 151.02 ? 406 LYS   A N   1 
ATOM   2702 C  CA  . LYS   A 1 386 ? -26.779 -36.050 -35.235 1.00 159.59 ? 406 LYS   A CA  1 
ATOM   2703 C  C   . LYS   A 1 386 ? -27.808 -35.339 -34.355 1.00 155.87 ? 406 LYS   A C   1 
ATOM   2704 O  O   . LYS   A 1 386 ? -28.943 -35.805 -34.237 1.00 161.42 ? 406 LYS   A O   1 
ATOM   2705 C  CB  . LYS   A 1 386 ? -26.684 -37.532 -34.852 1.00 165.41 ? 406 LYS   A CB  1 
ATOM   2706 C  CG  . LYS   A 1 386 ? -25.765 -38.330 -35.758 1.00 167.25 ? 406 LYS   A CG  1 
ATOM   2707 C  CD  . LYS   A 1 386 ? -26.263 -39.747 -35.974 1.00 180.56 ? 406 LYS   A CD  1 
ATOM   2708 C  CE  . LYS   A 1 386 ? -25.406 -40.465 -37.007 1.00 189.79 ? 406 LYS   A CE  1 
ATOM   2709 N  NZ  . LYS   A 1 386 ? -25.955 -41.804 -37.353 1.00 185.13 ? 406 LYS   A NZ  1 
ATOM   2710 N  N   . TYR   A 1 387 ? -27.416 -34.225 -33.729 1.00 163.49 ? 407 TYR   A N   1 
ATOM   2711 C  CA  . TYR   A 1 387 ? -28.329 -33.340 -33.011 1.00 164.59 ? 407 TYR   A CA  1 
ATOM   2712 C  C   . TYR   A 1 387 ? -28.101 -31.862 -33.292 1.00 164.92 ? 407 TYR   A C   1 
ATOM   2713 O  O   . TYR   A 1 387 ? -29.053 -31.083 -33.175 1.00 166.60 ? 407 TYR   A O   1 
ATOM   2714 C  CB  . TYR   A 1 387 ? -28.229 -33.565 -31.493 1.00 156.64 ? 407 TYR   A CB  1 
ATOM   2715 C  CG  . TYR   A 1 387 ? -29.095 -34.686 -30.962 1.00 169.54 ? 407 TYR   A CG  1 
ATOM   2716 C  CD1 . TYR   A 1 387 ? -30.425 -34.463 -30.630 1.00 172.81 ? 407 TYR   A CD1 1 
ATOM   2717 C  CD2 . TYR   A 1 387 ? -28.578 -35.962 -30.780 1.00 165.45 ? 407 TYR   A CD2 1 
ATOM   2718 C  CE1 . TYR   A 1 387 ? -31.219 -35.481 -30.143 1.00 181.54 ? 407 TYR   A CE1 1 
ATOM   2719 C  CE2 . TYR   A 1 387 ? -29.366 -36.988 -30.292 1.00 175.03 ? 407 TYR   A CE2 1 
ATOM   2720 C  CZ  . TYR   A 1 387 ? -30.686 -36.740 -29.975 1.00 181.99 ? 407 TYR   A CZ  1 
ATOM   2721 O  OH  . TYR   A 1 387 ? -31.483 -37.750 -29.489 1.00 192.77 ? 407 TYR   A OH  1 
ATOM   2722 N  N   . TRP   A 1 388 ? -26.890 -31.444 -33.658 1.00 149.64 ? 408 TRP   A N   1 
ATOM   2723 C  CA  . TRP   A 1 388 ? -26.538 -30.039 -33.815 1.00 141.52 ? 408 TRP   A CA  1 
ATOM   2724 C  C   . TRP   A 1 388 ? -26.027 -29.791 -35.227 1.00 142.86 ? 408 TRP   A C   1 
ATOM   2725 O  O   . TRP   A 1 388 ? -25.113 -30.482 -35.690 1.00 149.52 ? 408 TRP   A O   1 
ATOM   2726 C  CB  . TRP   A 1 388 ? -25.475 -29.629 -32.793 1.00 130.59 ? 408 TRP   A CB  1 
ATOM   2727 C  CG  . TRP   A 1 388 ? -25.837 -29.977 -31.384 1.00 117.99 ? 408 TRP   A CG  1 
ATOM   2728 C  CD1 . TRP   A 1 388 ? -25.420 -31.065 -30.674 1.00 103.17 ? 408 TRP   A CD1 1 
ATOM   2729 C  CD2 . TRP   A 1 388 ? -26.692 -29.231 -30.511 1.00 124.79 ? 408 TRP   A CD2 1 
ATOM   2730 N  NE1 . TRP   A 1 388 ? -25.962 -31.042 -29.412 1.00 101.99 ? 408 TRP   A NE1 1 
ATOM   2731 C  CE2 . TRP   A 1 388 ? -26.748 -29.926 -29.287 1.00 124.53 ? 408 TRP   A CE2 1 
ATOM   2732 C  CE3 . TRP   A 1 388 ? -27.417 -28.043 -30.646 1.00 115.40 ? 408 TRP   A CE3 1 
ATOM   2733 C  CZ2 . TRP   A 1 388 ? -27.498 -29.472 -28.205 1.00 106.01 ? 408 TRP   A CZ2 1 
ATOM   2734 C  CZ3 . TRP   A 1 388 ? -28.161 -27.594 -29.570 1.00 113.15 ? 408 TRP   A CZ3 1 
ATOM   2735 C  CH2 . TRP   A 1 388 ? -28.196 -28.307 -28.366 1.00 113.02 ? 408 TRP   A CH2 1 
ATOM   2736 N  N   . THR   A 1 389 ? -26.621 -28.809 -35.902 1.00 140.24 ? 409 THR   A N   1 
ATOM   2737 C  CA  . THR   A 1 389 ? -26.154 -28.390 -37.216 1.00 149.50 ? 409 THR   A CA  1 
ATOM   2738 C  C   . THR   A 1 389 ? -24.912 -27.520 -37.068 1.00 142.73 ? 409 THR   A C   1 
ATOM   2739 O  O   . THR   A 1 389 ? -24.937 -26.509 -36.358 1.00 136.64 ? 409 THR   A O   1 
ATOM   2740 C  CB  . THR   A 1 389 ? -27.252 -27.621 -37.953 1.00 150.27 ? 409 THR   A CB  1 
ATOM   2741 O  OG1 . THR   A 1 389 ? -27.564 -26.421 -37.234 1.00 144.55 ? 409 THR   A OG1 1 
ATOM   2742 C  CG2 . THR   A 1 389 ? -28.511 -28.469 -38.077 1.00 130.66 ? 409 THR   A CG2 1 
ATOM   2743 N  N   . GLU   A 1 390 ? -23.828 -27.912 -37.749 1.00 145.29 ? 410 GLU   A N   1 
ATOM   2744 C  CA  . GLU   A 1 390 ? -22.533 -27.247 -37.645 1.00 149.56 ? 410 GLU   A CA  1 
ATOM   2745 C  C   . GLU   A 1 390 ? -22.164 -27.090 -36.174 1.00 146.34 ? 410 GLU   A C   1 
ATOM   2746 O  O   . GLU   A 1 390 ? -22.198 -25.976 -35.636 1.00 139.64 ? 410 GLU   A O   1 
ATOM   2747 C  CB  . GLU   A 1 390 ? -22.559 -25.893 -38.358 1.00 156.27 ? 410 GLU   A CB  1 
ATOM   2748 C  CG  . GLU   A 1 390 ? -22.651 -25.999 -39.875 1.00 162.90 ? 410 GLU   A CG  1 
ATOM   2749 C  CD  . GLU   A 1 390 ? -22.737 -24.646 -40.557 1.00 168.69 ? 410 GLU   A CD  1 
ATOM   2750 O  OE1 . GLU   A 1 390 ? -23.453 -23.762 -40.042 1.00 164.86 ? 410 GLU   A OE1 1 
ATOM   2751 O  OE2 . GLU   A 1 390 ? -22.085 -24.466 -41.608 1.00 170.66 ? 410 GLU   A OE2 1 
ATOM   2752 N  N   . PRO   A 1 391 ? -21.801 -28.183 -35.496 1.00 151.42 ? 411 PRO   A N   1 
ATOM   2753 C  CA  . PRO   A 1 391 ? -21.733 -28.140 -34.026 1.00 143.17 ? 411 PRO   A CA  1 
ATOM   2754 C  C   . PRO   A 1 391 ? -20.598 -27.292 -33.479 1.00 137.99 ? 411 PRO   A C   1 
ATOM   2755 O  O   . PRO   A 1 391 ? -20.731 -26.750 -32.375 1.00 140.95 ? 411 PRO   A O   1 
ATOM   2756 C  CB  . PRO   A 1 391 ? -21.566 -29.617 -33.644 1.00 142.47 ? 411 PRO   A CB  1 
ATOM   2757 C  CG  . PRO   A 1 391 ? -20.913 -30.237 -34.835 1.00 150.65 ? 411 PRO   A CG  1 
ATOM   2758 C  CD  . PRO   A 1 391 ? -21.458 -29.511 -36.033 1.00 155.37 ? 411 PRO   A CD  1 
ATOM   2759 N  N   . GLU   A 1 392 ? -19.489 -27.156 -34.205 1.00 135.67 ? 412 GLU   A N   1 
ATOM   2760 C  CA  . GLU   A 1 392 ? -18.346 -26.414 -33.686 1.00 136.71 ? 412 GLU   A CA  1 
ATOM   2761 C  C   . GLU   A 1 392 ? -18.533 -24.904 -33.738 1.00 132.01 ? 412 GLU   A C   1 
ATOM   2762 O  O   . GLU   A 1 392 ? -17.688 -24.176 -33.206 1.00 127.37 ? 412 GLU   A O   1 
ATOM   2763 C  CB  . GLU   A 1 392 ? -17.073 -26.791 -34.452 1.00 146.56 ? 412 GLU   A CB  1 
ATOM   2764 C  CG  . GLU   A 1 392 ? -16.548 -28.188 -34.154 1.00 148.20 ? 412 GLU   A CG  1 
ATOM   2765 C  CD  . GLU   A 1 392 ? -17.339 -29.275 -34.854 1.00 167.06 ? 412 GLU   A CD  1 
ATOM   2766 O  OE1 . GLU   A 1 392 ? -18.080 -28.951 -35.806 1.00 169.43 ? 412 GLU   A OE1 1 
ATOM   2767 O  OE2 . GLU   A 1 392 ? -17.220 -30.451 -34.452 1.00 167.15 ? 412 GLU   A OE2 1 
ATOM   2768 N  N   . LYS   A 1 393 ? -19.608 -24.416 -34.350 1.00 136.61 ? 413 LYS   A N   1 
ATOM   2769 C  CA  . LYS   A 1 393 ? -19.801 -22.985 -34.536 1.00 132.07 ? 413 LYS   A CA  1 
ATOM   2770 C  C   . LYS   A 1 393 ? -20.619 -22.396 -33.394 1.00 125.95 ? 413 LYS   A C   1 
ATOM   2771 O  O   . LYS   A 1 393 ? -21.584 -23.005 -32.922 1.00 122.89 ? 413 LYS   A O   1 
ATOM   2772 C  CB  . LYS   A 1 393 ? -20.490 -22.706 -35.872 1.00 124.51 ? 413 LYS   A CB  1 
ATOM   2773 C  CG  . LYS   A 1 393 ? -19.890 -23.472 -37.040 1.00 142.96 ? 413 LYS   A CG  1 
ATOM   2774 C  CD  . LYS   A 1 393 ? -20.267 -22.845 -38.371 1.00 151.00 ? 413 LYS   A CD  1 
ATOM   2775 C  CE  . LYS   A 1 393 ? -19.635 -21.471 -38.525 1.00 142.14 ? 413 LYS   A CE  1 
ATOM   2776 N  NZ  . LYS   A 1 393 ? -19.903 -20.881 -39.864 1.00 141.87 ? 413 LYS   A NZ  1 
ATOM   2777 N  N   . PHE   A 1 394 ? -20.223 -21.203 -32.955 1.00 119.06 ? 414 PHE   A N   1 
ATOM   2778 C  CA  . PHE   A 1 394 ? -20.924 -20.487 -31.894 1.00 118.63 ? 414 PHE   A CA  1 
ATOM   2779 C  C   . PHE   A 1 394 ? -22.167 -19.831 -32.483 1.00 127.33 ? 414 PHE   A C   1 
ATOM   2780 O  O   . PHE   A 1 394 ? -22.065 -18.874 -33.257 1.00 134.67 ? 414 PHE   A O   1 
ATOM   2781 C  CB  . PHE   A 1 394 ? -19.999 -19.455 -31.256 1.00 125.25 ? 414 PHE   A CB  1 
ATOM   2782 C  CG  . PHE   A 1 394 ? -20.657 -18.612 -30.201 1.00 111.44 ? 414 PHE   A CG  1 
ATOM   2783 C  CD1 . PHE   A 1 394 ? -20.825 -19.094 -28.913 1.00 104.39 ? 414 PHE   A CD1 1 
ATOM   2784 C  CD2 . PHE   A 1 394 ? -21.092 -17.329 -30.492 1.00 125.71 ? 414 PHE   A CD2 1 
ATOM   2785 C  CE1 . PHE   A 1 394 ? -21.425 -18.318 -27.939 1.00 109.92 ? 414 PHE   A CE1 1 
ATOM   2786 C  CE2 . PHE   A 1 394 ? -21.691 -16.548 -29.523 1.00 121.84 ? 414 PHE   A CE2 1 
ATOM   2787 C  CZ  . PHE   A 1 394 ? -21.859 -17.043 -28.245 1.00 108.01 ? 414 PHE   A CZ  1 
ATOM   2788 N  N   . LEU   A 1 395 ? -23.342 -20.345 -32.121 1.00 119.99 ? 415 LEU   A N   1 
ATOM   2789 C  CA  . LEU   A 1 395 ? -24.610 -19.855 -32.658 1.00 116.72 ? 415 LEU   A CA  1 
ATOM   2790 C  C   . LEU   A 1 395 ? -25.640 -19.804 -31.539 1.00 125.16 ? 415 LEU   A C   1 
ATOM   2791 O  O   . LEU   A 1 395 ? -26.301 -20.806 -31.236 1.00 130.46 ? 415 LEU   A O   1 
ATOM   2792 C  CB  . LEU   A 1 395 ? -25.098 -20.733 -33.811 1.00 111.32 ? 415 LEU   A CB  1 
ATOM   2793 C  CG  . LEU   A 1 395 ? -24.313 -20.639 -35.120 1.00 105.27 ? 415 LEU   A CG  1 
ATOM   2794 C  CD1 . LEU   A 1 395 ? -24.600 -21.837 -36.009 1.00 122.23 ? 415 LEU   A CD1 1 
ATOM   2795 C  CD2 . LEU   A 1 395 ? -24.650 -19.345 -35.843 1.00 116.34 ? 415 LEU   A CD2 1 
ATOM   2796 N  N   . PRO   A 1 396 ? -25.803 -18.645 -30.897 1.00 124.51 ? 416 PRO   A N   1 
ATOM   2797 C  CA  . PRO   A 1 396 ? -26.813 -18.534 -29.831 1.00 125.14 ? 416 PRO   A CA  1 
ATOM   2798 C  C   . PRO   A 1 396 ? -28.240 -18.698 -30.321 1.00 131.08 ? 416 PRO   A C   1 
ATOM   2799 O  O   . PRO   A 1 396 ? -29.136 -18.929 -29.499 1.00 133.16 ? 416 PRO   A O   1 
ATOM   2800 C  CB  . PRO   A 1 396 ? -26.577 -17.126 -29.265 1.00 122.23 ? 416 PRO   A CB  1 
ATOM   2801 C  CG  . PRO   A 1 396 ? -25.184 -16.776 -29.670 1.00 124.26 ? 416 PRO   A CG  1 
ATOM   2802 C  CD  . PRO   A 1 396 ? -24.974 -17.434 -31.000 1.00 126.10 ? 416 PRO   A CD  1 
ATOM   2803 N  N   . GLU   A 1 397 ? -28.484 -18.592 -31.630 1.00 128.11 ? 417 GLU   A N   1 
ATOM   2804 C  CA  . GLU   A 1 397 ? -29.831 -18.761 -32.164 1.00 132.90 ? 417 GLU   A CA  1 
ATOM   2805 C  C   . GLU   A 1 397 ? -30.363 -20.179 -32.000 1.00 132.30 ? 417 GLU   A C   1 
ATOM   2806 O  O   . GLU   A 1 397 ? -31.542 -20.413 -32.286 1.00 137.09 ? 417 GLU   A O   1 
ATOM   2807 C  CB  . GLU   A 1 397 ? -29.867 -18.362 -33.641 1.00 141.30 ? 417 GLU   A CB  1 
ATOM   2808 C  CG  . GLU   A 1 397 ? -29.936 -16.861 -33.875 1.00 152.23 ? 417 GLU   A CG  1 
ATOM   2809 C  CD  . GLU   A 1 397 ? -31.262 -16.262 -33.442 1.00 162.87 ? 417 GLU   A CD  1 
ATOM   2810 O  OE1 . GLU   A 1 397 ? -32.278 -16.990 -33.454 1.00 168.16 ? 417 GLU   A OE1 1 
ATOM   2811 O  OE2 . GLU   A 1 397 ? -31.289 -15.065 -33.086 1.00 160.89 ? 417 GLU   A OE2 1 
ATOM   2812 N  N   . ARG   A 1 398 ? -29.532 -21.127 -31.555 1.00 121.24 ? 418 ARG   A N   1 
ATOM   2813 C  CA  . ARG   A 1 398 ? -30.041 -22.455 -31.231 1.00 119.67 ? 418 ARG   A CA  1 
ATOM   2814 C  C   . ARG   A 1 398 ? -31.041 -22.402 -30.085 1.00 117.85 ? 418 ARG   A C   1 
ATOM   2815 O  O   . ARG   A 1 398 ? -31.931 -23.256 -29.997 1.00 130.60 ? 418 ARG   A O   1 
ATOM   2816 C  CB  . ARG   A 1 398 ? -28.894 -23.398 -30.863 1.00 124.58 ? 418 ARG   A CB  1 
ATOM   2817 C  CG  . ARG   A 1 398 ? -27.804 -23.557 -31.908 1.00 117.59 ? 418 ARG   A CG  1 
ATOM   2818 C  CD  . ARG   A 1 398 ? -26.776 -24.575 -31.429 1.00 104.51 ? 418 ARG   A CD  1 
ATOM   2819 N  NE  . ARG   A 1 398 ? -25.493 -24.452 -32.111 1.00 121.98 ? 418 ARG   A NE  1 
ATOM   2820 C  CZ  . ARG   A 1 398 ? -25.126 -25.176 -33.159 1.00 126.39 ? 418 ARG   A CZ  1 
ATOM   2821 N  NH1 . ARG   A 1 398 ? -25.931 -26.083 -33.689 1.00 129.00 ? 418 ARG   A NH1 1 
ATOM   2822 N  NH2 . ARG   A 1 398 ? -23.919 -24.988 -33.687 1.00 127.31 ? 418 ARG   A NH2 1 
ATOM   2823 N  N   . PHE   A 1 399 ? -30.913 -21.412 -29.199 1.00 114.38 ? 419 PHE   A N   1 
ATOM   2824 C  CA  . PHE   A 1 399 ? -31.710 -21.340 -27.981 1.00 122.82 ? 419 PHE   A CA  1 
ATOM   2825 C  C   . PHE   A 1 399 ? -32.750 -20.226 -28.020 1.00 119.26 ? 419 PHE   A C   1 
ATOM   2826 O  O   . PHE   A 1 399 ? -33.248 -19.812 -26.969 1.00 121.66 ? 419 PHE   A O   1 
ATOM   2827 C  CB  . PHE   A 1 399 ? -30.797 -21.175 -26.767 1.00 113.55 ? 419 PHE   A CB  1 
ATOM   2828 C  CG  . PHE   A 1 399 ? -29.883 -22.342 -26.542 1.00 111.43 ? 419 PHE   A CG  1 
ATOM   2829 C  CD1 . PHE   A 1 399 ? -30.328 -23.466 -25.867 1.00 118.82 ? 419 PHE   A CD1 1 
ATOM   2830 C  CD2 . PHE   A 1 399 ? -28.582 -22.321 -27.013 1.00 120.19 ? 419 PHE   A CD2 1 
ATOM   2831 C  CE1 . PHE   A 1 399 ? -29.492 -24.545 -25.662 1.00 119.85 ? 419 PHE   A CE1 1 
ATOM   2832 C  CE2 . PHE   A 1 399 ? -27.741 -23.398 -26.812 1.00 116.80 ? 419 PHE   A CE2 1 
ATOM   2833 C  CZ  . PHE   A 1 399 ? -28.196 -24.511 -26.134 1.00 105.31 ? 419 PHE   A CZ  1 
ATOM   2834 N  N   . SER   A 1 400 ? -33.086 -19.730 -29.207 1.00 137.39 ? 420 SER   A N   1 
ATOM   2835 C  CA  . SER   A 1 400 ? -34.216 -18.825 -29.327 1.00 138.33 ? 420 SER   A CA  1 
ATOM   2836 C  C   . SER   A 1 400 ? -35.520 -19.600 -29.160 1.00 152.85 ? 420 SER   A C   1 
ATOM   2837 O  O   . SER   A 1 400 ? -35.588 -20.810 -29.396 1.00 147.28 ? 420 SER   A O   1 
ATOM   2838 C  CB  . SER   A 1 400 ? -34.196 -18.109 -30.678 1.00 141.40 ? 420 SER   A CB  1 
ATOM   2839 O  OG  . SER   A 1 400 ? -34.326 -19.029 -31.748 1.00 131.01 ? 420 SER   A OG  1 
ATOM   2840 N  N   . LYS   A 1 401 ? -36.569 -18.886 -28.747 1.00 160.29 ? 421 LYS   A N   1 
ATOM   2841 C  CA  . LYS   A 1 401 ? -37.867 -19.525 -28.555 1.00 164.57 ? 421 LYS   A CA  1 
ATOM   2842 C  C   . LYS   A 1 401 ? -38.453 -20.060 -29.856 1.00 163.79 ? 421 LYS   A C   1 
ATOM   2843 O  O   . LYS   A 1 401 ? -39.456 -20.781 -29.814 1.00 167.26 ? 421 LYS   A O   1 
ATOM   2844 C  CB  . LYS   A 1 401 ? -38.840 -18.548 -27.893 1.00 166.81 ? 421 LYS   A CB  1 
ATOM   2845 C  CG  . LYS   A 1 401 ? -39.252 -18.971 -26.490 1.00 173.40 ? 421 LYS   A CG  1 
ATOM   2846 C  CD  . LYS   A 1 401 ? -39.407 -17.780 -25.559 1.00 175.84 ? 421 LYS   A CD  1 
ATOM   2847 C  CE  . LYS   A 1 401 ? -40.566 -16.893 -25.972 1.00 172.16 ? 421 LYS   A CE  1 
ATOM   2848 N  NZ  . LYS   A 1 401 ? -40.772 -15.785 -25.000 1.00 166.75 ? 421 LYS   A NZ  1 
ATOM   2849 N  N   . LYS   A 1 402 ? -37.855 -19.726 -31.001 1.00 150.58 ? 422 LYS   A N   1 
ATOM   2850 C  CA  . LYS   A 1 402 ? -38.222 -20.350 -32.264 1.00 147.56 ? 422 LYS   A CA  1 
ATOM   2851 C  C   . LYS   A 1 402 ? -37.552 -21.709 -32.438 1.00 146.57 ? 422 LYS   A C   1 
ATOM   2852 O  O   . LYS   A 1 402 ? -38.088 -22.576 -33.140 1.00 149.02 ? 422 LYS   A O   1 
ATOM   2853 C  CB  . LYS   A 1 402 ? -37.853 -19.420 -33.424 1.00 150.56 ? 422 LYS   A CB  1 
ATOM   2854 C  CG  . LYS   A 1 402 ? -38.072 -19.995 -34.816 1.00 155.90 ? 422 LYS   A CG  1 
ATOM   2855 C  CD  . LYS   A 1 402 ? -37.621 -19.016 -35.887 1.00 164.97 ? 422 LYS   A CD  1 
ATOM   2856 C  CE  . LYS   A 1 402 ? -37.405 -19.716 -37.217 1.00 172.40 ? 422 LYS   A CE  1 
ATOM   2857 N  NZ  . LYS   A 1 402 ? -36.329 -20.742 -37.120 1.00 157.93 ? 422 LYS   A NZ  1 
ATOM   2858 N  N   . ASN   A 1 403 ? -36.397 -21.923 -31.798 1.00 156.70 ? 423 ASN   A N   1 
ATOM   2859 C  CA  . ASN   A 1 403 ? -35.641 -23.157 -31.956 1.00 150.31 ? 423 ASN   A CA  1 
ATOM   2860 C  C   . ASN   A 1 403 ? -35.365 -23.901 -30.656 1.00 146.94 ? 423 ASN   A C   1 
ATOM   2861 O  O   . ASN   A 1 403 ? -34.867 -25.031 -30.714 1.00 153.89 ? 423 ASN   A O   1 
ATOM   2862 C  CB  . ASN   A 1 403 ? -34.297 -22.875 -32.648 1.00 133.11 ? 423 ASN   A CB  1 
ATOM   2863 C  CG  . ASN   A 1 403 ? -34.465 -22.282 -34.032 1.00 147.62 ? 423 ASN   A CG  1 
ATOM   2864 O  OD1 . ASN   A 1 403 ? -35.520 -22.404 -34.652 1.00 160.41 ? 423 ASN   A OD1 1 
ATOM   2865 N  ND2 . ASN   A 1 403 ? -33.413 -21.642 -34.529 1.00 134.23 ? 423 ASN   A ND2 1 
ATOM   2866 N  N   . LYS   A 1 404 ? -35.670 -23.318 -29.493 1.00 134.77 ? 424 LYS   A N   1 
ATOM   2867 C  CA  . LYS   A 1 404 ? -35.339 -23.965 -28.226 1.00 138.25 ? 424 LYS   A CA  1 
ATOM   2868 C  C   . LYS   A 1 404 ? -36.121 -25.249 -27.986 1.00 150.20 ? 424 LYS   A C   1 
ATOM   2869 O  O   . LYS   A 1 404 ? -35.816 -25.969 -27.029 1.00 144.17 ? 424 LYS   A O   1 
ATOM   2870 C  CB  . LYS   A 1 404 ? -35.578 -23.010 -27.055 1.00 148.36 ? 424 LYS   A CB  1 
ATOM   2871 C  CG  . LYS   A 1 404 ? -37.040 -22.670 -26.818 1.00 163.02 ? 424 LYS   A CG  1 
ATOM   2872 C  CD  . LYS   A 1 404 ? -37.292 -22.284 -25.368 1.00 165.10 ? 424 LYS   A CD  1 
ATOM   2873 C  CE  . LYS   A 1 404 ? -36.401 -21.133 -24.931 1.00 171.12 ? 424 LYS   A CE  1 
ATOM   2874 N  NZ  . LYS   A 1 404 ? -36.619 -20.779 -23.500 1.00 188.61 ? 424 LYS   A NZ  1 
ATOM   2875 N  N   . ASP   A 1 405 ? -37.114 -25.552 -28.819 1.00 158.54 ? 425 ASP   A N   1 
ATOM   2876 C  CA  . ASP   A 1 405 ? -37.924 -26.750 -28.642 1.00 155.16 ? 425 ASP   A CA  1 
ATOM   2877 C  C   . ASP   A 1 405 ? -37.416 -27.976 -29.387 1.00 154.93 ? 425 ASP   A C   1 
ATOM   2878 O  O   . ASP   A 1 405 ? -37.860 -29.094 -29.097 1.00 154.08 ? 425 ASP   A O   1 
ATOM   2879 C  CB  . ASP   A 1 405 ? -39.321 -26.522 -29.222 1.00 163.86 ? 425 ASP   A CB  1 
ATOM   2880 C  CG  . ASP   A 1 405 ? -39.649 -25.051 -29.381 1.00 167.60 ? 425 ASP   A CG  1 
ATOM   2881 O  OD1 . ASP   A 1 405 ? -39.607 -24.316 -28.371 1.00 167.87 ? 425 ASP   A OD1 1 
ATOM   2882 O  OD2 . ASP   A 1 405 ? -39.931 -24.625 -30.520 1.00 163.48 ? 425 ASP   A OD2 1 
ATOM   2883 N  N   . ASN   A 1 406 ? -36.496 -27.792 -30.335 1.00 190.71 ? 426 ASN   A N   1 
ATOM   2884 C  CA  . ASN   A 1 406 ? -35.904 -28.902 -31.070 1.00 191.33 ? 426 ASN   A CA  1 
ATOM   2885 C  C   . ASN   A 1 406 ? -34.637 -29.382 -30.380 1.00 188.82 ? 426 ASN   A C   1 
ATOM   2886 O  O   . ASN   A 1 406 ? -33.689 -29.828 -31.036 1.00 194.82 ? 426 ASN   A O   1 
ATOM   2887 C  CB  . ASN   A 1 406 ? -35.588 -28.491 -32.510 1.00 197.14 ? 426 ASN   A CB  1 
ATOM   2888 C  CG  . ASN   A 1 406 ? -36.582 -27.490 -33.063 1.00 203.42 ? 426 ASN   A CG  1 
ATOM   2889 O  OD1 . ASN   A 1 406 ? -37.777 -27.557 -32.779 1.00 203.78 ? 426 ASN   A OD1 1 
ATOM   2890 N  ND2 . ASN   A 1 406 ? -36.087 -26.550 -33.861 1.00 208.04 ? 426 ASN   A ND2 1 
ATOM   2891 N  N   . ILE   A 1 407 ? -34.610 -29.285 -29.055 1.00 144.94 ? 427 ILE   A N   1 
ATOM   2892 C  CA  . ILE   A 1 407 ? -33.436 -29.608 -28.257 1.00 127.87 ? 427 ILE   A CA  1 
ATOM   2893 C  C   . ILE   A 1 407 ? -33.875 -30.525 -27.126 1.00 129.34 ? 427 ILE   A C   1 
ATOM   2894 O  O   . ILE   A 1 407 ? -34.716 -30.143 -26.303 1.00 126.50 ? 427 ILE   A O   1 
ATOM   2895 C  CB  . ILE   A 1 407 ? -32.756 -28.344 -27.705 1.00 128.68 ? 427 ILE   A CB  1 
ATOM   2896 C  CG1 . ILE   A 1 407 ? -32.109 -27.554 -28.843 1.00 130.97 ? 427 ILE   A CG1 1 
ATOM   2897 C  CG2 . ILE   A 1 407 ? -31.727 -28.711 -26.647 1.00 120.18 ? 427 ILE   A CG2 1 
ATOM   2898 C  CD1 . ILE   A 1 407 ? -31.526 -26.229 -28.413 1.00 128.84 ? 427 ILE   A CD1 1 
ATOM   2899 N  N   . ASP   A 1 408 ? -33.311 -31.726 -27.090 1.00 112.21 ? 428 ASP   A N   1 
ATOM   2900 C  CA  . ASP   A 1 408 ? -33.608 -32.687 -26.035 1.00 111.18 ? 428 ASP   A CA  1 
ATOM   2901 C  C   . ASP   A 1 408 ? -32.925 -32.274 -24.737 1.00 103.69 ? 428 ASP   A C   1 
ATOM   2902 O  O   . ASP   A 1 408 ? -31.691 -32.193 -24.693 1.00 103.53 ? 428 ASP   A O   1 
ATOM   2903 C  CB  . ASP   A 1 408 ? -33.145 -34.075 -26.450 1.00 117.75 ? 428 ASP   A CB  1 
ATOM   2904 C  CG  . ASP   A 1 408 ? -33.944 -35.188 -25.793 1.00 122.44 ? 428 ASP   A CG  1 
ATOM   2905 O  OD1 . ASP   A 1 408 ? -34.347 -35.045 -24.618 1.00 123.43 ? 428 ASP   A OD1 1 
ATOM   2906 O  OD2 . ASP   A 1 408 ? -34.168 -36.218 -26.463 1.00 116.33 ? 428 ASP   A OD2 1 
ATOM   2907 N  N   . PRO   A 1 409 ? -33.677 -32.023 -23.664 1.00 104.00 ? 429 PRO   A N   1 
ATOM   2908 C  CA  . PRO   A 1 409 ? -33.070 -31.693 -22.372 1.00 103.99 ? 429 PRO   A CA  1 
ATOM   2909 C  C   . PRO   A 1 409 ? -32.310 -32.839 -21.722 1.00 103.50 ? 429 PRO   A C   1 
ATOM   2910 O  O   . PRO   A 1 409 ? -31.867 -32.694 -20.580 1.00 96.08  ? 429 PRO   A O   1 
ATOM   2911 C  CB  . PRO   A 1 409 ? -34.289 -31.296 -21.527 1.00 118.35 ? 429 PRO   A CB  1 
ATOM   2912 C  CG  . PRO   A 1 409 ? -35.424 -32.076 -22.121 1.00 121.48 ? 429 PRO   A CG  1 
ATOM   2913 C  CD  . PRO   A 1 409 ? -35.146 -32.115 -23.594 1.00 120.79 ? 429 PRO   A CD  1 
ATOM   2914 N  N   . TYR   A 1 410 ? -32.157 -33.973 -22.406 1.00 104.86 ? 430 TYR   A N   1 
ATOM   2915 C  CA  . TYR   A 1 410 ? -31.297 -35.064 -21.959 1.00 104.24 ? 430 TYR   A CA  1 
ATOM   2916 C  C   . TYR   A 1 410 ? -30.118 -35.271 -22.900 1.00 112.33 ? 430 TYR   A C   1 
ATOM   2917 O  O   . TYR   A 1 410 ? -29.359 -36.231 -22.730 1.00 116.15 ? 430 TYR   A O   1 
ATOM   2918 C  CB  . TYR   A 1 410 ? -32.098 -36.362 -21.799 1.00 102.56 ? 430 TYR   A CB  1 
ATOM   2919 C  CG  . TYR   A 1 410 ? -33.155 -36.236 -20.725 1.00 114.30 ? 430 TYR   A CG  1 
ATOM   2920 C  CD1 . TYR   A 1 410 ? -32.825 -36.369 -19.383 1.00 112.08 ? 430 TYR   A CD1 1 
ATOM   2921 C  CD2 . TYR   A 1 410 ? -34.474 -35.946 -21.050 1.00 98.94  ? 430 TYR   A CD2 1 
ATOM   2922 C  CE1 . TYR   A 1 410 ? -33.777 -36.230 -18.396 1.00 112.30 ? 430 TYR   A CE1 1 
ATOM   2923 C  CE2 . TYR   A 1 410 ? -35.439 -35.806 -20.065 1.00 108.39 ? 430 TYR   A CE2 1 
ATOM   2924 C  CZ  . TYR   A 1 410 ? -35.080 -35.949 -18.738 1.00 118.39 ? 430 TYR   A CZ  1 
ATOM   2925 O  OH  . TYR   A 1 410 ? -36.014 -35.817 -17.735 1.00 138.86 ? 430 TYR   A OH  1 
ATOM   2926 N  N   . ILE   A 1 411 ? -29.970 -34.402 -23.896 1.00 109.01 ? 431 ILE   A N   1 
ATOM   2927 C  CA  . ILE   A 1 411 ? -28.737 -34.262 -24.654 1.00 104.91 ? 431 ILE   A CA  1 
ATOM   2928 C  C   . ILE   A 1 411 ? -27.971 -33.016 -24.229 1.00 111.60 ? 431 ILE   A C   1 
ATOM   2929 O  O   . ILE   A 1 411 ? -26.751 -33.058 -24.062 1.00 115.08 ? 431 ILE   A O   1 
ATOM   2930 C  CB  . ILE   A 1 411 ? -29.035 -34.237 -26.168 1.00 113.57 ? 431 ILE   A CB  1 
ATOM   2931 C  CG1 . ILE   A 1 411 ? -29.742 -35.523 -26.597 1.00 112.82 ? 431 ILE   A CG1 1 
ATOM   2932 C  CG2 . ILE   A 1 411 ? -27.753 -34.047 -26.960 1.00 116.07 ? 431 ILE   A CG2 1 
ATOM   2933 C  CD1 . ILE   A 1 411 ? -28.973 -36.775 -26.248 1.00 120.61 ? 431 ILE   A CD1 1 
ATOM   2934 N  N   . TYR   A 1 412 ? -28.677 -31.901 -24.045 1.00 97.98  ? 432 TYR   A N   1 
ATOM   2935 C  CA  . TYR   A 1 412 ? -28.085 -30.679 -23.504 1.00 107.25 ? 432 TYR   A CA  1 
ATOM   2936 C  C   . TYR   A 1 412 ? -28.304 -30.685 -21.997 1.00 101.71 ? 432 TYR   A C   1 
ATOM   2937 O  O   . TYR   A 1 412 ? -29.372 -30.305 -21.510 1.00 104.71 ? 432 TYR   A O   1 
ATOM   2938 C  CB  . TYR   A 1 412 ? -28.696 -29.442 -24.154 1.00 97.97  ? 432 TYR   A CB  1 
ATOM   2939 C  CG  . TYR   A 1 412 ? -28.143 -28.143 -23.615 1.00 90.08  ? 432 TYR   A CG  1 
ATOM   2940 C  CD1 . TYR   A 1 412 ? -26.864 -27.722 -23.952 1.00 99.32  ? 432 TYR   A CD1 1 
ATOM   2941 C  CD2 . TYR   A 1 412 ? -28.897 -27.338 -22.772 1.00 86.62  ? 432 TYR   A CD2 1 
ATOM   2942 C  CE1 . TYR   A 1 412 ? -26.350 -26.539 -23.463 1.00 97.65  ? 432 TYR   A CE1 1 
ATOM   2943 C  CE2 . TYR   A 1 412 ? -28.392 -26.149 -22.280 1.00 95.56  ? 432 TYR   A CE2 1 
ATOM   2944 C  CZ  . TYR   A 1 412 ? -27.117 -25.756 -22.629 1.00 94.34  ? 432 TYR   A CZ  1 
ATOM   2945 O  OH  . TYR   A 1 412 ? -26.604 -24.576 -22.143 1.00 100.44 ? 432 TYR   A OH  1 
ATOM   2946 N  N   . THR   A 1 413 ? -27.294 -31.130 -21.253 1.00 106.47 ? 433 THR   A N   1 
ATOM   2947 C  CA  . THR   A 1 413 ? -27.354 -31.214 -19.794 1.00 106.61 ? 433 THR   A CA  1 
ATOM   2948 C  C   . THR   A 1 413 ? -26.107 -30.574 -19.196 1.00 108.42 ? 433 THR   A C   1 
ATOM   2949 O  O   . THR   A 1 413 ? -25.225 -31.267 -18.675 1.00 111.78 ? 433 THR   A O   1 
ATOM   2950 C  CB  . THR   A 1 413 ? -27.489 -32.665 -19.329 1.00 111.35 ? 433 THR   A CB  1 
ATOM   2951 O  OG1 . THR   A 1 413 ? -26.408 -33.442 -19.861 1.00 116.14 ? 433 THR   A OG1 1 
ATOM   2952 C  CG2 . THR   A 1 413 ? -28.812 -33.257 -19.789 1.00 111.01 ? 433 THR   A CG2 1 
ATOM   2953 N  N   . PRO   A 1 414 ? -26.004 -29.242 -19.246 1.00 103.82 ? 434 PRO   A N   1 
ATOM   2954 C  CA  . PRO   A 1 414 ? -24.858 -28.572 -18.618 1.00 102.41 ? 434 PRO   A CA  1 
ATOM   2955 C  C   . PRO   A 1 414 ? -24.947 -28.500 -17.103 1.00 100.75 ? 434 PRO   A C   1 
ATOM   2956 O  O   . PRO   A 1 414 ? -23.930 -28.220 -16.454 1.00 103.10 ? 434 PRO   A O   1 
ATOM   2957 C  CB  . PRO   A 1 414 ? -24.900 -27.171 -19.237 1.00 84.88  ? 434 PRO   A CB  1 
ATOM   2958 C  CG  . PRO   A 1 414 ? -26.349 -26.936 -19.474 1.00 95.44  ? 434 PRO   A CG  1 
ATOM   2959 C  CD  . PRO   A 1 414 ? -26.939 -28.276 -19.851 1.00 100.27 ? 434 PRO   A CD  1 
ATOM   2960 N  N   . PHE   A 1 415 ? -26.125 -28.741 -16.524 1.00 95.21  ? 435 PHE   A N   1 
ATOM   2961 C  CA  . PHE   A 1 415 ? -26.313 -28.734 -15.077 1.00 102.74 ? 435 PHE   A CA  1 
ATOM   2962 C  C   . PHE   A 1 415 ? -26.786 -30.088 -14.561 1.00 96.58  ? 435 PHE   A C   1 
ATOM   2963 O  O   . PHE   A 1 415 ? -27.319 -30.174 -13.450 1.00 83.54  ? 435 PHE   A O   1 
ATOM   2964 C  CB  . PHE   A 1 415 ? -27.302 -27.641 -14.669 1.00 89.57  ? 435 PHE   A CB  1 
ATOM   2965 C  CG  . PHE   A 1 415 ? -26.808 -26.248 -14.925 1.00 94.16  ? 435 PHE   A CG  1 
ATOM   2966 C  CD1 . PHE   A 1 415 ? -26.004 -25.604 -14.000 1.00 99.98  ? 435 PHE   A CD1 1 
ATOM   2967 C  CD2 . PHE   A 1 415 ? -27.153 -25.578 -16.087 1.00 96.94  ? 435 PHE   A CD2 1 
ATOM   2968 C  CE1 . PHE   A 1 415 ? -25.549 -24.321 -14.229 1.00 94.11  ? 435 PHE   A CE1 1 
ATOM   2969 C  CE2 . PHE   A 1 415 ? -26.702 -24.295 -16.322 1.00 97.24  ? 435 PHE   A CE2 1 
ATOM   2970 C  CZ  . PHE   A 1 415 ? -25.898 -23.666 -15.392 1.00 91.68  ? 435 PHE   A CZ  1 
ATOM   2971 N  N   . GLY   A 1 416 ? -26.604 -31.146 -15.348 1.00 91.42  ? 436 GLY   A N   1 
ATOM   2972 C  CA  . GLY   A 1 416 ? -27.102 -32.454 -14.978 1.00 92.59  ? 436 GLY   A CA  1 
ATOM   2973 C  C   . GLY   A 1 416 ? -28.613 -32.547 -15.099 1.00 85.83  ? 436 GLY   A C   1 
ATOM   2974 O  O   . GLY   A 1 416 ? -29.266 -31.783 -15.820 1.00 99.50  ? 436 GLY   A O   1 
ATOM   2975 N  N   . SER   A 1 417 ? -29.173 -33.508 -14.370 1.00 91.61  ? 437 SER   A N   1 
ATOM   2976 C  CA  . SER   A 1 417 ? -30.614 -33.721 -14.348 1.00 93.90  ? 437 SER   A CA  1 
ATOM   2977 C  C   . SER   A 1 417 ? -30.953 -34.623 -13.172 1.00 82.81  ? 437 SER   A C   1 
ATOM   2978 O  O   . SER   A 1 417 ? -30.079 -35.280 -12.598 1.00 87.06  ? 437 SER   A O   1 
ATOM   2979 C  CB  . SER   A 1 417 ? -31.118 -34.337 -15.658 1.00 97.36  ? 437 SER   A CB  1 
ATOM   2980 O  OG  . SER   A 1 417 ? -31.941 -33.427 -16.367 1.00 101.77 ? 437 SER   A OG  1 
ATOM   2981 N  N   . GLY   A 1 418 ? -32.235 -34.646 -12.823 1.00 90.76  ? 438 GLY   A N   1 
ATOM   2982 C  CA  . GLY   A 1 418 ? -32.715 -35.487 -11.754 1.00 85.15  ? 438 GLY   A CA  1 
ATOM   2983 C  C   . GLY   A 1 418 ? -32.437 -34.903 -10.385 1.00 89.05  ? 438 GLY   A C   1 
ATOM   2984 O  O   . GLY   A 1 418 ? -32.026 -33.747 -10.244 1.00 73.10  ? 438 GLY   A O   1 
ATOM   2985 N  N   . PRO   A 1 419 ? -32.659 -35.706 -9.339  1.00 93.62  ? 439 PRO   A N   1 
ATOM   2986 C  CA  . PRO   A 1 419 ? -32.481 -35.204 -7.966  1.00 102.00 ? 439 PRO   A CA  1 
ATOM   2987 C  C   . PRO   A 1 419 ? -31.046 -34.850 -7.612  1.00 99.42  ? 439 PRO   A C   1 
ATOM   2988 O  O   . PRO   A 1 419 ? -30.831 -34.197 -6.582  1.00 101.31 ? 439 PRO   A O   1 
ATOM   2989 C  CB  . PRO   A 1 419 ? -32.988 -36.365 -7.098  1.00 90.66  ? 439 PRO   A CB  1 
ATOM   2990 C  CG  . PRO   A 1 419 ? -33.833 -37.199 -8.015  1.00 96.78  ? 439 PRO   A CG  1 
ATOM   2991 C  CD  . PRO   A 1 419 ? -33.210 -37.070 -9.365  1.00 94.73  ? 439 PRO   A CD  1 
ATOM   2992 N  N   . ARG   A 1 420 ? -30.061 -35.253 -8.416  1.00 95.13  ? 440 ARG   A N   1 
ATOM   2993 C  CA  . ARG   A 1 420 ? -28.658 -34.988 -8.125  1.00 93.69  ? 440 ARG   A CA  1 
ATOM   2994 C  C   . ARG   A 1 420 ? -28.054 -33.952 -9.073  1.00 87.01  ? 440 ARG   A C   1 
ATOM   2995 O  O   . ARG   A 1 420 ? -26.828 -33.868 -9.199  1.00 99.71  ? 440 ARG   A O   1 
ATOM   2996 C  CB  . ARG   A 1 420 ? -27.857 -36.292 -8.168  1.00 84.41  ? 440 ARG   A CB  1 
ATOM   2997 C  CG  . ARG   A 1 420 ? -26.540 -36.249 -7.402  1.00 92.89  ? 440 ARG   A CG  1 
ATOM   2998 C  CD  . ARG   A 1 420 ? -26.472 -37.315 -6.327  1.00 86.05  ? 440 ARG   A CD  1 
ATOM   2999 N  NE  . ARG   A 1 420 ? -25.307 -37.134 -5.470  1.00 77.34  ? 440 ARG   A NE  1 
ATOM   3000 C  CZ  . ARG   A 1 420 ? -24.968 -37.950 -4.482  1.00 83.02  ? 440 ARG   A CZ  1 
ATOM   3001 N  NH1 . ARG   A 1 420 ? -25.681 -39.028 -4.201  1.00 98.21  ? 440 ARG   A NH1 1 
ATOM   3002 N  NH2 . ARG   A 1 420 ? -23.887 -37.677 -3.757  1.00 78.25  ? 440 ARG   A NH2 1 
ATOM   3003 N  N   . ASN   A 1 421 ? -28.886 -33.151 -9.734  1.00 87.60  ? 441 ASN   A N   1 
ATOM   3004 C  CA  . ASN   A 1 421 ? -28.371 -32.139 -10.644 1.00 87.13  ? 441 ASN   A CA  1 
ATOM   3005 C  C   . ASN   A 1 421 ? -27.671 -31.031 -9.854  1.00 92.69  ? 441 ASN   A C   1 
ATOM   3006 O  O   . ASN   A 1 421 ? -27.603 -31.051 -8.621  1.00 86.91  ? 441 ASN   A O   1 
ATOM   3007 C  CB  . ASN   A 1 421 ? -29.497 -31.576 -11.511 1.00 86.57  ? 441 ASN   A CB  1 
ATOM   3008 C  CG  . ASN   A 1 421 ? -30.361 -30.566 -10.775 1.00 100.81 ? 441 ASN   A CG  1 
ATOM   3009 O  OD1 . ASN   A 1 421 ? -30.596 -30.684 -9.573  1.00 94.01  ? 441 ASN   A OD1 1 
ATOM   3010 N  ND2 . ASN   A 1 421 ? -30.841 -29.563 -11.503 1.00 106.05 ? 441 ASN   A ND2 1 
ATOM   3011 N  N   . CYS   A 1 422 ? -27.138 -30.049 -10.582 1.00 84.01  ? 442 CYS   A N   1 
ATOM   3012 C  CA  . CYS   A 1 422 ? -26.447 -28.925 -9.961  1.00 90.81  ? 442 CYS   A CA  1 
ATOM   3013 C  C   . CYS   A 1 422 ? -27.379 -28.169 -9.023  1.00 95.37  ? 442 CYS   A C   1 
ATOM   3014 O  O   . CYS   A 1 422 ? -28.352 -27.553 -9.468  1.00 93.54  ? 442 CYS   A O   1 
ATOM   3015 C  CB  . CYS   A 1 422 ? -25.888 -27.981 -11.027 1.00 103.16 ? 442 CYS   A CB  1 
ATOM   3016 S  SG  . CYS   A 1 422 ? -24.995 -26.555 -10.364 1.00 97.14  ? 442 CYS   A SG  1 
ATOM   3017 N  N   . ILE   A 1 423 ? -27.086 -28.210 -7.720  1.00 94.05  ? 443 ILE   A N   1 
ATOM   3018 C  CA  . ILE   A 1 423 ? -27.969 -27.579 -6.744  1.00 101.67 ? 443 ILE   A CA  1 
ATOM   3019 C  C   . ILE   A 1 423 ? -27.917 -26.061 -6.865  1.00 107.73 ? 443 ILE   A C   1 
ATOM   3020 O  O   . ILE   A 1 423 ? -28.890 -25.372 -6.532  1.00 126.03 ? 443 ILE   A O   1 
ATOM   3021 C  CB  . ILE   A 1 423 ? -27.614 -28.049 -5.320  1.00 97.38  ? 443 ILE   A CB  1 
ATOM   3022 C  CG1 . ILE   A 1 423 ? -28.745 -27.716 -4.345  1.00 118.90 ? 443 ILE   A CG1 1 
ATOM   3023 C  CG2 . ILE   A 1 423 ? -26.314 -27.418 -4.848  1.00 100.49 ? 443 ILE   A CG2 1 
ATOM   3024 C  CD1 . ILE   A 1 423 ? -28.450 -28.110 -2.913  1.00 106.35 ? 443 ILE   A CD1 1 
ATOM   3025 N  N   . GLY   A 1 424 ? -26.804 -25.514 -7.350  1.00 109.48 ? 444 GLY   A N   1 
ATOM   3026 C  CA  . GLY   A 1 424 ? -26.668 -24.078 -7.492  1.00 115.20 ? 444 GLY   A CA  1 
ATOM   3027 C  C   . GLY   A 1 424 ? -26.810 -23.612 -8.926  1.00 109.29 ? 444 GLY   A C   1 
ATOM   3028 O  O   . GLY   A 1 424 ? -26.158 -22.650 -9.342  1.00 102.65 ? 444 GLY   A O   1 
ATOM   3029 N  N   . MET   A 1 425 ? -27.666 -24.294 -9.691  1.00 115.78 ? 445 MET   A N   1 
ATOM   3030 C  CA  . MET   A 1 425 ? -27.865 -23.933 -11.091 1.00 100.47 ? 445 MET   A CA  1 
ATOM   3031 C  C   . MET   A 1 425 ? -28.488 -22.548 -11.221 1.00 104.54 ? 445 MET   A C   1 
ATOM   3032 O  O   . MET   A 1 425 ? -28.027 -21.719 -12.014 1.00 116.17 ? 445 MET   A O   1 
ATOM   3033 C  CB  . MET   A 1 425 ? -28.738 -24.983 -11.780 1.00 95.61  ? 445 MET   A CB  1 
ATOM   3034 C  CG  . MET   A 1 425 ? -29.354 -24.517 -13.090 1.00 100.44 ? 445 MET   A CG  1 
ATOM   3035 S  SD  . MET   A 1 425 ? -30.313 -25.805 -13.910 1.00 112.21 ? 445 MET   A SD  1 
ATOM   3036 C  CE  . MET   A 1 425 ? -31.408 -26.313 -12.587 1.00 111.41 ? 445 MET   A CE  1 
ATOM   3037 N  N   . ARG   A 1 426 ? -29.538 -22.278 -10.442 1.00 107.48 ? 446 ARG   A N   1 
ATOM   3038 C  CA  . ARG   A 1 426 ? -30.239 -21.004 -10.563 1.00 108.14 ? 446 ARG   A CA  1 
ATOM   3039 C  C   . ARG   A 1 426 ? -29.401 -19.844 -10.036 1.00 118.52 ? 446 ARG   A C   1 
ATOM   3040 O  O   . ARG   A 1 426 ? -29.526 -18.719 -10.532 1.00 122.30 ? 446 ARG   A O   1 
ATOM   3041 C  CB  . ARG   A 1 426 ? -31.583 -21.083 -9.837  1.00 106.67 ? 446 ARG   A CB  1 
ATOM   3042 C  CG  . ARG   A 1 426 ? -32.462 -22.223 -10.337 1.00 112.70 ? 446 ARG   A CG  1 
ATOM   3043 C  CD  . ARG   A 1 426 ? -33.683 -22.461 -9.458  1.00 125.20 ? 446 ARG   A CD  1 
ATOM   3044 N  NE  . ARG   A 1 426 ? -34.821 -21.632 -9.840  1.00 144.70 ? 446 ARG   A NE  1 
ATOM   3045 C  CZ  . ARG   A 1 426 ? -35.318 -20.652 -9.098  1.00 145.89 ? 446 ARG   A CZ  1 
ATOM   3046 N  NH1 . ARG   A 1 426 ? -34.804 -20.349 -7.918  1.00 144.70 ? 446 ARG   A NH1 1 
ATOM   3047 N  NH2 . ARG   A 1 426 ? -36.364 -19.964 -9.549  1.00 146.23 ? 446 ARG   A NH2 1 
ATOM   3048 N  N   . PHE   A 1 427 ? -28.543 -20.094 -9.045  1.00 118.12 ? 447 PHE   A N   1 
ATOM   3049 C  CA  . PHE   A 1 427 ? -27.653 -19.042 -8.563  1.00 115.03 ? 447 PHE   A CA  1 
ATOM   3050 C  C   . PHE   A 1 427 ? -26.563 -18.732 -9.582  1.00 113.16 ? 447 PHE   A C   1 
ATOM   3051 O  O   . PHE   A 1 427 ? -26.241 -17.562 -9.818  1.00 117.03 ? 447 PHE   A O   1 
ATOM   3052 C  CB  . PHE   A 1 427 ? -27.033 -19.444 -7.224  1.00 113.79 ? 447 PHE   A CB  1 
ATOM   3053 C  CG  . PHE   A 1 427 ? -25.852 -18.600 -6.823  1.00 117.61 ? 447 PHE   A CG  1 
ATOM   3054 C  CD1 . PHE   A 1 427 ? -26.036 -17.374 -6.205  1.00 117.25 ? 447 PHE   A CD1 1 
ATOM   3055 C  CD2 . PHE   A 1 427 ? -24.557 -19.037 -7.059  1.00 128.51 ? 447 PHE   A CD2 1 
ATOM   3056 C  CE1 . PHE   A 1 427 ? -24.952 -16.598 -5.836  1.00 132.51 ? 447 PHE   A CE1 1 
ATOM   3057 C  CE2 . PHE   A 1 427 ? -23.470 -18.266 -6.694  1.00 127.66 ? 447 PHE   A CE2 1 
ATOM   3058 C  CZ  . PHE   A 1 427 ? -23.668 -17.045 -6.080  1.00 135.47 ? 447 PHE   A CZ  1 
ATOM   3059 N  N   . ALA   A 1 428 ? -25.980 -19.769 -10.191 1.00 118.25 ? 448 ALA   A N   1 
ATOM   3060 C  CA  . ALA   A 1 428 ? -24.885 -19.558 -11.131 1.00 115.80 ? 448 ALA   A CA  1 
ATOM   3061 C  C   . ALA   A 1 428 ? -25.348 -18.781 -12.357 1.00 104.09 ? 448 ALA   A C   1 
ATOM   3062 O  O   . ALA   A 1 428 ? -24.633 -17.899 -12.848 1.00 108.24 ? 448 ALA   A O   1 
ATOM   3063 C  CB  . ALA   A 1 428 ? -24.279 -20.899 -11.541 1.00 101.81 ? 448 ALA   A CB  1 
ATOM   3064 N  N   . LEU   A 1 429 ? -26.541 -19.094 -12.867 1.00 103.55 ? 449 LEU   A N   1 
ATOM   3065 C  CA  . LEU   A 1 429 ? -27.092 -18.326 -13.978 1.00 105.35 ? 449 LEU   A CA  1 
ATOM   3066 C  C   . LEU   A 1 429 ? -27.341 -16.879 -13.574 1.00 120.73 ? 449 LEU   A C   1 
ATOM   3067 O  O   . LEU   A 1 429 ? -27.078 -15.955 -14.352 1.00 126.46 ? 449 LEU   A O   1 
ATOM   3068 C  CB  . LEU   A 1 429 ? -28.386 -18.974 -14.473 1.00 100.59 ? 449 LEU   A CB  1 
ATOM   3069 C  CG  . LEU   A 1 429 ? -28.258 -20.333 -15.163 1.00 110.05 ? 449 LEU   A CG  1 
ATOM   3070 C  CD1 . LEU   A 1 429 ? -29.620 -20.992 -15.293 1.00 115.43 ? 449 LEU   A CD1 1 
ATOM   3071 C  CD2 . LEU   A 1 429 ? -27.608 -20.176 -16.528 1.00 96.84  ? 449 LEU   A CD2 1 
ATOM   3072 N  N   . MET   A 1 430 ? -27.841 -16.664 -12.356 1.00 120.22 ? 450 MET   A N   1 
ATOM   3073 C  CA  A MET   A 1 430 ? -28.104 -15.304 -11.897 0.43 112.55 ? 450 MET   A CA  1 
ATOM   3074 C  CA  B MET   A 1 430 ? -28.103 -15.306 -11.891 0.57 115.55 ? 450 MET   A CA  1 
ATOM   3075 C  C   . MET   A 1 430 ? -26.808 -14.549 -11.624 1.00 114.84 ? 450 MET   A C   1 
ATOM   3076 O  O   . MET   A 1 430 ? -26.684 -13.372 -11.983 1.00 125.27 ? 450 MET   A O   1 
ATOM   3077 C  CB  A MET   A 1 430 ? -28.984 -15.334 -10.648 0.43 116.92 ? 450 MET   A CB  1 
ATOM   3078 C  CB  B MET   A 1 430 ? -28.971 -15.346 -10.634 0.57 116.79 ? 450 MET   A CB  1 
ATOM   3079 C  CG  A MET   A 1 430 ? -29.310 -13.961 -10.082 0.43 117.80 ? 450 MET   A CG  1 
ATOM   3080 C  CG  B MET   A 1 430 ? -28.975 -14.054 -9.837  0.57 118.45 ? 450 MET   A CG  1 
ATOM   3081 S  SD  A MET   A 1 430 ? -30.165 -12.903 -11.265 0.43 112.22 ? 450 MET   A SD  1 
ATOM   3082 S  SD  B MET   A 1 430 ? -30.637 -13.600 -9.325  0.57 118.90 ? 450 MET   A SD  1 
ATOM   3083 C  CE  A MET   A 1 430 ? -31.627 -13.881 -11.602 0.43 123.63 ? 450 MET   A CE  1 
ATOM   3084 C  CE  B MET   A 1 430 ? -31.426 -13.450 -10.926 0.57 125.27 ? 450 MET   A CE  1 
ATOM   3085 N  N   . ASN   A 1 431 ? -25.833 -15.209 -10.995 1.00 114.27 ? 451 ASN   A N   1 
ATOM   3086 C  CA  . ASN   A 1 431 ? -24.573 -14.544 -10.681 1.00 119.41 ? 451 ASN   A CA  1 
ATOM   3087 C  C   . ASN   A 1 431 ? -23.826 -14.142 -11.947 1.00 122.04 ? 451 ASN   A C   1 
ATOM   3088 O  O   . ASN   A 1 431 ? -23.243 -13.054 -12.013 1.00 112.68 ? 451 ASN   A O   1 
ATOM   3089 C  CB  . ASN   A 1 431 ? -23.705 -15.454 -9.812  1.00 117.31 ? 451 ASN   A CB  1 
ATOM   3090 C  CG  . ASN   A 1 431 ? -22.466 -14.754 -9.294  1.00 125.89 ? 451 ASN   A CG  1 
ATOM   3091 O  OD1 . ASN   A 1 431 ? -22.474 -13.545 -9.064  1.00 136.69 ? 451 ASN   A OD1 1 
ATOM   3092 N  ND2 . ASN   A 1 431 ? -21.392 -15.512 -9.109  1.00 128.10 ? 451 ASN   A ND2 1 
ATOM   3093 N  N   . MET   A 1 432 ? -23.835 -15.006 -12.964 1.00 116.49 ? 452 MET   A N   1 
ATOM   3094 C  CA  . MET   A 1 432 ? -23.135 -14.690 -14.205 1.00 112.64 ? 452 MET   A CA  1 
ATOM   3095 C  C   . MET   A 1 432 ? -23.849 -13.593 -14.984 1.00 112.34 ? 452 MET   A C   1 
ATOM   3096 O  O   . MET   A 1 432 ? -23.203 -12.687 -15.523 1.00 119.15 ? 452 MET   A O   1 
ATOM   3097 C  CB  . MET   A 1 432 ? -22.988 -15.945 -15.065 1.00 107.97 ? 452 MET   A CB  1 
ATOM   3098 C  CG  . MET   A 1 432 ? -21.999 -16.962 -14.523 1.00 111.39 ? 452 MET   A CG  1 
ATOM   3099 S  SD  . MET   A 1 432 ? -21.737 -18.343 -15.654 1.00 112.23 ? 452 MET   A SD  1 
ATOM   3100 C  CE  . MET   A 1 432 ? -23.384 -19.043 -15.728 1.00 107.53 ? 452 MET   A CE  1 
ATOM   3101 N  N   . LYS   A 1 433 ? -25.181 -13.657 -15.057 1.00 121.20 ? 453 LYS   A N   1 
ATOM   3102 C  CA  . LYS   A 1 433 ? -25.925 -12.673 -15.838 1.00 127.47 ? 453 LYS   A CA  1 
ATOM   3103 C  C   . LYS   A 1 433 ? -25.832 -11.284 -15.217 1.00 127.32 ? 453 LYS   A C   1 
ATOM   3104 O  O   . LYS   A 1 433 ? -25.751 -10.283 -15.937 1.00 117.45 ? 453 LYS   A O   1 
ATOM   3105 C  CB  . LYS   A 1 433 ? -27.382 -13.110 -15.985 1.00 121.81 ? 453 LYS   A CB  1 
ATOM   3106 C  CG  . LYS   A 1 433 ? -27.580 -14.233 -16.993 1.00 112.66 ? 453 LYS   A CG  1 
ATOM   3107 C  CD  . LYS   A 1 433 ? -28.997 -14.779 -16.961 1.00 112.83 ? 453 LYS   A CD  1 
ATOM   3108 C  CE  . LYS   A 1 433 ? -29.163 -15.918 -17.955 1.00 104.10 ? 453 LYS   A CE  1 
ATOM   3109 N  NZ  . LYS   A 1 433 ? -30.483 -16.593 -17.819 1.00 107.65 ? 453 LYS   A NZ  1 
ATOM   3110 N  N   . LEU   A 1 434 ? -25.840 -11.201 -13.884 1.00 121.95 ? 454 LEU   A N   1 
ATOM   3111 C  CA  . LEU   A 1 434 ? -25.612 -9.915  -13.232 1.00 127.62 ? 454 LEU   A CA  1 
ATOM   3112 C  C   . LEU   A 1 434 ? -24.220 -9.378  -13.537 1.00 129.44 ? 454 LEU   A C   1 
ATOM   3113 O  O   . LEU   A 1 434 ? -24.024 -8.159  -13.598 1.00 132.93 ? 454 LEU   A O   1 
ATOM   3114 C  CB  . LEU   A 1 434 ? -25.811 -10.044 -11.721 1.00 121.03 ? 454 LEU   A CB  1 
ATOM   3115 C  CG  . LEU   A 1 434 ? -27.250 -10.128 -11.210 1.00 123.31 ? 454 LEU   A CG  1 
ATOM   3116 C  CD1 . LEU   A 1 434 ? -27.265 -10.412 -9.718  1.00 131.71 ? 454 LEU   A CD1 1 
ATOM   3117 C  CD2 . LEU   A 1 434 ? -28.000 -8.842  -11.515 1.00 106.26 ? 454 LEU   A CD2 1 
ATOM   3118 N  N   . ALA   A 1 435 ? -23.246 -10.268 -13.738 1.00 119.70 ? 455 ALA   A N   1 
ATOM   3119 C  CA  . ALA   A 1 435 ? -21.896 -9.836  -14.081 1.00 115.98 ? 455 ALA   A CA  1 
ATOM   3120 C  C   . ALA   A 1 435 ? -21.787 -9.451  -15.551 1.00 125.87 ? 455 ALA   A C   1 
ATOM   3121 O  O   . ALA   A 1 435 ? -21.091 -8.489  -15.892 1.00 133.53 ? 455 ALA   A O   1 
ATOM   3122 C  CB  . ALA   A 1 435 ? -20.891 -10.938 -13.745 1.00 122.89 ? 455 ALA   A CB  1 
ATOM   3123 N  N   . LEU   A 1 436 ? -22.463 -10.191 -16.433 1.00 119.11 ? 456 LEU   A N   1 
ATOM   3124 C  CA  . LEU   A 1 436 ? -22.412 -9.871  -17.856 1.00 124.19 ? 456 LEU   A CA  1 
ATOM   3125 C  C   . LEU   A 1 436 ? -23.127 -8.560  -18.156 1.00 132.66 ? 456 LEU   A C   1 
ATOM   3126 O  O   . LEU   A 1 436 ? -22.704 -7.804  -19.037 1.00 127.62 ? 456 LEU   A O   1 
ATOM   3127 C  CB  . LEU   A 1 436 ? -23.018 -11.010 -18.675 1.00 131.29 ? 456 LEU   A CB  1 
ATOM   3128 C  CG  . LEU   A 1 436 ? -22.193 -12.294 -18.754 1.00 130.58 ? 456 LEU   A CG  1 
ATOM   3129 C  CD1 . LEU   A 1 436 ? -22.901 -13.334 -19.606 1.00 120.44 ? 456 LEU   A CD1 1 
ATOM   3130 C  CD2 . LEU   A 1 436 ? -20.815 -11.992 -19.309 1.00 128.32 ? 456 LEU   A CD2 1 
ATOM   3131 N  N   . ILE   A 1 437 ? -24.213 -8.277  -17.436 1.00 136.69 ? 457 ILE   A N   1 
ATOM   3132 C  CA  . ILE   A 1 437 ? -24.949 -7.035  -17.654 1.00 139.96 ? 457 ILE   A CA  1 
ATOM   3133 C  C   . ILE   A 1 437 ? -24.092 -5.834  -17.276 1.00 137.76 ? 457 ILE   A C   1 
ATOM   3134 O  O   . ILE   A 1 437 ? -23.931 -4.893  -18.062 1.00 144.35 ? 457 ILE   A O   1 
ATOM   3135 C  CB  . ILE   A 1 437 ? -26.271 -7.049  -16.866 1.00 137.36 ? 457 ILE   A CB  1 
ATOM   3136 C  CG1 . ILE   A 1 437 ? -27.273 -8.013  -17.503 1.00 131.59 ? 457 ILE   A CG1 1 
ATOM   3137 C  CG2 . ILE   A 1 437 ? -26.853 -5.649  -16.782 1.00 134.83 ? 457 ILE   A CG2 1 
ATOM   3138 C  CD1 . ILE   A 1 437 ? -28.513 -8.232  -16.665 1.00 125.13 ? 457 ILE   A CD1 1 
ATOM   3139 N  N   . ARG   A 1 438 ? -23.521 -5.853  -16.070 1.00 133.75 ? 458 ARG   A N   1 
ATOM   3140 C  CA  . ARG   A 1 438 ? -22.813 -4.681  -15.566 1.00 143.20 ? 458 ARG   A CA  1 
ATOM   3141 C  C   . ARG   A 1 438 ? -21.516 -4.425  -16.324 1.00 147.35 ? 458 ARG   A C   1 
ATOM   3142 O  O   . ARG   A 1 438 ? -21.066 -3.276  -16.404 1.00 149.12 ? 458 ARG   A O   1 
ATOM   3143 C  CB  . ARG   A 1 438 ? -22.536 -4.844  -14.071 1.00 133.10 ? 458 ARG   A CB  1 
ATOM   3144 C  CG  . ARG   A 1 438 ? -22.749 -3.576  -13.264 1.00 160.47 ? 458 ARG   A CG  1 
ATOM   3145 C  CD  . ARG   A 1 438 ? -24.069 -2.921  -13.636 1.00 164.04 ? 458 ARG   A CD  1 
ATOM   3146 N  NE  . ARG   A 1 438 ? -24.346 -1.738  -12.832 1.00 166.61 ? 458 ARG   A NE  1 
ATOM   3147 C  CZ  . ARG   A 1 438 ? -25.240 -0.812  -13.149 1.00 164.39 ? 458 ARG   A CZ  1 
ATOM   3148 N  NH1 . ARG   A 1 438 ? -25.948 -0.888  -14.264 1.00 156.41 ? 458 ARG   A NH1 1 
ATOM   3149 N  NH2 . ARG   A 1 438 ? -25.425 0.219   -12.329 1.00 171.45 ? 458 ARG   A NH2 1 
ATOM   3150 N  N   . VAL   A 1 439 ? -20.905 -5.466  -16.882 1.00 152.19 ? 459 VAL   A N   1 
ATOM   3151 C  CA  . VAL   A 1 439 ? -19.646 -5.312  -17.609 1.00 145.83 ? 459 VAL   A CA  1 
ATOM   3152 C  C   . VAL   A 1 439 ? -19.885 -4.907  -19.057 1.00 146.39 ? 459 VAL   A C   1 
ATOM   3153 O  O   . VAL   A 1 439 ? -19.228 -4.000  -19.576 1.00 148.41 ? 459 VAL   A O   1 
ATOM   3154 C  CB  . VAL   A 1 439 ? -18.819 -6.611  -17.513 1.00 130.53 ? 459 VAL   A CB  1 
ATOM   3155 C  CG1 . VAL   A 1 439 ? -17.646 -6.571  -18.477 1.00 130.43 ? 459 VAL   A CG1 1 
ATOM   3156 C  CG2 . VAL   A 1 439 ? -18.325 -6.812  -16.093 1.00 122.36 ? 459 VAL   A CG2 1 
ATOM   3157 N  N   . LEU   A 1 440 ? -20.825 -5.567  -19.736 1.00 148.43 ? 460 LEU   A N   1 
ATOM   3158 C  CA  . LEU   A 1 440 ? -21.154 -5.193  -21.106 1.00 144.81 ? 460 LEU   A CA  1 
ATOM   3159 C  C   . LEU   A 1 440 ? -21.896 -3.866  -21.190 1.00 150.40 ? 460 LEU   A C   1 
ATOM   3160 O  O   . LEU   A 1 440 ? -22.006 -3.306  -22.286 1.00 153.35 ? 460 LEU   A O   1 
ATOM   3161 C  CB  . LEU   A 1 440 ? -21.978 -6.299  -21.769 1.00 130.85 ? 460 LEU   A CB  1 
ATOM   3162 C  CG  . LEU   A 1 440 ? -21.208 -7.588  -22.065 1.00 125.58 ? 460 LEU   A CG  1 
ATOM   3163 C  CD1 . LEU   A 1 440 ? -22.160 -8.723  -22.391 1.00 118.39 ? 460 LEU   A CD1 1 
ATOM   3164 C  CD2 . LEU   A 1 440 ? -20.224 -7.370  -23.205 1.00 126.03 ? 460 LEU   A CD2 1 
ATOM   3165 N  N   . GLN   A 1 441 ? -22.406 -3.354  -20.068 1.00 152.13 ? 461 GLN   A N   1 
ATOM   3166 C  CA  . GLN   A 1 441 ? -22.997 -2.022  -20.054 1.00 157.12 ? 461 GLN   A CA  1 
ATOM   3167 C  C   . GLN   A 1 441 ? -21.948 -0.926  -20.172 1.00 165.12 ? 461 GLN   A C   1 
ATOM   3168 O  O   . GLN   A 1 441 ? -22.279 0.189   -20.588 1.00 163.82 ? 461 GLN   A O   1 
ATOM   3169 C  CB  . GLN   A 1 441 ? -23.805 -1.814  -18.771 1.00 155.34 ? 461 GLN   A CB  1 
ATOM   3170 C  CG  . GLN   A 1 441 ? -25.301 -1.669  -18.982 1.00 152.40 ? 461 GLN   A CG  1 
ATOM   3171 C  CD  . GLN   A 1 441 ? -26.054 -1.503  -17.677 1.00 153.56 ? 461 GLN   A CD  1 
ATOM   3172 O  OE1 . GLN   A 1 441 ? -25.452 -1.299  -16.622 1.00 151.78 ? 461 GLN   A OE1 1 
ATOM   3173 N  NE2 . GLN   A 1 441 ? -27.377 -1.593  -17.741 1.00 151.80 ? 461 GLN   A NE2 1 
ATOM   3174 N  N   . ASN   A 1 442 ? -20.698 -1.218  -19.821 1.00 173.12 ? 462 ASN   A N   1 
ATOM   3175 C  CA  . ASN   A 1 442 ? -19.644 -0.216  -19.775 1.00 174.02 ? 462 ASN   A CA  1 
ATOM   3176 C  C   . ASN   A 1 442 ? -18.501 -0.464  -20.746 1.00 174.33 ? 462 ASN   A C   1 
ATOM   3177 O  O   . ASN   A 1 442 ? -17.826 0.494   -21.128 1.00 179.58 ? 462 ASN   A O   1 
ATOM   3178 C  CB  . ASN   A 1 442 ? -19.063 -0.119  -18.355 1.00 174.76 ? 462 ASN   A CB  1 
ATOM   3179 C  CG  . ASN   A 1 442 ? -20.034 0.492   -17.366 1.00 180.00 ? 462 ASN   A CG  1 
ATOM   3180 O  OD1 . ASN   A 1 442 ? -19.902 1.657   -16.990 1.00 184.75 ? 462 ASN   A OD1 1 
ATOM   3181 N  ND2 . ASN   A 1 442 ? -21.019 -0.290  -16.941 1.00 179.99 ? 462 ASN   A ND2 1 
ATOM   3182 N  N   . PHE   A 1 443 ? -18.261 -1.708  -21.154 1.00 148.82 ? 463 PHE   A N   1 
ATOM   3183 C  CA  . PHE   A 1 443 ? -17.091 -2.038  -21.951 1.00 153.96 ? 463 PHE   A CA  1 
ATOM   3184 C  C   . PHE   A 1 443 ? -17.465 -2.910  -23.141 1.00 161.51 ? 463 PHE   A C   1 
ATOM   3185 O  O   . PHE   A 1 443 ? -18.457 -3.644  -23.112 1.00 161.85 ? 463 PHE   A O   1 
ATOM   3186 C  CB  . PHE   A 1 443 ? -16.028 -2.770  -21.118 1.00 155.18 ? 463 PHE   A CB  1 
ATOM   3187 C  CG  . PHE   A 1 443 ? -15.659 -2.067  -19.845 1.00 157.23 ? 463 PHE   A CG  1 
ATOM   3188 C  CD1 . PHE   A 1 443 ? -14.703 -1.065  -19.842 1.00 163.87 ? 463 PHE   A CD1 1 
ATOM   3189 C  CD2 . PHE   A 1 443 ? -16.261 -2.417  -18.648 1.00 154.71 ? 463 PHE   A CD2 1 
ATOM   3190 C  CE1 . PHE   A 1 443 ? -14.359 -0.420  -18.668 1.00 171.06 ? 463 PHE   A CE1 1 
ATOM   3191 C  CE2 . PHE   A 1 443 ? -15.922 -1.777  -17.473 1.00 158.78 ? 463 PHE   A CE2 1 
ATOM   3192 C  CZ  . PHE   A 1 443 ? -14.970 -0.777  -17.482 1.00 171.74 ? 463 PHE   A CZ  1 
ATOM   3193 N  N   . SER   A 1 444 ? -16.652 -2.814  -24.188 1.00 150.82 ? 464 SER   A N   1 
ATOM   3194 C  CA  . SER   A 1 444 ? -16.637 -3.758  -25.293 1.00 148.20 ? 464 SER   A CA  1 
ATOM   3195 C  C   . SER   A 1 444 ? -15.326 -4.533  -25.259 1.00 141.15 ? 464 SER   A C   1 
ATOM   3196 O  O   . SER   A 1 444 ? -14.342 -4.102  -24.652 1.00 139.33 ? 464 SER   A O   1 
ATOM   3197 C  CB  . SER   A 1 444 ? -16.805 -3.047  -26.640 1.00 146.71 ? 464 SER   A CB  1 
ATOM   3198 O  OG  . SER   A 1 444 ? -18.094 -2.470  -26.756 1.00 144.12 ? 464 SER   A OG  1 
ATOM   3199 N  N   . PHE   A 1 445 ? -15.318 -5.692  -25.915 1.00 148.95 ? 465 PHE   A N   1 
ATOM   3200 C  CA  . PHE   A 1 445 ? -14.193 -6.616  -25.832 1.00 143.82 ? 465 PHE   A CA  1 
ATOM   3201 C  C   . PHE   A 1 445 ? -13.741 -7.005  -27.230 1.00 154.47 ? 465 PHE   A C   1 
ATOM   3202 O  O   . PHE   A 1 445 ? -14.545 -7.487  -28.035 1.00 152.25 ? 465 PHE   A O   1 
ATOM   3203 C  CB  . PHE   A 1 445 ? -14.566 -7.856  -25.014 1.00 127.49 ? 465 PHE   A CB  1 
ATOM   3204 C  CG  . PHE   A 1 445 ? -14.708 -7.586  -23.542 1.00 136.94 ? 465 PHE   A CG  1 
ATOM   3205 C  CD1 . PHE   A 1 445 ? -15.834 -6.951  -23.045 1.00 136.34 ? 465 PHE   A CD1 1 
ATOM   3206 C  CD2 . PHE   A 1 445 ? -13.713 -7.963  -22.656 1.00 139.27 ? 465 PHE   A CD2 1 
ATOM   3207 C  CE1 . PHE   A 1 445 ? -15.966 -6.697  -21.693 1.00 137.12 ? 465 PHE   A CE1 1 
ATOM   3208 C  CE2 . PHE   A 1 445 ? -13.839 -7.713  -21.303 1.00 130.47 ? 465 PHE   A CE2 1 
ATOM   3209 C  CZ  . PHE   A 1 445 ? -14.967 -7.079  -20.821 1.00 131.83 ? 465 PHE   A CZ  1 
ATOM   3210 N  N   . LYS   A 1 446 ? -12.455 -6.798  -27.511 1.00 169.33 ? 466 LYS   A N   1 
ATOM   3211 C  CA  . LYS   A 1 446 ? -11.822 -7.142  -28.772 1.00 171.00 ? 466 LYS   A CA  1 
ATOM   3212 C  C   . LYS   A 1 446 ? -10.671 -8.112  -28.531 1.00 158.42 ? 466 LYS   A C   1 
ATOM   3213 O  O   . LYS   A 1 446 ? -10.022 -8.062  -27.482 1.00 160.47 ? 466 LYS   A O   1 
ATOM   3214 C  CB  . LYS   A 1 446 ? -11.284 -5.893  -29.484 1.00 162.74 ? 466 LYS   A CB  1 
ATOM   3215 C  CG  . LYS   A 1 446 ? -12.297 -4.772  -29.652 1.00 164.44 ? 466 LYS   A CG  1 
ATOM   3216 C  CD  . LYS   A 1 446 ? -13.479 -5.210  -30.499 1.00 170.40 ? 466 LYS   A CD  1 
ATOM   3217 C  CE  . LYS   A 1 446 ? -14.386 -4.034  -30.820 1.00 162.27 ? 466 LYS   A CE  1 
ATOM   3218 N  NZ  . LYS   A 1 446 ? -13.679 -2.999  -31.626 1.00 172.06 ? 466 LYS   A NZ  1 
ATOM   3219 N  N   . PRO   A 1 447 ? -10.400 -9.010  -29.475 1.00 163.54 ? 467 PRO   A N   1 
ATOM   3220 C  CA  . PRO   A 1 447 ? -9.238  -9.893  -29.338 1.00 164.16 ? 467 PRO   A CA  1 
ATOM   3221 C  C   . PRO   A 1 447 ? -7.935  -9.112  -29.428 1.00 174.01 ? 467 PRO   A C   1 
ATOM   3222 O  O   . PRO   A 1 447 ? -7.869  -8.008  -29.972 1.00 170.47 ? 467 PRO   A O   1 
ATOM   3223 C  CB  . PRO   A 1 447 ? -9.383  -10.866 -30.514 1.00 159.80 ? 467 PRO   A CB  1 
ATOM   3224 C  CG  . PRO   A 1 447 ? -10.826 -10.781 -30.911 1.00 149.76 ? 467 PRO   A CG  1 
ATOM   3225 C  CD  . PRO   A 1 447 ? -11.229 -9.365  -30.639 1.00 155.20 ? 467 PRO   A CD  1 
ATOM   3226 N  N   . CYS   A 1 448 ? -6.884  -9.709  -28.875 1.00 177.44 ? 468 CYS   A N   1 
ATOM   3227 C  CA  . CYS   A 1 448 ? -5.547  -9.136  -28.885 1.00 175.93 ? 468 CYS   A CA  1 
ATOM   3228 C  C   . CYS   A 1 448 ? -4.630  -9.961  -29.782 1.00 177.74 ? 468 CYS   A C   1 
ATOM   3229 O  O   . CYS   A 1 448 ? -5.017  -10.995 -30.334 1.00 174.18 ? 468 CYS   A O   1 
ATOM   3230 C  CB  . CYS   A 1 448 ? -4.982  -9.050  -27.465 1.00 170.84 ? 468 CYS   A CB  1 
ATOM   3231 S  SG  . CYS   A 1 448 ? -5.535  -7.621  -26.515 1.00 178.83 ? 468 CYS   A SG  1 
ATOM   3232 N  N   . LYS   A 1 449 ? -3.391  -9.482  -29.923 1.00 190.15 ? 469 LYS   A N   1 
ATOM   3233 C  CA  . LYS   A 1 449 ? -2.390  -10.221 -30.682 1.00 190.54 ? 469 LYS   A CA  1 
ATOM   3234 C  C   . LYS   A 1 449 ? -2.059  -11.552 -30.019 1.00 188.12 ? 469 LYS   A C   1 
ATOM   3235 O  O   . LYS   A 1 449 ? -1.793  -12.543 -30.710 1.00 190.29 ? 469 LYS   A O   1 
ATOM   3236 C  CB  . LYS   A 1 449 ? -1.131  -9.365  -30.844 1.00 178.61 ? 469 LYS   A CB  1 
ATOM   3237 C  CG  . LYS   A 1 449 ? 0.178   -10.090 -30.576 1.00 188.12 ? 469 LYS   A CG  1 
ATOM   3238 C  CD  . LYS   A 1 449 ? 1.322   -9.103  -30.413 1.00 202.59 ? 469 LYS   A CD  1 
ATOM   3239 C  CE  . LYS   A 1 449 ? 2.577   -9.793  -29.908 1.00 204.66 ? 469 LYS   A CE  1 
ATOM   3240 N  NZ  . LYS   A 1 449 ? 3.648   -8.816  -29.570 1.00 208.75 ? 469 LYS   A NZ  1 
ATOM   3241 N  N   . GLU   A 1 450 ? -2.087  -11.600 -28.690 1.00 181.22 ? 470 GLU   A N   1 
ATOM   3242 C  CA  . GLU   A 1 450 ? -1.782  -12.811 -27.941 1.00 187.07 ? 470 GLU   A CA  1 
ATOM   3243 C  C   . GLU   A 1 450 ? -3.018  -13.639 -27.613 1.00 185.51 ? 470 GLU   A C   1 
ATOM   3244 O  O   . GLU   A 1 450 ? -2.894  -14.667 -26.939 1.00 184.13 ? 470 GLU   A O   1 
ATOM   3245 C  CB  . GLU   A 1 450 ? -1.038  -12.451 -26.650 1.00 195.25 ? 470 GLU   A CB  1 
ATOM   3246 C  CG  . GLU   A 1 450 ? -1.667  -11.308 -25.870 1.00 188.82 ? 470 GLU   A CG  1 
ATOM   3247 C  CD  . GLU   A 1 450 ? -0.799  -10.843 -24.717 1.00 198.18 ? 470 GLU   A CD  1 
ATOM   3248 O  OE1 . GLU   A 1 450 ? 0.180   -11.545 -24.388 1.00 217.20 ? 470 GLU   A OE1 1 
ATOM   3249 O  OE2 . GLU   A 1 450 ? -1.093  -9.773  -24.144 1.00 191.23 ? 470 GLU   A OE2 1 
ATOM   3250 N  N   . THR   A 1 451 ? -4.198  -13.222 -28.067 1.00 181.62 ? 471 THR   A N   1 
ATOM   3251 C  CA  . THR   A 1 451 ? -5.409  -13.999 -27.837 1.00 176.42 ? 471 THR   A CA  1 
ATOM   3252 C  C   . THR   A 1 451 ? -5.353  -15.301 -28.627 1.00 167.04 ? 471 THR   A C   1 
ATOM   3253 O  O   . THR   A 1 451 ? -5.041  -15.304 -29.822 1.00 173.97 ? 471 THR   A O   1 
ATOM   3254 C  CB  . THR   A 1 451 ? -6.645  -13.188 -28.230 1.00 169.06 ? 471 THR   A CB  1 
ATOM   3255 O  OG1 . THR   A 1 451 ? -6.794  -12.077 -27.337 1.00 164.73 ? 471 THR   A OG1 1 
ATOM   3256 C  CG2 . THR   A 1 451 ? -7.898  -14.051 -28.171 1.00 151.27 ? 471 THR   A CG2 1 
ATOM   3257 N  N   . GLN   A 1 452 ? -5.654  -16.411 -27.956 1.00 154.20 ? 472 GLN   A N   1 
ATOM   3258 C  CA  . GLN   A 1 452 ? -5.576  -17.734 -28.567 1.00 163.09 ? 472 GLN   A CA  1 
ATOM   3259 C  C   . GLN   A 1 452 ? -6.815  -17.968 -29.423 1.00 156.73 ? 472 GLN   A C   1 
ATOM   3260 O  O   . GLN   A 1 452 ? -7.914  -18.173 -28.896 1.00 153.84 ? 472 GLN   A O   1 
ATOM   3261 C  CB  . GLN   A 1 452 ? -5.439  -18.806 -27.490 1.00 162.54 ? 472 GLN   A CB  1 
ATOM   3262 C  CG  . GLN   A 1 452 ? -5.121  -20.191 -28.022 1.00 142.25 ? 472 GLN   A CG  1 
ATOM   3263 C  CD  . GLN   A 1 452 ? -4.919  -21.205 -26.914 1.00 153.80 ? 472 GLN   A CD  1 
ATOM   3264 O  OE1 . GLN   A 1 452 ? -5.672  -21.236 -25.941 1.00 157.02 ? 472 GLN   A OE1 1 
ATOM   3265 N  NE2 . GLN   A 1 452 ? -3.892  -22.035 -27.051 1.00 152.94 ? 472 GLN   A NE2 1 
ATOM   3266 N  N   . ILE   A 1 453 ? -6.642  -17.935 -30.745 1.00 155.88 ? 473 ILE   A N   1 
ATOM   3267 C  CA  . ILE   A 1 453 ? -7.724  -18.159 -31.691 1.00 147.73 ? 473 ILE   A CA  1 
ATOM   3268 C  C   . ILE   A 1 453 ? -7.238  -19.144 -32.748 1.00 153.79 ? 473 ILE   A C   1 
ATOM   3269 O  O   . ILE   A 1 453 ? -6.276  -18.853 -33.464 1.00 160.55 ? 473 ILE   A O   1 
ATOM   3270 C  CB  . ILE   A 1 453 ? -8.202  -16.858 -32.358 1.00 150.90 ? 473 ILE   A CB  1 
ATOM   3271 C  CG1 . ILE   A 1 453 ? -8.731  -15.879 -31.308 1.00 157.00 ? 473 ILE   A CG1 1 
ATOM   3272 C  CG2 . ILE   A 1 453 ? -9.267  -17.158 -33.404 1.00 144.82 ? 473 ILE   A CG2 1 
ATOM   3273 C  CD1 . ILE   A 1 453 ? -9.160  -14.543 -31.875 1.00 163.56 ? 473 ILE   A CD1 1 
ATOM   3274 N  N   . PRO   A 1 454 ? -7.864  -20.321 -32.891 1.00 152.08 ? 474 PRO   A N   1 
ATOM   3275 C  CA  . PRO   A 1 454 ? -9.011  -20.829 -32.126 1.00 141.68 ? 474 PRO   A CA  1 
ATOM   3276 C  C   . PRO   A 1 454 ? -8.607  -21.252 -30.718 1.00 150.25 ? 474 PRO   A C   1 
ATOM   3277 O  O   . PRO   A 1 454 ? -7.463  -21.635 -30.485 1.00 151.76 ? 474 PRO   A O   1 
ATOM   3278 C  CB  . PRO   A 1 454 ? -9.486  -22.015 -32.974 1.00 133.15 ? 474 PRO   A CB  1 
ATOM   3279 C  CG  . PRO   A 1 454 ? -8.229  -22.527 -33.610 1.00 147.64 ? 474 PRO   A CG  1 
ATOM   3280 C  CD  . PRO   A 1 454 ? -7.416  -21.290 -33.909 1.00 154.94 ? 474 PRO   A CD  1 
ATOM   3281 N  N   . LEU   A 1 455 ? -9.528  -21.187 -29.761 1.00 138.72 ? 475 LEU   A N   1 
ATOM   3282 C  CA  . LEU   A 1 455 ? -9.199  -21.494 -28.375 1.00 137.31 ? 475 LEU   A CA  1 
ATOM   3283 C  C   . LEU   A 1 455 ? -8.950  -22.988 -28.213 1.00 142.05 ? 475 LEU   A C   1 
ATOM   3284 O  O   . LEU   A 1 455 ? -9.851  -23.804 -28.436 1.00 150.82 ? 475 LEU   A O   1 
ATOM   3285 C  CB  . LEU   A 1 455 ? -10.322 -21.033 -27.450 1.00 131.84 ? 475 LEU   A CB  1 
ATOM   3286 C  CG  . LEU   A 1 455 ? -10.124 -21.306 -25.957 1.00 136.47 ? 475 LEU   A CG  1 
ATOM   3287 C  CD1 . LEU   A 1 455 ? -10.379 -20.047 -25.143 1.00 140.32 ? 475 LEU   A CD1 1 
ATOM   3288 C  CD2 . LEU   A 1 455 ? -11.026 -22.438 -25.489 1.00 116.25 ? 475 LEU   A CD2 1 
ATOM   3289 N  N   . LYS   A 1 456 ? -7.727  -23.345 -27.829 1.00 138.90 ? 476 LYS   A N   1 
ATOM   3290 C  CA  . LYS   A 1 456 ? -7.401  -24.731 -27.526 1.00 142.90 ? 476 LYS   A CA  1 
ATOM   3291 C  C   . LYS   A 1 456 ? -7.881  -25.081 -26.124 1.00 146.91 ? 476 LYS   A C   1 
ATOM   3292 O  O   . LYS   A 1 456 ? -7.532  -24.405 -25.152 1.00 144.62 ? 476 LYS   A O   1 
ATOM   3293 C  CB  . LYS   A 1 456 ? -5.895  -24.969 -27.637 1.00 148.55 ? 476 LYS   A CB  1 
ATOM   3294 C  CG  . LYS   A 1 456 ? -5.391  -25.247 -29.045 1.00 145.00 ? 476 LYS   A CG  1 
ATOM   3295 C  CD  . LYS   A 1 456 ? -4.000  -25.867 -29.000 1.00 152.08 ? 476 LYS   A CD  1 
ATOM   3296 C  CE  . LYS   A 1 456 ? -2.915  -24.871 -29.378 1.00 167.96 ? 476 LYS   A CE  1 
ATOM   3297 N  NZ  . LYS   A 1 456 ? -2.678  -24.848 -30.849 1.00 175.92 ? 476 LYS   A NZ  1 
ATOM   3298 N  N   . LEU   A 1 457 ? -8.688  -26.134 -26.021 1.00 144.74 ? 477 LEU   A N   1 
ATOM   3299 C  CA  . LEU   A 1 457 ? -9.089  -26.634 -24.715 1.00 144.56 ? 477 LEU   A CA  1 
ATOM   3300 C  C   . LEU   A 1 457 ? -7.904  -27.281 -24.009 1.00 152.80 ? 477 LEU   A C   1 
ATOM   3301 O  O   . LEU   A 1 457 ? -6.958  -27.754 -24.645 1.00 160.87 ? 477 LEU   A O   1 
ATOM   3302 C  CB  . LEU   A 1 457 ? -10.228 -27.643 -24.852 1.00 134.29 ? 477 LEU   A CB  1 
ATOM   3303 C  CG  . LEU   A 1 457 ? -11.645 -27.074 -24.892 1.00 122.52 ? 477 LEU   A CG  1 
ATOM   3304 C  CD1 . LEU   A 1 457 ? -12.657 -28.192 -25.068 1.00 127.83 ? 477 LEU   A CD1 1 
ATOM   3305 C  CD2 . LEU   A 1 457 ? -11.927 -26.287 -23.624 1.00 126.20 ? 477 LEU   A CD2 1 
ATOM   3306 N  N   . SER   A 1 458 ? -7.957  -27.294 -22.678 1.00 163.66 ? 478 SER   A N   1 
ATOM   3307 C  CA  . SER   A 1 458 ? -6.920  -27.960 -21.900 1.00 165.29 ? 478 SER   A CA  1 
ATOM   3308 C  C   . SER   A 1 458 ? -6.960  -29.458 -22.162 1.00 170.78 ? 478 SER   A C   1 
ATOM   3309 O  O   . SER   A 1 458 ? -7.926  -30.135 -21.793 1.00 165.09 ? 478 SER   A O   1 
ATOM   3310 C  CB  . SER   A 1 458 ? -7.087  -27.676 -20.407 1.00 156.39 ? 478 SER   A CB  1 
ATOM   3311 O  OG  . SER   A 1 458 ? -6.139  -28.396 -19.641 1.00 165.85 ? 478 SER   A OG  1 
ATOM   3312 N  N   . LEU   A 1 459 ? -5.907  -29.984 -22.792 1.00 210.28 ? 479 LEU   A N   1 
ATOM   3313 C  CA  . LEU   A 1 459 ? -5.835  -31.399 -23.145 1.00 210.94 ? 479 LEU   A CA  1 
ATOM   3314 C  C   . LEU   A 1 459 ? -5.684  -32.245 -21.888 1.00 209.61 ? 479 LEU   A C   1 
ATOM   3315 O  O   . LEU   A 1 459 ? -5.560  -33.473 -21.965 1.00 210.73 ? 479 LEU   A O   1 
ATOM   3316 C  CB  . LEU   A 1 459 ? -4.676  -31.658 -24.115 1.00 214.90 ? 479 LEU   A CB  1 
ATOM   3317 C  CG  . LEU   A 1 459 ? -4.927  -31.587 -25.623 1.00 222.66 ? 479 LEU   A CG  1 
ATOM   3318 C  CD1 . LEU   A 1 459 ? -5.445  -30.224 -26.062 1.00 213.36 ? 479 LEU   A CD1 1 
ATOM   3319 C  CD2 . LEU   A 1 459 ? -3.657  -31.944 -26.385 1.00 218.27 ? 479 LEU   A CD2 1 
ATOM   3320 N  N   . GLY   A 1 460 ? -5.699  -31.590 -20.733 1.00 194.25 ? 480 GLY   A N   1 
ATOM   3321 C  CA  . GLY   A 1 460 ? -5.507  -32.246 -19.460 1.00 169.54 ? 480 GLY   A CA  1 
ATOM   3322 C  C   . GLY   A 1 460 ? -6.778  -32.805 -18.859 1.00 172.81 ? 480 GLY   A C   1 
ATOM   3323 O  O   . GLY   A 1 460 ? -7.513  -33.544 -19.521 1.00 166.85 ? 480 GLY   A O   1 
ATOM   3324 N  N   . GLY   A 1 461 ? -7.048  -32.451 -17.602 1.00 152.85 ? 481 GLY   A N   1 
ATOM   3325 C  CA  . GLY   A 1 461 ? -8.110  -33.074 -16.834 1.00 155.82 ? 481 GLY   A CA  1 
ATOM   3326 C  C   . GLY   A 1 461 ? -9.429  -32.330 -16.819 1.00 168.39 ? 481 GLY   A C   1 
ATOM   3327 O  O   . GLY   A 1 461 ? -10.462 -32.894 -17.188 1.00 158.78 ? 481 GLY   A O   1 
ATOM   3328 N  N   . LEU   A 1 462 ? -9.417  -31.073 -16.392 1.00 179.46 ? 482 LEU   A N   1 
ATOM   3329 C  CA  . LEU   A 1 462 ? -10.637 -30.289 -16.263 1.00 169.24 ? 482 LEU   A CA  1 
ATOM   3330 C  C   . LEU   A 1 462 ? -10.792 -29.330 -17.439 1.00 161.67 ? 482 LEU   A C   1 
ATOM   3331 O  O   . LEU   A 1 462 ? -9.821  -28.954 -18.100 1.00 167.01 ? 482 LEU   A O   1 
ATOM   3332 C  CB  . LEU   A 1 462 ? -10.658 -29.513 -14.940 1.00 175.63 ? 482 LEU   A CB  1 
ATOM   3333 C  CG  . LEU   A 1 462 ? -9.504  -28.574 -14.576 1.00 187.03 ? 482 LEU   A CG  1 
ATOM   3334 C  CD1 . LEU   A 1 462 ? -9.986  -27.525 -13.591 1.00 184.49 ? 482 LEU   A CD1 1 
ATOM   3335 C  CD2 . LEU   A 1 462 ? -8.326  -29.338 -13.985 1.00 181.75 ? 482 LEU   A CD2 1 
ATOM   3336 N  N   . LEU   A 1 463 ? -12.039 -28.935 -17.692 1.00 148.71 ? 483 LEU   A N   1 
ATOM   3337 C  CA  . LEU   A 1 463 ? -12.371 -28.133 -18.868 1.00 144.60 ? 483 LEU   A CA  1 
ATOM   3338 C  C   . LEU   A 1 463 ? -11.935 -26.693 -18.633 1.00 150.90 ? 483 LEU   A C   1 
ATOM   3339 O  O   . LEU   A 1 463 ? -12.658 -25.900 -18.025 1.00 141.40 ? 483 LEU   A O   1 
ATOM   3340 C  CB  . LEU   A 1 463 ? -13.861 -28.216 -19.180 1.00 116.67 ? 483 LEU   A CB  1 
ATOM   3341 C  CG  . LEU   A 1 463 ? -14.196 -27.913 -20.642 1.00 110.22 ? 483 LEU   A CG  1 
ATOM   3342 C  CD1 . LEU   A 1 463 ? -13.528 -28.934 -21.548 1.00 119.11 ? 483 LEU   A CD1 1 
ATOM   3343 C  CD2 . LEU   A 1 463 ? -15.693 -27.892 -20.876 1.00 114.68 ? 483 LEU   A CD2 1 
ATOM   3344 N  N   . GLN   A 1 464 ? -10.747 -26.355 -19.124 1.00 143.24 ? 484 GLN   A N   1 
ATOM   3345 C  CA  . GLN   A 1 464 ? -10.194 -25.009 -19.056 1.00 145.45 ? 484 GLN   A CA  1 
ATOM   3346 C  C   . GLN   A 1 464 ? -9.463  -24.716 -20.360 1.00 143.88 ? 484 GLN   A C   1 
ATOM   3347 O  O   . GLN   A 1 464 ? -9.247  -25.632 -21.163 1.00 147.51 ? 484 GLN   A O   1 
ATOM   3348 C  CB  . GLN   A 1 464 ? -9.252  -24.868 -17.857 1.00 155.30 ? 484 GLN   A CB  1 
ATOM   3349 C  CG  . GLN   A 1 464 ? -9.951  -24.842 -16.506 1.00 162.83 ? 484 GLN   A CG  1 
ATOM   3350 C  CD  . GLN   A 1 464 ? -8.981  -24.681 -15.351 1.00 168.31 ? 484 GLN   A CD  1 
ATOM   3351 O  OE1 . GLN   A 1 464 ? -7.784  -24.933 -15.490 1.00 166.81 ? 484 GLN   A OE1 1 
ATOM   3352 N  NE2 . GLN   A 1 464 ? -9.494  -24.255 -14.202 1.00 169.22 ? 484 GLN   A NE2 1 
ATOM   3353 N  N   . PRO   A 1 465 ? -9.097  -23.467 -20.632 1.00 150.48 ? 485 PRO   A N   1 
ATOM   3354 C  CA  . PRO   A 1 465 ? -8.241  -23.193 -21.789 1.00 152.10 ? 485 PRO   A CA  1 
ATOM   3355 C  C   . PRO   A 1 465 ? -6.776  -23.442 -21.470 1.00 150.85 ? 485 PRO   A C   1 
ATOM   3356 O  O   . PRO   A 1 465 ? -6.331  -23.312 -20.327 1.00 148.37 ? 485 PRO   A O   1 
ATOM   3357 C  CB  . PRO   A 1 465 ? -8.495  -21.706 -22.078 1.00 136.08 ? 485 PRO   A CB  1 
ATOM   3358 C  CG  . PRO   A 1 465 ? -9.713  -21.339 -21.275 1.00 124.55 ? 485 PRO   A CG  1 
ATOM   3359 C  CD  . PRO   A 1 465 ? -9.681  -22.233 -20.084 1.00 130.81 ? 485 PRO   A CD  1 
ATOM   3360 N  N   . GLU   A 1 466 ? -6.025  -23.816 -22.507 1.00 147.58 ? 486 GLU   A N   1 
ATOM   3361 C  CA  . GLU   A 1 466 ? -4.580  -23.971 -22.375 1.00 150.51 ? 486 GLU   A CA  1 
ATOM   3362 C  C   . GLU   A 1 466 ? -3.956  -22.646 -21.961 1.00 151.92 ? 486 GLU   A C   1 
ATOM   3363 O  O   . GLU   A 1 466 ? -3.470  -22.504 -20.834 1.00 155.13 ? 486 GLU   A O   1 
ATOM   3364 C  CB  . GLU   A 1 466 ? -3.958  -24.467 -23.682 1.00 157.48 ? 486 GLU   A CB  1 
ATOM   3365 C  CG  . GLU   A 1 466 ? -4.197  -25.938 -23.982 1.00 161.22 ? 486 GLU   A CG  1 
ATOM   3366 C  CD  . GLU   A 1 466 ? -3.410  -26.416 -25.188 1.00 171.97 ? 486 GLU   A CD  1 
ATOM   3367 O  OE1 . GLU   A 1 466 ? -2.650  -25.607 -25.761 1.00 168.55 ? 486 GLU   A OE1 1 
ATOM   3368 O  OE2 . GLU   A 1 466 ? -3.550  -27.599 -25.563 1.00 184.10 ? 486 GLU   A OE2 1 
ATOM   3369 N  N   . LYS   A 1 467 ? -3.966  -21.672 -22.867 1.00 148.01 ? 487 LYS   A N   1 
ATOM   3370 C  CA  . LYS   A 1 467 ? -3.547  -20.326 -22.509 1.00 155.45 ? 487 LYS   A CA  1 
ATOM   3371 C  C   . LYS   A 1 467 ? -4.709  -19.582 -21.854 1.00 146.61 ? 487 LYS   A C   1 
ATOM   3372 O  O   . LYS   A 1 467 ? -5.857  -19.726 -22.283 1.00 130.58 ? 487 LYS   A O   1 
ATOM   3373 C  CB  . LYS   A 1 467 ? -3.074  -19.558 -23.743 1.00 151.39 ? 487 LYS   A CB  1 
ATOM   3374 C  CG  . LYS   A 1 467 ? -1.935  -20.225 -24.501 1.00 145.60 ? 487 LYS   A CG  1 
ATOM   3375 C  CD  . LYS   A 1 467 ? -1.674  -19.531 -25.832 1.00 150.27 ? 487 LYS   A CD  1 
ATOM   3376 C  CE  . LYS   A 1 467 ? -0.965  -18.196 -25.651 1.00 162.28 ? 487 LYS   A CE  1 
ATOM   3377 N  NZ  . LYS   A 1 467 ? 0.485   -18.367 -25.356 1.00 165.40 ? 487 LYS   A NZ  1 
ATOM   3378 N  N   . PRO   A 1 468 ? -4.444  -18.803 -20.805 1.00 143.91 ? 488 PRO   A N   1 
ATOM   3379 C  CA  . PRO   A 1 468 ? -5.508  -17.988 -20.210 1.00 139.91 ? 488 PRO   A CA  1 
ATOM   3380 C  C   . PRO   A 1 468 ? -6.108  -17.035 -21.233 1.00 138.68 ? 488 PRO   A C   1 
ATOM   3381 O  O   . PRO   A 1 468 ? -5.437  -16.577 -22.160 1.00 141.02 ? 488 PRO   A O   1 
ATOM   3382 C  CB  . PRO   A 1 468 ? -4.788  -17.230 -19.089 1.00 143.45 ? 488 PRO   A CB  1 
ATOM   3383 C  CG  . PRO   A 1 468 ? -3.631  -18.108 -18.736 1.00 137.20 ? 488 PRO   A CG  1 
ATOM   3384 C  CD  . PRO   A 1 468 ? -3.193  -18.735 -20.031 1.00 141.37 ? 488 PRO   A CD  1 
ATOM   3385 N  N   . VAL   A 1 469 ? -7.394  -16.744 -21.056 1.00 137.40 ? 489 VAL   A N   1 
ATOM   3386 C  CA  . VAL   A 1 469 ? -8.141  -15.930 -22.009 1.00 150.02 ? 489 VAL   A CA  1 
ATOM   3387 C  C   . VAL   A 1 469 ? -7.797  -14.463 -21.770 1.00 159.47 ? 489 VAL   A C   1 
ATOM   3388 O  O   . VAL   A 1 469 ? -8.115  -13.902 -20.719 1.00 157.67 ? 489 VAL   A O   1 
ATOM   3389 C  CB  . VAL   A 1 469 ? -9.649  -16.172 -21.892 1.00 134.14 ? 489 VAL   A CB  1 
ATOM   3390 C  CG1 . VAL   A 1 469 ? -10.402 -15.284 -22.869 1.00 134.86 ? 489 VAL   A CG1 1 
ATOM   3391 C  CG2 . VAL   A 1 469 ? -9.970  -17.638 -22.140 1.00 126.25 ? 489 VAL   A CG2 1 
ATOM   3392 N  N   . VAL   A 1 470 ? -7.149  -13.838 -22.751 1.00 149.83 ? 490 VAL   A N   1 
ATOM   3393 C  CA  . VAL   A 1 470 ? -6.773  -12.432 -22.693 1.00 154.10 ? 490 VAL   A CA  1 
ATOM   3394 C  C   . VAL   A 1 470 ? -7.417  -11.705 -23.865 1.00 162.71 ? 490 VAL   A C   1 
ATOM   3395 O  O   . VAL   A 1 470 ? -7.396  -12.194 -25.000 1.00 162.45 ? 490 VAL   A O   1 
ATOM   3396 C  CB  . VAL   A 1 470 ? -5.241  -12.249 -22.709 1.00 159.79 ? 490 VAL   A CB  1 
ATOM   3397 C  CG1 . VAL   A 1 470 ? -4.652  -12.609 -21.359 1.00 159.88 ? 490 VAL   A CG1 1 
ATOM   3398 C  CG2 . VAL   A 1 470 ? -4.615  -13.103 -23.802 1.00 161.66 ? 490 VAL   A CG2 1 
ATOM   3399 N  N   . LEU   A 1 471 ? -7.992  -10.536 -23.585 1.00 167.80 ? 491 LEU   A N   1 
ATOM   3400 C  CA  . LEU   A 1 471 ? -8.666  -9.734  -24.595 1.00 165.86 ? 491 LEU   A CA  1 
ATOM   3401 C  C   . LEU   A 1 471 ? -8.423  -8.259  -24.308 1.00 161.17 ? 491 LEU   A C   1 
ATOM   3402 O  O   . LEU   A 1 471 ? -8.029  -7.878  -23.203 1.00 160.22 ? 491 LEU   A O   1 
ATOM   3403 C  CB  . LEU   A 1 471 ? -10.176 -10.014 -24.632 1.00 154.65 ? 491 LEU   A CB  1 
ATOM   3404 C  CG  . LEU   A 1 471 ? -10.647 -11.437 -24.937 1.00 137.90 ? 491 LEU   A CG  1 
ATOM   3405 C  CD1 . LEU   A 1 471 ? -12.139 -11.556 -24.693 1.00 138.31 ? 491 LEU   A CD1 1 
ATOM   3406 C  CD2 . LEU   A 1 471 ? -10.307 -11.824 -26.367 1.00 147.74 ? 491 LEU   A CD2 1 
ATOM   3407 N  N   . LYS   A 1 472 ? -8.667  -7.428  -25.319 1.00 160.14 ? 492 LYS   A N   1 
ATOM   3408 C  CA  . LYS   A 1 472 ? -8.584  -5.984  -25.158 1.00 156.65 ? 492 LYS   A CA  1 
ATOM   3409 C  C   . LYS   A 1 472 ? -9.938  -5.439  -24.726 1.00 152.87 ? 492 LYS   A C   1 
ATOM   3410 O  O   . LYS   A 1 472 ? -10.984 -5.896  -25.196 1.00 139.96 ? 492 LYS   A O   1 
ATOM   3411 C  CB  . LYS   A 1 472 ? -8.136  -5.307  -26.455 1.00 151.67 ? 492 LYS   A CB  1 
ATOM   3412 C  CG  . LYS   A 1 472 ? -7.331  -4.036  -26.229 1.00 147.90 ? 492 LYS   A CG  1 
ATOM   3413 C  CD  . LYS   A 1 472 ? -6.916  -3.382  -27.537 1.00 169.50 ? 492 LYS   A CD  1 
ATOM   3414 C  CE  . LYS   A 1 472 ? -8.101  -2.738  -28.235 1.00 172.19 ? 492 LYS   A CE  1 
ATOM   3415 N  NZ  . LYS   A 1 472 ? -7.680  -1.954  -29.430 1.00 140.93 ? 492 LYS   A NZ  1 
ATOM   3416 N  N   . VAL   A 1 473 ? -9.912  -4.461  -23.826 1.00 155.89 ? 493 VAL   A N   1 
ATOM   3417 C  CA  . VAL   A 1 473 ? -11.119 -3.877  -23.254 1.00 150.92 ? 493 VAL   A CA  1 
ATOM   3418 C  C   . VAL   A 1 473 ? -11.156 -2.400  -23.618 1.00 160.92 ? 493 VAL   A C   1 
ATOM   3419 O  O   . VAL   A 1 473 ? -10.148 -1.696  -23.481 1.00 159.64 ? 493 VAL   A O   1 
ATOM   3420 C  CB  . VAL   A 1 473 ? -11.172 -4.070  -21.728 1.00 145.43 ? 493 VAL   A CB  1 
ATOM   3421 C  CG1 . VAL   A 1 473 ? -12.501 -3.582  -21.177 1.00 134.13 ? 493 VAL   A CG1 1 
ATOM   3422 C  CG2 . VAL   A 1 473 ? -10.945 -5.531  -21.370 1.00 143.52 ? 493 VAL   A CG2 1 
ATOM   3423 N  N   . GLU   A 1 474 ? -12.314 -1.934  -24.082 1.00 163.06 ? 494 GLU   A N   1 
ATOM   3424 C  CA  . GLU   A 1 474 ? -12.507 -0.544  -24.466 1.00 157.55 ? 494 GLU   A CA  1 
ATOM   3425 C  C   . GLU   A 1 474 ? -13.736 0.010   -23.760 1.00 159.73 ? 494 GLU   A C   1 
ATOM   3426 O  O   . GLU   A 1 474 ? -14.733 -0.696  -23.585 1.00 146.75 ? 494 GLU   A O   1 
ATOM   3427 C  CB  . GLU   A 1 474 ? -12.657 -0.401  -25.986 1.00 152.36 ? 494 GLU   A CB  1 
ATOM   3428 C  CG  . GLU   A 1 474 ? -11.395 -0.751  -26.762 1.00 166.23 ? 494 GLU   A CG  1 
ATOM   3429 C  CD  . GLU   A 1 474 ? -11.619 -0.788  -28.262 1.00 179.11 ? 494 GLU   A CD  1 
ATOM   3430 O  OE1 . GLU   A 1 474 ? -12.751 -1.097  -28.690 1.00 174.90 ? 494 GLU   A OE1 1 
ATOM   3431 O  OE2 . GLU   A 1 474 ? -10.661 -0.505  -29.012 1.00 171.00 ? 494 GLU   A OE2 1 
ATOM   3432 N  N   . SER   A 1 475 ? -13.660 1.275   -23.358 1.00 172.45 ? 495 SER   A N   1 
ATOM   3433 C  CA  . SER   A 1 475 ? -14.708 1.902   -22.563 1.00 169.17 ? 495 SER   A CA  1 
ATOM   3434 C  C   . SER   A 1 475 ? -15.708 2.611   -23.467 1.00 175.25 ? 495 SER   A C   1 
ATOM   3435 O  O   . SER   A 1 475 ? -15.319 3.322   -24.400 1.00 182.90 ? 495 SER   A O   1 
ATOM   3436 C  CB  . SER   A 1 475 ? -14.106 2.890   -21.564 1.00 171.28 ? 495 SER   A CB  1 
ATOM   3437 O  OG  . SER   A 1 475 ? -15.110 3.458   -20.743 1.00 175.27 ? 495 SER   A OG  1 
ATOM   3438 N  N   . ARG   A 1 476 ? -16.993 2.418   -23.183 1.00 170.56 ? 496 ARG   A N   1 
ATOM   3439 C  CA  . ARG   A 1 476 ? -18.057 3.040   -23.962 1.00 166.39 ? 496 ARG   A CA  1 
ATOM   3440 C  C   . ARG   A 1 476 ? -18.383 4.431   -23.427 1.00 163.23 ? 496 ARG   A C   1 
ATOM   3441 O  O   . ARG   A 1 476 ? -17.956 5.439   -23.990 1.00 166.98 ? 496 ARG   A O   1 
ATOM   3442 C  CB  . ARG   A 1 476 ? -19.313 2.166   -23.947 1.00 153.91 ? 496 ARG   A CB  1 
ATOM   3443 C  CG  . ARG   A 1 476 ? -19.047 0.688   -24.184 1.00 149.84 ? 496 ARG   A CG  1 
ATOM   3444 C  CD  . ARG   A 1 476 ? -20.334 -0.119  -24.120 1.00 150.12 ? 496 ARG   A CD  1 
ATOM   3445 N  NE  . ARG   A 1 476 ? -21.178 0.106   -25.287 1.00 150.20 ? 496 ARG   A NE  1 
ATOM   3446 C  CZ  . ARG   A 1 476 ? -22.421 -0.339  -25.409 1.00 153.71 ? 496 ARG   A CZ  1 
ATOM   3447 N  NH1 . ARG   A 1 476 ? -23.010 -1.019  -24.438 1.00 145.92 ? 496 ARG   A NH1 1 
ATOM   3448 N  NH2 . ARG   A 1 476 ? -23.091 -0.095  -26.532 1.00 146.96 ? 496 ARG   A NH2 1 
HETATM 3449 C  CHA . HEM   B 2 .   ? -23.315 -30.533 -9.282  1.00 94.50  ? 601 HEM   A CHA 1 
HETATM 3450 C  CHB . HEM   B 2 .   ? -22.667 -27.854 -13.286 1.00 93.88  ? 601 HEM   A CHB 1 
HETATM 3451 C  CHC . HEM   B 2 .   ? -22.176 -23.873 -10.563 1.00 92.16  ? 601 HEM   A CHC 1 
HETATM 3452 C  CHD . HEM   B 2 .   ? -22.900 -26.526 -6.557  1.00 97.15  ? 601 HEM   A CHD 1 
HETATM 3453 C  C1A . HEM   B 2 .   ? -23.178 -30.162 -10.603 1.00 99.78  ? 601 HEM   A C1A 1 
HETATM 3454 C  C2A . HEM   B 2 .   ? -23.246 -31.041 -11.753 1.00 94.86  ? 601 HEM   A C2A 1 
HETATM 3455 C  C3A . HEM   B 2 .   ? -23.065 -30.300 -12.851 1.00 82.57  ? 601 HEM   A C3A 1 
HETATM 3456 C  C4A . HEM   B 2 .   ? -22.879 -28.924 -12.444 1.00 77.36  ? 601 HEM   A C4A 1 
HETATM 3457 C  CMA . HEM   B 2 .   ? -23.056 -30.805 -14.309 1.00 91.00  ? 601 HEM   A CMA 1 
HETATM 3458 C  CAA . HEM   B 2 .   ? -23.478 -32.568 -11.708 1.00 86.38  ? 601 HEM   A CAA 1 
HETATM 3459 C  CBA . HEM   B 2 .   ? -24.930 -32.891 -12.044 1.00 85.94  ? 601 HEM   A CBA 1 
HETATM 3460 C  CGA . HEM   B 2 .   ? -25.116 -34.386 -12.070 1.00 91.73  ? 601 HEM   A CGA 1 
HETATM 3461 O  O1A . HEM   B 2 .   ? -26.203 -34.848 -12.503 1.00 86.75  ? 601 HEM   A O1A 1 
HETATM 3462 O  O2A . HEM   B 2 .   ? -24.176 -35.116 -11.662 1.00 94.53  ? 601 HEM   A O2A 1 
HETATM 3463 C  C1B . HEM   B 2 .   ? -22.486 -26.543 -12.905 1.00 91.39  ? 601 HEM   A C1B 1 
HETATM 3464 C  C2B . HEM   B 2 .   ? -22.289 -25.418 -13.798 1.00 93.12  ? 601 HEM   A C2B 1 
HETATM 3465 C  C3B . HEM   B 2 .   ? -22.152 -24.310 -13.044 1.00 99.65  ? 601 HEM   A C3B 1 
HETATM 3466 C  C4B . HEM   B 2 .   ? -22.260 -24.711 -11.654 1.00 95.99  ? 601 HEM   A C4B 1 
HETATM 3467 C  CMB . HEM   B 2 .   ? -22.255 -25.556 -15.338 1.00 98.81  ? 601 HEM   A CMB 1 
HETATM 3468 C  CAB . HEM   B 2 .   ? -21.919 -22.835 -13.470 1.00 103.38 ? 601 HEM   A CAB 1 
HETATM 3469 C  CBB . HEM   B 2 .   ? -21.815 -22.410 -14.735 1.00 95.35  ? 601 HEM   A CBB 1 
HETATM 3470 C  C1C . HEM   B 2 .   ? -22.379 -24.227 -9.246  1.00 99.83  ? 601 HEM   A C1C 1 
HETATM 3471 C  C2C . HEM   B 2 .   ? -22.468 -23.317 -8.125  1.00 116.14 ? 601 HEM   A C2C 1 
HETATM 3472 C  C3C . HEM   B 2 .   ? -22.668 -24.029 -7.012  1.00 108.35 ? 601 HEM   A C3C 1 
HETATM 3473 C  C4C . HEM   B 2 .   ? -22.715 -25.437 -7.387  1.00 99.91  ? 601 HEM   A C4C 1 
HETATM 3474 C  CMC . HEM   B 2 .   ? -22.350 -21.779 -8.202  1.00 105.60 ? 601 HEM   A CMC 1 
HETATM 3475 C  CAC . HEM   B 2 .   ? -22.813 -23.398 -5.605  1.00 96.22  ? 601 HEM   A CAC 1 
HETATM 3476 C  CBC . HEM   B 2 .   ? -22.959 -24.121 -4.489  1.00 109.61 ? 601 HEM   A CBC 1 
HETATM 3477 C  C1D . HEM   B 2 .   ? -23.028 -27.846 -6.939  1.00 99.71  ? 601 HEM   A C1D 1 
HETATM 3478 C  C2D . HEM   B 2 .   ? -23.120 -28.990 -6.052  1.00 99.93  ? 601 HEM   A C2D 1 
HETATM 3479 C  C3D . HEM   B 2 .   ? -23.234 -30.090 -6.800  1.00 87.23  ? 601 HEM   A C3D 1 
HETATM 3480 C  C4D . HEM   B 2 .   ? -23.220 -29.692 -8.193  1.00 94.20  ? 601 HEM   A C4D 1 
HETATM 3481 C  CMD . HEM   B 2 .   ? -23.090 -28.951 -4.509  1.00 102.73 ? 601 HEM   A CMD 1 
HETATM 3482 C  CAD . HEM   B 2 .   ? -23.364 -31.533 -6.268  1.00 85.80  ? 601 HEM   A CAD 1 
HETATM 3483 C  CBD . HEM   B 2 .   ? -24.827 -31.950 -6.381  1.00 102.00 ? 601 HEM   A CBD 1 
HETATM 3484 C  CGD . HEM   B 2 .   ? -25.110 -33.126 -5.484  1.00 102.18 ? 601 HEM   A CGD 1 
HETATM 3485 O  O1D . HEM   B 2 .   ? -26.246 -33.203 -4.948  1.00 85.29  ? 601 HEM   A O1D 1 
HETATM 3486 O  O2D . HEM   B 2 .   ? -24.204 -33.977 -5.294  1.00 112.39 ? 601 HEM   A O2D 1 
HETATM 3487 N  NA  . HEM   B 2 .   ? -22.955 -28.877 -11.064 1.00 94.40  ? 601 HEM   A NA  1 
HETATM 3488 N  NB  . HEM   B 2 .   ? -22.463 -26.075 -11.607 1.00 90.50  ? 601 HEM   A NB  1 
HETATM 3489 N  NC  . HEM   B 2 .   ? -22.534 -25.511 -8.758  1.00 91.43  ? 601 HEM   A NC  1 
HETATM 3490 N  ND  . HEM   B 2 .   ? -23.093 -28.316 -8.238  1.00 93.02  ? 601 HEM   A ND  1 
HETATM 3491 FE FE  . HEM   B 2 .   ? -22.743 -27.197 -9.914  1.00 90.71  ? 601 HEM   A FE  1 
HETATM 3492 C  C10 . A1A4U C 3 .   ? -19.887 -27.891 -11.013 1.00 101.06 ? 602 A1A4U A C10 1 
HETATM 3493 C  C11 . A1A4U C 3 .   ? -18.475 -27.976 -10.950 1.00 102.44 ? 602 A1A4U A C11 1 
HETATM 3494 C  C12 . A1A4U C 3 .   ? -17.841 -27.972 -9.674  1.00 103.56 ? 602 A1A4U A C12 1 
HETATM 3495 C  C13 . A1A4U C 3 .   ? -14.894 -32.806 -6.172  1.00 136.52 ? 602 A1A4U A C13 1 
HETATM 3496 C  C14 . A1A4U C 3 .   ? -13.875 -32.476 -5.039  1.00 143.65 ? 602 A1A4U A C14 1 
HETATM 3497 C  C15 . A1A4U C 3 .   ? -13.589 -30.978 -4.751  1.00 139.59 ? 602 A1A4U A C15 1 
HETATM 3498 C  C16 . A1A4U C 3 .   ? -12.895 -30.171 -5.686  1.00 134.52 ? 602 A1A4U A C16 1 
HETATM 3499 C  C17 . A1A4U C 3 .   ? -12.634 -28.803 -5.422  1.00 134.21 ? 602 A1A4U A C17 1 
HETATM 3500 C  C18 . A1A4U C 3 .   ? -13.063 -28.215 -4.213  1.00 130.45 ? 602 A1A4U A C18 1 
HETATM 3501 C  C19 . A1A4U C 3 .   ? -13.754 -29.007 -3.276  1.00 129.56 ? 602 A1A4U A C19 1 
HETATM 3502 C  C20 . A1A4U C 3 .   ? -14.008 -30.377 -3.554  1.00 136.91 ? 602 A1A4U A C20 1 
HETATM 3503 C  C22 . A1A4U C 3 .   ? -16.966 -35.122 -6.675  1.00 129.39 ? 602 A1A4U A C22 1 
HETATM 3504 C  C23 . A1A4U C 3 .   ? -17.166 -35.031 -8.265  1.00 136.73 ? 602 A1A4U A C23 1 
HETATM 3505 C  C24 . A1A4U C 3 .   ? -18.688 -34.726 -8.661  1.00 125.15 ? 602 A1A4U A C24 1 
HETATM 3506 C  C02 . A1A4U C 3 .   ? -16.232 -32.051 -6.083  1.00 127.57 ? 602 A1A4U A C02 1 
HETATM 3507 C  C04 . A1A4U C 3 .   ? -18.093 -30.556 -7.088  1.00 112.19 ? 602 A1A4U A C04 1 
HETATM 3508 C  C05 . A1A4U C 3 .   ? -18.043 -29.217 -6.263  1.00 109.59 ? 602 A1A4U A C05 1 
HETATM 3509 C  C06 . A1A4U C 3 .   ? -17.973 -27.876 -7.080  1.00 109.49 ? 602 A1A4U A C06 1 
HETATM 3510 C  C07 . A1A4U C 3 .   ? -18.615 -27.889 -8.488  1.00 91.47  ? 602 A1A4U A C07 1 
HETATM 3511 C  C08 . A1A4U C 3 .   ? -20.025 -27.806 -8.655  1.00 89.26  ? 602 A1A4U A C08 1 
HETATM 3512 C  C25 . A1A4U C 3 .   ? -18.909 -33.511 -9.627  1.00 117.09 ? 602 A1A4U A C25 1 
HETATM 3513 C  C26 . A1A4U C 3 .   ? -19.844 -32.516 -9.290  1.00 108.40 ? 602 A1A4U A C26 1 
HETATM 3514 C  C27 . A1A4U C 3 .   ? -20.084 -31.391 -10.125 1.00 107.41 ? 602 A1A4U A C27 1 
HETATM 3515 C  C28 . A1A4U C 3 .   ? -19.381 -31.250 -11.333 1.00 109.08 ? 602 A1A4U A C28 1 
HETATM 3516 C  C29 . A1A4U C 3 .   ? -18.443 -32.237 -11.684 1.00 124.47 ? 602 A1A4U A C29 1 
HETATM 3517 C  C30 . A1A4U C 3 .   ? -18.207 -33.364 -10.838 1.00 127.23 ? 602 A1A4U A C30 1 
HETATM 3518 C  C35 . A1A4U C 3 .   ? -14.386 -34.865 -10.453 1.00 159.18 ? 602 A1A4U A C35 1 
HETATM 3519 C  C36 . A1A4U C 3 .   ? -14.890 -33.558 -10.163 1.00 149.82 ? 602 A1A4U A C36 1 
HETATM 3520 C  C37 . A1A4U C 3 .   ? -14.212 -32.363 -10.545 1.00 149.97 ? 602 A1A4U A C37 1 
HETATM 3521 C  C38 . A1A4U C 3 .   ? -12.988 -32.432 -11.247 1.00 161.31 ? 602 A1A4U A C38 1 
HETATM 3522 C  C39 . A1A4U C 3 .   ? -12.443 -33.698 -11.566 1.00 162.53 ? 602 A1A4U A C39 1 
HETATM 3523 C  C40 . A1A4U C 3 .   ? -13.147 -34.874 -11.168 1.00 164.53 ? 602 A1A4U A C40 1 
HETATM 3524 N  N03 . A1A4U C 3 .   ? -16.796 -31.293 -7.165  1.00 121.86 ? 602 A1A4U A N03 1 
HETATM 3525 N  N09 . A1A4U C 3 .   ? -20.630 -27.810 -9.876  1.00 90.17  ? 602 A1A4U A N09 1 
HETATM 3526 N  N31 . A1A4U C 3 .   ? -16.692 -36.254 -9.060  1.00 155.45 ? 602 A1A4U A N31 1 
HETATM 3527 O  O01 . A1A4U C 3 .   ? -16.876 -32.101 -5.022  1.00 123.32 ? 602 A1A4U A O01 1 
HETATM 3528 O  O33 . A1A4U C 3 .   ? -14.333 -37.210 -9.158  1.00 166.04 ? 602 A1A4U A O33 1 
HETATM 3529 O  O34 . A1A4U C 3 .   ? -15.416 -37.286 -11.133 1.00 177.84 ? 602 A1A4U A O34 1 
HETATM 3530 S  S21 . A1A4U C 3 .   ? -15.205 -34.670 -6.174  1.00 154.71 ? 602 A1A4U A S21 1 
HETATM 3531 S  S32 . A1A4U C 3 .   ? -15.258 -36.458 -9.961  1.00 190.64 ? 602 A1A4U A S32 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   ? 1.6392 1.5078 1.8264 0.2962  -0.0808 -0.1447 29  SER   A N   
2    C  CA  . SER   A 9   ? 1.6005 1.4954 1.8017 0.2587  -0.0671 -0.1296 29  SER   A CA  
3    C  C   . SER   A 9   ? 1.4942 1.4432 1.6988 0.2545  -0.0658 -0.1490 29  SER   A C   
4    O  O   . SER   A 9   ? 1.3374 1.3021 1.5546 0.2256  -0.0582 -0.1421 29  SER   A O   
5    C  CB  . SER   A 9   ? 1.3066 1.2330 1.5006 0.2509  -0.0534 -0.1025 29  SER   A CB  
6    O  OG  . SER   A 9   ? 1.5393 1.4874 1.7437 0.2175  -0.0396 -0.0891 29  SER   A OG  
7    N  N   . HIS   A 10  ? 1.4036 1.3800 1.5948 0.2858  -0.0719 -0.1722 30  HIS   A N   
8    C  CA  . HIS   A 10  ? 1.2740 1.3003 1.4597 0.2878  -0.0686 -0.1896 30  HIS   A CA  
9    C  C   . HIS   A 10  ? 1.3485 1.3348 1.5281 0.2899  -0.0854 -0.2164 30  HIS   A C   
10   O  O   . HIS   A 10  ? 1.4080 1.4277 1.5752 0.2937  -0.0847 -0.2319 30  HIS   A O   
11   C  CB  . HIS   A 10  ? 1.3981 1.4810 1.5719 0.3220  -0.0620 -0.1992 30  HIS   A CB  
12   C  CG  . HIS   A 10  ? 1.4604 1.6084 1.6458 0.3119  -0.0457 -0.1771 30  HIS   A CG  
13   N  ND1 . HIS   A 10  ? 1.4262 1.6460 1.6128 0.3222  -0.0328 -0.1806 30  HIS   A ND1 
14   C  CD2 . HIS   A 10  ? 1.4521 1.6016 1.6478 0.2922  -0.0412 -0.1515 30  HIS   A CD2 
15   C  CE1 . HIS   A 10  ? 1.4336 1.6966 1.6365 0.3067  -0.0233 -0.1588 30  HIS   A CE1 
16   N  NE2 . HIS   A 10  ? 1.2687 1.4888 1.4737 0.2897  -0.0295 -0.1424 30  HIS   A NE2 
17   N  N   . GLY   A 11  ? 1.4155 1.3295 1.6026 0.2875  -0.1016 -0.2220 31  GLY   A N   
18   C  CA  . GLY   A 11  ? 1.3682 1.2378 1.5544 0.2863  -0.1233 -0.2486 31  GLY   A CA  
19   C  C   . GLY   A 11  ? 1.4707 1.3157 1.6896 0.2454  -0.1282 -0.2384 31  GLY   A C   
20   O  O   . GLY   A 11  ? 1.6488 1.4492 1.8766 0.2405  -0.1510 -0.2593 31  GLY   A O   
21   N  N   . LEU   A 12  ? 1.6019 1.4752 1.8408 0.2170  -0.1084 -0.2080 32  LEU   A N   
22   C  CA  . LEU   A 12  ? 1.4741 1.3268 1.7502 0.1798  -0.1092 -0.1952 32  LEU   A CA  
23   C  C   . LEU   A 12  ? 1.4736 1.3454 1.7547 0.1712  -0.1235 -0.2158 32  LEU   A C   
24   O  O   . LEU   A 12  ? 1.5908 1.4284 1.9042 0.1511  -0.1401 -0.2222 32  LEU   A O   
25   C  CB  . LEU   A 12  ? 1.3219 1.2037 1.6095 0.1574  -0.0826 -0.1600 32  LEU   A CB  
26   C  CG  . LEU   A 12  ? 1.3972 1.2702 1.7246 0.1210  -0.0759 -0.1428 32  LEU   A CG  
27   C  CD1 . LEU   A 12  ? 1.6226 1.4288 1.9838 0.1083  -0.0868 -0.1409 32  LEU   A CD1 
28   C  CD2 . LEU   A 12  ? 1.3600 1.2588 1.6860 0.1065  -0.0482 -0.1104 32  LEU   A CD2 
29   N  N   . PHE   A 13  ? 1.4251 1.3513 1.6760 0.1861  -0.1181 -0.2255 33  PHE   A N   
30   C  CA  . PHE   A 13  ? 1.4212 1.3653 1.6667 0.1820  -0.1317 -0.2435 33  PHE   A CA  
31   C  C   . PHE   A 13  ? 1.6379 1.5492 1.8561 0.2087  -0.1602 -0.2818 33  PHE   A C   
32   O  O   . PHE   A 13  ? 1.6763 1.5765 1.8975 0.2019  -0.1827 -0.3002 33  PHE   A O   
33   C  CB  . PHE   A 13  ? 1.4120 1.4243 1.6341 0.1854  -0.1112 -0.2337 33  PHE   A CB  
34   C  CG  . PHE   A 13  ? 1.4002 1.4399 1.6475 0.1561  -0.0890 -0.2010 33  PHE   A CG  
35   C  CD1 . PHE   A 13  ? 1.3350 1.3541 1.6219 0.1263  -0.0922 -0.1893 33  PHE   A CD1 
36   C  CD2 . PHE   A 13  ? 1.2286 1.3136 1.4622 0.1591  -0.0654 -0.1826 33  PHE   A CD2 
37   C  CE1 . PHE   A 13  ? 1.2530 1.2939 1.5583 0.1033  -0.0703 -0.1606 33  PHE   A CE1 
38   C  CE2 . PHE   A 13  ? 1.1476 1.2506 1.3987 0.1340  -0.0475 -0.1554 33  PHE   A CE2 
39   C  CZ  . PHE   A 13  ? 1.2988 1.3783 1.5822 0.1077  -0.0488 -0.1447 33  PHE   A CZ  
40   N  N   . LYS   A 14  ? 1.7101 1.6040 1.9002 0.2412  -0.1617 -0.2956 34  LYS   A N   
41   C  CA  . LYS   A 14  ? 1.8013 1.6477 1.9653 0.2672  -0.1910 -0.3335 34  LYS   A CA  
42   C  C   . LYS   A 14  ? 1.7905 1.5647 1.9936 0.2459  -0.2176 -0.3402 34  LYS   A C   
43   O  O   . LYS   A 14  ? 1.8444 1.5808 2.0421 0.2492  -0.2498 -0.3707 34  LYS   A O   
44   C  CB  . LYS   A 14  ? 1.9684 1.8120 2.0965 0.3092  -0.1842 -0.3452 34  LYS   A CB  
45   C  CG  . LYS   A 14  ? 2.0430 1.9566 2.1333 0.3358  -0.1613 -0.3458 34  LYS   A CG  
46   C  CD  . LYS   A 14  ? 2.2498 2.1600 2.3128 0.3798  -0.1559 -0.3590 34  LYS   A CD  
47   C  CE  . LYS   A 14  ? 2.2574 2.2436 2.2925 0.4052  -0.1293 -0.3566 34  LYS   A CE  
48   N  NZ  . LYS   A 14  ? 2.2679 2.2582 2.2851 0.4496  -0.1219 -0.3678 34  LYS   A NZ  
49   N  N   . LYS   A 15  ? 1.6488 1.4016 1.8908 0.2238  -0.2048 -0.3115 35  LYS   A N   
50   C  CA  . LYS   A 15  ? 1.6636 1.3504 1.9515 0.1989  -0.2243 -0.3110 35  LYS   A CA  
51   C  C   . LYS   A 15  ? 1.6878 1.3850 2.0177 0.1647  -0.2374 -0.3109 35  LYS   A C   
52   O  O   . LYS   A 15  ? 1.7226 1.3759 2.0732 0.1568  -0.2711 -0.3351 35  LYS   A O   
53   C  CB  . LYS   A 15  ? 1.7227 1.3903 2.0376 0.1836  -0.2009 -0.2743 35  LYS   A CB  
54   C  CG  . LYS   A 15  ? 1.8425 1.4647 2.2188 0.1450  -0.2066 -0.2581 35  LYS   A CG  
55   C  CD  . LYS   A 15  ? 1.8974 1.5304 2.2953 0.1244  -0.1718 -0.2131 35  LYS   A CD  
56   C  CE  . LYS   A 15  ? 1.9729 1.5772 2.4372 0.0838  -0.1700 -0.1932 35  LYS   A CE  
57   N  NZ  . LYS   A 15  ? 1.8379 1.4543 2.3151 0.0665  -0.1324 -0.1491 35  LYS   A NZ  
58   N  N   . LEU   A 16  ? 1.6497 1.4042 1.9942 0.1449  -0.2130 -0.2846 36  LEU   A N   
59   C  CA  . LEU   A 16  ? 1.5628 1.3336 1.9521 0.1137  -0.2217 -0.2800 36  LEU   A CA  
60   C  C   . LEU   A 16  ? 1.6830 1.4713 2.0456 0.1264  -0.2495 -0.3122 36  LEU   A C   
61   O  O   . LEU   A 16  ? 1.7714 1.5723 2.1709 0.1038  -0.2632 -0.3122 36  LEU   A O   
62   C  CB  . LEU   A 16  ? 1.5401 1.3636 1.9458 0.0937  -0.1860 -0.2429 36  LEU   A CB  
63   C  CG  . LEU   A 16  ? 1.5741 1.3794 2.0105 0.0754  -0.1586 -0.2073 36  LEU   A CG  
64   C  CD1 . LEU   A 16  ? 1.5245 1.3825 1.9573 0.0647  -0.1249 -0.1770 36  LEU   A CD1 
65   C  CD2 . LEU   A 16  ? 1.5262 1.2888 2.0301 0.0451  -0.1698 -0.2005 36  LEU   A CD2 
66   N  N   . GLY   A 17  ? 1.6169 1.4065 1.9158 0.1636  -0.2578 -0.3388 37  GLY   A N   
67   C  CA  . GLY   A 17  ? 1.6538 1.4587 1.9152 0.1794  -0.2814 -0.3675 37  GLY   A CA  
68   C  C   . GLY   A 17  ? 1.7756 1.6470 2.0274 0.1719  -0.2605 -0.3484 37  GLY   A C   
69   O  O   . GLY   A 17  ? 1.8150 1.6969 2.0616 0.1691  -0.2820 -0.3619 37  GLY   A O   
70   N  N   . ILE   A 18  ? 1.7644 1.6778 2.0131 0.1688  -0.2215 -0.3175 38  ILE   A N   
71   C  CA  . ILE   A 18  ? 1.6818 1.6545 1.9221 0.1603  -0.1990 -0.2966 38  ILE   A CA  
72   C  C   . ILE   A 18  ? 1.5880 1.5965 1.7649 0.1929  -0.1820 -0.3024 38  ILE   A C   
73   O  O   . ILE   A 18  ? 1.6381 1.6528 1.8032 0.2073  -0.1626 -0.2955 38  ILE   A O   
74   C  CB  . ILE   A 18  ? 1.5937 1.5865 1.8761 0.1322  -0.1684 -0.2582 38  ILE   A CB  
75   C  CG1 . ILE   A 18  ? 1.5387 1.5047 1.8870 0.0999  -0.1803 -0.2495 38  ILE   A CG1 
76   C  CG2 . ILE   A 18  ? 1.4954 1.5454 1.7601 0.1283  -0.1440 -0.2384 38  ILE   A CG2 
77   C  CD1 . ILE   A 18  ? 1.5180 1.4939 1.9030 0.0758  -0.1488 -0.2129 38  ILE   A CD1 
78   N  N   . PRO   A 19  ? 1.4675 1.5010 1.6047 0.2060  -0.1876 -0.3134 39  PRO   A N   
79   C  CA  . PRO   A 19  ? 1.5863 1.6543 1.6648 0.2380  -0.1682 -0.3176 39  PRO   A CA  
80   C  C   . PRO   A 19  ? 1.6435 1.7650 1.7316 0.2275  -0.1288 -0.2835 39  PRO   A C   
81   O  O   . PRO   A 19  ? 1.5756 1.7092 1.7040 0.1969  -0.1175 -0.2578 39  PRO   A O   
82   C  CB  . PRO   A 19  ? 1.5581 1.6341 1.5943 0.2494  -0.1846 -0.3331 39  PRO   A CB  
83   C  CG  . PRO   A 19  ? 1.3278 1.3996 1.4117 0.2152  -0.1997 -0.3215 39  PRO   A CG  
84   C  CD  . PRO   A 19  ? 1.4802 1.5132 1.6255 0.1929  -0.2112 -0.3202 39  PRO   A CD  
85   N  N   . GLY   A 20  ? 1.5160 1.6695 1.5672 0.2545  -0.1080 -0.2844 40  GLY   A N   
86   C  CA  . GLY   A 20  ? 1.4044 1.6106 1.4658 0.2466  -0.0739 -0.2552 40  GLY   A CA  
87   C  C   . GLY   A 20  ? 1.5097 1.7459 1.5433 0.2797  -0.0551 -0.2606 40  GLY   A C   
88   O  O   . GLY   A 20  ? 1.5290 1.7391 1.5375 0.3105  -0.0670 -0.2867 40  GLY   A O   
89   N  N   . PRO   A 21  ? 1.5086 1.8007 1.5495 0.2744  -0.0255 -0.2364 41  PRO   A N   
90   C  CA  . PRO   A 21  ? 1.4892 1.8209 1.5152 0.3047  -0.0045 -0.2382 41  PRO   A CA  
91   C  C   . PRO   A 21  ? 1.4056 1.7190 1.4535 0.3180  -0.0100 -0.2447 41  PRO   A C   
92   O  O   . PRO   A 21  ? 1.3431 1.6285 1.4242 0.2962  -0.0197 -0.2351 41  PRO   A O   
93   C  CB  . PRO   A 21  ? 1.4040 1.7967 1.4496 0.2849  0.0244  -0.2068 41  PRO   A CB  
94   C  CG  . PRO   A 21  ? 1.3786 1.7532 1.4565 0.2450  0.0168  -0.1888 41  PRO   A CG  
95   C  CD  . PRO   A 21  ? 1.2242 1.5455 1.2906 0.2404  -0.0105 -0.2065 41  PRO   A CD  
96   N  N   . THR   A 22  ? 1.4638 1.7921 1.4901 0.3567  -0.0022 -0.2601 42  THR   A N   
97   C  CA  . THR   A 22  ? 1.3139 1.6236 1.3560 0.3765  -0.0083 -0.2680 42  THR   A CA  
98   C  C   . THR   A 22  ? 1.2959 1.6530 1.3809 0.3627  0.0093  -0.2401 42  THR   A C   
99   O  O   . THR   A 22  ? 1.1468 1.5696 1.2389 0.3679  0.0338  -0.2269 42  THR   A O   
100  C  CB  . THR   A 22  ? 1.4482 1.7619 1.4534 0.4261  -0.0041 -0.2938 42  THR   A CB  
101  O  OG1 . THR   A 22  ? 1.4156 1.6853 1.3728 0.4396  -0.0225 -0.3214 42  THR   A OG1 
102  C  CG2 . THR   A 22  ? 1.4540 1.7356 1.4726 0.4492  -0.0156 -0.3050 42  THR   A CG2 
103  N  N   . PRO   A 23  ? 1.1876 1.5135 1.3012 0.3452  -0.0026 -0.2298 43  PRO   A N   
104  C  CA  . PRO   A 23  ? 0.9919 1.3584 1.1404 0.3327  0.0092  -0.2049 43  PRO   A CA  
105  C  C   . PRO   A 23  ? 1.3735 1.7662 1.5312 0.3688  0.0136  -0.2105 43  PRO   A C   
106  O  O   . PRO   A 23  ? 1.4373 1.7936 1.5777 0.4008  0.0023  -0.2321 43  PRO   A O   
107  C  CB  . PRO   A 23  ? 1.1913 1.5038 1.3556 0.3051  -0.0062 -0.1937 43  PRO   A CB  
108  C  CG  . PRO   A 23  ? 1.2480 1.4915 1.3946 0.3181  -0.0270 -0.2167 43  PRO   A CG  
109  C  CD  . PRO   A 23  ? 1.1888 1.4391 1.3040 0.3337  -0.0276 -0.2388 43  PRO   A CD  
110  N  N   . LEU   A 24  ? 1.2561 1.7126 1.4442 0.3635  0.0286  -0.1911 44  LEU   A N   
111  C  CA  . LEU   A 24  ? 1.1345 1.6252 1.3446 0.3936  0.0310  -0.1914 44  LEU   A CA  
112  C  C   . LEU   A 24  ? 1.2288 1.6830 1.4551 0.3854  0.0124  -0.1809 44  LEU   A C   
113  O  O   . LEU   A 24  ? 1.1099 1.5330 1.3373 0.3510  0.0054  -0.1666 44  LEU   A O   
114  C  CB  . LEU   A 24  ? 1.0208 1.6020 1.2638 0.3900  0.0540  -0.1750 44  LEU   A CB  
115  C  CG  . LEU   A 24  ? 1.2305 1.8565 1.4576 0.4033  0.0790  -0.1808 44  LEU   A CG  
116  C  CD1 . LEU   A 24  ? 1.0926 1.8071 1.3632 0.3924  0.1026  -0.1588 44  LEU   A CD1 
117  C  CD2 . LEU   A 24  ? 1.2767 1.8924 1.4765 0.4538  0.0815  -0.2071 44  LEU   A CD2 
118  N  N   . PRO   A 25  ? 1.1727 1.6270 1.4082 0.4190  0.0047  -0.1871 45  PRO   A N   
119  C  CA  . PRO   A 25  ? 1.2464 1.6642 1.4911 0.4146  -0.0133 -0.1748 45  PRO   A CA  
120  C  C   . PRO   A 25  ? 1.2632 1.7230 1.5348 0.3837  -0.0112 -0.1498 45  PRO   A C   
121  O  O   . PRO   A 25  ? 1.1883 1.7232 1.4880 0.3796  0.0021  -0.1428 45  PRO   A O   
122  C  CB  . PRO   A 25  ? 1.3364 1.7653 1.5894 0.4622  -0.0192 -0.1862 45  PRO   A CB  
123  C  CG  . PRO   A 25  ? 1.2604 1.6923 1.4925 0.4920  -0.0089 -0.2114 45  PRO   A CG  
124  C  CD  . PRO   A 25  ? 1.1062 1.5836 1.3372 0.4667  0.0112  -0.2070 45  PRO   A CD  
125  N  N   . PHE   A 26  ? 1.2863 1.6938 1.5478 0.3615  -0.0240 -0.1363 46  PHE   A N   
126  C  CA  . PHE   A 26  ? 1.1749 1.6039 1.4503 0.3334  -0.0266 -0.1148 46  PHE   A CA  
127  C  C   . PHE   A 26  ? 1.1056 1.5668 1.3870 0.2976  -0.0115 -0.1070 46  PHE   A C   
128  O  O   . PHE   A 26  ? 1.3241 1.7530 1.5933 0.2671  -0.0127 -0.0948 46  PHE   A O   
129  C  CB  . PHE   A 26  ? 1.0625 1.5516 1.3699 0.3529  -0.0336 -0.1096 46  PHE   A CB  
130  C  CG  . PHE   A 26  ? 1.3947 1.8501 1.6952 0.3885  -0.0515 -0.1136 46  PHE   A CG  
131  C  CD1 . PHE   A 26  ? 1.5377 1.9425 1.8194 0.3833  -0.0689 -0.0997 46  PHE   A CD1 
132  C  CD2 . PHE   A 26  ? 1.5527 2.0237 1.8612 0.4297  -0.0501 -0.1307 46  PHE   A CD2 
133  C  CE1 . PHE   A 26  ? 1.8363 2.2055 2.1079 0.4174  -0.0857 -0.1011 46  PHE   A CE1 
134  C  CE2 . PHE   A 26  ? 1.5832 2.0192 1.8845 0.4646  -0.0675 -0.1340 46  PHE   A CE2 
135  C  CZ  . PHE   A 26  ? 1.7930 2.1774 2.0762 0.4578  -0.0859 -0.1184 46  PHE   A CZ  
136  N  N   . LEU   A 27  ? 1.1766 1.6999 1.4752 0.3025  0.0044  -0.1125 47  LEU   A N   
137  C  CA  . LEU   A 27  ? 1.2147 1.7689 1.5190 0.2701  0.0191  -0.1029 47  LEU   A CA  
138  C  C   . LEU   A 27  ? 1.2167 1.7197 1.4901 0.2526  0.0225  -0.1075 47  LEU   A C   
139  O  O   . LEU   A 27  ? 1.0671 1.5750 1.3398 0.2219  0.0296  -0.0963 47  LEU   A O   
140  C  CB  . LEU   A 27  ? 1.0151 1.6461 1.3434 0.2818  0.0385  -0.1049 47  LEU   A CB  
141  C  CG  . LEU   A 27  ? 1.0702 1.7700 1.4446 0.2953  0.0379  -0.0984 47  LEU   A CG  
142  C  CD1 . LEU   A 27  ? 1.0997 1.8775 1.5021 0.2988  0.0638  -0.0951 47  LEU   A CD1 
143  C  CD2 . LEU   A 27  ? 1.0940 1.7961 1.4870 0.2673  0.0221  -0.0819 47  LEU   A CD2 
144  N  N   . GLY   A 28  ? 1.2781 1.7315 1.5287 0.2714  0.0156  -0.1242 48  GLY   A N   
145  C  CA  . GLY   A 28  ? 1.0605 1.4741 1.2890 0.2569  0.0160  -0.1312 48  GLY   A CA  
146  C  C   . GLY   A 28  ? 0.9861 1.4437 1.2083 0.2566  0.0319  -0.1356 48  GLY   A C   
147  O  O   . GLY   A 28  ? 1.1588 1.6465 1.3754 0.2859  0.0396  -0.1484 48  GLY   A O   
148  N  N   . ASN   A 29  ? 1.0712 1.5321 1.2916 0.2257  0.0384  -0.1237 49  ASN   A N   
149  C  CA  . ASN   A 29  ? 1.0814 1.5796 1.2915 0.2232  0.0542  -0.1233 49  ASN   A CA  
150  C  C   . ASN   A 29  ? 0.9947 1.5417 1.2270 0.1975  0.0687  -0.1006 49  ASN   A C   
151  O  O   . ASN   A 29  ? 1.0622 1.6276 1.2849 0.1855  0.0813  -0.0939 49  ASN   A O   
152  C  CB  . ASN   A 29  ? 1.1448 1.5996 1.3292 0.2128  0.0468  -0.1315 49  ASN   A CB  
153  C  CG  . ASN   A 29  ? 1.2191 1.6150 1.3897 0.2289  0.0269  -0.1526 49  ASN   A CG  
154  O  OD1 . ASN   A 29  ? 1.1335 1.4870 1.3162 0.2168  0.0150  -0.1487 49  ASN   A OD1 
155  N  ND2 . ASN   A 29  ? 1.3050 1.6949 1.4484 0.2566  0.0234  -0.1747 49  ASN   A ND2 
156  N  N   . ILE   A 30  ? 0.9164 1.4815 1.1767 0.1894  0.0651  -0.0889 50  ILE   A N   
157  C  CA  . ILE   A 30  ? 1.0177 1.6196 1.3004 0.1612  0.0734  -0.0690 50  ILE   A CA  
158  C  C   . ILE   A 30  ? 1.0942 1.7647 1.3954 0.1664  0.0943  -0.0627 50  ILE   A C   
159  O  O   . ILE   A 30  ? 1.1396 1.8359 1.4545 0.1405  0.1046  -0.0462 50  ILE   A O   
160  C  CB  . ILE   A 30  ? 0.9959 1.5985 1.3012 0.1535  0.0596  -0.0607 50  ILE   A CB  
161  C  CG1 . ILE   A 30  ? 1.0852 1.7286 1.4154 0.1827  0.0567  -0.0668 50  ILE   A CG1 
162  C  CG2 . ILE   A 30  ? 1.1815 1.7145 1.4647 0.1474  0.0441  -0.0622 50  ILE   A CG2 
163  C  CD1 . ILE   A 30  ? 1.0339 1.7019 1.3948 0.1735  0.0439  -0.0561 50  ILE   A CD1 
164  N  N   . LEU   A 31  ? 1.1017 1.8015 1.4040 0.2000  0.1028  -0.0745 51  LEU   A N   
165  C  CA  . LEU   A 31  ? 1.0226 1.7900 1.3422 0.2070  0.1285  -0.0662 51  LEU   A CA  
166  C  C   . LEU   A 31  ? 1.1252 1.8854 1.4122 0.1958  0.1444  -0.0606 51  LEU   A C   
167  O  O   . LEU   A 31  ? 1.2359 2.0453 1.5378 0.1867  0.1675  -0.0442 51  LEU   A O   
168  C  CB  . LEU   A 31  ? 1.0439 1.8397 1.3648 0.2507  0.1367  -0.0815 51  LEU   A CB  
169  C  CG  . LEU   A 31  ? 1.0143 1.8401 1.3780 0.2667  0.1263  -0.0830 51  LEU   A CG  
170  C  CD1 . LEU   A 31  ? 0.8998 1.7676 1.2692 0.3112  0.1425  -0.0951 51  LEU   A CD1 
171  C  CD2 . LEU   A 31  ? 0.8321 1.7089 1.2498 0.2368  0.1268  -0.0614 51  LEU   A CD2 
172  N  N   . SER   A 32  ? 1.1136 1.8131 1.3582 0.1961  0.1318  -0.0727 52  SER   A N   
173  C  CA  . SER   A 32  ? 1.2487 1.9358 1.4592 0.1870  0.1413  -0.0681 52  SER   A CA  
174  C  C   . SER   A 32  ? 1.2785 1.9668 1.5037 0.1474  0.1446  -0.0453 52  SER   A C   
175  O  O   . SER   A 32  ? 1.3032 1.9900 1.5049 0.1389  0.1558  -0.0362 52  SER   A O   
176  C  CB  . SER   A 32  ? 1.2775 1.9006 1.4473 0.1973  0.1213  -0.0888 52  SER   A CB  
177  O  OG  . SER   A 32  ? 1.1818 1.7959 1.3333 0.2345  0.1162  -0.1122 52  SER   A OG  
178  N  N   . TYR   A 33  ? 1.2176 1.9045 1.4762 0.1253  0.1341  -0.0366 53  TYR   A N   
179  C  CA  . TYR   A 33  ? 1.1971 1.8814 1.4688 0.0893  0.1355  -0.0171 53  TYR   A CA  
180  C  C   . TYR   A 33  ? 1.4482 2.1926 1.7509 0.0764  0.1567  0.0026  53  TYR   A C   
181  O  O   . TYR   A 33  ? 1.4720 2.2174 1.7946 0.0457  0.1552  0.0181  53  TYR   A O   
182  C  CB  . TYR   A 33  ? 0.9924 1.6491 1.2814 0.0735  0.1154  -0.0168 53  TYR   A CB  
183  C  CG  . TYR   A 33  ? 1.2601 1.8533 1.5231 0.0763  0.0986  -0.0287 53  TYR   A CG  
184  C  CD1 . TYR   A 33  ? 1.1656 1.7267 1.3992 0.0779  0.0988  -0.0342 53  TYR   A CD1 
185  C  CD2 . TYR   A 33  ? 1.1960 1.7620 1.4657 0.0775  0.0826  -0.0329 53  TYR   A CD2 
186  C  CE1 . TYR   A 33  ? 1.0740 1.5822 1.2950 0.0781  0.0840  -0.0436 53  TYR   A CE1 
187  C  CE2 . TYR   A 33  ? 1.1375 1.6472 1.3886 0.0785  0.0713  -0.0403 53  TYR   A CE2 
188  C  CZ  . TYR   A 33  ? 1.2418 1.7250 1.4732 0.0775  0.0725  -0.0455 53  TYR   A CZ  
189  O  OH  . TYR   A 33  ? 1.2677 1.6999 1.4912 0.0762  0.0618  -0.0516 53  TYR   A OH  
190  N  N   . HIS   A 34  ? 1.6706 2.4636 1.9789 0.0992  0.1771  0.0026  54  HIS   A N   
191  C  CA  . HIS   A 34  ? 1.7641 2.6194 2.1101 0.0860  0.2010  0.0242  54  HIS   A CA  
192  C  C   . HIS   A 34  ? 1.7161 2.5620 2.0399 0.0650  0.2176  0.0434  54  HIS   A C   
193  O  O   . HIS   A 34  ? 1.8049 2.6876 2.1641 0.0411  0.2330  0.0657  54  HIS   A O   
194  C  CB  . HIS   A 34  ? 1.9178 2.8300 2.2760 0.1198  0.2230  0.0202  54  HIS   A CB  
195  C  CG  . HIS   A 34  ? 2.0423 2.9466 2.3458 0.1452  0.2431  0.0160  54  HIS   A CG  
196  N  ND1 . HIS   A 34  ? 2.0211 2.8661 2.2670 0.1638  0.2269  -0.0053 54  HIS   A ND1 
197  C  CD2 . HIS   A 34  ? 2.0205 2.9679 2.3163 0.1560  0.2775  0.0306  54  HIS   A CD2 
198  C  CE1 . HIS   A 34  ? 2.0451 2.8945 2.2457 0.1862  0.2468  -0.0060 54  HIS   A CE1 
199  N  NE2 . HIS   A 34  ? 2.0324 2.9426 2.2585 0.1831  0.2797  0.0164  54  HIS   A NE2 
200  N  N   . LYS   A 35  ? 1.6160 2.4129 1.8845 0.0732  0.2133  0.0357  55  LYS   A N   
201  C  CA  . LYS   A 35  ? 1.6236 2.4013 1.8651 0.0553  0.2239  0.0532  55  LYS   A CA  
202  C  C   . LYS   A 35  ? 1.4830 2.2064 1.7192 0.0285  0.2017  0.0543  55  LYS   A C   
203  O  O   . LYS   A 35  ? 1.6544 2.3523 1.8650 0.0160  0.2057  0.0664  55  LYS   A O   
204  C  CB  . LYS   A 35  ? 1.5408 2.3015 1.7221 0.0842  0.2322  0.0449  55  LYS   A CB  
205  C  CG  . LYS   A 35  ? 1.7149 2.5279 1.8889 0.1098  0.2637  0.0512  55  LYS   A CG  
206  C  CD  . LYS   A 35  ? 1.8121 2.5982 1.9140 0.1410  0.2673  0.0400  55  LYS   A CD  
207  C  CE  . LYS   A 35  ? 1.7962 2.6318 1.8812 0.1686  0.3039  0.0489  55  LYS   A CE  
208  N  NZ  . LYS   A 35  ? 1.7385 2.6112 1.8443 0.1446  0.3366  0.0858  55  LYS   A NZ  
209  N  N   . GLY   A 36  ? 1.2859 1.9904 1.5432 0.0218  0.1797  0.0428  56  GLY   A N   
210  C  CA  . GLY   A 36  ? 1.4495 2.1028 1.6997 0.0008  0.1616  0.0428  56  GLY   A CA  
211  C  C   . GLY   A 36  ? 1.4563 2.0612 1.6733 0.0164  0.1459  0.0248  56  GLY   A C   
212  O  O   . GLY   A 36  ? 1.4304 2.0341 1.6213 0.0408  0.1473  0.0130  56  GLY   A O   
213  N  N   . PHE   A 37  ? 1.1108 1.6745 1.3300 0.0020  0.1303  0.0225  57  PHE   A N   
214  C  CA  . PHE   A 37  ? 1.1559 1.6751 1.3555 0.0118  0.1160  0.0083  57  PHE   A CA  
215  C  C   . PHE   A 37  ? 1.2392 1.7461 1.4089 0.0190  0.1183  0.0084  57  PHE   A C   
216  O  O   . PHE   A 37  ? 1.2510 1.7407 1.4039 0.0377  0.1077  -0.0080 57  PHE   A O   
217  C  CB  . PHE   A 37  ? 1.3220 1.8023 1.5286 -0.0070 0.1061  0.0119  57  PHE   A CB  
218  C  CG  . PHE   A 37  ? 1.4824 1.9672 1.7092 -0.0135 0.1006  0.0123  57  PHE   A CG  
219  C  CD1 . PHE   A 37  ? 1.7422 2.2520 1.9865 -0.0306 0.1049  0.0244  57  PHE   A CD1 
220  C  CD2 . PHE   A 37  ? 1.2495 1.7102 1.4774 -0.0031 0.0892  0.0013  57  PHE   A CD2 
221  C  CE1 . PHE   A 37  ? 1.8881 2.4008 2.1485 -0.0352 0.0947  0.0230  57  PHE   A CE1 
222  C  CE2 . PHE   A 37  ? 1.4370 1.8982 1.6762 -0.0063 0.0821  0.0024  57  PHE   A CE2 
223  C  CZ  . PHE   A 37  ? 1.8930 2.3808 2.1474 -0.0215 0.0832  0.0121  57  PHE   A CZ  
224  N  N   . CYS   A 38  ? 1.2624 1.7749 1.4241 0.0046  0.1298  0.0265  58  CYS   A N   
225  C  CA  . CYS   A 38  ? 1.3279 1.8218 1.4579 0.0107  0.1288  0.0290  58  CYS   A CA  
226  C  C   . CYS   A 38  ? 1.3000 1.8122 1.4001 0.0384  0.1330  0.0192  58  CYS   A C   
227  O  O   . CYS   A 38  ? 1.3257 1.8142 1.4022 0.0551  0.1176  0.0035  58  CYS   A O   
228  C  CB  . CYS   A 38  ? 1.3647 1.8583 1.4908 -0.0098 0.1416  0.0531  58  CYS   A CB  
229  S  SG  . CYS   A 38  ? 1.3968 1.8584 1.5467 -0.0388 0.1349  0.0617  58  CYS   A SG  
230  N  N   . MET   A 39  ? 1.2400 1.7945 1.3413 0.0445  0.1535  0.0276  59  MET   A N   
231  C  CA  . MET   A 39  ? 1.3295 1.9013 1.3954 0.0746  0.1618  0.0188  59  MET   A CA  
232  C  C   . MET   A 39  ? 1.2664 1.8267 1.3285 0.0990  0.1443  -0.0103 59  MET   A C   
233  O  O   . MET   A 39  ? 1.3799 1.9291 1.4022 0.1255  0.1379  -0.0261 59  MET   A O   
234  C  CB  . MET   A 39  ? 1.4013 2.0263 1.4781 0.0760  0.1921  0.0360  59  MET   A CB  
235  C  CG  . MET   A 39  ? 1.4314 2.0671 1.5217 0.0472  0.2097  0.0667  59  MET   A CG  
236  S  SD  . MET   A 39  ? 1.9475 2.5398 1.9872 0.0444  0.2059  0.0790  59  MET   A SD  
237  C  CE  . MET   A 39  ? 1.7582 2.3619 1.7351 0.0852  0.2178  0.0715  59  MET   A CE  
238  N  N   . PHE   A 40  ? 1.1039 1.6621 1.2032 0.0916  0.1350  -0.0178 60  PHE   A N   
239  C  CA  . PHE   A 40  ? 1.2072 1.7478 1.3050 0.1130  0.1179  -0.0435 60  PHE   A CA  
240  C  C   . PHE   A 40  ? 1.3287 1.8199 1.4100 0.1149  0.0931  -0.0587 60  PHE   A C   
241  O  O   . PHE   A 40  ? 1.3065 1.7808 1.3624 0.1389  0.0797  -0.0805 60  PHE   A O   
242  C  CB  . PHE   A 40  ? 1.2550 1.8005 1.3938 0.1036  0.1137  -0.0439 60  PHE   A CB  
243  C  CG  . PHE   A 40  ? 1.1448 1.6611 1.2843 0.1214  0.0948  -0.0669 60  PHE   A CG  
244  C  CD1 . PHE   A 40  ? 1.0894 1.6153 1.2115 0.1533  0.0950  -0.0850 60  PHE   A CD1 
245  C  CD2 . PHE   A 40  ? 1.1598 1.6366 1.3164 0.1071  0.0784  -0.0694 60  PHE   A CD2 
246  C  CE1 . PHE   A 40  ? 1.1423 1.6350 1.2650 0.1691  0.0763  -0.1061 60  PHE   A CE1 
247  C  CE2 . PHE   A 40  ? 1.2388 1.6852 1.3982 0.1214  0.0624  -0.0876 60  PHE   A CE2 
248  C  CZ  . PHE   A 40  ? 1.2415 1.6940 1.3845 0.1517  0.0598  -0.1063 60  PHE   A CZ  
249  N  N   . ASP   A 41  ? 1.3436 1.8113 1.4412 0.0902  0.0858  -0.0482 61  ASP   A N   
250  C  CA  . ASP   A 41  ? 1.1262 1.5536 1.2208 0.0898  0.0630  -0.0604 61  ASP   A CA  
251  C  C   . ASP   A 41  ? 1.2390 1.6608 1.2931 0.1042  0.0562  -0.0651 61  ASP   A C   
252  O  O   . ASP   A 41  ? 1.3105 1.7065 1.3528 0.1177  0.0330  -0.0856 61  ASP   A O   
253  C  CB  . ASP   A 41  ? 1.1221 1.5305 1.2453 0.0627  0.0615  -0.0462 61  ASP   A CB  
254  C  CG  . ASP   A 41  ? 1.1265 1.5310 1.2807 0.0518  0.0643  -0.0437 61  ASP   A CG  
255  O  OD1 . ASP   A 41  ? 1.0586 1.4613 1.2178 0.0656  0.0584  -0.0577 61  ASP   A OD1 
256  O  OD2 . ASP   A 41  ? 1.0696 1.4691 1.2388 0.0313  0.0713  -0.0282 61  ASP   A OD2 
257  N  N   . MET   A 42  ? 1.2504 1.6936 1.2820 0.1015  0.0747  -0.0459 62  MET   A N   
258  C  CA  A MET   A 42  ? 1.3312 1.7675 1.3147 0.1183  0.0695  -0.0476 62  MET   A CA  
259  C  CA  B MET   A 42  ? 1.3540 1.7900 1.3378 0.1183  0.0692  -0.0478 62  MET   A CA  
260  C  C   . MET   A 42  ? 1.3330 1.7702 1.2783 0.1518  0.0627  -0.0715 62  MET   A C   
261  O  O   . MET   A 42  ? 1.4562 1.8680 1.3682 0.1691  0.0395  -0.0889 62  MET   A O   
262  C  CB  A MET   A 42  ? 1.3680 1.8275 1.3328 0.1103  0.0961  -0.0191 62  MET   A CB  
263  C  CB  B MET   A 42  ? 1.3376 1.7957 1.3023 0.1102  0.0952  -0.0193 62  MET   A CB  
264  C  CG  A MET   A 42  ? 1.3417 1.7887 1.3304 0.0815  0.0982  0.0024  62  MET   A CG  
265  C  CG  B MET   A 42  ? 1.3244 1.7690 1.3131 0.0816  0.0963  0.0015  62  MET   A CG  
266  S  SD  A MET   A 42  ? 1.3290 1.7405 1.2902 0.0865  0.0754  0.0025  62  MET   A SD  
267  S  SD  B MET   A 42  ? 1.4963 1.9489 1.4489 0.0770  0.1184  0.0326  62  MET   A SD  
268  C  CE  A MET   A 42  ? 1.2818 1.7059 1.1741 0.1096  0.0910  0.0143  62  MET   A CE  
269  C  CE  B MET   A 42  ? 1.2833 1.7126 1.1739 0.1085  0.0972  0.0188  62  MET   A CE  
270  N  N   . GLU   A 43  ? 1.4236 1.8893 1.3730 0.1630  0.0810  -0.0740 63  GLU   A N   
271  C  CA  . GLU   A 43  ? 1.4072 1.8716 1.3189 0.1984  0.0764  -0.0984 63  GLU   A CA  
272  C  C   . GLU   A 43  ? 1.4560 1.8807 1.3804 0.2051  0.0429  -0.1284 63  GLU   A C   
273  O  O   . GLU   A 43  ? 1.5833 1.9811 1.4685 0.2287  0.0208  -0.1527 63  GLU   A O   
274  C  CB  . GLU   A 43  ? 1.4122 1.9207 1.3340 0.2095  0.1057  -0.0924 63  GLU   A CB  
275  C  CG  . GLU   A 43  ? 1.5097 2.0608 1.4192 0.2062  0.1413  -0.0636 63  GLU   A CG  
276  C  CD  . GLU   A 43  ? 1.9188 2.5203 1.8500 0.2176  0.1696  -0.0582 63  GLU   A CD  
277  O  OE1 . GLU   A 43  ? 2.0017 2.6016 1.9489 0.2330  0.1599  -0.0791 63  GLU   A OE1 
278  O  OE2 . GLU   A 43  ? 1.9207 2.5636 1.8565 0.2111  0.2015  -0.0322 63  GLU   A OE2 
279  N  N   . CYS   A 44  ? 1.4616 1.8793 1.4391 0.1845  0.0380  -0.1266 64  CYS   A N   
280  C  CA  . CYS   A 44  ? 1.3861 1.7640 1.3823 0.1868  0.0091  -0.1504 64  CYS   A CA  
281  C  C   . CYS   A 44  ? 1.3655 1.7093 1.3574 0.1807  -0.0199 -0.1600 64  CYS   A C   
282  O  O   . CYS   A 44  ? 1.4347 1.7457 1.4188 0.1941  -0.0482 -0.1866 64  CYS   A O   
283  C  CB  . CYS   A 44  ? 1.4068 1.7822 1.4569 0.1639  0.0131  -0.1401 64  CYS   A CB  
284  S  SG  . CYS   A 44  ? 1.3702 1.7728 1.4314 0.1789  0.0310  -0.1411 64  CYS   A SG  
285  N  N   . HIS   A 45  ? 1.4542 1.8046 1.4540 0.1608  -0.0152 -0.1392 65  HIS   A N   
286  C  CA  . HIS   A 45  ? 1.4869 1.8115 1.4862 0.1571  -0.0431 -0.1467 65  HIS   A CA  
287  C  C   . HIS   A 45  ? 1.5117 1.8258 1.4497 0.1872  -0.0609 -0.1666 65  HIS   A C   
288  O  O   . HIS   A 45  ? 1.5415 1.8266 1.4785 0.1927  -0.0960 -0.1872 65  HIS   A O   
289  C  CB  . HIS   A 45  ? 1.4952 1.8302 1.5098 0.1345  -0.0316 -0.1192 65  HIS   A CB  
290  C  CG  . HIS   A 45  ? 1.4990 1.8136 1.5167 0.1328  -0.0595 -0.1245 65  HIS   A CG  
291  N  ND1 . HIS   A 45  ? 1.5262 1.8151 1.5745 0.1319  -0.0919 -0.1462 65  HIS   A ND1 
292  C  CD2 . HIS   A 45  ? 1.5347 1.8517 1.5326 0.1319  -0.0612 -0.1102 65  HIS   A CD2 
293  C  CE1 . HIS   A 45  ? 1.5929 1.8737 1.6440 0.1307  -0.1135 -0.1460 65  HIS   A CE1 
294  N  NE2 . HIS   A 45  ? 1.6434 1.9396 1.6613 0.1322  -0.0956 -0.1243 65  HIS   A NE2 
295  N  N   . LYS   A 46  ? 1.4795 1.8168 1.3662 0.2077  -0.0377 -0.1607 66  LYS   A N   
296  C  CA  . LYS   A 46  ? 1.5453 1.8705 1.3615 0.2412  -0.0510 -0.1791 66  LYS   A CA  
297  C  C   . LYS   A 46  ? 1.6771 1.9844 1.4722 0.2687  -0.0642 -0.2121 66  LYS   A C   
298  O  O   . LYS   A 46  ? 1.8491 2.1283 1.5934 0.2951  -0.0914 -0.2386 66  LYS   A O   
299  C  CB  . LYS   A 46  ? 1.5866 1.9436 1.3533 0.2529  -0.0157 -0.1552 66  LYS   A CB  
300  C  CG  . LYS   A 46  ? 1.7150 2.0556 1.4019 0.2831  -0.0288 -0.1644 66  LYS   A CG  
301  C  CD  . LYS   A 46  ? 1.8609 2.2330 1.4939 0.3016  0.0130  -0.1434 66  LYS   A CD  
302  C  CE  . LYS   A 46  ? 1.9917 2.3687 1.5838 0.3379  0.0226  -0.1663 66  LYS   A CE  
303  N  NZ  . LYS   A 46  ? 2.2425 2.5749 1.7722 0.3709  -0.0170 -0.2034 66  LYS   A NZ  
304  N  N   . LYS   A 47  ? 1.6485 1.9681 1.4790 0.2647  -0.0480 -0.2122 67  LYS   A N   
305  C  CA  . LYS   A 47  ? 1.6455 1.9487 1.4532 0.2944  -0.0560 -0.2415 67  LYS   A CA  
306  C  C   . LYS   A 47  ? 1.6253 1.8782 1.4579 0.2910  -0.0985 -0.2710 67  LYS   A C   
307  O  O   . LYS   A 47  ? 1.7416 1.9633 1.5350 0.3201  -0.1203 -0.3032 67  LYS   A O   
308  C  CB  . LYS   A 47  ? 1.6179 1.9541 1.4559 0.2937  -0.0239 -0.2294 67  LYS   A CB  
309  C  CG  . LYS   A 47  ? 1.6237 1.9864 1.4121 0.3311  0.0015  -0.2352 67  LYS   A CG  
310  C  CD  . LYS   A 47  ? 1.8325 2.2336 1.6627 0.3290  0.0302  -0.2221 67  LYS   A CD  
311  C  CE  . LYS   A 47  ? 1.7339 2.1784 1.6076 0.2949  0.0570  -0.1842 67  LYS   A CE  
312  N  NZ  . LYS   A 47  ? 1.4386 1.9248 1.3528 0.2945  0.0817  -0.1724 67  LYS   A NZ  
313  N  N   . TYR   A 48  ? 1.6079 1.8503 1.5047 0.2565  -0.1101 -0.2605 68  TYR   A N   
314  C  CA  . TYR   A 48  ? 1.6035 1.8016 1.5383 0.2481  -0.1448 -0.2830 68  TYR   A CA  
315  C  C   . TYR   A 48  ? 1.6052 1.7857 1.5747 0.2251  -0.1745 -0.2830 68  TYR   A C   
316  O  O   . TYR   A 48  ? 1.4568 1.5987 1.4495 0.2226  -0.2101 -0.3069 68  TYR   A O   
317  C  CB  . TYR   A 48  ? 1.5511 1.7496 1.5415 0.2303  -0.1292 -0.2714 68  TYR   A CB  
318  C  CG  . TYR   A 48  ? 1.5109 1.7348 1.4784 0.2516  -0.0999 -0.2682 68  TYR   A CG  
319  C  CD1 . TYR   A 48  ? 1.5865 1.7887 1.5195 0.2850  -0.1096 -0.2966 68  TYR   A CD1 
320  C  CD2 . TYR   A 48  ? 1.5914 1.8614 1.5737 0.2395  -0.0640 -0.2377 68  TYR   A CD2 
321  C  CE1 . TYR   A 48  ? 1.5816 1.8121 1.4991 0.3072  -0.0820 -0.2933 68  TYR   A CE1 
322  C  CE2 . TYR   A 48  ? 1.5388 1.8384 1.5095 0.2586  -0.0390 -0.2345 68  TYR   A CE2 
323  C  CZ  . TYR   A 48  ? 1.5373 1.8195 1.4773 0.2932  -0.0469 -0.2616 68  TYR   A CZ  
324  O  OH  . TYR   A 48  ? 1.5578 1.8739 1.4916 0.3148  -0.0213 -0.2582 68  TYR   A OH  
325  N  N   . GLY   A 49  ? 1.6393 1.8458 1.6170 0.2085  -0.1622 -0.2575 69  GLY   A N   
326  C  CA  . GLY   A 49  ? 1.5803 1.7741 1.5887 0.1925  -0.1914 -0.2588 69  GLY   A CA  
327  C  C   . GLY   A 49  ? 1.4685 1.6708 1.5530 0.1569  -0.1810 -0.2347 69  GLY   A C   
328  O  O   . GLY   A 49  ? 1.4212 1.6501 1.5153 0.1435  -0.1466 -0.2064 69  GLY   A O   
329  N  N   . LYS   A 50  ? 1.4699 1.6488 1.6095 0.1416  -0.2105 -0.2461 70  LYS   A N   
330  C  CA  . LYS   A 50  ? 1.3170 1.5050 1.5279 0.1108  -0.2008 -0.2231 70  LYS   A CA  
331  C  C   . LYS   A 50  ? 1.1858 1.3719 1.4327 0.0946  -0.1720 -0.2077 70  LYS   A C   
332  O  O   . LYS   A 50  ? 1.1020 1.3025 1.3847 0.0742  -0.1486 -0.1818 70  LYS   A O   
333  C  CB  . LYS   A 50  ? 1.3592 1.5281 1.6246 0.0998  -0.2407 -0.2387 70  LYS   A CB  
334  C  CG  . LYS   A 50  ? 1.4730 1.6075 1.7775 0.0934  -0.2597 -0.2584 70  LYS   A CG  
335  C  CD  . LYS   A 50  ? 1.5635 1.6760 1.8997 0.0919  -0.3107 -0.2852 70  LYS   A CD  
336  C  CE  . LYS   A 50  ? 1.6830 1.7608 2.0792 0.0758  -0.3258 -0.2973 70  LYS   A CE  
337  N  NZ  . LYS   A 50  ? 1.7066 1.7599 2.0626 0.0900  -0.3110 -0.3060 70  LYS   A NZ  
338  N  N   . VAL   A 51  ? 1.3250 1.4907 1.5588 0.1058  -0.1738 -0.2233 71  VAL   A N   
339  C  CA  . VAL   A 51  ? 1.3466 1.5043 1.6113 0.0936  -0.1515 -0.2101 71  VAL   A CA  
340  C  C   . VAL   A 51  ? 1.4090 1.5638 1.6272 0.1176  -0.1424 -0.2215 71  VAL   A C   
341  O  O   . VAL   A 51  ? 1.2909 1.4255 1.4769 0.1401  -0.1652 -0.2496 71  VAL   A O   
342  C  CB  . VAL   A 51  ? 1.2735 1.3968 1.6015 0.0756  -0.1701 -0.2161 71  VAL   A CB  
343  C  CG1 . VAL   A 51  ? 1.2481 1.3493 1.5854 0.0747  -0.1550 -0.2117 71  VAL   A CG1 
344  C  CG2 . VAL   A 51  ? 1.2735 1.4098 1.6602 0.0488  -0.1622 -0.1936 71  VAL   A CG2 
345  N  N   . TRP   A 52  ? 1.3184 1.4934 1.5333 0.1146  -0.1105 -0.2008 72  TRP   A N   
346  C  CA  . TRP   A 52  ? 1.3612 1.5385 1.5450 0.1365  -0.1001 -0.2086 72  TRP   A CA  
347  C  C   . TRP   A 52  ? 1.2578 1.4365 1.4691 0.1234  -0.0778 -0.1873 72  TRP   A C   
348  O  O   . TRP   A 52  ? 1.2805 1.4597 1.5257 0.0990  -0.0673 -0.1662 72  TRP   A O   
349  C  CB  . TRP   A 52  ? 1.4145 1.6305 1.5464 0.1568  -0.0845 -0.2076 72  TRP   A CB  
350  C  CG  . TRP   A 52  ? 1.2910 1.5462 1.4277 0.1406  -0.0556 -0.1777 72  TRP   A CG  
351  C  CD1 . TRP   A 52  ? 1.3470 1.6274 1.4884 0.1381  -0.0306 -0.1609 72  TRP   A CD1 
352  C  CD2 . TRP   A 52  ? 1.1770 1.4477 1.3145 0.1254  -0.0516 -0.1622 72  TRP   A CD2 
353  N  NE1 . TRP   A 52  ? 1.3371 1.6452 1.4824 0.1203  -0.0121 -0.1370 72  TRP   A NE1 
354  C  CE2 . TRP   A 52  ? 1.1941 1.4953 1.3356 0.1130  -0.0232 -0.1368 72  TRP   A CE2 
355  C  CE3 . TRP   A 52  ? 1.2757 1.5361 1.4119 0.1220  -0.0716 -0.1678 72  TRP   A CE3 
356  C  CZ2 . TRP   A 52  ? 1.1938 1.5108 1.3356 0.0973  -0.0128 -0.1170 72  TRP   A CZ2 
357  C  CZ3 . TRP   A 52  ? 1.3689 1.6482 1.5057 0.1084  -0.0605 -0.1469 72  TRP   A CZ3 
358  C  CH2 . TRP   A 52  ? 1.3551 1.6601 1.4935 0.0962  -0.0305 -0.1218 72  TRP   A CH2 
359  N  N   . GLY   A 53  ? 1.1213 1.2999 1.3148 0.1427  -0.0710 -0.1934 73  GLY   A N   
360  C  CA  . GLY   A 53  ? 1.2137 1.3908 1.4261 0.1354  -0.0543 -0.1754 73  GLY   A CA  
361  C  C   . GLY   A 53  ? 1.1745 1.3854 1.3612 0.1568  -0.0387 -0.1742 73  GLY   A C   
362  O  O   . GLY   A 53  ? 1.3351 1.5612 1.4905 0.1820  -0.0410 -0.1913 73  GLY   A O   
363  N  N   . PHE   A 54  ? 1.1395 1.3627 1.3401 0.1477  -0.0226 -0.1537 74  PHE   A N   
364  C  CA  . PHE   A 54  ? 1.0761 1.3355 1.2653 0.1650  -0.0094 -0.1500 74  PHE   A CA  
365  C  C   . PHE   A 54  ? 1.0790 1.3261 1.2862 0.1565  -0.0043 -0.1331 74  PHE   A C   
366  O  O   . PHE   A 54  ? 1.0753 1.2835 1.2982 0.1397  -0.0081 -0.1245 74  PHE   A O   
367  C  CB  . PHE   A 54  ? 0.9841 1.2981 1.1627 0.1606  0.0079  -0.1391 74  PHE   A CB  
368  C  CG  . PHE   A 54  ? 1.0862 1.4068 1.2792 0.1297  0.0169  -0.1170 74  PHE   A CG  
369  C  CD1 . PHE   A 54  ? 1.0456 1.3518 1.2390 0.1151  0.0113  -0.1167 74  PHE   A CD1 
370  C  CD2 . PHE   A 54  ? 1.0467 1.3869 1.2517 0.1173  0.0290  -0.0980 74  PHE   A CD2 
371  C  CE1 . PHE   A 54  ? 1.0876 1.3979 1.2930 0.0902  0.0205  -0.0972 74  PHE   A CE1 
372  C  CE2 . PHE   A 54  ? 1.2351 1.5756 1.4479 0.0915  0.0367  -0.0801 74  PHE   A CE2 
373  C  CZ  . PHE   A 54  ? 1.0473 1.3727 1.2601 0.0788  0.0339  -0.0794 74  PHE   A CZ  
374  N  N   . TYR   A 55  ? 1.1562 1.4378 1.3612 0.1693  0.0046  -0.1275 75  TYR   A N   
375  C  CA  . TYR   A 55  ? 1.0493 1.3183 1.2638 0.1686  0.0048  -0.1145 75  TYR   A CA  
376  C  C   . TYR   A 55  ? 1.0129 1.3325 1.2335 0.1605  0.0166  -0.0984 75  TYR   A C   
377  O  O   . TYR   A 55  ? 1.0939 1.4610 1.3169 0.1765  0.0219  -0.1027 75  TYR   A O   
378  C  CB  . TYR   A 55  ? 1.1086 1.3587 1.3181 0.1993  -0.0055 -0.1284 75  TYR   A CB  
379  C  CG  . TYR   A 55  ? 1.1001 1.2926 1.3054 0.2061  -0.0206 -0.1455 75  TYR   A CG  
380  C  CD1 . TYR   A 55  ? 1.0851 1.2776 1.2762 0.2215  -0.0283 -0.1692 75  TYR   A CD1 
381  C  CD2 . TYR   A 55  ? 1.0665 1.2022 1.2809 0.1971  -0.0276 -0.1376 75  TYR   A CD2 
382  C  CE1 . TYR   A 55  ? 1.1267 1.2632 1.3157 0.2264  -0.0469 -0.1874 75  TYR   A CE1 
383  C  CE2 . TYR   A 55  ? 1.2309 1.3126 1.4488 0.1999  -0.0427 -0.1525 75  TYR   A CE2 
384  C  CZ  . TYR   A 55  ? 1.2839 1.3658 1.4906 0.2138  -0.0546 -0.1788 75  TYR   A CZ  
385  O  OH  . TYR   A 55  ? 1.2458 1.2708 1.4577 0.2152  -0.0743 -0.1962 75  TYR   A OH  
386  N  N   . ASP   A 56  ? 1.1469 1.4562 1.3716 0.1362  0.0209  -0.0804 76  ASP   A N   
387  C  CA  . ASP   A 56  ? 1.0401 1.3854 1.2702 0.1270  0.0264  -0.0662 76  ASP   A CA  
388  C  C   . ASP   A 56  ? 1.1257 1.4611 1.3558 0.1436  0.0168  -0.0638 76  ASP   A C   
389  O  O   . ASP   A 56  ? 1.1249 1.4197 1.3451 0.1373  0.0130  -0.0534 76  ASP   A O   
390  C  CB  . ASP   A 56  ? 1.1445 1.4746 1.3715 0.0982  0.0327  -0.0507 76  ASP   A CB  
391  C  CG  . ASP   A 56  ? 1.1853 1.5350 1.4134 0.0835  0.0415  -0.0506 76  ASP   A CG  
392  O  OD1 . ASP   A 56  ? 1.2106 1.5881 1.4385 0.0954  0.0434  -0.0612 76  ASP   A OD1 
393  O  OD2 . ASP   A 56  ? 1.1527 1.4882 1.3785 0.0624  0.0470  -0.0394 76  ASP   A OD2 
394  N  N   . GLY   A 57  ? 1.2870 1.6601 1.5269 0.1675  0.0138  -0.0728 77  GLY   A N   
395  C  CA  . GLY   A 57  ? 1.2681 1.6312 1.5086 0.1898  0.0018  -0.0731 77  GLY   A CA  
396  C  C   . GLY   A 57  ? 1.1708 1.4736 1.3973 0.2059  -0.0058 -0.0823 77  GLY   A C   
397  O  O   . GLY   A 57  ? 1.2525 1.5535 1.4778 0.2237  -0.0066 -0.0996 77  GLY   A O   
398  N  N   . GLN   A 58  ? 1.1698 1.4197 1.3833 0.2004  -0.0113 -0.0704 78  GLN   A N   
399  C  CA  . GLN   A 58  ? 1.2358 1.4203 1.4397 0.2077  -0.0164 -0.0743 78  GLN   A CA  
400  C  C   . GLN   A 58  ? 1.2499 1.3960 1.4535 0.1792  -0.0082 -0.0663 78  GLN   A C   
401  O  O   . GLN   A 58  ? 1.3028 1.3943 1.5064 0.1791  -0.0113 -0.0669 78  GLN   A O   
402  C  CB  . GLN   A 58  ? 1.4638 1.6109 1.6539 0.2245  -0.0261 -0.0637 78  GLN   A CB  
403  C  CG  . GLN   A 58  ? 1.7483 1.9206 1.9428 0.2599  -0.0377 -0.0748 78  GLN   A CG  
404  C  CD  . GLN   A 58  ? 1.7023 1.8502 1.8979 0.2825  -0.0428 -0.0957 78  GLN   A CD  
405  O  OE1 . GLN   A 58  ? 1.7346 1.8303 1.9259 0.2721  -0.0429 -0.0996 78  GLN   A OE1 
406  N  NE2 . GLN   A 58  ? 1.7103 1.8961 1.9138 0.3142  -0.0477 -0.1100 78  GLN   A NE2 
407  N  N   . GLN   A 59  ? 1.2935 1.4672 1.5007 0.1553  0.0021  -0.0585 79  GLN   A N   
408  C  CA  . GLN   A 59  ? 1.0286 1.1723 1.2395 0.1299  0.0114  -0.0492 79  GLN   A CA  
409  C  C   . GLN   A 59  ? 1.0646 1.2144 1.2898 0.1249  0.0095  -0.0651 79  GLN   A C   
410  O  O   . GLN   A 59  ? 1.0351 1.2301 1.2613 0.1239  0.0118  -0.0727 79  GLN   A O   
411  C  CB  . GLN   A 59  ? 1.1269 1.2923 1.3315 0.1097  0.0219  -0.0342 79  GLN   A CB  
412  C  CG  . GLN   A 59  ? 1.2195 1.3669 1.4320 0.0858  0.0335  -0.0265 79  GLN   A CG  
413  C  CD  . GLN   A 59  ? 1.2496 1.3403 1.4624 0.0808  0.0398  -0.0138 79  GLN   A CD  
414  O  OE1 . GLN   A 59  ? 0.9965 1.0614 1.1881 0.0849  0.0438  0.0008  79  GLN   A OE1 
415  N  NE2 . GLN   A 59  ? 1.1081 1.1788 1.3453 0.0719  0.0404  -0.0185 79  GLN   A NE2 
416  N  N   . PRO   A 60  ? 0.9801 1.0851 1.2167 0.1217  0.0043  -0.0701 80  PRO   A N   
417  C  CA  . PRO   A 60  ? 1.0531 1.1620 1.3024 0.1167  -0.0027 -0.0870 80  PRO   A CA  
418  C  C   . PRO   A 60  ? 1.1741 1.2985 1.4347 0.0913  0.0075  -0.0763 80  PRO   A C   
419  O  O   . PRO   A 60  ? 1.1426 1.2459 1.4127 0.0742  0.0184  -0.0580 80  PRO   A O   
420  C  CB  . PRO   A 60  ? 1.0054 1.0568 1.2695 0.1181  -0.0141 -0.0936 80  PRO   A CB  
421  C  CG  . PRO   A 60  ? 1.2137 1.2303 1.4781 0.1107  -0.0032 -0.0697 80  PRO   A CG  
422  C  CD  . PRO   A 60  ? 1.1917 1.2386 1.4307 0.1227  0.0030  -0.0604 80  PRO   A CD  
423  N  N   . VAL   A 61  ? 1.0436 1.2039 1.3004 0.0914  0.0053  -0.0871 81  VAL   A N   
424  C  CA  . VAL   A 61  ? 1.0043 1.1808 1.2696 0.0711  0.0127  -0.0786 81  VAL   A CA  
425  C  C   . VAL   A 61  ? 1.0877 1.2607 1.3616 0.0722  -0.0022 -0.0965 81  VAL   A C   
426  O  O   . VAL   A 61  ? 1.2258 1.4135 1.4812 0.0906  -0.0121 -0.1150 81  VAL   A O   
427  C  CB  . VAL   A 61  ? 1.0356 1.2582 1.2841 0.0688  0.0240  -0.0706 81  VAL   A CB  
428  C  CG1 . VAL   A 61  ? 1.0486 1.2792 1.3040 0.0487  0.0317  -0.0602 81  VAL   A CG1 
429  C  CG2 . VAL   A 61  ? 1.0425 1.2692 1.2822 0.0701  0.0318  -0.0573 81  VAL   A CG2 
430  N  N   . LEU   A 62  ? 1.1103 1.2647 1.4119 0.0543  -0.0041 -0.0912 82  LEU   A N   
431  C  CA  . LEU   A 62  ? 1.1948 1.3453 1.5100 0.0531  -0.0228 -0.1076 82  LEU   A CA  
432  C  C   . LEU   A 62  ? 1.1646 1.3446 1.4790 0.0422  -0.0165 -0.0990 82  LEU   A C   
433  O  O   . LEU   A 62  ? 1.0443 1.2265 1.3736 0.0260  -0.0003 -0.0790 82  LEU   A O   
434  C  CB  . LEU   A 62  ? 1.0607 1.1714 1.4188 0.0403  -0.0329 -0.1083 82  LEU   A CB  
435  C  CG  . LEU   A 62  ? 0.9279 1.0319 1.3083 0.0377  -0.0590 -0.1277 82  LEU   A CG  
436  C  CD1 . LEU   A 62  ? 1.1465 1.2400 1.4968 0.0612  -0.0828 -0.1573 82  LEU   A CD1 
437  C  CD2 . LEU   A 62  ? 1.0570 1.1300 1.4953 0.0177  -0.0640 -0.1213 82  LEU   A CD2 
438  N  N   . ALA   A 63  ? 1.0669 1.2658 1.3593 0.0534  -0.0288 -0.1138 83  ALA   A N   
439  C  CA  . ALA   A 63  ? 1.0557 1.2799 1.3404 0.0467  -0.0247 -0.1058 83  ALA   A CA  
440  C  C   . ALA   A 63  ? 1.1781 1.3909 1.4841 0.0441  -0.0484 -0.1183 83  ALA   A C   
441  O  O   . ALA   A 63  ? 1.2881 1.4920 1.5789 0.0592  -0.0715 -0.1414 83  ALA   A O   
442  C  CB  . ALA   A 63  ? 1.0770 1.3328 1.3172 0.0621  -0.0185 -0.1089 83  ALA   A CB  
443  N  N   . ILE   A 64  ? 1.1725 1.3857 1.5132 0.0266  -0.0441 -0.1041 84  ILE   A N   
444  C  CA  . ILE   A 64  ? 1.1533 1.3616 1.5254 0.0223  -0.0675 -0.1134 84  ILE   A CA  
445  C  C   . ILE   A 64  ? 1.0290 1.2614 1.3812 0.0242  -0.0664 -0.1058 84  ILE   A C   
446  O  O   . ILE   A 64  ? 1.1114 1.3582 1.4490 0.0186  -0.0420 -0.0861 84  ILE   A O   
447  C  CB  . ILE   A 64  ? 1.2640 1.4569 1.7008 0.0025  -0.0633 -0.1021 84  ILE   A CB  
448  C  CG1 . ILE   A 64  ? 1.1619 1.3662 1.6065 -0.0096 -0.0318 -0.0747 84  ILE   A CG1 
449  C  CG2 . ILE   A 64  ? 1.1237 1.2867 1.5771 0.0005  -0.0637 -0.1069 84  ILE   A CG2 
450  C  CD1 . ILE   A 64  ? 0.9936 1.1885 1.5007 -0.0262 -0.0226 -0.0609 84  ILE   A CD1 
451  N  N   . THR   A 65  ? 1.0883 1.3214 1.4368 0.0332  -0.0950 -0.1220 85  THR   A N   
452  C  CA  . THR   A 65  ? 1.1732 1.4242 1.5018 0.0375  -0.0982 -0.1148 85  THR   A CA  
453  C  C   . THR   A 65  ? 1.3263 1.5753 1.7007 0.0330  -0.1259 -0.1212 85  THR   A C   
454  O  O   . THR   A 65  ? 1.3265 1.5865 1.6826 0.0409  -0.1371 -0.1192 85  THR   A O   
455  C  CB  . THR   A 65  ? 1.2679 1.5263 1.5277 0.0597  -0.1055 -0.1262 85  THR   A CB  
456  O  OG1 . THR   A 65  ? 1.2655 1.5069 1.5160 0.0745  -0.1395 -0.1551 85  THR   A OG1 
457  C  CG2 . THR   A 65  ? 1.1820 1.4502 1.4063 0.0643  -0.0778 -0.1191 85  THR   A CG2 
458  N  N   . ASP   A 66  ? 1.4094 1.6454 1.8455 0.0206  -0.1376 -0.1277 86  ASP   A N   
459  C  CA  . ASP   A 66  ? 1.4054 1.6446 1.8989 0.0144  -0.1658 -0.1342 86  ASP   A CA  
460  C  C   . ASP   A 66  ? 1.3706 1.6267 1.9132 -0.0002 -0.1418 -0.1079 86  ASP   A C   
461  O  O   . ASP   A 66  ? 1.3426 1.5939 1.9134 -0.0140 -0.1122 -0.0917 86  ASP   A O   
462  C  CB  . ASP   A 66  ? 1.4896 1.7075 2.0349 0.0054  -0.1891 -0.1520 86  ASP   A CB  
463  C  CG  . ASP   A 66  ? 1.5745 1.7989 2.1861 -0.0017 -0.2246 -0.1619 86  ASP   A CG  
464  O  OD1 . ASP   A 66  ? 1.7330 1.9570 2.3177 0.0136  -0.2625 -0.1832 86  ASP   A OD1 
465  O  OD2 . ASP   A 66  ? 1.5510 1.7821 2.2421 -0.0217 -0.2147 -0.1480 86  ASP   A OD2 
466  N  N   . PRO   A 67  ? 1.2994 1.5727 1.8494 0.0049  -0.1530 -0.1029 87  PRO   A N   
467  C  CA  . PRO   A 67  ? 1.2095 1.4977 1.8015 -0.0049 -0.1273 -0.0781 87  PRO   A CA  
468  C  C   . PRO   A 67  ? 1.2111 1.5012 1.8904 -0.0230 -0.1191 -0.0711 87  PRO   A C   
469  O  O   . PRO   A 67  ? 1.1251 1.4171 1.8233 -0.0317 -0.0824 -0.0492 87  PRO   A O   
470  C  CB  . PRO   A 67  ? 1.2631 1.5668 1.8522 0.0077  -0.1523 -0.0799 87  PRO   A CB  
471  C  CG  . PRO   A 67  ? 1.3492 1.6439 1.8624 0.0258  -0.1760 -0.0978 87  PRO   A CG  
472  C  CD  . PRO   A 67  ? 1.2039 1.4813 1.7146 0.0234  -0.1875 -0.1184 87  PRO   A CD  
473  N  N   . ASP   A 68  ? 1.1005 1.3885 1.8333 -0.0287 -0.1519 -0.0889 88  ASP   A N   
474  C  CA  . ASP   A 68  ? 1.1991 1.4880 2.0199 -0.0486 -0.1417 -0.0801 88  ASP   A CA  
475  C  C   . ASP   A 68  ? 1.1124 1.3762 1.9161 -0.0574 -0.1105 -0.0714 88  ASP   A C   
476  O  O   . ASP   A 68  ? 1.0611 1.3249 1.9069 -0.0701 -0.0771 -0.0497 88  ASP   A O   
477  C  CB  . ASP   A 68  ? 1.3943 1.6834 2.2775 -0.0549 -0.1886 -0.1030 88  ASP   A CB  
478  C  CG  . ASP   A 68  ? 1.3735 1.6934 2.3049 -0.0503 -0.2166 -0.1056 88  ASP   A CG  
479  O  OD1 . ASP   A 68  ? 1.2598 1.6047 2.2380 -0.0545 -0.1908 -0.0827 88  ASP   A OD1 
480  O  OD2 . ASP   A 68  ? 1.3007 1.6188 2.2206 -0.0402 -0.2651 -0.1310 88  ASP   A OD2 
481  N  N   . MET   A 69  ? 1.1851 1.4270 1.9247 -0.0483 -0.1202 -0.0875 89  MET   A N   
482  C  CA  . MET   A 69  ? 1.1152 1.3329 1.8332 -0.0530 -0.0939 -0.0799 89  MET   A CA  
483  C  C   . MET   A 69  ? 1.0421 1.2650 1.7191 -0.0510 -0.0518 -0.0558 89  MET   A C   
484  O  O   . MET   A 69  ? 0.9948 1.2030 1.6787 -0.0589 -0.0224 -0.0395 89  MET   A O   
485  C  CB  . MET   A 69  ? 1.1931 1.3899 1.8535 -0.0396 -0.1159 -0.1043 89  MET   A CB  
486  C  CG  . MET   A 69  ? 1.1523 1.3176 1.8154 -0.0451 -0.1057 -0.1042 89  MET   A CG  
487  S  SD  . MET   A 69  ? 1.2923 1.4328 1.8957 -0.0251 -0.1362 -0.1371 89  MET   A SD  
488  C  CE  . MET   A 69  ? 1.4017 1.5400 2.0424 -0.0247 -0.1896 -0.1664 89  MET   A CE  
489  N  N   . ILE   A 70  ? 0.9610 1.2009 1.5929 -0.0401 -0.0496 -0.0534 90  ILE   A N   
490  C  CA  . ILE   A 70  ? 1.1605 1.4026 1.7559 -0.0395 -0.0141 -0.0326 90  ILE   A CA  
491  C  C   . ILE   A 70  ? 1.1016 1.3498 1.7494 -0.0488 0.0108  -0.0115 90  ILE   A C   
492  O  O   . ILE   A 70  ? 0.9305 1.1665 1.5688 -0.0530 0.0434  0.0056  90  ILE   A O   
493  C  CB  . ILE   A 70  ? 1.1456 1.4009 1.6835 -0.0272 -0.0195 -0.0346 90  ILE   A CB  
494  C  CG1 . ILE   A 70  ? 1.0945 1.3458 1.5764 -0.0161 -0.0348 -0.0519 90  ILE   A CG1 
495  C  CG2 . ILE   A 70  ? 0.9183 1.1730 1.4275 -0.0291 0.0134  -0.0139 90  ILE   A CG2 
496  C  CD1 . ILE   A 70  ? 1.0033 1.2679 1.4312 -0.0041 -0.0398 -0.0525 90  ILE   A CD1 
497  N  N   . LYS   A 71  ? 1.1292 1.3968 1.8317 -0.0500 -0.0044 -0.0126 91  LYS   A N   
498  C  CA  . LYS   A 71  ? 1.0320 1.3106 1.7941 -0.0566 0.0203  0.0072  91  LYS   A CA  
499  C  C   . LYS   A 71  ? 0.9265 1.1914 1.7355 -0.0704 0.0409  0.0177  91  LYS   A C   
500  O  O   . LYS   A 71  ? 0.8754 1.1386 1.7022 -0.0734 0.0776  0.0394  91  LYS   A O   
501  C  CB  . LYS   A 71  ? 1.1032 1.4097 1.9269 -0.0547 -0.0058 0.0016  91  LYS   A CB  
502  C  CG  . LYS   A 71  ? 1.1562 1.4816 2.0533 -0.0594 0.0197  0.0218  91  LYS   A CG  
503  C  CD  . LYS   A 71  ? 1.2006 1.5577 2.1753 -0.0591 -0.0128 0.0139  91  LYS   A CD  
504  C  CE  . LYS   A 71  ? 1.2833 1.6657 2.3391 -0.0620 0.0158  0.0353  91  LYS   A CE  
505  N  NZ  . LYS   A 71  ? 1.4680 1.8850 2.6237 -0.0673 -0.0174 0.0275  91  LYS   A NZ  
506  N  N   . THR   A 72  ? 0.8983 1.1495 1.7237 -0.0775 0.0187  0.0032  92  THR   A N   
507  C  CA  . THR   A 72  ? 0.9133 1.1452 1.7803 -0.0912 0.0377  0.0150  92  THR   A CA  
508  C  C   . THR   A 72  ? 1.1807 1.3861 1.9842 -0.0872 0.0722  0.0297  92  THR   A C   
509  O  O   . THR   A 72  ? 1.2249 1.4187 2.0498 -0.0937 0.1064  0.0519  92  THR   A O   
510  C  CB  . THR   A 72  ? 0.9476 1.1639 1.8406 -0.0985 0.0017  -0.0064 92  THR   A CB  
511  O  OG1 . THR   A 72  ? 1.2171 1.4568 2.1660 -0.1012 -0.0360 -0.0227 92  THR   A OG1 
512  C  CG2 . THR   A 72  ? 0.7865 0.9793 1.7294 -0.1147 0.0212  0.0085  92  THR   A CG2 
513  N  N   . VAL   A 73  ? 1.0262 1.2228 1.7516 -0.0757 0.0639  0.0184  93  VAL   A N   
514  C  CA  . VAL   A 73  ? 0.9123 1.0854 1.5787 -0.0712 0.0893  0.0293  93  VAL   A CA  
515  C  C   . VAL   A 73  ? 0.9839 1.1610 1.6225 -0.0668 0.1211  0.0480  93  VAL   A C   
516  O  O   . VAL   A 73  ? 1.0346 1.1922 1.6629 -0.0676 0.1521  0.0665  93  VAL   A O   
517  C  CB  . VAL   A 73  ? 1.1070 1.2751 1.7096 -0.0606 0.0686  0.0106  93  VAL   A CB  
518  C  CG1 . VAL   A 73  ? 0.9338 1.0849 1.4777 -0.0548 0.0913  0.0215  93  VAL   A CG1 
519  C  CG2 . VAL   A 73  ? 1.0755 1.2294 1.6977 -0.0617 0.0409  -0.0080 93  VAL   A CG2 
520  N  N   . LEU   A 74  ? 0.8931 1.0907 1.5144 -0.0605 0.1135  0.0433  94  LEU   A N   
521  C  CA  . LEU   A 74  ? 0.9769 1.1717 1.5631 -0.0549 0.1398  0.0575  94  LEU   A CA  
522  C  C   . LEU   A 74  ? 1.0731 1.2717 1.7096 -0.0567 0.1676  0.0760  94  LEU   A C   
523  O  O   . LEU   A 74  ? 0.9785 1.1610 1.5846 -0.0516 0.1983  0.0909  94  LEU   A O   
524  C  CB  . LEU   A 74  ? 0.9447 1.1557 1.4989 -0.0480 0.1236  0.0487  94  LEU   A CB  
525  C  CG  . LEU   A 74  ? 0.9220 1.1329 1.4195 -0.0442 0.1048  0.0349  94  LEU   A CG  
526  C  CD1 . LEU   A 74  ? 0.8659 1.0910 1.3369 -0.0386 0.0943  0.0318  94  LEU   A CD1 
527  C  CD2 . LEU   A 74  ? 0.9410 1.1315 1.3892 -0.0438 0.1219  0.0409  94  LEU   A CD2 
528  N  N   . VAL   A 75  ? 1.0416 1.2617 1.7551 -0.0629 0.1571  0.0750  95  VAL   A N   
529  C  CA  . VAL   A 75  ? 1.2473 1.4820 2.0196 -0.0629 0.1828  0.0923  95  VAL   A CA  
530  C  C   . VAL   A 75  ? 1.0653 1.2996 1.9100 -0.0759 0.1960  0.1039  95  VAL   A C   
531  O  O   . VAL   A 75  ? 1.0162 1.2371 1.8654 -0.0756 0.2359  0.1256  95  VAL   A O   
532  C  CB  . VAL   A 75  ? 1.1171 1.3849 1.9300 -0.0580 0.1605  0.0846  95  VAL   A CB  
533  C  CG1 . VAL   A 75  ? 0.9469 1.2343 1.8245 -0.0550 0.1892  0.1032  95  VAL   A CG1 
534  C  CG2 . VAL   A 75  ? 1.1658 1.4293 1.9057 -0.0463 0.1487  0.0761  95  VAL   A CG2 
535  N  N   . LYS   A 76  ? 1.0320 1.2781 1.9322 -0.0872 0.1630  0.0900  96  LYS   A N   
536  C  CA  . LYS   A 76  ? 1.0301 1.2809 2.0187 -0.1030 0.1721  0.1015  96  LYS   A CA  
537  C  C   . LYS   A 76  ? 1.0923 1.3050 2.0556 -0.1087 0.1999  0.1167  96  LYS   A C   
538  O  O   . LYS   A 76  ? 1.0511 1.2612 2.0611 -0.1157 0.2357  0.1412  96  LYS   A O   
539  C  CB  . LYS   A 76  ? 1.0647 1.3297 2.1111 -0.1141 0.1236  0.0790  96  LYS   A CB  
540  C  CG  . LYS   A 76  ? 0.8975 1.2008 1.9799 -0.1081 0.0942  0.0662  96  LYS   A CG  
541  C  CD  . LYS   A 76  ? 1.0105 1.3201 2.1310 -0.1158 0.0400  0.0394  96  LYS   A CD  
542  C  CE  . LYS   A 76  ? 1.4051 1.7523 2.5633 -0.1082 0.0086  0.0283  96  LYS   A CE  
543  N  NZ  . LYS   A 76  ? 1.5436 1.8914 2.7197 -0.1114 -0.0490 -0.0015 96  LYS   A NZ  
544  N  N   . GLU   A 77  ? 1.2818 1.4653 2.1723 -0.1044 0.1850  0.1041  97  GLU   A N   
545  C  CA  . GLU   A 77  ? 1.2078 1.3524 2.0728 -0.1077 0.2053  0.1173  97  GLU   A CA  
546  C  C   . GLU   A 77  ? 1.1615 1.2824 1.9272 -0.0921 0.2244  0.1227  97  GLU   A C   
547  O  O   . GLU   A 77  ? 1.2206 1.3134 1.9353 -0.0884 0.2160  0.1172  97  GLU   A O   
548  C  CB  . GLU   A 77  ? 1.1753 1.3016 2.0502 -0.1157 0.1692  0.0980  97  GLU   A CB  
549  C  CG  . GLU   A 77  ? 1.2424 1.3891 2.2113 -0.1314 0.1398  0.0863  97  GLU   A CG  
550  C  CD  . GLU   A 77  ? 1.3612 1.5144 2.4209 -0.1483 0.1692  0.1126  97  GLU   A CD  
551  O  OE1 . GLU   A 77  ? 1.4149 1.5381 2.4634 -0.1512 0.2052  0.1370  97  GLU   A OE1 
552  O  OE2 . GLU   A 77  ? 1.4076 1.5968 2.5508 -0.1578 0.1567  0.1100  97  GLU   A OE2 
553  N  N   . CYS   A 78  ? 1.1201 1.2507 1.8594 -0.0820 0.2485  0.1327  98  CYS   A N   
554  C  CA  . CYS   A 78  ? 1.0211 1.1283 1.6680 -0.0681 0.2626  0.1358  98  CYS   A CA  
555  C  C   . CYS   A 78  ? 1.1963 1.2685 1.8174 -0.0642 0.3018  0.1608  98  CYS   A C   
556  O  O   . CYS   A 78  ? 1.2272 1.2684 1.7890 -0.0588 0.3001  0.1611  98  CYS   A O   
557  C  CB  . CYS   A 78  ? 1.2381 1.3627 1.8611 -0.0581 0.2684  0.1335  98  CYS   A CB  
558  S  SG  . CYS   A 78  ? 1.0403 1.1320 1.5583 -0.0427 0.2885  0.1390  98  CYS   A SG  
559  N  N   . TYR   A 79  ? 1.3718 1.4492 2.0361 -0.0648 0.3383  0.1830  99  TYR   A N   
560  C  CA  . TYR   A 79  ? 1.1376 1.1803 1.7706 -0.0580 0.3812  0.2098  99  TYR   A CA  
561  C  C   . TYR   A 79  ? 1.2116 1.2259 1.8581 -0.0678 0.3808  0.2196  99  TYR   A C   
562  O  O   . TYR   A 79  ? 1.3846 1.3604 1.9818 -0.0594 0.4094  0.2399  99  TYR   A O   
563  C  CB  . TYR   A 79  ? 1.0955 1.1555 1.7833 -0.0562 0.4235  0.2328  99  TYR   A CB  
564  C  CG  . TYR   A 79  ? 1.3598 1.4316 2.0135 -0.0395 0.4358  0.2292  99  TYR   A CG  
565  C  CD1 . TYR   A 79  ? 1.4144 1.4506 1.9725 -0.0204 0.4576  0.2348  99  TYR   A CD1 
566  C  CD2 . TYR   A 79  ? 1.2799 1.3948 1.9953 -0.0416 0.4234  0.2197  99  TYR   A CD2 
567  C  CE1 . TYR   A 79  ? 1.4028 1.4428 1.9276 -0.0048 0.4673  0.2299  99  TYR   A CE1 
568  C  CE2 . TYR   A 79  ? 1.3775 1.4979 2.0607 -0.0249 0.4345  0.2169  99  TYR   A CE2 
569  C  CZ  . TYR   A 79  ? 1.5654 1.6467 2.1534 -0.0070 0.4568  0.2216  99  TYR   A CZ  
570  O  OH  . TYR   A 79  ? 1.5745 1.6545 2.1281 0.0099  0.4660  0.2171  99  TYR   A OH  
571  N  N   . SER   A 80  ? 1.1713 1.1987 1.8784 -0.0838 0.3481  0.2053  100 SER   A N   
572  C  CA  . SER   A 80  ? 1.2916 1.2890 2.0235 -0.0948 0.3468  0.2146  100 SER   A CA  
573  C  C   . SER   A 80  ? 1.4195 1.3921 2.0926 -0.0890 0.3116  0.1942  100 SER   A C   
574  O  O   . SER   A 80  ? 1.4099 1.3409 2.0378 -0.0828 0.3228  0.2071  100 SER   A O   
575  C  CB  . SER   A 80  ? 1.2612 1.2840 2.1066 -0.1171 0.3332  0.2123  100 SER   A CB  
576  O  OG  . SER   A 80  ? 1.2540 1.3097 2.1209 -0.1200 0.2877  0.1803  100 SER   A OG  
577  N  N   . VAL   A 81  ? 1.3564 1.3538 2.0274 -0.0886 0.2704  0.1635  101 VAL   A N   
578  C  CA  . VAL   A 81  ? 1.2515 1.2326 1.8848 -0.0834 0.2361  0.1423  101 VAL   A CA  
579  C  C   . VAL   A 81  ? 1.1896 1.1823 1.7464 -0.0675 0.2218  0.1259  101 VAL   A C   
580  O  O   . VAL   A 81  ? 1.2715 1.2424 1.7712 -0.0563 0.2139  0.1220  101 VAL   A O   
581  C  CB  . VAL   A 81  ? 1.3451 1.3408 2.0416 -0.0956 0.1982  0.1191  101 VAL   A CB  
582  C  CG1 . VAL   A 81  ? 1.2205 1.1938 1.8771 -0.0869 0.1671  0.0982  101 VAL   A CG1 
583  C  CG2 . VAL   A 81  ? 1.1010 1.0893 1.8861 -0.1154 0.2101  0.1352  101 VAL   A CG2 
584  N  N   . PHE   A 82  ? 1.1307 1.1579 1.6891 -0.0665 0.2174  0.1169  102 PHE   A N   
585  C  CA  . PHE   A 82  ? 0.9346 0.9760 1.4318 -0.0555 0.2016  0.1011  102 PHE   A CA  
586  C  C   . PHE   A 82  ? 1.1604 1.2007 1.6183 -0.0487 0.2283  0.1146  102 PHE   A C   
587  O  O   . PHE   A 82  ? 1.2924 1.3571 1.7534 -0.0484 0.2260  0.1089  102 PHE   A O   
588  C  CB  . PHE   A 82  ? 0.8827 0.9590 1.4057 -0.0586 0.1701  0.0777  102 PHE   A CB  
589  C  CG  . PHE   A 82  ? 1.1215 1.1959 1.6887 -0.0649 0.1434  0.0627  102 PHE   A CG  
590  C  CD1 . PHE   A 82  ? 1.1482 1.2085 1.6842 -0.0571 0.1225  0.0476  102 PHE   A CD1 
591  C  CD2 . PHE   A 82  ? 1.2111 1.2972 1.8530 -0.0775 0.1375  0.0625  102 PHE   A CD2 
592  C  CE1 . PHE   A 82  ? 1.1820 1.2339 1.7532 -0.0607 0.0964  0.0312  102 PHE   A CE1 
593  C  CE2 . PHE   A 82  ? 1.1997 1.2791 1.8811 -0.0838 0.1085  0.0459  102 PHE   A CE2 
594  C  CZ  . PHE   A 82  ? 1.1072 1.1664 1.7496 -0.0749 0.0880  0.0296  102 PHE   A CZ  
595  N  N   . THR   A 83  ? 1.2768 1.2837 1.6920 -0.0413 0.2527  0.1323  103 THR   A N   
596  C  CA  . THR   A 83  ? 1.1482 1.1445 1.5167 -0.0320 0.2781  0.1441  103 THR   A CA  
597  C  C   . THR   A 83  ? 0.9556 0.9486 1.2524 -0.0228 0.2611  0.1312  103 THR   A C   
598  O  O   . THR   A 83  ? 1.0242 1.0216 1.2934 -0.0190 0.2665  0.1292  103 THR   A O   
599  C  CB  . THR   A 83  ? 1.2784 1.2367 1.6291 -0.0261 0.3142  0.1705  103 THR   A CB  
600  O  OG1 . THR   A 83  ? 1.4177 1.3822 1.8457 -0.0378 0.3316  0.1847  103 THR   A OG1 
601  C  CG2 . THR   A 83  ? 1.2769 1.2211 1.5767 -0.0135 0.3420  0.1810  103 THR   A CG2 
602  N  N   . ASN   A 84  ? 1.1503 1.1359 1.4204 -0.0192 0.2396  0.1223  104 ASN   A N   
603  C  CA  . ASN   A 84  ? 1.1460 1.1281 1.3534 -0.0106 0.2250  0.1134  104 ASN   A CA  
604  C  C   . ASN   A 84  ? 1.1080 1.1240 1.3263 -0.0140 0.1928  0.0918  104 ASN   A C   
605  O  O   . ASN   A 84  ? 1.2304 1.2616 1.4908 -0.0185 0.1795  0.0830  104 ASN   A O   
606  C  CB  . ASN   A 84  ? 1.2466 1.1910 1.4061 0.0013  0.2296  0.1240  104 ASN   A CB  
607  C  CG  . ASN   A 84  ? 1.3645 1.2742 1.5274 0.0040  0.2635  0.1486  104 ASN   A CG  
608  O  OD1 . ASN   A 84  ? 1.4301 1.3266 1.5734 0.0080  0.2897  0.1607  104 ASN   A OD1 
609  N  ND2 . ASN   A 84  ? 1.4003 1.2933 1.5884 0.0026  0.2647  0.1569  104 ASN   A ND2 
610  N  N   . ARG   A 85  ? 1.0054 1.0317 1.1844 -0.0114 0.1805  0.0833  105 ARG   A N   
611  C  CA  . ARG   A 85  ? 0.9845 1.0455 1.1698 -0.0135 0.1551  0.0661  105 ARG   A CA  
612  C  C   . ARG   A 85  ? 1.2603 1.3178 1.4260 -0.0035 0.1397  0.0613  105 ARG   A C   
613  O  O   . ARG   A 85  ? 1.2326 1.2579 1.3807 0.0047  0.1468  0.0714  105 ARG   A O   
614  C  CB  . ARG   A 85  ? 1.2403 1.3164 1.4029 -0.0184 0.1508  0.0616  105 ARG   A CB  
615  C  CG  . ARG   A 85  ? 1.1431 1.2202 1.3220 -0.0249 0.1648  0.0662  105 ARG   A CG  
616  C  CD  . ARG   A 85  ? 1.0302 1.1165 1.1851 -0.0301 0.1583  0.0616  105 ARG   A CD  
617  N  NE  . ARG   A 85  ? 1.1723 1.2625 1.3459 -0.0344 0.1676  0.0644  105 ARG   A NE  
618  C  CZ  . ARG   A 85  ? 1.1106 1.1757 1.2655 -0.0317 0.1847  0.0720  105 ARG   A CZ  
619  N  NH1 . ARG   A 85  ? 1.3208 1.3524 1.4320 -0.0248 0.1946  0.0771  105 ARG   A NH1 
620  N  NH2 . ARG   A 85  ? 0.9167 0.9888 1.0938 -0.0334 0.1912  0.0740  105 ARG   A NH2 
621  N  N   . ARG   A 86  ? 1.2977 1.3885 1.4661 -0.0025 0.1199  0.0472  106 ARG   A N   
622  C  CA  . ARG   A 86  ? 1.3068 1.4016 1.4619 0.0096  0.1045  0.0415  106 ARG   A CA  
623  C  C   . ARG   A 86  ? 1.4184 1.4926 1.5285 0.0157  0.1035  0.0492  106 ARG   A C   
624  O  O   . ARG   A 86  ? 1.5934 1.6710 1.6837 0.0086  0.1045  0.0499  106 ARG   A O   
625  C  CB  . ARG   A 86  ? 1.1557 1.2968 1.3251 0.0101  0.0880  0.0264  106 ARG   A CB  
626  C  CG  . ARG   A 86  ? 1.2822 1.4343 1.4516 0.0258  0.0730  0.0181  106 ARG   A CG  
627  C  CD  . ARG   A 86  ? 1.2483 1.4510 1.4270 0.0270  0.0619  0.0070  106 ARG   A CD  
628  N  NE  . ARG   A 86  ? 0.8184 1.0445 1.0181 0.0212  0.0643  -0.0008 106 ARG   A NE  
629  C  CZ  . ARG   A 86  ? 0.9832 1.2317 1.1961 0.0324  0.0571  -0.0137 106 ARG   A CZ  
630  N  NH1 . ARG   A 86  ? 1.2491 1.5024 1.4615 0.0502  0.0481  -0.0208 106 ARG   A NH1 
631  N  NH2 . ARG   A 86  ? 0.8815 1.1461 1.1045 0.0282  0.0584  -0.0201 106 ARG   A NH2 
632  N  N   . PRO   A 87  ? 1.4489 1.4972 1.5388 0.0295  0.0997  0.0545  107 PRO   A N   
633  C  CA  . PRO   A 87  ? 1.5891 1.6146 1.6296 0.0381  0.0948  0.0610  107 PRO   A CA  
634  C  C   . PRO   A 87  ? 1.6941 1.7572 1.7303 0.0361  0.0727  0.0491  107 PRO   A C   
635  O  O   . PRO   A 87  ? 1.6143 1.7190 1.6812 0.0370  0.0593  0.0380  107 PRO   A O   
636  C  CB  . PRO   A 87  ? 1.5622 1.5578 1.5885 0.0556  0.0911  0.0680  107 PRO   A CB  
637  C  CG  . PRO   A 87  ? 1.6288 1.6442 1.7011 0.0563  0.0859  0.0586  107 PRO   A CG  
638  C  CD  . PRO   A 87  ? 1.4230 1.4560 1.5309 0.0390  0.0980  0.0550  107 PRO   A CD  
639  N  N   . PHE   A 88  ? 1.7843 1.8319 1.7828 0.0335  0.0694  0.0514  108 PHE   A N   
640  C  CA  . PHE   A 88  ? 1.8071 1.8874 1.8062 0.0262  0.0483  0.0411  108 PHE   A CA  
641  C  C   . PHE   A 88  ? 1.9811 2.0353 1.9322 0.0381  0.0303  0.0423  108 PHE   A C   
642  O  O   . PHE   A 88  ? 1.9686 1.9737 1.8702 0.0437  0.0399  0.0503  108 PHE   A O   
643  C  CB  . PHE   A 88  ? 1.8077 1.8933 1.8111 0.0075  0.0570  0.0394  108 PHE   A CB  
644  C  CG  . PHE   A 88  ? 1.8358 1.9603 1.8553 -0.0052 0.0376  0.0302  108 PHE   A CG  
645  C  CD1 . PHE   A 88  ? 1.9023 2.0800 1.9689 -0.0114 0.0334  0.0245  108 PHE   A CD1 
646  C  CD2 . PHE   A 88  ? 1.9156 2.0214 1.9027 -0.0111 0.0243  0.0274  108 PHE   A CD2 
647  C  CE1 . PHE   A 88  ? 2.0647 2.2804 2.1518 -0.0249 0.0196  0.0196  108 PHE   A CE1 
648  C  CE2 . PHE   A 88  ? 2.0493 2.1906 2.0592 -0.0264 0.0059  0.0201  108 PHE   A CE2 
649  C  CZ  . PHE   A 88  ? 2.0779 2.2761 2.1408 -0.0342 0.0053  0.0178  108 PHE   A CZ  
650  N  N   . GLY   A 89  ? 2.0315 2.1192 1.9963 0.0440  0.0041  0.0342  109 GLY   A N   
651  C  CA  . GLY   A 89  ? 2.0525 2.1211 1.9763 0.0566  -0.0202 0.0332  109 GLY   A CA  
652  C  C   . GLY   A 89  ? 1.9971 2.1215 1.9572 0.0551  -0.0504 0.0220  109 GLY   A C   
653  O  O   . GLY   A 89  ? 1.9011 2.0782 1.9163 0.0498  -0.0486 0.0170  109 GLY   A O   
654  N  N   . PRO   A 90  ? 2.0745 2.1893 2.0046 0.0610  -0.0792 0.0176  110 PRO   A N   
655  C  CA  . PRO   A 90  ? 2.2217 2.2719 2.0759 0.0715  -0.0853 0.0216  110 PRO   A CA  
656  C  C   . PRO   A 90  ? 2.2455 2.2691 2.0738 0.0532  -0.0762 0.0186  110 PRO   A C   
657  O  O   . PRO   A 90  ? 2.2838 2.3402 2.1447 0.0321  -0.0883 0.0091  110 PRO   A O   
658  C  CB  . PRO   A 90  ? 2.1865 2.2521 2.0332 0.0834  -0.1278 0.0133  110 PRO   A CB  
659  C  CG  . PRO   A 90  ? 2.0165 2.1587 1.9412 0.0645  -0.1421 0.0029  110 PRO   A CG  
660  C  CD  . PRO   A 90  ? 1.9741 2.1469 1.9474 0.0597  -0.1106 0.0076  110 PRO   A CD  
661  N  N   . VAL   A 91  ? 2.1662 2.1286 1.9361 0.0617  -0.0531 0.0279  111 VAL   A N   
662  C  CA  . VAL   A 91  ? 2.0975 2.0295 1.8390 0.0493  -0.0407 0.0253  111 VAL   A CA  
663  C  C   . VAL   A 91  ? 2.1422 2.0123 1.7975 0.0644  -0.0546 0.0225  111 VAL   A C   
664  O  O   . VAL   A 91  ? 2.2849 2.1350 1.9163 0.0539  -0.0619 0.0126  111 VAL   A O   
665  C  CB  . VAL   A 91  ? 2.0291 1.9465 1.7812 0.0460  0.0027  0.0375  111 VAL   A CB  
666  C  CG1 . VAL   A 91  ? 2.0615 2.0355 1.8898 0.0257  0.0107  0.0343  111 VAL   A CG1 
667  C  CG2 . VAL   A 91  ? 2.0630 1.9536 1.7974 0.0660  0.0228  0.0532  111 VAL   A CG2 
668  N  N   . GLY   A 92  ? 2.1505 1.9852 1.7538 0.0900  -0.0589 0.0308  112 GLY   A N   
669  C  CA  . GLY   A 92  ? 2.2113 1.9829 1.7217 0.1083  -0.0727 0.0280  112 GLY   A CA  
670  C  C   . GLY   A 92  ? 2.2871 2.0034 1.7449 0.1143  -0.0320 0.0379  112 GLY   A C   
671  O  O   . GLY   A 92  ? 2.2992 2.0080 1.7690 0.1188  0.0082  0.0560  112 GLY   A O   
672  N  N   . PHE   A 93  ? 2.2484 1.9254 1.6499 0.1148  -0.0426 0.0255  113 PHE   A N   
673  C  CA  . PHE   A 93  ? 2.2669 1.8928 1.6179 0.1232  -0.0030 0.0332  113 PHE   A CA  
674  C  C   . PHE   A 93  ? 2.1803 1.8407 1.6028 0.1008  0.0287  0.0366  113 PHE   A C   
675  O  O   . PHE   A 93  ? 2.1730 1.8040 1.5750 0.1082  0.0690  0.0477  113 PHE   A O   
676  C  CB  . PHE   A 93  ? 2.2468 1.8184 1.5159 0.1315  -0.0258 0.0153  113 PHE   A CB  
677  C  CG  . PHE   A 93  ? 2.2889 1.8862 1.6007 0.1037  -0.0524 -0.0060 113 PHE   A CG  
678  C  CD1 . PHE   A 93  ? 2.3772 2.0154 1.7304 0.0872  -0.1015 -0.0215 113 PHE   A CD1 
679  C  CD2 . PHE   A 93  ? 2.3519 1.9323 1.6652 0.0943  -0.0276 -0.0090 113 PHE   A CD2 
680  C  CE1 . PHE   A 93  ? 2.3878 2.0482 1.7840 0.0591  -0.1237 -0.0380 113 PHE   A CE1 
681  C  CE2 . PHE   A 93  ? 2.3145 1.9126 1.6652 0.0684  -0.0513 -0.0263 113 PHE   A CE2 
682  C  CZ  . PHE   A 93  ? 2.3421 1.9793 1.7345 0.0494  -0.0986 -0.0401 113 PHE   A CZ  
683  N  N   . MET   A 94  ? 2.0489 1.7717 1.5543 0.0756  0.0119  0.0284  114 MET   A N   
684  C  CA  . MET   A 94  ? 2.0277 1.7853 1.6002 0.0559  0.0380  0.0322  114 MET   A CA  
685  C  C   . MET   A 94  ? 2.0571 1.8309 1.6683 0.0605  0.0733  0.0509  114 MET   A C   
686  O  O   . MET   A 94  ? 2.0043 1.8063 1.6707 0.0465  0.0938  0.0543  114 MET   A O   
687  C  CB  . MET   A 94  ? 2.0688 1.8865 1.7120 0.0300  0.0106  0.0199  114 MET   A CB  
688  C  CG  . MET   A 94  ? 2.1622 1.9667 1.7861 0.0169  -0.0194 0.0024  114 MET   A CG  
689  S  SD  . MET   A 94  ? 2.0657 1.8302 1.6677 0.0110  0.0068  0.0006  114 MET   A SD  
690  C  CE  . MET   A 94  ? 1.8404 1.6660 1.5349 -0.0079 0.0332  0.0116  114 MET   A CE  
691  N  N   . LYS   A 95  ? 2.2812 2.0358 1.8655 0.0793  0.0787  0.0632  115 LYS   A N   
692  C  CA  . LYS   A 95  ? 2.2393 1.9993 1.8577 0.0826  0.1130  0.0819  115 LYS   A CA  
693  C  C   . LYS   A 95  ? 2.1922 1.9233 1.7980 0.0858  0.1555  0.0939  115 LYS   A C   
694  O  O   . LYS   A 95  ? 2.1009 1.8517 1.7615 0.0787  0.1826  0.1053  115 LYS   A O   
695  C  CB  . LYS   A 95  ? 2.2732 2.0063 1.8553 0.1035  0.1113  0.0950  115 LYS   A CB  
696  C  CG  . LYS   A 95  ? 2.3745 2.0396 1.8605 0.1278  0.1244  0.1050  115 LYS   A CG  
697  C  CD  . LYS   A 95  ? 2.5628 2.1965 2.0156 0.1487  0.1331  0.1248  115 LYS   A CD  
698  C  CE  . LYS   A 95  ? 2.6112 2.1774 1.9770 0.1718  0.1657  0.1427  115 LYS   A CE  
699  N  NZ  . LYS   A 95  ? 2.5667 2.1009 1.8593 0.1805  0.1500  0.1262  115 LYS   A NZ  
700  N  N   . SER   A 96  ? 2.1713 1.8561 1.7070 0.0977  0.1606  0.0906  116 SER   A N   
701  C  CA  A SER   A 96  ? 2.1304 1.7876 1.6503 0.1049  0.2026  0.1013  116 SER   A CA  
702  C  CA  B SER   A 96  ? 2.1280 1.7852 1.6479 0.1049  0.2026  0.1013  116 SER   A CA  
703  C  C   . SER   A 96  ? 2.0063 1.6917 1.5757 0.0867  0.2058  0.0908  116 SER   A C   
704  O  O   . SER   A 96  ? 2.0166 1.6859 1.5833 0.0930  0.2398  0.0986  116 SER   A O   
705  C  CB  A SER   A 96  ? 2.2105 1.8008 1.6250 0.1303  0.2082  0.1010  116 SER   A CB  
706  C  CB  B SER   A 96  ? 2.2086 1.7989 1.6231 0.1303  0.2082  0.1010  116 SER   A CB  
707  O  OG  A SER   A 96  ? 2.1846 1.7633 1.5609 0.1269  0.1669  0.0769  116 SER   A OG  
708  O  OG  B SER   A 96  ? 2.2930 1.8517 1.6538 0.1503  0.2075  0.1138  116 SER   A OG  
709  N  N   . ALA   A 97  ? 1.8194 1.5462 1.4335 0.0660  0.1731  0.0751  117 ALA   A N   
710  C  CA  . ALA   A 97  ? 1.7808 1.5327 1.4408 0.0490  0.1756  0.0677  117 ALA   A CA  
711  C  C   . ALA   A 97  ? 1.7409 1.5239 1.4684 0.0437  0.2061  0.0814  117 ALA   A C   
712  O  O   . ALA   A 97  ? 1.7868 1.5928 1.5513 0.0422  0.2101  0.0904  117 ALA   A O   
713  C  CB  . ALA   A 97  ? 1.7240 1.5165 1.4207 0.0276  0.1373  0.0523  117 ALA   A CB  
714  N  N   . ILE   A 98  ? 1.4741 1.2561 1.2187 0.0415  0.2251  0.0820  118 ILE   A N   
715  C  CA  . ILE   A 98  ? 1.5316 1.3399 1.3390 0.0390  0.2537  0.0951  118 ILE   A CA  
716  C  C   . ILE   A 98  ? 1.5984 1.4612 1.4777 0.0205  0.2355  0.0916  118 ILE   A C   
717  O  O   . ILE   A 98  ? 1.5376 1.4214 1.4653 0.0187  0.2489  0.1015  118 ILE   A O   
718  C  CB  . ILE   A 98  ? 1.4725 1.2700 1.2834 0.0430  0.2738  0.0951  118 ILE   A CB  
719  C  CG1 . ILE   A 98  ? 1.3330 1.1634 1.2173 0.0405  0.2996  0.1081  118 ILE   A CG1 
720  C  CG2 . ILE   A 98  ? 1.3238 1.1292 1.1358 0.0293  0.2460  0.0787  118 ILE   A CG2 
721  C  CD1 . ILE   A 98  ? 1.3735 1.1951 1.2654 0.0492  0.3224  0.1105  118 ILE   A CD1 
722  N  N   . SER   A 99  ? 1.4800 1.3522 1.3564 0.0085  0.2099  0.0768  119 SER   A N   
723  C  CA  . SER   A 99  ? 1.4028 1.3285 1.3398 -0.0065 0.1926  0.0724  119 SER   A CA  
724  C  C   . SER   A 99  ? 1.4406 1.3727 1.3756 -0.0029 0.1797  0.0721  119 SER   A C   
725  O  O   . SER   A 99  ? 1.3472 1.3202 1.3276 -0.0112 0.1668  0.0677  119 SER   A O   
726  C  CB  . SER   A 99  ? 1.4368 1.3872 1.3841 -0.0209 0.1667  0.0607  119 SER   A CB  
727  O  OG  . SER   A 99  ? 1.5544 1.4882 1.4599 -0.0202 0.1423  0.0519  119 SER   A OG  
728  N  N   . ILE   A 100 ? 1.4396 1.3483 1.3342 0.0097  0.1785  0.0786  120 ILE   A N   
729  C  CA  . ILE   A 100 ? 1.5204 1.4323 1.4086 0.0162  0.1642  0.0794  120 ILE   A CA  
730  C  C   . ILE   A 100 ? 1.6686 1.5463 1.5393 0.0307  0.1904  0.0968  120 ILE   A C   
731  O  O   . ILE   A 100 ? 1.7632 1.6450 1.6494 0.0348  0.1872  0.1021  120 ILE   A O   
732  C  CB  . ILE   A 100 ? 1.6957 1.5969 1.5364 0.0195  0.1349  0.0689  120 ILE   A CB  
733  C  CG1 . ILE   A 100 ? 1.6373 1.5751 1.5053 0.0015  0.1120  0.0548  120 ILE   A CG1 
734  C  CG2 . ILE   A 100 ? 1.6482 1.5531 1.4824 0.0298  0.1187  0.0703  120 ILE   A CG2 
735  C  CD1 . ILE   A 100 ? 1.6366 1.5677 1.4696 0.0005  0.0808  0.0435  120 ILE   A CD1 
736  N  N   . ALA   A 101 ? 1.6103 1.4530 1.4498 0.0393  0.2184  0.1068  121 ALA   A N   
737  C  CA  . ALA   A 101 ? 1.5616 1.3705 1.3832 0.0531  0.2495  0.1273  121 ALA   A CA  
738  C  C   . ALA   A 101 ? 1.4403 1.2755 1.3372 0.0434  0.2649  0.1374  121 ALA   A C   
739  O  O   . ALA   A 101 ? 1.3649 1.2405 1.3223 0.0286  0.2561  0.1282  121 ALA   A O   
740  C  CB  . ALA   A 101 ? 1.6325 1.4043 1.4103 0.0654  0.2807  0.1358  121 ALA   A CB  
741  N  N   . GLU   A 102 ? 1.3416 1.1501 1.2327 0.0521  0.2872  0.1568  122 GLU   A N   
742  C  CA  . GLU   A 102 ? 1.3941 1.2203 1.3558 0.0420  0.2973  0.1663  122 GLU   A CA  
743  C  C   . GLU   A 102 ? 1.5708 1.3696 1.5387 0.0476  0.3416  0.1928  122 GLU   A C   
744  O  O   . GLU   A 102 ? 1.6093 1.3661 1.5109 0.0646  0.3635  0.2070  122 GLU   A O   
745  C  CB  . GLU   A 102 ? 1.5117 1.3359 1.4751 0.0437  0.2737  0.1637  122 GLU   A CB  
746  C  CG  . GLU   A 102 ? 1.7917 1.6502 1.7604 0.0390  0.2333  0.1396  122 GLU   A CG  
747  C  CD  . GLU   A 102 ? 1.9695 1.8212 1.9307 0.0471  0.2124  0.1380  122 GLU   A CD  
748  O  OE1 . GLU   A 102 ? 2.0601 1.8697 1.9836 0.0604  0.2243  0.1551  122 GLU   A OE1 
749  O  OE2 . GLU   A 102 ? 2.0318 1.9191 2.0230 0.0422  0.1856  0.1207  122 GLU   A OE2 
750  N  N   . ASP   A 103 ? 1.5809 1.4044 1.6300 0.0334  0.3541  0.1995  123 ASP   A N   
751  C  CA  . ASP   A 103 ? 1.5159 1.3220 1.5967 0.0331  0.3945  0.2271  123 ASP   A CA  
752  C  C   . ASP   A 103 ? 1.6502 1.4371 1.6936 0.0470  0.4341  0.2419  123 ASP   A C   
753  O  O   . ASP   A 103 ? 1.5931 1.4013 1.6427 0.0468  0.4328  0.2295  123 ASP   A O   
754  C  CB  . ASP   A 103 ? 1.7275 1.4971 1.7838 0.0386  0.3945  0.2416  123 ASP   A CB  
755  C  CG  . ASP   A 103 ? 1.8475 1.6365 1.9753 0.0221  0.3723  0.2348  123 ASP   A CG  
756  O  OD1 . ASP   A 103 ? 1.6772 1.5089 1.8701 0.0070  0.3557  0.2179  123 ASP   A OD1 
757  O  OD2 . ASP   A 103 ? 2.1316 1.8894 2.2468 0.0260  0.3703  0.2458  123 ASP   A OD2 
758  N  N   . GLU   A 104 ? 1.7811 1.5258 1.7826 0.0611  0.4708  0.2686  124 GLU   A N   
759  C  CA  . GLU   A 104 ? 1.8504 1.5782 1.8224 0.0766  0.5154  0.2848  124 GLU   A CA  
760  C  C   . GLU   A 104 ? 1.8233 1.5285 1.7028 0.0952  0.5031  0.2674  124 GLU   A C   
761  O  O   . GLU   A 104 ? 1.8403 1.5420 1.7042 0.1065  0.5292  0.2692  124 GLU   A O   
762  C  CB  . GLU   A 104 ? 2.0103 1.6958 1.9545 0.0886  0.5598  0.3201  124 GLU   A CB  
763  C  CG  . GLU   A 104 ? 1.9738 1.6729 2.0076 0.0682  0.5696  0.3387  124 GLU   A CG  
764  C  CD  . GLU   A 104 ? 2.2034 1.9568 2.3534 0.0475  0.5794  0.3378  124 GLU   A CD  
765  O  OE1 . GLU   A 104 ? 2.4303 2.2003 2.5893 0.0562  0.6028  0.3388  124 GLU   A OE1 
766  O  OE2 . GLU   A 104 ? 2.1477 1.9274 2.3782 0.0251  0.5557  0.3313  124 GLU   A OE2 
767  N  N   . GLU   A 105 ? 1.7791 1.4680 1.5991 0.0990  0.4628  0.2499  125 GLU   A N   
768  C  CA  . GLU   A 105 ? 1.8063 1.4759 1.5481 0.1120  0.4434  0.2299  125 GLU   A CA  
769  C  C   . GLU   A 105 ? 1.7123 1.4224 1.5012 0.0985  0.4268  0.2083  125 GLU   A C   
770  O  O   . GLU   A 105 ? 1.7242 1.4177 1.4695 0.1095  0.4323  0.1994  125 GLU   A O   
771  C  CB  . GLU   A 105 ? 1.9598 1.6127 1.6453 0.1158  0.3998  0.2157  125 GLU   A CB  
772  C  CG  . GLU   A 105 ? 2.2360 1.8630 1.8383 0.1285  0.3763  0.1956  125 GLU   A CG  
773  C  CD  . GLU   A 105 ? 2.2994 1.9301 1.8758 0.1257  0.3255  0.1773  125 GLU   A CD  
774  O  OE1 . GLU   A 105 ? 2.2101 1.8766 1.8466 0.1109  0.3056  0.1743  125 GLU   A OE1 
775  O  OE2 . GLU   A 105 ? 2.3846 1.9828 1.8819 0.1393  0.3046  0.1651  125 GLU   A OE2 
776  N  N   . TRP   A 106 ? 1.6059 1.3647 1.4797 0.0762  0.4060  0.1996  126 TRP   A N   
777  C  CA  . TRP   A 106 ? 1.4796 1.2756 1.3968 0.0641  0.3899  0.1815  126 TRP   A CA  
778  C  C   . TRP   A 106 ? 1.5223 1.3291 1.4810 0.0678  0.4272  0.1931  126 TRP   A C   
779  O  O   . TRP   A 106 ? 1.4716 1.2803 1.4193 0.0722  0.4266  0.1824  126 TRP   A O   
780  C  CB  . TRP   A 106 ? 1.2997 1.1417 1.2877 0.0429  0.3581  0.1696  126 TRP   A CB  
781  C  CG  . TRP   A 106 ? 1.2977 1.1793 1.3436 0.0313  0.3503  0.1586  126 TRP   A CG  
782  C  CD1 . TRP   A 106 ? 1.3575 1.2484 1.3860 0.0280  0.3281  0.1409  126 TRP   A CD1 
783  C  CD2 . TRP   A 106 ? 1.3724 1.2878 1.5031 0.0217  0.3630  0.1654  126 TRP   A CD2 
784  N  NE1 . TRP   A 106 ? 1.1495 1.0753 1.2406 0.0191  0.3273  0.1375  126 TRP   A NE1 
785  C  CE2 . TRP   A 106 ? 1.2810 1.2239 1.4359 0.0157  0.3467  0.1511  126 TRP   A CE2 
786  C  CE3 . TRP   A 106 ? 1.3403 1.2643 1.5312 0.0168  0.3850  0.1827  126 TRP   A CE3 
787  C  CZ2 . TRP   A 106 ? 1.2804 1.2599 1.5135 0.0077  0.3492  0.1524  126 TRP   A CZ2 
788  C  CZ3 . TRP   A 106 ? 1.2179 1.1809 1.4934 0.0062  0.3866  0.1828  126 TRP   A CZ3 
789  C  CH2 . TRP   A 106 ? 1.3587 1.3494 1.6528 0.0030  0.3677  0.1671  126 TRP   A CH2 
790  N  N   . LYS   A 107 ? 1.5844 1.3991 1.5955 0.0661  0.4597  0.2155  127 LYS   A N   
791  C  CA  . LYS   A 107 ? 1.4989 1.3320 1.5632 0.0697  0.4966  0.2284  127 LYS   A CA  
792  C  C   . LYS   A 107 ? 1.5312 1.3261 1.5208 0.0956  0.5278  0.2332  127 LYS   A C   
793  O  O   . LYS   A 107 ? 1.5699 1.3791 1.5832 0.1024  0.5436  0.2312  127 LYS   A O   
794  C  CB  . LYS   A 107 ? 1.5559 1.4007 1.6887 0.0622  0.5275  0.2544  127 LYS   A CB  
795  C  CG  . LYS   A 107 ? 1.5250 1.4240 1.7728 0.0453  0.5282  0.2551  127 LYS   A CG  
796  C  CD  . LYS   A 107 ? 1.5574 1.4768 1.8723 0.0227  0.5049  0.2549  127 LYS   A CD  
797  C  CE  . LYS   A 107 ? 1.6947 1.5853 2.0095 0.0229  0.5360  0.2826  127 LYS   A CE  
798  N  NZ  . LYS   A 107 ? 1.3115 1.2154 1.6917 0.0010  0.5114  0.2808  127 LYS   A NZ  
799  N  N   . ARG   A 108 ? 1.5667 1.3103 1.4618 0.1128  0.5355  0.2387  128 ARG   A N   
800  C  CA  . ARG   A 108 ? 1.6083 1.3071 1.4172 0.1407  0.5616  0.2399  128 ARG   A CA  
801  C  C   . ARG   A 108 ? 1.6402 1.3306 1.4072 0.1424  0.5268  0.2104  128 ARG   A C   
802  O  O   . ARG   A 108 ? 1.8732 1.5502 1.6190 0.1584  0.5458  0.2064  128 ARG   A O   
803  C  CB  . ARG   A 108 ? 1.7071 1.3498 1.4196 0.1598  0.5738  0.2526  128 ARG   A CB  
804  C  CG  . ARG   A 108 ? 1.8726 1.4584 1.4723 0.1910  0.5888  0.2472  128 ARG   A CG  
805  C  CD  . ARG   A 108 ? 2.3415 1.8717 1.8446 0.2109  0.5982  0.2613  128 ARG   A CD  
806  N  NE  . ARG   A 108 ? 2.5800 2.0562 1.9653 0.2318  0.5732  0.2398  128 ARG   A NE  
807  C  CZ  . ARG   A 108 ? 2.6135 2.0847 1.9685 0.2217  0.5160  0.2147  128 ARG   A CZ  
808  N  NH1 . ARG   A 108 ? 2.4308 1.9474 1.8587 0.1935  0.4805  0.2079  128 ARG   A NH1 
809  N  NH2 . ARG   A 108 ? 2.7070 2.1267 1.9573 0.2409  0.4937  0.1954  128 ARG   A NH2 
810  N  N   . LEU   A 109 ? 1.5737 1.2717 1.3318 0.1261  0.4767  0.1902  129 LEU   A N   
811  C  CA  . LEU   A 109 ? 1.5666 1.2566 1.2910 0.1236  0.4427  0.1642  129 LEU   A CA  
812  C  C   . LEU   A 109 ? 1.5765 1.3085 1.3772 0.1113  0.4398  0.1575  129 LEU   A C   
813  O  O   . LEU   A 109 ? 1.4570 1.1718 1.2304 0.1192  0.4369  0.1453  129 LEU   A O   
814  C  CB  . LEU   A 109 ? 1.7497 1.4440 1.4555 0.1083  0.3932  0.1477  129 LEU   A CB  
815  C  CG  . LEU   A 109 ? 1.6682 1.3205 1.2941 0.1218  0.3859  0.1511  129 LEU   A CG  
816  C  CD1 . LEU   A 109 ? 1.7767 1.4534 1.4200 0.1044  0.3414  0.1398  129 LEU   A CD1 
817  C  CD2 . LEU   A 109 ? 1.8562 1.4507 1.3795 0.1432  0.3822  0.1391  129 LEU   A CD2 
818  N  N   . ARG   A 110 ? 1.5897 1.3730 1.4832 0.0931  0.4380  0.1647  130 ARG   A N   
819  C  CA  . ARG   A 110 ? 1.4443 1.2680 1.4093 0.0831  0.4319  0.1589  130 ARG   A CA  
820  C  C   . ARG   A 110 ? 1.5873 1.4049 1.5633 0.1026  0.4721  0.1693  130 ARG   A C   
821  O  O   . ARG   A 110 ? 1.6884 1.5141 1.6798 0.1050  0.4659  0.1599  130 ARG   A O   
822  C  CB  . ARG   A 110 ? 1.2365 1.1117 1.2935 0.0626  0.4212  0.1640  130 ARG   A CB  
823  C  CG  . ARG   A 110 ? 1.1771 1.0949 1.3064 0.0531  0.4094  0.1575  130 ARG   A CG  
824  C  CD  . ARG   A 110 ? 1.1808 1.1113 1.3013 0.0385  0.3655  0.1376  130 ARG   A CD  
825  N  NE  . ARG   A 110 ? 1.3801 1.3408 1.5513 0.0345  0.3557  0.1326  130 ARG   A NE  
826  C  CZ  . ARG   A 110 ? 1.2747 1.2591 1.4624 0.0205  0.3222  0.1204  130 ARG   A CZ  
827  N  NH1 . ARG   A 110 ? 1.4010 1.3881 1.5665 0.0085  0.2964  0.1114  130 ARG   A NH1 
828  N  NH2 . ARG   A 110 ? 1.0117 1.0180 1.2387 0.0206  0.3154  0.1183  130 ARG   A NH2 
829  N  N   . SER   A 111 ? 1.4812 1.2841 1.4497 0.1182  0.5155  0.1902  131 SER   A N   
830  C  CA  . SER   A 111 ? 1.5392 1.3374 1.5161 0.1407  0.5594  0.2016  131 SER   A CA  
831  C  C   . SER   A 111 ? 1.5973 1.3380 1.4714 0.1654  0.5634  0.1886  131 SER   A C   
832  O  O   . SER   A 111 ? 1.7781 1.5158 1.6568 0.1807  0.5774  0.1843  131 SER   A O   
833  C  CB  . SER   A 111 ? 1.6896 1.4905 1.6909 0.1495  0.6086  0.2307  131 SER   A CB  
834  O  OG  . SER   A 111 ? 1.7064 1.5614 1.8192 0.1428  0.6296  0.2445  131 SER   A OG  
835  N  N   . LEU   A 112 ? 1.6153 1.3079 1.3955 0.1708  0.5484  0.1809  132 LEU   A N   
836  C  CA  . LEU   A 112 ? 1.7850 1.4158 1.4603 0.1947  0.5479  0.1660  132 LEU   A CA  
837  C  C   . LEU   A 112 ? 1.7052 1.3327 1.3767 0.1844  0.5075  0.1405  132 LEU   A C   
838  O  O   . LEU   A 112 ? 1.8609 1.4477 1.4790 0.2046  0.5142  0.1293  132 LEU   A O   
839  C  CB  . LEU   A 112 ? 1.9113 1.4938 1.4909 0.2017  0.5349  0.1631  132 LEU   A CB  
840  C  CG  . LEU   A 112 ? 2.1121 1.6222 1.5705 0.2281  0.5304  0.1464  132 LEU   A CG  
841  C  CD1 . LEU   A 112 ? 2.3297 1.7962 1.7138 0.2604  0.5766  0.1653  132 LEU   A CD1 
842  C  CD2 . LEU   A 112 ? 2.2094 1.6980 1.6170 0.2129  0.4725  0.1230  132 LEU   A CD2 
843  N  N   . LEU   A 113 ? 1.7989 1.4656 1.5242 0.1543  0.4671  0.1318  133 LEU   A N   
844  C  CA  . LEU   A 113 ? 1.7972 1.4612 1.5200 0.1413  0.4289  0.1110  133 LEU   A CA  
845  C  C   . LEU   A 113 ? 1.6906 1.4002 1.4997 0.1328  0.4301  0.1139  133 LEU   A C   
846  O  O   . LEU   A 113 ? 1.7618 1.4681 1.5715 0.1231  0.4023  0.1002  133 LEU   A O   
847  C  CB  . LEU   A 113 ? 1.7713 1.4462 1.4882 0.1156  0.3828  0.0993  133 LEU   A CB  
848  C  CG  . LEU   A 113 ? 1.7698 1.4011 1.4018 0.1232  0.3712  0.0937  133 LEU   A CG  
849  C  CD1 . LEU   A 113 ? 1.6391 1.2914 1.2804 0.0980  0.3250  0.0823  133 LEU   A CD1 
850  C  CD2 . LEU   A 113 ? 1.9038 1.4678 1.4428 0.1453  0.3726  0.0798  133 LEU   A CD2 
851  N  N   . SER   A 114 ? 1.6442 1.3953 1.5272 0.1360  0.4600  0.1321  134 SER   A N   
852  C  CA  . SER   A 114 ? 1.6048 1.3993 1.5697 0.1313  0.4589  0.1345  134 SER   A CA  
853  C  C   . SER   A 114 ? 1.7070 1.4721 1.6470 0.1538  0.4715  0.1285  134 SER   A C   
854  O  O   . SER   A 114 ? 1.7858 1.5624 1.7519 0.1460  0.4474  0.1201  134 SER   A O   
855  C  CB  . SER   A 114 ? 1.6694 1.5141 1.7225 0.1300  0.4869  0.1548  134 SER   A CB  
856  O  OG  . SER   A 114 ? 1.6967 1.5704 1.7839 0.1064  0.4672  0.1574  134 SER   A OG  
857  N  N   . PRO   A 115 ? 1.7013 1.4256 1.5881 0.1839  0.5087  0.1325  135 PRO   A N   
858  C  CA  . PRO   A 115 ? 1.6912 1.3867 1.5574 0.2083  0.5207  0.1255  135 PRO   A CA  
859  C  C   . PRO   A 115 ? 1.8092 1.4473 1.5967 0.2059  0.4856  0.1024  135 PRO   A C   
860  O  O   . PRO   A 115 ? 1.9741 1.5631 1.7094 0.2313  0.4976  0.0935  135 PRO   A O   
861  C  CB  . PRO   A 115 ? 1.9210 1.5894 1.7481 0.2428  0.5741  0.1371  135 PRO   A CB  
862  C  CG  . PRO   A 115 ? 1.7496 1.4500 1.6092 0.2327  0.5938  0.1566  135 PRO   A CG  
863  C  CD  . PRO   A 115 ? 1.6353 1.3417 1.4866 0.2002  0.5469  0.1466  135 PRO   A CD  
864  N  N   . THR   A 116 ? 1.8445 1.4873 1.6247 0.1758  0.4427  0.0924  136 THR   A N   
865  C  CA  . THR   A 116 ? 1.9305 1.5259 1.6523 0.1673  0.4065  0.0722  136 THR   A CA  
866  C  C   . THR   A 116 ? 1.9032 1.5214 1.6777 0.1524  0.3831  0.0702  136 THR   A C   
867  O  O   . THR   A 116 ? 1.9384 1.5107 1.6727 0.1544  0.3658  0.0575  136 THR   A O   
868  C  CB  . THR   A 116 ? 1.9294 1.5170 1.6138 0.1439  0.3735  0.0632  136 THR   A CB  
869  O  OG1 . THR   A 116 ? 1.9709 1.5401 1.6083 0.1589  0.3949  0.0682  136 THR   A OG1 
870  C  CG2 . THR   A 116 ? 1.9819 1.5140 1.6018 0.1363  0.3385  0.0421  136 THR   A CG2 
871  N  N   . PHE   A 117 ? 1.7443 1.4279 1.6046 0.1387  0.3814  0.0827  137 PHE   A N   
872  C  CA  . PHE   A 117 ? 1.7511 1.4591 1.6592 0.1262  0.3588  0.0831  137 PHE   A CA  
873  C  C   . PHE   A 117 ? 1.6854 1.4299 1.6628 0.1445  0.3819  0.0956  137 PHE   A C   
874  O  O   . PHE   A 117 ? 1.6740 1.4664 1.7170 0.1327  0.3670  0.1018  137 PHE   A O   
875  C  CB  . PHE   A 117 ? 1.8692 1.6217 1.8135 0.0940  0.3282  0.0839  137 PHE   A CB  
876  C  CG  . PHE   A 117 ? 1.9388 1.6675 1.8292 0.0759  0.3056  0.0732  137 PHE   A CG  
877  C  CD1 . PHE   A 117 ? 1.7880 1.4690 1.6257 0.0684  0.2831  0.0607  137 PHE   A CD1 
878  C  CD2 . PHE   A 117 ? 1.8246 1.5785 1.7212 0.0662  0.3052  0.0758  137 PHE   A CD2 
879  C  CE1 . PHE   A 117 ? 1.8105 1.4747 1.6074 0.0510  0.2594  0.0505  137 PHE   A CE1 
880  C  CE2 . PHE   A 117 ? 1.7491 1.4849 1.6006 0.0518  0.2822  0.0659  137 PHE   A CE2 
881  C  CZ  . PHE   A 117 ? 1.8520 1.5457 1.6562 0.0439  0.2588  0.0530  137 PHE   A CZ  
882  N  N   . THR   A 118 ? 1.9444 1.6681 1.9083 0.1754  0.4184  0.0993  138 THR   A N   
883  C  CA  . THR   A 118 ? 1.9835 1.7416 2.0164 0.1956  0.4398  0.1105  138 THR   A CA  
884  C  C   . THR   A 118 ? 2.1026 1.8379 2.1312 0.2022  0.4196  0.1044  138 THR   A C   
885  O  O   . THR   A 118 ? 2.0839 1.7672 2.0491 0.1939  0.3959  0.0919  138 THR   A O   
886  C  CB  . THR   A 118 ? 1.9257 1.6687 1.9452 0.2295  0.4888  0.1174  138 THR   A CB  
887  O  OG1 . THR   A 118 ? 1.9344 1.6011 1.8601 0.2508  0.4939  0.1034  138 THR   A OG1 
888  C  CG2 . THR   A 118 ? 1.3931 1.1532 1.4123 0.2232  0.5109  0.1269  138 THR   A CG2 
889  N  N   . SER   A 119 ? 2.0316 1.8062 2.1318 0.2172  0.4280  0.1143  139 SER   A N   
890  C  CA  . SER   A 119 ? 2.0091 1.7623 2.1084 0.2274  0.4100  0.1114  139 SER   A CA  
891  C  C   . SER   A 119 ? 2.1201 1.7967 2.1430 0.2549  0.4244  0.1010  139 SER   A C   
892  O  O   . SER   A 119 ? 2.1478 1.7826 2.1413 0.2567  0.4027  0.0949  139 SER   A O   
893  C  CB  . SER   A 119 ? 2.0592 1.8719 2.2527 0.2426  0.4164  0.1241  139 SER   A CB  
894  O  OG  . SER   A 119 ? 2.0828 1.9338 2.3261 0.2591  0.4554  0.1340  139 SER   A OG  
895  N  N   . GLY   A 120 ? 2.4458 2.0988 2.4320 0.2772  0.4605  0.0990  140 GLY   A N   
896  C  CA  . GLY   A 120 ? 2.4647 2.0387 2.3678 0.3059  0.4738  0.0859  140 GLY   A CA  
897  C  C   . GLY   A 120 ? 2.4581 1.9654 2.2658 0.2875  0.4492  0.0681  140 GLY   A C   
898  O  O   . GLY   A 120 ? 2.5478 1.9859 2.2943 0.2945  0.4330  0.0538  140 GLY   A O   
899  N  N   . LYS   A 121 ? 2.2969 1.8232 2.0937 0.2641  0.4445  0.0685  141 LYS   A N   
900  C  CA  . LYS   A 121 ? 2.1788 1.6503 1.8939 0.2452  0.4171  0.0517  141 LYS   A CA  
901  C  C   . LYS   A 121 ? 2.1562 1.6190 1.8764 0.2130  0.3715  0.0460  141 LYS   A C   
902  O  O   . LYS   A 121 ? 2.1551 1.5555 1.8087 0.2037  0.3471  0.0299  141 LYS   A O   
903  C  CB  . LYS   A 121 ? 2.0793 1.5804 1.7909 0.2286  0.4207  0.0558  141 LYS   A CB  
904  C  CG  . LYS   A 121 ? 2.0661 1.5639 1.7561 0.2589  0.4671  0.0630  141 LYS   A CG  
905  C  CD  . LYS   A 121 ? 2.1678 1.5792 1.7465 0.2855  0.4750  0.0453  141 LYS   A CD  
906  C  CE  . LYS   A 121 ? 2.1617 1.5695 1.7136 0.3188  0.5264  0.0555  141 LYS   A CE  
907  N  NZ  . LYS   A 121 ? 2.0402 1.4965 1.6221 0.3003  0.5343  0.0709  141 LYS   A NZ  
908  N  N   . LEU   A 122 ? 2.0499 1.5733 1.8476 0.1957  0.3594  0.0593  142 LEU   A N   
909  C  CA  . LEU   A 122 ? 2.0439 1.5604 1.8467 0.1680  0.3217  0.0580  142 LEU   A CA  
910  C  C   . LEU   A 122 ? 2.0818 1.5410 1.8595 0.1855  0.3167  0.0539  142 LEU   A C   
911  O  O   . LEU   A 122 ? 2.1080 1.5225 1.8515 0.1664  0.2884  0.0471  142 LEU   A O   
912  C  CB  . LEU   A 122 ? 1.8367 1.4309 1.7205 0.1492  0.3114  0.0732  142 LEU   A CB  
913  C  CG  . LEU   A 122 ? 1.7745 1.4045 1.6683 0.1134  0.2888  0.0733  142 LEU   A CG  
914  C  CD1 . LEU   A 122 ? 1.8834 1.5079 1.7434 0.1123  0.3000  0.0663  142 LEU   A CD1 
915  C  CD2 . LEU   A 122 ? 1.8166 1.5212 1.7876 0.1040  0.2844  0.0864  142 LEU   A CD2 
916  N  N   . LYS   A 123 ? 2.1380 1.5979 1.9358 0.2220  0.3445  0.0588  143 LYS   A N   
917  C  CA  . LYS   A 123 ? 2.1725 1.5761 1.9474 0.2438  0.3411  0.0553  143 LYS   A CA  
918  C  C   . LYS   A 123 ? 2.2963 1.6052 1.9764 0.2525  0.3363  0.0344  143 LYS   A C   
919  O  O   . LYS   A 123 ? 2.2661 1.5133 1.9141 0.2538  0.3177  0.0282  143 LYS   A O   
920  C  CB  . LYS   A 123 ? 2.1256 1.5572 1.9481 0.2846  0.3740  0.0648  143 LYS   A CB  
921  C  CG  . LYS   A 123 ? 2.2955 1.6863 2.1160 0.3080  0.3676  0.0660  143 LYS   A CG  
922  C  CD  . LYS   A 123 ? 2.2448 1.7075 2.1572 0.3191  0.3706  0.0845  143 LYS   A CD  
923  C  CE  . LYS   A 123 ? 2.0752 1.6038 2.0471 0.3406  0.4081  0.0922  143 LYS   A CE  
924  N  NZ  . LYS   A 123 ? 1.9187 1.5233 1.9887 0.3472  0.4047  0.1087  143 LYS   A NZ  
925  N  N   . GLU   A 124 ? 2.2774 1.5692 1.9090 0.2589  0.3510  0.0233  144 GLU   A N   
926  C  CA  . GLU   A 124 ? 2.2656 1.4657 1.8008 0.2656  0.3403  0.0002  144 GLU   A CA  
927  C  C   . GLU   A 124 ? 2.3052 1.4803 1.8161 0.2214  0.2952  -0.0088 144 GLU   A C   
928  O  O   . GLU   A 124 ? 2.2050 1.2985 1.6460 0.2206  0.2750  -0.0284 144 GLU   A O   
929  C  CB  . GLU   A 124 ? 2.2940 1.4837 1.7793 0.2881  0.3689  -0.0078 144 GLU   A CB  
930  C  CG  . GLU   A 124 ? 2.4687 1.6895 1.9832 0.3308  0.4196  0.0039  144 GLU   A CG  
931  C  CD  . GLU   A 124 ? 2.6652 1.8800 2.1310 0.3503  0.4512  0.0011  144 GLU   A CD  
932  O  OE1 . GLU   A 124 ? 2.7292 1.8925 2.1157 0.3407  0.4317  -0.0160 144 GLU   A OE1 
933  O  OE2 . GLU   A 124 ? 2.8183 2.0804 2.3264 0.3752  0.4951  0.0170  144 GLU   A OE2 
934  N  N   . MET   A 125 ? 2.2848 1.5283 1.8537 0.1853  0.2790  0.0044  145 MET   A N   
935  C  CA  . MET   A 125 ? 2.3116 1.5443 1.8694 0.1428  0.2400  -0.0011 145 MET   A CA  
936  C  C   . MET   A 125 ? 2.3223 1.5347 1.9000 0.1237  0.2163  0.0060  145 MET   A C   
937  O  O   . MET   A 125 ? 2.2449 1.4252 1.8023 0.0922  0.1852  -0.0008 145 MET   A O   
938  C  CB  . MET   A 125 ? 2.1027 1.4172 1.7100 0.1155  0.2356  0.0097  145 MET   A CB  
939  C  CG  . MET   A 125 ? 2.2025 1.5316 1.7853 0.1285  0.2544  0.0042  145 MET   A CG  
940  S  SD  . MET   A 125 ? 2.0874 1.5093 1.7320 0.1002  0.2501  0.0176  145 MET   A SD  
941  C  CE  . MET   A 125 ? 1.9197 1.3298 1.5134 0.1221  0.2731  0.0106  145 MET   A CE  
942  N  N   . VAL   A 126 ? 2.3258 1.5561 1.9443 0.1420  0.2298  0.0209  146 VAL   A N   
943  C  CA  . VAL   A 126 ? 2.3612 1.5684 1.9939 0.1265  0.2089  0.0311  146 VAL   A CA  
944  C  C   . VAL   A 126 ? 2.3159 1.4201 1.8828 0.1269  0.1910  0.0149  146 VAL   A C   
945  O  O   . VAL   A 126 ? 2.2697 1.3491 1.8349 0.0925  0.1632  0.0181  146 VAL   A O   
946  C  CB  . VAL   A 126 ? 2.3239 1.5675 2.0083 0.1522  0.2256  0.0493  146 VAL   A CB  
947  C  CG1 . VAL   A 126 ? 2.1163 1.3289 1.8065 0.1397  0.2046  0.0620  146 VAL   A CG1 
948  C  CG2 . VAL   A 126 ? 2.1493 1.4922 1.9011 0.1457  0.2358  0.0633  146 VAL   A CG2 
949  N  N   . PRO   A 127 ? 2.3747 1.4143 1.8867 0.1637  0.2055  -0.0025 147 PRO   A N   
950  C  CA  . PRO   A 127 ? 2.5356 1.4698 1.9794 0.1614  0.1830  -0.0220 147 PRO   A CA  
951  C  C   . PRO   A 127 ? 2.5753 1.4862 1.9849 0.1245  0.1526  -0.0385 147 PRO   A C   
952  O  O   . PRO   A 127 ? 2.6317 1.4738 2.0125 0.1022  0.1224  -0.0480 147 PRO   A O   
953  C  CB  . PRO   A 127 ? 2.4181 1.2995 1.8082 0.2145  0.2102  -0.0388 147 PRO   A CB  
954  C  CG  . PRO   A 127 ? 2.4424 1.4004 1.8926 0.2439  0.2463  -0.0197 147 PRO   A CG  
955  C  CD  . PRO   A 127 ? 2.3214 1.3766 1.8333 0.2110  0.2438  -0.0040 147 PRO   A CD  
956  N  N   . ILE   A 128 ? 2.5203 1.4859 1.9352 0.1172  0.1583  -0.0418 148 ILE   A N   
957  C  CA  . ILE   A 128 ? 2.4638 1.4132 1.8500 0.0847  0.1271  -0.0576 148 ILE   A CA  
958  C  C   . ILE   A 128 ? 2.5027 1.5048 1.9505 0.0348  0.1032  -0.0407 148 ILE   A C   
959  O  O   . ILE   A 128 ? 2.6095 1.5742 2.0454 0.0016  0.0696  -0.0495 148 ILE   A O   
960  C  CB  . ILE   A 128 ? 2.5041 1.4862 1.8664 0.0999  0.1424  -0.0666 148 ILE   A CB  
961  C  CG1 . ILE   A 128 ? 2.6191 1.5209 1.8927 0.1421  0.1548  -0.0908 148 ILE   A CG1 
962  C  CG2 . ILE   A 128 ? 2.6104 1.6183 1.9778 0.0604  0.1109  -0.0727 148 ILE   A CG2 
963  C  CD1 . ILE   A 128 ? 2.6012 1.5027 1.8759 0.1904  0.1985  -0.0831 148 ILE   A CD1 
964  N  N   . ILE   A 129 ? 2.5004 1.5895 2.0155 0.0294  0.1199  -0.0166 149 ILE   A N   
965  C  CA  . ILE   A 129 ? 2.4784 1.6206 2.0489 -0.0130 0.1023  0.0008  149 ILE   A CA  
966  C  C   . ILE   A 129 ? 2.6987 1.7902 2.2728 -0.0318 0.0853  0.0101  149 ILE   A C   
967  O  O   . ILE   A 129 ? 2.6645 1.7677 2.2642 -0.0722 0.0639  0.0183  149 ILE   A O   
968  C  CB  . ILE   A 129 ? 2.2128 1.4507 1.8458 -0.0083 0.1242  0.0223  149 ILE   A CB  
969  C  CG1 . ILE   A 129 ? 2.2650 1.5517 1.8987 0.0011  0.1368  0.0148  149 ILE   A CG1 
970  C  CG2 . ILE   A 129 ? 2.1988 1.4864 1.8830 -0.0454 0.1103  0.0420  149 ILE   A CG2 
971  C  CD1 . ILE   A 129 ? 2.1375 1.5134 1.8324 0.0041  0.1550  0.0329  149 ILE   A CD1 
972  N  N   . ALA   A 130 ? 2.7703 1.8021 2.3186 -0.0024 0.0952  0.0095  150 ALA   A N   
973  C  CA  . ALA   A 130 ? 2.7636 1.7462 2.3164 -0.0149 0.0832  0.0230  150 ALA   A CA  
974  C  C   . ALA   A 130 ? 2.8354 1.7405 2.3556 -0.0469 0.0504  0.0088  150 ALA   A C   
975  O  O   . ALA   A 130 ? 2.9463 1.7995 2.4675 -0.0619 0.0382  0.0198  150 ALA   A O   
976  C  CB  . ALA   A 130 ? 2.8132 1.7484 2.3443 0.0301  0.1016  0.0240  150 ALA   A CB  
977  N  N   . GLN   A 131 ? 2.7206 1.6151 2.2125 -0.0576 0.0342  -0.0152 151 GLN   A N   
978  C  CA  . GLN   A 131 ? 2.7371 1.5614 2.2030 -0.0898 -0.0024 -0.0318 151 GLN   A CA  
979  C  C   . GLN   A 131 ? 2.6588 1.5395 2.1839 -0.1433 -0.0218 -0.0163 151 GLN   A C   
980  O  O   . GLN   A 131 ? 2.7452 1.5888 2.2878 -0.1766 -0.0407 -0.0064 151 GLN   A O   
981  C  CB  . GLN   A 131 ? 2.9157 1.6940 2.3161 -0.0730 -0.0154 -0.0673 151 GLN   A CB  
982  C  CG  . GLN   A 131 ? 2.8717 1.5956 2.2556 -0.1118 -0.0601 -0.0867 151 GLN   A CG  
983  C  CD  . GLN   A 131 ? 2.9546 1.6413 2.2717 -0.0956 -0.0773 -0.1219 151 GLN   A CD  
984  O  OE1 . GLN   A 131 ? 3.0901 1.7318 2.3417 -0.0492 -0.0599 -0.1391 151 GLN   A OE1 
985  N  NE2 . GLN   A 131 ? 2.8004 1.5063 2.1332 -0.1322 -0.1116 -0.1321 151 GLN   A NE2 
986  N  N   . TYR   A 132 ? 2.6307 1.6009 2.1889 -0.1513 -0.0157 -0.0128 152 TYR   A N   
987  C  CA  . TYR   A 132 ? 2.5481 1.5758 2.1623 -0.1984 -0.0330 -0.0008 152 TYR   A CA  
988  C  C   . TYR   A 132 ? 2.5406 1.6175 2.2121 -0.2164 -0.0176 0.0349  152 TYR   A C   
989  O  O   . TYR   A 132 ? 2.5133 1.6247 2.2311 -0.2573 -0.0297 0.0489  152 TYR   A O   
990  C  CB  . TYR   A 132 ? 2.4670 1.5706 2.0946 -0.1967 -0.0314 -0.0091 152 TYR   A CB  
991  C  CG  . TYR   A 132 ? 2.5736 1.6286 2.1367 -0.1754 -0.0451 -0.0421 152 TYR   A CG  
992  C  CD1 . TYR   A 132 ? 2.5822 1.5873 2.1228 -0.1995 -0.0845 -0.0646 152 TYR   A CD1 
993  C  CD2 . TYR   A 132 ? 2.5048 1.5621 2.0286 -0.1305 -0.0189 -0.0504 152 TYR   A CD2 
994  C  CE1 . TYR   A 132 ? 2.6527 1.6083 2.1243 -0.1768 -0.0991 -0.0958 152 TYR   A CE1 
995  C  CE2 . TYR   A 132 ? 2.6519 1.6615 2.1083 -0.1080 -0.0281 -0.0785 152 TYR   A CE2 
996  C  CZ  . TYR   A 132 ? 2.6829 1.6398 2.1087 -0.1299 -0.0691 -0.1019 152 TYR   A CZ  
997  O  OH  . TYR   A 132 ? 2.7392 1.6443 2.0884 -0.1045 -0.0803 -0.1308 152 TYR   A OH  
998  N  N   . GLY   A 133 ? 2.4819 1.5640 2.1511 -0.1858 0.0087  0.0503  153 GLY   A N   
999  C  CA  . GLY   A 133 ? 2.3497 1.4590 2.0582 -0.1994 0.0196  0.0834  153 GLY   A CA  
1000 C  C   . GLY   A 133 ? 2.5369 1.5709 2.2410 -0.2279 0.0022  0.0930  153 GLY   A C   
1001 O  O   . GLY   A 133 ? 2.6119 1.6726 2.3560 -0.2599 0.0027  0.1196  153 GLY   A O   
1002 N  N   . ASP   A 134 ? 2.7957 1.7316 2.4494 -0.2161 -0.0124 0.0717  154 ASP   A N   
1003 C  CA  . ASP   A 134 ? 2.9017 1.7557 2.5503 -0.2469 -0.0341 0.0767  154 ASP   A CA  
1004 C  C   . ASP   A 134 ? 2.8639 1.7306 2.5432 -0.2967 -0.0623 0.0687  154 ASP   A C   
1005 O  O   . ASP   A 134 ? 2.9703 1.8185 2.6829 -0.3377 -0.0736 0.0877  154 ASP   A O   
1006 C  CB  . ASP   A 134 ? 3.0285 1.7697 2.6108 -0.2173 -0.0439 0.0522  154 ASP   A CB  
1007 C  CG  . ASP   A 134 ? 3.1482 1.8723 2.7097 -0.1706 -0.0175 0.0643  154 ASP   A CG  
1008 O  OD1 . ASP   A 134 ? 3.1734 1.9467 2.7711 -0.1717 0.0001  0.0968  154 ASP   A OD1 
1009 O  OD2 . ASP   A 134 ? 3.2352 1.8971 2.7437 -0.1308 -0.0148 0.0412  154 ASP   A OD2 
1010 N  N   . VAL   A 135 ? 2.6921 1.5907 2.3630 -0.2937 -0.0740 0.0421  155 VAL   A N   
1011 C  CA  . VAL   A 135 ? 2.5779 1.5116 2.2899 -0.3386 -0.1002 0.0366  155 VAL   A CA  
1012 C  C   . VAL   A 135 ? 2.6313 1.6682 2.4160 -0.3644 -0.0819 0.0702  155 VAL   A C   
1013 O  O   . VAL   A 135 ? 2.5929 1.6533 2.4294 -0.4096 -0.0970 0.0812  155 VAL   A O   
1014 C  CB  . VAL   A 135 ? 2.5164 1.4635 2.1971 -0.3228 -0.1158 0.0019  155 VAL   A CB  
1015 C  CG1 . VAL   A 135 ? 2.4383 1.4189 2.1631 -0.3675 -0.1485 -0.0058 155 VAL   A CG1 
1016 C  CG2 . VAL   A 135 ? 2.4785 1.3208 2.0766 -0.2905 -0.1290 -0.0310 155 VAL   A CG2 
1017 N  N   . LEU   A 136 ? 2.5123 1.6119 2.3032 -0.3355 -0.0494 0.0868  156 LEU   A N   
1018 C  CA  . LEU   A 136 ? 2.2812 1.4736 2.1307 -0.3537 -0.0304 0.1175  156 LEU   A CA  
1019 C  C   . LEU   A 136 ? 2.3547 1.5220 2.2261 -0.3773 -0.0221 0.1516  156 LEU   A C   
1020 O  O   . LEU   A 136 ? 2.3561 1.5721 2.2803 -0.4136 -0.0194 0.1742  156 LEU   A O   
1021 C  CB  . LEU   A 136 ? 2.1402 1.3970 1.9846 -0.3144 -0.0023 0.1222  156 LEU   A CB  
1022 C  CG  . LEU   A 136 ? 2.1483 1.4954 2.0393 -0.3218 0.0196  0.1514  156 LEU   A CG  
1023 C  CD1 . LEU   A 136 ? 1.9726 1.3861 1.9138 -0.3568 0.0103  0.1526  156 LEU   A CD1 
1024 C  CD2 . LEU   A 136 ? 2.1699 1.5664 2.0506 -0.2811 0.0402  0.1485  156 LEU   A CD2 
1025 N  N   . VAL   A 137 ? 2.4024 1.4939 2.2337 -0.3556 -0.0164 0.1574  157 VAL   A N   
1026 C  CA  . VAL   A 137 ? 2.4966 1.5524 2.3406 -0.3757 -0.0090 0.1915  157 VAL   A CA  
1027 C  C   . VAL   A 137 ? 2.6583 1.6617 2.5256 -0.4253 -0.0346 0.1916  157 VAL   A C   
1028 O  O   . VAL   A 137 ? 2.5316 1.5560 2.4441 -0.4624 -0.0277 0.2234  157 VAL   A O   
1029 C  CB  . VAL   A 137 ? 2.4691 1.4512 2.2624 -0.3366 0.0001  0.1955  157 VAL   A CB  
1030 C  CG1 . VAL   A 137 ? 2.6131 1.5411 2.4117 -0.3578 0.0039  0.2303  157 VAL   A CG1 
1031 C  CG2 . VAL   A 137 ? 2.4252 1.4702 2.2110 -0.2926 0.0249  0.2006  157 VAL   A CG2 
1032 N  N   . ARG   A 138 ? 2.7584 1.6926 2.5956 -0.4269 -0.0646 0.1564  158 ARG   A N   
1033 C  CA  . ARG   A 138 ? 2.7593 1.6377 2.6201 -0.4750 -0.0953 0.1523  158 ARG   A CA  
1034 C  C   . ARG   A 138 ? 2.6919 1.6574 2.6241 -0.5178 -0.1046 0.1567  158 ARG   A C   
1035 O  O   . ARG   A 138 ? 2.8262 1.7815 2.8090 -0.5663 -0.1163 0.1739  158 ARG   A O   
1036 C  CB  . ARG   A 138 ? 2.8864 1.6670 2.6891 -0.4614 -0.1285 0.1090  158 ARG   A CB  
1037 C  CG  . ARG   A 138 ? 3.0788 1.7371 2.8572 -0.4758 -0.1460 0.1111  158 ARG   A CG  
1038 C  CD  . ARG   A 138 ? 3.1559 1.7141 2.8656 -0.4547 -0.1779 0.0644  158 ARG   A CD  
1039 N  NE  . ARG   A 138 ? 3.2093 1.7967 2.9270 -0.4703 -0.2085 0.0314  158 ARG   A NE  
1040 C  CZ  . ARG   A 138 ? 3.1925 1.8087 2.8688 -0.4329 -0.2075 0.0024  158 ARG   A CZ  
1041 N  NH1 . ARG   A 138 ? 3.1681 1.7899 2.7972 -0.3792 -0.1765 0.0010  158 ARG   A NH1 
1042 N  NH2 . ARG   A 138 ? 3.1612 1.8015 2.8457 -0.4497 -0.2384 -0.0245 158 ARG   A NH2 
1043 N  N   . ASN   A 139 ? 2.5167 1.5682 2.4578 -0.5008 -0.0992 0.1425  159 ASN   A N   
1044 C  CA  . ASN   A 139 ? 2.4996 1.6443 2.5124 -0.5359 -0.1034 0.1502  159 ASN   A CA  
1045 C  C   . ASN   A 139 ? 2.3738 1.5892 2.4382 -0.5518 -0.0685 0.1957  159 ASN   A C   
1046 O  O   . ASN   A 139 ? 2.4295 1.6987 2.5630 -0.5930 -0.0700 0.2129  159 ASN   A O   
1047 C  CB  . ASN   A 139 ? 2.4789 1.6910 2.4823 -0.5096 -0.1063 0.1240  159 ASN   A CB  
1048 C  CG  . ASN   A 139 ? 2.5732 1.7340 2.5445 -0.5095 -0.1473 0.0814  159 ASN   A CG  
1049 O  OD1 . ASN   A 139 ? 2.6795 1.7815 2.6626 -0.5431 -0.1802 0.0714  159 ASN   A OD1 
1050 N  ND2 . ASN   A 139 ? 2.3443 1.5250 2.2734 -0.4716 -0.1465 0.0565  159 ASN   A ND2 
1051 N  N   . LEU   A 140 ? 2.4043 1.6219 2.4362 -0.5183 -0.0372 0.2156  160 LEU   A N   
1052 C  CA  . LEU   A 140 ? 2.3297 1.6011 2.3953 -0.5285 -0.0043 0.2591  160 LEU   A CA  
1053 C  C   . LEU   A 140 ? 2.5163 1.7158 2.5873 -0.5566 -0.0010 0.2902  160 LEU   A C   
1054 O  O   . LEU   A 140 ? 2.5716 1.8123 2.6809 -0.5785 0.0233  0.3293  160 LEU   A O   
1055 C  CB  . LEU   A 140 ? 2.2027 1.5079 2.2303 -0.4798 0.0236  0.2665  160 LEU   A CB  
1056 C  CG  . LEU   A 140 ? 2.1260 1.5298 2.1683 -0.4597 0.0327  0.2530  160 LEU   A CG  
1057 C  CD1 . LEU   A 140 ? 2.1005 1.5261 2.1068 -0.4137 0.0557  0.2592  160 LEU   A CD1 
1058 C  CD2 . LEU   A 140 ? 1.9788 1.4696 2.0868 -0.4925 0.0439  0.2740  160 LEU   A CD2 
1059 N  N   . ARG   A 141 ? 2.5921 1.6825 2.6232 -0.5553 -0.0235 0.2745  161 ARG   A N   
1060 C  CA  . ARG   A 141 ? 2.6035 1.6140 2.6379 -0.5827 -0.0231 0.3032  161 ARG   A CA  
1061 C  C   . ARG   A 141 ? 2.7595 1.7940 2.8675 -0.6308 -0.0338 0.3048  161 ARG   A C   
1062 O  O   . ARG   A 141 ? 2.9960 2.0131 3.1293 -0.6483 -0.0171 0.3318  161 ARG   A O   
1063 C  CB  . ARG   A 141 ? 2.5853 1.4735 2.5522 -0.5580 -0.0431 0.2802  161 ARG   A CB  
1064 C  CG  . ARG   A 141 ? 2.6736 1.4870 2.6394 -0.5671 -0.0377 0.3026  161 ARG   A CG  
1065 C  CD  . ARG   A 141 ? 2.6640 1.3792 2.5529 -0.5235 -0.0400 0.2950  161 ARG   A CD  
1066 N  NE  . ARG   A 141 ? 2.6759 1.4156 2.5361 -0.4915 -0.0097 0.3261  161 ARG   A NE  
1067 C  CZ  . ARG   A 141 ? 2.8661 1.5598 2.6684 -0.4403 -0.0045 0.3183  161 ARG   A CZ  
1068 N  NH1 . ARG   A 141 ? 2.8705 1.4758 2.6270 -0.4186 -0.0263 0.2843  161 ARG   A NH1 
1069 N  NH2 . ARG   A 141 ? 2.9784 1.7167 2.7684 -0.4084 0.0224  0.3444  161 ARG   A NH2 
1070 N  N   . ARG   A 142 ? 2.8021 1.8800 2.9457 -0.6498 -0.0596 0.2760  162 ARG   A N   
1071 C  CA  . ARG   A 142 ? 2.9266 2.0364 3.1448 -0.6922 -0.0722 0.2726  162 ARG   A CA  
1072 C  C   . ARG   A 142 ? 2.9758 2.2003 3.2655 -0.7112 -0.0382 0.3052  162 ARG   A C   
1073 O  O   . ARG   A 142 ? 2.9853 2.2236 3.3293 -0.7423 -0.0270 0.3230  162 ARG   A O   
1074 C  CB  . ARG   A 142 ? 2.9051 2.0129 3.1282 -0.7006 -0.1175 0.2268  162 ARG   A CB  
1075 C  CG  . ARG   A 142 ? 2.8169 1.8055 2.9673 -0.6825 -0.1521 0.1903  162 ARG   A CG  
1076 C  CD  . ARG   A 142 ? 2.8310 1.8192 2.9682 -0.6815 -0.1947 0.1445  162 ARG   A CD  
1077 N  NE  . ARG   A 142 ? 2.9298 1.8020 2.9937 -0.6622 -0.2268 0.1072  162 ARG   A NE  
1078 C  CZ  . ARG   A 142 ? 2.9893 1.8336 3.0127 -0.6499 -0.2640 0.0635  162 ARG   A CZ  
1079 N  NH1 . ARG   A 142 ? 3.0326 1.9535 3.0818 -0.6558 -0.2766 0.0515  162 ARG   A NH1 
1080 N  NH2 . ARG   A 142 ? 2.9574 1.6935 2.9088 -0.6282 -0.2884 0.0310  162 ARG   A NH2 
1081 N  N   . GLU   A 143 ? 2.8735 2.1790 3.1622 -0.6919 -0.0200 0.3125  163 GLU   A N   
1082 C  CA  . GLU   A 143 ? 2.8159 2.2306 3.1634 -0.7020 0.0146  0.3407  163 GLU   A CA  
1083 C  C   . GLU   A 143 ? 2.8142 2.2318 3.1371 -0.6858 0.0596  0.3830  163 GLU   A C   
1084 O  O   . GLU   A 143 ? 2.7791 2.2811 3.1362 -0.6877 0.0927  0.4069  163 GLU   A O   
1085 C  CB  . GLU   A 143 ? 2.7463 2.2495 3.1055 -0.6874 0.0117  0.3263  163 GLU   A CB  
1086 C  CG  . GLU   A 143 ? 2.7889 2.3348 3.2030 -0.7103 -0.0223 0.2955  163 GLU   A CG  
1087 C  CD  . GLU   A 143 ? 2.7857 2.2409 3.1635 -0.7139 -0.0715 0.2560  163 GLU   A CD  
1088 O  OE1 . GLU   A 143 ? 2.7538 2.1396 3.1361 -0.7338 -0.0867 0.2516  163 GLU   A OE1 
1089 O  OE2 . GLU   A 143 ? 2.8082 2.2582 3.1483 -0.6957 -0.0944 0.2286  163 GLU   A OE2 
1090 N  N   . ALA   A 144 ? 3.0060 2.3322 3.2663 -0.6669 0.0610  0.3916  164 ALA   A N   
1091 C  CA  . ALA   A 144 ? 2.9247 2.2399 3.1551 -0.6509 0.0990  0.4319  164 ALA   A CA  
1092 C  C   . ALA   A 144 ? 3.0763 2.3293 3.3192 -0.6755 0.1086  0.4524  164 ALA   A C   
1093 O  O   . ALA   A 144 ? 2.9720 2.2509 3.2228 -0.6806 0.1453  0.4883  164 ALA   A O   
1094 C  CB  . ALA   A 144 ? 2.7023 1.9607 2.8538 -0.6092 0.0961  0.4317  164 ALA   A CB  
1095 N  N   . GLU   A 145 ? 3.4376 2.6052 3.6773 -0.6902 0.0764  0.4295  165 GLU   A N   
1096 C  CA  . GLU   A 145 ? 3.5519 2.6605 3.8112 -0.7186 0.0826  0.4461  165 GLU   A CA  
1097 C  C   . GLU   A 145 ? 3.3933 2.5746 3.7336 -0.7613 0.0956  0.4560  165 GLU   A C   
1098 O  O   . GLU   A 145 ? 3.4928 2.6477 3.8526 -0.7860 0.1157  0.4818  165 GLU   A O   
1099 C  CB  . GLU   A 145 ? 3.6718 2.6758 3.9100 -0.7231 0.0412  0.4135  165 GLU   A CB  
1100 C  CG  . GLU   A 145 ? 3.8668 2.7877 4.0225 -0.6793 0.0319  0.4060  165 GLU   A CG  
1101 C  CD  . GLU   A 145 ? 3.9067 2.7292 4.0350 -0.6781 -0.0102 0.3665  165 GLU   A CD  
1102 O  OE1 . GLU   A 145 ? 3.9691 2.7983 4.1374 -0.7078 -0.0391 0.3379  165 GLU   A OE1 
1103 O  OE2 . GLU   A 145 ? 3.9486 2.6871 4.0131 -0.6450 -0.0152 0.3631  165 GLU   A OE2 
1104 N  N   . THR   A 146 ? 3.0873 2.3581 3.4751 -0.7699 0.0846  0.4362  166 THR   A N   
1105 C  CA  . THR   A 146 ? 2.9253 2.2869 3.3910 -0.8019 0.1025  0.4481  166 THR   A CA  
1106 C  C   . THR   A 146 ? 2.8735 2.3295 3.3332 -0.7768 0.1392  0.4688  166 THR   A C   
1107 O  O   . THR   A 146 ? 2.8079 2.3175 3.2645 -0.7563 0.1270  0.4483  166 THR   A O   
1108 C  CB  . THR   A 146 ? 2.7888 2.1853 3.3143 -0.8266 0.0617  0.4102  166 THR   A CB  
1109 O  OG1 . THR   A 146 ? 2.4551 1.9168 2.9737 -0.8016 0.0506  0.3895  166 THR   A OG1 
1110 C  CG2 . THR   A 146 ? 2.9008 2.1924 3.4041 -0.8362 0.0161  0.3789  166 THR   A CG2 
1111 N  N   . GLY   A 147 ? 2.9518 2.4240 3.4044 -0.7776 0.1833  0.5085  167 GLY   A N   
1112 C  CA  . GLY   A 147 ? 2.9412 2.4878 3.3713 -0.7487 0.2194  0.5296  167 GLY   A CA  
1113 C  C   . GLY   A 147 ? 2.7267 2.3878 3.2110 -0.7482 0.2207  0.5144  167 GLY   A C   
1114 O  O   . GLY   A 147 ? 2.6357 2.3707 3.1479 -0.7517 0.2551  0.5354  167 GLY   A O   
1115 N  N   . LYS   A 148 ? 2.5348 2.2084 3.0296 -0.7414 0.1834  0.4779  168 LYS   A N   
1116 C  CA  . LYS   A 148 ? 2.3962 2.1702 2.9413 -0.7395 0.1774  0.4590  168 LYS   A CA  
1117 C  C   . LYS   A 148 ? 2.2725 2.0754 2.7675 -0.6973 0.1798  0.4511  168 LYS   A C   
1118 O  O   . LYS   A 148 ? 2.3378 2.0805 2.7840 -0.6812 0.1537  0.4336  168 LYS   A O   
1119 C  CB  . LYS   A 148 ? 2.4133 2.1783 3.0065 -0.7654 0.1297  0.4225  168 LYS   A CB  
1120 C  CG  . LYS   A 148 ? 2.4943 2.3619 3.1507 -0.7689 0.1204  0.4040  168 LYS   A CG  
1121 C  CD  . LYS   A 148 ? 2.4654 2.3110 3.1566 -0.7917 0.0674  0.3668  168 LYS   A CD  
1122 C  CE  . LYS   A 148 ? 2.4344 2.3804 3.1885 -0.7935 0.0549  0.3484  168 LYS   A CE  
1123 N  NZ  . LYS   A 148 ? 2.1141 2.1353 2.9469 -0.8175 0.0816  0.3682  168 LYS   A NZ  
1124 N  N   . PRO   A 149 ? 2.1931 2.0833 2.6958 -0.6778 0.2103  0.4630  169 PRO   A N   
1125 C  CA  . PRO   A 149 ? 2.2663 2.1864 2.7239 -0.6382 0.2118  0.4543  169 PRO   A CA  
1126 C  C   . PRO   A 149 ? 2.3522 2.2719 2.8167 -0.6362 0.1699  0.4169  169 PRO   A C   
1127 O  O   . PRO   A 149 ? 2.4102 2.3424 2.9277 -0.6619 0.1429  0.3959  169 PRO   A O   
1128 C  CB  . PRO   A 149 ? 2.0601 2.0814 2.5452 -0.6257 0.2463  0.4663  169 PRO   A CB  
1129 C  CG  . PRO   A 149 ? 1.9635 1.9821 2.4726 -0.6496 0.2759  0.4955  169 PRO   A CG  
1130 C  CD  . PRO   A 149 ? 2.1039 2.0641 2.6515 -0.6896 0.2472  0.4860  169 PRO   A CD  
1131 N  N   . VAL   A 150 ? 2.2386 2.1427 2.6466 -0.6053 0.1637  0.4089  170 VAL   A N   
1132 C  CA  . VAL   A 150 ? 2.3022 2.1776 2.6920 -0.5999 0.1249  0.3740  170 VAL   A CA  
1133 C  C   . VAL   A 150 ? 2.3223 2.2711 2.7008 -0.5627 0.1303  0.3529  170 VAL   A C   
1134 O  O   . VAL   A 150 ? 2.2193 2.1971 2.5654 -0.5319 0.1575  0.3658  170 VAL   A O   
1135 C  CB  . VAL   A 150 ? 2.1962 1.9684 2.5104 -0.5779 0.1128  0.3640  170 VAL   A CB  
1136 C  CG1 . VAL   A 150 ? 2.1777 1.9216 2.4584 -0.5553 0.0801  0.3178  170 VAL   A CG1 
1137 C  CG2 . VAL   A 150 ? 2.4045 2.0955 2.7280 -0.6144 0.1051  0.3835  170 VAL   A CG2 
1138 N  N   . THR   A 151 ? 2.5776 2.5532 2.9812 -0.5653 0.1024  0.3204  171 THR   A N   
1139 C  CA  . THR   A 151 ? 2.5036 2.5310 2.8892 -0.5288 0.1013  0.2957  171 THR   A CA  
1140 C  C   . THR   A 151 ? 2.4816 2.4411 2.7931 -0.4948 0.0873  0.2704  171 THR   A C   
1141 O  O   . THR   A 151 ? 2.5334 2.4318 2.8270 -0.5010 0.0578  0.2471  171 THR   A O   
1142 C  CB  . THR   A 151 ? 2.4950 2.5751 2.9353 -0.5439 0.0767  0.2737  171 THR   A CB  
1143 O  OG1 . THR   A 151 ? 2.5485 2.5622 2.9817 -0.5613 0.0373  0.2491  171 THR   A OG1 
1144 C  CG2 . THR   A 151 ? 2.4727 2.6266 2.9969 -0.5776 0.0925  0.3003  171 THR   A CG2 
1145 N  N   . LEU   A 152 ? 2.1514 2.1211 2.4203 -0.4582 0.1082  0.2747  172 LEU   A N   
1146 C  CA  . LEU   A 152 ? 2.0073 1.9160 2.2136 -0.4263 0.0999  0.2564  172 LEU   A CA  
1147 C  C   . LEU   A 152 ? 1.9592 1.8703 2.1538 -0.4099 0.0775  0.2199  172 LEU   A C   
1148 O  O   . LEU   A 152 ? 1.9407 1.7849 2.0982 -0.4016 0.0597  0.2004  172 LEU   A O   
1149 C  CB  . LEU   A 152 ? 1.9521 1.8791 2.1255 -0.3930 0.1247  0.2701  172 LEU   A CB  
1150 C  CG  . LEU   A 152 ? 1.9460 1.8593 2.1155 -0.4037 0.1471  0.3078  172 LEU   A CG  
1151 C  CD1 . LEU   A 152 ? 1.8749 1.8199 2.0138 -0.3697 0.1684  0.3192  172 LEU   A CD1 
1152 C  CD2 . LEU   A 152 ? 1.8896 1.7088 2.0295 -0.4118 0.1369  0.3137  172 LEU   A CD2 
1153 N  N   . LYS   A 153 ? 1.9521 1.9366 2.1748 -0.4034 0.0791  0.2111  173 LYS   A N   
1154 C  CA  . LYS   A 153 ? 1.8479 1.8348 2.0533 -0.3833 0.0613  0.1800  173 LYS   A CA  
1155 C  C   . LYS   A 153 ? 1.9562 1.8995 2.1633 -0.4032 0.0290  0.1596  173 LYS   A C   
1156 O  O   . LYS   A 153 ? 1.8747 1.7860 2.0446 -0.3839 0.0134  0.1343  173 LYS   A O   
1157 C  CB  . LYS   A 153 ? 1.7744 1.8465 2.0118 -0.3733 0.0689  0.1770  173 LYS   A CB  
1158 C  CG  . LYS   A 153 ? 1.3725 1.4489 1.5799 -0.3406 0.0633  0.1529  173 LYS   A CG  
1159 C  CD  . LYS   A 153 ? 1.4811 1.6332 1.7101 -0.3239 0.0788  0.1559  173 LYS   A CD  
1160 C  CE  . LYS   A 153 ? 1.5078 1.6611 1.7108 -0.2939 0.0734  0.1341  173 LYS   A CE  
1161 N  NZ  . LYS   A 153 ? 1.7241 1.9408 1.9428 -0.2754 0.0882  0.1364  173 LYS   A NZ  
1162 N  N   . ASP   A 154 ? 1.9243 1.8637 2.1729 -0.4414 0.0180  0.1703  174 ASP   A N   
1163 C  CA  . ASP   A 154 ? 1.9709 1.8610 2.2195 -0.4621 -0.0181 0.1492  174 ASP   A CA  
1164 C  C   . ASP   A 154 ? 1.9115 1.7005 2.0975 -0.4520 -0.0270 0.1386  174 ASP   A C   
1165 O  O   . ASP   A 154 ? 1.8178 1.5610 1.9595 -0.4354 -0.0478 0.1105  174 ASP   A O   
1166 C  CB  . ASP   A 154 ? 2.2191 2.1322 2.5375 -0.5087 -0.0280 0.1650  174 ASP   A CB  
1167 C  CG  . ASP   A 154 ? 2.2578 2.2714 2.6428 -0.5175 -0.0246 0.1700  174 ASP   A CG  
1168 O  OD1 . ASP   A 154 ? 2.1138 2.1718 2.4853 -0.4871 -0.0184 0.1584  174 ASP   A OD1 
1169 O  OD2 . ASP   A 154 ? 2.3287 2.3770 2.7826 -0.5547 -0.0276 0.1862  174 ASP   A OD2 
1170 N  N   . VAL   A 155 ? 2.0780 1.8292 2.2562 -0.4593 -0.0102 0.1618  175 VAL   A N   
1171 C  CA  . VAL   A 155 ? 1.9872 1.6413 2.1080 -0.4474 -0.0172 0.1533  175 VAL   A CA  
1172 C  C   . VAL   A 155 ? 1.9743 1.6164 2.0400 -0.4003 -0.0023 0.1419  175 VAL   A C   
1173 O  O   . VAL   A 155 ? 1.9514 1.5202 1.9657 -0.3818 -0.0115 0.1244  175 VAL   A O   
1174 C  CB  . VAL   A 155 ? 1.9617 1.5779 2.0918 -0.4682 -0.0038 0.1840  175 VAL   A CB  
1175 C  CG1 . VAL   A 155 ? 1.9391 1.5919 2.0611 -0.4452 0.0319  0.2105  175 VAL   A CG1 
1176 C  CG2 . VAL   A 155 ? 1.9636 1.4702 2.0450 -0.4659 -0.0210 0.1720  175 VAL   A CG2 
1177 N  N   . PHE   A 156 ? 2.0360 1.7484 2.1132 -0.3800 0.0204  0.1509  176 PHE   A N   
1178 C  CA  . PHE   A 156 ? 1.8487 1.5584 1.8855 -0.3384 0.0321  0.1390  176 PHE   A CA  
1179 C  C   . PHE   A 156 ? 1.8333 1.5480 1.8537 -0.3249 0.0165  0.1100  176 PHE   A C   
1180 O  O   . PHE   A 156 ? 1.9572 1.6264 1.9312 -0.2979 0.0162  0.0935  176 PHE   A O   
1181 C  CB  . PHE   A 156 ? 1.7849 1.5631 1.8396 -0.3226 0.0577  0.1569  176 PHE   A CB  
1182 C  CG  . PHE   A 156 ? 1.8942 1.6541 1.9413 -0.3199 0.0751  0.1831  176 PHE   A CG  
1183 C  CD1 . PHE   A 156 ? 1.9445 1.6266 1.9553 -0.3111 0.0726  0.1841  176 PHE   A CD1 
1184 C  CD2 . PHE   A 156 ? 1.7775 1.5952 1.8490 -0.3230 0.0939  0.2066  176 PHE   A CD2 
1185 C  CE1 . PHE   A 156 ? 1.9099 1.5724 1.9109 -0.3063 0.0867  0.2094  176 PHE   A CE1 
1186 C  CE2 . PHE   A 156 ? 1.7348 1.5321 1.7915 -0.3180 0.1087  0.2318  176 PHE   A CE2 
1187 C  CZ  . PHE   A 156 ? 1.7962 1.5159 1.8185 -0.3099 0.1042  0.2338  176 PHE   A CZ  
1188 N  N   . GLY   A 157 ? 1.9170 1.6868 1.9742 -0.3414 0.0048  0.1050  177 GLY   A N   
1189 C  CA  . GLY   A 157 ? 1.8589 1.6301 1.8969 -0.3286 -0.0126 0.0792  177 GLY   A CA  
1190 C  C   . GLY   A 157 ? 2.0324 1.7236 2.0300 -0.3337 -0.0402 0.0573  177 GLY   A C   
1191 O  O   . GLY   A 157 ? 1.9506 1.6091 1.8997 -0.3085 -0.0463 0.0364  177 GLY   A O   
1192 N  N   . ALA   A 158 ? 2.0412 1.6971 2.0564 -0.3661 -0.0572 0.0619  178 ALA   A N   
1193 C  CA  . ALA   A 158 ? 2.0328 1.6007 2.0042 -0.3705 -0.0856 0.0396  178 ALA   A CA  
1194 C  C   . ALA   A 158 ? 2.0485 1.5452 1.9542 -0.3367 -0.0703 0.0333  178 ALA   A C   
1195 O  O   . ALA   A 158 ? 2.1284 1.5653 1.9764 -0.3171 -0.0843 0.0082  178 ALA   A O   
1196 C  CB  . ALA   A 158 ? 2.1049 1.6465 2.1145 -0.4141 -0.1047 0.0491  178 ALA   A CB  
1197 N  N   . TYR   A 159 ? 2.0032 1.5063 1.9155 -0.3270 -0.0416 0.0559  179 TYR   A N   
1198 C  CA  . TYR   A 159 ? 1.9979 1.4472 1.8581 -0.2911 -0.0245 0.0520  179 TYR   A CA  
1199 C  C   . TYR   A 159 ? 2.0505 1.5289 1.8864 -0.2546 -0.0095 0.0401  179 TYR   A C   
1200 O  O   . TYR   A 159 ? 2.0432 1.4678 1.8254 -0.2268 -0.0081 0.0223  179 TYR   A O   
1201 C  CB  . TYR   A 159 ? 1.9799 1.4370 1.8584 -0.2891 -0.0005 0.0804  179 TYR   A CB  
1202 C  CG  . TYR   A 159 ? 2.1045 1.5521 1.9530 -0.2471 0.0235  0.0814  179 TYR   A CG  
1203 C  CD1 . TYR   A 159 ? 2.2271 1.5942 2.0279 -0.2249 0.0241  0.0717  179 TYR   A CD1 
1204 C  CD2 . TYR   A 159 ? 2.0741 1.5936 1.9453 -0.2293 0.0447  0.0915  179 TYR   A CD2 
1205 C  CE1 . TYR   A 159 ? 2.1429 1.5081 1.9257 -0.1861 0.0468  0.0735  179 TYR   A CE1 
1206 C  CE2 . TYR   A 159 ? 1.9793 1.4945 1.8333 -0.1933 0.0643  0.0925  179 TYR   A CE2 
1207 C  CZ  . TYR   A 159 ? 2.0161 1.4575 1.8290 -0.1719 0.0661  0.0844  179 TYR   A CZ  
1208 O  OH  . TYR   A 159 ? 1.7750 1.2186 1.5798 -0.1356 0.0862  0.0863  179 TYR   A OH  
1209 N  N   . SER   A 160 ? 2.1910 1.7527 2.0656 -0.2536 0.0034  0.0505  180 SER   A N   
1210 C  CA  . SER   A 160 ? 1.9596 1.5505 1.8185 -0.2214 0.0197  0.0431  180 SER   A CA  
1211 C  C   . SER   A 160 ? 2.0210 1.5845 1.8397 -0.2120 0.0025  0.0182  180 SER   A C   
1212 O  O   . SER   A 160 ? 1.9707 1.5147 1.7503 -0.1804 0.0162  0.0087  180 SER   A O   
1213 C  CB  . SER   A 160 ? 1.8961 1.5761 1.8046 -0.2251 0.0322  0.0575  180 SER   A CB  
1214 O  OG  . SER   A 160 ? 1.9245 1.6275 1.8623 -0.2322 0.0466  0.0803  180 SER   A OG  
1215 N  N   . MET   A 161 ? 2.0879 1.6502 1.9162 -0.2385 -0.0276 0.0082  181 MET   A N   
1216 C  CA  . MET   A 161 ? 2.1201 1.6497 1.9028 -0.2286 -0.0496 -0.0167 181 MET   A CA  
1217 C  C   . MET   A 161 ? 2.2001 1.6330 1.9126 -0.2113 -0.0561 -0.0347 181 MET   A C   
1218 O  O   . MET   A 161 ? 2.1281 1.5272 1.7825 -0.1838 -0.0563 -0.0521 181 MET   A O   
1219 C  CB  . MET   A 161 ? 2.1863 1.7406 2.0029 -0.2619 -0.0851 -0.0235 181 MET   A CB  
1220 C  CG  . MET   A 161 ? 2.2121 1.7345 1.9801 -0.2515 -0.1141 -0.0499 181 MET   A CG  
1221 S  SD  . MET   A 161 ? 2.3742 1.9319 2.1125 -0.2126 -0.0927 -0.0519 181 MET   A SD  
1222 C  CE  . MET   A 161 ? 1.9383 1.6063 1.7641 -0.2324 -0.0890 -0.0332 181 MET   A CE  
1223 N  N   . ASP   A 162 ? 2.3186 1.7031 2.0319 -0.2249 -0.0600 -0.0303 182 ASP   A N   
1224 C  CA  . ASP   A 162 ? 2.4076 1.6961 2.0528 -0.2047 -0.0640 -0.0476 182 ASP   A CA  
1225 C  C   . ASP   A 162 ? 2.3548 1.6339 1.9646 -0.1604 -0.0271 -0.0451 182 ASP   A C   
1226 O  O   . ASP   A 162 ? 2.4426 1.6573 1.9846 -0.1314 -0.0254 -0.0641 182 ASP   A O   
1227 C  CB  . ASP   A 162 ? 2.4765 1.7166 2.1357 -0.2282 -0.0734 -0.0396 182 ASP   A CB  
1228 C  CG  . ASP   A 162 ? 2.5587 1.7917 2.2491 -0.2728 -0.1124 -0.0451 182 ASP   A CG  
1229 O  OD1 . ASP   A 162 ? 2.6217 1.8888 2.3220 -0.2832 -0.1343 -0.0572 182 ASP   A OD1 
1230 O  OD2 . ASP   A 162 ? 2.5719 1.7654 2.2798 -0.2976 -0.1216 -0.0365 182 ASP   A OD2 
1231 N  N   . VAL   A 163 ? 2.2648 1.6078 1.9203 -0.1538 0.0024  -0.0222 183 VAL   A N   
1232 C  CA  . VAL   A 163 ? 2.2837 1.6259 1.9208 -0.1146 0.0367  -0.0177 183 VAL   A CA  
1233 C  C   . VAL   A 163 ? 2.3483 1.7160 1.9632 -0.0917 0.0485  -0.0260 183 VAL   A C   
1234 O  O   . VAL   A 163 ? 2.4423 1.7741 2.0109 -0.0575 0.0682  -0.0339 183 VAL   A O   
1235 C  CB  . VAL   A 163 ? 2.1490 1.5484 1.8440 -0.1165 0.0586  0.0084  183 VAL   A CB  
1236 C  CG1 . VAL   A 163 ? 2.0212 1.4240 1.7083 -0.0776 0.0911  0.0130  183 VAL   A CG1 
1237 C  CG2 . VAL   A 163 ? 2.1444 1.5135 1.8551 -0.1383 0.0481  0.0198  183 VAL   A CG2 
1238 N  N   . ILE   A 164 ? 2.1875 1.6158 1.8341 -0.1089 0.0382  -0.0233 184 ILE   A N   
1239 C  CA  . ILE   A 164 ? 2.1822 1.6384 1.8132 -0.0875 0.0517  -0.0263 184 ILE   A CA  
1240 C  C   . ILE   A 164 ? 2.2172 1.6100 1.7717 -0.0717 0.0368  -0.0493 184 ILE   A C   
1241 O  O   . ILE   A 164 ? 2.1629 1.5453 1.6781 -0.0409 0.0584  -0.0519 184 ILE   A O   
1242 C  CB  . ILE   A 164 ? 2.1471 1.6841 1.8341 -0.1079 0.0445  -0.0164 184 ILE   A CB  
1243 C  CG1 . ILE   A 164 ? 1.9048 1.4961 1.6234 -0.0897 0.0764  -0.0015 184 ILE   A CG1 
1244 C  CG2 . ILE   A 164 ? 2.1210 1.6549 1.7808 -0.1122 0.0188  -0.0316 184 ILE   A CG2 
1245 C  CD1 . ILE   A 164 ? 1.9581 1.5272 1.6321 -0.0570 0.0973  -0.0067 184 ILE   A CD1 
1246 N  N   . THR   A 165 ? 2.3329 1.6805 1.8635 -0.0916 -0.0001 -0.0659 185 THR   A N   
1247 C  CA  . THR   A 165 ? 2.3178 1.5995 1.7681 -0.0753 -0.0200 -0.0908 185 THR   A CA  
1248 C  C   . THR   A 165 ? 2.5786 1.7795 1.9583 -0.0413 -0.0016 -0.1019 185 THR   A C   
1249 O  O   . THR   A 165 ? 2.6968 1.8487 1.9997 -0.0132 -0.0013 -0.1183 185 THR   A O   
1250 C  CB  . THR   A 165 ? 2.4128 1.6708 1.8647 -0.1087 -0.0701 -0.1072 185 THR   A CB  
1251 O  OG1 . THR   A 165 ? 2.5253 1.7574 2.0059 -0.1323 -0.0784 -0.1033 185 THR   A OG1 
1252 C  CG2 . THR   A 165 ? 2.3717 1.7105 1.8864 -0.1356 -0.0880 -0.0989 185 THR   A CG2 
1253 N  N   . SER   A 166 ? 2.6862 1.8711 2.0870 -0.0403 0.0146  -0.0927 186 SER   A N   
1254 C  CA  . SER   A 166 ? 2.7721 1.8824 2.1124 -0.0059 0.0336  -0.1025 186 SER   A CA  
1255 C  C   . SER   A 166 ? 2.7304 1.8725 2.0830 0.0287  0.0836  -0.0856 186 SER   A C   
1256 O  O   . SER   A 166 ? 2.8175 1.9098 2.1086 0.0670  0.1061  -0.0948 186 SER   A O   
1257 C  CB  . SER   A 166 ? 2.7431 1.8067 2.0957 -0.0227 0.0189  -0.1035 186 SER   A CB  
1258 O  OG  . SER   A 166 ? 2.7060 1.8352 2.1432 -0.0523 0.0216  -0.0790 186 SER   A OG  
1259 N  N   . THR   A 167 ? 2.4286 1.6521 1.8598 0.0171  0.1014  -0.0615 187 THR   A N   
1260 C  CA  . THR   A 167 ? 2.4092 1.6687 1.8635 0.0465  0.1451  -0.0455 187 THR   A CA  
1261 C  C   . THR   A 167 ? 2.5128 1.7893 1.9392 0.0683  0.1656  -0.0459 187 THR   A C   
1262 O  O   . THR   A 167 ? 2.5647 1.8526 1.9940 0.0983  0.2044  -0.0360 187 THR   A O   
1263 C  CB  . THR   A 167 ? 2.3782 1.7172 1.9216 0.0273  0.1526  -0.0222 187 THR   A CB  
1264 O  OG1 . THR   A 167 ? 2.3545 1.7434 1.9322 -0.0059 0.1287  -0.0192 187 THR   A OG1 
1265 C  CG2 . THR   A 167 ? 2.3633 1.6805 1.9284 0.0194  0.1466  -0.0160 187 THR   A CG2 
1266 N  N   . SER   A 168 ? 2.5480 1.8271 1.9501 0.0543  0.1408  -0.0553 188 SER   A N   
1267 C  CA  . SER   A 168 ? 2.4388 1.7315 1.8113 0.0737  0.1578  -0.0532 188 SER   A CA  
1268 C  C   . SER   A 168 ? 2.5518 1.7697 1.8236 0.0928  0.1429  -0.0757 188 SER   A C   
1269 O  O   . SER   A 168 ? 2.6334 1.8371 1.8574 0.1239  0.1706  -0.0732 188 SER   A O   
1270 C  CB  . SER   A 168 ? 2.3848 1.7506 1.8131 0.0470  0.1433  -0.0428 188 SER   A CB  
1271 O  OG  . SER   A 168 ? 2.3704 1.8044 1.8834 0.0348  0.1596  -0.0228 188 SER   A OG  
1272 N  N   . PHE   A 169 ? 2.6381 1.8065 1.8757 0.0754  0.0996  -0.0971 189 PHE   A N   
1273 C  CA  . PHE   A 169 ? 2.5363 1.6289 1.6737 0.0930  0.0772  -0.1222 189 PHE   A CA  
1274 C  C   . PHE   A 169 ? 2.6831 1.6873 1.7630 0.1051  0.0667  -0.1434 189 PHE   A C   
1275 O  O   . PHE   A 169 ? 2.9558 1.9011 1.9584 0.1458  0.0913  -0.1524 189 PHE   A O   
1276 C  CB  . PHE   A 169 ? 2.5150 1.6243 1.6588 0.0624  0.0273  -0.1329 189 PHE   A CB  
1277 C  CG  . PHE   A 169 ? 2.3701 1.5665 1.5769 0.0492  0.0347  -0.1127 189 PHE   A CG  
1278 C  CD1 . PHE   A 169 ? 2.3498 1.5504 1.5134 0.0731  0.0484  -0.1087 189 PHE   A CD1 
1279 C  CD2 . PHE   A 169 ? 2.1617 1.4314 1.4664 0.0146  0.0288  -0.0973 189 PHE   A CD2 
1280 C  CE1 . PHE   A 169 ? 2.3632 1.6378 1.5836 0.0619  0.0540  -0.0908 189 PHE   A CE1 
1281 C  CE2 . PHE   A 169 ? 2.1391 1.4840 1.4978 0.0051  0.0350  -0.0810 189 PHE   A CE2 
1282 C  CZ  . PHE   A 169 ? 2.2475 1.5939 1.5655 0.0284  0.0466  -0.0784 189 PHE   A CZ  
1283 N  N   . GLY   A 170 ? 2.9362 1.9269 2.0503 0.0721  0.0324  -0.1507 190 GLY   A N   
1284 C  CA  . GLY   A 170 ? 2.9208 1.8235 1.9851 0.0816  0.0209  -0.1701 190 GLY   A CA  
1285 C  C   . GLY   A 170 ? 2.9973 1.8546 2.0516 0.0468  -0.0381 -0.1924 190 GLY   A C   
1286 O  O   . GLY   A 170 ? 3.0104 1.7787 2.0069 0.0552  -0.0565 -0.2148 190 GLY   A O   
1287 N  N   . VAL   A 171 ? 2.9093 1.8267 2.0226 0.0077  -0.0683 -0.1867 191 VAL   A N   
1288 C  CA  . VAL   A 171 ? 3.0383 1.9262 2.1584 -0.0301 -0.1256 -0.2055 191 VAL   A CA  
1289 C  C   . VAL   A 171 ? 3.0060 1.9124 2.2070 -0.0676 -0.1304 -0.1902 191 VAL   A C   
1290 O  O   . VAL   A 171 ? 2.8695 1.8572 2.1513 -0.0828 -0.1060 -0.1618 191 VAL   A O   
1291 C  CB  . VAL   A 171 ? 3.0235 1.9704 2.1708 -0.0515 -0.1555 -0.2063 191 VAL   A CB  
1292 C  CG1 . VAL   A 171 ? 3.1183 2.0491 2.2950 -0.0955 -0.2143 -0.2224 191 VAL   A CG1 
1293 C  CG2 . VAL   A 171 ? 3.0621 1.9773 2.1166 -0.0126 -0.1544 -0.2217 191 VAL   A CG2 
1294 N  N   . ASN   A 172 ? 3.1140 1.9405 2.2896 -0.0818 -0.1625 -0.2091 192 ASN   A N   
1295 C  CA  . ASN   A 172 ? 3.1229 1.9492 2.3641 -0.1169 -0.1689 -0.1948 192 ASN   A CA  
1296 C  C   . ASN   A 172 ? 3.0930 1.9336 2.3845 -0.1688 -0.2199 -0.2009 192 ASN   A C   
1297 O  O   . ASN   A 172 ? 3.1260 1.9010 2.3688 -0.1752 -0.2648 -0.2311 192 ASN   A O   
1298 C  CB  . ASN   A 172 ? 3.2277 1.9498 2.4103 -0.0962 -0.1662 -0.2088 192 ASN   A CB  
1299 C  CG  . ASN   A 172 ? 3.3965 2.0170 2.4740 -0.0737 -0.1978 -0.2487 192 ASN   A CG  
1300 O  OD1 . ASN   A 172 ? 3.4296 2.0187 2.4286 -0.0255 -0.1738 -0.2605 192 ASN   A OD1 
1301 N  ND2 . ASN   A 172 ? 3.3931 1.9609 2.4684 -0.1082 -0.2520 -0.2697 192 ASN   A ND2 
1302 N  N   . ILE   A 173 ? 2.9933 1.9195 2.3826 -0.2049 -0.2132 -0.1726 193 ILE   A N   
1303 C  CA  . ILE   A 173 ? 2.9304 1.8895 2.3860 -0.2557 -0.2542 -0.1721 193 ILE   A CA  
1304 C  C   . ILE   A 173 ? 2.9373 1.9415 2.4804 -0.2901 -0.2371 -0.1393 193 ILE   A C   
1305 O  O   . ILE   A 173 ? 2.7061 1.7758 2.2852 -0.2796 -0.1960 -0.1123 193 ILE   A O   
1306 C  CB  . ILE   A 173 ? 2.8599 1.9019 2.3436 -0.2600 -0.2650 -0.1721 193 ILE   A CB  
1307 C  CG1 . ILE   A 173 ? 2.8197 1.8054 2.2159 -0.2353 -0.2972 -0.2069 193 ILE   A CG1 
1308 C  CG2 . ILE   A 173 ? 2.9509 2.0589 2.5331 -0.3125 -0.2914 -0.1593 193 ILE   A CG2 
1309 C  CD1 . ILE   A 173 ? 2.7157 1.7744 2.1312 -0.2350 -0.3104 -0.2074 193 ILE   A CD1 
1310 N  N   . ASP   A 174 ? 3.1001 2.0665 2.6756 -0.3310 -0.2693 -0.1413 194 ASP   A N   
1311 C  CA  . ASP   A 174 ? 3.0784 2.0870 2.7387 -0.3690 -0.2563 -0.1080 194 ASP   A CA  
1312 C  C   . ASP   A 174 ? 3.0593 2.1759 2.8042 -0.4005 -0.2630 -0.0931 194 ASP   A C   
1313 O  O   . ASP   A 174 ? 3.1069 2.2280 2.8852 -0.4340 -0.3045 -0.1055 194 ASP   A O   
1314 C  CB  . ASP   A 174 ? 2.9769 1.8983 2.6396 -0.4013 -0.2870 -0.1146 194 ASP   A CB  
1315 C  CG  . ASP   A 174 ? 2.9074 1.8632 2.6509 -0.4393 -0.2697 -0.0766 194 ASP   A CG  
1316 O  OD1 . ASP   A 174 ? 2.8822 1.9217 2.6677 -0.4339 -0.2310 -0.0465 194 ASP   A OD1 
1317 O  OD2 . ASP   A 174 ? 3.0190 1.9146 2.7815 -0.4745 -0.2953 -0.0767 194 ASP   A OD2 
1318 N  N   . SER   A 175 ? 2.8165 2.0210 2.5987 -0.3889 -0.2234 -0.0670 195 SER   A N   
1319 C  CA  . SER   A 175 ? 2.7243 2.0330 2.5758 -0.4076 -0.2251 -0.0556 195 SER   A CA  
1320 C  C   . SER   A 175 ? 2.8377 2.1896 2.7804 -0.4585 -0.2331 -0.0325 195 SER   A C   
1321 O  O   . SER   A 175 ? 2.6905 2.1268 2.6929 -0.4670 -0.2046 -0.0043 195 SER   A O   
1322 C  CB  . SER   A 175 ? 2.6021 1.9845 2.4606 -0.3775 -0.1812 -0.0370 195 SER   A CB  
1323 O  OG  . SER   A 175 ? 2.6413 2.0071 2.4334 -0.3364 -0.1772 -0.0571 195 SER   A OG  
1324 N  N   . LEU   A 176 ? 2.9623 2.2556 2.9162 -0.4923 -0.2709 -0.0441 196 LEU   A N   
1325 C  CA  . LEU   A 176 ? 2.9252 2.2667 2.9742 -0.5447 -0.2871 -0.0271 196 LEU   A CA  
1326 C  C   . LEU   A 176 ? 2.9831 2.3202 3.0517 -0.5682 -0.3429 -0.0557 196 LEU   A C   
1327 O  O   . LEU   A 176 ? 2.8419 2.2331 3.0009 -0.6118 -0.3594 -0.0433 196 LEU   A O   
1328 C  CB  . LEU   A 176 ? 2.8691 2.1532 2.9386 -0.5748 -0.2809 -0.0066 196 LEU   A CB  
1329 C  CG  . LEU   A 176 ? 2.7577 2.1245 2.9162 -0.6050 -0.2483 0.0370  196 LEU   A CG  
1330 C  CD1 . LEU   A 176 ? 2.5905 2.0250 2.7374 -0.5685 -0.1993 0.0573  196 LEU   A CD1 
1331 C  CD2 . LEU   A 176 ? 2.6705 1.9740 2.8458 -0.6356 -0.2428 0.0598  196 LEU   A CD2 
1332 N  N   . ASP   A 197 ? 2.2839 2.9914 2.7705 -0.1326 0.0192  0.0492  217 ASP   A N   
1333 C  CA  . ASP   A 197 ? 2.2371 2.9673 2.7220 -0.0983 0.0241  0.0407  217 ASP   A CA  
1334 C  C   . ASP   A 197 ? 2.3612 3.1508 2.8998 -0.0891 0.0068  0.0368  217 ASP   A C   
1335 O  O   . ASP   A 197 ? 2.3248 3.1808 2.9098 -0.0805 0.0233  0.0423  217 ASP   A O   
1336 C  CB  . ASP   A 197 ? 2.1385 2.8945 2.6225 -0.0862 0.0570  0.0470  217 ASP   A CB  
1337 C  CG  . ASP   A 197 ? 2.0983 2.8542 2.5625 -0.0495 0.0615  0.0347  217 ASP   A CG  
1338 O  OD1 . ASP   A 197 ? 2.1462 2.9377 2.6382 -0.0308 0.0514  0.0281  217 ASP   A OD1 
1339 O  OD2 . ASP   A 197 ? 2.0198 2.7383 2.4421 -0.0389 0.0733  0.0312  217 ASP   A OD2 
1340 N  N   . PRO   A 198 ? 2.3858 3.1529 2.9177 -0.0891 -0.0263 0.0279  218 PRO   A N   
1341 C  CA  . PRO   A 198 ? 2.3317 3.1531 2.9124 -0.0752 -0.0472 0.0229  218 PRO   A CA  
1342 C  C   . PRO   A 198 ? 2.2175 3.0055 2.7601 -0.0428 -0.0666 0.0104  218 PRO   A C   
1343 O  O   . PRO   A 198 ? 2.1191 2.9518 2.6941 -0.0183 -0.0735 0.0063  218 PRO   A O   
1344 C  CB  . PRO   A 198 ? 2.2994 3.1288 2.9133 -0.1071 -0.0755 0.0245  218 PRO   A CB  
1345 C  CG  . PRO   A 198 ? 2.3650 3.1106 2.9140 -0.1258 -0.0789 0.0232  218 PRO   A CG  
1346 C  CD  . PRO   A 198 ? 2.4402 3.1465 2.9369 -0.1108 -0.0476 0.0252  218 PRO   A CD  
1347 N  N   . PHE   A 199 ? 2.3446 3.0542 2.8194 -0.0413 -0.0739 0.0058  219 PHE   A N   
1348 C  CA  . PHE   A 199 ? 2.3033 2.9698 2.7362 -0.0166 -0.0958 -0.0026 219 PHE   A CA  
1349 C  C   . PHE   A 199 ? 2.2584 2.8637 2.6321 0.0008  -0.0774 -0.0039 219 PHE   A C   
1350 O  O   . PHE   A 199 ? 2.1185 2.7063 2.4727 0.0286  -0.0840 -0.0082 219 PHE   A O   
1351 C  CB  . PHE   A 199 ? 2.3734 3.0015 2.7815 -0.0325 -0.1281 -0.0062 219 PHE   A CB  
1352 C  CG  . PHE   A 199 ? 2.3145 2.8642 2.6466 -0.0152 -0.1381 -0.0102 219 PHE   A CG  
1353 C  CD1 . PHE   A 199 ? 2.1771 2.7189 2.4936 0.0127  -0.1610 -0.0147 219 PHE   A CD1 
1354 C  CD2 . PHE   A 199 ? 2.4156 2.8995 2.6920 -0.0257 -0.1234 -0.0078 219 PHE   A CD2 
1355 C  CE1 . PHE   A 199 ? 2.1159 2.5833 2.3592 0.0289  -0.1667 -0.0150 219 PHE   A CE1 
1356 C  CE2 . PHE   A 199 ? 2.4359 2.8504 2.6446 -0.0095 -0.1275 -0.0088 219 PHE   A CE2 
1357 C  CZ  . PHE   A 199 ? 2.2589 2.6638 2.4492 0.0173  -0.1482 -0.0114 219 PHE   A CZ  
1358 N  N   . PHE   A 200 ? 2.4541 3.0264 2.8022 -0.0152 -0.0556 0.0005  220 PHE   A N   
1359 C  CA  . PHE   A 200 ? 2.5017 3.0247 2.8070 -0.0010 -0.0379 -0.0003 220 PHE   A CA  
1360 C  C   . PHE   A 200 ? 2.3984 2.9533 2.7240 0.0216  -0.0230 -0.0040 220 PHE   A C   
1361 O  O   . PHE   A 200 ? 2.3932 2.9092 2.6899 0.0376  -0.0152 -0.0072 220 PHE   A O   
1362 C  CB  . PHE   A 200 ? 2.5285 3.0184 2.8117 -0.0224 -0.0197 0.0050  220 PHE   A CB  
1363 C  CG  . PHE   A 200 ? 2.6372 3.0897 2.8955 -0.0427 -0.0324 0.0070  220 PHE   A CG  
1364 C  CD1 . PHE   A 200 ? 2.6273 3.1081 2.9152 -0.0674 -0.0403 0.0098  220 PHE   A CD1 
1365 C  CD2 . PHE   A 200 ? 2.6597 3.0464 2.8644 -0.0365 -0.0354 0.0063  220 PHE   A CD2 
1366 C  CE1 . PHE   A 200 ? 2.6650 3.1049 2.9263 -0.0849 -0.0548 0.0087  220 PHE   A CE1 
1367 C  CE2 . PHE   A 200 ? 2.7124 3.0607 2.8870 -0.0512 -0.0466 0.0061  220 PHE   A CE2 
1368 C  CZ  . PHE   A 200 ? 2.7440 3.1167 2.9454 -0.0752 -0.0581 0.0058  220 PHE   A CZ  
1369 N  N   . LEU   A 201 ? 2.1242 2.7480 2.4996 0.0232  -0.0182 -0.0036 221 LEU   A N   
1370 C  CA  . LEU   A 201 ? 2.0463 2.7017 2.4379 0.0503  -0.0059 -0.0095 221 LEU   A CA  
1371 C  C   . LEU   A 201 ? 1.8663 2.5004 2.2441 0.0804  -0.0226 -0.0172 221 LEU   A C   
1372 O  O   . LEU   A 201 ? 1.8028 2.4220 2.1673 0.1039  -0.0140 -0.0242 221 LEU   A O   
1373 C  CB  . LEU   A 201 ? 1.9751 2.7129 2.4256 0.0485  0.0027  -0.0057 221 LEU   A CB  
1374 C  CG  . LEU   A 201 ? 1.9234 2.6943 2.3829 0.0576  0.0323  -0.0053 221 LEU   A CG  
1375 C  CD1 . LEU   A 201 ? 1.7282 2.5028 2.1811 0.0966  0.0352  -0.0177 221 LEU   A CD1 
1376 C  CD2 . LEU   A 201 ? 1.9789 2.7039 2.3981 0.0415  0.0474  -0.0020 221 LEU   A CD2 
1377 N  N   . SER   A 202 ? 2.1243 2.7522 2.5020 0.0809  -0.0484 -0.0162 222 SER   A N   
1378 C  CA  . SER   A 202 ? 2.0919 2.6929 2.4503 0.1102  -0.0661 -0.0208 222 SER   A CA  
1379 C  C   . SER   A 202 ? 2.1344 2.6508 2.4313 0.1119  -0.0655 -0.0184 222 SER   A C   
1380 O  O   . SER   A 202 ? 2.1059 2.5892 2.3811 0.1372  -0.0725 -0.0202 222 SER   A O   
1381 C  CB  . SER   A 202 ? 1.9766 2.6058 2.3575 0.1128  -0.0971 -0.0204 222 SER   A CB  
1382 O  OG  . SER   A 202 ? 1.7715 2.4847 2.2203 0.1072  -0.0967 -0.0203 222 SER   A OG  
1383 N  N   . ILE   A 203 ? 1.9407 2.4215 2.2111 0.0865  -0.0558 -0.0131 223 ILE   A N   
1384 C  CA  . ILE   A 203 ? 1.9484 2.3539 2.1662 0.0874  -0.0506 -0.0086 223 ILE   A CA  
1385 C  C   . ILE   A 203 ? 2.0707 2.4536 2.2836 0.1020  -0.0340 -0.0117 223 ILE   A C   
1386 O  O   . ILE   A 203 ? 2.1386 2.4703 2.3221 0.1166  -0.0355 -0.0088 223 ILE   A O   
1387 C  CB  . ILE   A 203 ? 1.8623 2.2419 2.0597 0.0590  -0.0410 -0.0030 223 ILE   A CB  
1388 C  CG1 . ILE   A 203 ? 1.9976 2.3588 2.1707 0.0513  -0.0626 -0.0008 223 ILE   A CG1 
1389 C  CG2 . ILE   A 203 ? 1.7715 2.0935 1.9361 0.0579  -0.0215 0.0015  223 ILE   A CG2 
1390 C  CD1 . ILE   A 203 ? 2.2353 2.5632 2.3821 0.0272  -0.0540 0.0031  223 ILE   A CD1 
1391 N  N   . THR   A 204 ? 1.8887 2.3065 2.1284 0.0986  -0.0188 -0.0174 224 THR   A N   
1392 C  CA  . THR   A 204 ? 1.7753 2.1661 2.0074 0.1086  -0.0060 -0.0229 224 THR   A CA  
1393 C  C   . THR   A 204 ? 1.7286 2.1217 1.9674 0.1401  -0.0139 -0.0316 224 THR   A C   
1394 O  O   . THR   A 204 ? 1.8593 2.2042 2.0806 0.1513  -0.0124 -0.0341 224 THR   A O   
1395 C  CB  . THR   A 204 ? 1.6035 2.0252 1.8523 0.0964  0.0102  -0.0269 224 THR   A CB  
1396 O  OG1 . THR   A 204 ? 1.7946 2.2372 2.0498 0.0708  0.0135  -0.0188 224 THR   A OG1 
1397 C  CG2 . THR   A 204 ? 1.6436 2.0192 1.8749 0.0923  0.0202  -0.0289 224 THR   A CG2 
1398 N  N   . VAL   A 205 ? 1.8050 2.2534 2.0725 0.1551  -0.0222 -0.0361 225 VAL   A N   
1399 C  CA  . VAL   A 205 ? 1.9295 2.3786 2.2024 0.1891  -0.0312 -0.0444 225 VAL   A CA  
1400 C  C   . VAL   A 205 ? 2.1325 2.5416 2.3826 0.2018  -0.0507 -0.0373 225 VAL   A C   
1401 O  O   . VAL   A 205 ? 2.0863 2.4655 2.3258 0.2286  -0.0576 -0.0411 225 VAL   A O   
1402 C  CB  . VAL   A 205 ? 1.9211 2.4487 2.2375 0.2045  -0.0305 -0.0511 225 VAL   A CB  
1403 C  CG1 . VAL   A 205 ? 1.7721 2.2971 2.0912 0.2430  -0.0334 -0.0634 225 VAL   A CG1 
1404 C  CG2 . VAL   A 205 ? 1.7032 2.2737 2.0376 0.1864  -0.0098 -0.0519 225 VAL   A CG2 
1405 N  N   . PHE   A 206 ? 2.4102 2.8122 2.6471 0.1846  -0.0607 -0.0271 226 PHE   A N   
1406 C  CA  . PHE   A 206 ? 2.5019 2.8581 2.7043 0.1965  -0.0792 -0.0188 226 PHE   A CA  
1407 C  C   . PHE   A 206 ? 2.5077 2.8019 2.6652 0.1755  -0.0705 -0.0074 226 PHE   A C   
1408 O  O   . PHE   A 206 ? 2.5226 2.8088 2.6590 0.1651  -0.0818 -0.0012 226 PHE   A O   
1409 C  CB  . PHE   A 206 ? 2.5542 2.9561 2.7756 0.2014  -0.1043 -0.0186 226 PHE   A CB  
1410 C  CG  . PHE   A 206 ? 2.5587 3.0381 2.8373 0.2177  -0.1090 -0.0281 226 PHE   A CG  
1411 C  CD1 . PHE   A 206 ? 2.5684 3.0529 2.8592 0.2457  -0.1012 -0.0363 226 PHE   A CD1 
1412 C  CD2 . PHE   A 206 ? 2.5493 3.0962 2.8714 0.2055  -0.1208 -0.0287 226 PHE   A CD2 
1413 C  CE1 . PHE   A 206 ? 2.5773 3.1348 2.9196 0.2641  -0.1018 -0.0446 226 PHE   A CE1 
1414 C  CE2 . PHE   A 206 ? 2.5095 3.1335 2.8909 0.2207  -0.1212 -0.0350 226 PHE   A CE2 
1415 C  CZ  . PHE   A 206 ? 2.4937 3.1241 2.8836 0.2516  -0.1100 -0.0427 226 PHE   A CZ  
1416 N  N   . PRO   A 207 ? 2.1928 2.4423 2.3357 0.1698  -0.0510 -0.0049 227 PRO   A N   
1417 C  CA  . PRO   A 207 ? 2.1436 2.3339 2.2463 0.1546  -0.0402 0.0082  227 PRO   A CA  
1418 C  C   . PRO   A 207 ? 2.1527 2.2880 2.2115 0.1733  -0.0502 0.0202  227 PRO   A C   
1419 O  O   . PRO   A 207 ? 2.0997 2.1913 2.1175 0.1649  -0.0437 0.0326  227 PRO   A O   
1420 C  CB  . PRO   A 207 ? 2.1169 2.2838 2.2300 0.1455  -0.0189 0.0068  227 PRO   A CB  
1421 C  CG  . PRO   A 207 ? 2.2311 2.4110 2.3669 0.1677  -0.0250 -0.0049 227 PRO   A CG  
1422 C  CD  . PRO   A 207 ? 2.2342 2.4794 2.3948 0.1798  -0.0402 -0.0141 227 PRO   A CD  
1423 N  N   . PHE   A 208 ? 2.0871 2.2215 2.1499 0.2011  -0.0648 0.0174  228 PHE   A N   
1424 C  CA  . PHE   A 208 ? 2.1865 2.2725 2.2053 0.2230  -0.0788 0.0296  228 PHE   A CA  
1425 C  C   . PHE   A 208 ? 2.1632 2.2684 2.1619 0.2249  -0.1026 0.0308  228 PHE   A C   
1426 O  O   . PHE   A 208 ? 2.1838 2.2399 2.1298 0.2385  -0.1127 0.0430  228 PHE   A O   
1427 C  CB  . PHE   A 208 ? 2.2803 2.3640 2.3128 0.2544  -0.0908 0.0247  228 PHE   A CB  
1428 C  CG  . PHE   A 208 ? 2.2984 2.4596 2.3817 0.2658  -0.1050 0.0072  228 PHE   A CG  
1429 C  CD1 . PHE   A 208 ? 2.2727 2.4736 2.3636 0.2804  -0.1316 0.0052  228 PHE   A CD1 
1430 C  CD2 . PHE   A 208 ? 2.2347 2.4296 2.3584 0.2634  -0.0918 -0.0069 228 PHE   A CD2 
1431 C  CE1 . PHE   A 208 ? 2.2367 2.5145 2.3823 0.2910  -0.1413 -0.0086 228 PHE   A CE1 
1432 C  CE2 . PHE   A 208 ? 2.2811 2.5484 2.4495 0.2762  -0.0997 -0.0208 228 PHE   A CE2 
1433 C  CZ  . PHE   A 208 ? 2.3246 2.6358 2.5080 0.2894  -0.1227 -0.0207 228 PHE   A CZ  
1434 N  N   . LEU   A 209 ? 2.1828 2.3563 2.2215 0.2118  -0.1126 0.0187  229 LEU   A N   
1435 C  CA  . LEU   A 209 ? 2.1182 2.3123 2.1460 0.2087  -0.1387 0.0172  229 LEU   A CA  
1436 C  C   . LEU   A 209 ? 2.1420 2.3030 2.1302 0.1841  -0.1301 0.0227  229 LEU   A C   
1437 O  O   . LEU   A 209 ? 2.1394 2.2980 2.1024 0.1831  -0.1538 0.0214  229 LEU   A O   
1438 C  CB  . LEU   A 209 ? 2.1646 2.4469 2.2596 0.2024  -0.1523 0.0037  229 LEU   A CB  
1439 C  CG  . LEU   A 209 ? 2.1335 2.4585 2.2637 0.2329  -0.1745 -0.0023 229 LEU   A CG  
1440 C  CD1 . LEU   A 209 ? 2.1060 2.5230 2.3076 0.2225  -0.1835 -0.0126 229 LEU   A CD1 
1441 C  CD2 . LEU   A 209 ? 2.1552 2.4434 2.2405 0.2564  -0.2057 0.0040  229 LEU   A CD2 
1442 N  N   . ILE   A 210 ? 2.1615 2.2969 2.1444 0.1658  -0.0987 0.0274  230 ILE   A N   
1443 C  CA  . ILE   A 210 ? 2.0972 2.1969 2.0401 0.1467  -0.0875 0.0331  230 ILE   A CA  
1444 C  C   . ILE   A 210 ? 2.2081 2.2393 2.0759 0.1638  -0.0933 0.0457  230 ILE   A C   
1445 O  O   . ILE   A 210 ? 2.2510 2.2679 2.0808 0.1591  -0.1075 0.0438  230 ILE   A O   
1446 C  CB  . ILE   A 210 ? 1.9561 2.0455 1.9146 0.1273  -0.0529 0.0363  230 ILE   A CB  
1447 C  CG1 . ILE   A 210 ? 1.8451 1.9997 1.8633 0.1085  -0.0501 0.0241  230 ILE   A CG1 
1448 C  CG2 . ILE   A 210 ? 2.0961 2.1365 2.0063 0.1155  -0.0368 0.0455  230 ILE   A CG2 
1449 C  CD1 . ILE   A 210 ? 1.8206 1.9676 1.8527 0.0901  -0.0214 0.0260  230 ILE   A CD1 
1450 N  N   . PRO   A 211 ? 2.2090 2.1926 2.0489 0.1843  -0.0836 0.0590  231 PRO   A N   
1451 C  CA  . PRO   A 211 ? 2.2596 2.1780 2.0213 0.2038  -0.0898 0.0732  231 PRO   A CA  
1452 C  C   . PRO   A 211 ? 2.2823 2.2154 2.0224 0.2214  -0.1330 0.0654  231 PRO   A C   
1453 O  O   . PRO   A 211 ? 2.2727 2.1599 1.9423 0.2315  -0.1443 0.0713  231 PRO   A O   
1454 C  CB  . PRO   A 211 ? 2.1761 2.0504 1.9283 0.2218  -0.0730 0.0892  231 PRO   A CB  
1455 C  CG  . PRO   A 211 ? 2.1724 2.0725 1.9867 0.2032  -0.0486 0.0842  231 PRO   A CG  
1456 C  CD  . PRO   A 211 ? 2.1871 2.1645 2.0587 0.1895  -0.0645 0.0630  231 PRO   A CD  
1457 N  N   . ILE   A 212 ? 2.3255 2.3221 2.1242 0.2270  -0.1581 0.0521  232 ILE   A N   
1458 C  CA  . ILE   A 212 ? 2.3009 2.3230 2.0941 0.2414  -0.2026 0.0432  232 ILE   A CA  
1459 C  C   . ILE   A 212 ? 2.2790 2.3127 2.0605 0.2191  -0.2176 0.0328  232 ILE   A C   
1460 O  O   . ILE   A 212 ? 2.3601 2.3611 2.0833 0.2302  -0.2454 0.0320  232 ILE   A O   
1461 C  CB  . ILE   A 212 ? 2.2796 2.3786 2.1525 0.2497  -0.2211 0.0312  232 ILE   A CB  
1462 C  CG1 . ILE   A 212 ? 2.2826 2.3579 2.1524 0.2806  -0.2168 0.0399  232 ILE   A CG1 
1463 C  CG2 . ILE   A 212 ? 2.2296 2.3750 2.1204 0.2541  -0.2670 0.0193  232 ILE   A CG2 
1464 C  CD1 . ILE   A 212 ? 2.2834 2.4051 2.1873 0.3083  -0.2534 0.0322  232 ILE   A CD1 
1465 N  N   . LEU   A 213 ? 2.1927 2.2688 2.0259 0.1882  -0.2010 0.0243  233 LEU   A N   
1466 C  CA  . LEU   A 213 ? 2.1748 2.2647 2.0068 0.1649  -0.2170 0.0133  233 LEU   A CA  
1467 C  C   . LEU   A 213 ? 2.3997 2.4140 2.1481 0.1621  -0.2040 0.0194  233 LEU   A C   
1468 O  O   . LEU   A 213 ? 2.4034 2.4074 2.1244 0.1530  -0.2274 0.0094  233 LEU   A O   
1469 C  CB  . LEU   A 213 ? 2.1407 2.2919 2.0483 0.1342  -0.1997 0.0058  233 LEU   A CB  
1470 C  CG  . LEU   A 213 ? 2.0410 2.2675 2.0300 0.1381  -0.2023 0.0010  233 LEU   A CG  
1471 C  CD1 . LEU   A 213 ? 2.0524 2.3301 2.1023 0.1090  -0.1802 -0.0033 233 LEU   A CD1 
1472 C  CD2 . LEU   A 213 ? 1.9555 2.2272 1.9731 0.1506  -0.2460 -0.0073 233 LEU   A CD2 
1473 N  N   . GLU   A 214 ? 2.4757 2.4368 2.1847 0.1702  -0.1671 0.0353  234 GLU   A N   
1474 C  CA  . GLU   A 214 ? 2.5436 2.4344 2.1732 0.1714  -0.1490 0.0434  234 GLU   A CA  
1475 C  C   . GLU   A 214 ? 2.6265 2.4650 2.1703 0.1983  -0.1785 0.0454  234 GLU   A C   
1476 O  O   . GLU   A 214 ? 2.7087 2.4991 2.1840 0.1991  -0.1790 0.0435  234 GLU   A O   
1477 C  CB  . GLU   A 214 ? 2.5472 2.3999 2.1658 0.1737  -0.1010 0.0625  234 GLU   A CB  
1478 C  CG  . GLU   A 214 ? 2.5250 2.4202 2.2182 0.1486  -0.0727 0.0601  234 GLU   A CG  
1479 C  CD  . GLU   A 214 ? 2.4761 2.3586 2.1597 0.1276  -0.0502 0.0582  234 GLU   A CD  
1480 O  OE1 . GLU   A 214 ? 2.5240 2.3839 2.1608 0.1266  -0.0656 0.0510  234 GLU   A OE1 
1481 O  OE2 . GLU   A 214 ? 2.4146 2.3075 2.1368 0.1136  -0.0189 0.0631  234 GLU   A OE2 
1482 N  N   . VAL   A 215 ? 2.4146 2.2589 1.9565 0.2231  -0.2040 0.0487  235 VAL   A N   
1483 C  CA  . VAL   A 215 ? 2.4097 2.2031 1.8661 0.2526  -0.2359 0.0515  235 VAL   A CA  
1484 C  C   . VAL   A 215 ? 2.4482 2.2798 1.9189 0.2498  -0.2925 0.0291  235 VAL   A C   
1485 O  O   . VAL   A 215 ? 2.4487 2.2391 1.8457 0.2731  -0.3272 0.0269  235 VAL   A O   
1486 C  CB  . VAL   A 215 ? 2.3028 2.0739 1.7425 0.2844  -0.2366 0.0687  235 VAL   A CB  
1487 C  CG1 . VAL   A 215 ? 2.2978 2.1370 1.8071 0.2928  -0.2767 0.0564  235 VAL   A CG1 
1488 C  CG2 . VAL   A 215 ? 2.3168 2.0036 1.6397 0.3163  -0.2444 0.0831  235 VAL   A CG2 
1489 N  N   . LEU   A 216 ? 2.2287 2.1367 1.7915 0.2218  -0.3034 0.0132  236 LEU   A N   
1490 C  CA  . LEU   A 216 ? 2.2339 2.1851 1.8268 0.2125  -0.3554 -0.0073 236 LEU   A CA  
1491 C  C   . LEU   A 216 ? 2.3452 2.2845 1.9262 0.1834  -0.3575 -0.0209 236 LEU   A C   
1492 O  O   . LEU   A 216 ? 2.3864 2.3645 2.0056 0.1674  -0.3983 -0.0387 236 LEU   A O   
1493 C  CB  . LEU   A 216 ? 2.0466 2.0947 1.7557 0.2013  -0.3669 -0.0143 236 LEU   A CB  
1494 C  CG  . LEU   A 216 ? 1.9263 1.9971 1.6684 0.2256  -0.3553 -0.0028 236 LEU   A CG  
1495 C  CD1 . LEU   A 216 ? 1.7822 1.9523 1.6381 0.2137  -0.3644 -0.0122 236 LEU   A CD1 
1496 C  CD2 . LEU   A 216 ? 2.0915 2.1201 1.7691 0.2655  -0.3872 0.0034  236 LEU   A CD2 
1497 N  N   . ASN   A 217 ? 2.2600 2.1473 1.7935 0.1762  -0.3149 -0.0127 237 ASN   A N   
1498 C  CA  . ASN   A 217 ? 2.3423 2.2169 1.8703 0.1488  -0.3072 -0.0237 237 ASN   A CA  
1499 C  C   . ASN   A 217 ? 2.3387 2.2922 1.9750 0.1131  -0.3054 -0.0323 237 ASN   A C   
1500 O  O   . ASN   A 217 ? 2.5386 2.4894 2.1823 0.0879  -0.3085 -0.0431 237 ASN   A O   
1501 C  CB  . ASN   A 217 ? 2.4793 2.3077 1.9349 0.1547  -0.3522 -0.0409 237 ASN   A CB  
1502 C  CG  . ASN   A 217 ? 2.6005 2.3746 2.0029 0.1414  -0.3318 -0.0469 237 ASN   A CG  
1503 O  OD1 . ASN   A 217 ? 2.8461 2.5569 2.1592 0.1551  -0.3549 -0.0575 237 ASN   A OD1 
1504 N  ND2 . ASN   A 217 ? 2.4631 2.2592 1.9165 0.1177  -0.2892 -0.0408 237 ASN   A ND2 
1505 N  N   . ILE   A 218 ? 2.3944 2.4151 2.1116 0.1120  -0.2995 -0.0270 238 ILE   A N   
1506 C  CA  . ILE   A 218 ? 2.2870 2.3809 2.1012 0.0813  -0.2893 -0.0312 238 ILE   A CA  
1507 C  C   . ILE   A 218 ? 2.4354 2.5083 2.2462 0.0646  -0.2410 -0.0234 238 ILE   A C   
1508 O  O   . ILE   A 218 ? 2.4581 2.4909 2.2307 0.0791  -0.2070 -0.0105 238 ILE   A O   
1509 C  CB  . ILE   A 218 ? 2.0320 2.1960 1.9217 0.0910  -0.2894 -0.0269 238 ILE   A CB  
1510 C  CG1 . ILE   A 218 ? 2.0748 2.2738 1.9859 0.1044  -0.3414 -0.0364 238 ILE   A CG1 
1511 C  CG2 . ILE   A 218 ? 1.9999 2.2318 1.9778 0.0636  -0.2661 -0.0271 238 ILE   A CG2 
1512 C  CD1 . ILE   A 218 ? 1.9472 2.2245 1.9423 0.1139  -0.3430 -0.0343 238 ILE   A CD1 
1513 N  N   . CYS   A 219 ? 2.6777 2.7767 2.5303 0.0336  -0.2386 -0.0303 239 CYS   A N   
1514 C  CA  . CYS   A 219 ? 2.7138 2.7919 2.5620 0.0180  -0.1981 -0.0242 239 CYS   A CA  
1515 C  C   . CYS   A 219 ? 2.6687 2.8141 2.6032 -0.0103 -0.1889 -0.0249 239 CYS   A C   
1516 O  O   . CYS   A 219 ? 2.7119 2.8990 2.6927 -0.0283 -0.2170 -0.0333 239 CYS   A O   
1517 C  CB  . CYS   A 219 ? 2.7887 2.7988 2.5662 0.0132  -0.2022 -0.0310 239 CYS   A CB  
1518 S  SG  . CYS   A 219 ? 2.8850 2.8420 2.6209 0.0147  -0.1485 -0.0191 239 CYS   A SG  
1519 N  N   . VAL   A 220 ? 2.4453 2.6009 2.4018 -0.0141 -0.1496 -0.0151 240 VAL   A N   
1520 C  CA  . VAL   A 220 ? 2.4071 2.6167 2.4316 -0.0388 -0.1361 -0.0137 240 VAL   A CA  
1521 C  C   . VAL   A 220 ? 2.4179 2.6085 2.4369 -0.0651 -0.1433 -0.0189 240 VAL   A C   
1522 O  O   . VAL   A 220 ? 2.3656 2.6019 2.4422 -0.0890 -0.1441 -0.0183 240 VAL   A O   
1523 C  CB  . VAL   A 220 ? 2.2881 2.5012 2.3243 -0.0348 -0.0961 -0.0038 240 VAL   A CB  
1524 C  CG1 . VAL   A 220 ? 2.2471 2.4813 2.2973 -0.0111 -0.0922 -0.0005 240 VAL   A CG1 
1525 C  CG2 . VAL   A 220 ? 2.2967 2.4427 2.2745 -0.0307 -0.0734 0.0009  240 VAL   A CG2 
1526 N  N   . PHE   A 221 ? 2.2838 2.4044 2.2323 -0.0600 -0.1469 -0.0232 241 PHE   A N   
1527 C  CA  . PHE   A 221 ? 2.3365 2.4272 2.2694 -0.0811 -0.1610 -0.0317 241 PHE   A CA  
1528 C  C   . PHE   A 221 ? 2.3940 2.4757 2.3096 -0.0804 -0.2090 -0.0459 241 PHE   A C   
1529 O  O   . PHE   A 221 ? 2.5608 2.5966 2.4095 -0.0556 -0.2220 -0.0502 241 PHE   A O   
1530 C  CB  . PHE   A 221 ? 2.4347 2.4523 2.2977 -0.0723 -0.1369 -0.0302 241 PHE   A CB  
1531 C  CG  . PHE   A 221 ? 2.3828 2.4006 2.2475 -0.0597 -0.0943 -0.0162 241 PHE   A CG  
1532 C  CD1 . PHE   A 221 ? 2.3116 2.3660 2.2291 -0.0749 -0.0702 -0.0084 241 PHE   A CD1 
1533 C  CD2 . PHE   A 221 ? 2.3955 2.3756 2.2092 -0.0330 -0.0797 -0.0102 241 PHE   A CD2 
1534 C  CE1 . PHE   A 221 ? 2.1585 2.2133 2.0807 -0.0640 -0.0366 0.0022  241 PHE   A CE1 
1535 C  CE2 . PHE   A 221 ? 2.2025 2.1839 2.0266 -0.0245 -0.0430 0.0025  241 PHE   A CE2 
1536 C  CZ  . PHE   A 221 ? 2.0479 2.0673 1.9276 -0.0402 -0.0236 0.0072  241 PHE   A CZ  
1537 N  N   . PRO   A 222 ? 2.3437 2.4674 2.3178 -0.1064 -0.2369 -0.0527 242 PRO   A N   
1538 C  CA  . PRO   A 222 ? 2.5071 2.6343 2.4796 -0.1061 -0.2883 -0.0671 242 PRO   A CA  
1539 C  C   . PRO   A 222 ? 2.5611 2.6004 2.4345 -0.0919 -0.3104 -0.0808 242 PRO   A C   
1540 O  O   . PRO   A 222 ? 2.5778 2.5614 2.4082 -0.1002 -0.2989 -0.0848 242 PRO   A O   
1541 C  CB  . PRO   A 222 ? 2.5063 2.6832 2.5606 -0.1443 -0.3064 -0.0700 242 PRO   A CB  
1542 C  CG  . PRO   A 222 ? 2.3732 2.5459 2.4432 -0.1628 -0.2651 -0.0585 242 PRO   A CG  
1543 C  CD  . PRO   A 222 ? 2.1518 2.3214 2.1978 -0.1379 -0.2226 -0.0461 242 PRO   A CD  
1544 N  N   . ARG   A 223 ? 2.6268 2.6520 2.4600 -0.0674 -0.3425 -0.0882 243 ARG   A N   
1545 C  CA  . ARG   A 223 ? 2.7284 2.6658 2.4510 -0.0440 -0.3582 -0.0988 243 ARG   A CA  
1546 C  C   . ARG   A 223 ? 2.7599 2.6515 2.4541 -0.0632 -0.3931 -0.1192 243 ARG   A C   
1547 O  O   . ARG   A 223 ? 2.8076 2.6175 2.4014 -0.0438 -0.4002 -0.1293 243 ARG   A O   
1548 C  CB  . ARG   A 223 ? 2.7174 2.6535 2.4060 -0.0135 -0.3903 -0.1015 243 ARG   A CB  
1549 C  CG  . ARG   A 223 ? 2.7545 2.7239 2.4817 -0.0244 -0.4537 -0.1189 243 ARG   A CG  
1550 C  CD  . ARG   A 223 ? 2.8406 2.8061 2.5291 0.0109  -0.4844 -0.1198 243 ARG   A CD  
1551 N  NE  . ARG   A 223 ? 2.9075 2.7936 2.4822 0.0467  -0.4593 -0.1115 243 ARG   A NE  
1552 C  CZ  . ARG   A 223 ? 3.0021 2.8026 2.4681 0.0634  -0.4760 -0.1231 243 ARG   A CZ  
1553 N  NH1 . ARG   A 223 ? 3.0007 2.7775 2.4516 0.0479  -0.5226 -0.1467 243 ARG   A NH1 
1554 N  NH2 . ARG   A 223 ? 3.0499 2.7852 2.4192 0.0966  -0.4444 -0.1106 243 ARG   A NH2 
1555 N  N   . GLU   A 224 ? 2.8918 2.8305 2.6695 -0.0999 -0.4142 -0.1251 244 GLU   A N   
1556 C  CA  . GLU   A 224 ? 2.9464 2.8375 2.7040 -0.1225 -0.4455 -0.1440 244 GLU   A CA  
1557 C  C   . GLU   A 224 ? 2.9147 2.7688 2.6602 -0.1373 -0.4049 -0.1382 244 GLU   A C   
1558 O  O   . GLU   A 224 ? 2.9780 2.7626 2.6694 -0.1434 -0.4217 -0.1543 244 GLU   A O   
1559 C  CB  . GLU   A 224 ? 3.0465 3.0030 2.9048 -0.1578 -0.4895 -0.1519 244 GLU   A CB  
1560 C  CG  . GLU   A 224 ? 2.9888 3.0389 2.9634 -0.1826 -0.4584 -0.1316 244 GLU   A CG  
1561 C  CD  . GLU   A 224 ? 3.1352 3.2638 3.2139 -0.2089 -0.4998 -0.1358 244 GLU   A CD  
1562 O  OE1 . GLU   A 224 ? 3.0797 3.1961 3.1430 -0.2040 -0.5557 -0.1545 244 GLU   A OE1 
1563 O  OE2 . GLU   A 224 ? 3.1162 3.3196 3.2923 -0.2333 -0.4765 -0.1199 244 GLU   A OE2 
1564 N  N   . VAL   A 225 ? 2.7645 2.6609 2.5569 -0.1414 -0.3543 -0.1168 245 VAL   A N   
1565 C  CA  . VAL   A 225 ? 2.6879 2.5475 2.4629 -0.1491 -0.3147 -0.1098 245 VAL   A CA  
1566 C  C   . VAL   A 225 ? 2.6948 2.4779 2.3652 -0.1142 -0.2892 -0.1106 245 VAL   A C   
1567 O  O   . VAL   A 225 ? 2.5862 2.3047 2.2045 -0.1134 -0.2794 -0.1174 245 VAL   A O   
1568 C  CB  . VAL   A 225 ? 2.4622 2.3915 2.3178 -0.1624 -0.2726 -0.0876 245 VAL   A CB  
1569 C  CG1 . VAL   A 225 ? 2.2397 2.1299 2.0709 -0.1634 -0.2313 -0.0791 245 VAL   A CG1 
1570 C  CG2 . VAL   A 225 ? 2.4349 2.4340 2.3902 -0.1983 -0.2922 -0.0850 245 VAL   A CG2 
1571 N  N   . THR   A 226 ? 2.7162 2.5044 2.3552 -0.0839 -0.2766 -0.1025 246 THR   A N   
1572 C  CA  . THR   A 226 ? 2.7166 2.4357 2.2595 -0.0503 -0.2489 -0.0996 246 THR   A CA  
1573 C  C   . THR   A 226 ? 2.9646 2.6061 2.4102 -0.0333 -0.2855 -0.1209 246 THR   A C   
1574 O  O   . THR   A 226 ? 3.0118 2.5815 2.3785 -0.0168 -0.2668 -0.1255 246 THR   A O   
1575 C  CB  . THR   A 226 ? 2.6609 2.4057 2.2020 -0.0251 -0.2244 -0.0823 246 THR   A CB  
1576 O  OG1 . THR   A 226 ? 2.8938 2.6680 2.4462 -0.0187 -0.2651 -0.0880 246 THR   A OG1 
1577 C  CG2 . THR   A 226 ? 2.3031 2.1119 1.9272 -0.0383 -0.1860 -0.0638 246 THR   A CG2 
1578 N  N   . ASN   A 227 ? 3.2348 2.8891 2.6831 -0.0349 -0.3386 -0.1348 247 ASN   A N   
1579 C  CA  . ASN   A 227 ? 3.3445 2.9233 2.6983 -0.0193 -0.3814 -0.1584 247 ASN   A CA  
1580 C  C   . ASN   A 227 ? 3.4057 2.9358 2.7452 -0.0408 -0.3957 -0.1770 247 ASN   A C   
1581 O  O   . ASN   A 227 ? 3.5510 2.9957 2.7888 -0.0210 -0.4097 -0.1948 247 ASN   A O   
1582 C  CB  . ASN   A 227 ? 3.3884 2.9993 2.7635 -0.0206 -0.4420 -0.1710 247 ASN   A CB  
1583 C  CG  . ASN   A 227 ? 3.4319 3.0432 2.7602 0.0168  -0.4387 -0.1598 247 ASN   A CG  
1584 O  OD1 . ASN   A 227 ? 3.4631 3.0211 2.7073 0.0483  -0.4018 -0.1491 247 ASN   A OD1 
1585 N  ND2 . ASN   A 227 ? 3.4335 3.1046 2.8180 0.0142  -0.4764 -0.1609 247 ASN   A ND2 
1586 N  N   . PHE   A 228 ? 3.0700 2.6489 2.5059 -0.0796 -0.3918 -0.1728 248 PHE   A N   
1587 C  CA  . PHE   A 228 ? 2.9693 2.4980 2.3941 -0.0997 -0.3957 -0.1855 248 PHE   A CA  
1588 C  C   . PHE   A 228 ? 2.8700 2.3377 2.2236 -0.0754 -0.3439 -0.1786 248 PHE   A C   
1589 O  O   . PHE   A 228 ? 2.8743 2.2739 2.1805 -0.0774 -0.3492 -0.1937 248 PHE   A O   
1590 C  CB  . PHE   A 228 ? 2.7512 2.3481 2.2959 -0.1446 -0.3937 -0.1756 248 PHE   A CB  
1591 C  CG  . PHE   A 228 ? 2.6466 2.1931 2.1866 -0.1659 -0.3902 -0.1830 248 PHE   A CG  
1592 C  CD1 . PHE   A 228 ? 2.7445 2.2193 2.2342 -0.1730 -0.4370 -0.2108 248 PHE   A CD1 
1593 C  CD2 . PHE   A 228 ? 2.3337 1.9009 1.9174 -0.1776 -0.3426 -0.1629 248 PHE   A CD2 
1594 C  CE1 . PHE   A 228 ? 2.6408 2.0628 2.1245 -0.1915 -0.4345 -0.2179 248 PHE   A CE1 
1595 C  CE2 . PHE   A 228 ? 2.4569 1.9742 2.0344 -0.1949 -0.3398 -0.1684 248 PHE   A CE2 
1596 C  CZ  . PHE   A 228 ? 2.5895 2.0331 2.1177 -0.2021 -0.3849 -0.1956 248 PHE   A CZ  
1597 N  N   . LEU   A 229 ? 3.0128 2.5025 2.3600 -0.0519 -0.2950 -0.1565 249 LEU   A N   
1598 C  CA  . LEU   A 229 ? 2.9821 2.4258 2.2750 -0.0283 -0.2426 -0.1468 249 LEU   A CA  
1599 C  C   . LEU   A 229 ? 3.2102 2.6086 2.4068 0.0154  -0.2231 -0.1426 249 LEU   A C   
1600 O  O   . LEU   A 229 ? 3.2175 2.5597 2.3483 0.0391  -0.1873 -0.1405 249 LEU   A O   
1601 C  CB  . LEU   A 229 ? 2.7931 2.3011 2.1704 -0.0412 -0.1946 -0.1212 249 LEU   A CB  
1602 C  CG  . LEU   A 229 ? 2.6444 2.2056 2.1198 -0.0829 -0.2072 -0.1191 249 LEU   A CG  
1603 C  CD1 . LEU   A 229 ? 2.3470 1.9748 1.8976 -0.0905 -0.1641 -0.0944 249 LEU   A CD1 
1604 C  CD2 . LEU   A 229 ? 2.4997 2.0016 1.9520 -0.0965 -0.2171 -0.1333 249 LEU   A CD2 
1605 N  N   . ARG   A 230 ? 3.2624 2.6829 2.4488 0.0283  -0.2435 -0.1398 250 ARG   A N   
1606 C  CA  . ARG   A 230 ? 3.4133 2.7824 2.4987 0.0705  -0.2279 -0.1347 250 ARG   A CA  
1607 C  C   . ARG   A 230 ? 3.5508 2.8232 2.5165 0.0937  -0.2496 -0.1586 250 ARG   A C   
1608 O  O   . ARG   A 230 ? 3.5695 2.7867 2.4371 0.1323  -0.2264 -0.1531 250 ARG   A O   
1609 C  CB  . ARG   A 230 ? 3.3793 2.7858 2.4748 0.0794  -0.2546 -0.1290 250 ARG   A CB  
1610 C  CG  . ARG   A 230 ? 3.2584 2.7484 2.4517 0.0676  -0.2256 -0.1043 250 ARG   A CG  
1611 C  CD  . ARG   A 230 ? 3.2097 2.7280 2.4043 0.0823  -0.2501 -0.0984 250 ARG   A CD  
1612 N  NE  . ARG   A 230 ? 3.2891 2.7491 2.3830 0.1227  -0.2299 -0.0873 250 ARG   A NE  
1613 C  CZ  . ARG   A 230 ? 3.2631 2.7368 2.3471 0.1424  -0.2343 -0.0741 250 ARG   A CZ  
1614 N  NH1 . ARG   A 230 ? 3.1374 2.6827 2.3065 0.1280  -0.2582 -0.0718 250 ARG   A NH1 
1615 N  NH2 . ARG   A 230 ? 3.3405 2.7530 2.3259 0.1791  -0.2123 -0.0616 250 ARG   A NH2 
1616 N  N   . LYS   A 231 ? 3.8538 3.1021 2.8234 0.0717  -0.2929 -0.1844 251 LYS   A N   
1617 C  CA  . LYS   A 231 ? 3.9695 3.1203 2.8291 0.0912  -0.3127 -0.2106 251 LYS   A CA  
1618 C  C   . LYS   A 231 ? 3.9347 3.0559 2.8092 0.0753  -0.2950 -0.2184 251 LYS   A C   
1619 O  O   . LYS   A 231 ? 4.0493 3.0872 2.8261 0.1024  -0.2832 -0.2317 251 LYS   A O   
1620 C  CB  . LYS   A 231 ? 4.0731 3.2020 2.9068 0.0827  -0.3912 -0.2404 251 LYS   A CB  
1621 C  CG  . LYS   A 231 ? 4.0191 3.2317 2.9830 0.0354  -0.4306 -0.2420 251 LYS   A CG  
1622 C  CD  . LYS   A 231 ? 4.1040 3.2955 3.0490 0.0259  -0.5106 -0.2726 251 LYS   A CD  
1623 C  CE  . LYS   A 231 ? 4.0178 3.3090 3.0961 -0.0131 -0.5442 -0.2673 251 LYS   A CE  
1624 N  NZ  . LYS   A 231 ? 3.9494 3.2997 3.1437 -0.0542 -0.5149 -0.2524 251 LYS   A NZ  
1625 N  N   . SER   A 232 ? 3.4601 2.6449 2.4502 0.0349  -0.2911 -0.2096 252 SER   A N   
1626 C  CA  . SER   A 232 ? 3.4471 2.6016 2.4531 0.0191  -0.2778 -0.2157 252 SER   A CA  
1627 C  C   . SER   A 232 ? 3.4750 2.6041 2.4447 0.0481  -0.2114 -0.1993 252 SER   A C   
1628 O  O   . SER   A 232 ? 3.4745 2.5420 2.4024 0.0558  -0.2010 -0.2109 252 SER   A O   
1629 C  CB  . SER   A 232 ? 3.2038 2.4353 2.3402 -0.0287 -0.2845 -0.2049 252 SER   A CB  
1630 O  OG  . SER   A 232 ? 3.1141 2.3667 2.2909 -0.0581 -0.3460 -0.2212 252 SER   A OG  
1631 N  N   . VAL   A 233 ? 3.3582 2.5339 2.3479 0.0640  -0.1666 -0.1724 253 VAL   A N   
1632 C  CA  . VAL   A 233 ? 3.2736 2.4289 2.2339 0.0922  -0.1039 -0.1560 253 VAL   A CA  
1633 C  C   . VAL   A 233 ? 3.3561 2.4228 2.1820 0.1375  -0.0951 -0.1680 253 VAL   A C   
1634 O  O   . VAL   A 233 ? 3.2932 2.3089 2.0700 0.1605  -0.0609 -0.1700 253 VAL   A O   
1635 C  CB  . VAL   A 233 ? 3.0716 2.3028 2.1004 0.0925  -0.0614 -0.1240 253 VAL   A CB  
1636 C  CG1 . VAL   A 233 ? 2.9534 2.1741 1.9745 0.1152  0.0017  -0.1061 253 VAL   A CG1 
1637 C  CG2 . VAL   A 233 ? 2.8754 2.1908 2.0254 0.0509  -0.0753 -0.1151 253 VAL   A CG2 
1638 N  N   . LYS   A 234 ? 3.4703 2.5168 2.2321 0.1537  -0.1253 -0.1757 254 LYS   A N   
1639 C  CA  . LYS   A 234 ? 3.5328 2.4851 2.1536 0.1958  -0.1297 -0.1929 254 LYS   A CA  
1640 C  C   . LYS   A 234 ? 3.5478 2.4274 2.1172 0.1906  -0.1733 -0.2290 254 LYS   A C   
1641 O  O   . LYS   A 234 ? 3.5713 2.3638 2.0248 0.2275  -0.1648 -0.2449 254 LYS   A O   
1642 C  CB  . LYS   A 234 ? 3.4443 2.3915 2.0090 0.2127  -0.1609 -0.1938 254 LYS   A CB  
1643 C  CG  . LYS   A 234 ? 3.2943 2.3073 1.9082 0.2170  -0.1236 -0.1590 254 LYS   A CG  
1644 C  CD  . LYS   A 234 ? 3.3301 2.3373 1.8934 0.2318  -0.1625 -0.1611 254 LYS   A CD  
1645 C  CE  . LYS   A 234 ? 3.0182 2.0883 1.6361 0.2339  -0.1287 -0.1269 254 LYS   A CE  
1646 N  NZ  . LYS   A 234 ? 3.0238 2.0894 1.5970 0.2489  -0.1692 -0.1280 254 LYS   A NZ  
1647 N  N   . ARG   A 235 ? 3.5440 2.4557 2.1970 0.1461  -0.2185 -0.2419 255 ARG   A N   
1648 C  CA  . ARG   A 235 ? 3.6395 2.4876 2.2664 0.1321  -0.2606 -0.2740 255 ARG   A CA  
1649 C  C   . ARG   A 235 ? 3.5723 2.4016 2.2228 0.1297  -0.2197 -0.2693 255 ARG   A C   
1650 O  O   . ARG   A 235 ? 3.6055 2.3934 2.2617 0.1095  -0.2514 -0.2910 255 ARG   A O   
1651 C  CB  . ARG   A 235 ? 3.6970 2.5934 2.4158 0.0821  -0.3231 -0.2851 255 ARG   A CB  
1652 C  CG  . ARG   A 235 ? 3.7536 2.5771 2.4280 0.0689  -0.3892 -0.3240 255 ARG   A CG  
1653 C  CD  . ARG   A 235 ? 3.7283 2.6161 2.5270 0.0119  -0.4350 -0.3260 255 ARG   A CD  
1654 N  NE  . ARG   A 235 ? 3.7506 2.7317 2.6223 -0.0013 -0.4449 -0.3080 255 ARG   A NE  
1655 C  CZ  . ARG   A 235 ? 3.6368 2.6988 2.6313 -0.0467 -0.4688 -0.2998 255 ARG   A CZ  
1656 N  NH1 . ARG   A 235 ? 3.5860 2.6498 2.6487 -0.0867 -0.4845 -0.3051 255 ARG   A NH1 
1657 N  NH2 . ARG   A 235 ? 3.5418 2.6838 2.5917 -0.0508 -0.4753 -0.2847 255 ARG   A NH2 
1658 N  N   . MET   A 236 ? 3.5885 2.4471 2.2569 0.1493  -0.1521 -0.2412 256 MET   A N   
1659 C  CA  . MET   A 236 ? 3.4854 2.3294 2.1763 0.1526  -0.1114 -0.2350 256 MET   A CA  
1660 C  C   . MET   A 236 ? 3.3737 2.1911 1.9989 0.2017  -0.0459 -0.2202 256 MET   A C   
1661 O  O   . MET   A 236 ? 3.3006 2.1713 1.9906 0.2033  0.0061  -0.1926 256 MET   A O   
1662 C  CB  . MET   A 236 ? 3.3869 2.3223 2.2161 0.1129  -0.0958 -0.2105 256 MET   A CB  
1663 C  CG  . MET   A 236 ? 3.3575 2.3194 2.2617 0.0632  -0.1495 -0.2211 256 MET   A CG  
1664 S  SD  . MET   A 236 ? 3.0158 2.0763 2.0648 0.0253  -0.1211 -0.1898 256 MET   A SD  
1665 C  CE  . MET   A 236 ? 3.1461 2.2280 2.2655 -0.0292 -0.1853 -0.2029 256 MET   A CE  
1666 N  N   . ASP   A 250 ? 3.1600 2.2852 2.3366 0.2595  0.3366  -0.0511 270 ASP   A N   
1667 C  CA  . ASP   A 250 ? 3.0461 2.2219 2.2812 0.2132  0.2969  -0.0477 270 ASP   A CA  
1668 C  C   . ASP   A 250 ? 2.9039 2.1364 2.1636 0.2057  0.3079  -0.0317 270 ASP   A C   
1669 O  O   . ASP   A 250 ? 2.9153 2.1350 2.1311 0.2343  0.3408  -0.0255 270 ASP   A O   
1670 C  CB  . ASP   A 250 ? 3.1694 2.2881 2.3487 0.1923  0.2434  -0.0734 270 ASP   A CB  
1671 C  CG  . ASP   A 250 ? 3.2713 2.3361 2.4400 0.1906  0.2262  -0.0874 270 ASP   A CG  
1672 O  OD1 . ASP   A 250 ? 3.2381 2.3289 2.4649 0.1943  0.2468  -0.0736 270 ASP   A OD1 
1673 O  OD2 . ASP   A 250 ? 3.3775 2.3718 2.4802 0.1855  0.1900  -0.1122 270 ASP   A OD2 
1674 N  N   . PHE   A 251 ? 2.7070 1.9996 2.0353 0.1681  0.2816  -0.0244 271 PHE   A N   
1675 C  CA  . PHE   A 251 ? 2.4846 1.8300 1.8410 0.1590  0.2875  -0.0102 271 PHE   A CA  
1676 C  C   . PHE   A 251 ? 2.4719 1.7703 1.7370 0.1748  0.2805  -0.0203 271 PHE   A C   
1677 O  O   . PHE   A 251 ? 2.4489 1.7614 1.7033 0.1909  0.3094  -0.0058 271 PHE   A O   
1678 C  CB  . PHE   A 251 ? 2.3861 1.7900 1.8145 0.1180  0.2528  -0.0070 271 PHE   A CB  
1679 C  CG  . PHE   A 251 ? 2.3732 1.8129 1.8098 0.1066  0.2428  -0.0011 271 PHE   A CG  
1680 C  CD1 . PHE   A 251 ? 2.3084 1.8013 1.7968 0.1097  0.2714  0.0194  271 PHE   A CD1 
1681 C  CD2 . PHE   A 251 ? 2.3845 1.8049 1.7817 0.0922  0.2021  -0.0164 271 PHE   A CD2 
1682 C  CE1 . PHE   A 251 ? 2.1258 1.6464 1.6203 0.1006  0.2613  0.0249  271 PHE   A CE1 
1683 C  CE2 . PHE   A 251 ? 2.2651 1.7183 1.6707 0.0845  0.1917  -0.0108 271 PHE   A CE2 
1684 C  CZ  . PHE   A 251 ? 2.0277 1.5287 1.4796 0.0895  0.2219  0.0100  271 PHE   A CZ  
1685 N  N   . LEU   A 252 ? 2.7360 1.9755 1.9335 0.1704  0.2411  -0.0449 272 LEU   A N   
1686 C  CA  . LEU   A 252 ? 2.6502 1.8356 1.7488 0.1901  0.2302  -0.0576 272 LEU   A CA  
1687 C  C   . LEU   A 252 ? 2.7849 1.9188 1.8078 0.2370  0.2769  -0.0550 272 LEU   A C   
1688 O  O   . LEU   A 252 ? 2.7833 1.9012 1.7483 0.2595  0.2948  -0.0483 272 LEU   A O   
1689 C  CB  . LEU   A 252 ? 2.6015 1.7321 1.6485 0.1752  0.1743  -0.0872 272 LEU   A CB  
1690 C  CG  . LEU   A 252 ? 2.5987 1.6545 1.5270 0.1997  0.1545  -0.1080 272 LEU   A CG  
1691 C  CD1 . LEU   A 252 ? 2.6148 1.7032 1.5404 0.1915  0.1359  -0.1015 272 LEU   A CD1 
1692 C  CD2 . LEU   A 252 ? 2.8409 1.8320 1.7248 0.1877  0.1040  -0.1396 272 LEU   A CD2 
1693 N  N   . GLN   A 253 ? 2.8357 1.9427 1.8570 0.2543  0.2992  -0.0587 273 GLN   A N   
1694 C  CA  . GLN   A 253 ? 3.0070 2.0713 1.9644 0.3017  0.3496  -0.0547 273 GLN   A CA  
1695 C  C   . GLN   A 253 ? 3.0138 2.1413 2.0290 0.3122  0.4038  -0.0217 273 GLN   A C   
1696 O  O   . GLN   A 253 ? 3.0023 2.1073 1.9564 0.3426  0.4383  -0.0120 273 GLN   A O   
1697 C  CB  . GLN   A 253 ? 3.1036 2.1324 2.0603 0.3173  0.3602  -0.0653 273 GLN   A CB  
1698 C  CG  . GLN   A 253 ? 3.2299 2.2122 2.1195 0.3701  0.4135  -0.0634 273 GLN   A CG  
1699 C  CD  . GLN   A 253 ? 3.3871 2.2634 2.1410 0.3986  0.3938  -0.0951 273 GLN   A CD  
1700 O  OE1 . GLN   A 253 ? 3.5313 2.3533 2.2585 0.4036  0.3740  -0.1172 273 GLN   A OE1 
1701 N  NE2 . GLN   A 253 ? 3.3766 2.2185 2.0402 0.4187  0.3975  -0.0979 273 GLN   A NE2 
1702 N  N   . LEU   A 254 ? 2.9019 2.1073 2.0344 0.2868  0.4108  -0.0036 274 LEU   A N   
1703 C  CA  . LEU   A 254 ? 2.8910 2.1595 2.0951 0.2927  0.4589  0.0268  274 LEU   A CA  
1704 C  C   . LEU   A 254 ? 2.8318 2.1241 2.0314 0.2843  0.4608  0.0414  274 LEU   A C   
1705 O  O   . LEU   A 254 ? 2.7993 2.1420 2.0614 0.2853  0.4983  0.0674  274 LEU   A O   
1706 C  CB  . LEU   A 254 ? 2.7502 2.0915 2.0770 0.2658  0.4549  0.0379  274 LEU   A CB  
1707 C  CG  . LEU   A 254 ? 2.7401 2.0656 2.0854 0.2720  0.4515  0.0277  274 LEU   A CG  
1708 C  CD1 . LEU   A 254 ? 2.4984 1.8964 1.9580 0.2430  0.4396  0.0391  274 LEU   A CD1 
1709 C  CD2 . LEU   A 254 ? 2.7957 2.0929 2.1127 0.3167  0.5031  0.0330  274 LEU   A CD2 
1710 N  N   . MET   A 255 ? 2.8043 2.0619 1.9362 0.2760  0.4207  0.0261  275 MET   A N   
1711 C  CA  . MET   A 255 ? 2.9021 2.1754 2.0216 0.2717  0.4197  0.0394  275 MET   A CA  
1712 C  C   . MET   A 255 ? 3.1567 2.3652 2.1604 0.3112  0.4461  0.0420  275 MET   A C   
1713 O  O   . MET   A 255 ? 3.3329 2.5571 2.3408 0.3244  0.4870  0.0681  275 MET   A O   
1714 C  CB  . MET   A 255 ? 2.7588 2.0432 1.8841 0.2390  0.3579  0.0234  275 MET   A CB  
1715 C  CG  . MET   A 255 ? 2.6565 2.0139 1.8972 0.2002  0.3372  0.0274  275 MET   A CG  
1716 S  SD  . MET   A 255 ? 2.5730 1.9522 1.8266 0.1651  0.2730  0.0129  275 MET   A SD  
1717 C  CE  . MET   A 255 ? 2.3953 1.8216 1.6844 0.1631  0.2898  0.0375  275 MET   A CE  
1718 N  N   . ILE   A 256 ? 3.2546 2.3868 2.1516 0.3307  0.4229  0.0155  276 ILE   A N   
1719 C  CA  . ILE   A 256 ? 3.3284 2.3916 2.1014 0.3732  0.4477  0.0160  276 ILE   A CA  
1720 C  C   . ILE   A 256 ? 3.5629 2.6197 2.3311 0.4092  0.5190  0.0350  276 ILE   A C   
1721 O  O   . ILE   A 256 ? 3.5943 2.6325 2.3150 0.4367  0.5538  0.0543  276 ILE   A O   
1722 C  CB  . ILE   A 256 ? 3.3445 2.3239 2.0031 0.3855  0.3995  -0.0211 276 ILE   A CB  
1723 C  CG1 . ILE   A 256 ? 3.1842 2.1859 1.8887 0.3414  0.3286  -0.0420 276 ILE   A CG1 
1724 C  CG2 . ILE   A 256 ? 3.2521 2.1675 1.7802 0.4205  0.4042  -0.0217 276 ILE   A CG2 
1725 C  CD1 . ILE   A 256 ? 2.9651 1.8894 1.5781 0.3461  0.2760  -0.0800 276 ILE   A CD1 
1726 N  N   . ASP   A 257 ? 3.7434 2.8251 2.5808 0.4057  0.5339  0.0330  277 ASP   A N   
1727 C  CA  . ASP   A 257 ? 3.8260 2.9158 2.6827 0.4372  0.5975  0.0527  277 ASP   A CA  
1728 C  C   . ASP   A 257 ? 3.7676 2.9328 2.7234 0.4263  0.6370  0.0923  277 ASP   A C   
1729 O  O   . ASP   A 257 ? 3.6546 2.8269 2.6233 0.4478  0.6766  0.1154  277 ASP   A O   
1730 C  CB  . ASP   A 257 ? 3.7343 2.8348 2.6454 0.4365  0.6006  0.0405  277 ASP   A CB  
1731 C  CG  . ASP   A 257 ? 3.8345 2.8586 2.6615 0.4427  0.5550  0.0025  277 ASP   A CG  
1732 O  OD1 . ASP   A 257 ? 3.9061 2.8719 2.6341 0.4458  0.5192  -0.0170 277 ASP   A OD1 
1733 O  OD2 . ASP   A 257 ? 3.9475 2.9683 2.8086 0.4443  0.5527  -0.0081 277 ASP   A OD2 
1734 N  N   . SER   A 258 ? 3.6424 2.8643 2.6747 0.3908  0.6224  0.1004  278 SER   A N   
1735 C  CA  . SER   A 258 ? 3.6051 2.8893 2.7231 0.3776  0.6529  0.1347  278 SER   A CA  
1736 C  C   . SER   A 258 ? 3.6849 2.9465 2.7438 0.3777  0.6423  0.1446  278 SER   A C   
1737 O  O   . SER   A 258 ? 3.6508 2.9574 2.7775 0.3632  0.6588  0.1712  278 SER   A O   
1738 C  CB  . SER   A 258 ? 3.3372 2.6995 2.5859 0.3365  0.6321  0.1386  278 SER   A CB  
1739 O  OG  . SER   A 258 ? 3.2590 2.6166 2.5015 0.3088  0.5670  0.1122  278 SER   A OG  
1740 N  N   . GLN   A 259 ? 3.6137 2.8047 2.5491 0.3939  0.6116  0.1227  279 GLN   A N   
1741 C  CA  . GLN   A 259 ? 3.5962 2.7562 2.4621 0.4026  0.6013  0.1317  279 GLN   A CA  
1742 C  C   . GLN   A 259 ? 3.6578 2.7759 2.4641 0.4401  0.6335  0.1450  279 GLN   A C   
1743 O  O   . GLN   A 259 ? 3.6392 2.7729 2.4689 0.4453  0.6635  0.1746  279 GLN   A O   
1744 C  CB  . GLN   A 259 ? 3.4595 2.5690 2.2276 0.3986  0.5428  0.0999  279 GLN   A CB  
1745 C  CG  . GLN   A 259 ? 3.4826 2.5439 2.1556 0.4179  0.5262  0.1035  279 GLN   A CG  
1746 C  CD  . GLN   A 259 ? 3.5133 2.5233 2.0916 0.4160  0.4614  0.0683  279 GLN   A CD  
1747 O  OE1 . GLN   A 259 ? 3.3856 2.4306 2.0282 0.3806  0.4128  0.0495  279 GLN   A OE1 
1748 N  NE2 . GLN   A 259 ? 3.4718 2.4186 1.9454 0.4444  0.4436  0.0601  279 GLN   A NE2 
1749 N  N   . ASN   A 260 ? 3.7432 2.8053 2.4718 0.4666  0.6277  0.1234  280 ASN   A N   
1750 C  CA  . ASN   A 260 ? 3.6833 2.7010 2.3472 0.5057  0.6588  0.1337  280 ASN   A CA  
1751 C  C   . ASN   A 260 ? 3.6613 2.6437 2.2507 0.5208  0.6557  0.1467  280 ASN   A C   
1752 O  O   . ASN   A 260 ? 3.6918 2.6156 2.1880 0.5558  0.6639  0.1453  280 ASN   A O   
1753 C  CB  . ASN   A 260 ? 3.5881 2.6567 2.3485 0.5114  0.7171  0.1634  280 ASN   A CB  
1754 C  CG  . ASN   A 260 ? 3.5261 2.6149 2.3390 0.5090  0.7222  0.1496  280 ASN   A CG  
1755 O  OD1 . ASN   A 260 ? 3.4766 2.5134 2.2174 0.5231  0.6977  0.1199  280 ASN   A OD1 
1756 N  ND2 . ASN   A 260 ? 3.4600 2.6226 2.4001 0.4913  0.7512  0.1703  280 ASN   A ND2 
1757 N  N   . LYS   A 268 ? 3.2492 2.5659 2.4084 0.3355  0.6963  0.3138  288 LYS   A N   
1758 C  CA  . LYS   A 268 ? 3.0839 2.4683 2.3716 0.3077  0.7059  0.3147  288 LYS   A CA  
1759 C  C   . LYS   A 268 ? 3.1388 2.5280 2.4158 0.3101  0.6929  0.2876  288 LYS   A C   
1760 O  O   . LYS   A 268 ? 3.0308 2.4700 2.4024 0.2947  0.7029  0.2861  288 LYS   A O   
1761 C  CB  . LYS   A 268 ? 3.0548 2.4671 2.4239 0.3091  0.7530  0.3413  288 LYS   A CB  
1762 C  CG  . LYS   A 268 ? 2.9100 2.3937 2.4241 0.2746  0.7555  0.3493  288 LYS   A CG  
1763 C  CD  . LYS   A 268 ? 2.8896 2.3978 2.4799 0.2767  0.7992  0.3755  288 LYS   A CD  
1764 C  CE  . LYS   A 268 ? 2.7335 2.3116 2.4685 0.2428  0.7955  0.3800  288 LYS   A CE  
1765 N  NZ  . LYS   A 268 ? 2.6109 2.2156 2.4238 0.2447  0.8357  0.4038  288 LYS   A NZ  
1766 N  N   . ALA   A 269 ? 3.2624 2.5964 2.4220 0.3302  0.6680  0.2653  289 ALA   A N   
1767 C  CA  . ALA   A 269 ? 3.2111 2.5357 2.3419 0.3339  0.6506  0.2366  289 ALA   A CA  
1768 C  C   . ALA   A 269 ? 3.1532 2.4674 2.2394 0.3182  0.5999  0.2131  289 ALA   A C   
1769 O  O   . ALA   A 269 ? 3.1886 2.5248 2.3077 0.2980  0.5735  0.2186  289 ALA   A O   
1770 C  CB  . ALA   A 269 ? 3.2898 2.5536 2.3214 0.3719  0.6638  0.2280  289 ALA   A CB  
1771 N  N   . LEU   A 270 ? 3.1637 2.4539 2.2049 0.3221  0.5666  0.1807  290 LEU   A N   
1772 C  CA  . LEU   A 270 ? 3.1754 2.4763 2.2245 0.2969  0.4972  0.1510  290 LEU   A CA  
1773 C  C   . LEU   A 270 ? 3.2435 2.4794 2.1678 0.3159  0.4604  0.1345  290 LEU   A C   
1774 O  O   . LEU   A 270 ? 3.4422 2.6129 2.2572 0.3514  0.4804  0.1327  290 LEU   A O   
1775 C  CB  . LEU   A 270 ? 3.0161 2.3315 2.1028 0.2842  0.4774  0.1259  290 LEU   A CB  
1776 C  CG  . LEU   A 270 ? 3.0254 2.3568 2.1323 0.2549  0.4103  0.0975  290 LEU   A CG  
1777 C  CD1 . LEU   A 270 ? 2.8737 2.2752 2.0848 0.2213  0.3922  0.1069  290 LEU   A CD1 
1778 C  CD2 . LEU   A 270 ? 2.9935 2.3218 2.1176 0.2486  0.3983  0.0762  290 LEU   A CD2 
1779 N  N   . SER   A 271 ? 2.9787 2.2336 1.9196 0.2937  0.4053  0.1216  291 SER   A N   
1780 C  CA  . SER   A 271 ? 2.8696 2.0725 1.7068 0.3081  0.3607  0.1045  291 SER   A CA  
1781 C  C   . SER   A 271 ? 2.9296 2.1190 1.7497 0.2962  0.3077  0.0666  291 SER   A C   
1782 O  O   . SER   A 271 ? 3.0117 2.2125 1.8717 0.2869  0.3166  0.0563  291 SER   A O   
1783 C  CB  . SER   A 271 ? 2.7821 2.0141 1.6496 0.2944  0.3339  0.1151  291 SER   A CB  
1784 O  OG  . SER   A 271 ? 2.7661 1.9634 1.5571 0.3017  0.2774  0.0932  291 SER   A OG  
1785 N  N   . ASP   A 272 ? 2.6706 1.8353 1.4350 0.2957  0.2511  0.0462  292 ASP   A N   
1786 C  CA  . ASP   A 272 ? 2.7245 1.8728 1.4732 0.2822  0.1970  0.0106  292 ASP   A CA  
1787 C  C   . ASP   A 272 ? 2.6004 1.8086 1.4334 0.2445  0.1432  -0.0007 292 ASP   A C   
1788 O  O   . ASP   A 272 ? 2.5347 1.7713 1.4302 0.2166  0.1208  -0.0169 292 ASP   A O   
1789 C  CB  . ASP   A 272 ? 2.8233 1.8855 1.4294 0.3149  0.1706  -0.0093 292 ASP   A CB  
1790 C  CG  . ASP   A 272 ? 3.0612 2.0585 1.5788 0.3521  0.2184  -0.0076 292 ASP   A CG  
1791 O  OD1 . ASP   A 272 ? 2.8685 1.8922 1.4426 0.3519  0.2729  0.0105  292 ASP   A OD1 
1792 O  OD2 . ASP   A 272 ? 3.3653 2.2853 1.7565 0.3831  0.2007  -0.0252 292 ASP   A OD2 
1793 N  N   . LEU   A 273 ? 2.5145 1.7413 1.3496 0.2445  0.1226  0.0083  293 LEU   A N   
1794 C  CA  . LEU   A 273 ? 2.5508 1.8436 1.4767 0.2109  0.0792  0.0009  293 LEU   A CA  
1795 C  C   . LEU   A 273 ? 2.5019 1.8663 1.5494 0.1832  0.1073  0.0152  293 LEU   A C   
1796 O  O   . LEU   A 273 ? 2.4003 1.8173 1.5273 0.1526  0.0778  0.0046  293 LEU   A O   
1797 C  CB  . LEU   A 273 ? 2.4515 1.7493 1.3557 0.2218  0.0568  0.0101  293 LEU   A CB  
1798 C  CG  . LEU   A 273 ? 2.3806 1.7473 1.3742 0.1931  0.0127  0.0031  293 LEU   A CG  
1799 C  CD1 . LEU   A 273 ? 2.4523 1.8258 1.4597 0.1714  -0.0408 -0.0277 293 LEU   A CD1 
1800 C  CD2 . LEU   A 273 ? 2.5889 1.9515 1.5502 0.2111  -0.0075 0.0128  293 LEU   A CD2 
1801 N  N   . GLU   A 274 ? 2.5291 1.8963 1.5926 0.1941  0.1639  0.0396  294 GLU   A N   
1802 C  CA  . GLU   A 274 ? 2.3650 1.7947 1.5388 0.1700  0.1886  0.0509  294 GLU   A CA  
1803 C  C   . GLU   A 274 ? 2.3040 1.7340 1.5011 0.1584  0.1913  0.0366  294 GLU   A C   
1804 O  O   . GLU   A 274 ? 2.1443 1.6283 1.4315 0.1326  0.1895  0.0368  294 GLU   A O   
1805 C  CB  . GLU   A 274 ? 2.4781 1.9116 1.6685 0.1838  0.2451  0.0812  294 GLU   A CB  
1806 C  CG  . GLU   A 274 ? 2.6655 2.0900 1.8287 0.1966  0.2459  0.0985  294 GLU   A CG  
1807 C  CD  . GLU   A 274 ? 2.7787 2.2025 1.9608 0.2077  0.3035  0.1306  294 GLU   A CD  
1808 O  OE1 . GLU   A 274 ? 2.7242 2.1276 1.8903 0.2208  0.3465  0.1395  294 GLU   A OE1 
1809 O  OE2 . GLU   A 274 ? 2.8186 2.2626 2.0353 0.2032  0.3060  0.1473  294 GLU   A OE2 
1810 N  N   . LEU   A 275 ? 2.4659 1.8323 1.5781 0.1792  0.1948  0.0240  295 LEU   A N   
1811 C  CA  . LEU   A 275 ? 2.3843 1.7416 1.5109 0.1700  0.1924  0.0084  295 LEU   A CA  
1812 C  C   . LEU   A 275 ? 2.2773 1.6604 1.4461 0.1376  0.1380  -0.0126 295 LEU   A C   
1813 O  O   . LEU   A 275 ? 2.1825 1.5931 1.4140 0.1163  0.1367  -0.0163 295 LEU   A O   
1814 C  CB  . LEU   A 275 ? 2.4089 1.6843 1.4250 0.2026  0.2038  -0.0035 295 LEU   A CB  
1815 C  CG  . LEU   A 275 ? 2.5350 1.7840 1.5484 0.2042  0.2130  -0.0171 295 LEU   A CG  
1816 C  CD1 . LEU   A 275 ? 2.7153 1.8957 1.6314 0.2468  0.2528  -0.0158 295 LEU   A CD1 
1817 C  CD2 . LEU   A 275 ? 2.5782 1.8056 1.5797 0.1834  0.1558  -0.0470 295 LEU   A CD2 
1818 N  N   . VAL   A 276 ? 2.2816 1.6573 1.4188 0.1340  0.0932  -0.0248 296 VAL   A N   
1819 C  CA  . VAL   A 276 ? 2.2834 1.6916 1.4709 0.1018  0.0428  -0.0420 296 VAL   A CA  
1820 C  C   . VAL   A 276 ? 2.1470 1.6389 1.4467 0.0747  0.0484  -0.0278 296 VAL   A C   
1821 O  O   . VAL   A 276 ? 2.0532 1.5792 1.4161 0.0470  0.0330  -0.0339 296 VAL   A O   
1822 C  CB  . VAL   A 276 ? 2.3725 1.7583 1.5051 0.1069  -0.0068 -0.0575 296 VAL   A CB  
1823 C  CG1 . VAL   A 276 ? 2.3618 1.7889 1.5588 0.0716  -0.0573 -0.0734 296 VAL   A CG1 
1824 C  CG2 . VAL   A 276 ? 2.5249 1.8212 1.5362 0.1363  -0.0148 -0.0742 296 VAL   A CG2 
1825 N  N   . ALA   A 277 ? 2.0302 1.5525 1.3528 0.0833  0.0710  -0.0083 297 ALA   A N   
1826 C  CA  . ALA   A 277 ? 2.0040 1.6006 1.4248 0.0613  0.0738  0.0027  297 ALA   A CA  
1827 C  C   . ALA   A 277 ? 1.9083 1.5312 1.3904 0.0481  0.1018  0.0095  297 ALA   A C   
1828 O  O   . ALA   A 277 ? 1.7889 1.4642 1.3439 0.0238  0.0904  0.0089  297 ALA   A O   
1829 C  CB  . ALA   A 277 ? 2.1148 1.7262 1.5406 0.0758  0.0935  0.0215  297 ALA   A CB  
1830 N  N   . GLN   A 278 ? 1.9556 1.5435 1.4083 0.0660  0.1393  0.0167  298 GLN   A N   
1831 C  CA  . GLN   A 278 ? 1.8603 1.4711 1.3694 0.0565  0.1627  0.0223  298 GLN   A CA  
1832 C  C   . GLN   A 278 ? 1.7846 1.3828 1.2954 0.0399  0.1375  0.0056  298 GLN   A C   
1833 O  O   . GLN   A 278 ? 1.8742 1.5081 1.4479 0.0221  0.1401  0.0089  298 GLN   A O   
1834 C  CB  . GLN   A 278 ? 1.8004 1.3802 1.2827 0.0820  0.2098  0.0348  298 GLN   A CB  
1835 C  CG  . GLN   A 278 ? 1.8333 1.4115 1.3013 0.1002  0.2382  0.0534  298 GLN   A CG  
1836 C  CD  . GLN   A 278 ? 1.8134 1.4527 1.3614 0.0837  0.2381  0.0660  298 GLN   A CD  
1837 O  OE1 . GLN   A 278 ? 1.9051 1.5916 1.5267 0.0635  0.2323  0.0653  298 GLN   A OE1 
1838 N  NE2 . GLN   A 278 ? 1.7821 1.4161 1.3109 0.0940  0.2441  0.0776  298 GLN   A NE2 
1839 N  N   . SER   A 279 ? 1.7108 1.2553 1.1514 0.0454  0.1115  -0.0122 299 SER   A N   
1840 C  CA  . SER   A 279 ? 1.8499 1.3778 1.2941 0.0262  0.0832  -0.0284 299 SER   A CA  
1841 C  C   . SER   A 279 ? 1.8241 1.4123 1.3420 -0.0073 0.0528  -0.0291 299 SER   A C   
1842 O  O   . SER   A 279 ? 1.8483 1.4539 1.4119 -0.0282 0.0484  -0.0289 299 SER   A O   
1843 C  CB  . SER   A 279 ? 2.0193 1.4751 1.3725 0.0384  0.0558  -0.0498 299 SER   A CB  
1844 O  OG  . SER   A 279 ? 2.2163 1.6136 1.4947 0.0729  0.0876  -0.0492 299 SER   A OG  
1845 N  N   . ILE   A 280 ? 1.7205 1.3412 1.2501 -0.0109 0.0336  -0.0283 300 ILE   A N   
1846 C  CA  . ILE   A 280 ? 1.6034 1.2863 1.2044 -0.0393 0.0081  -0.0281 300 ILE   A CA  
1847 C  C   . ILE   A 280 ? 1.6565 1.3949 1.3318 -0.0500 0.0341  -0.0122 300 ILE   A C   
1848 O  O   . ILE   A 280 ? 1.6818 1.4559 1.4103 -0.0742 0.0233  -0.0112 300 ILE   A O   
1849 C  CB  . ILE   A 280 ? 1.6537 1.3605 1.2514 -0.0343 -0.0141 -0.0295 300 ILE   A CB  
1850 C  CG1 . ILE   A 280 ? 1.8157 1.4626 1.3312 -0.0201 -0.0430 -0.0461 300 ILE   A CG1 
1851 C  CG2 . ILE   A 280 ? 1.6606 1.4346 1.3342 -0.0612 -0.0388 -0.0297 300 ILE   A CG2 
1852 C  CD1 . ILE   A 280 ? 1.9828 1.6424 1.4804 -0.0069 -0.0621 -0.0456 300 ILE   A CD1 
1853 N  N   . ILE   A 281 ? 1.6335 1.3790 1.3133 -0.0322 0.0683  0.0011  301 ILE   A N   
1854 C  CA  . ILE   A 281 ? 1.6078 1.4020 1.3544 -0.0401 0.0897  0.0140  301 ILE   A CA  
1855 C  C   . ILE   A 281 ? 1.5913 1.3731 1.3508 -0.0488 0.0974  0.0141  301 ILE   A C   
1856 O  O   . ILE   A 281 ? 1.7144 1.5352 1.5257 -0.0669 0.0933  0.0186  301 ILE   A O   
1857 C  CB  . ILE   A 281 ? 1.6057 1.4033 1.3551 -0.0201 0.1225  0.0272  301 ILE   A CB  
1858 C  CG1 . ILE   A 281 ? 1.7264 1.5404 1.4722 -0.0137 0.1136  0.0296  301 ILE   A CG1 
1859 C  CG2 . ILE   A 281 ? 1.5912 1.4303 1.4053 -0.0267 0.1417  0.0377  301 ILE   A CG2 
1860 C  CD1 . ILE   A 281 ? 1.7726 1.6464 1.5770 -0.0310 0.0940  0.0287  301 ILE   A CD1 
1861 N  N   . PHE   A 282 ? 1.6206 1.3452 1.3290 -0.0335 0.1096  0.0098  302 PHE   A N   
1862 C  CA  . PHE   A 282 ? 1.7389 1.4449 1.4555 -0.0372 0.1180  0.0103  302 PHE   A CA  
1863 C  C   . PHE   A 282 ? 1.7471 1.4463 1.4702 -0.0626 0.0866  0.0011  302 PHE   A C   
1864 O  O   . PHE   A 282 ? 1.7673 1.4829 1.5287 -0.0767 0.0882  0.0076  302 PHE   A O   
1865 C  CB  . PHE   A 282 ? 1.8562 1.4997 1.5125 -0.0107 0.1393  0.0064  302 PHE   A CB  
1866 C  CG  . PHE   A 282 ? 1.8617 1.5185 1.5336 0.0111  0.1790  0.0209  302 PHE   A CG  
1867 C  CD1 . PHE   A 282 ? 1.8583 1.5502 1.5518 0.0151  0.1898  0.0310  302 PHE   A CD1 
1868 C  CD2 . PHE   A 282 ? 1.9358 1.5691 1.6040 0.0277  0.2051  0.0247  302 PHE   A CD2 
1869 C  CE1 . PHE   A 282 ? 1.7392 1.4434 1.4548 0.0317  0.2258  0.0454  302 PHE   A CE1 
1870 C  CE2 . PHE   A 282 ? 1.8210 1.4721 1.5138 0.0462  0.2417  0.0390  302 PHE   A CE2 
1871 C  CZ  . PHE   A 282 ? 1.7511 1.4378 1.4694 0.0465  0.2520  0.0497  302 PHE   A CZ  
1872 N  N   . ILE   A 283 ? 1.7409 1.4151 1.4280 -0.0690 0.0569  -0.0130 303 ILE   A N   
1873 C  CA  . ILE   A 283 ? 1.6669 1.3315 1.3645 -0.0959 0.0254  -0.0218 303 ILE   A CA  
1874 C  C   . ILE   A 283 ? 1.6402 1.3759 1.4136 -0.1221 0.0184  -0.0106 303 ILE   A C   
1875 O  O   . ILE   A 283 ? 1.8066 1.5466 1.6098 -0.1436 0.0121  -0.0064 303 ILE   A O   
1876 C  CB  . ILE   A 283 ? 1.6817 1.3077 1.3285 -0.0965 -0.0092 -0.0409 303 ILE   A CB  
1877 C  CG1 . ILE   A 283 ? 1.8422 1.3850 1.4046 -0.0711 -0.0036 -0.0541 303 ILE   A CG1 
1878 C  CG2 . ILE   A 283 ? 1.6988 1.3341 1.3791 -0.1305 -0.0456 -0.0480 303 ILE   A CG2 
1879 C  CD1 . ILE   A 283 ? 1.8861 1.3856 1.3828 -0.0626 -0.0354 -0.0736 303 ILE   A CD1 
1880 N  N   . PHE   A 284 ? 1.5108 1.3006 1.3138 -0.1192 0.0212  -0.0048 304 PHE   A N   
1881 C  CA  . PHE   A 284 ? 1.5604 1.4185 1.4310 -0.1385 0.0195  0.0058  304 PHE   A CA  
1882 C  C   . PHE   A 284 ? 1.6239 1.5008 1.5244 -0.1365 0.0464  0.0199  304 PHE   A C   
1883 O  O   . PHE   A 284 ? 1.7593 1.6615 1.6967 -0.1552 0.0449  0.0282  304 PHE   A O   
1884 C  CB  . PHE   A 284 ? 1.4761 1.3815 1.3659 -0.1313 0.0158  0.0067  304 PHE   A CB  
1885 C  CG  . PHE   A 284 ? 1.5365 1.5114 1.4900 -0.1431 0.0211  0.0173  304 PHE   A CG  
1886 C  CD1 . PHE   A 284 ? 1.5551 1.5686 1.5482 -0.1658 0.0017  0.0175  304 PHE   A CD1 
1887 C  CD2 . PHE   A 284 ? 1.4939 1.4952 1.4679 -0.1307 0.0455  0.0267  304 PHE   A CD2 
1888 C  CE1 . PHE   A 284 ? 1.4953 1.5718 1.5412 -0.1730 0.0103  0.0277  304 PHE   A CE1 
1889 C  CE2 . PHE   A 284 ? 1.5457 1.6052 1.5687 -0.1381 0.0494  0.0342  304 PHE   A CE2 
1890 C  CZ  . PHE   A 284 ? 1.5200 1.6168 1.5758 -0.1578 0.0337  0.0350  304 PHE   A CZ  
1891 N  N   . ALA   A 285 ? 1.6241 1.4898 1.5104 -0.1134 0.0710  0.0238  305 ALA   A N   
1892 C  CA  . ALA   A 285 ? 1.6746 1.5626 1.5932 -0.1091 0.0927  0.0359  305 ALA   A CA  
1893 C  C   . ALA   A 285 ? 1.6945 1.5538 1.6103 -0.1180 0.0930  0.0395  305 ALA   A C   
1894 O  O   . ALA   A 285 ? 1.6753 1.5641 1.6258 -0.1287 0.0955  0.0499  305 ALA   A O   
1895 C  CB  . ALA   A 285 ? 1.4587 1.3353 1.3659 -0.0839 0.1173  0.0388  305 ALA   A CB  
1896 N  N   . GLY   A 286 ? 1.9255 1.7230 1.7955 -0.1118 0.0902  0.0310  306 GLY   A N   
1897 C  CA  . GLY   A 286 ? 2.0065 1.7676 1.8699 -0.1183 0.0897  0.0338  306 GLY   A CA  
1898 C  C   . GLY   A 286 ? 2.0269 1.7938 1.9097 -0.1491 0.0675  0.0358  306 GLY   A C   
1899 O  O   . GLY   A 286 ? 2.0282 1.7809 1.9210 -0.1581 0.0697  0.0450  306 GLY   A O   
1900 N  N   . TYR   A 287 ? 1.8001 1.5884 1.6914 -0.1652 0.0465  0.0289  307 TYR   A N   
1901 C  CA  . TYR   A 287 ? 1.7455 1.5472 1.6669 -0.1971 0.0268  0.0327  307 TYR   A CA  
1902 C  C   . TYR   A 287 ? 1.7432 1.6155 1.7202 -0.2083 0.0374  0.0500  307 TYR   A C   
1903 O  O   . TYR   A 287 ? 1.7606 1.6351 1.7560 -0.2200 0.0448  0.0644  307 TYR   A O   
1904 C  CB  . TYR   A 287 ? 1.8260 1.6249 1.7403 -0.2096 -0.0029 0.0176  307 TYR   A CB  
1905 C  CG  . TYR   A 287 ? 1.9159 1.7474 1.8797 -0.2445 -0.0218 0.0238  307 TYR   A CG  
1906 C  CD1 . TYR   A 287 ? 2.0193 1.8070 1.9825 -0.2677 -0.0359 0.0239  307 TYR   A CD1 
1907 C  CD2 . TYR   A 287 ? 1.8902 1.7963 1.9045 -0.2539 -0.0239 0.0304  307 TYR   A CD2 
1908 C  CE1 . TYR   A 287 ? 1.9858 1.8057 2.0019 -0.3020 -0.0505 0.0325  307 TYR   A CE1 
1909 C  CE2 . TYR   A 287 ? 1.8378 1.7797 1.9042 -0.2852 -0.0369 0.0383  307 TYR   A CE2 
1910 C  CZ  . TYR   A 287 ? 1.9727 1.8727 2.0421 -0.3106 -0.0495 0.0404  307 TYR   A CZ  
1911 O  OH  . TYR   A 287 ? 2.1938 2.1314 2.3222 -0.3443 -0.0601 0.0510  307 TYR   A OH  
1912 N  N   . GLU   A 288 ? 1.6511 1.5780 1.6505 -0.2027 0.0384  0.0490  308 GLU   A N   
1913 C  CA  . GLU   A 288 ? 1.6374 1.6313 1.6859 -0.2133 0.0450  0.0622  308 GLU   A CA  
1914 C  C   . GLU   A 288 ? 1.5849 1.5918 1.6402 -0.2007 0.0679  0.0752  308 GLU   A C   
1915 O  O   . GLU   A 288 ? 1.5695 1.5997 1.6480 -0.2128 0.0744  0.0899  308 GLU   A O   
1916 C  CB  . GLU   A 288 ? 1.6425 1.6849 1.7083 -0.2058 0.0394  0.0555  308 GLU   A CB  
1917 C  CG  . GLU   A 288 ? 1.6090 1.7143 1.7251 -0.2242 0.0342  0.0631  308 GLU   A CG  
1918 C  CD  . GLU   A 288 ? 1.7223 1.8656 1.8635 -0.2240 0.0554  0.0797  308 GLU   A CD  
1919 O  OE1 . GLU   A 288 ? 1.7136 1.8579 1.8424 -0.2032 0.0703  0.0807  308 GLU   A OE1 
1920 O  OE2 . GLU   A 288 ? 1.5508 1.7221 1.7237 -0.2447 0.0569  0.0922  308 GLU   A OE2 
1921 N  N   . THR   A 289 ? 1.6085 1.6009 1.6444 -0.1760 0.0800  0.0709  309 THR   A N   
1922 C  CA  . THR   A 289 ? 1.5590 1.5674 1.6060 -0.1628 0.0968  0.0810  309 THR   A CA  
1923 C  C   . THR   A 289 ? 1.6433 1.6180 1.6813 -0.1684 0.1006  0.0921  309 THR   A C   
1924 O  O   . THR   A 289 ? 1.4929 1.4908 1.5465 -0.1704 0.1072  0.1056  309 THR   A O   
1925 C  CB  . THR   A 289 ? 1.4861 1.4842 1.5219 -0.1378 0.1078  0.0744  309 THR   A CB  
1926 O  OG1 . THR   A 289 ? 1.5733 1.5135 1.5752 -0.1293 0.1108  0.0695  309 THR   A OG1 
1927 C  CG2 . THR   A 289 ? 1.4635 1.4853 1.5029 -0.1322 0.1038  0.0652  309 THR   A CG2 
1928 N  N   . THR   A 290 ? 1.7756 1.6910 1.7835 -0.1689 0.0960  0.0865  310 THR   A N   
1929 C  CA  . THR   A 290 ? 1.6991 1.5738 1.6953 -0.1719 0.0987  0.0966  310 THR   A CA  
1930 C  C   . THR   A 290 ? 1.5931 1.4788 1.6079 -0.2002 0.0919  0.1103  310 THR   A C   
1931 O  O   . THR   A 290 ? 1.6112 1.4982 1.6317 -0.2017 0.0999  0.1273  310 THR   A O   
1932 C  CB  . THR   A 290 ? 1.6853 1.4895 1.6415 -0.1647 0.0942  0.0849  310 THR   A CB  
1933 O  OG1 . THR   A 290 ? 1.7906 1.5890 1.7311 -0.1378 0.1056  0.0749  310 THR   A OG1 
1934 C  CG2 . THR   A 290 ? 1.6838 1.4416 1.6268 -0.1629 0.0979  0.0951  310 THR   A CG2 
1935 N  N   . SER   A 291 ? 1.6810 1.5759 1.7072 -0.2225 0.0772  0.1045  311 SER   A N   
1936 C  CA  . SER   A 291 ? 1.5408 1.4495 1.5938 -0.2524 0.0726  0.1193  311 SER   A CA  
1937 C  C   . SER   A 291 ? 1.3998 1.3762 1.4848 -0.2531 0.0872  0.1356  311 SER   A C   
1938 O  O   . SER   A 291 ? 1.4218 1.4035 1.5187 -0.2671 0.0955  0.1560  311 SER   A O   
1939 C  CB  . SER   A 291 ? 1.5841 1.4933 1.6506 -0.2756 0.0507  0.1076  311 SER   A CB  
1940 O  OG  . SER   A 291 ? 1.5425 1.5017 1.6234 -0.2673 0.0469  0.0966  311 SER   A OG  
1941 N  N   . SER   A 292 ? 1.3424 1.3669 1.4377 -0.2369 0.0913  0.1273  312 SER   A N   
1942 C  CA  . SER   A 292 ? 1.3880 1.4747 1.5085 -0.2345 0.1037  0.1391  312 SER   A CA  
1943 C  C   . SER   A 292 ? 1.3280 1.4088 1.4330 -0.2185 0.1176  0.1524  312 SER   A C   
1944 O  O   . SER   A 292 ? 1.3363 1.4409 1.4493 -0.2248 0.1283  0.1707  312 SER   A O   
1945 C  CB  . SER   A 292 ? 1.4467 1.5775 1.5786 -0.2192 0.1019  0.1245  312 SER   A CB  
1946 O  OG  . SER   A 292 ? 1.4829 1.6712 1.6361 -0.2152 0.1129  0.1331  312 SER   A OG  
1947 N  N   . VAL   A 293 ? 1.4493 1.4996 1.5322 -0.1964 0.1180  0.1442  313 VAL   A N   
1948 C  CA  . VAL   A 293 ? 1.4403 1.4864 1.5115 -0.1789 0.1263  0.1550  313 VAL   A CA  
1949 C  C   . VAL   A 293 ? 1.3282 1.3323 1.3843 -0.1901 0.1287  0.1737  313 VAL   A C   
1950 O  O   . VAL   A 293 ? 1.2692 1.2813 1.3182 -0.1848 0.1362  0.1909  313 VAL   A O   
1951 C  CB  . VAL   A 293 ? 1.3854 1.4145 1.4479 -0.1535 0.1256  0.1420  313 VAL   A CB  
1952 C  CG1 . VAL   A 293 ? 1.4255 1.4538 1.4816 -0.1349 0.1292  0.1519  313 VAL   A CG1 
1953 C  CG2 . VAL   A 293 ? 1.2399 1.3067 1.3181 -0.1446 0.1242  0.1264  313 VAL   A CG2 
1954 N  N   . LEU   A 294 ? 1.4096 1.3640 1.4566 -0.2047 0.1213  0.1706  314 LEU   A N   
1955 C  CA  . LEU   A 294 ? 1.5345 1.4424 1.5685 -0.2182 0.1223  0.1886  314 LEU   A CA  
1956 C  C   . LEU   A 294 ? 1.4742 1.4135 1.5283 -0.2429 0.1297  0.2100  314 LEU   A C   
1957 O  O   . LEU   A 294 ? 1.4598 1.3798 1.5028 -0.2468 0.1381  0.2330  314 LEU   A O   
1958 C  CB  . LEU   A 294 ? 1.5107 1.3560 1.5302 -0.2297 0.1099  0.1771  314 LEU   A CB  
1959 C  CG  . LEU   A 294 ? 1.6011 1.3974 1.5915 -0.2030 0.1085  0.1633  314 LEU   A CG  
1960 C  CD1 . LEU   A 294 ? 1.5954 1.3303 1.5649 -0.2132 0.0953  0.1483  314 LEU   A CD1 
1961 C  CD2 . LEU   A 294 ? 1.5380 1.3070 1.5130 -0.1860 0.1159  0.1796  314 LEU   A CD2 
1962 N  N   . SER   A 295 ? 1.3518 1.3403 1.4363 -0.2584 0.1282  0.2044  315 SER   A N   
1963 C  CA  . SER   A 295 ? 1.2815 1.3120 1.3923 -0.2791 0.1401  0.2257  315 SER   A CA  
1964 C  C   . SER   A 295 ? 1.3330 1.4005 1.4318 -0.2582 0.1572  0.2398  315 SER   A C   
1965 O  O   . SER   A 295 ? 1.4100 1.4821 1.5061 -0.2669 0.1721  0.2660  315 SER   A O   
1966 C  CB  . SER   A 295 ? 1.3086 1.3900 1.4589 -0.2951 0.1339  0.2145  315 SER   A CB  
1967 O  OG  . SER   A 295 ? 1.4906 1.5354 1.6465 -0.3122 0.1132  0.1989  315 SER   A OG  
1968 N  N   . PHE   A 296 ? 1.2851 1.3763 1.3743 -0.2301 0.1549  0.2230  316 PHE   A N   
1969 C  CA  . PHE   A 296 ? 1.1795 1.3002 1.2521 -0.2074 0.1655  0.2316  316 PHE   A CA  
1970 C  C   . PHE   A 296 ? 1.2353 1.3106 1.2737 -0.1954 0.1673  0.2480  316 PHE   A C   
1971 O  O   . PHE   A 296 ? 1.1073 1.1952 1.1265 -0.1871 0.1786  0.2672  316 PHE   A O   
1972 C  CB  . PHE   A 296 ? 1.2879 1.4362 1.3619 -0.1824 0.1578  0.2075  316 PHE   A CB  
1973 C  CG  . PHE   A 296 ? 1.1632 1.3655 1.2646 -0.1864 0.1592  0.1958  316 PHE   A CG  
1974 C  CD1 . PHE   A 296 ? 1.2292 1.4760 1.3440 -0.1951 0.1734  0.2099  316 PHE   A CD1 
1975 C  CD2 . PHE   A 296 ? 1.2223 1.4305 1.3358 -0.1796 0.1478  0.1724  316 PHE   A CD2 
1976 C  CE1 . PHE   A 296 ? 1.1868 1.4848 1.3294 -0.1955 0.1746  0.1989  316 PHE   A CE1 
1977 C  CE2 . PHE   A 296 ? 1.2398 1.4945 1.3771 -0.1808 0.1475  0.1622  316 PHE   A CE2 
1978 C  CZ  . PHE   A 296 ? 1.2328 1.5334 1.3861 -0.1881 0.1600  0.1746  316 PHE   A CZ  
1979 N  N   . ILE   A 297 ? 1.2889 1.3101 1.3159 -0.1915 0.1566  0.2410  317 ILE   A N   
1980 C  CA  . ILE   A 297 ? 1.4070 1.3847 1.4035 -0.1754 0.1559  0.2548  317 ILE   A CA  
1981 C  C   . ILE   A 297 ? 1.4348 1.3830 1.4189 -0.1952 0.1663  0.2851  317 ILE   A C   
1982 O  O   . ILE   A 297 ? 1.4529 1.3940 1.4098 -0.1826 0.1733  0.3061  317 ILE   A O   
1983 C  CB  . ILE   A 297 ? 1.4713 1.4004 1.4621 -0.1637 0.1443  0.2391  317 ILE   A CB  
1984 C  CG1 . ILE   A 297 ? 1.4409 1.4002 1.4433 -0.1402 0.1381  0.2156  317 ILE   A CG1 
1985 C  CG2 . ILE   A 297 ? 1.5102 1.3873 1.4729 -0.1502 0.1430  0.2558  317 ILE   A CG2 
1986 C  CD1 . ILE   A 297 ? 1.5179 1.4368 1.5174 -0.1250 0.1320  0.2022  317 ILE   A CD1 
1987 N  N   . MET   A 298 ? 1.4156 1.3442 1.4190 -0.2267 0.1663  0.2883  318 MET   A N   
1988 C  CA  . MET   A 298 ? 1.5635 1.4593 1.5618 -0.2498 0.1762  0.3185  318 MET   A CA  
1989 C  C   . MET   A 298 ? 1.4405 1.3884 1.4456 -0.2576 0.1974  0.3427  318 MET   A C   
1990 O  O   . MET   A 298 ? 1.4116 1.3363 1.3987 -0.2646 0.2113  0.3741  318 MET   A O   
1991 C  CB  . MET   A 298 ? 1.4938 1.3559 1.5169 -0.2837 0.1670  0.3132  318 MET   A CB  
1992 C  CG  . MET   A 298 ? 1.6754 1.4799 1.6832 -0.2738 0.1481  0.2889  318 MET   A CG  
1993 S  SD  . MET   A 298 ? 1.9303 1.6778 1.8927 -0.2382 0.1469  0.2958  318 MET   A SD  
1994 C  CE  . MET   A 298 ? 1.8667 1.5602 1.8140 -0.2598 0.1561  0.3346  318 MET   A CE  
1995 N  N   . TYR   A 299 ? 1.3234 1.3393 1.3518 -0.2547 0.2020  0.3298  319 TYR   A N   
1996 C  CA  . TYR   A 299 ? 1.3318 1.4000 1.3609 -0.2541 0.2248  0.3507  319 TYR   A CA  
1997 C  C   . TYR   A 299 ? 1.3360 1.3975 1.3134 -0.2205 0.2303  0.3620  319 TYR   A C   
1998 O  O   . TYR   A 299 ? 1.5721 1.6326 1.5261 -0.2208 0.2501  0.3929  319 TYR   A O   
1999 C  CB  . TYR   A 299 ? 1.3854 1.5245 1.4478 -0.2524 0.2264  0.3308  319 TYR   A CB  
2000 C  CG  . TYR   A 299 ? 1.4794 1.6738 1.5330 -0.2400 0.2500  0.3463  319 TYR   A CG  
2001 C  CD1 . TYR   A 299 ? 1.5524 1.7762 1.6311 -0.2636 0.2750  0.3741  319 TYR   A CD1 
2002 C  CD2 . TYR   A 299 ? 1.3212 1.5374 1.3416 -0.2040 0.2477  0.3331  319 TYR   A CD2 
2003 C  CE1 . TYR   A 299 ? 1.4929 1.7667 1.5587 -0.2486 0.3007  0.3890  319 TYR   A CE1 
2004 C  CE2 . TYR   A 299 ? 1.4260 1.6872 1.4295 -0.1889 0.2688  0.3449  319 TYR   A CE2 
2005 C  CZ  . TYR   A 299 ? 1.6345 1.9245 1.6581 -0.2097 0.2971  0.3732  319 TYR   A CZ  
2006 O  OH  . TYR   A 299 ? 1.8182 2.1531 1.8208 -0.1913 0.3221  0.3856  319 TYR   A OH  
2007 N  N   . GLU   A 300 ? 1.4248 1.4817 1.3845 -0.1908 0.2123  0.3379  320 GLU   A N   
2008 C  CA  . GLU   A 300 ? 1.5033 1.5563 1.4171 -0.1573 0.2106  0.3442  320 GLU   A CA  
2009 C  C   . GLU   A 300 ? 1.5942 1.5845 1.4723 -0.1541 0.2108  0.3703  320 GLU   A C   
2010 O  O   . GLU   A 300 ? 1.6342 1.6196 1.4691 -0.1355 0.2182  0.3911  320 GLU   A O   
2011 C  CB  . GLU   A 300 ? 1.3989 1.4624 1.3144 -0.1303 0.1887  0.3118  320 GLU   A CB  
2012 C  CG  . GLU   A 300 ? 1.3801 1.5039 1.3176 -0.1249 0.1886  0.2889  320 GLU   A CG  
2013 C  CD  . GLU   A 300 ? 1.5663 1.7277 1.4750 -0.1083 0.2014  0.2989  320 GLU   A CD  
2014 O  OE1 . GLU   A 300 ? 1.5962 1.7359 1.4609 -0.0945 0.2061  0.3204  320 GLU   A OE1 
2015 O  OE2 . GLU   A 300 ? 1.5637 1.7739 1.4897 -0.1067 0.2068  0.2851  320 GLU   A OE2 
2016 N  N   . LEU   A 301 ? 1.5609 1.4987 1.4514 -0.1696 0.2020  0.3694  321 LEU   A N   
2017 C  CA  . LEU   A 301 ? 1.5809 1.4531 1.4385 -0.1669 0.2022  0.3950  321 LEU   A CA  
2018 C  C   . LEU   A 301 ? 1.7937 1.6577 1.6419 -0.1906 0.2267  0.4336  321 LEU   A C   
2019 O  O   . LEU   A 301 ? 2.0230 1.8491 1.8284 -0.1791 0.2331  0.4623  321 LEU   A O   
2020 C  CB  . LEU   A 301 ? 1.6223 1.4370 1.4943 -0.1770 0.1876  0.3825  321 LEU   A CB  
2021 C  CG  . LEU   A 301 ? 1.6513 1.4653 1.5315 -0.1525 0.1678  0.3492  321 LEU   A CG  
2022 C  CD1 . LEU   A 301 ? 1.6529 1.4005 1.5352 -0.1586 0.1580  0.3420  321 LEU   A CD1 
2023 C  CD2 . LEU   A 301 ? 1.6446 1.4677 1.4976 -0.1137 0.1587  0.3490  321 LEU   A CD2 
2024 N  N   . ALA   A 302 ? 1.8063 1.7063 1.6957 -0.2231 0.2409  0.4364  322 ALA   A N   
2025 C  CA  . ALA   A 302 ? 1.7885 1.6874 1.6808 -0.2492 0.2677  0.4751  322 ALA   A CA  
2026 C  C   . ALA   A 302 ? 1.8107 1.7526 1.6674 -0.2276 0.2904  0.4954  322 ALA   A C   
2027 O  O   . ALA   A 302 ? 1.9219 1.8377 1.7440 -0.2282 0.3103  0.5334  322 ALA   A O   
2028 C  CB  . ALA   A 302 ? 1.8119 1.7431 1.7688 -0.2902 0.2739  0.4708  322 ALA   A CB  
2029 N  N   . THR   A 303 ? 1.7819 1.7858 1.6420 -0.2070 0.2881  0.4708  323 THR   A N   
2030 C  CA  . THR   A 303 ? 1.8062 1.8491 1.6257 -0.1817 0.3073  0.4844  323 THR   A CA  
2031 C  C   . THR   A 303 ? 1.8883 1.8970 1.6393 -0.1409 0.2927  0.4861  323 THR   A C   
2032 O  O   . THR   A 303 ? 1.7589 1.7847 1.4605 -0.1172 0.3071  0.5014  323 THR   A O   
2033 C  CB  . THR   A 303 ? 1.7064 1.8223 1.5527 -0.1725 0.3073  0.4548  323 THR   A CB  
2034 O  OG1 . THR   A 303 ? 1.6472 1.7604 1.4963 -0.1521 0.2752  0.4158  323 THR   A OG1 
2035 C  CG2 . THR   A 303 ? 1.6102 1.7644 1.5267 -0.2105 0.3193  0.4535  323 THR   A CG2 
2036 N  N   . HIS   A 304 ? 1.9157 1.8776 1.6622 -0.1305 0.2641  0.4704  324 HIS   A N   
2037 C  CA  . HIS   A 304 ? 1.8487 1.7754 1.5388 -0.0930 0.2459  0.4729  324 HIS   A CA  
2038 C  C   . HIS   A 304 ? 1.8564 1.7089 1.5408 -0.1011 0.2372  0.4892  324 HIS   A C   
2039 O  O   . HIS   A 304 ? 1.8838 1.7123 1.5879 -0.0947 0.2131  0.4656  324 HIS   A O   
2040 C  CB  . HIS   A 304 ? 1.8070 1.7611 1.5050 -0.0649 0.2165  0.4320  324 HIS   A CB  
2041 C  CG  . HIS   A 304 ? 1.6950 1.7139 1.3943 -0.0541 0.2221  0.4140  324 HIS   A CG  
2042 N  ND1 . HIS   A 304 ? 1.6851 1.7505 1.4327 -0.0777 0.2356  0.4014  324 HIS   A ND1 
2043 C  CD2 . HIS   A 304 ? 1.7035 1.7452 1.3597 -0.0202 0.2138  0.4053  324 HIS   A CD2 
2044 C  CE1 . HIS   A 304 ? 1.6262 1.7396 1.3609 -0.0582 0.2376  0.3864  324 HIS   A CE1 
2045 N  NE2 . HIS   A 304 ? 1.7004 1.7990 1.3784 -0.0237 0.2242  0.3875  324 HIS   A NE2 
2046 N  N   . PRO   A 305 ? 1.9176 1.7303 1.5745 -0.1143 0.2582  0.5307  325 PRO   A N   
2047 C  CA  . PRO   A 305 ? 1.9568 1.6926 1.6120 -0.1263 0.2512  0.5466  325 PRO   A CA  
2048 C  C   . PRO   A 305 ? 2.0880 1.7789 1.7040 -0.0877 0.2240  0.5411  325 PRO   A C   
2049 O  O   . PRO   A 305 ? 2.0387 1.6759 1.6674 -0.0911 0.2096  0.5359  325 PRO   A O   
2050 C  CB  . PRO   A 305 ? 1.9675 1.6767 1.5989 -0.1474 0.2831  0.5961  325 PRO   A CB  
2051 C  CG  . PRO   A 305 ? 1.9718 1.7550 1.6155 -0.1569 0.3105  0.6013  325 PRO   A CG  
2052 C  CD  . PRO   A 305 ? 1.9868 1.8218 1.6167 -0.1210 0.2924  0.5658  325 PRO   A CD  
2053 N  N   . ASP   A 306 ? 2.1795 1.8902 1.7483 -0.0496 0.2152  0.5412  326 ASP   A N   
2054 C  CA  . ASP   A 306 ? 2.0719 1.7461 1.6094 -0.0113 0.1858  0.5358  326 ASP   A CA  
2055 C  C   . ASP   A 306 ? 1.9772 1.6622 1.5659 -0.0049 0.1597  0.4944  326 ASP   A C   
2056 O  O   . ASP   A 306 ? 1.9516 1.5909 1.5396 0.0115  0.1414  0.4920  326 ASP   A O   
2057 C  CB  . ASP   A 306 ? 2.1958 1.8964 1.6764 0.0274  0.1768  0.5386  326 ASP   A CB  
2058 C  CG  . ASP   A 306 ? 2.3056 2.0820 1.8067 0.0298  0.1766  0.5081  326 ASP   A CG  
2059 O  OD1 . ASP   A 306 ? 2.2027 2.0137 1.7502 -0.0022 0.1956  0.4991  326 ASP   A OD1 
2060 O  OD2 . ASP   A 306 ? 2.5096 2.3089 1.9804 0.0645  0.1552  0.4926  326 ASP   A OD2 
2061 N  N   . VAL   A 307 ? 2.0572 1.8017 1.6903 -0.0162 0.1596  0.4629  327 VAL   A N   
2062 C  CA  . VAL   A 307 ? 2.0032 1.7587 1.6857 -0.0127 0.1403  0.4264  327 VAL   A CA  
2063 C  C   . VAL   A 307 ? 1.8805 1.5880 1.5909 -0.0387 0.1456  0.4270  327 VAL   A C   
2064 O  O   . VAL   A 307 ? 1.7832 1.4667 1.5128 -0.0264 0.1302  0.4092  327 VAL   A O   
2065 C  CB  . VAL   A 307 ? 1.7862 1.6121 1.5045 -0.0193 0.1408  0.3961  327 VAL   A CB  
2066 C  CG1 . VAL   A 307 ? 1.6652 1.5019 1.4310 -0.0137 0.1233  0.3615  327 VAL   A CG1 
2067 C  CG2 . VAL   A 307 ? 1.8593 1.7256 1.5435 0.0069  0.1345  0.3943  327 VAL   A CG2 
2068 N  N   . GLN   A 308 ? 1.8940 1.5859 1.6078 -0.0741 0.1671  0.4472  328 GLN   A N   
2069 C  CA  . GLN   A 308 ? 1.8771 1.5200 1.6161 -0.1009 0.1684  0.4448  328 GLN   A CA  
2070 C  C   . GLN   A 308 ? 1.9154 1.4780 1.6240 -0.0862 0.1598  0.4626  328 GLN   A C   
2071 O  O   . GLN   A 308 ? 1.8906 1.4128 1.6147 -0.0844 0.1487  0.4457  328 GLN   A O   
2072 C  CB  . GLN   A 308 ? 1.8916 1.5407 1.6484 -0.1443 0.1903  0.4627  328 GLN   A CB  
2073 C  CG  . GLN   A 308 ? 1.9153 1.5138 1.6995 -0.1755 0.1872  0.4569  328 GLN   A CG  
2074 C  CD  . GLN   A 308 ? 1.8639 1.4871 1.6835 -0.2200 0.2036  0.4663  328 GLN   A CD  
2075 O  OE1 . GLN   A 308 ? 1.8810 1.4693 1.7269 -0.2493 0.1983  0.4595  328 GLN   A OE1 
2076 N  NE2 . GLN   A 308 ? 1.8127 1.4970 1.6343 -0.2240 0.2226  0.4808  328 GLN   A NE2 
2077 N  N   . GLN   A 309 ? 1.9986 1.5342 1.6599 -0.0728 0.1653  0.4970  329 GLN   A N   
2078 C  CA  . GLN   A 309 ? 2.0544 1.5105 1.6835 -0.0555 0.1562  0.5161  329 GLN   A CA  
2079 C  C   . GLN   A 309 ? 2.0310 1.4874 1.6620 -0.0128 0.1305  0.4923  329 GLN   A C   
2080 O  O   . GLN   A 309 ? 2.0235 1.4276 1.6618 -0.0038 0.1203  0.4843  329 GLN   A O   
2081 C  CB  . GLN   A 309 ? 2.0803 1.5082 1.6531 -0.0486 0.1685  0.5608  329 GLN   A CB  
2082 C  CG  . GLN   A 309 ? 2.1228 1.4661 1.6571 -0.0258 0.1572  0.5829  329 GLN   A CG  
2083 C  CD  . GLN   A 309 ? 2.1917 1.5017 1.6642 -0.0186 0.1709  0.6306  329 GLN   A CD  
2084 O  OE1 . GLN   A 309 ? 2.1217 1.4410 1.5884 -0.0493 0.1982  0.6569  329 GLN   A OE1 
2085 N  NE2 . GLN   A 309 ? 2.0384 1.3104 1.4647 0.0233  0.1526  0.6434  329 GLN   A NE2 
2086 N  N   . LYS   A 310 ? 2.0377 1.5531 1.6648 0.0143  0.1193  0.4801  330 LYS   A N   
2087 C  CA  . LYS   A 310 ? 1.8466 1.3735 1.4890 0.0523  0.0941  0.4566  330 LYS   A CA  
2088 C  C   . LYS   A 310 ? 1.8937 1.4311 1.5904 0.0439  0.0916  0.4223  330 LYS   A C   
2089 O  O   . LYS   A 310 ? 1.9343 1.4574 1.6479 0.0707  0.0771  0.4083  330 LYS   A O   
2090 C  CB  . LYS   A 310 ? 1.8155 1.4082 1.4515 0.0762  0.0807  0.4458  330 LYS   A CB  
2091 C  CG  . LYS   A 310 ? 1.9325 1.5392 1.5868 0.1163  0.0513  0.4266  330 LYS   A CG  
2092 C  CD  . LYS   A 310 ? 1.9716 1.6416 1.6226 0.1356  0.0344  0.4126  330 LYS   A CD  
2093 C  CE  . LYS   A 310 ? 1.9757 1.6642 1.6570 0.1722  0.0026  0.3930  330 LYS   A CE  
2094 N  NZ  . LYS   A 310 ? 1.9458 1.6934 1.6287 0.1889  -0.0189 0.3754  330 LYS   A NZ  
2095 N  N   . LEU   A 311 ? 1.8217 1.3844 1.5455 0.0091  0.1063  0.4092  331 LEU   A N   
2096 C  CA  . LEU   A 311 ? 1.7190 1.2822 1.4837 0.0007  0.1056  0.3793  331 LEU   A CA  
2097 C  C   . LEU   A 311 ? 1.9387 1.4208 1.6930 -0.0080 0.1081  0.3860  331 LEU   A C   
2098 O  O   . LEU   A 311 ? 1.9482 1.4070 1.7173 0.0090  0.1016  0.3669  331 LEU   A O   
2099 C  CB  . LEU   A 311 ? 1.7642 1.3784 1.5568 -0.0313 0.1169  0.3635  331 LEU   A CB  
2100 C  CG  . LEU   A 311 ? 1.7605 1.3845 1.5903 -0.0381 0.1160  0.3313  331 LEU   A CG  
2101 C  CD1 . LEU   A 311 ? 1.7169 1.3603 1.5669 -0.0027 0.1041  0.3117  331 LEU   A CD1 
2102 C  CD2 . LEU   A 311 ? 1.5831 1.2654 1.4373 -0.0636 0.1239  0.3179  331 LEU   A CD2 
2103 N  N   . GLN   A 312 ? 2.0748 1.5112 1.8034 -0.0337 0.1184  0.4136  332 GLN   A N   
2104 C  CA  . GLN   A 312 ? 1.9858 1.3360 1.7013 -0.0432 0.1181  0.4210  332 GLN   A CA  
2105 C  C   . GLN   A 312 ? 2.1418 1.4392 1.8320 -0.0027 0.1058  0.4298  332 GLN   A C   
2106 O  O   . GLN   A 312 ? 2.2240 1.4574 1.9107 0.0041  0.1014  0.4217  332 GLN   A O   
2107 C  CB  . GLN   A 312 ? 1.9359 1.2507 1.6347 -0.0812 0.1317  0.4526  332 GLN   A CB  
2108 C  CG  . GLN   A 312 ? 1.9394 1.2969 1.6714 -0.1242 0.1426  0.4434  332 GLN   A CG  
2109 C  CD  . GLN   A 312 ? 2.1112 1.4471 1.8359 -0.1612 0.1587  0.4791  332 GLN   A CD  
2110 O  OE1 . GLN   A 312 ? 2.1119 1.4362 1.8035 -0.1521 0.1678  0.5132  332 GLN   A OE1 
2111 N  NE2 . GLN   A 312 ? 2.0860 1.4161 1.8422 -0.2028 0.1621  0.4724  332 GLN   A NE2 
2112 N  N   . GLU   A 313 ? 2.1291 1.4510 1.7997 0.0267  0.0985  0.4455  333 GLU   A N   
2113 C  CA  . GLU   A 313 ? 2.0751 1.3532 1.7252 0.0687  0.0836  0.4543  333 GLU   A CA  
2114 C  C   . GLU   A 313 ? 2.1163 1.4164 1.8049 0.0981  0.0729  0.4208  333 GLU   A C   
2115 O  O   . GLU   A 313 ? 2.2640 1.5092 1.9482 0.1228  0.0666  0.4191  333 GLU   A O   
2116 C  CB  . GLU   A 313 ? 2.1632 1.4664 1.7813 0.0936  0.0746  0.4776  333 GLU   A CB  
2117 C  CG  . GLU   A 313 ? 2.1403 1.4111 1.7110 0.0719  0.0889  0.5175  333 GLU   A CG  
2118 C  CD  . GLU   A 313 ? 2.2996 1.6126 1.8357 0.0932  0.0833  0.5345  333 GLU   A CD  
2119 O  OE1 . GLU   A 313 ? 2.3125 1.6827 1.8663 0.1214  0.0649  0.5119  333 GLU   A OE1 
2120 O  OE2 . GLU   A 313 ? 2.5345 1.8219 2.0247 0.0820  0.0973  0.5706  333 GLU   A OE2 
2121 N  N   . GLU   A 314 ? 1.9896 1.3690 1.7174 0.0969  0.0724  0.3950  334 GLU   A N   
2122 C  CA  . GLU   A 314 ? 2.0474 1.4528 1.8174 0.1222  0.0669  0.3657  334 GLU   A CA  
2123 C  C   . GLU   A 314 ? 2.1389 1.5027 1.9183 0.1079  0.0787  0.3468  334 GLU   A C   
2124 O  O   . GLU   A 314 ? 2.0309 1.3782 1.8271 0.1354  0.0776  0.3316  334 GLU   A O   
2125 C  CB  . GLU   A 314 ? 2.0031 1.4999 1.8120 0.1219  0.0637  0.3456  334 GLU   A CB  
2126 C  CG  . GLU   A 314 ? 1.9525 1.4846 1.8112 0.1501  0.0585  0.3206  334 GLU   A CG  
2127 C  CD  . GLU   A 314 ? 1.9126 1.5186 1.8126 0.1358  0.0630  0.2970  334 GLU   A CD  
2128 O  OE1 . GLU   A 314 ? 1.9411 1.5522 1.8349 0.1022  0.0760  0.2912  334 GLU   A OE1 
2129 O  OE2 . GLU   A 314 ? 1.9298 1.5883 1.8710 0.1580  0.0524  0.2847  334 GLU   A OE2 
2130 N  N   . ILE   A 315 ? 2.1648 1.5120 1.9335 0.0669  0.0895  0.3471  335 ILE   A N   
2131 C  CA  . ILE   A 315 ? 2.2374 1.5404 2.0080 0.0527  0.0963  0.3272  335 ILE   A CA  
2132 C  C   . ILE   A 315 ? 2.3374 1.5449 2.0767 0.0683  0.0927  0.3364  335 ILE   A C   
2133 O  O   . ILE   A 315 ? 2.3478 1.5194 2.0886 0.0855  0.0945  0.3158  335 ILE   A O   
2134 C  CB  . ILE   A 315 ? 2.0898 1.3996 1.8600 0.0043  0.1036  0.3262  335 ILE   A CB  
2135 C  CG1 . ILE   A 315 ? 1.9053 1.3069 1.7082 -0.0059 0.1074  0.3114  335 ILE   A CG1 
2136 C  CG2 . ILE   A 315 ? 2.1585 1.4083 1.9207 -0.0108 0.1047  0.3071  335 ILE   A CG2 
2137 C  CD1 . ILE   A 315 ? 1.9678 1.3851 1.7775 -0.0497 0.1135  0.3084  335 ILE   A CD1 
2138 N  N   . ASP   A 316 ? 2.4848 1.6464 2.1920 0.0647  0.0888  0.3681  336 ASP   A N   
2139 C  CA  . ASP   A 316 ? 2.5360 1.6013 2.2110 0.0816  0.0838  0.3798  336 ASP   A CA  
2140 C  C   . ASP   A 316 ? 2.5574 1.6212 2.2363 0.1359  0.0748  0.3794  336 ASP   A C   
2141 O  O   . ASP   A 316 ? 2.6369 1.6235 2.2945 0.1585  0.0712  0.3816  336 ASP   A O   
2142 C  CB  . ASP   A 316 ? 2.6161 1.6303 2.2556 0.0577  0.0844  0.4177  336 ASP   A CB  
2143 C  CG  . ASP   A 316 ? 2.6565 1.6747 2.3017 0.0027  0.0938  0.4208  336 ASP   A CG  
2144 O  OD1 . ASP   A 316 ? 2.6597 1.6746 2.3219 -0.0165 0.0948  0.3929  336 ASP   A OD1 
2145 O  OD2 . ASP   A 316 ? 2.6109 1.6368 2.2437 -0.0201 0.1005  0.4517  336 ASP   A OD2 
2146 N  N   . ALA   A 317 ? 2.3910 1.5371 2.0988 0.1578  0.0695  0.3760  337 ALA   A N   
2147 C  CA  . ALA   A 317 ? 2.1993 1.3553 1.9235 0.2090  0.0585  0.3737  337 ALA   A CA  
2148 C  C   . ALA   A 317 ? 2.2030 1.3754 1.9650 0.2292  0.0668  0.3413  337 ALA   A C   
2149 O  O   . ALA   A 317 ? 2.3698 1.4971 2.1305 0.2648  0.0658  0.3375  337 ALA   A O   
2150 C  CB  . ALA   A 317 ? 2.0737 1.3097 1.8166 0.2235  0.0455  0.3817  337 ALA   A CB  
2151 N  N   . VAL   A 318 ? 2.1263 1.3620 1.9205 0.2090  0.0768  0.3188  338 VAL   A N   
2152 C  CA  . VAL   A 318 ? 2.1146 1.3646 1.9395 0.2262  0.0893  0.2904  338 VAL   A CA  
2153 C  C   . VAL   A 318 ? 2.2089 1.3728 1.9970 0.2165  0.0991  0.2790  338 VAL   A C   
2154 O  O   . VAL   A 318 ? 2.2753 1.4117 2.0672 0.2467  0.1080  0.2626  338 VAL   A O   
2155 C  CB  . VAL   A 318 ? 2.0479 1.3853 1.9129 0.2068  0.0969  0.2724  338 VAL   A CB  
2156 C  CG1 . VAL   A 318 ? 2.0529 1.4037 1.9462 0.2247  0.1137  0.2464  338 VAL   A CG1 
2157 C  CG2 . VAL   A 318 ? 1.9732 1.3891 1.8728 0.2175  0.0833  0.2809  338 VAL   A CG2 
2158 N  N   . LEU   A 319 ? 2.3143 1.4335 2.0669 0.1755  0.0972  0.2872  339 LEU   A N   
2159 C  CA  . LEU   A 319 ? 2.3415 1.3753 2.0581 0.1602  0.1007  0.2749  339 LEU   A CA  
2160 C  C   . LEU   A 319 ? 2.5835 1.5328 2.2593 0.1464  0.0906  0.3011  339 LEU   A C   
2161 O  O   . LEU   A 319 ? 2.6768 1.6138 2.3401 0.1022  0.0883  0.3132  339 LEU   A O   
2162 C  CB  . LEU   A 319 ? 2.3570 1.4167 2.0776 0.1185  0.1059  0.2570  339 LEU   A CB  
2163 C  CG  . LEU   A 319 ? 2.2026 1.3375 1.9580 0.1285  0.1175  0.2323  339 LEU   A CG  
2164 C  CD1 . LEU   A 319 ? 2.2416 1.3949 1.9948 0.0866  0.1189  0.2184  339 LEU   A CD1 
2165 C  CD2 . LEU   A 319 ? 2.2271 1.3303 1.9785 0.1696  0.1284  0.2118  339 LEU   A CD2 
2166 N  N   . PRO   A 320 ? 2.5810 1.4712 2.2382 0.1835  0.0852  0.3121  340 PRO   A N   
2167 C  CA  . PRO   A 320 ? 2.6311 1.4295 2.2462 0.1715  0.0763  0.3384  340 PRO   A CA  
2168 C  C   . PRO   A 320 ? 2.8644 1.5711 2.4481 0.1467  0.0754  0.3231  340 PRO   A C   
2169 O  O   . PRO   A 320 ? 2.9273 1.6244 2.5109 0.1548  0.0805  0.2904  340 PRO   A O   
2170 C  CB  . PRO   A 320 ? 2.4793 1.2451 2.0869 0.2262  0.0699  0.3499  340 PRO   A CB  
2171 C  CG  . PRO   A 320 ? 2.4873 1.2951 2.1271 0.2644  0.0786  0.3193  340 PRO   A CG  
2172 C  CD  . PRO   A 320 ? 2.5110 1.4180 2.1891 0.2390  0.0873  0.3029  340 PRO   A CD  
2173 N  N   . ASN   A 321 ? 3.1357 1.7722 2.6912 0.1157  0.0685  0.3478  341 ASN   A N   
2174 C  CA  . ASN   A 321 ? 3.2029 1.7455 2.7309 0.0849  0.0622  0.3365  341 ASN   A CA  
2175 C  C   . ASN   A 321 ? 3.1403 1.7253 2.6868 0.0464  0.0639  0.3090  341 ASN   A C   
2176 O  O   . ASN   A 321 ? 3.2347 1.7557 2.7607 0.0361  0.0569  0.2830  341 ASN   A O   
2177 C  CB  . ASN   A 321 ? 3.2729 1.7211 2.7682 0.1261  0.0577  0.3169  341 ASN   A CB  
2178 C  CG  . ASN   A 321 ? 3.2998 1.6939 2.7743 0.1646  0.0531  0.3447  341 ASN   A CG  
2179 O  OD1 . ASN   A 321 ? 3.3102 1.6931 2.7773 0.1476  0.0496  0.3821  341 ASN   A OD1 
2180 N  ND2 . ASN   A 321 ? 3.3188 1.6788 2.7825 0.2191  0.0543  0.3277  341 ASN   A ND2 
2181 N  N   . LYS   A 322 ? 2.8061 1.4959 2.3882 0.0269  0.0712  0.3138  342 LYS   A N   
2182 C  CA  . LYS   A 322 ? 2.7200 1.4627 2.3237 -0.0054 0.0727  0.2894  342 LYS   A CA  
2183 C  C   . LYS   A 322 ? 2.7159 1.4518 2.3114 0.0239  0.0752  0.2496  342 LYS   A C   
2184 O  O   . LYS   A 322 ? 2.7824 1.4704 2.3588 0.0067  0.0676  0.2248  342 LYS   A O   
2185 C  CB  . LYS   A 322 ? 2.6892 1.3838 2.2881 -0.0609 0.0629  0.2948  342 LYS   A CB  
2186 C  CG  . LYS   A 322 ? 2.7579 1.4686 2.3693 -0.0942 0.0666  0.3364  342 LYS   A CG  
2187 C  CD  . LYS   A 322 ? 2.8781 1.5549 2.4999 -0.1522 0.0583  0.3398  342 LYS   A CD  
2188 C  CE  . LYS   A 322 ? 2.8198 1.5179 2.4575 -0.1859 0.0681  0.3841  342 LYS   A CE  
2189 N  NZ  . LYS   A 322 ? 2.7968 1.4780 2.4599 -0.2453 0.0618  0.3880  342 LYS   A NZ  
2190 N  N   . ALA   A 323 ? 2.5357 1.3207 2.1459 0.0694  0.0858  0.2444  343 ALA   A N   
2191 C  CA  . ALA   A 323 ? 2.5308 1.3116 2.1342 0.1035  0.0943  0.2117  343 ALA   A CA  
2192 C  C   . ALA   A 323 ? 2.4825 1.3307 2.1045 0.0819  0.0999  0.1895  343 ALA   A C   
2193 O  O   . ALA   A 323 ? 2.3238 1.2499 1.9781 0.0547  0.1006  0.2005  343 ALA   A O   
2194 C  CB  . ALA   A 323 ? 2.5194 1.3405 2.1449 0.1567  0.1054  0.2159  343 ALA   A CB  
2195 N  N   . PRO   A 324 ? 2.4800 1.2963 2.0775 0.0957  0.1040  0.1584  344 PRO   A N   
2196 C  CA  . PRO   A 324 ? 2.4017 1.2771 2.0109 0.0800  0.1094  0.1380  344 PRO   A CA  
2197 C  C   . PRO   A 324 ? 2.3238 1.3007 1.9784 0.1033  0.1276  0.1412  344 PRO   A C   
2198 O  O   . PRO   A 324 ? 2.2877 1.2710 1.9510 0.1476  0.1416  0.1395  344 PRO   A O   
2199 C  CB  . PRO   A 324 ? 2.4403 1.2407 1.9994 0.0999  0.1103  0.1056  344 PRO   A CB  
2200 C  CG  . PRO   A 324 ? 2.4947 1.1865 2.0147 0.1096  0.0984  0.1086  344 PRO   A CG  
2201 C  CD  . PRO   A 324 ? 2.4797 1.1940 2.0289 0.1255  0.1025  0.1402  344 PRO   A CD  
2202 N  N   . PRO   A 325 ? 2.3077 1.3659 1.9958 0.0749  0.1275  0.1459  345 PRO   A N   
2203 C  CA  . PRO   A 325 ? 2.1219 1.2746 1.8561 0.0936  0.1419  0.1485  345 PRO   A CA  
2204 C  C   . PRO   A 325 ? 2.1445 1.3076 1.8747 0.1203  0.1600  0.1246  345 PRO   A C   
2205 O  O   . PRO   A 325 ? 2.2573 1.4070 1.9629 0.1046  0.1596  0.1060  345 PRO   A O   
2206 C  CB  . PRO   A 325 ? 2.0494 1.2691 1.8097 0.0529  0.1349  0.1568  345 PRO   A CB  
2207 C  CG  . PRO   A 325 ? 2.0876 1.2555 1.8167 0.0162  0.1216  0.1481  345 PRO   A CG  
2208 C  CD  . PRO   A 325 ? 2.2950 1.3628 1.9849 0.0243  0.1133  0.1501  345 PRO   A CD  
2209 N  N   . THR   A 326 ? 2.1356 1.3233 1.8908 0.1617  0.1762  0.1264  346 THR   A N   
2210 C  CA  . THR   A 326 ? 2.1781 1.3866 1.9387 0.1904  0.1999  0.1094  346 THR   A CA  
2211 C  C   . THR   A 326 ? 2.1543 1.4661 1.9758 0.1868  0.2095  0.1157  346 THR   A C   
2212 O  O   . THR   A 326 ? 2.1305 1.4934 1.9849 0.1657  0.1961  0.1306  346 THR   A O   
2213 C  CB  . THR   A 326 ? 2.1534 1.3229 1.9086 0.2399  0.2148  0.1072  346 THR   A CB  
2214 O  OG1 . THR   A 326 ? 2.1190 1.3267 1.9212 0.2559  0.2095  0.1282  346 THR   A OG1 
2215 C  CG2 . THR   A 326 ? 2.2277 1.2854 1.9160 0.2447  0.2049  0.0969  346 THR   A CG2 
2216 N  N   . TYR   A 327 ? 2.1210 1.4603 1.9549 0.2086  0.2337  0.1043  347 TYR   A N   
2217 C  CA  . TYR   A 327 ? 2.0925 1.5238 1.9855 0.2041  0.2435  0.1093  347 TYR   A CA  
2218 C  C   . TYR   A 327 ? 2.1664 1.6533 2.1221 0.2185  0.2380  0.1264  347 TYR   A C   
2219 O  O   . TYR   A 327 ? 2.0921 1.6416 2.0869 0.1986  0.2260  0.1350  347 TYR   A O   
2220 C  CB  . TYR   A 327 ? 2.1558 1.5987 2.0503 0.2283  0.2748  0.0975  347 TYR   A CB  
2221 C  CG  . TYR   A 327 ? 2.0453 1.5757 1.9997 0.2208  0.2862  0.1026  347 TYR   A CG  
2222 C  CD1 . TYR   A 327 ? 1.9819 1.5759 2.0101 0.2401  0.2947  0.1142  347 TYR   A CD1 
2223 C  CD2 . TYR   A 327 ? 1.9623 1.5095 1.9015 0.1948  0.2865  0.0955  347 TYR   A CD2 
2224 C  CE1 . TYR   A 327 ? 1.9029 1.5718 1.9886 0.2310  0.3029  0.1182  347 TYR   A CE1 
2225 C  CE2 . TYR   A 327 ? 1.8737 1.4938 1.8661 0.1879  0.2963  0.1005  347 TYR   A CE2 
2226 C  CZ  . TYR   A 327 ? 1.8356 1.5148 1.9014 0.2050  0.3046  0.1117  347 TYR   A CZ  
2227 O  OH  . TYR   A 327 ? 1.7648 1.5121 1.8866 0.1960  0.3124  0.1161  347 TYR   A OH  
2228 N  N   . ASP   A 328 ? 2.2672 1.7305 2.2316 0.2554  0.2447  0.1305  348 ASP   A N   
2229 C  CA  . ASP   A 328 ? 2.2184 1.7381 2.2472 0.2747  0.2383  0.1451  348 ASP   A CA  
2230 C  C   . ASP   A 328 ? 2.1792 1.6928 2.2006 0.2574  0.2074  0.1605  348 ASP   A C   
2231 O  O   . ASP   A 328 ? 2.1019 1.6754 2.1720 0.2597  0.1941  0.1714  348 ASP   A O   
2232 C  CB  . ASP   A 328 ? 2.2906 1.7894 2.3341 0.3229  0.2555  0.1448  348 ASP   A CB  
2233 C  CG  . ASP   A 328 ? 2.3041 1.8241 2.3658 0.3444  0.2916  0.1337  348 ASP   A CG  
2234 O  OD1 . ASP   A 328 ? 2.0807 1.6793 2.2062 0.3411  0.3019  0.1370  348 ASP   A OD1 
2235 O  OD2 . ASP   A 328 ? 2.3688 1.8237 2.3781 0.3644  0.3100  0.1218  348 ASP   A OD2 
2236 N  N   . THR   A 329 ? 2.1860 1.6265 2.1462 0.2401  0.1955  0.1622  349 THR   A N   
2237 C  CA  . THR   A 329 ? 2.0983 1.5293 2.0463 0.2221  0.1708  0.1804  349 THR   A CA  
2238 C  C   . THR   A 329 ? 2.0656 1.5472 2.0215 0.1821  0.1606  0.1837  349 THR   A C   
2239 O  O   . THR   A 329 ? 2.0145 1.5141 1.9736 0.1722  0.1436  0.2002  349 THR   A O   
2240 C  CB  . THR   A 329 ? 2.0056 1.3390 1.8911 0.2152  0.1632  0.1836  349 THR   A CB  
2241 O  OG1 . THR   A 329 ? 2.1229 1.4190 1.9702 0.1902  0.1692  0.1667  349 THR   A OG1 
2242 C  CG2 . THR   A 329 ? 1.8792 1.1592 1.7556 0.2595  0.1693  0.1832  349 THR   A CG2 
2243 N  N   . VAL   A 330 ? 2.0855 1.5889 2.0414 0.1618  0.1712  0.1689  350 VAL   A N   
2244 C  CA  . VAL   A 330 ? 1.9993 1.5523 1.9649 0.1271  0.1627  0.1707  350 VAL   A CA  
2245 C  C   . VAL   A 330 ? 2.0048 1.6403 2.0276 0.1359  0.1595  0.1742  350 VAL   A C   
2246 O  O   . VAL   A 330 ? 2.0621 1.7323 2.0921 0.1199  0.1445  0.1835  350 VAL   A O   
2247 C  CB  . VAL   A 330 ? 1.8264 1.3722 1.7718 0.1053  0.1724  0.1536  350 VAL   A CB  
2248 C  CG1 . VAL   A 330 ? 1.7266 1.3364 1.6944 0.0774  0.1668  0.1536  350 VAL   A CG1 
2249 C  CG2 . VAL   A 330 ? 1.7801 1.2475 1.6702 0.0871  0.1657  0.1506  350 VAL   A CG2 
2250 N  N   . LEU   A 331 ? 2.0173 1.6843 2.0821 0.1618  0.1734  0.1667  351 LEU   A N   
2251 C  CA  . LEU   A 331 ? 1.9737 1.7172 2.1008 0.1693  0.1676  0.1686  351 LEU   A CA  
2252 C  C   . LEU   A 331 ? 1.9693 1.7243 2.1151 0.1887  0.1465  0.1825  351 LEU   A C   
2253 O  O   . LEU   A 331 ? 1.7609 1.5765 1.9534 0.1920  0.1333  0.1837  351 LEU   A O   
2254 C  CB  . LEU   A 331 ? 1.6379 1.4120 1.8118 0.1901  0.1907  0.1594  351 LEU   A CB  
2255 C  CG  . LEU   A 331 ? 1.7557 1.5327 1.9175 0.1733  0.2110  0.1469  351 LEU   A CG  
2256 C  CD1 . LEU   A 331 ? 1.6796 1.4850 1.8876 0.1971  0.2383  0.1426  351 LEU   A CD1 
2257 C  CD2 . LEU   A 331 ? 1.9368 1.7577 2.1076 0.1418  0.1982  0.1452  351 LEU   A CD2 
2258 N  N   . GLN   A 332 ? 2.0116 1.7069 2.1204 0.2024  0.1410  0.1926  352 GLN   A N   
2259 C  CA  . GLN   A 332 ? 2.0040 1.7039 2.1227 0.2235  0.1192  0.2077  352 GLN   A CA  
2260 C  C   . GLN   A 332 ? 2.0791 1.7793 2.1633 0.2004  0.0990  0.2208  352 GLN   A C   
2261 O  O   . GLN   A 332 ? 2.2472 1.9796 2.3475 0.2128  0.0778  0.2297  352 GLN   A O   
2262 C  CB  . GLN   A 332 ? 2.0935 1.7251 2.1856 0.2516  0.1225  0.2146  352 GLN   A CB  
2263 C  CG  . GLN   A 332 ? 2.1380 1.7651 2.2334 0.2772  0.0988  0.2322  352 GLN   A CG  
2264 C  CD  . GLN   A 332 ? 2.2001 1.7525 2.2658 0.3058  0.1022  0.2393  352 GLN   A CD  
2265 O  OE1 . GLN   A 332 ? 2.2506 1.7641 2.3054 0.3142  0.1235  0.2277  352 GLN   A OE1 
2266 N  NE2 . GLN   A 332 ? 2.3406 1.8686 2.3880 0.3231  0.0806  0.2582  352 GLN   A NE2 
2267 N  N   . MET   A 333 ? 1.8756 1.5421 1.9133 0.1682  0.1049  0.2222  353 MET   A N   
2268 C  CA  . MET   A 333 ? 1.8963 1.5608 1.8997 0.1460  0.0920  0.2373  353 MET   A CA  
2269 C  C   . MET   A 333 ? 1.8231 1.5620 1.8556 0.1350  0.0840  0.2307  353 MET   A C   
2270 O  O   . MET   A 333 ? 1.7405 1.5045 1.7797 0.1109  0.0936  0.2188  353 MET   A O   
2271 C  CB  . MET   A 333 ? 1.8026 1.4166 1.7613 0.1133  0.1021  0.2399  353 MET   A CB  
2272 C  CG  . MET   A 333 ? 1.9554 1.4886 1.8840 0.1226  0.1084  0.2418  353 MET   A CG  
2273 S  SD  . MET   A 333 ? 2.1610 1.6302 2.0405 0.0810  0.1122  0.2477  353 MET   A SD  
2274 C  CE  . MET   A 333 ? 2.0119 1.3854 1.8616 0.1026  0.1158  0.2435  353 MET   A CE  
2275 N  N   . GLU   A 334 ? 1.6650 1.4365 1.7125 0.1544  0.0638  0.2377  354 GLU   A N   
2276 C  CA  . GLU   A 334 ? 1.6352 1.4729 1.7100 0.1481  0.0521  0.2285  354 GLU   A CA  
2277 C  C   . GLU   A 334 ? 1.5812 1.4212 1.6116 0.1240  0.0493  0.2377  354 GLU   A C   
2278 O  O   . GLU   A 334 ? 1.6287 1.5116 1.6719 0.1074  0.0504  0.2261  354 GLU   A O   
2279 C  CB  . GLU   A 334 ? 1.7703 1.6418 1.8797 0.1794  0.0272  0.2291  354 GLU   A CB  
2280 C  CG  . GLU   A 334 ? 2.0038 1.8906 2.1742 0.2035  0.0317  0.2195  354 GLU   A CG  
2281 C  CD  . GLU   A 334 ? 2.3382 2.2654 2.5534 0.2327  0.0030  0.2195  354 GLU   A CD  
2282 O  OE1 . GLU   A 334 ? 2.4454 2.3932 2.6436 0.2326  -0.0222 0.2221  354 GLU   A OE1 
2283 O  OE2 . GLU   A 334 ? 2.2933 2.2321 2.5607 0.2572  0.0051  0.2164  354 GLU   A OE2 
2284 N  N   . TYR   A 335 ? 1.6929 1.4869 1.6718 0.1228  0.0474  0.2597  355 TYR   A N   
2285 C  CA  . TYR   A 335 ? 1.6112 1.4084 1.5496 0.0998  0.0508  0.2716  355 TYR   A CA  
2286 C  C   . TYR   A 335 ? 1.5695 1.3634 1.5074 0.0649  0.0715  0.2644  355 TYR   A C   
2287 O  O   . TYR   A 335 ? 1.5876 1.4120 1.5169 0.0454  0.0760  0.2643  355 TYR   A O   
2288 C  CB  . TYR   A 335 ? 1.6073 1.3525 1.4918 0.1058  0.0478  0.3008  355 TYR   A CB  
2289 C  CG  . TYR   A 335 ? 1.6980 1.4577 1.5419 0.0927  0.0495  0.3164  355 TYR   A CG  
2290 C  CD1 . TYR   A 335 ? 1.7194 1.5189 1.5540 0.1121  0.0311  0.3146  355 TYR   A CD1 
2291 C  CD2 . TYR   A 335 ? 1.6793 1.4135 1.4952 0.0618  0.0696  0.3325  355 TYR   A CD2 
2292 C  CE1 . TYR   A 335 ? 1.7304 1.5417 1.5212 0.1043  0.0357  0.3286  355 TYR   A CE1 
2293 C  CE2 . TYR   A 335 ? 1.6187 1.3701 1.4000 0.0516  0.0763  0.3488  355 TYR   A CE2 
2294 C  CZ  . TYR   A 335 ? 1.7048 1.4938 1.4699 0.0746  0.0607  0.3468  355 TYR   A CZ  
2295 O  OH  . TYR   A 335 ? 1.8002 1.6049 1.5243 0.0686  0.0700  0.3627  355 TYR   A OH  
2296 N  N   . LEU   A 336 ? 1.5485 1.3055 1.4945 0.0590  0.0831  0.2575  356 LEU   A N   
2297 C  CA  . LEU   A 336 ? 1.5125 1.2699 1.4623 0.0291  0.0976  0.2461  356 LEU   A CA  
2298 C  C   . LEU   A 336 ? 1.5287 1.3481 1.5161 0.0262  0.0983  0.2248  356 LEU   A C   
2299 O  O   . LEU   A 336 ? 1.4466 1.2907 1.4334 0.0027  0.1041  0.2198  356 LEU   A O   
2300 C  CB  . LEU   A 336 ? 1.4479 1.1490 1.3928 0.0294  0.1062  0.2397  356 LEU   A CB  
2301 C  CG  . LEU   A 336 ? 1.6093 1.2980 1.5502 0.0003  0.1166  0.2273  356 LEU   A CG  
2302 C  CD1 . LEU   A 336 ? 1.4864 1.1650 1.4047 -0.0319 0.1179  0.2429  356 LEU   A CD1 
2303 C  CD2 . LEU   A 336 ? 1.7468 1.3743 1.6753 0.0084  0.1221  0.2182  356 LEU   A CD2 
2304 N  N   . ASP   A 337 ? 1.4787 1.3243 1.5024 0.0503  0.0925  0.2131  357 ASP   A N   
2305 C  CA  . ASP   A 337 ? 1.3167 1.2181 1.3791 0.0478  0.0923  0.1949  357 ASP   A CA  
2306 C  C   . ASP   A 337 ? 1.3503 1.2944 1.4078 0.0430  0.0799  0.1962  357 ASP   A C   
2307 O  O   . ASP   A 337 ? 1.2986 1.2780 1.3700 0.0295  0.0828  0.1840  357 ASP   A O   
2308 C  CB  . ASP   A 337 ? 1.4349 1.3551 1.5444 0.0737  0.0891  0.1856  357 ASP   A CB  
2309 C  CG  . ASP   A 337 ? 1.4943 1.4690 1.6487 0.0703  0.0886  0.1691  357 ASP   A CG  
2310 O  OD1 . ASP   A 337 ? 1.5135 1.4896 1.6746 0.0567  0.1046  0.1590  357 ASP   A OD1 
2311 O  OD2 . ASP   A 337 ? 1.4507 1.4637 1.6320 0.0817  0.0703  0.1660  357 ASP   A OD2 
2312 N  N   . MET   A 338 ? 1.3784 1.3164 1.4113 0.0565  0.0660  0.2109  358 MET   A N   
2313 C  CA  . MET   A 338 ? 1.3460 1.3191 1.3633 0.0564  0.0544  0.2117  358 MET   A CA  
2314 C  C   . MET   A 338 ? 1.4388 1.4120 1.4252 0.0298  0.0695  0.2190  358 MET   A C   
2315 O  O   . MET   A 338 ? 1.4037 1.4157 1.3916 0.0237  0.0683  0.2101  358 MET   A O   
2316 C  CB  . MET   A 338 ? 1.3347 1.2950 1.3237 0.0806  0.0356  0.2270  358 MET   A CB  
2317 C  CG  . MET   A 338 ? 1.5028 1.4782 1.5317 0.1089  0.0145  0.2178  358 MET   A CG  
2318 S  SD  . MET   A 338 ? 1.4247 1.3674 1.4176 0.1400  -0.0071 0.2393  358 MET   A SD  
2319 C  CE  . MET   A 338 ? 1.6155 1.5681 1.5447 0.1382  -0.0156 0.2499  358 MET   A CE  
2320 N  N   . VAL   A 339 ? 1.4885 1.4186 1.4501 0.0140  0.0834  0.2349  359 VAL   A N   
2321 C  CA  . VAL   A 339 ? 1.3109 1.2448 1.2553 -0.0141 0.0984  0.2426  359 VAL   A CA  
2322 C  C   . VAL   A 339 ? 1.1072 1.0685 1.0833 -0.0313 0.1055  0.2217  359 VAL   A C   
2323 O  O   . VAL   A 339 ? 1.1864 1.1808 1.1632 -0.0459 0.1116  0.2191  359 VAL   A O   
2324 C  CB  . VAL   A 339 ? 1.3837 1.2613 1.3016 -0.0292 0.1086  0.2645  359 VAL   A CB  
2325 C  CG1 . VAL   A 339 ? 1.3739 1.2598 1.2899 -0.0623 0.1237  0.2707  359 VAL   A CG1 
2326 C  CG2 . VAL   A 339 ? 1.3487 1.1997 1.2283 -0.0124 0.1030  0.2894  359 VAL   A CG2 
2327 N  N   . VAL   A 340 ? 1.2854 1.2330 1.2860 -0.0273 0.1059  0.2072  360 VAL   A N   
2328 C  CA  . VAL   A 340 ? 1.3972 1.3644 1.4212 -0.0410 0.1125  0.1889  360 VAL   A CA  
2329 C  C   . VAL   A 340 ? 1.4009 1.4217 1.4489 -0.0333 0.1061  0.1744  360 VAL   A C   
2330 O  O   . VAL   A 340 ? 1.1947 1.2431 1.2488 -0.0473 0.1103  0.1665  360 VAL   A O   
2331 C  CB  . VAL   A 340 ? 1.2551 1.1900 1.2913 -0.0343 0.1172  0.1788  360 VAL   A CB  
2332 C  CG1 . VAL   A 340 ? 1.3922 1.3487 1.4488 -0.0426 0.1232  0.1605  360 VAL   A CG1 
2333 C  CG2 . VAL   A 340 ? 1.2018 1.0778 1.2101 -0.0452 0.1221  0.1891  360 VAL   A CG2 
2334 N  N   . ASN   A 341 ? 1.3832 1.4188 1.4474 -0.0106 0.0937  0.1702  361 ASN   A N   
2335 C  CA  . ASN   A 341 ? 1.2660 1.3466 1.3559 -0.0038 0.0841  0.1545  361 ASN   A CA  
2336 C  C   . ASN   A 341 ? 1.2138 1.3203 1.2788 -0.0083 0.0805  0.1570  361 ASN   A C   
2337 O  O   . ASN   A 341 ? 1.3507 1.4877 1.4279 -0.0139 0.0809  0.1438  361 ASN   A O   
2338 C  CB  . ASN   A 341 ? 1.2366 1.3270 1.3533 0.0201  0.0674  0.1500  361 ASN   A CB  
2339 C  CG  . ASN   A 341 ? 1.2415 1.3172 1.3927 0.0272  0.0749  0.1460  361 ASN   A CG  
2340 O  OD1 . ASN   A 341 ? 1.2369 1.2984 1.3911 0.0155  0.0919  0.1421  361 ASN   A OD1 
2341 N  ND2 . ASN   A 341 ? 1.3412 1.4213 1.5184 0.0486  0.0622  0.1468  361 ASN   A ND2 
2342 N  N   . GLU   A 342 ? 1.2526 1.3453 1.2800 -0.0039 0.0788  0.1748  362 GLU   A N   
2343 C  CA  . GLU   A 342 ? 1.1908 1.3077 1.1889 -0.0035 0.0788  0.1789  362 GLU   A CA  
2344 C  C   . GLU   A 342 ? 1.3595 1.4899 1.3564 -0.0274 0.0976  0.1809  362 GLU   A C   
2345 O  O   . GLU   A 342 ? 1.4389 1.6038 1.4340 -0.0269 0.0990  0.1724  362 GLU   A O   
2346 C  CB  . GLU   A 342 ? 1.2175 1.3118 1.1705 0.0080  0.0762  0.2016  362 GLU   A CB  
2347 C  CG  . GLU   A 342 ? 1.3110 1.4252 1.2239 0.0092  0.0833  0.2111  362 GLU   A CG  
2348 C  CD  . GLU   A 342 ? 1.3261 1.4723 1.2323 0.0307  0.0647  0.1922  362 GLU   A CD  
2349 O  OE1 . GLU   A 342 ? 1.3943 1.5503 1.3352 0.0406  0.0451  0.1713  362 GLU   A OE1 
2350 O  OE2 . GLU   A 342 ? 1.3949 1.5551 1.2609 0.0380  0.0701  0.1983  362 GLU   A OE2 
2351 N  N   . THR   A 343 ? 1.2969 1.4002 1.2962 -0.0472 0.1104  0.1910  363 THR   A N   
2352 C  CA  . THR   A 343 ? 1.2341 1.3528 1.2410 -0.0711 0.1243  0.1917  363 THR   A CA  
2353 C  C   . THR   A 343 ? 1.2545 1.4008 1.2923 -0.0729 0.1212  0.1683  363 THR   A C   
2354 O  O   . THR   A 343 ? 1.1765 1.3556 1.2208 -0.0809 0.1268  0.1636  363 THR   A O   
2355 C  CB  . THR   A 343 ? 1.2390 1.3173 1.2439 -0.0923 0.1326  0.2043  363 THR   A CB  
2356 O  OG1 . THR   A 343 ? 1.2925 1.3384 1.2679 -0.0895 0.1352  0.2278  363 THR   A OG1 
2357 C  CG2 . THR   A 343 ? 1.3367 1.4352 1.3540 -0.1183 0.1434  0.2068  363 THR   A CG2 
2358 N  N   . LEU   A 344 ? 1.2869 1.4205 1.3448 -0.0641 0.1138  0.1549  364 LEU   A N   
2359 C  CA  . LEU   A 344 ? 1.1221 1.2775 1.2069 -0.0639 0.1118  0.1353  364 LEU   A CA  
2360 C  C   . LEU   A 344 ? 1.1131 1.3050 1.2040 -0.0499 0.1024  0.1238  364 LEU   A C   
2361 O  O   . LEU   A 344 ? 1.1419 1.3553 1.2497 -0.0521 0.1023  0.1101  364 LEU   A O   
2362 C  CB  . LEU   A 344 ? 1.0428 1.1751 1.1475 -0.0568 0.1106  0.1274  364 LEU   A CB  
2363 C  CG  . LEU   A 344 ? 1.0619 1.1579 1.1595 -0.0698 0.1199  0.1300  364 LEU   A CG  
2364 C  CD1 . LEU   A 344 ? 1.2729 1.3486 1.3865 -0.0574 0.1228  0.1225  364 LEU   A CD1 
2365 C  CD2 . LEU   A 344 ? 0.9496 1.0587 1.0480 -0.0872 0.1237  0.1237  364 LEU   A CD2 
2366 N  N   . ARG   A 345 ? 1.0095 1.2050 1.0837 -0.0342 0.0925  0.1283  365 ARG   A N   
2367 C  CA  . ARG   A 345 ? 1.1040 1.3292 1.1749 -0.0200 0.0811  0.1155  365 ARG   A CA  
2368 C  C   . ARG   A 345 ? 1.1001 1.3498 1.1508 -0.0262 0.0928  0.1187  365 ARG   A C   
2369 O  O   . ARG   A 345 ? 1.0354 1.3098 1.0965 -0.0231 0.0907  0.1033  365 ARG   A O   
2370 C  CB  . ARG   A 345 ? 1.0092 1.2284 1.0601 0.0005  0.0643  0.1189  365 ARG   A CB  
2371 C  CG  . ARG   A 345 ? 1.1064 1.3495 1.1498 0.0177  0.0468  0.1017  365 ARG   A CG  
2372 C  CD  . ARG   A 345 ? 1.0738 1.3086 1.0858 0.0392  0.0276  0.1060  365 ARG   A CD  
2373 N  NE  . ARG   A 345 ? 1.1773 1.4031 1.1363 0.0409  0.0413  0.1282  365 ARG   A NE  
2374 C  CZ  . ARG   A 345 ? 1.2515 1.4938 1.1715 0.0477  0.0489  0.1294  365 ARG   A CZ  
2375 N  NH1 . ARG   A 345 ? 1.3186 1.5849 1.2433 0.0550  0.0421  0.1075  365 ARG   A NH1 
2376 N  NH2 . ARG   A 345 ? 1.3810 1.6138 1.2557 0.0483  0.0654  0.1542  365 ARG   A NH2 
2377 N  N   . LEU   A 346 ? 1.2008 1.4438 1.2252 -0.0348 0.1065  0.1397  366 LEU   A N   
2378 C  CA  . LEU   A 346 ? 1.2375 1.5092 1.2493 -0.0409 0.1218  0.1461  366 LEU   A CA  
2379 C  C   . LEU   A 346 ? 1.0601 1.3473 1.1037 -0.0602 0.1307  0.1399  366 LEU   A C   
2380 O  O   . LEU   A 346 ? 0.9201 1.2414 0.9679 -0.0593 0.1378  0.1348  366 LEU   A O   
2381 C  CB  . LEU   A 346 ? 1.1039 1.3638 1.0852 -0.0477 0.1368  0.1741  366 LEU   A CB  
2382 C  CG  . LEU   A 346 ? 1.1475 1.3976 1.0838 -0.0247 0.1306  0.1834  366 LEU   A CG  
2383 C  CD1 . LEU   A 346 ? 1.4218 1.6547 1.3283 -0.0341 0.1493  0.2155  366 LEU   A CD1 
2384 C  CD2 . LEU   A 346 ? 0.9021 1.1842 0.8177 -0.0034 0.1266  0.1688  366 LEU   A CD2 
2385 N  N   . PHE   A 347 ? 0.9565 1.2185 1.0199 -0.0749 0.1294  0.1395  367 PHE   A N   
2386 C  CA  . PHE   A 347 ? 0.9971 1.2676 1.0847 -0.0928 0.1342  0.1342  367 PHE   A CA  
2387 C  C   . PHE   A 347 ? 1.0757 1.3257 1.1808 -0.0909 0.1251  0.1187  367 PHE   A C   
2388 O  O   . PHE   A 347 ? 1.1388 1.3574 1.2456 -0.1021 0.1260  0.1219  367 PHE   A O   
2389 C  CB  . PHE   A 347 ? 1.0188 1.2748 1.1059 -0.1165 0.1441  0.1527  367 PHE   A CB  
2390 C  CG  . PHE   A 347 ? 1.1579 1.4250 1.2261 -0.1189 0.1571  0.1744  367 PHE   A CG  
2391 C  CD1 . PHE   A 347 ? 1.1272 1.4399 1.1978 -0.1160 0.1684  0.1772  367 PHE   A CD1 
2392 C  CD2 . PHE   A 347 ? 1.1326 1.3632 1.1787 -0.1220 0.1598  0.1933  367 PHE   A CD2 
2393 C  CE1 . PHE   A 347 ? 1.0446 1.3677 1.0946 -0.1167 0.1850  0.2000  367 PHE   A CE1 
2394 C  CE2 . PHE   A 347 ? 1.2442 1.4814 1.2687 -0.1237 0.1742  0.2167  367 PHE   A CE2 
2395 C  CZ  . PHE   A 347 ? 1.1847 1.4692 1.2106 -0.1214 0.1882  0.2208  367 PHE   A CZ  
2396 N  N   . PRO   A 348 ? 0.9081 1.1723 1.0248 -0.0763 0.1171  0.1021  368 PRO   A N   
2397 C  CA  . PRO   A 348 ? 1.0728 1.3215 1.2082 -0.0762 0.1136  0.0902  368 PRO   A CA  
2398 C  C   . PRO   A 348 ? 1.2228 1.4818 1.3663 -0.0876 0.1166  0.0854  368 PRO   A C   
2399 O  O   . PRO   A 348 ? 1.2293 1.5161 1.3815 -0.0819 0.1143  0.0762  368 PRO   A O   
2400 C  CB  . PRO   A 348 ? 1.1877 1.4491 1.3357 -0.0587 0.1036  0.0765  368 PRO   A CB  
2401 C  CG  . PRO   A 348 ? 1.1312 1.4222 1.2650 -0.0506 0.1014  0.0749  368 PRO   A CG  
2402 C  CD  . PRO   A 348 ? 1.0212 1.3109 1.1318 -0.0584 0.1107  0.0936  368 PRO   A CD  
2403 N  N   . ILE   A 349 ? 1.1053 1.3395 1.2445 -0.1020 0.1194  0.0905  369 ILE   A N   
2404 C  CA  . ILE   A 349 ? 1.1097 1.3521 1.2543 -0.1149 0.1180  0.0876  369 ILE   A CA  
2405 C  C   . ILE   A 349 ? 1.0945 1.3497 1.2496 -0.1050 0.1136  0.0737  369 ILE   A C   
2406 O  O   . ILE   A 349 ? 1.1982 1.4747 1.3613 -0.1099 0.1101  0.0700  369 ILE   A O   
2407 C  CB  . ILE   A 349 ? 1.1844 1.3856 1.3169 -0.1282 0.1167  0.0907  369 ILE   A CB  
2408 C  CG1 . ILE   A 349 ? 1.2095 1.3737 1.3326 -0.1159 0.1187  0.0852  369 ILE   A CG1 
2409 C  CG2 . ILE   A 349 ? 1.0687 1.2570 1.1933 -0.1420 0.1200  0.1059  369 ILE   A CG2 
2410 C  CD1 . ILE   A 349 ? 1.2155 1.3335 1.3182 -0.1234 0.1181  0.0852  369 ILE   A CD1 
2411 N  N   . ALA   A 350 ? 1.2174 1.4599 1.3757 -0.0912 0.1134  0.0670  370 ALA   A N   
2412 C  CA  . ALA   A 350 ? 1.1016 1.3499 1.2695 -0.0820 0.1103  0.0562  370 ALA   A CA  
2413 C  C   . ALA   A 350 ? 1.0325 1.3153 1.2116 -0.0714 0.1058  0.0488  370 ALA   A C   
2414 O  O   . ALA   A 350 ? 0.9363 1.2283 1.1222 -0.0652 0.1022  0.0406  370 ALA   A O   
2415 C  CB  . ALA   A 350 ? 0.9057 1.1256 1.0785 -0.0737 0.1143  0.0541  370 ALA   A CB  
2416 N  N   . MET   A 351 ? 0.9860 1.2837 1.1624 -0.0665 0.1054  0.0511  371 MET   A N   
2417 C  CA  . MET   A 351 ? 0.9642 1.2912 1.1417 -0.0534 0.1011  0.0427  371 MET   A CA  
2418 C  C   . MET   A 351 ? 0.9315 1.2510 1.1220 -0.0402 0.0921  0.0284  371 MET   A C   
2419 O  O   . MET   A 351 ? 0.8948 1.2218 1.0837 -0.0279 0.0839  0.0200  371 MET   A O   
2420 C  CB  . MET   A 351 ? 1.0991 1.4579 1.2788 -0.0557 0.1049  0.0427  371 MET   A CB  
2421 C  CG  . MET   A 351 ? 1.2710 1.6445 1.4458 -0.0702 0.1141  0.0580  371 MET   A CG  
2422 S  SD  . MET   A 351 ? 1.4548 1.8702 1.6485 -0.0763 0.1177  0.0590  371 MET   A SD  
2423 C  CE  . MET   A 351 ? 1.5511 1.9390 1.7521 -0.0841 0.1067  0.0526  371 MET   A CE  
2424 N  N   . ARG   A 352 ? 0.9748 1.2767 1.1762 -0.0425 0.0926  0.0257  372 ARG   A N   
2425 C  CA  . ARG   A 352 ? 0.9498 1.2418 1.1673 -0.0328 0.0859  0.0147  372 ARG   A CA  
2426 C  C   . ARG   A 352 ? 0.9029 1.1639 1.1320 -0.0381 0.0923  0.0203  372 ARG   A C   
2427 O  O   . ARG   A 352 ? 0.9913 1.2377 1.2086 -0.0463 0.1013  0.0293  372 ARG   A O   
2428 C  CB  . ARG   A 352 ? 0.8387 1.1431 1.0558 -0.0252 0.0825  0.0064  372 ARG   A CB  
2429 C  CG  . ARG   A 352 ? 0.9058 1.2432 1.1137 -0.0150 0.0793  -0.0006 372 ARG   A CG  
2430 C  CD  . ARG   A 352 ? 1.0663 1.4173 1.2768 -0.0069 0.0778  -0.0066 372 ARG   A CD  
2431 N  NE  . ARG   A 352 ? 0.9305 1.3084 1.1353 0.0101  0.0748  -0.0177 372 ARG   A NE  
2432 C  CZ  . ARG   A 352 ? 0.9266 1.3163 1.1350 0.0239  0.0717  -0.0266 372 ARG   A CZ  
2433 N  NH1 . ARG   A 352 ? 1.1619 1.5386 1.3790 0.0224  0.0691  -0.0249 372 ARG   A NH1 
2434 N  NH2 . ARG   A 352 ? 1.0484 1.4614 1.2479 0.0425  0.0712  -0.0373 372 ARG   A NH2 
2435 N  N   . LEU   A 353 ? 0.8419 1.0924 1.0947 -0.0330 0.0879  0.0148  373 LEU   A N   
2436 C  CA  . LEU   A 353 ? 0.9040 1.1285 1.1739 -0.0359 0.0976  0.0210  373 LEU   A CA  
2437 C  C   . LEU   A 353 ? 0.9600 1.1762 1.2429 -0.0304 0.0932  0.0141  373 LEU   A C   
2438 O  O   . LEU   A 353 ? 0.9133 1.1384 1.2101 -0.0242 0.0789  0.0018  373 LEU   A O   
2439 C  CB  . LEU   A 353 ? 0.9762 1.1965 1.2747 -0.0369 0.0982  0.0241  373 LEU   A CB  
2440 C  CG  . LEU   A 353 ? 1.0426 1.2672 1.3293 -0.0392 0.1004  0.0310  373 LEU   A CG  
2441 C  CD1 . LEU   A 353 ? 1.0096 1.2365 1.3307 -0.0360 0.0950  0.0314  373 LEU   A CD1 
2442 C  CD2 . LEU   A 353 ? 0.9263 1.1307 1.1902 -0.0447 0.1171  0.0422  373 LEU   A CD2 
2443 N  N   . GLU   A 354 ? 0.9552 1.1502 1.2292 -0.0312 0.1042  0.0217  374 GLU   A N   
2444 C  CA  . GLU   A 354 ? 0.7868 0.9691 1.0661 -0.0249 0.1005  0.0177  374 GLU   A CA  
2445 C  C   . GLU   A 354 ? 0.8189 0.9695 1.1106 -0.0274 0.1166  0.0304  374 GLU   A C   
2446 O  O   . GLU   A 354 ? 1.0053 1.1417 1.2819 -0.0305 0.1331  0.0425  374 GLU   A O   
2447 C  CB  . GLU   A 354 ? 1.1562 1.3456 1.4052 -0.0190 0.0961  0.0152  374 GLU   A CB  
2448 C  CG  . GLU   A 354 ? 1.1507 1.3755 1.3930 -0.0148 0.0843  0.0043  374 GLU   A CG  
2449 C  CD  . GLU   A 354 ? 1.2611 1.4990 1.4872 -0.0069 0.0791  0.0011  374 GLU   A CD  
2450 O  OE1 . GLU   A 354 ? 1.2936 1.5106 1.5081 -0.0050 0.0818  0.0073  374 GLU   A OE1 
2451 O  OE2 . GLU   A 354 ? 1.3800 1.6499 1.6048 -0.0010 0.0726  -0.0070 374 GLU   A OE2 
2452 N  N   . ARG   A 355 ? 1.1122 1.2492 1.4299 -0.0254 0.1126  0.0277  375 ARG   A N   
2453 C  CA  . ARG   A 355 ? 1.0144 1.1204 1.3474 -0.0279 0.1300  0.0423  375 ARG   A CA  
2454 C  C   . ARG   A 355 ? 1.0154 1.1014 1.3475 -0.0213 0.1219  0.0389  375 ARG   A C   
2455 O  O   . ARG   A 355 ? 0.9992 1.0954 1.3421 -0.0169 0.1012  0.0222  375 ARG   A O   
2456 C  CB  . ARG   A 355 ? 0.8938 1.0021 1.2809 -0.0369 0.1356  0.0465  375 ARG   A CB  
2457 C  CG  . ARG   A 355 ? 1.0966 1.2227 1.4896 -0.0407 0.1434  0.0505  375 ARG   A CG  
2458 C  CD  . ARG   A 355 ? 1.0337 1.1407 1.4005 -0.0392 0.1713  0.0682  375 ARG   A CD  
2459 N  NE  . ARG   A 355 ? 1.0034 1.1229 1.3807 -0.0407 0.1796  0.0720  375 ARG   A NE  
2460 C  CZ  . ARG   A 355 ? 0.8130 0.9425 1.1584 -0.0393 0.1731  0.0670  375 ARG   A CZ  
2461 N  NH1 . ARG   A 355 ? 0.9351 1.0687 1.2409 -0.0381 0.1594  0.0585  375 ARG   A NH1 
2462 N  NH2 . ARG   A 355 ? 0.9572 1.0930 1.3145 -0.0390 0.1808  0.0714  375 ARG   A NH2 
2463 N  N   . VAL   A 356 ? 1.1824 1.2363 1.4970 -0.0184 0.1382  0.0547  376 VAL   A N   
2464 C  CA  . VAL   A 356 ? 0.9657 0.9925 1.2772 -0.0109 0.1324  0.0553  376 VAL   A CA  
2465 C  C   . VAL   A 356 ? 1.1864 1.1899 1.5474 -0.0206 0.1416  0.0646  376 VAL   A C   
2466 O  O   . VAL   A 356 ? 1.1704 1.1593 1.5432 -0.0274 0.1674  0.0847  376 VAL   A O   
2467 C  CB  . VAL   A 356 ? 1.0282 1.0297 1.2880 -0.0002 0.1424  0.0685  376 VAL   A CB  
2468 C  CG1 . VAL   A 356 ? 1.0715 1.0338 1.3319 0.0067  0.1433  0.0768  376 VAL   A CG1 
2469 C  CG2 . VAL   A 356 ? 1.2691 1.2963 1.4931 0.0091  0.1248  0.0556  376 VAL   A CG2 
2470 N  N   . CYS   A 357 ? 1.2671 1.2670 1.6588 -0.0212 0.1210  0.0499  377 CYS   A N   
2471 C  CA  . CYS   A 357 ? 1.3005 1.2741 1.7443 -0.0324 0.1252  0.0576  377 CYS   A CA  
2472 C  C   . CYS   A 357 ? 1.2505 1.1789 1.6741 -0.0281 0.1447  0.0800  377 CYS   A C   
2473 O  O   . CYS   A 357 ? 1.3703 1.2788 1.7578 -0.0139 0.1336  0.0755  377 CYS   A O   
2474 C  CB  . CYS   A 357 ? 1.1709 1.1444 1.6426 -0.0317 0.0933  0.0326  377 CYS   A CB  
2475 S  SG  . CYS   A 357 ? 1.4112 1.3477 1.9530 -0.0482 0.0904  0.0382  377 CYS   A SG  
2476 N  N   . LYS   A 358 ? 1.0749 0.9870 1.5202 -0.0383 0.1751  0.1056  378 LYS   A N   
2477 C  CA  . LYS   A 358 ? 1.3866 1.2539 1.8019 -0.0324 0.1996  0.1318  378 LYS   A CA  
2478 C  C   . LYS   A 358 ? 1.4749 1.3044 1.9383 -0.0430 0.2038  0.1439  378 LYS   A C   
2479 O  O   . LYS   A 358 ? 1.4462 1.2324 1.8839 -0.0377 0.2243  0.1680  378 LYS   A O   
2480 C  CB  . LYS   A 358 ? 1.1964 1.0635 1.5921 -0.0328 0.2364  0.1560  378 LYS   A CB  
2481 C  CG  . LYS   A 358 ? 1.3949 1.2641 1.8585 -0.0500 0.2636  0.1750  378 LYS   A CG  
2482 C  CD  . LYS   A 358 ? 1.4945 1.3519 1.9267 -0.0441 0.3063  0.2026  378 LYS   A CD  
2483 C  CE  . LYS   A 358 ? 1.4126 1.3058 1.8251 -0.0396 0.3079  0.1923  378 LYS   A CE  
2484 N  NZ  . LYS   A 358 ? 1.5288 1.4110 1.9243 -0.0341 0.3516  0.2178  378 LYS   A NZ  
2485 N  N   . LYS   A 359 ? 1.3146 1.1559 1.8450 -0.0579 0.1837  0.1281  379 LYS   A N   
2486 C  CA  . LYS   A 359 ? 1.4428 1.2452 2.0230 -0.0699 0.1801  0.1349  379 LYS   A CA  
2487 C  C   . LYS   A 359 ? 1.5651 1.3867 2.2031 -0.0811 0.1433  0.1046  379 LYS   A C   
2488 O  O   . LYS   A 359 ? 1.6563 1.5233 2.3066 -0.0829 0.1299  0.0867  379 LYS   A O   
2489 C  CB  . LYS   A 359 ? 1.4627 1.2477 2.0875 -0.0866 0.2204  0.1710  379 LYS   A CB  
2490 C  CG  . LYS   A 359 ? 1.3046 1.1348 1.9951 -0.1035 0.2328  0.1741  379 LYS   A CG  
2491 C  CD  . LYS   A 359 ? 1.1931 1.0070 1.9270 -0.1171 0.2784  0.2132  379 LYS   A CD  
2492 C  CE  . LYS   A 359 ? 1.2357 1.0987 2.0428 -0.1317 0.2925  0.2176  379 LYS   A CE  
2493 N  NZ  . LYS   A 359 ? 1.4698 1.3219 2.3194 -0.1424 0.3433  0.2582  379 LYS   A NZ  
2494 N  N   . ASP   A 360 ? 1.4771 1.2588 2.1466 -0.0875 0.1258  0.0991  380 ASP   A N   
2495 C  CA  . ASP   A 360 ? 1.4861 1.2749 2.2020 -0.0953 0.0854  0.0668  380 ASP   A CA  
2496 C  C   . ASP   A 360 ? 1.5177 1.3462 2.3092 -0.1172 0.0848  0.0662  380 ASP   A C   
2497 O  O   . ASP   A 360 ? 1.7054 1.5346 2.5495 -0.1353 0.1149  0.0948  380 ASP   A O   
2498 C  CB  . ASP   A 360 ? 1.5889 1.3187 2.3330 -0.1019 0.0704  0.0652  380 ASP   A CB  
2499 C  CG  . ASP   A 360 ? 1.7169 1.4082 2.3889 -0.0760 0.0618  0.0590  380 ASP   A CG  
2500 O  OD1 . ASP   A 360 ? 1.7509 1.4648 2.3558 -0.0546 0.0690  0.0580  380 ASP   A OD1 
2501 O  OD2 . ASP   A 360 ? 1.9158 1.5540 2.6014 -0.0768 0.0464  0.0547  380 ASP   A OD2 
2502 N  N   . VAL   A 361 ? 1.2504 1.1131 2.0467 -0.1136 0.0509  0.0341  381 VAL   A N   
2503 C  CA  . VAL   A 361 ? 1.3723 1.2750 2.2370 -0.1303 0.0416  0.0287  381 VAL   A CA  
2504 C  C   . VAL   A 361 ? 1.3873 1.2946 2.2631 -0.1273 -0.0098 -0.0114 381 VAL   A C   
2505 O  O   . VAL   A 361 ? 1.3733 1.2630 2.1911 -0.1080 -0.0326 -0.0353 381 VAL   A O   
2506 C  CB  . VAL   A 361 ? 1.4140 1.3660 2.2546 -0.1236 0.0636  0.0383  381 VAL   A CB  
2507 C  CG1 . VAL   A 361 ? 1.4310 1.3842 2.2979 -0.1339 0.1116  0.0769  381 VAL   A CG1 
2508 C  CG2 . VAL   A 361 ? 1.4314 1.3893 2.1776 -0.0990 0.0631  0.0284  381 VAL   A CG2 
2509 N  N   . GLU   A 362 ? 1.7637 1.6954 2.7148 -0.1448 -0.0283 -0.0190 382 GLU   A N   
2510 C  CA  . GLU   A 362 ? 1.7789 1.7176 2.7425 -0.1420 -0.0800 -0.0574 382 GLU   A CA  
2511 C  C   . GLU   A 362 ? 1.7372 1.7322 2.7290 -0.1447 -0.0841 -0.0587 382 GLU   A C   
2512 O  O   . GLU   A 362 ? 1.8185 1.8310 2.8967 -0.1643 -0.0969 -0.0576 382 GLU   A O   
2513 C  CB  . GLU   A 362 ? 1.9397 1.8401 2.9770 -0.1625 -0.1094 -0.0686 382 GLU   A CB  
2514 C  CG  . GLU   A 362 ? 1.9592 1.8592 3.0052 -0.1582 -0.1679 -0.1117 382 GLU   A CG  
2515 C  CD  . GLU   A 362 ? 2.2823 2.1452 3.4132 -0.1831 -0.1995 -0.1223 382 GLU   A CD  
2516 O  OE1 . GLU   A 362 ? 2.5024 2.3201 3.6547 -0.1954 -0.1817 -0.1043 382 GLU   A OE1 
2517 O  OE2 . GLU   A 362 ? 2.1738 2.0509 3.3507 -0.1905 -0.2435 -0.1483 382 GLU   A OE2 
2518 N  N   . ILE   A 363 ? 1.5078 1.5314 2.4300 -0.1250 -0.0736 -0.0601 383 ILE   A N   
2519 C  CA  . ILE   A 363 ? 1.5944 1.6669 2.5326 -0.1242 -0.0746 -0.0586 383 ILE   A CA  
2520 C  C   . ILE   A 363 ? 1.7131 1.7959 2.6449 -0.1152 -0.1259 -0.0945 383 ILE   A C   
2521 O  O   . ILE   A 363 ? 1.6579 1.7218 2.5245 -0.0972 -0.1484 -0.1192 383 ILE   A O   
2522 C  CB  . ILE   A 363 ? 1.4421 1.5350 2.3092 -0.1087 -0.0409 -0.0428 383 ILE   A CB  
2523 C  CG1 . ILE   A 363 ? 1.4165 1.5045 2.1940 -0.0857 -0.0569 -0.0646 383 ILE   A CG1 
2524 C  CG2 . ILE   A 363 ? 1.3808 1.4548 2.2401 -0.1137 0.0052  -0.0111 383 ILE   A CG2 
2525 C  CD1 . ILE   A 363 ? 1.3872 1.4990 2.1039 -0.0736 -0.0309 -0.0520 383 ILE   A CD1 
2526 N  N   . ASN   A 364 ? 1.7534 1.8663 2.7533 -0.1260 -0.1446 -0.0972 384 ASN   A N   
2527 C  CA  . ASN   A 364 ? 1.7420 1.8681 2.7377 -0.1165 -0.1949 -0.1289 384 ASN   A CA  
2528 C  C   . ASN   A 364 ? 1.7139 1.7986 2.6781 -0.1082 -0.2368 -0.1637 384 ASN   A C   
2529 O  O   . ASN   A 364 ? 1.6860 1.7703 2.5830 -0.0859 -0.2649 -0.1899 384 ASN   A O   
2530 C  CB  . ASN   A 364 ? 1.6523 1.8080 2.5737 -0.0942 -0.1887 -0.1296 384 ASN   A CB  
2531 C  CG  . ASN   A 364 ? 1.4959 1.6912 2.4543 -0.1001 -0.1592 -0.1021 384 ASN   A CG  
2532 O  OD1 . ASN   A 364 ? 1.5003 1.7246 2.4989 -0.1001 -0.1819 -0.1074 384 ASN   A OD1 
2533 N  ND2 . ASN   A 364 ? 1.3867 1.5815 2.3289 -0.1028 -0.1102 -0.0737 384 ASN   A ND2 
2534 N  N   . GLY   A 365 ? 1.6433 1.6899 2.6521 -0.1246 -0.2393 -0.1632 385 GLY   A N   
2535 C  CA  . GLY   A 365 ? 1.7320 1.7320 2.7192 -0.1179 -0.2805 -0.1970 385 GLY   A CA  
2536 C  C   . GLY   A 365 ? 1.7795 1.7474 2.6717 -0.0941 -0.2681 -0.2049 385 GLY   A C   
2537 O  O   . GLY   A 365 ? 1.7341 1.6638 2.5939 -0.0812 -0.3031 -0.2369 385 GLY   A O   
2538 N  N   . MET   A 366 ? 1.6814 1.6633 2.5291 -0.0866 -0.2214 -0.1781 386 MET   A N   
2539 C  CA  . MET   A 366 ? 1.5640 1.5235 2.3285 -0.0635 -0.2086 -0.1833 386 MET   A CA  
2540 C  C   . MET   A 366 ? 1.5287 1.4701 2.3024 -0.0732 -0.1662 -0.1506 386 MET   A C   
2541 O  O   . MET   A 366 ? 1.4093 1.3775 2.1992 -0.0833 -0.1300 -0.1199 386 MET   A O   
2542 C  CB  . MET   A 366 ? 1.5933 1.5902 2.2801 -0.0398 -0.1982 -0.1859 386 MET   A CB  
2543 C  CG  . MET   A 366 ? 1.5682 1.5522 2.1788 -0.0164 -0.1823 -0.1888 386 MET   A CG  
2544 S  SD  . MET   A 366 ? 1.5391 1.5717 2.0731 0.0055  -0.1648 -0.1857 386 MET   A SD  
2545 C  CE  . MET   A 366 ? 1.4144 1.4587 1.9376 0.0159  -0.2086 -0.2168 386 MET   A CE  
2546 N  N   . PHE   A 367 ? 1.5467 1.4394 2.3048 -0.0676 -0.1713 -0.1576 387 PHE   A N   
2547 C  CA  . PHE   A 367 ? 1.4516 1.3212 2.2039 -0.0714 -0.1336 -0.1273 387 PHE   A CA  
2548 C  C   . PHE   A 367 ? 1.4447 1.3373 2.1182 -0.0485 -0.1076 -0.1184 387 PHE   A C   
2549 O  O   . PHE   A 367 ? 1.4872 1.3909 2.1028 -0.0246 -0.1230 -0.1416 387 PHE   A O   
2550 C  CB  . PHE   A 367 ? 1.4602 1.2662 2.2181 -0.0702 -0.1500 -0.1377 387 PHE   A CB  
2551 C  CG  . PHE   A 367 ? 1.5597 1.3368 2.2905 -0.0652 -0.1157 -0.1099 387 PHE   A CG  
2552 C  CD1 . PHE   A 367 ? 1.6248 1.3919 2.4017 -0.0877 -0.0820 -0.0723 387 PHE   A CD1 
2553 C  CD2 . PHE   A 367 ? 1.5141 1.2748 2.1724 -0.0360 -0.1167 -0.1207 387 PHE   A CD2 
2554 C  CE1 . PHE   A 367 ? 1.5820 1.3183 2.3254 -0.0804 -0.0520 -0.0462 387 PHE   A CE1 
2555 C  CE2 . PHE   A 367 ? 1.5586 1.2923 2.1905 -0.0292 -0.0892 -0.0955 387 PHE   A CE2 
2556 C  CZ  . PHE   A 367 ? 1.5116 1.2307 2.1823 -0.0511 -0.0579 -0.0583 387 PHE   A CZ  
2557 N  N   . ILE   A 368 ? 1.5228 1.4226 2.1950 -0.0555 -0.0678 -0.0844 388 ILE   A N   
2558 C  CA  . ILE   A 368 ? 1.3265 1.2451 1.9316 -0.0375 -0.0441 -0.0736 388 ILE   A CA  
2559 C  C   . ILE   A 368 ? 1.5217 1.4029 2.1160 -0.0374 -0.0185 -0.0481 388 ILE   A C   
2560 O  O   . ILE   A 368 ? 1.4349 1.3050 2.0674 -0.0557 0.0062  -0.0205 388 ILE   A O   
2561 C  CB  . ILE   A 368 ? 1.4022 1.3694 2.0024 -0.0426 -0.0231 -0.0587 388 ILE   A CB  
2562 C  CG1 . ILE   A 368 ? 1.3503 1.3517 1.9525 -0.0392 -0.0493 -0.0824 388 ILE   A CG1 
2563 C  CG2 . ILE   A 368 ? 1.2723 1.2532 1.8090 -0.0275 -0.0003 -0.0466 388 ILE   A CG2 
2564 C  CD1 . ILE   A 368 ? 1.1153 1.1600 1.7078 -0.0418 -0.0313 -0.0692 388 ILE   A CD1 
2565 N  N   . PRO   A 369 ? 1.4770 1.3384 2.0196 -0.0155 -0.0221 -0.0549 389 PRO   A N   
2566 C  CA  . PRO   A 369 ? 1.3460 1.1654 1.8750 -0.0127 -0.0022 -0.0311 389 PRO   A CA  
2567 C  C   . PRO   A 369 ? 1.3805 1.2195 1.8787 -0.0122 0.0318  -0.0023 389 PRO   A C   
2568 O  O   . PRO   A 369 ? 1.4341 1.3186 1.9128 -0.0102 0.0381  -0.0039 389 PRO   A O   
2569 C  CB  . PRO   A 369 ? 1.3764 1.1762 1.8583 0.0155  -0.0219 -0.0521 389 PRO   A CB  
2570 C  CG  . PRO   A 369 ? 1.4362 1.2653 1.9107 0.0259  -0.0507 -0.0876 389 PRO   A CG  
2571 C  CD  . PRO   A 369 ? 1.4007 1.2784 1.8942 0.0102  -0.0434 -0.0835 389 PRO   A CD  
2572 N  N   . LYS   A 370 ? 1.3561 1.1548 1.8463 -0.0129 0.0530  0.0243  390 LYS   A N   
2573 C  CA  . LYS   A 370 ? 1.4505 1.2567 1.9041 -0.0101 0.0840  0.0515  390 LYS   A CA  
2574 C  C   . LYS   A 370 ? 1.3883 1.2172 1.7781 0.0139  0.0763  0.0413  390 LYS   A C   
2575 O  O   . LYS   A 370 ? 1.5157 1.3294 1.8819 0.0329  0.0578  0.0275  390 LYS   A O   
2576 C  CB  . LYS   A 370 ? 1.4215 1.1730 1.8745 -0.0135 0.1074  0.0828  390 LYS   A CB  
2577 C  CG  . LYS   A 370 ? 1.2097 0.9601 1.6166 -0.0079 0.1395  0.1114  390 LYS   A CG  
2578 C  CD  . LYS   A 370 ? 1.6202 1.3128 2.0251 -0.0108 0.1653  0.1449  390 LYS   A CD  
2579 C  CE  . LYS   A 370 ? 1.8183 1.5053 2.1686 -0.0024 0.1975  0.1726  390 LYS   A CE  
2580 N  NZ  . LYS   A 370 ? 2.0133 1.6425 2.3574 -0.0042 0.2275  0.2090  390 LYS   A NZ  
2581 N  N   . GLY   A 371 ? 1.2765 1.1423 1.6422 0.0131  0.0901  0.0480  391 GLY   A N   
2582 C  CA  . GLY   A 371 ? 1.2179 1.1089 1.5315 0.0311  0.0843  0.0415  391 GLY   A CA  
2583 C  C   . GLY   A 371 ? 1.2813 1.2248 1.5950 0.0337  0.0678  0.0172  391 GLY   A C   
2584 O  O   . GLY   A 371 ? 1.2659 1.2389 1.5459 0.0428  0.0671  0.0150  391 GLY   A O   
2585 N  N   . VAL   A 372 ? 1.2146 1.1691 1.5649 0.0258  0.0539  -0.0003 392 VAL   A N   
2586 C  CA  . VAL   A 372 ? 1.0721 1.0719 1.4163 0.0309  0.0390  -0.0222 392 VAL   A CA  
2587 C  C   . VAL   A 372 ? 1.1508 1.1850 1.4898 0.0194  0.0537  -0.0121 392 VAL   A C   
2588 O  O   . VAL   A 372 ? 1.3001 1.3277 1.6638 0.0034  0.0685  0.0024  392 VAL   A O   
2589 C  CB  . VAL   A 372 ? 1.1078 1.1035 1.4861 0.0273  0.0177  -0.0438 392 VAL   A CB  
2590 C  CG1 . VAL   A 372 ? 1.1374 1.1781 1.5045 0.0319  0.0064  -0.0619 392 VAL   A CG1 
2591 C  CG2 . VAL   A 372 ? 1.3013 1.2613 1.6761 0.0427  -0.0004 -0.0588 392 VAL   A CG2 
2592 N  N   . VAL   A 373 ? 1.2112 1.2819 1.5207 0.0278  0.0507  -0.0190 393 VAL   A N   
2593 C  CA  . VAL   A 373 ? 1.1110 1.2119 1.4135 0.0175  0.0612  -0.0121 393 VAL   A CA  
2594 C  C   . VAL   A 373 ? 1.1077 1.2314 1.4316 0.0125  0.0501  -0.0261 393 VAL   A C   
2595 O  O   . VAL   A 373 ? 1.1462 1.2898 1.4599 0.0237  0.0351  -0.0440 393 VAL   A O   
2596 C  CB  . VAL   A 373 ? 0.9570 1.0859 1.2244 0.0258  0.0617  -0.0119 393 VAL   A CB  
2597 C  CG1 . VAL   A 373 ? 0.8296 0.9883 1.0923 0.0147  0.0683  -0.0085 393 VAL   A CG1 
2598 C  CG2 . VAL   A 373 ? 0.8954 1.0003 1.1384 0.0301  0.0705  0.0033  393 VAL   A CG2 
2599 N  N   . VAL   A 374 ? 1.0221 1.1428 1.3743 -0.0021 0.0575  -0.0177 394 VAL   A N   
2600 C  CA  . VAL   A 374 ? 1.0357 1.1771 1.4078 -0.0063 0.0450  -0.0292 394 VAL   A CA  
2601 C  C   . VAL   A 374 ? 0.9424 1.1146 1.2891 -0.0074 0.0521  -0.0246 394 VAL   A C   
2602 O  O   . VAL   A 374 ? 0.9951 1.1654 1.3337 -0.0148 0.0703  -0.0082 394 VAL   A O   
2603 C  CB  . VAL   A 374 ? 0.8817 1.0096 1.3045 -0.0206 0.0481  -0.0217 394 VAL   A CB  
2604 C  CG1 . VAL   A 374 ? 0.8971 1.0444 1.3421 -0.0219 0.0270  -0.0370 394 VAL   A CG1 
2605 C  CG2 . VAL   A 374 ? 0.8417 0.9338 1.2920 -0.0234 0.0464  -0.0199 394 VAL   A CG2 
2606 N  N   . MET   A 375 ? 0.9716 1.1683 1.3025 0.0007  0.0384  -0.0388 395 MET   A N   
2607 C  CA  A MET   A 375 ? 1.1235 1.3478 1.4289 -0.0004 0.0451  -0.0335 395 MET   A CA  
2608 C  CA  B MET   A 375 ? 1.0565 1.2809 1.3617 -0.0004 0.0450  -0.0336 395 MET   A CA  
2609 C  C   . MET   A 375 ? 0.9629 1.2007 1.2742 0.0000  0.0331  -0.0407 395 MET   A C   
2610 O  O   . MET   A 375 ? 1.0775 1.3132 1.3950 0.0086  0.0137  -0.0578 395 MET   A O   
2611 C  CB  A MET   A 375 ? 1.0486 1.2940 1.3226 0.0110  0.0448  -0.0390 395 MET   A CB  
2612 C  CB  B MET   A 375 ? 0.9859 1.2313 1.2600 0.0113  0.0443  -0.0395 395 MET   A CB  
2613 C  CG  A MET   A 375 ? 0.9556 1.2283 1.2083 0.0061  0.0545  -0.0297 395 MET   A CG  
2614 C  CG  B MET   A 375 ? 0.9516 1.2252 1.2043 0.0070  0.0533  -0.0310 395 MET   A CG  
2615 S  SD  A MET   A 375 ? 0.7752 1.0742 1.0120 0.0136  0.0467  -0.0379 395 MET   A SD  
2616 S  SD  B MET   A 375 ? 1.1136 1.4229 1.3425 0.0233  0.0502  -0.0415 395 MET   A SD  
2617 C  CE  A MET   A 375 ? 0.8996 1.2092 1.1229 0.0363  0.0360  -0.0581 395 MET   A CE  
2618 C  CE  B MET   A 375 ? 0.9156 1.2257 1.1377 0.0354  0.0347  -0.0581 395 MET   A CE  
2619 N  N   . ILE   A 376 ? 0.8764 1.1244 1.1827 -0.0077 0.0425  -0.0285 396 ILE   A N   
2620 C  CA  . ILE   A 376 ? 0.9941 1.2542 1.2999 -0.0057 0.0318  -0.0317 396 ILE   A CA  
2621 C  C   . ILE   A 376 ? 0.8965 1.1780 1.1627 -0.0024 0.0386  -0.0266 396 ILE   A C   
2622 O  O   . ILE   A 376 ? 0.8937 1.1763 1.1504 -0.0118 0.0544  -0.0116 396 ILE   A O   
2623 C  CB  . ILE   A 376 ? 1.0095 1.2618 1.3457 -0.0156 0.0375  -0.0199 396 ILE   A CB  
2624 C  CG1 . ILE   A 376 ? 0.9361 1.1721 1.3210 -0.0205 0.0332  -0.0227 396 ILE   A CG1 
2625 C  CG2 . ILE   A 376 ? 0.8634 1.1283 1.1942 -0.0109 0.0249  -0.0217 396 ILE   A CG2 
2626 C  CD1 . ILE   A 376 ? 0.9160 1.1338 1.3107 -0.0285 0.0563  -0.0080 396 ILE   A CD1 
2627 N  N   . PRO   A 377 ? 0.8461 1.1428 1.0876 0.0109  0.0280  -0.0381 397 PRO   A N   
2628 C  CA  . PRO   A 377 ? 0.9635 1.2826 1.1709 0.0130  0.0388  -0.0295 397 PRO   A CA  
2629 C  C   . PRO   A 377 ? 0.9695 1.2881 1.1687 0.0073  0.0411  -0.0166 397 PRO   A C   
2630 O  O   . PRO   A 377 ? 0.9529 1.2755 1.1339 0.0181  0.0294  -0.0214 397 PRO   A O   
2631 C  CB  . PRO   A 377 ? 1.1533 1.4851 1.3354 0.0330  0.0283  -0.0462 397 PRO   A CB  
2632 C  CG  . PRO   A 377 ? 1.0955 1.4070 1.2940 0.0401  0.0044  -0.0639 397 PRO   A CG  
2633 C  CD  . PRO   A 377 ? 0.9685 1.2600 1.2102 0.0253  0.0063  -0.0595 397 PRO   A CD  
2634 N  N   . SER   A 378 ? 1.0594 1.3696 1.2675 -0.0075 0.0549  -0.0007 398 SER   A N   
2635 C  CA  . SER   A 378 ? 0.7231 1.0263 0.9259 -0.0119 0.0568  0.0119  398 SER   A CA  
2636 C  C   . SER   A 378 ? 0.9026 1.2205 1.0691 -0.0075 0.0603  0.0196  398 SER   A C   
2637 O  O   . SER   A 378 ? 0.9252 1.2391 1.0782 -0.0003 0.0519  0.0228  398 SER   A O   
2638 C  CB  . SER   A 378 ? 0.8635 1.1502 1.0760 -0.0264 0.0721  0.0255  398 SER   A CB  
2639 O  OG  . SER   A 378 ? 1.0893 1.3604 1.3328 -0.0283 0.0724  0.0220  398 SER   A OG  
2640 N  N   . TYR   A 379 ? 0.8921 1.2279 1.0437 -0.0112 0.0732  0.0243  399 TYR   A N   
2641 C  CA  . TYR   A 379 ? 0.9782 1.3306 1.0983 -0.0078 0.0815  0.0349  399 TYR   A CA  
2642 C  C   . TYR   A 379 ? 0.9657 1.3258 1.0602 0.0143  0.0692  0.0228  399 TYR   A C   
2643 O  O   . TYR   A 379 ? 0.9530 1.3130 1.0164 0.0215  0.0698  0.0320  399 TYR   A O   
2644 C  CB  . TYR   A 379 ? 1.0554 1.4329 1.1761 -0.0158 0.0977  0.0413  399 TYR   A CB  
2645 C  CG  . TYR   A 379 ? 0.9367 1.3347 1.0320 -0.0155 0.1123  0.0568  399 TYR   A CG  
2646 C  CD1 . TYR   A 379 ? 1.0402 1.4605 1.1103 0.0044  0.1151  0.0510  399 TYR   A CD1 
2647 C  CD2 . TYR   A 379 ? 1.0409 1.4329 1.1358 -0.0345 0.1246  0.0781  399 TYR   A CD2 
2648 C  CE1 . TYR   A 379 ? 1.1304 1.5700 1.1759 0.0057  0.1333  0.0684  399 TYR   A CE1 
2649 C  CE2 . TYR   A 379 ? 1.1493 1.5588 1.2243 -0.0363 0.1407  0.0959  399 TYR   A CE2 
2650 C  CZ  . TYR   A 379 ? 1.1742 1.6092 1.2247 -0.0159 0.1468  0.0923  399 TYR   A CZ  
2651 O  OH  . TYR   A 379 ? 1.1571 1.6102 1.1863 -0.0166 0.1676  0.1132  399 TYR   A OH  
2652 N  N   . ALA   A 380 ? 1.0060 1.3685 1.1088 0.0264  0.0568  0.0019  400 ALA   A N   
2653 C  CA  . ALA   A 380 ? 1.1514 1.5157 1.2249 0.0495  0.0415  -0.0140 400 ALA   A CA  
2654 C  C   . ALA   A 380 ? 1.1674 1.5112 1.2402 0.0549  0.0188  -0.0184 400 ALA   A C   
2655 O  O   . ALA   A 380 ? 1.2409 1.5838 1.2744 0.0717  0.0090  -0.0207 400 ALA   A O   
2656 C  CB  . ALA   A 380 ? 1.1147 1.4798 1.1989 0.0607  0.0315  -0.0369 400 ALA   A CB  
2657 N  N   . LEU   A 381 ? 0.9212 1.2495 1.0369 0.0425  0.0106  -0.0188 401 LEU   A N   
2658 C  CA  . LEU   A 381 ? 1.0542 1.3690 1.1819 0.0475  -0.0123 -0.0231 401 LEU   A CA  
2659 C  C   . LEU   A 381 ? 1.0935 1.4048 1.1972 0.0474  -0.0065 -0.0029 401 LEU   A C   
2660 O  O   . LEU   A 381 ? 1.2744 1.5795 1.3602 0.0614  -0.0268 -0.0061 401 LEU   A O   
2661 C  CB  . LEU   A 381 ? 1.1098 1.4139 1.2964 0.0343  -0.0169 -0.0260 401 LEU   A CB  
2662 C  CG  . LEU   A 381 ? 1.0810 1.3815 1.2949 0.0331  -0.0233 -0.0434 401 LEU   A CG  
2663 C  CD1 . LEU   A 381 ? 0.9589 1.2485 1.2309 0.0193  -0.0229 -0.0406 401 LEU   A CD1 
2664 C  CD2 . LEU   A 381 ? 1.1109 1.4086 1.3085 0.0511  -0.0513 -0.0675 401 LEU   A CD2 
2665 N  N   . HIS   A 382 ? 1.0415 1.3532 1.1430 0.0323  0.0187  0.0177  402 HIS   A N   
2666 C  CA  . HIS   A 382 ? 1.0601 1.3623 1.1382 0.0308  0.0257  0.0386  402 HIS   A CA  
2667 C  C   . HIS   A 382 ? 1.2062 1.5148 1.2279 0.0458  0.0273  0.0452  402 HIS   A C   
2668 O  O   . HIS   A 382 ? 1.2346 1.5308 1.2306 0.0486  0.0294  0.0630  402 HIS   A O   
2669 C  CB  . HIS   A 382 ? 1.0616 1.3585 1.1495 0.0098  0.0506  0.0568  402 HIS   A CB  
2670 C  CG  . HIS   A 382 ? 1.0555 1.3388 1.1864 -0.0017 0.0520  0.0547  402 HIS   A CG  
2671 N  ND1 . HIS   A 382 ? 1.0599 1.3282 1.1960 -0.0172 0.0687  0.0687  402 HIS   A ND1 
2672 C  CD2 . HIS   A 382 ? 1.1631 1.4441 1.3325 0.0007  0.0404  0.0411  402 HIS   A CD2 
2673 C  CE1 . HIS   A 382 ? 1.0694 1.3264 1.2391 -0.0210 0.0689  0.0635  402 HIS   A CE1 
2674 N  NE2 . HIS   A 382 ? 1.1046 1.3710 1.2982 -0.0113 0.0536  0.0486  402 HIS   A NE2 
2675 N  N   . ARG   A 383 ? 1.2343 1.5597 1.2332 0.0575  0.0280  0.0325  403 ARG   A N   
2676 C  CA  . ARG   A 383 ? 1.4072 1.7400 1.3474 0.0749  0.0345  0.0393  403 ARG   A CA  
2677 C  C   . ARG   A 383 ? 1.4586 1.7904 1.3697 0.1017  0.0097  0.0137  403 ARG   A C   
2678 O  O   . ARG   A 383 ? 1.3779 1.7192 1.2381 0.1198  0.0184  0.0133  403 ARG   A O   
2679 C  CB  . ARG   A 383 ? 1.2411 1.5982 1.1735 0.0660  0.0667  0.0522  403 ARG   A CB  
2680 C  CG  . ARG   A 383 ? 1.1615 1.5178 1.1270 0.0375  0.0864  0.0725  403 ARG   A CG  
2681 C  CD  . ARG   A 383 ? 1.3085 1.6878 1.2601 0.0290  0.1162  0.0928  403 ARG   A CD  
2682 N  NE  . ARG   A 383 ? 1.2289 1.5996 1.2064 0.0014  0.1298  0.1129  403 ARG   A NE  
2683 C  CZ  . ARG   A 383 ? 1.0731 1.4518 1.0413 -0.0117 0.1527  0.1380  403 ARG   A CZ  
2684 N  NH1 . ARG   A 383 ? 1.1403 1.5388 1.0735 0.0008  0.1693  0.1495  403 ARG   A NH1 
2685 N  NH2 . ARG   A 383 ? 1.1340 1.4982 1.1277 -0.0377 0.1595  0.1521  403 ARG   A NH2 
2686 N  N   . ASP   A 384 ? 1.4638 1.7835 1.4064 0.1048  -0.0208 -0.0076 404 ASP   A N   
2687 C  CA  . ASP   A 384 ? 1.6587 1.9720 1.5778 0.1283  -0.0504 -0.0356 404 ASP   A CA  
2688 C  C   . ASP   A 384 ? 1.7826 2.0811 1.6530 0.1492  -0.0731 -0.0340 404 ASP   A C   
2689 O  O   . ASP   A 384 ? 1.8333 2.1216 1.7287 0.1439  -0.0890 -0.0270 404 ASP   A O   
2690 C  CB  . ASP   A 384 ? 1.7172 2.0228 1.6972 0.1200  -0.0751 -0.0579 404 ASP   A CB  
2691 C  CG  . ASP   A 384 ? 1.8402 2.1351 1.8012 0.1412  -0.1075 -0.0902 404 ASP   A CG  
2692 O  OD1 . ASP   A 384 ? 1.9267 2.2207 1.8215 0.1652  -0.1083 -0.0970 404 ASP   A OD1 
2693 O  OD2 . ASP   A 384 ? 1.8651 2.1506 1.8769 0.1343  -0.1316 -0.1086 404 ASP   A OD2 
2694 N  N   . PRO   A 385 ? 1.9356 2.2320 1.7344 0.1755  -0.0748 -0.0398 405 PRO   A N   
2695 C  CA  . PRO   A 385 ? 1.9062 2.1842 1.6493 0.1991  -0.0998 -0.0390 405 PRO   A CA  
2696 C  C   . PRO   A 385 ? 1.8915 2.1541 1.6612 0.2074  -0.1507 -0.0666 405 PRO   A C   
2697 O  O   . PRO   A 385 ? 1.9014 2.1498 1.6449 0.2218  -0.1766 -0.0636 405 PRO   A O   
2698 C  CB  . PRO   A 385 ? 1.8810 2.1602 1.5401 0.2277  -0.0880 -0.0436 405 PRO   A CB  
2699 C  CG  . PRO   A 385 ? 1.7159 2.0212 1.3918 0.2130  -0.0439 -0.0311 405 PRO   A CG  
2700 C  CD  . PRO   A 385 ? 1.7538 2.0663 1.5148 0.1863  -0.0483 -0.0420 405 PRO   A CD  
2701 N  N   . LYS   A 386 ? 1.8836 2.1479 1.7067 0.1985  -0.1669 -0.0924 406 LYS   A N   
2702 C  CA  . LYS   A 386 ? 1.9812 2.2342 1.8484 0.1996  -0.2142 -0.1167 406 LYS   A CA  
2703 C  C   . LYS   A 386 ? 1.9067 2.1665 1.8491 0.1774  -0.2168 -0.1006 406 LYS   A C   
2704 O  O   . LYS   A 386 ? 1.9592 2.2170 1.9572 0.1736  -0.2518 -0.1170 406 LYS   A O   
2705 C  CB  . LYS   A 386 ? 2.0444 2.2935 1.9470 0.1952  -0.2278 -0.1468 406 LYS   A CB  
2706 C  CG  . LYS   A 386 ? 2.0958 2.3347 1.9242 0.2220  -0.2293 -0.1675 406 LYS   A CG  
2707 C  CD  . LYS   A 386 ? 2.2651 2.4833 2.1120 0.2294  -0.2710 -0.2071 406 LYS   A CD  
2708 C  CE  . LYS   A 386 ? 2.4159 2.6185 2.1766 0.2628  -0.2748 -0.2299 406 LYS   A CE  
2709 N  NZ  . LYS   A 386 ? 2.3637 2.5370 2.1335 0.2728  -0.3222 -0.2718 406 LYS   A NZ  
2710 N  N   . TYR   A 387 ? 1.9990 2.2667 1.9460 0.1629  -0.1797 -0.0691 407 TYR   A N   
2711 C  CA  . TYR   A 387 ? 1.9937 2.2640 1.9959 0.1481  -0.1783 -0.0514 407 TYR   A CA  
2712 C  C   . TYR   A 387 ? 2.0146 2.2780 1.9736 0.1520  -0.1580 -0.0204 407 TYR   A C   
2713 O  O   . TYR   A 387 ? 2.0285 2.2874 2.0140 0.1522  -0.1694 -0.0095 407 TYR   A O   
2714 C  CB  . TYR   A 387 ? 1.8661 2.1465 1.9389 0.1199  -0.1521 -0.0457 407 TYR   A CB  
2715 C  CG  . TYR   A 387 ? 2.0041 2.2883 2.1492 0.1109  -0.1754 -0.0677 407 TYR   A CG  
2716 C  CD1 . TYR   A 387 ? 2.0223 2.3113 2.2325 0.1055  -0.1939 -0.0666 407 TYR   A CD1 
2717 C  CD2 . TYR   A 387 ? 1.9505 2.2334 2.1026 0.1078  -0.1773 -0.0879 407 TYR   A CD2 
2718 C  CE1 . TYR   A 387 ? 2.1066 2.4012 2.3900 0.0947  -0.2125 -0.0835 407 TYR   A CE1 
2719 C  CE2 . TYR   A 387 ? 2.0495 2.3316 2.2695 0.0975  -0.1975 -0.1055 407 TYR   A CE2 
2720 C  CZ  . TYR   A 387 ? 2.1129 2.4019 2.4002 0.0896  -0.2142 -0.1024 407 TYR   A CZ  
2721 O  OH  . TYR   A 387 ? 2.2239 2.5144 2.5862 0.0768  -0.2319 -0.1169 407 TYR   A OH  
2722 N  N   . TRP   A 388 ? 1.8420 2.1043 1.7393 0.1553  -0.1280 -0.0049 408 TRP   A N   
2723 C  CA  . TRP   A 388 ? 1.7545 2.0073 1.6155 0.1538  -0.1034 0.0278  408 TRP   A CA  
2724 C  C   . TRP   A 388 ? 1.8049 2.0478 1.5752 0.1799  -0.1047 0.0345  408 TRP   A C   
2725 O  O   . TRP   A 388 ? 1.8995 2.1509 1.6306 0.1889  -0.0937 0.0251  408 TRP   A O   
2726 C  CB  . TRP   A 388 ? 1.6067 1.8684 1.4866 0.1279  -0.0599 0.0463  408 TRP   A CB  
2727 C  CG  . TRP   A 388 ? 1.4192 1.6881 1.3759 0.1052  -0.0556 0.0390  408 TRP   A CG  
2728 C  CD1 . TRP   A 388 ? 1.2156 1.4982 1.2061 0.0946  -0.0503 0.0219  408 TRP   A CD1 
2729 C  CD2 . TRP   A 388 ? 1.4925 1.7523 1.4967 0.0930  -0.0544 0.0498  408 TRP   A CD2 
2730 N  NE1 . TRP   A 388 ? 1.1800 1.4620 1.2332 0.0761  -0.0451 0.0229  408 TRP   A NE1 
2731 C  CE2 . TRP   A 388 ? 1.4665 1.7357 1.5293 0.0753  -0.0465 0.0392  408 TRP   A CE2 
2732 C  CE3 . TRP   A 388 ? 1.3806 1.6232 1.3809 0.0978  -0.0585 0.0678  408 TRP   A CE3 
2733 C  CZ2 . TRP   A 388 ? 1.2168 1.4799 1.3314 0.0631  -0.0401 0.0460  408 TRP   A CZ2 
2734 C  CZ3 . TRP   A 388 ? 1.3354 1.5728 1.3909 0.0861  -0.0534 0.0729  408 TRP   A CZ3 
2735 C  CH2 . TRP   A 388 ? 1.3117 1.5600 1.4224 0.0692  -0.0431 0.0620  408 TRP   A CH2 
2736 N  N   . THR   A 389 ? 1.7900 2.0136 1.5247 0.1943  -0.1169 0.0516  409 THR   A N   
2737 C  CA  . THR   A 389 ? 1.9436 2.1524 1.5841 0.2199  -0.1135 0.0648  409 THR   A CA  
2738 C  C   . THR   A 389 ? 1.8665 2.0768 1.4796 0.2053  -0.0627 0.0987  409 THR   A C   
2739 O  O   . THR   A 389 ? 1.7818 1.9842 1.4255 0.1847  -0.0441 0.1226  409 THR   A O   
2740 C  CB  . THR   A 389 ? 1.9709 2.1556 1.5831 0.2413  -0.1461 0.0733  409 THR   A CB  
2741 O  OG1 . THR   A 389 ? 1.8899 2.0646 1.5378 0.2240  -0.1302 0.1006  409 THR   A OG1 
2742 C  CG2 . THR   A 389 ? 1.7080 1.8963 1.3601 0.2532  -0.1996 0.0395  409 THR   A CG2 
2743 N  N   . GLU   A 390 ? 1.9145 2.1345 1.4713 0.2166  -0.0406 0.1003  410 GLU   A N   
2744 C  CA  . GLU   A 390 ? 1.9710 2.2009 1.5107 0.2014  0.0092  0.1312  410 GLU   A CA  
2745 C  C   . GLU   A 390 ? 1.8973 2.1434 1.5194 0.1638  0.0298  0.1354  410 GLU   A C   
2746 O  O   . GLU   A 390 ? 1.8101 2.0426 1.4529 0.1439  0.0445  0.1607  410 GLU   A O   
2747 C  CB  . GLU   A 390 ? 2.0840 2.2864 1.5671 0.2087  0.0223  0.1687  410 GLU   A CB  
2748 C  CG  . GLU   A 390 ? 2.2065 2.3918 1.5910 0.2484  0.0103  0.1700  410 GLU   A CG  
2749 C  CD  . GLU   A 390 ? 2.3103 2.4630 1.6363 0.2567  0.0226  0.2100  410 GLU   A CD  
2750 O  OE1 . GLU   A 390 ? 2.2572 2.3892 1.6175 0.2437  0.0122  0.2237  410 GLU   A OE1 
2751 O  OE2 . GLU   A 390 ? 2.3650 2.5107 1.6087 0.2776  0.0445  0.2288  410 GLU   A OE2 
2752 N  N   . PRO   A 391 ? 1.9387 2.2097 1.6050 0.1547  0.0300  0.1107  411 PRO   A N   
2753 C  CA  . PRO   A 391 ? 1.8052 2.0857 1.5487 0.1230  0.0394  0.1096  411 PRO   A CA  
2754 C  C   . PRO   A 391 ? 1.7324 2.0224 1.4880 0.0975  0.0791  0.1377  411 PRO   A C   
2755 O  O   . PRO   A 391 ? 1.7562 2.0392 1.5602 0.0728  0.0843  0.1447  411 PRO   A O   
2756 C  CB  . PRO   A 391 ? 1.7794 2.0806 1.5530 0.1256  0.0285  0.0770  411 PRO   A CB  
2757 C  CG  . PRO   A 391 ? 1.9011 2.2116 1.6111 0.1527  0.0323  0.0691  411 PRO   A CG  
2758 C  CD  . PRO   A 391 ? 1.9912 2.2777 1.6343 0.1755  0.0205  0.0822  411 PRO   A CD  
2759 N  N   . GLU   A 392 ? 1.7115 2.0172 1.4261 0.1029  0.1071  0.1540  412 GLU   A N   
2760 C  CA  . GLU   A 392 ? 1.7124 2.0326 1.4494 0.0759  0.1435  0.1801  412 GLU   A CA  
2761 C  C   . GLU   A 392 ? 1.6673 1.9566 1.3921 0.0621  0.1541  0.2135  412 GLU   A C   
2762 O  O   . GLU   A 392 ? 1.5978 1.8928 1.3488 0.0350  0.1799  0.2350  412 GLU   A O   
2763 C  CB  . GLU   A 392 ? 1.8365 2.1898 1.5423 0.0861  0.1736  0.1883  412 GLU   A CB  
2764 C  CG  . GLU   A 392 ? 1.8381 2.2251 1.5679 0.0940  0.1713  0.1588  412 GLU   A CG  
2765 C  CD  . GLU   A 392 ? 2.0928 2.4689 1.7857 0.1271  0.1400  0.1272  412 GLU   A CD  
2766 O  OE1 . GLU   A 392 ? 2.1501 2.4998 1.7877 0.1483  0.1243  0.1304  412 GLU   A OE1 
2767 O  OE2 . GLU   A 392 ? 2.0803 2.4717 1.7991 0.1323  0.1289  0.0988  412 GLU   A OE2 
2768 N  N   . LYS   A 393 ? 1.7489 2.0044 1.4372 0.0799  0.1327  0.2179  413 LYS   A N   
2769 C  CA  . LYS   A 393 ? 1.7101 1.9302 1.3779 0.0718  0.1420  0.2509  413 LYS   A CA  
2770 C  C   . LYS   A 393 ? 1.6240 1.8189 1.3426 0.0538  0.1268  0.2474  413 LYS   A C   
2771 O  O   . LYS   A 393 ? 1.5753 1.7703 1.3236 0.0614  0.0991  0.2213  413 LYS   A O   
2772 C  CB  . LYS   A 393 ? 1.6475 1.8418 1.2413 0.1050  0.1271  0.2603  413 LYS   A CB  
2773 C  CG  . LYS   A 393 ? 1.8944 2.1097 1.4275 0.1316  0.1363  0.2563  413 LYS   A CG  
2774 C  CD  . LYS   A 393 ? 2.0356 2.2190 1.4825 0.1608  0.1325  0.2781  413 LYS   A CD  
2775 C  CE  . LYS   A 393 ? 1.9365 2.0988 1.3653 0.1430  0.1684  0.3248  413 LYS   A CE  
2776 N  NZ  . LYS   A 393 ? 1.9751 2.1040 1.3112 0.1735  0.1690  0.3501  413 LYS   A NZ  
2777 N  N   . PHE   A 394 ? 1.5409 1.7130 1.2698 0.0300  0.1461  0.2743  414 PHE   A N   
2778 C  CA  . PHE   A 394 ? 1.5329 1.6741 1.3006 0.0150  0.1354  0.2733  414 PHE   A CA  
2779 C  C   . PHE   A 394 ? 1.6663 1.7693 1.4022 0.0385  0.1134  0.2811  414 PHE   A C   
2780 O  O   . PHE   A 394 ? 1.7845 1.8580 1.4744 0.0438  0.1227  0.3104  414 PHE   A O   
2781 C  CB  . PHE   A 394 ? 1.6155 1.7413 1.4021 -0.0181 0.1611  0.2971  414 PHE   A CB  
2782 C  CG  . PHE   A 394 ? 1.4441 1.5300 1.2600 -0.0312 0.1516  0.2966  414 PHE   A CG  
2783 C  CD1 . PHE   A 394 ? 1.3354 1.4303 1.2008 -0.0430 0.1438  0.2720  414 PHE   A CD1 
2784 C  CD2 . PHE   A 394 ? 1.6504 1.6861 1.4397 -0.0295 0.1517  0.3213  414 PHE   A CD2 
2785 C  CE1 . PHE   A 394 ? 1.4117 1.4676 1.2972 -0.0514 0.1374  0.2706  414 PHE   A CE1 
2786 C  CE2 . PHE   A 394 ? 1.6070 1.6027 1.4197 -0.0381 0.1438  0.3192  414 PHE   A CE2 
2787 C  CZ  . PHE   A 394 ? 1.4126 1.4191 1.2724 -0.0485 0.1373  0.2931  414 PHE   A CZ  
2788 N  N   . LEU   A 395 ? 1.5640 1.6679 1.3270 0.0528  0.0845  0.2563  415 LEU   A N   
2789 C  CA  . LEU   A 395 ? 1.5386 1.6144 1.2818 0.0781  0.0585  0.2596  415 LEU   A CA  
2790 C  C   . LEU   A 395 ? 1.6282 1.6967 1.4304 0.0749  0.0431  0.2432  415 LEU   A C   
2791 O  O   . LEU   A 395 ? 1.6742 1.7686 1.5139 0.0826  0.0239  0.2161  415 LEU   A O   
2792 C  CB  . LEU   A 395 ? 1.4765 1.5697 1.1836 0.1095  0.0331  0.2447  415 LEU   A CB  
2793 C  CG  . LEU   A 395 ? 1.4258 1.5172 1.0569 0.1233  0.0466  0.2639  415 LEU   A CG  
2794 C  CD1 . LEU   A 395 ? 1.6429 1.7573 1.2442 0.1513  0.0219  0.2384  415 LEU   A CD1 
2795 C  CD2 . LEU   A 395 ? 1.5985 1.6448 1.1772 0.1362  0.0467  0.2969  415 LEU   A CD2 
2796 N  N   . PRO   A 396 ? 1.6292 1.6606 1.4411 0.0640  0.0525  0.2596  416 PRO   A N   
2797 C  CA  . PRO   A 396 ? 1.6227 1.6455 1.4865 0.0651  0.0418  0.2452  416 PRO   A CA  
2798 C  C   . PRO   A 396 ? 1.6937 1.7193 1.5676 0.0957  0.0104  0.2358  416 PRO   A C   
2799 O  O   . PRO   A 396 ? 1.6996 1.7332 1.6266 0.0990  0.0015  0.2200  416 PRO   A O   
2800 C  CB  . PRO   A 396 ? 1.6049 1.5788 1.4605 0.0510  0.0587  0.2673  416 PRO   A CB  
2801 C  CG  . PRO   A 396 ? 1.6438 1.6128 1.4648 0.0300  0.0822  0.2881  416 PRO   A CG  
2802 C  CD  . PRO   A 396 ? 1.6717 1.6674 1.4522 0.0475  0.0764  0.2909  416 PRO   A CD  
2803 N  N   . GLU   A 397 ? 1.6738 1.6943 1.4995 0.1190  -0.0068 0.2454  417 GLU   A N   
2804 C  CA  . GLU   A 397 ? 1.7289 1.7547 1.5660 0.1492  -0.0425 0.2353  417 GLU   A CA  
2805 C  C   . GLU   A 397 ? 1.6897 1.7611 1.5759 0.1528  -0.0637 0.2025  417 GLU   A C   
2806 O  O   . GLU   A 397 ? 1.7375 1.8198 1.6515 0.1740  -0.0956 0.1908  417 GLU   A O   
2807 C  CB  . GLU   A 397 ? 1.8661 1.8730 1.6295 0.1746  -0.0582 0.2527  417 GLU   A CB  
2808 C  CG  . GLU   A 397 ? 2.0350 1.9894 1.7595 0.1812  -0.0495 0.2858  417 GLU   A CG  
2809 C  CD  . GLU   A 397 ? 2.1612 2.1002 1.9268 0.1989  -0.0702 0.2836  417 GLU   A CD  
2810 O  OE1 . GLU   A 397 ? 2.2026 2.1737 2.0128 0.2155  -0.1001 0.2604  417 GLU   A OE1 
2811 O  OE2 . GLU   A 397 ? 2.1539 2.0487 1.9106 0.1965  -0.0566 0.3051  417 GLU   A OE2 
2812 N  N   . ARG   A 398 ? 1.5360 1.6337 1.4368 0.1328  -0.0484 0.1879  418 ARG   A N   
2813 C  CA  . ARG   A 398 ? 1.4862 1.6207 1.4399 0.1329  -0.0662 0.1579  418 ARG   A CA  
2814 C  C   . ARG   A 398 ? 1.4365 1.5764 1.4648 0.1285  -0.0675 0.1499  418 ARG   A C   
2815 O  O   . ARG   A 398 ? 1.5719 1.7384 1.6518 0.1355  -0.0901 0.1298  418 ARG   A O   
2816 C  CB  . ARG   A 398 ? 1.5412 1.6973 1.4951 0.1127  -0.0463 0.1465  418 ARG   A CB  
2817 C  CG  . ARG   A 398 ? 1.4748 1.6323 1.3606 0.1171  -0.0383 0.1536  418 ARG   A CG  
2818 C  CD  . ARG   A 398 ? 1.2960 1.4797 1.1952 0.0997  -0.0206 0.1394  418 ARG   A CD  
2819 N  NE  . ARG   A 398 ? 1.5351 1.7213 1.3784 0.0977  0.0016  0.1534  418 ARG   A NE  
2820 C  CZ  . ARG   A 398 ? 1.6015 1.8007 1.4002 0.1156  -0.0062 0.1443  418 ARG   A CZ  
2821 N  NH1 . ARG   A 398 ? 1.6315 1.8384 1.4316 0.1359  -0.0403 0.1192  418 ARG   A NH1 
2822 N  NH2 . ARG   A 398 ? 1.6267 1.8311 1.3796 0.1132  0.0209  0.1603  418 ARG   A NH2 
2823 N  N   . PHE   A 399 ? 1.3987 1.5129 1.4342 0.1174  -0.0432 0.1653  419 PHE   A N   
2824 C  CA  . PHE   A 399 ? 1.4836 1.6005 1.5827 0.1135  -0.0359 0.1587  419 PHE   A CA  
2825 C  C   . PHE   A 399 ? 1.4432 1.5365 1.5516 0.1338  -0.0446 0.1715  419 PHE   A C   
2826 O  O   . PHE   A 399 ? 1.4639 1.5481 1.6106 0.1321  -0.0300 0.1720  419 PHE   A O   
2827 C  CB  . PHE   A 399 ? 1.3697 1.4736 1.4709 0.0876  -0.0024 0.1612  419 PHE   A CB  
2828 C  CG  . PHE   A 399 ? 1.3330 1.4636 1.4373 0.0698  0.0055  0.1471  419 PHE   A CG  
2829 C  CD1 . PHE   A 399 ? 1.3994 1.5580 1.5572 0.0658  0.0026  0.1277  419 PHE   A CD1 
2830 C  CD2 . PHE   A 399 ? 1.4607 1.5887 1.5171 0.0580  0.0169  0.1547  419 PHE   A CD2 
2831 C  CE1 . PHE   A 399 ? 1.4052 1.5843 1.5641 0.0518  0.0086  0.1151  419 PHE   A CE1 
2832 C  CE2 . PHE   A 399 ? 1.4074 1.5614 1.4689 0.0450  0.0237  0.1414  419 PHE   A CE2 
2833 C  CZ  . PHE   A 399 ? 1.2379 1.4151 1.3484 0.0426  0.0184  0.1211  419 PHE   A CZ  
2834 N  N   . SER   A 400 ? 1.6894 1.7709 1.7600 0.1556  -0.0676 0.1821  420 SER   A N   
2835 C  CA  . SER   A 400 ? 1.7014 1.7663 1.7882 0.1801  -0.0824 0.1918  420 SER   A CA  
2836 C  C   . SER   A 400 ? 1.8448 1.9522 2.0104 0.1936  -0.1069 0.1723  420 SER   A C   
2837 O  O   . SER   A 400 ? 1.7532 1.8975 1.9452 0.1886  -0.1229 0.1528  420 SER   A O   
2838 C  CB  . SER   A 400 ? 1.7717 1.8100 1.7911 0.2016  -0.1024 0.2100  420 SER   A CB  
2839 O  OG  . SER   A 400 ? 1.6357 1.7022 1.6401 0.2138  -0.1331 0.1968  420 SER   A OG  
2840 N  N   . LYS   A 401 ? 1.9271 2.0290 2.1342 0.2112  -0.1096 0.1780  421 LYS   A N   
2841 C  CA  . LYS   A 401 ? 1.9375 2.0841 2.2313 0.2240  -0.1306 0.1626  421 LYS   A CA  
2842 C  C   . LYS   A 401 ? 1.9187 2.0905 2.2140 0.2432  -0.1785 0.1532  421 LYS   A C   
2843 O  O   . LYS   A 401 ? 1.9224 2.1373 2.2955 0.2496  -0.2018 0.1376  421 LYS   A O   
2844 C  CB  . LYS   A 401 ? 1.9556 2.0914 2.2912 0.2429  -0.1213 0.1727  421 LYS   A CB  
2845 C  CG  . LYS   A 401 ? 2.0068 2.1659 2.4158 0.2315  -0.0923 0.1636  421 LYS   A CG  
2846 C  CD  . LYS   A 401 ? 2.0529 2.1731 2.4553 0.2406  -0.0618 0.1767  421 LYS   A CD  
2847 C  CE  . LYS   A 401 ? 1.9985 2.1161 2.4268 0.2762  -0.0812 0.1862  421 LYS   A CE  
2848 N  NZ  . LYS   A 401 ? 1.9446 2.0224 2.3688 0.2879  -0.0503 0.1963  421 LYS   A NZ  
2849 N  N   . LYS   A 402 ? 1.7882 1.9335 1.9997 0.2526  -0.1940 0.1626  422 LYS   A N   
2850 C  CA  . LYS   A 402 ? 1.7491 1.9130 1.9446 0.2705  -0.2402 0.1506  422 LYS   A CA  
2851 C  C   . LYS   A 402 ? 1.7304 1.9180 1.9206 0.2513  -0.2437 0.1288  422 LYS   A C   
2852 O  O   . LYS   A 402 ? 1.7460 1.9600 1.9561 0.2614  -0.2838 0.1087  422 LYS   A O   
2853 C  CB  . LYS   A 402 ? 1.8338 1.9549 1.9320 0.2920  -0.2524 0.1717  422 LYS   A CB  
2854 C  CG  . LYS   A 402 ? 1.9121 2.0424 1.9688 0.3138  -0.2994 0.1602  422 LYS   A CG  
2855 C  CD  . LYS   A 402 ? 2.0783 2.1606 2.0291 0.3353  -0.3037 0.1860  422 LYS   A CD  
2856 C  CE  . LYS   A 402 ? 2.1942 2.2786 2.0774 0.3524  -0.3386 0.1742  422 LYS   A CE  
2857 N  NZ  . LYS   A 402 ? 2.0130 2.1113 1.8762 0.3277  -0.3171 0.1592  422 LYS   A NZ  
2858 N  N   . ASN   A 403 ? 1.8702 2.0479 2.0359 0.2246  -0.2047 0.1311  423 ASN   A N   
2859 C  CA  . ASN   A 403 ? 1.7872 1.9829 1.9410 0.2086  -0.2047 0.1122  423 ASN   A CA  
2860 C  C   . ASN   A 403 ? 1.7183 1.9336 1.9311 0.1806  -0.1757 0.1014  423 ASN   A C   
2861 O  O   . ASN   A 403 ? 1.8003 2.0322 2.0146 0.1686  -0.1785 0.0837  423 ASN   A O   
2862 C  CB  . ASN   A 403 ? 1.6113 1.7793 1.6669 0.2057  -0.1877 0.1252  423 ASN   A CB  
2863 C  CG  . ASN   A 403 ? 1.8266 1.9723 1.8099 0.2348  -0.2150 0.1366  423 ASN   A CG  
2864 O  OD1 . ASN   A 403 ? 1.9789 2.1350 1.9809 0.2582  -0.2569 0.1270  423 ASN   A OD1 
2865 N  ND2 . ASN   A 403 ? 1.6947 1.8099 1.5954 0.2338  -0.1918 0.1583  423 ASN   A ND2 
2866 N  N   . LYS   A 404 ? 1.5512 1.7618 1.8077 0.1722  -0.1482 0.1113  424 LYS   A N   
2867 C  CA  . LYS   A 404 ? 1.5766 1.7998 1.8765 0.1476  -0.1182 0.1037  424 LYS   A CA  
2868 C  C   . LYS   A 404 ? 1.6885 1.9514 2.0671 0.1430  -0.1360 0.0822  424 LYS   A C   
2869 O  O   . LYS   A 404 ? 1.5984 1.8710 2.0085 0.1233  -0.1134 0.0756  424 LYS   A O   
2870 C  CB  . LYS   A 404 ? 1.7035 1.9082 2.0254 0.1445  -0.0864 0.1182  424 LYS   A CB  
2871 C  CG  . LYS   A 404 ? 1.8605 2.0817 2.2518 0.1633  -0.0981 0.1192  424 LYS   A CG  
2872 C  CD  . LYS   A 404 ? 1.8764 2.0905 2.3061 0.1567  -0.0611 0.1251  424 LYS   A CD  
2873 C  CE  . LYS   A 404 ? 1.9917 2.1557 2.3544 0.1516  -0.0331 0.1408  424 LYS   A CE  
2874 N  NZ  . LYS   A 404 ? 2.2082 2.3597 2.5983 0.1478  0.0011  0.1434  424 LYS   A NZ  
2875 N  N   . ASP   A 405 ? 1.7761 2.0602 2.1877 0.1603  -0.1771 0.0719  425 ASP   A N   
2876 C  CA  . ASP   A 405 ? 1.6928 2.0143 2.1882 0.1539  -0.1977 0.0520  425 ASP   A CA  
2877 C  C   . ASP   A 405 ? 1.6972 2.0231 2.1665 0.1458  -0.2184 0.0308  425 ASP   A C   
2878 O  O   . ASP   A 405 ? 1.6593 2.0062 2.1886 0.1308  -0.2217 0.0154  425 ASP   A O   
2879 C  CB  . ASP   A 405 ? 1.7760 2.1211 2.3291 0.1754  -0.2372 0.0488  425 ASP   A CB  
2880 C  CG  . ASP   A 405 ? 1.8392 2.1640 2.3648 0.1974  -0.2328 0.0702  425 ASP   A CG  
2881 O  OD1 . ASP   A 405 ? 1.8433 2.1555 2.3793 0.1931  -0.1940 0.0857  425 ASP   A OD1 
2882 O  OD2 . ASP   A 405 ? 1.8021 2.1191 2.2902 0.2205  -0.2691 0.0711  425 ASP   A OD2 
2883 N  N   . ASN   A 406 ? 2.1875 2.4918 2.5670 0.1565  -0.2305 0.0305  426 ASN   A N   
2884 C  CA  . ASN   A 406 ? 2.2067 2.5118 2.5512 0.1551  -0.2512 0.0091  426 ASN   A CA  
2885 C  C   . ASN   A 406 ? 2.1867 2.4836 2.5040 0.1341  -0.2128 0.0096  426 ASN   A C   
2886 O  O   . ASN   A 406 ? 2.2873 2.5743 2.5406 0.1369  -0.2148 0.0016  426 ASN   A O   
2887 C  CB  . ASN   A 406 ? 2.3168 2.6023 2.5712 0.1799  -0.2779 0.0096  426 ASN   A CB  
2888 C  CG  . ASN   A 406 ? 2.3962 2.6788 2.6542 0.2033  -0.3037 0.0212  426 ASN   A CG  
2889 O  OD1 . ASN   A 406 ? 2.3652 2.6714 2.7061 0.2062  -0.3248 0.0157  426 ASN   A OD1 
2890 N  ND2 . ASN   A 406 ? 2.4936 2.7475 2.6634 0.2209  -0.3013 0.0389  426 ASN   A ND2 
2891 N  N   . ILE   A 407 ? 1.6140 1.9150 1.9779 0.1153  -0.1776 0.0191  427 ILE   A N   
2892 C  CA  . ILE   A 407 ? 1.4082 1.7009 1.7494 0.0961  -0.1412 0.0220  427 ILE   A CA  
2893 C  C   . ILE   A 407 ? 1.3957 1.7042 1.8143 0.0787  -0.1300 0.0138  427 ILE   A C   
2894 O  O   . ILE   A 407 ? 1.3380 1.6542 1.8141 0.0757  -0.1175 0.0231  427 ILE   A O   
2895 C  CB  . ILE   A 407 ? 1.4391 1.7102 1.7398 0.0913  -0.1051 0.0462  427 ILE   A CB  
2896 C  CG1 . ILE   A 407 ? 1.5016 1.7543 1.7204 0.1050  -0.1110 0.0571  427 ILE   A CG1 
2897 C  CG2 . ILE   A 407 ? 1.3345 1.6014 1.6306 0.0701  -0.0707 0.0478  427 ILE   A CG2 
2898 C  CD1 . ILE   A 407 ? 1.4949 1.7222 1.6780 0.0994  -0.0802 0.0819  427 ILE   A CD1 
2899 N  N   . ASP   A 408 ? 1.1779 1.4896 1.5960 0.0691  -0.1329 -0.0023 428 ASP   A N   
2900 C  CA  . ASP   A 408 ? 1.1397 1.4609 1.6238 0.0520  -0.1206 -0.0081 428 ASP   A CA  
2901 C  C   . ASP   A 408 ? 1.0521 1.3618 1.5259 0.0385  -0.0757 0.0084  428 ASP   A C   
2902 O  O   . ASP   A 408 ? 1.0736 1.3708 1.4893 0.0346  -0.0597 0.0109  428 ASP   A O   
2903 C  CB  . ASP   A 408 ? 1.2249 1.5457 1.7034 0.0481  -0.1392 -0.0305 428 ASP   A CB  
2904 C  CG  . ASP   A 408 ? 1.2526 1.5842 1.8153 0.0342  -0.1451 -0.0398 428 ASP   A CG  
2905 O  OD1 . ASP   A 408 ? 1.2473 1.5838 1.8588 0.0225  -0.1162 -0.0253 428 ASP   A OD1 
2906 O  OD2 . ASP   A 408 ? 1.1696 1.5022 1.7481 0.0355  -0.1784 -0.0617 428 ASP   A OD2 
2907 N  N   . PRO   A 409 ? 1.0363 1.3505 1.5647 0.0323  -0.0549 0.0194  429 PRO   A N   
2908 C  CA  . PRO   A 409 ? 1.0462 1.3450 1.5601 0.0216  -0.0149 0.0326  429 PRO   A CA  
2909 C  C   . PRO   A 409 ? 1.0420 1.3363 1.5542 0.0077  -0.0028 0.0255  429 PRO   A C   
2910 O  O   . PRO   A 409 ? 0.9557 1.2368 1.4580 -0.0003 0.0275  0.0352  429 PRO   A O   
2911 C  CB  . PRO   A 409 ? 1.2041 1.5111 1.7817 0.0235  0.0006  0.0436  429 PRO   A CB  
2912 C  CG  . PRO   A 409 ? 1.2106 1.5451 1.8601 0.0259  -0.0294 0.0325  429 PRO   A CG  
2913 C  CD  . PRO   A 409 ? 1.2147 1.5504 1.8244 0.0361  -0.0683 0.0191  429 PRO   A CD  
2914 N  N   . TYR   A 410 ? 1.0547 1.3563 1.5734 0.0067  -0.0271 0.0081  430 TYR   A N   
2915 C  CA  . TYR   A 410 ? 1.0532 1.3468 1.5606 -0.0029 -0.0192 0.0002  430 TYR   A CA  
2916 C  C   . TYR   A 410 ? 1.1783 1.4684 1.6215 0.0038  -0.0322 -0.0111 430 TYR   A C   
2917 O  O   . TYR   A 410 ? 1.2323 1.5173 1.6636 0.0000  -0.0305 -0.0204 430 TYR   A O   
2918 C  CB  . TYR   A 410 ? 1.0074 1.3075 1.5820 -0.0103 -0.0327 -0.0106 430 TYR   A CB  
2919 C  CG  . TYR   A 410 ? 1.1319 1.4382 1.7727 -0.0179 -0.0109 0.0043  430 TYR   A CG  
2920 C  CD1 . TYR   A 410 ? 1.1089 1.4015 1.7480 -0.0265 0.0251  0.0177  430 TYR   A CD1 
2921 C  CD2 . TYR   A 410 ? 0.9097 1.2366 1.6129 -0.0142 -0.0253 0.0058  430 TYR   A CD2 
2922 C  CE1 . TYR   A 410 ? 1.0922 1.3896 1.7852 -0.0304 0.0499  0.0329  430 TYR   A CE1 
2923 C  CE2 . TYR   A 410 ? 1.0047 1.3418 1.7719 -0.0192 -0.0006 0.0212  430 TYR   A CE2 
2924 C  CZ  . TYR   A 410 ? 1.1394 1.4606 1.8984 -0.0269 0.0391  0.0351  430 TYR   A CZ  
2925 O  OH  . TYR   A 410 ? 1.3767 1.7065 2.1927 -0.0291 0.0686  0.0519  430 TYR   A OH  
2926 N  N   . ILE   A 411 ? 1.1493 1.4417 1.5509 0.0155  -0.0439 -0.0092 431 ILE   A N   
2927 C  CA  . ILE   A 411 ? 1.1208 1.4108 1.4545 0.0223  -0.0439 -0.0119 431 ILE   A CA  
2928 C  C   . ILE   A 411 ? 1.2208 1.5036 1.5160 0.0175  -0.0165 0.0083  431 ILE   A C   
2929 O  O   . ILE   A 411 ? 1.2764 1.5591 1.5369 0.0129  -0.0011 0.0107  431 ILE   A O   
2930 C  CB  . ILE   A 411 ? 1.2385 1.5323 1.5443 0.0401  -0.0762 -0.0233 431 ILE   A CB  
2931 C  CG1 . ILE   A 411 ? 1.2156 1.5123 1.5590 0.0437  -0.1086 -0.0471 431 ILE   A CG1 
2932 C  CG2 . ILE   A 411 ? 1.2948 1.5875 1.5278 0.0491  -0.0700 -0.0228 431 ILE   A CG2 
2933 C  CD1 . ILE   A 411 ? 1.3162 1.6078 1.6587 0.0381  -0.1039 -0.0608 431 ILE   A CD1 
2934 N  N   . TYR   A 412 ? 1.0472 1.3237 1.3518 0.0187  -0.0114 0.0224  432 TYR   A N   
2935 C  CA  . TYR   A 412 ? 1.1794 1.4418 1.4539 0.0123  0.0132  0.0409  432 TYR   A CA  
2936 C  C   . TYR   A 412 ? 1.1017 1.3547 1.4083 0.0008  0.0356  0.0463  432 TYR   A C   
2937 O  O   . TYR   A 412 ? 1.1290 1.3780 1.4714 0.0037  0.0392  0.0516  432 TYR   A O   
2938 C  CB  . TYR   A 412 ? 1.0698 1.3232 1.3294 0.0228  0.0060  0.0531  432 TYR   A CB  
2939 C  CG  . TYR   A 412 ? 0.9870 1.2188 1.2169 0.0154  0.0290  0.0717  432 TYR   A CG  
2940 C  CD1 . TYR   A 412 ? 1.1217 1.3489 1.3032 0.0087  0.0395  0.0797  432 TYR   A CD1 
2941 C  CD2 . TYR   A 412 ? 0.9412 1.1564 1.1935 0.0154  0.0404  0.0810  432 TYR   A CD2 
2942 C  CE1 . TYR   A 412 ? 1.1155 1.3201 1.2745 -0.0011 0.0574  0.0959  432 TYR   A CE1 
2943 C  CE2 . TYR   A 412 ? 1.0734 1.2618 1.2956 0.0089  0.0583  0.0953  432 TYR   A CE2 
2944 C  CZ  . TYR   A 412 ? 1.0751 1.2573 1.2521 -0.0009 0.0651  0.1025  432 TYR   A CZ  
2945 O  OH  . TYR   A 412 ? 1.1704 1.3235 1.3222 -0.0103 0.0800  0.1161  432 TYR   A OH  
2946 N  N   . THR   A 413 ? 1.1676 1.4175 1.4602 -0.0098 0.0508  0.0450  433 THR   A N   
2947 C  CA  . THR   A 413 ? 1.1680 1.4048 1.4779 -0.0186 0.0719  0.0496  433 THR   A CA  
2948 C  C   . THR   A 413 ? 1.2091 1.4328 1.4776 -0.0281 0.0877  0.0569  433 THR   A C   
2949 O  O   . THR   A 413 ? 1.2536 1.4799 1.5138 -0.0344 0.0927  0.0522  433 THR   A O   
2950 C  CB  . THR   A 413 ? 1.2149 1.4588 1.5572 -0.0214 0.0702  0.0391  433 THR   A CB  
2951 O  OG1 . THR   A 413 ? 1.2805 1.5341 1.5984 -0.0218 0.0612  0.0288  433 THR   A OG1 
2952 C  CG2 . THR   A 413 ? 1.1891 1.4449 1.5840 -0.0158 0.0538  0.0324  433 THR   A CG2 
2953 N  N   . PRO   A 414 ? 1.1642 1.3721 1.4082 -0.0294 0.0937  0.0684  434 PRO   A N   
2954 C  CA  . PRO   A 414 ? 1.1623 1.3553 1.3733 -0.0413 0.1058  0.0747  434 PRO   A CA  
2955 C  C   . PRO   A 414 ? 1.1484 1.3182 1.3613 -0.0457 0.1210  0.0754  434 PRO   A C   
2956 O  O   . PRO   A 414 ? 1.1900 1.3489 1.3785 -0.0559 0.1264  0.0764  434 PRO   A O   
2957 C  CB  . PRO   A 414 ? 0.9533 1.1310 1.1408 -0.0409 0.1053  0.0871  434 PRO   A CB  
2958 C  CG  . PRO   A 414 ? 1.0804 1.2535 1.2924 -0.0269 0.1000  0.0884  434 PRO   A CG  
2959 C  CD  . PRO   A 414 ? 1.1208 1.3210 1.3680 -0.0199 0.0878  0.0761  434 PRO   A CD  
2960 N  N   . PHE   A 415 ? 1.0713 1.2339 1.3125 -0.0376 0.1280  0.0752  435 PHE   A N   
2961 C  CA  . PHE   A 415 ? 1.1759 1.3145 1.4135 -0.0376 0.1459  0.0769  435 PHE   A CA  
2962 C  C   . PHE   A 415 ? 1.0834 1.2331 1.3532 -0.0349 0.1512  0.0728  435 PHE   A C   
2963 O  O   . PHE   A 415 ? 0.9226 1.0545 1.1970 -0.0307 0.1694  0.0770  435 PHE   A O   
2964 C  CB  . PHE   A 415 ? 1.0166 1.1310 1.2555 -0.0282 0.1575  0.0844  435 PHE   A CB  
2965 C  CG  . PHE   A 415 ? 1.0948 1.1855 1.2972 -0.0317 0.1544  0.0897  435 PHE   A CG  
2966 C  CD1 . PHE   A 415 ? 1.1923 1.2509 1.3557 -0.0393 0.1609  0.0895  435 PHE   A CD1 
2967 C  CD2 . PHE   A 415 ? 1.1267 1.2238 1.3327 -0.0272 0.1431  0.0951  435 PHE   A CD2 
2968 C  CE1 . PHE   A 415 ? 1.1364 1.1690 1.2704 -0.0452 0.1568  0.0945  435 PHE   A CE1 
2969 C  CE2 . PHE   A 415 ? 1.1505 1.2210 1.3233 -0.0314 0.1415  0.1025  435 PHE   A CE2 
2970 C  CZ  . PHE   A 415 ? 1.1020 1.1399 1.2414 -0.0418 0.1486  0.1023  435 PHE   A CZ  
2971 N  N   . GLY   A 416 ? 1.0028 1.1783 1.2925 -0.0364 0.1366  0.0651  436 GLY   A N   
2972 C  CA  . GLY   A 416 ? 1.0036 1.1862 1.3284 -0.0354 0.1392  0.0616  436 GLY   A CA  
2973 C  C   . GLY   A 416 ? 0.8977 1.0887 1.2749 -0.0294 0.1422  0.0651  436 GLY   A C   
2974 O  O   . GLY   A 416 ? 1.0638 1.2630 1.4536 -0.0237 0.1341  0.0668  436 GLY   A O   
2975 N  N   . SER   A 417 ? 0.9601 1.1495 1.3710 -0.0305 0.1540  0.0677  437 SER   A N   
2976 C  CA  . SER   A 417 ? 0.9640 1.1661 1.4375 -0.0271 0.1600  0.0730  437 SER   A CA  
2977 C  C   . SER   A 417 ? 0.8202 1.0109 1.3154 -0.0300 0.1839  0.0817  437 SER   A C   
2978 O  O   . SER   A 417 ? 0.8900 1.0645 1.3535 -0.0339 0.1883  0.0808  437 SER   A O   
2979 C  CB  . SER   A 417 ? 0.9841 1.2135 1.5015 -0.0283 0.1301  0.0618  437 SER   A CB  
2980 O  OG  . SER   A 417 ? 1.0285 1.2719 1.5664 -0.0202 0.1200  0.0633  437 SER   A OG  
2981 N  N   . GLY   A 418 ? 0.8989 1.0994 1.4502 -0.0269 0.2002  0.0917  438 GLY   A N   
2982 C  CA  . GLY   A 418 ? 0.8216 1.0131 1.4007 -0.0296 0.2274  0.1041  438 GLY   A CA  
2983 C  C   . GLY   A 418 ? 0.8994 1.0589 1.4251 -0.0209 0.2611  0.1163  438 GLY   A C   
2984 O  O   . GLY   A 418 ? 0.7192 0.8636 1.1945 -0.0131 0.2630  0.1142  438 GLY   A O   
2985 N  N   . PRO   A 419 ? 0.9600 1.1042 1.4928 -0.0215 0.2880  0.1293  439 PRO   A N   
2986 C  CA  . PRO   A 419 ? 1.0967 1.2062 1.5725 -0.0096 0.3214  0.1411  439 PRO   A CA  
2987 C  C   . PRO   A 419 ? 1.1032 1.1824 1.4918 -0.0080 0.3096  0.1319  439 PRO   A C   
2988 O  O   . PRO   A 419 ? 1.1568 1.2040 1.4886 0.0033  0.3297  0.1369  439 PRO   A O   
2989 C  CB  . PRO   A 419 ? 0.9462 1.0474 1.4512 -0.0121 0.3495  0.1585  439 PRO   A CB  
2990 C  CG  . PRO   A 419 ? 0.9802 1.1180 1.5789 -0.0254 0.3352  0.1577  439 PRO   A CG  
2991 C  CD  . PRO   A 419 ? 0.9494 1.1050 1.5450 -0.0322 0.2901  0.1354  439 PRO   A CD  
2992 N  N   . ARG   A 420 ? 1.0497 1.1383 1.4267 -0.0178 0.2775  0.1179  440 ARG   A N   
2993 C  CA  . ARG   A 420 ? 1.0617 1.1295 1.3685 -0.0178 0.2646  0.1096  440 ARG   A CA  
2994 C  C   . ARG   A 420 ? 0.9789 1.0592 1.2678 -0.0214 0.2404  0.0971  440 ARG   A C   
2995 O  O   . ARG   A 420 ? 1.1540 1.2308 1.4038 -0.0259 0.2231  0.0886  440 ARG   A O   
2996 C  CB  . ARG   A 420 ? 0.9453 1.0129 1.2492 -0.0239 0.2511  0.1058  440 ARG   A CB  
2997 C  CG  . ARG   A 420 ? 1.0839 1.1262 1.3192 -0.0204 0.2457  0.1025  440 ARG   A CG  
2998 C  CD  . ARG   A 420 ? 1.0117 1.0272 1.2305 -0.0149 0.2617  0.1139  440 ARG   A CD  
2999 N  NE  . ARG   A 420 ? 0.9335 0.9224 1.0827 -0.0083 0.2555  0.1112  440 ARG   A NE  
3000 C  CZ  . ARG   A 420 ? 1.0259 0.9861 1.1424 -0.0005 0.2640  0.1200  440 ARG   A CZ  
3001 N  NH1 . ARG   A 420 ? 1.2112 1.1628 1.3575 0.0004  0.2824  0.1342  440 ARG   A NH1 
3002 N  NH2 . ARG   A 420 ? 0.9939 0.9322 1.0472 0.0065  0.2526  0.1153  440 ARG   A NH2 
3003 N  N   . ASN   A 421 ? 0.9715 1.0668 1.2901 -0.0190 0.2395  0.0975  441 ASN   A N   
3004 C  CA  . ASN   A 421 ? 0.9694 1.0722 1.2690 -0.0218 0.2191  0.0892  441 ASN   A CA  
3005 C  C   . ASN   A 421 ? 1.0719 1.1407 1.3090 -0.0190 0.2253  0.0892  441 ASN   A C   
3006 O  O   . ASN   A 421 ? 1.0196 1.0588 1.2238 -0.0127 0.2434  0.0935  441 ASN   A O   
3007 C  CB  . ASN   A 421 ? 0.9404 1.0637 1.2853 -0.0171 0.2154  0.0911  441 ASN   A CB  
3008 C  CG  . ASN   A 421 ? 1.1284 1.2323 1.4696 -0.0044 0.2392  0.1000  441 ASN   A CG  
3009 O  OD1 . ASN   A 421 ? 1.0547 1.1364 1.3808 0.0025  0.2653  0.1073  441 ASN   A OD1 
3010 N  ND2 . ASN   A 421 ? 1.1893 1.2995 1.5406 0.0013  0.2310  0.0999  441 ASN   A ND2 
3011 N  N   . CYS   A 422 ? 0.9679 1.0380 1.1862 -0.0238 0.2090  0.0843  442 CYS   A N   
3012 C  CA  . CYS   A 422 ? 1.0833 1.1195 1.2476 -0.0245 0.2097  0.0827  442 CYS   A CA  
3013 C  C   . CYS   A 422 ? 1.1567 1.1601 1.3067 -0.0096 0.2331  0.0882  442 CYS   A C   
3014 O  O   . CYS   A 422 ? 1.1233 1.1314 1.2994 -0.0014 0.2390  0.0924  442 CYS   A O   
3015 C  CB  . CYS   A 422 ? 1.2397 1.2834 1.3966 -0.0333 0.1908  0.0802  442 CYS   A CB  
3016 S  SG  . CYS   A 422 ? 1.1977 1.1971 1.2961 -0.0391 0.1869  0.0777  442 CYS   A SG  
3017 N  N   . ILE   A 423 ? 1.1662 1.1353 1.2719 -0.0035 0.2463  0.0879  443 ILE   A N   
3018 C  CA  . ILE   A 423 ? 1.2810 1.2162 1.3658 0.0148  0.2726  0.0927  443 ILE   A CA  
3019 C  C   . ILE   A 423 ? 1.3779 1.2832 1.4321 0.0182  0.2664  0.0878  443 ILE   A C   
3020 O  O   . ILE   A 423 ? 1.6160 1.5027 1.6700 0.0356  0.2858  0.0916  443 ILE   A O   
3021 C  CB  . ILE   A 423 ? 1.2550 1.1563 1.2888 0.0232  0.2873  0.0933  443 ILE   A CB  
3022 C  CG1 . ILE   A 423 ? 1.5410 1.4150 1.5616 0.0462  0.3230  0.1015  443 ILE   A CG1 
3023 C  CG2 . ILE   A 423 ? 1.3272 1.1946 1.2963 0.0165  0.2659  0.0813  443 ILE   A CG2 
3024 C  CD1 . ILE   A 423 ? 1.4160 1.2502 1.3745 0.0586  0.3398  0.1034  443 ILE   A CD1 
3025 N  N   . GLY   A 424 ? 1.4096 1.3095 1.4408 0.0023  0.2405  0.0804  444 GLY   A N   
3026 C  CA  . GLY   A 424 ? 1.5027 1.3690 1.5054 0.0021  0.2326  0.0768  444 GLY   A CA  
3027 C  C   . GLY   A 424 ? 1.4067 1.2998 1.4459 -0.0061 0.2187  0.0814  444 GLY   A C   
3028 O  O   . GLY   A 424 ? 1.3358 1.2104 1.3541 -0.0169 0.2032  0.0798  444 GLY   A O   
3029 N  N   . MET   A 425 ? 1.4570 1.3919 1.5502 -0.0011 0.2231  0.0878  445 MET   A N   
3030 C  CA  . MET   A 425 ? 1.2447 1.2048 1.3677 -0.0052 0.2081  0.0922  445 MET   A CA  
3031 C  C   . MET   A 425 ? 1.3113 1.2390 1.4218 0.0068  0.2113  0.0962  445 MET   A C   
3032 O  O   . MET   A 425 ? 1.4662 1.3844 1.5634 -0.0015 0.1961  0.0990  445 MET   A O   
3033 C  CB  . MET   A 425 ? 1.1477 1.1551 1.3301 -0.0003 0.2087  0.0954  445 MET   A CB  
3034 C  CG  . MET   A 425 ? 1.1923 1.2199 1.4041 0.0044  0.1951  0.1001  445 MET   A CG  
3035 S  SD  . MET   A 425 ? 1.2999 1.3815 1.5822 0.0084  0.1877  0.0998  445 MET   A SD  
3036 C  CE  . MET   A 425 ? 1.2798 1.3589 1.5945 0.0211  0.2185  0.1037  445 MET   A CE  
3037 N  N   . ARG   A 426 ? 1.3534 1.2627 1.4676 0.0277  0.2328  0.0977  446 ARG   A N   
3038 C  CA  . ARG   A 426 ? 1.3748 1.2534 1.4806 0.0440  0.2369  0.1011  446 ARG   A CA  
3039 C  C   . ARG   A 426 ? 1.5475 1.3660 1.5897 0.0386  0.2307  0.0952  446 ARG   A C   
3040 O  O   . ARG   A 426 ? 1.6086 1.3995 1.6387 0.0424  0.2229  0.0986  446 ARG   A O   
3041 C  CB  . ARG   A 426 ? 1.3475 1.2269 1.4785 0.0704  0.2648  0.1044  446 ARG   A CB  
3042 C  CG  . ARG   A 426 ? 1.3795 1.3189 1.5838 0.0730  0.2693  0.1107  446 ARG   A CG  
3043 C  CD  . ARG   A 426 ? 1.5252 1.4710 1.7609 0.0956  0.3021  0.1162  446 ARG   A CD  
3044 N  NE  . ARG   A 426 ? 1.7593 1.7097 2.0289 0.1181  0.3076  0.1218  446 ARG   A NE  
3045 C  CZ  . ARG   A 426 ? 1.7968 1.7078 2.0387 0.1421  0.3284  0.1220  446 ARG   A CZ  
3046 N  NH1 . ARG   A 426 ? 1.8208 1.6813 1.9959 0.1470  0.3452  0.1157  446 ARG   A NH1 
3047 N  NH2 . ARG   A 426 ? 1.7850 1.7059 2.0652 0.1640  0.3311  0.1276  446 ARG   A NH2 
3048 N  N   . PHE   A 427 ? 1.5639 1.3589 1.5651 0.0297  0.2315  0.0863  447 PHE   A N   
3049 C  CA  . PHE   A 427 ? 1.5627 1.3009 1.5071 0.0207  0.2193  0.0782  447 PHE   A CA  
3050 C  C   . PHE   A 427 ? 1.5337 1.2835 1.4824 -0.0069 0.1940  0.0817  447 PHE   A C   
3051 O  O   . PHE   A 427 ? 1.6039 1.3137 1.5292 -0.0133 0.1834  0.0826  447 PHE   A O   
3052 C  CB  . PHE   A 427 ? 1.5708 1.2826 1.4701 0.0201  0.2229  0.0667  447 PHE   A CB  
3053 C  CG  . PHE   A 427 ? 1.6518 1.3156 1.5011 0.0032  0.2009  0.0560  447 PHE   A CG  
3054 C  CD1 . PHE   A 427 ? 1.6858 1.2818 1.4874 0.0149  0.2009  0.0477  447 PHE   A CD1 
3055 C  CD2 . PHE   A 427 ? 1.7811 1.4676 1.6342 -0.0240 0.1790  0.0534  447 PHE   A CD2 
3056 C  CE1 . PHE   A 427 ? 1.9085 1.4579 1.6685 -0.0032 0.1768  0.0365  447 PHE   A CE1 
3057 C  CE2 . PHE   A 427 ? 1.7954 1.4423 1.6128 -0.0420 0.1566  0.0439  447 PHE   A CE2 
3058 C  CZ  . PHE   A 427 ? 1.9329 1.5100 1.7042 -0.0331 0.1540  0.0350  447 PHE   A CZ  
3059 N  N   . ALA   A 428 ? 1.5707 1.3732 1.5489 -0.0227 0.1857  0.0844  448 ALA   A N   
3060 C  CA  . ALA   A 428 ? 1.5327 1.3516 1.5156 -0.0475 0.1663  0.0890  448 ALA   A CA  
3061 C  C   . ALA   A 428 ? 1.3791 1.1993 1.3767 -0.0451 0.1624  0.1016  448 ALA   A C   
3062 O  O   . ALA   A 428 ? 1.4436 1.2430 1.4260 -0.0611 0.1514  0.1077  448 ALA   A O   
3063 C  CB  . ALA   A 428 ? 1.3271 1.2032 1.3380 -0.0587 0.1614  0.0885  448 ALA   A CB  
3064 N  N   . LEU   A 429 ? 1.3539 1.1980 1.3824 -0.0254 0.1704  0.1069  449 LEU   A N   
3065 C  CA  . LEU   A 429 ? 1.3745 1.2158 1.4124 -0.0179 0.1646  0.1189  449 LEU   A CA  
3066 C  C   . LEU   A 429 ? 1.6020 1.3788 1.6065 -0.0098 0.1667  0.1207  449 LEU   A C   
3067 O  O   . LEU   A 429 ? 1.6862 1.4408 1.6778 -0.0163 0.1572  0.1315  449 LEU   A O   
3068 C  CB  . LEU   A 429 ? 1.2866 1.1667 1.3686 0.0034  0.1692  0.1215  449 LEU   A CB  
3069 C  CG  . LEU   A 429 ? 1.3750 1.3147 1.4917 -0.0032 0.1620  0.1199  449 LEU   A CG  
3070 C  CD1 . LEU   A 429 ? 1.4163 1.3878 1.5818 0.0167  0.1667  0.1192  449 LEU   A CD1 
3071 C  CD2 . LEU   A 429 ? 1.2042 1.1609 1.3143 -0.0144 0.1456  0.1283  449 LEU   A CD2 
3072 N  N   . MET   A 430 ? 1.6129 1.3553 1.5997 0.0058  0.1801  0.1107  450 MET   A N   
3073 C  CA  A MET   A 430 ? 1.5505 1.2251 1.5007 0.0171  0.1820  0.1093  450 MET   A CA  
3074 C  CA  B MET   A 430 ? 1.5886 1.2632 1.5387 0.0171  0.1821  0.1092  450 MET   A CA  
3075 C  C   . MET   A 430 ? 1.6084 1.2372 1.5179 -0.0090 0.1671  0.1053  450 MET   A C   
3076 O  O   . MET   A 430 ? 1.7627 1.3448 1.6521 -0.0125 0.1590  0.1116  450 MET   A O   
3077 C  CB  A MET   A 430 ? 1.6181 1.2687 1.5558 0.0442  0.2030  0.0987  450 MET   A CB  
3078 C  CB  B MET   A 430 ? 1.6164 1.2671 1.5539 0.0440  0.2030  0.0986  450 MET   A CB  
3079 C  CG  A MET   A 430 ? 1.6686 1.2441 1.5633 0.0613  0.2063  0.0939  450 MET   A CG  
3080 C  CG  B MET   A 430 ? 1.6819 1.2525 1.5663 0.0549  0.2044  0.0902  450 MET   A CG  
3081 S  SD  A MET   A 430 ? 1.5961 1.1584 1.5092 0.0782  0.2008  0.1096  450 MET   A SD  
3082 S  SD  B MET   A 430 ? 1.6920 1.2430 1.5826 0.1010  0.2307  0.0898  450 MET   A SD  
3083 C  CE  A MET   A 430 ? 1.6943 1.3284 1.6746 0.1057  0.2177  0.1161  450 MET   A CE  
3084 C  CE  B MET   A 430 ? 1.7391 1.3337 1.6868 0.1083  0.2220  0.1090  450 MET   A CE  
3085 N  N   . ASN   A 431 ? 1.6003 1.2411 1.5002 -0.0279 0.1620  0.0954  451 ASN   A N   
3086 C  CA  . ASN   A 431 ? 1.6880 1.2907 1.5582 -0.0547 0.1446  0.0902  451 ASN   A CA  
3087 C  C   . ASN   A 431 ? 1.7095 1.3289 1.5985 -0.0798 0.1324  0.1069  451 ASN   A C   
3088 O  O   . ASN   A 431 ? 1.6134 1.1850 1.4829 -0.0963 0.1212  0.1102  451 ASN   A O   
3089 C  CB  . ASN   A 431 ? 1.6575 1.2794 1.5203 -0.0674 0.1394  0.0770  451 ASN   A CB  
3090 C  CG  . ASN   A 431 ? 1.7894 1.3699 1.6241 -0.0930 0.1181  0.0682  451 ASN   A CG  
3091 O  OD1 . ASN   A 431 ? 1.9572 1.4738 1.7625 -0.0944 0.1106  0.0650  451 ASN   A OD1 
3092 N  ND2 . ASN   A 431 ? 1.8014 1.4178 1.6479 -0.1135 0.1065  0.0636  451 ASN   A ND2 
3093 N  N   . MET   A 432 ? 1.6055 1.2898 1.5308 -0.0825 0.1350  0.1178  452 MET   A N   
3094 C  CA  . MET   A 432 ? 1.5463 1.2490 1.4844 -0.1030 0.1277  0.1355  452 MET   A CA  
3095 C  C   . MET   A 432 ? 1.5580 1.2242 1.4861 -0.0912 0.1287  0.1510  452 MET   A C   
3096 O  O   . MET   A 432 ? 1.6571 1.2952 1.5747 -0.1100 0.1225  0.1647  452 MET   A O   
3097 C  CB  . MET   A 432 ? 1.4513 1.2288 1.4222 -0.1042 0.1302  0.1404  452 MET   A CB  
3098 C  CG  . MET   A 432 ? 1.4786 1.2932 1.4606 -0.1200 0.1268  0.1293  452 MET   A CG  
3099 S  SD  . MET   A 432 ? 1.4513 1.3458 1.4671 -0.1202 0.1286  0.1347  452 MET   A SD  
3100 C  CE  . MET   A 432 ? 1.3817 1.2910 1.4131 -0.0878 0.1361  0.1298  452 MET   A CE  
3101 N  N   . LYS   A 433 ? 1.6681 1.3347 1.6024 -0.0600 0.1365  0.1505  453 LYS   A N   
3102 C  CA  . LYS   A 433 ? 1.7606 1.3958 1.6871 -0.0442 0.1353  0.1656  453 LYS   A CA  
3103 C  C   . LYS   A 433 ? 1.7984 1.3508 1.6885 -0.0457 0.1323  0.1641  453 LYS   A C   
3104 O  O   . LYS   A 433 ? 1.6905 1.2056 1.5664 -0.0497 0.1270  0.1809  453 LYS   A O   
3105 C  CB  . LYS   A 433 ? 1.6724 1.3330 1.6228 -0.0095 0.1423  0.1638  453 LYS   A CB  
3106 C  CG  . LYS   A 433 ? 1.5212 1.2534 1.5059 -0.0073 0.1388  0.1692  453 LYS   A CG  
3107 C  CD  . LYS   A 433 ? 1.5020 1.2638 1.5213 0.0233  0.1434  0.1642  453 LYS   A CD  
3108 C  CE  . LYS   A 433 ? 1.3584 1.1863 1.4108 0.0239  0.1349  0.1663  453 LYS   A CE  
3109 N  NZ  . LYS   A 433 ? 1.3767 1.2391 1.4743 0.0485  0.1378  0.1597  453 LYS   A NZ  
3110 N  N   . LEU   A 434 ? 1.7484 1.2665 1.6186 -0.0413 0.1352  0.1442  454 LEU   A N   
3111 C  CA  . LEU   A 434 ? 1.8616 1.2953 1.6920 -0.0448 0.1286  0.1385  454 LEU   A CA  
3112 C  C   . LEU   A 434 ? 1.8934 1.3073 1.7175 -0.0852 0.1136  0.1465  454 LEU   A C   
3113 O  O   . LEU   A 434 ? 1.9679 1.3142 1.7685 -0.0932 0.1054  0.1525  454 LEU   A O   
3114 C  CB  . LEU   A 434 ? 1.7977 1.2000 1.6009 -0.0310 0.1336  0.1134  454 LEU   A CB  
3115 C  CG  . LEU   A 434 ? 1.8291 1.2257 1.6304 0.0118  0.1523  0.1064  454 LEU   A CG  
3116 C  CD1 . LEU   A 434 ? 1.9548 1.3260 1.7235 0.0232  0.1603  0.0834  454 LEU   A CD1 
3117 C  CD2 . LEU   A 434 ? 1.6395 0.9750 1.4228 0.0337  0.1525  0.1137  454 LEU   A CD2 
3118 N  N   . ALA   A 435 ? 1.7426 1.2147 1.5910 -0.1110 0.1102  0.1474  455 ALA   A N   
3119 C  CA  . ALA   A 435 ? 1.6953 1.1614 1.5500 -0.1505 0.0985  0.1573  455 ALA   A CA  
3120 C  C   . ALA   A 435 ? 1.8111 1.2919 1.6793 -0.1590 0.1028  0.1871  455 ALA   A C   
3121 O  O   . ALA   A 435 ? 1.9231 1.3643 1.7862 -0.1839 0.0968  0.2017  455 ALA   A O   
3122 C  CB  . ALA   A 435 ? 1.7548 1.2811 1.6333 -0.1713 0.0944  0.1477  455 ALA   A CB  
3123 N  N   . LEU   A 436 ? 1.7022 1.2373 1.5863 -0.1387 0.1126  0.1969  456 LEU   A N   
3124 C  CA  . LEU   A 436 ? 1.7614 1.3090 1.6485 -0.1417 0.1165  0.2251  456 LEU   A CA  
3125 C  C   . LEU   A 436 ? 1.9018 1.3774 1.7614 -0.1269 0.1147  0.2388  456 LEU   A C   
3126 O  O   . LEU   A 436 ? 1.8488 1.3010 1.6993 -0.1411 0.1153  0.2642  456 LEU   A O   
3127 C  CB  . LEU   A 436 ? 1.8215 1.4399 1.7270 -0.1205 0.1224  0.2279  456 LEU   A CB  
3128 C  CG  . LEU   A 436 ? 1.7797 1.4706 1.7112 -0.1357 0.1249  0.2208  456 LEU   A CG  
3129 C  CD1 . LEU   A 436 ? 1.6274 1.3764 1.5725 -0.1124 0.1275  0.2219  456 LEU   A CD1 
3130 C  CD2 . LEU   A 436 ? 1.7459 1.4467 1.6831 -0.1698 0.1269  0.2383  456 LEU   A CD2 
3131 N  N   . ILE   A 437 ? 1.9696 1.4085 1.8154 -0.0968 0.1142  0.2237  457 ILE   A N   
3132 C  CA  . ILE   A 437 ? 2.0436 1.4112 1.8630 -0.0777 0.1120  0.2348  457 ILE   A CA  
3133 C  C   . ILE   A 437 ? 2.0494 1.3392 1.8457 -0.1060 0.1038  0.2388  457 ILE   A C   
3134 O  O   . ILE   A 437 ? 2.1516 1.3988 1.9341 -0.1140 0.1020  0.2634  457 ILE   A O   
3135 C  CB  . ILE   A 437 ? 2.0181 1.3685 1.8325 -0.0373 0.1160  0.2158  457 ILE   A CB  
3136 C  CG1 . ILE   A 437 ? 1.9117 1.3323 1.7559 -0.0089 0.1214  0.2184  457 ILE   A CG1 
3137 C  CG2 . ILE   A 437 ? 2.0257 1.2887 1.8086 -0.0190 0.1124  0.2217  457 ILE   A CG2 
3138 C  CD1 . ILE   A 437 ? 1.8266 1.2475 1.6803 0.0276  0.1294  0.2003  457 ILE   A CD1 
3139 N  N   . ARG   A 438 ? 2.0077 1.2755 1.7985 -0.1219 0.0972  0.2149  458 ARG   A N   
3140 C  CA  . ARG   A 438 ? 2.1622 1.3478 1.9310 -0.1469 0.0844  0.2130  458 ARG   A CA  
3141 C  C   . ARG   A 438 ? 2.2038 1.4012 1.9937 -0.1921 0.0810  0.2366  458 ARG   A C   
3142 O  O   . ARG   A 438 ? 2.2537 1.3810 2.0312 -0.2132 0.0728  0.2483  458 ARG   A O   
3143 C  CB  . ARG   A 438 ? 2.0474 1.2085 1.8013 -0.1501 0.0746  0.1789  458 ARG   A CB  
3144 C  CG  . ARG   A 438 ? 2.4440 1.4980 2.1552 -0.1433 0.0626  0.1650  458 ARG   A CG  
3145 C  CD  . ARG   A 438 ? 2.5102 1.5227 2.2000 -0.1015 0.0724  0.1736  458 ARG   A CD  
3146 N  NE  . ARG   A 438 ? 2.5931 1.4995 2.2379 -0.0890 0.0622  0.1578  458 ARG   A NE  
3147 C  CZ  . ARG   A 438 ? 2.5927 1.4386 2.2147 -0.0593 0.0655  0.1670  458 ARG   A CZ  
3148 N  NH1 . ARG   A 438 ? 2.4743 1.3546 2.1142 -0.0396 0.0764  0.1930  458 ARG   A NH1 
3149 N  NH2 . ARG   A 438 ? 2.7301 1.4761 2.3080 -0.0472 0.0554  0.1488  458 ARG   A NH2 
3150 N  N   . VAL   A 439 ? 2.2253 1.5089 2.0484 -0.2072 0.0885  0.2447  459 VAL   A N   
3151 C  CA  . VAL   A 439 ? 2.1288 1.4347 1.9775 -0.2485 0.0903  0.2685  459 VAL   A CA  
3152 C  C   . VAL   A 439 ? 2.1375 1.4449 1.9798 -0.2430 0.1037  0.3055  459 VAL   A C   
3153 O  O   . VAL   A 439 ? 2.1757 1.4446 2.0185 -0.2702 0.1052  0.3310  459 VAL   A O   
3154 C  CB  . VAL   A 439 ? 1.8924 1.2891 1.7779 -0.2645 0.0933  0.2594  459 VAL   A CB  
3155 C  CG1 . VAL   A 439 ? 1.8679 1.3032 1.7846 -0.2999 0.1022  0.2882  459 VAL   A CG1 
3156 C  CG2 . VAL   A 439 ? 1.7921 1.1762 1.6808 -0.2769 0.0764  0.2272  459 VAL   A CG2 
3157 N  N   . LEU   A 440 ? 2.1513 1.5013 1.9868 -0.2079 0.1126  0.3098  460 LEU   A N   
3158 C  CA  . LEU   A 440 ? 2.1118 1.4591 1.9313 -0.1964 0.1220  0.3434  460 LEU   A CA  
3159 C  C   . LEU   A 440 ? 2.2249 1.4800 2.0097 -0.1798 0.1166  0.3556  460 LEU   A C   
3160 O  O   . LEU   A 440 ? 2.2753 1.5103 2.0411 -0.1753 0.1228  0.3879  460 LEU   A O   
3161 C  CB  . LEU   A 440 ? 1.9109 1.3278 1.7330 -0.1624 0.1270  0.3405  460 LEU   A CB  
3162 C  CG  . LEU   A 440 ? 1.8048 1.3111 1.6554 -0.1764 0.1346  0.3364  460 LEU   A CG  
3163 C  CD1 . LEU   A 440 ? 1.6929 1.2573 1.5479 -0.1415 0.1335  0.3233  460 LEU   A CD1 
3164 C  CD2 . LEU   A 440 ? 1.8049 1.3287 1.6550 -0.2003 0.1480  0.3700  460 LEU   A CD2 
3165 N  N   . GLN   A 441 ? 2.2707 1.4669 2.0427 -0.1681 0.1056  0.3310  461 GLN   A N   
3166 C  CA  . GLN   A 441 ? 2.3771 1.4772 2.1157 -0.1537 0.0995  0.3405  461 GLN   A CA  
3167 C  C   . GLN   A 441 ? 2.5017 1.5360 2.2359 -0.1955 0.0961  0.3609  461 GLN   A C   
3168 O  O   . GLN   A 441 ? 2.5201 1.4777 2.2266 -0.1883 0.0941  0.3817  461 GLN   A O   
3169 C  CB  . GLN   A 441 ? 2.3746 1.4297 2.0979 -0.1270 0.0908  0.3061  461 GLN   A CB  
3170 C  CG  . GLN   A 441 ? 2.3469 1.3895 2.0541 -0.0746 0.0929  0.3053  461 GLN   A CG  
3171 C  CD  . GLN   A 441 ? 2.3793 1.3826 2.0728 -0.0471 0.0898  0.2720  461 GLN   A CD  
3172 O  OE1 . GLN   A 441 ? 2.3720 1.3388 2.0560 -0.0665 0.0833  0.2500  461 GLN   A OE1 
3173 N  NE2 . GLN   A 441 ? 2.3545 1.3662 2.0471 -0.0001 0.0945  0.2679  461 GLN   A NE2 
3174 N  N   . ASN   A 442 ? 2.5836 1.6462 2.3481 -0.2391 0.0946  0.3564  462 ASN   A N   
3175 C  CA  . ASN   A 442 ? 2.6119 1.6155 2.3846 -0.2841 0.0888  0.3722  462 ASN   A CA  
3176 C  C   . ASN   A 442 ? 2.5859 1.6454 2.3926 -0.3221 0.1044  0.4055  462 ASN   A C   
3177 O  O   . ASN   A 442 ? 2.6675 1.6763 2.4795 -0.3547 0.1065  0.4330  462 ASN   A O   
3178 C  CB  . ASN   A 442 ? 2.6273 1.6020 2.4108 -0.3070 0.0685  0.3362  462 ASN   A CB  
3179 C  CG  . ASN   A 442 ? 2.7352 1.6274 2.4765 -0.2742 0.0542  0.3072  462 ASN   A CG  
3180 O  OD1 . ASN   A 442 ? 2.8344 1.6301 2.5554 -0.2863 0.0403  0.3059  462 ASN   A OD1 
3181 N  ND2 . ASN   A 442 ? 2.7271 1.6559 2.4559 -0.2320 0.0587  0.2840  462 ASN   A ND2 
3182 N  N   . PHE   A 443 ? 2.2213 1.3816 2.0515 -0.3185 0.1167  0.4045  463 PHE   A N   
3183 C  CA  . PHE   A 443 ? 2.2545 1.4752 2.1200 -0.3532 0.1336  0.4320  463 PHE   A CA  
3184 C  C   . PHE   A 443 ? 2.3299 1.6227 2.1842 -0.3258 0.1535  0.4502  463 PHE   A C   
3185 O  O   . PHE   A 443 ? 2.3304 1.6522 2.1669 -0.2860 0.1498  0.4312  463 PHE   A O   
3186 C  CB  . PHE   A 443 ? 2.2344 1.5126 2.1492 -0.3847 0.1261  0.4080  463 PHE   A CB  
3187 C  CG  . PHE   A 443 ? 2.2795 1.4919 2.2025 -0.4089 0.1006  0.3828  463 PHE   A CG  
3188 C  CD1 . PHE   A 443 ? 2.3712 1.5358 2.3194 -0.4547 0.0952  0.4010  463 PHE   A CD1 
3189 C  CD2 . PHE   A 443 ? 2.2589 1.4560 2.1635 -0.3859 0.0818  0.3408  463 PHE   A CD2 
3190 C  CE1 . PHE   A 443 ? 2.4821 1.5819 2.4355 -0.4768 0.0667  0.3745  463 PHE   A CE1 
3191 C  CE2 . PHE   A 443 ? 2.3328 1.4649 2.2354 -0.4048 0.0564  0.3153  463 PHE   A CE2 
3192 C  CZ  . PHE   A 443 ? 2.5056 1.5878 2.4319 -0.4503 0.0465  0.3305  463 PHE   A CZ  
3193 N  N   . SER   A 444 ? 2.1816 1.5018 2.0468 -0.3478 0.1747  0.4875  464 SER   A N   
3194 C  CA  . SER   A 444 ? 2.1245 1.5232 1.9831 -0.3297 0.1947  0.5033  464 SER   A CA  
3195 C  C   . SER   A 444 ? 1.9910 1.4704 1.9018 -0.3626 0.2073  0.5030  464 SER   A C   
3196 O  O   . SER   A 444 ? 1.9572 1.4262 1.9104 -0.4043 0.2037  0.5030  464 SER   A O   
3197 C  CB  . SER   A 444 ? 2.1301 1.4957 1.9486 -0.3209 0.2132  0.5497  464 SER   A CB  
3198 O  OG  . SER   A 444 ? 2.1350 1.4358 1.9052 -0.2832 0.2000  0.5492  464 SER   A OG  
3199 N  N   . PHE   A 445 ? 2.0633 1.6233 1.9728 -0.3424 0.2203  0.5014  465 PHE   A N   
3200 C  CA  . PHE   A 445 ? 1.9539 1.5982 1.9123 -0.3643 0.2312  0.4953  465 PHE   A CA  
3201 C  C   . PHE   A 445 ? 2.0753 1.7722 2.0216 -0.3579 0.2621  0.5287  465 PHE   A C   
3202 O  O   . PHE   A 445 ? 2.0582 1.7681 1.9584 -0.3191 0.2659  0.5312  465 PHE   A O   
3203 C  CB  . PHE   A 445 ? 1.7262 1.4207 1.6971 -0.3438 0.2144  0.4512  465 PHE   A CB  
3204 C  CG  . PHE   A 445 ? 1.8540 1.5079 1.8410 -0.3547 0.1881  0.4184  465 PHE   A CG  
3205 C  CD1 . PHE   A 445 ? 1.8827 1.4639 1.8338 -0.3332 0.1718  0.4058  465 PHE   A CD1 
3206 C  CD2 . PHE   A 445 ? 1.8560 1.5439 1.8917 -0.3838 0.1794  0.3999  465 PHE   A CD2 
3207 C  CE1 . PHE   A 445 ? 1.9041 1.4444 1.8615 -0.3396 0.1499  0.3752  465 PHE   A CE1 
3208 C  CE2 . PHE   A 445 ? 1.7568 1.4028 1.7976 -0.3910 0.1537  0.3690  465 PHE   A CE2 
3209 C  CZ  . PHE   A 445 ? 1.8131 1.3839 1.8118 -0.3685 0.1402  0.3565  465 PHE   A CZ  
3210 N  N   . LYS   A 446 ? 2.2392 1.9669 2.2278 -0.3952 0.2838  0.5541  466 LYS   A N   
3211 C  CA  . LYS   A 446 ? 2.2443 2.0261 2.2266 -0.3928 0.3191  0.5879  466 LYS   A CA  
3212 C  C   . LYS   A 446 ? 2.0354 1.9076 2.0764 -0.4086 0.3286  0.5708  466 LYS   A C   
3213 O  O   . LYS   A 446 ? 2.0392 1.9201 2.1379 -0.4389 0.3130  0.5505  466 LYS   A O   
3214 C  CB  . LYS   A 446 ? 2.1612 1.8926 2.1297 -0.4136 0.3381  0.6192  466 LYS   A CB  
3215 C  CG  . LYS   A 446 ? 2.2336 1.8663 2.1479 -0.4018 0.3272  0.6373  466 LYS   A CG  
3216 C  CD  . LYS   A 446 ? 2.3329 1.9625 2.1790 -0.3516 0.3284  0.6488  466 LYS   A CD  
3217 C  CE  . LYS   A 446 ? 2.2805 1.8131 2.0719 -0.3371 0.3197  0.6704  466 LYS   A CE  
3218 N  NZ  . LYS   A 446 ? 2.4230 1.9187 2.1957 -0.3595 0.3397  0.7012  466 LYS   A NZ  
3219 N  N   . PRO   A 447 ? 2.0836 2.0215 2.1088 -0.3858 0.3517  0.5761  467 PRO   A N   
3220 C  CA  . PRO   A 447 ? 2.0448 2.0669 2.1256 -0.3974 0.3630  0.5606  467 PRO   A CA  
3221 C  C   . PRO   A 447 ? 2.1525 2.1778 2.2814 -0.4358 0.3799  0.5738  467 PRO   A C   
3222 O  O   . PRO   A 447 ? 2.1329 2.1043 2.2398 -0.4489 0.3923  0.6003  467 PRO   A O   
3223 C  CB  . PRO   A 447 ? 1.9872 2.0612 2.0233 -0.3586 0.3855  0.5669  467 PRO   A CB  
3224 C  CG  . PRO   A 447 ? 1.8998 1.9259 1.8647 -0.3242 0.3745  0.5751  467 PRO   A CG  
3225 C  CD  . PRO   A 447 ? 2.0021 1.9398 1.9552 -0.3432 0.3641  0.5922  467 PRO   A CD  
3226 N  N   . CYS   A 448 ? 2.1515 2.2417 2.3486 -0.4537 0.3793  0.5552  468 CYS   A N   
3227 C  CA  . CYS   A 448 ? 2.1060 2.2154 2.3632 -0.4903 0.3940  0.5646  468 CYS   A CA  
3228 C  C   . CYS   A 448 ? 2.0962 2.2883 2.3688 -0.4779 0.4270  0.5712  468 CYS   A C   
3229 O  O   . CYS   A 448 ? 2.0505 2.2817 2.2860 -0.4409 0.4360  0.5652  468 CYS   A O   
3230 C  CB  . CYS   A 448 ? 2.0151 2.1306 2.3452 -0.5226 0.3631  0.5379  468 CYS   A CB  
3231 S  SG  . CYS   A 448 ? 2.1538 2.1616 2.4792 -0.5515 0.3311  0.5361  468 CYS   A SG  
3232 N  N   . LYS   A 449 ? 2.2261 2.4435 2.5551 -0.5092 0.4449  0.5832  469 LYS   A N   
3233 C  CA  . LYS   A 449 ? 2.1957 2.4941 2.5498 -0.5001 0.4770  0.5889  469 LYS   A CA  
3234 C  C   . LYS   A 449 ? 2.1264 2.4983 2.5232 -0.4853 0.4627  0.5561  469 LYS   A C   
3235 O  O   . LYS   A 449 ? 2.1385 2.5688 2.5228 -0.4562 0.4840  0.5539  469 LYS   A O   
3236 C  CB  . LYS   A 449 ? 2.0201 2.3305 2.4358 -0.5408 0.4969  0.6088  469 LYS   A CB  
3237 C  CG  . LYS   A 449 ? 2.0822 2.4835 2.5820 -0.5512 0.5048  0.5955  469 LYS   A CG  
3238 C  CD  . LYS   A 449 ? 2.2396 2.6448 2.8131 -0.5990 0.5132  0.6110  469 LYS   A CD  
3239 C  CE  . LYS   A 449 ? 2.2049 2.6992 2.8720 -0.6112 0.5115  0.5935  469 LYS   A CE  
3240 N  NZ  . LYS   A 449 ? 2.2288 2.7264 2.9766 -0.6611 0.5114  0.6045  469 LYS   A NZ  
3241 N  N   . GLU   A 450 ? 2.0259 2.3918 2.4680 -0.5032 0.4259  0.5301  470 GLU   A N   
3242 C  CA  . GLU   A 450 ? 2.0653 2.4948 2.5477 -0.4912 0.4080  0.4990  470 GLU   A CA  
3243 C  C   . GLU   A 450 ? 2.0680 2.4837 2.4969 -0.4581 0.3872  0.4793  470 GLU   A C   
3244 O  O   . GLU   A 450 ? 2.0266 2.4878 2.4815 -0.4468 0.3701  0.4530  470 GLU   A O   
3245 C  CB  . GLU   A 450 ? 2.1406 2.5755 2.7025 -0.5290 0.3772  0.4811  470 GLU   A CB  
3246 C  CG  . GLU   A 450 ? 2.0919 2.4402 2.6421 -0.5549 0.3482  0.4802  470 GLU   A CG  
3247 C  CD  . GLU   A 450 ? 2.1840 2.5349 2.8110 -0.5940 0.3183  0.4638  470 GLU   A CD  
3248 O  OE1 . GLU   A 450 ? 2.3798 2.8037 3.0693 -0.5979 0.3147  0.4499  470 GLU   A OE1 
3249 O  OE2 . GLU   A 450 ? 2.1214 2.3996 2.7448 -0.6195 0.2965  0.4640  470 GLU   A OE2 
3250 N  N   . THR   A 451 ? 2.0632 2.4180 2.4196 -0.4422 0.3879  0.4918  471 THR   A N   
3251 C  CA  . THR   A 451 ? 2.0171 2.3618 2.3242 -0.4108 0.3701  0.4752  471 THR   A CA  
3252 C  C   . THR   A 451 ? 1.8849 2.2929 2.1688 -0.3724 0.3889  0.4684  471 THR   A C   
3253 O  O   . THR   A 451 ? 1.9770 2.4004 2.2328 -0.3577 0.4203  0.4878  471 THR   A O   
3254 C  CB  . THR   A 451 ? 1.9728 2.2395 2.2110 -0.4014 0.3672  0.4930  471 THR   A CB  
3255 O  OG1 . THR   A 451 ? 1.9332 2.1353 2.1906 -0.4337 0.3446  0.4934  471 THR   A OG1 
3256 C  CG2 . THR   A 451 ? 1.7647 2.0297 1.9531 -0.3659 0.3529  0.4787  471 THR   A CG2 
3257 N  N   . GLN   A 452 ? 1.7084 2.1497 2.0008 -0.3558 0.3692  0.4403  472 GLN   A N   
3258 C  CA  . GLN   A 452 ? 1.8076 2.3072 2.0819 -0.3193 0.3824  0.4285  472 GLN   A CA  
3259 C  C   . GLN   A 452 ? 1.7641 2.2355 1.9555 -0.2842 0.3871  0.4353  472 GLN   A C   
3260 O  O   . GLN   A 452 ? 1.7500 2.1837 1.9116 -0.2712 0.3592  0.4144  472 GLN   A O   
3261 C  CB  . GLN   A 452 ? 1.7737 2.3145 2.0877 -0.3156 0.3579  0.3961  472 GLN   A CB  
3262 C  CG  . GLN   A 452 ? 1.4981 2.1015 1.8054 -0.2806 0.3708  0.3814  472 GLN   A CG  
3263 C  CD  . GLN   A 452 ? 1.6181 2.2587 1.9667 -0.2784 0.3460  0.3507  472 GLN   A CD  
3264 O  OE1 . GLN   A 452 ? 1.6768 2.2744 2.0147 -0.2805 0.3133  0.3276  472 GLN   A OE1 
3265 N  NE2 . GLN   A 452 ? 1.5744 2.2763 1.9604 -0.2671 0.3566  0.3411  472 GLN   A NE2 
3266 N  N   . ILE   A 453 ? 1.7656 2.2433 1.9137 -0.2638 0.4166  0.4545  473 ILE   A N   
3267 C  CA  . ILE   A 453 ? 1.6985 2.1514 1.7631 -0.2271 0.4205  0.4617  473 ILE   A CA  
3268 C  C   . ILE   A 453 ? 1.7683 2.2707 1.8043 -0.1929 0.4444  0.4575  473 ILE   A C   
3269 O  O   . ILE   A 453 ? 1.8454 2.3656 1.8893 -0.1979 0.4733  0.4742  473 ILE   A O   
3270 C  CB  . ILE   A 453 ? 1.7762 2.1632 1.7940 -0.2337 0.4295  0.4941  473 ILE   A CB  
3271 C  CG1 . ILE   A 453 ? 1.8643 2.1949 1.9061 -0.2644 0.4046  0.4966  473 ILE   A CG1 
3272 C  CG2 . ILE   A 453 ? 1.7363 2.1017 1.6645 -0.1909 0.4312  0.5009  473 ILE   A CG2 
3273 C  CD1 . ILE   A 453 ? 1.9849 2.2448 1.9848 -0.2721 0.4116  0.5281  473 ILE   A CD1 
3274 N  N   . PRO   A 454 ? 1.7506 2.2754 1.7521 -0.1571 0.4338  0.4348  474 PRO   A N   
3275 C  CA  . PRO   A 454 ? 1.6349 2.1248 1.6236 -0.1449 0.3905  0.3972  474 PRO   A CA  
3276 C  C   . PRO   A 454 ? 1.7119 2.2241 1.7728 -0.1672 0.3695  0.3712  474 PRO   A C   
3277 O  O   . PRO   A 454 ? 1.6940 2.2637 1.8085 -0.1786 0.3848  0.3725  474 PRO   A O   
3278 C  CB  . PRO   A 454 ? 1.5413 2.0457 1.4721 -0.0983 0.3871  0.3756  474 PRO   A CB  
3279 C  CG  . PRO   A 454 ? 1.6981 2.2682 1.6432 -0.0905 0.4246  0.3879  474 PRO   A CG  
3280 C  CD  . PRO   A 454 ? 1.7846 2.3501 1.7523 -0.1210 0.4545  0.4274  474 PRO   A CD  
3281 N  N   . LEU   A 455 ? 1.5798 2.0481 1.6427 -0.1718 0.3349  0.3482  475 LEU   A N   
3282 C  CA  . LEU   A 455 ? 1.5386 2.0186 1.6598 -0.1920 0.3140  0.3252  475 LEU   A CA  
3283 C  C   . LEU   A 455 ? 1.5791 2.1064 1.7119 -0.1682 0.3077  0.2960  475 LEU   A C   
3284 O  O   . LEU   A 455 ? 1.7077 2.2211 1.8016 -0.1385 0.2927  0.2739  475 LEU   A O   
3285 C  CB  . LEU   A 455 ? 1.4939 1.9108 1.6044 -0.1981 0.2830  0.3098  475 LEU   A CB  
3286 C  CG  . LEU   A 455 ? 1.5371 1.9544 1.6938 -0.2154 0.2596  0.2854  475 LEU   A CG  
3287 C  CD1 . LEU   A 455 ? 1.6015 1.9628 1.7674 -0.2437 0.2468  0.2928  475 LEU   A CD1 
3288 C  CD2 . LEU   A 455 ? 1.2885 1.6999 1.4284 -0.1886 0.2374  0.2521  475 LEU   A CD2 
3289 N  N   . LYS   A 456 ? 1.5019 2.0845 1.6912 -0.1815 0.3178  0.2959  476 LYS   A N   
3290 C  CA  . LYS   A 456 ? 1.5328 2.1577 1.7391 -0.1603 0.3099  0.2682  476 LYS   A CA  
3291 C  C   . LYS   A 456 ? 1.5858 2.1845 1.8117 -0.1677 0.2752  0.2402  476 LYS   A C   
3292 O  O   . LYS   A 456 ? 1.5475 2.1354 1.8121 -0.1978 0.2639  0.2432  476 LYS   A O   
3293 C  CB  . LYS   A 456 ? 1.5613 2.2585 1.8244 -0.1691 0.3336  0.2798  476 LYS   A CB  
3294 C  CG  . LYS   A 456 ? 1.5112 2.2490 1.7490 -0.1454 0.3710  0.2976  476 LYS   A CG  
3295 C  CD  . LYS   A 456 ? 1.5574 2.3669 1.8539 -0.1434 0.3880  0.2963  476 LYS   A CD  
3296 C  CE  . LYS   A 456 ? 1.7425 2.5619 2.0774 -0.1691 0.4118  0.3222  476 LYS   A CE  
3297 N  NZ  . LYS   A 456 ? 1.8571 2.6824 2.1448 -0.1454 0.4474  0.3392  476 LYS   A NZ  
3298 N  N   . LEU   A 457 ? 1.5720 2.1579 1.7696 -0.1400 0.2580  0.2134  477 LEU   A N   
3299 C  CA  . LEU   A 457 ? 1.5709 2.1365 1.7853 -0.1432 0.2299  0.1884  477 LEU   A CA  
3300 C  C   . LEU   A 457 ? 1.6416 2.2564 1.9079 -0.1489 0.2277  0.1797  477 LEU   A C   
3301 O  O   . LEU   A 457 ? 1.7193 2.3886 2.0044 -0.1392 0.2466  0.1853  477 LEU   A O   
3302 C  CB  . LEU   A 457 ? 1.4613 2.0031 1.6382 -0.1133 0.2145  0.1648  477 LEU   A CB  
3303 C  CG  . LEU   A 457 ? 1.3434 1.8277 1.4843 -0.1111 0.2020  0.1646  477 LEU   A CG  
3304 C  CD1 . LEU   A 457 ? 1.4229 1.8942 1.5399 -0.0832 0.1864  0.1410  477 LEU   A CD1 
3305 C  CD2 . LEU   A 457 ? 1.3962 1.8434 1.5555 -0.1355 0.1883  0.1644  477 LEU   A CD2 
3306 N  N   . SER   A 458 ? 1.7785 2.3737 2.0663 -0.1626 0.2044  0.1660  478 SER   A N   
3307 C  CA  . SER   A 458 ? 1.7699 2.4067 2.1035 -0.1652 0.1958  0.1554  478 SER   A CA  
3308 C  C   . SER   A 458 ? 1.8353 2.4956 2.1580 -0.1311 0.1949  0.1359  478 SER   A C   
3309 O  O   . SER   A 458 ? 1.7852 2.4090 2.0785 -0.1153 0.1793  0.1177  478 SER   A O   
3310 C  CB  . SER   A 458 ? 1.6655 2.2665 2.0102 -0.1827 0.1684  0.1436  478 SER   A CB  
3311 O  OG  . SER   A 458 ? 1.7599 2.3983 2.1434 -0.1812 0.1559  0.1321  478 SER   A OG  
3312 N  N   . LEU   A 459 ? 2.3067 3.0274 2.6554 -0.1196 0.2123  0.1401  479 LEU   A N   
3313 C  CA  . LEU   A 459 ? 2.3116 3.0543 2.6489 -0.0848 0.2130  0.1215  479 LEU   A CA  
3314 C  C   . LEU   A 459 ? 2.2894 3.0277 2.6473 -0.0804 0.1874  0.1012  479 LEU   A C   
3315 O  O   . LEU   A 459 ? 2.3005 3.0523 2.6541 -0.0527 0.1839  0.0845  479 LEU   A O   
3316 C  CB  . LEU   A 459 ? 2.3314 3.1415 2.6923 -0.0717 0.2415  0.1326  479 LEU   A CB  
3317 C  CG  . LEU   A 459 ? 2.4429 3.2578 2.7593 -0.0522 0.2687  0.1432  479 LEU   A CG  
3318 C  CD1 . LEU   A 459 ? 2.3430 3.1263 2.6373 -0.0753 0.2787  0.1672  479 LEU   A CD1 
3319 C  CD2 . LEU   A 459 ? 2.3540 3.2405 2.6988 -0.0367 0.2991  0.1531  479 LEU   A CD2 
3320 N  N   . GLY   A 460 ? 2.0969 2.8114 2.4723 -0.1059 0.1690  0.1024  480 GLY   A N   
3321 C  CA  . GLY   A 460 ? 1.7818 2.4883 2.1716 -0.1032 0.1442  0.0863  480 GLY   A CA  
3322 C  C   . GLY   A 460 ? 1.8578 2.5036 2.2046 -0.0914 0.1284  0.0706  480 GLY   A C   
3323 O  O   . GLY   A 460 ? 1.7967 2.4286 2.1140 -0.0694 0.1336  0.0622  480 GLY   A O   
3324 N  N   . GLY   A 461 ? 1.6186 2.2272 1.9619 -0.1058 0.1090  0.0666  481 GLY   A N   
3325 C  CA  . GLY   A 461 ? 1.6847 2.2412 1.9945 -0.0941 0.0961  0.0534  481 GLY   A CA  
3326 C  C   . GLY   A 461 ? 1.8727 2.3759 2.1495 -0.1029 0.0986  0.0571  481 GLY   A C   
3327 O  O   . GLY   A 461 ? 1.7666 2.2462 2.0201 -0.0878 0.1017  0.0510  481 GLY   A O   
3328 N  N   . LEU   A 462 ? 2.0195 2.5026 2.2964 -0.1267 0.0958  0.0664  482 LEU   A N   
3329 C  CA  . LEU   A 462 ? 1.9177 2.3484 2.1645 -0.1332 0.0976  0.0698  482 LEU   A CA  
3330 C  C   . LEU   A 462 ? 1.8205 2.2572 2.0651 -0.1427 0.1129  0.0852  482 LEU   A C   
3331 O  O   . LEU   A 462 ? 1.8670 2.3434 2.1352 -0.1526 0.1222  0.0966  482 LEU   A O   
3332 C  CB  . LEU   A 462 ? 2.0148 2.4058 2.2525 -0.1493 0.0832  0.0679  482 LEU   A CB  
3333 C  CG  . LEU   A 462 ? 2.1456 2.5517 2.4089 -0.1742 0.0738  0.0740  482 LEU   A CG  
3334 C  CD1 . LEU   A 462 ? 2.1414 2.4892 2.3793 -0.1885 0.0622  0.0722  482 LEU   A CD1 
3335 C  CD2 . LEU   A 462 ? 2.0563 2.5012 2.3482 -0.1709 0.0592  0.0661  482 LEU   A CD2 
3336 N  N   . LEU   A 463 ? 1.6786 2.0759 1.8957 -0.1387 0.1163  0.0872  483 LEU   A N   
3337 C  CA  . LEU   A 463 ? 1.6306 2.0269 1.8366 -0.1418 0.1293  0.1019  483 LEU   A CA  
3338 C  C   . LEU   A 463 ? 1.7139 2.0936 1.9261 -0.1684 0.1305  0.1168  483 LEU   A C   
3339 O  O   . LEU   A 463 ? 1.6154 1.9467 1.8106 -0.1758 0.1245  0.1172  483 LEU   A O   
3340 C  CB  . LEU   A 463 ? 1.2975 1.6588 1.4768 -0.1269 0.1285  0.0981  483 LEU   A CB  
3341 C  CG  . LEU   A 463 ? 1.2183 1.5886 1.3811 -0.1185 0.1389  0.1090  483 LEU   A CG  
3342 C  CD1 . LEU   A 463 ? 1.3144 1.7307 1.4808 -0.1025 0.1453  0.1043  483 LEU   A CD1 
3343 C  CD2 . LEU   A 463 ? 1.2927 1.6289 1.4355 -0.1050 0.1331  0.1050  483 LEU   A CD2 
3344 N  N   . GLN   A 464 ? 1.5946 2.0142 1.8336 -0.1826 0.1392  0.1294  484 GLN   A N   
3345 C  CA  . GLN   A 464 ? 1.6217 2.0300 1.8748 -0.2113 0.1413  0.1461  484 GLN   A CA  
3346 C  C   . GLN   A 464 ? 1.5827 2.0333 1.8508 -0.2163 0.1639  0.1676  484 GLN   A C   
3347 O  O   . GLN   A 464 ? 1.6152 2.1069 1.8827 -0.1960 0.1759  0.1659  484 GLN   A O   
3348 C  CB  . GLN   A 464 ? 1.7339 2.1483 2.0185 -0.2306 0.1236  0.1385  484 GLN   A CB  
3349 C  CG  . GLN   A 464 ? 1.8554 2.2164 2.1150 -0.2281 0.1030  0.1210  484 GLN   A CG  
3350 C  CD  . GLN   A 464 ? 1.9158 2.2798 2.1993 -0.2453 0.0815  0.1123  484 GLN   A CD  
3351 O  OE1 . GLN   A 464 ? 1.8646 2.2817 2.1916 -0.2546 0.0796  0.1156  484 GLN   A OE1 
3352 N  NE2 . GLN   A 464 ? 1.9556 2.2633 2.2105 -0.2478 0.0644  0.1006  484 GLN   A NE2 
3353 N  N   . PRO   A 465 ? 1.6670 2.1055 1.9452 -0.2415 0.1718  0.1887  485 PRO   A N   
3354 C  CA  . PRO   A 465 ? 1.6661 2.1493 1.9638 -0.2485 0.1974  0.2129  485 PRO   A CA  
3355 C  C   . PRO   A 465 ? 1.6098 2.1531 1.9687 -0.2647 0.1989  0.2150  485 PRO   A C   
3356 O  O   . PRO   A 465 ? 1.5701 2.1085 1.9586 -0.2820 0.1767  0.2035  485 PRO   A O   
3357 C  CB  . PRO   A 465 ? 1.4822 1.9200 1.7682 -0.2713 0.2037  0.2361  485 PRO   A CB  
3358 C  CG  . PRO   A 465 ? 1.3710 1.7398 1.6213 -0.2668 0.1828  0.2213  485 PRO   A CG  
3359 C  CD  . PRO   A 465 ? 1.4446 1.8194 1.7062 -0.2596 0.1616  0.1936  485 PRO   A CD  
3360 N  N   . GLU   A 466 ? 1.5428 2.1446 1.9198 -0.2567 0.2251  0.2294  486 GLU   A N   
3361 C  CA  . GLU   A 466 ? 1.5352 2.2038 1.9796 -0.2718 0.2318  0.2362  486 GLU   A CA  
3362 C  C   . GLU   A 466 ? 1.5422 2.1997 2.0302 -0.3148 0.2276  0.2546  486 GLU   A C   
3363 O  O   . GLU   A 466 ? 1.5707 2.2271 2.0966 -0.3343 0.2008  0.2420  486 GLU   A O   
3364 C  CB  . GLU   A 466 ? 1.6008 2.3309 2.0519 -0.2536 0.2675  0.2525  486 GLU   A CB  
3365 C  CG  . GLU   A 466 ? 1.6491 2.4029 2.0736 -0.2123 0.2682  0.2303  486 GLU   A CG  
3366 C  CD  . GLU   A 466 ? 1.7611 2.5784 2.1945 -0.1931 0.3038  0.2445  486 GLU   A CD  
3367 O  OE1 . GLU   A 466 ? 1.7002 2.5418 2.1623 -0.2120 0.3290  0.2718  486 GLU   A OE1 
3368 O  OE2 . GLU   A 466 ? 1.9171 2.7521 2.3256 -0.1574 0.3061  0.2266  486 GLU   A OE2 
3369 N  N   . LYS   A 467 ? 1.4991 2.1447 1.9798 -0.3294 0.2522  0.2844  487 LYS   A N   
3370 C  CA  . LYS   A 467 ? 1.5903 2.2099 2.1060 -0.3717 0.2468  0.3025  487 LYS   A CA  
3371 C  C   . LYS   A 467 ? 1.5256 2.0544 1.9906 -0.3765 0.2225  0.2918  487 LYS   A C   
3372 O  O   . LYS   A 467 ? 1.3569 1.8462 1.7584 -0.3507 0.2265  0.2881  487 LYS   A O   
3373 C  CB  . LYS   A 467 ? 1.5350 2.1622 2.0550 -0.3805 0.2830  0.3353  487 LYS   A CB  
3374 C  CG  . LYS   A 467 ? 1.4264 2.1246 1.9812 -0.3658 0.3097  0.3386  487 LYS   A CG  
3375 C  CD  . LYS   A 467 ? 1.4942 2.1858 2.0295 -0.3659 0.3478  0.3678  487 LYS   A CD  
3376 C  CE  . LYS   A 467 ? 1.6384 2.3078 2.2195 -0.4083 0.3490  0.3853  487 LYS   A CE  
3377 N  NZ  . LYS   A 467 ? 1.6291 2.3612 2.2940 -0.4246 0.3508  0.3809  487 LYS   A NZ  
3378 N  N   . PRO   A 468 ? 1.4938 1.9885 1.9856 -0.4071 0.1957  0.2851  488 PRO   A N   
3379 C  CA  . PRO   A 468 ? 1.4893 1.8948 1.9317 -0.4105 0.1758  0.2763  488 PRO   A CA  
3380 C  C   . PRO   A 468 ? 1.4996 1.8634 1.9062 -0.4131 0.1988  0.3047  488 PRO   A C   
3381 O  O   . PRO   A 468 ? 1.5107 1.9035 1.9439 -0.4291 0.2259  0.3358  488 PRO   A O   
3382 C  CB  . PRO   A 468 ? 1.5261 1.9114 2.0128 -0.4473 0.1463  0.2684  488 PRO   A CB  
3383 C  CG  . PRO   A 468 ? 1.4002 1.8640 1.9489 -0.4506 0.1392  0.2589  488 PRO   A CG  
3384 C  CD  . PRO   A 468 ? 1.4229 1.9588 1.9899 -0.4359 0.1781  0.2804  488 PRO   A CD  
3385 N  N   . VAL   A 469 ? 1.5264 1.8219 1.8722 -0.3955 0.1890  0.2951  489 VAL   A N   
3386 C  CA  . VAL   A 469 ? 1.7155 1.9664 2.0181 -0.3901 0.2069  0.3195  489 VAL   A CA  
3387 C  C   . VAL   A 469 ? 1.8467 2.0452 2.1672 -0.4280 0.2018  0.3380  489 VAL   A C   
3388 O  O   . VAL   A 469 ? 1.8455 1.9866 2.1587 -0.4387 0.1746  0.3202  489 VAL   A O   
3389 C  CB  . VAL   A 469 ? 1.5518 1.7537 1.7912 -0.3560 0.1966  0.3020  489 VAL   A CB  
3390 C  CG1 . VAL   A 469 ? 1.5910 1.7462 1.7870 -0.3489 0.2114  0.3276  489 VAL   A CG1 
3391 C  CG2 . VAL   A 469 ? 1.4397 1.6907 1.6665 -0.3218 0.1997  0.2838  489 VAL   A CG2 
3392 N  N   . VAL   A 470 ? 1.7121 1.9270 2.0537 -0.4475 0.2289  0.3743  490 VAL   A N   
3393 C  CA  . VAL   A 470 ? 1.7759 1.9407 2.1383 -0.4861 0.2279  0.3975  490 VAL   A CA  
3394 C  C   . VAL   A 470 ? 1.9154 2.0387 2.2281 -0.4760 0.2534  0.4310  490 VAL   A C   
3395 O  O   . VAL   A 470 ? 1.9045 2.0697 2.1981 -0.4553 0.2832  0.4498  490 VAL   A O   
3396 C  CB  . VAL   A 470 ? 1.8049 2.0219 2.2444 -0.5187 0.2361  0.4063  490 VAL   A CB  
3397 C  CG1 . VAL   A 470 ? 1.7825 2.0198 2.2724 -0.5373 0.2008  0.3768  490 VAL   A CG1 
3398 C  CG2 . VAL   A 470 ? 1.7985 2.0951 2.2488 -0.4976 0.2712  0.4170  490 VAL   A CG2 
3399 N  N   . LEU   A 471 ? 2.0175 2.0543 2.3038 -0.4878 0.2404  0.4369  491 LEU   A N   
3400 C  CA  . LEU   A 471 ? 2.0272 2.0123 2.2624 -0.4774 0.2596  0.4685  491 LEU   A CA  
3401 C  C   . LEU   A 471 ? 1.9897 1.8983 2.2359 -0.5114 0.2516  0.4824  491 LEU   A C   
3402 O  O   . LEU   A 471 ? 1.9739 1.8579 2.2560 -0.5385 0.2245  0.4625  491 LEU   A O   
3403 C  CB  . LEU   A 471 ? 1.9229 1.8668 2.0862 -0.4323 0.2477  0.4496  491 LEU   A CB  
3404 C  CG  . LEU   A 471 ? 1.6980 1.7016 1.8398 -0.3924 0.2509  0.4290  491 LEU   A CG  
3405 C  CD1 . LEU   A 471 ? 1.7373 1.6934 1.8245 -0.3561 0.2324  0.4075  491 LEU   A CD1 
3406 C  CD2 . LEU   A 471 ? 1.8109 1.8643 1.9383 -0.3790 0.2848  0.4583  491 LEU   A CD2 
3407 N  N   . LYS   A 472 ? 2.0032 1.8695 2.2119 -0.5065 0.2735  0.5129  492 LYS   A N   
3408 C  CA  . LYS   A 472 ? 1.9876 1.7699 2.1944 -0.5323 0.2673  0.5250  492 LYS   A CA  
3409 C  C   . LYS   A 472 ? 1.9874 1.6815 2.1394 -0.5153 0.2443  0.5214  492 LYS   A C   
3410 O  O   . LYS   A 472 ? 1.8419 1.5344 1.9413 -0.4768 0.2478  0.5237  492 LYS   A O   
3411 C  CB  . LYS   A 472 ? 1.9325 1.7073 2.1229 -0.5368 0.3028  0.5613  492 LYS   A CB  
3412 C  CG  . LYS   A 472 ? 1.8894 1.6147 2.1152 -0.5782 0.3020  0.5705  492 LYS   A CG  
3413 C  CD  . LYS   A 472 ? 2.1734 1.8895 2.3775 -0.5837 0.3390  0.6090  492 LYS   A CD  
3414 C  CE  . LYS   A 472 ? 2.2616 1.8991 2.3816 -0.5571 0.3431  0.6322  492 LYS   A CE  
3415 N  NZ  . LYS   A 472 ? 1.8820 1.4974 1.9754 -0.5664 0.3753  0.6708  492 LYS   A NZ  
3416 N  N   . VAL   A 473 ? 2.0470 1.6669 2.2093 -0.5390 0.2194  0.5096  493 VAL   A N   
3417 C  CA  . VAL   A 473 ? 2.0313 1.5606 2.1423 -0.5216 0.1950  0.4984  493 VAL   A CA  
3418 C  C   . VAL   A 473 ? 2.1941 1.6336 2.2863 -0.5353 0.1996  0.5223  493 VAL   A C   
3419 O  O   . VAL   A 473 ? 2.1674 1.5963 2.3019 -0.5699 0.2018  0.5245  493 VAL   A O   
3420 C  CB  . VAL   A 473 ? 1.9635 1.4746 2.0874 -0.5253 0.1585  0.4502  493 VAL   A CB  
3421 C  CG1 . VAL   A 473 ? 1.8693 1.2957 1.9313 -0.4919 0.1396  0.4287  493 VAL   A CG1 
3422 C  CG2 . VAL   A 473 ? 1.9010 1.5052 2.0469 -0.5101 0.1568  0.4226  493 VAL   A CG2 
3423 N  N   . GLU   A 474 ? 2.2633 1.6394 2.2929 -0.5056 0.2006  0.5381  494 GLU   A N   
3424 C  CA  . GLU   A 474 ? 2.2334 1.5179 2.2348 -0.5096 0.2052  0.5593  494 GLU   A CA  
3425 C  C   . GLU   A 474 ? 2.3083 1.4992 2.2616 -0.4867 0.1764  0.5435  494 GLU   A C   
3426 O  O   . GLU   A 474 ? 2.1485 1.3589 2.0685 -0.4436 0.1691  0.5193  494 GLU   A O   
3427 C  CB  . GLU   A 474 ? 2.1777 1.4717 2.1395 -0.4914 0.2391  0.6002  494 GLU   A CB  
3428 C  CG  . GLU   A 474 ? 2.3155 1.6870 2.3134 -0.5147 0.2703  0.6167  494 GLU   A CG  
3429 C  CD  . GLU   A 474 ? 2.4924 1.8767 2.4361 -0.4917 0.3004  0.6531  494 GLU   A CD  
3430 O  OE1 . GLU   A 474 ? 2.4616 1.8339 2.3500 -0.4510 0.2958  0.6597  494 GLU   A OE1 
3431 O  OE2 . GLU   A 474 ? 2.3781 1.7848 2.3345 -0.5139 0.3272  0.6752  494 GLU   A OE2 
3432 N  N   . SER   A 475 ? 2.4999 1.6018 2.4507 -0.5009 0.1650  0.5413  495 SER   A N   
3433 C  CA  . SER   A 475 ? 2.5053 1.5114 2.4110 -0.4790 0.1371  0.5198  495 SER   A CA  
3434 C  C   . SER   A 475 ? 2.6219 1.5665 2.4702 -0.4444 0.1479  0.5493  495 SER   A C   
3435 O  O   . SER   A 475 ? 2.7225 1.6531 2.5739 -0.4524 0.1704  0.5845  495 SER   A O   
3436 C  CB  . SER   A 475 ? 2.5442 1.4855 2.4780 -0.5089 0.1148  0.4969  495 SER   A CB  
3437 O  OG  . SER   A 475 ? 2.6418 1.4906 2.5269 -0.4830 0.0890  0.4712  495 SER   A OG  
3438 N  N   . ARG   A 476 ? 2.5879 1.5051 2.3876 -0.3983 0.1351  0.5289  496 ARG   A N   
3439 C  CA  . ARG   A 476 ? 2.5725 1.4325 2.3170 -0.3590 0.1401  0.5524  496 ARG   A CA  
3440 C  C   . ARG   A 476 ? 2.5786 1.3205 2.3029 -0.3586 0.1224  0.5489  496 ARG   A C   
3441 O  O   . ARG   A 476 ? 2.6334 1.3404 2.3708 -0.3729 0.1310  0.5780  496 ARG   A O   
3442 C  CB  . ARG   A 476 ? 2.4082 1.3135 2.1261 -0.3021 0.1360  0.5275  496 ARG   A CB  
3443 C  CG  . ARG   A 476 ? 2.3076 1.3329 2.0528 -0.2982 0.1469  0.5161  496 ARG   A CG  
3444 C  CD  . ARG   A 476 ? 2.3054 1.3683 2.0302 -0.2449 0.1402  0.4911  496 ARG   A CD  
3445 N  NE  . ARG   A 476 ? 2.3240 1.3749 2.0082 -0.2087 0.1464  0.5195  496 ARG   A NE  
3446 C  CZ  . ARG   A 476 ? 2.3683 1.4378 2.0341 -0.1602 0.1379  0.5049  496 ARG   A CZ  
3447 N  NH1 . ARG   A 476 ? 2.2535 1.3529 1.9379 -0.1419 0.1270  0.4644  496 ARG   A NH1 
3448 N  NH2 . ARG   A 476 ? 2.2990 1.3569 1.9279 -0.1293 0.1401  0.5326  496 ARG   A NH2 
3449 C  CHA . HEM   B .   ? 1.1449 1.1905 1.2553 -0.0441 0.1791  0.0687  601 HEM   A CHA 
3450 C  CHB . HEM   B .   ? 1.1098 1.2096 1.2478 -0.0688 0.1441  0.0729  601 HEM   A CHB 
3451 C  CHC . HEM   B .   ? 1.1763 1.1259 1.1996 -0.0789 0.1492  0.0723  601 HEM   A CHC 
3452 C  CHD . HEM   B .   ? 1.2781 1.1777 1.2356 -0.0367 0.1846  0.0597  601 HEM   A CHD 
3453 C  C1A . HEM   B .   ? 1.1949 1.2684 1.3280 -0.0517 0.1665  0.0672  601 HEM   A C1A 
3454 C  C2A . HEM   B .   ? 1.1078 1.2188 1.2776 -0.0528 0.1572  0.0645  601 HEM   A C2A 
3455 C  C3A . HEM   B .   ? 0.9458 1.0722 1.1192 -0.0579 0.1475  0.0648  601 HEM   A C3A 
3456 C  C4A . HEM   B .   ? 0.8988 0.9974 1.0430 -0.0624 0.1504  0.0688  601 HEM   A C4A 
3457 C  CMA . HEM   B .   ? 1.0326 1.1945 1.2305 -0.0574 0.1349  0.0614  601 HEM   A CMA 
3458 C  CAA . HEM   B .   ? 0.9870 1.1118 1.1830 -0.0481 0.1577  0.0620  601 HEM   A CAA 
3459 C  CBA . HEM   B .   ? 0.9655 1.0961 1.2038 -0.0423 0.1656  0.0656  601 HEM   A CBA 
3460 C  CGA . HEM   B .   ? 1.0257 1.1663 1.2932 -0.0409 0.1635  0.0628  601 HEM   A CGA 
3461 O  O1A . HEM   B .   ? 0.9441 1.0954 1.2566 -0.0393 0.1643  0.0638  601 HEM   A O1A 
3462 O  O2A . HEM   B .   ? 1.0688 1.2058 1.3172 -0.0415 0.1593  0.0595  601 HEM   A O2A 
3463 C  C1B . HEM   B .   ? 1.0980 1.1653 1.2092 -0.0742 0.1453  0.0765  601 HEM   A C1B 
3464 C  C2B . HEM   B .   ? 1.1233 1.1867 1.2283 -0.0816 0.1398  0.0838  601 HEM   A C2B 
3465 C  C3B . HEM   B .   ? 1.2294 1.2505 1.3064 -0.0861 0.1414  0.0845  601 HEM   A C3B 
3466 C  C4B . HEM   B .   ? 1.1964 1.1943 1.2563 -0.0795 0.1477  0.0766  601 HEM   A C4B 
3467 C  CMB . HEM   B .   ? 1.1781 1.2760 1.3004 -0.0820 0.1331  0.0893  601 HEM   A CMB 
3468 C  CAB . HEM   B .   ? 1.2918 1.2846 1.3516 -0.0957 0.1372  0.0925  601 HEM   A CAB 
3469 C  CBB . HEM   B .   ? 1.1819 1.1907 1.2504 -0.1006 0.1336  0.1032  601 HEM   A CBB 
3470 C  C1C . HEM   B .   ? 1.2910 1.2139 1.2884 -0.0680 0.1571  0.0656  601 HEM   A C1C 
3471 C  C2C . HEM   B .   ? 1.5320 1.3979 1.4829 -0.0617 0.1595  0.0594  601 HEM   A C2C 
3472 C  C3C . HEM   B .   ? 1.4454 1.2974 1.3739 -0.0485 0.1695  0.0551  601 HEM   A C3C 
3473 C  C4C . HEM   B .   ? 1.3105 1.2100 1.2756 -0.0479 0.1736  0.0594  601 HEM   A C4C 
3474 C  CMC . HEM   B .   ? 1.4212 1.2434 1.3477 -0.0681 0.1517  0.0583  601 HEM   A CMC 
3475 C  CAC . HEM   B .   ? 1.3328 1.1227 1.2006 -0.0347 0.1751  0.0465  601 HEM   A CAC 
3476 C  CBC . HEM   B .   ? 1.5180 1.2917 1.3552 -0.0197 0.1863  0.0441  601 HEM   A CBC 
3477 C  C1D . HEM   B .   ? 1.2854 1.2236 1.2795 -0.0362 0.1883  0.0641  601 HEM   A C1D 
3478 C  C2D . HEM   B .   ? 1.2935 1.2263 1.2773 -0.0261 0.1991  0.0666  601 HEM   A C2D 
3479 C  C3D . HEM   B .   ? 1.1042 1.0765 1.1336 -0.0296 0.1978  0.0699  601 HEM   A C3D 
3480 C  C4D . HEM   B .   ? 1.1694 1.1746 1.2354 -0.0401 0.1859  0.0686  601 HEM   A C4D 
3481 C  CMD . HEM   B .   ? 1.3650 1.2495 1.2890 -0.0118 0.2097  0.0656  601 HEM   A CMD 
3482 C  CAD . HEM   B .   ? 1.0822 1.0584 1.1194 -0.0225 0.2072  0.0750  601 HEM   A CAD 
3483 C  CBD . HEM   B .   ? 1.2715 1.2542 1.3497 -0.0146 0.2316  0.0854  601 HEM   A CBD 
3484 C  CGD . HEM   B .   ? 1.2797 1.2489 1.3539 -0.0061 0.2490  0.0946  601 HEM   A CGD 
3485 O  O1D . HEM   B .   ? 1.0658 1.0228 1.1520 0.0039  0.2775  0.1062  601 HEM   A O1D 
3486 O  O2D . HEM   B .   ? 1.4132 1.3836 1.4734 -0.0083 0.2358  0.0919  601 HEM   A O2D 
3487 N  NA  . HEM   B .   ? 1.1336 1.1997 1.2533 -0.0581 0.1607  0.0683  601 HEM   A NA  
3488 N  NB  . HEM   B .   ? 1.1097 1.1373 1.1914 -0.0726 0.1513  0.0736  601 HEM   A NB  
3489 N  NC  . HEM   B .   ? 1.1756 1.1167 1.1817 -0.0596 0.1646  0.0640  601 HEM   A NC  
3490 N  ND  . HEM   B .   ? 1.1692 1.1528 1.2123 -0.0440 0.1816  0.0668  601 HEM   A ND  
3491 FE FE  . HEM   B .   ? 1.1243 1.1323 1.1898 -0.0595 0.1645  0.0680  601 HEM   A FE  
3492 C  C10 . A1A4U C .   ? 1.2208 1.3071 1.3120 -0.0897 0.1296  0.0610  602 A1A4U A C10 
3493 C  C11 . A1A4U C .   ? 1.2330 1.3366 1.3227 -0.1013 0.1148  0.0573  602 A1A4U A C11 
3494 C  C12 . A1A4U C .   ? 1.2653 1.3428 1.3267 -0.1013 0.1057  0.0508  602 A1A4U A C12 
3495 C  C13 . A1A4U C .   ? 1.7009 1.7798 1.7066 -0.0562 0.0608  0.0280  602 A1A4U A C13 
3496 C  C14 . A1A4U C .   ? 1.8103 1.8666 1.7810 -0.0542 0.0343  0.0198  602 A1A4U A C14 
3497 C  C15 . A1A4U C .   ? 1.7705 1.8065 1.7266 -0.0691 0.0208  0.0144  602 A1A4U A C15 
3498 C  C16 . A1A4U C .   ? 1.6778 1.7540 1.6795 -0.0913 0.0112  0.0136  602 A1A4U A C16 
3499 C  C17 . A1A4U C .   ? 1.6855 1.7374 1.6763 -0.1072 -0.0024 0.0094  602 A1A4U A C17 
3500 C  C18 . A1A4U C .   ? 1.6807 1.6662 1.6095 -0.0982 -0.0085 0.0028  602 A1A4U A C18 
3501 C  C19 . A1A4U C .   ? 1.6994 1.6460 1.5772 -0.0731 0.0033  0.0034  602 A1A4U A C19 
3502 C  C20 . A1A4U C .   ? 1.7781 1.7511 1.6726 -0.0602 0.0186  0.0107  602 A1A4U A C20 
3503 C  C22 . A1A4U C .   ? 1.6046 1.6771 1.6346 -0.0340 0.1031  0.0416  602 A1A4U A C22 
3504 C  C23 . A1A4U C .   ? 1.6652 1.7843 1.7458 -0.0442 0.1049  0.0398  602 A1A4U A C23 
3505 C  C24 . A1A4U C .   ? 1.5168 1.6253 1.6130 -0.0458 0.1258  0.0465  602 A1A4U A C24 
3506 C  C02 . A1A4U C .   ? 1.6044 1.6493 1.5935 -0.0564 0.0832  0.0341  602 A1A4U A C02 
3507 C  C04 . A1A4U C .   ? 1.4067 1.4409 1.4152 -0.0652 0.1133  0.0436  602 A1A4U A C04 
3508 C  C05 . A1A4U C .   ? 1.4029 1.3916 1.3693 -0.0676 0.1079  0.0399  602 A1A4U A C05 
3509 C  C06 . A1A4U C .   ? 1.3946 1.3888 1.3768 -0.0838 0.1028  0.0409  602 A1A4U A C06 
3510 C  C07 . A1A4U C .   ? 1.1397 1.1702 1.1656 -0.0881 0.1147  0.0488  602 A1A4U A C07 
3511 C  C08 . A1A4U C .   ? 1.1138 1.1321 1.1453 -0.0769 0.1350  0.0546  602 A1A4U A C08 
3512 C  C25 . A1A4U C .   ? 1.4030 1.5302 1.5157 -0.0573 0.1255  0.0467  602 A1A4U A C25 
3513 C  C26 . A1A4U C .   ? 1.3058 1.4060 1.4070 -0.0581 0.1383  0.0521  602 A1A4U A C26 
3514 C  C27 . A1A4U C .   ? 1.2864 1.3964 1.3983 -0.0665 0.1374  0.0538  602 A1A4U A C27 
3515 C  C28 . A1A4U C .   ? 1.2883 1.4357 1.4203 -0.0751 0.1259  0.0518  602 A1A4U A C28 
3516 C  C29 . A1A4U C .   ? 1.4693 1.6469 1.6131 -0.0739 0.1161  0.0464  602 A1A4U A C29 
3517 C  C30 . A1A4U C .   ? 1.5102 1.6781 1.6460 -0.0646 0.1146  0.0430  602 A1A4U A C30 
3518 C  C35 . A1A4U C .   ? 1.8899 2.1242 2.0339 -0.0586 0.0725  0.0267  602 A1A4U A C35 
3519 C  C36 . A1A4U C .   ? 1.7847 1.9943 1.9134 -0.0708 0.0774  0.0317  602 A1A4U A C36 
3520 C  C37 . A1A4U C .   ? 1.7776 2.0042 1.9163 -0.0874 0.0713  0.0336  602 A1A4U A C37 
3521 C  C38 . A1A4U C .   ? 1.8945 2.1705 2.0641 -0.0934 0.0632  0.0322  602 A1A4U A C38 
3522 C  C39 . A1A4U C .   ? 1.8940 2.2012 2.0803 -0.0793 0.0602  0.0267  602 A1A4U A C39 
3523 C  C40 . A1A4U C .   ? 1.9325 2.2157 2.1034 -0.0619 0.0632  0.0232  602 A1A4U A C40 
3524 N  N03 . A1A4U C .   ? 1.5155 1.5797 1.5351 -0.0680 0.0934  0.0379  602 A1A4U A N03 
3525 N  N09 . A1A4U C .   ? 1.1038 1.1512 1.1711 -0.0785 0.1405  0.0601  602 A1A4U A N09 
3526 N  N31 . A1A4U C .   ? 1.8816 2.0339 1.9909 -0.0384 0.0976  0.0348  602 A1A4U A N31 
3527 O  O01 . A1A4U C .   ? 1.5806 1.5784 1.5266 -0.0435 0.0940  0.0367  602 A1A4U A O01 
3528 O  O33 . A1A4U C .   ? 1.9962 2.1963 2.1163 -0.0287 0.0662  0.0226  602 A1A4U A O33 
3529 O  O34 . A1A4U C .   ? 2.1214 2.3530 2.2826 -0.0341 0.0817  0.0218  602 A1A4U A O34 
3530 S  S21 . A1A4U C .   ? 1.9270 2.0113 1.9400 -0.0373 0.0706  0.0316  602 A1A4U A S21 
3531 S  S32 . A1A4U C .   ? 2.3018 2.5062 2.4355 -0.0397 0.0799  0.0263  602 A1A4U A S32 
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