data_9COV
# 
_entry.id   9COV 
# 
_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   9COV         pdb_00009cov 10.2210/pdb9cov/pdb 
WWPDB D_1000285849 ?            ?                   
# 
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                        9COV 
_pdbx_database_status.recvd_initial_deposition_date   2024-07-17 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              sevrioui@uci.edu 
_pdbx_contact_author.name_first         Irina 
_pdbx_contact_author.name_last          Sevrioukova 
_pdbx_contact_author.name_mi            F 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-4498-6057 
# 
_audit_author.name               'Sevrioukova, I.F.' 
_audit_author.pdbx_ordinal       1 
_audit_author.identifier_ORCID   ? 
# 
_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 
;N-[(2S)-1-(1H-indol-3-yl)-3-{[(2R)-1-oxo-3-phenyl-1-{[3-(pyridin-3-yl)propyl]amino}propan-2-yl]sulfanyl}propan-2-yl]pyridine-3-carboxamide
;
577.739   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 
;N-[(2S)-1-(1H-indol-3-yl)-3-{[(2R)-1-oxo-3-phenyl-1-{[3-(pyridin-3-yl)propyl]amino}propan-2-yl]sulfanyl}propan-2-yl]pyridine-3-carboxamide
;
A1A4S 
# 
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 
A1A4S non-polymer         . 
;N-[(2S)-1-(1H-indol-3-yl)-3-{[(2R)-1-oxo-3-phenyl-1-{[3-(pyridin-3-yl)propyl]amino}propan-2-yl]sulfanyl}propan-2-yl]pyridine-3-carboxamide
;
?    'C34 H35 N5 O2 S'  577.739 
ALA   'L-peptide linking' y ALANINE ?    'C3 H7 N O2'       89.093  
ARG   'L-peptide linking' y ARGININE ?    'C6 H15 N4 O2 1'   175.209 
ASN   'L-peptide linking' y ASPARAGINE ?    'C4 H8 N2 O3'      132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID' ?    'C4 H7 N O4'       133.103 
CYS   'L-peptide linking' y CYSTEINE ?    'C3 H7 N O2 S'     121.158 
GLN   'L-peptide linking' y GLUTAMINE ?    'C5 H10 N2 O3'     146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID' ?    'C5 H9 N O4'       147.129 
GLY   'peptide linking'   y GLYCINE ?    'C2 H5 N O2'       75.067  
HEM   non-polymer         . 'PROTOPORPHYRIN IX CONTAINING FE' HEME 'C34 H32 Fe N4 O4' 616.487 
HIS   'L-peptide linking' y HISTIDINE ?    'C6 H10 N3 O2 1'   156.162 
ILE   'L-peptide linking' y ISOLEUCINE ?    'C6 H13 N O2'      131.173 
LEU   'L-peptide linking' y LEUCINE ?    'C6 H13 N O2'      131.173 
LYS   'L-peptide linking' y LYSINE ?    'C6 H15 N2 O2 1'   147.195 
MET   'L-peptide linking' y METHIONINE ?    'C5 H11 N O2 S'    149.211 
PHE   'L-peptide linking' y PHENYLALANINE ?    'C9 H11 N O2'      165.189 
PRO   'L-peptide linking' y PROLINE ?    'C5 H9 N O2'       115.130 
SER   'L-peptide linking' y SERINE ?    'C3 H7 N O3'       105.093 
THR   'L-peptide linking' y THREONINE ?    'C4 H9 N O3'       119.119 
TRP   'L-peptide linking' y TRYPTOPHAN ?    'C11 H12 N2 O2'    204.225 
TYR   'L-peptide linking' y TYROSINE ?    'C9 H11 N O3'      181.189 
VAL   'L-peptide linking' y VALINE ?    'C5 H11 N O2'      117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   ?   ?   ?   A . n 
A 1 2   ALA 2   2   ?   ?   ?   A . n 
A 1 3   TYR 3   23  ?   ?   ?   A . n 
A 1 4   LEU 4   24  ?   ?   ?   A . n 
A 1 5   TYR 5   25  ?   ?   ?   A . n 
A 1 6   GLY 6   26  ?   ?   ?   A . n 
A 1 7   THR 7   27  ?   ?   ?   A . n 
A 1 8   HIS 8   28  28  HIS HIS A . n 
A 1 9   SER 9   29  29  SER SER A . n 
A 1 10  HIS 10  30  30  HIS HIS A . n 
A 1 11  GLY 11  31  31  GLY GLY A . n 
A 1 12  LEU 12  32  32  LEU LEU A . n 
A 1 13  PHE 13  33  33  PHE PHE A . n 
A 1 14  LYS 14  34  34  LYS LYS A . n 
A 1 15  LYS 15  35  35  LYS LYS A . n 
A 1 16  LEU 16  36  36  LEU LEU A . n 
A 1 17  GLY 17  37  37  GLY GLY A . n 
A 1 18  ILE 18  38  38  ILE ILE A . n 
A 1 19  PRO 19  39  39  PRO PRO A . n 
A 1 20  GLY 20  40  40  GLY GLY A . n 
A 1 21  PRO 21  41  41  PRO PRO A . n 
A 1 22  THR 22  42  42  THR THR A . n 
A 1 23  PRO 23  43  43  PRO PRO A . n 
A 1 24  LEU 24  44  44  LEU LEU A . n 
A 1 25  PRO 25  45  45  PRO PRO A . n 
A 1 26  PHE 26  46  46  PHE PHE A . n 
A 1 27  LEU 27  47  47  LEU LEU A . n 
A 1 28  GLY 28  48  48  GLY GLY A . n 
A 1 29  ASN 29  49  49  ASN ASN A . n 
A 1 30  ILE 30  50  50  ILE ILE A . n 
A 1 31  LEU 31  51  51  LEU LEU A . n 
A 1 32  SER 32  52  52  SER SER A . n 
A 1 33  TYR 33  53  53  TYR TYR A . n 
A 1 34  HIS 34  54  54  HIS HIS A . n 
A 1 35  LYS 35  55  55  LYS LYS A . n 
A 1 36  GLY 36  56  56  GLY GLY A . n 
A 1 37  PHE 37  57  57  PHE PHE A . n 
A 1 38  CYS 38  58  58  CYS CYS A . n 
A 1 39  MET 39  59  59  MET MET A . n 
A 1 40  PHE 40  60  60  PHE PHE A . n 
A 1 41  ASP 41  61  61  ASP ASP A . n 
A 1 42  MET 42  62  62  MET MET A . n 
A 1 43  GLU 43  63  63  GLU GLU A . n 
A 1 44  CYS 44  64  64  CYS CYS A . n 
A 1 45  HIS 45  65  65  HIS HIS A . n 
A 1 46  LYS 46  66  66  LYS LYS A . n 
A 1 47  LYS 47  67  67  LYS LYS A . n 
A 1 48  TYR 48  68  68  TYR TYR A . n 
A 1 49  GLY 49  69  69  GLY GLY A . n 
A 1 50  LYS 50  70  70  LYS LYS A . n 
A 1 51  VAL 51  71  71  VAL VAL A . n 
A 1 52  TRP 52  72  72  TRP TRP A . n 
A 1 53  GLY 53  73  73  GLY GLY A . n 
A 1 54  PHE 54  74  74  PHE PHE A . n 
A 1 55  TYR 55  75  75  TYR TYR A . n 
A 1 56  ASP 56  76  76  ASP ASP A . n 
A 1 57  GLY 57  77  77  GLY GLY A . n 
A 1 58  GLN 58  78  78  GLN GLN A . n 
A 1 59  GLN 59  79  79  GLN GLN A . n 
A 1 60  PRO 60  80  80  PRO PRO A . n 
A 1 61  VAL 61  81  81  VAL VAL A . n 
A 1 62  LEU 62  82  82  LEU LEU A . n 
A 1 63  ALA 63  83  83  ALA ALA A . n 
A 1 64  ILE 64  84  84  ILE ILE A . n 
A 1 65  THR 65  85  85  THR THR A . n 
A 1 66  ASP 66  86  86  ASP ASP A . n 
A 1 67  PRO 67  87  87  PRO PRO A . n 
A 1 68  ASP 68  88  88  ASP ASP A . n 
A 1 69  MET 69  89  89  MET MET A . n 
A 1 70  ILE 70  90  90  ILE ILE A . n 
A 1 71  LYS 71  91  91  LYS LYS A . n 
A 1 72  THR 72  92  92  THR THR A . n 
A 1 73  VAL 73  93  93  VAL VAL A . n 
A 1 74  LEU 74  94  94  LEU LEU A . n 
A 1 75  VAL 75  95  95  VAL VAL A . n 
A 1 76  LYS 76  96  96  LYS LYS A . n 
A 1 77  GLU 77  97  97  GLU GLU A . n 
A 1 78  CYS 78  98  98  CYS CYS A . n 
A 1 79  TYR 79  99  99  TYR TYR A . n 
A 1 80  SER 80  100 100 SER SER A . n 
A 1 81  VAL 81  101 101 VAL VAL A . n 
A 1 82  PHE 82  102 102 PHE PHE A . n 
A 1 83  THR 83  103 103 THR THR A . n 
A 1 84  ASN 84  104 104 ASN ASN A . n 
A 1 85  ARG 85  105 105 ARG ARG A . n 
A 1 86  ARG 86  106 106 ARG ARG A . n 
A 1 87  PRO 87  107 107 PRO PRO A . n 
A 1 88  PHE 88  108 108 PHE PHE A . n 
A 1 89  GLY 89  109 109 GLY GLY A . n 
A 1 90  PRO 90  110 110 PRO PRO A . n 
A 1 91  VAL 91  111 111 VAL VAL A . n 
A 1 92  GLY 92  112 112 GLY GLY A . n 
A 1 93  PHE 93  113 113 PHE PHE A . n 
A 1 94  MET 94  114 114 MET MET A . n 
A 1 95  LYS 95  115 115 LYS LYS A . n 
A 1 96  SER 96  116 116 SER SER A . n 
A 1 97  ALA 97  117 117 ALA ALA A . n 
A 1 98  ILE 98  118 118 ILE ILE A . n 
A 1 99  SER 99  119 119 SER SER A . n 
A 1 100 ILE 100 120 120 ILE ILE A . n 
A 1 101 ALA 101 121 121 ALA ALA A . n 
A 1 102 GLU 102 122 122 GLU GLU A . n 
A 1 103 ASP 103 123 123 ASP ASP A . n 
A 1 104 GLU 104 124 124 GLU GLU A . n 
A 1 105 GLU 105 125 125 GLU GLU A . n 
A 1 106 TRP 106 126 126 TRP TRP A . n 
A 1 107 LYS 107 127 127 LYS LYS A . n 
A 1 108 ARG 108 128 128 ARG ARG A . n 
A 1 109 LEU 109 129 129 LEU LEU A . n 
A 1 110 ARG 110 130 130 ARG ARG A . n 
A 1 111 SER 111 131 131 SER SER A . n 
A 1 112 LEU 112 132 132 LEU LEU A . n 
A 1 113 LEU 113 133 133 LEU LEU A . n 
A 1 114 SER 114 134 134 SER SER A . n 
A 1 115 PRO 115 135 135 PRO PRO A . n 
A 1 116 THR 116 136 136 THR THR A . n 
A 1 117 PHE 117 137 137 PHE PHE A . n 
A 1 118 THR 118 138 138 THR THR A . n 
A 1 119 SER 119 139 139 SER SER A . n 
A 1 120 GLY 120 140 140 GLY GLY A . n 
A 1 121 LYS 121 141 141 LYS LYS A . n 
A 1 122 LEU 122 142 142 LEU LEU A . n 
A 1 123 LYS 123 143 143 LYS LYS A . n 
A 1 124 GLU 124 144 144 GLU GLU A . n 
A 1 125 MET 125 145 145 MET MET A . n 
A 1 126 VAL 126 146 146 VAL VAL A . n 
A 1 127 PRO 127 147 147 PRO PRO A . n 
A 1 128 ILE 128 148 148 ILE ILE A . n 
A 1 129 ILE 129 149 149 ILE ILE A . n 
A 1 130 ALA 130 150 150 ALA ALA A . n 
A 1 131 GLN 131 151 151 GLN GLN A . n 
A 1 132 TYR 132 152 152 TYR TYR A . n 
A 1 133 GLY 133 153 153 GLY GLY A . n 
A 1 134 ASP 134 154 154 ASP ASP A . n 
A 1 135 VAL 135 155 155 VAL VAL A . n 
A 1 136 LEU 136 156 156 LEU LEU A . n 
A 1 137 VAL 137 157 157 VAL VAL A . n 
A 1 138 ARG 138 158 158 ARG ARG A . n 
A 1 139 ASN 139 159 159 ASN ASN A . n 
A 1 140 LEU 140 160 160 LEU LEU A . n 
A 1 141 ARG 141 161 161 ARG ARG A . n 
A 1 142 ARG 142 162 162 ARG ARG A . n 
A 1 143 GLU 143 163 163 GLU GLU A . n 
A 1 144 ALA 144 164 164 ALA ALA A . n 
A 1 145 GLU 145 165 165 GLU GLU A . n 
A 1 146 THR 146 166 166 THR THR A . n 
A 1 147 GLY 147 167 167 GLY GLY A . n 
A 1 148 LYS 148 168 168 LYS LYS A . n 
A 1 149 PRO 149 169 169 PRO PRO A . n 
A 1 150 VAL 150 170 170 VAL VAL A . n 
A 1 151 THR 151 171 171 THR THR A . n 
A 1 152 LEU 152 172 172 LEU LEU A . n 
A 1 153 LYS 153 173 173 LYS LYS A . n 
A 1 154 ASP 154 174 174 ASP ASP A . n 
A 1 155 VAL 155 175 175 VAL VAL A . n 
A 1 156 PHE 156 176 176 PHE PHE A . n 
A 1 157 GLY 157 177 177 GLY GLY A . n 
A 1 158 ALA 158 178 178 ALA ALA A . n 
A 1 159 TYR 159 179 179 TYR TYR A . n 
A 1 160 SER 160 180 180 SER SER A . n 
A 1 161 MET 161 181 181 MET MET A . n 
A 1 162 ASP 162 182 182 ASP ASP A . n 
A 1 163 VAL 163 183 183 VAL VAL A . n 
A 1 164 ILE 164 184 184 ILE ILE A . n 
A 1 165 THR 165 185 185 THR THR A . n 
A 1 166 SER 166 186 186 SER SER A . n 
A 1 167 THR 167 187 187 THR THR A . n 
A 1 168 SER 168 188 188 SER SER A . n 
A 1 169 PHE 169 189 189 PHE PHE A . n 
A 1 170 GLY 170 190 190 GLY GLY A . n 
A 1 171 VAL 171 191 191 VAL VAL A . n 
A 1 172 ASN 172 192 192 ASN ASN A . n 
A 1 173 ILE 173 193 193 ILE ILE A . n 
A 1 174 ASP 174 194 194 ASP ASP A . n 
A 1 175 SER 175 195 195 SER SER A . n 
A 1 176 LEU 176 196 196 LEU LEU A . n 
A 1 177 ASN 177 197 197 ASN ASN A . n 
A 1 178 ASN 178 198 198 ASN ASN A . n 
A 1 179 PRO 179 199 199 PRO PRO A . n 
A 1 180 GLN 180 200 200 GLN GLN A . n 
A 1 181 ASP 181 201 201 ASP ASP A . n 
A 1 182 PRO 182 202 202 PRO PRO A . n 
A 1 183 PHE 183 203 203 PHE PHE 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 ?   ?   ?   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 ?   ?   ?   A . n 
A 1 221 PHE 221 241 ?   ?   ?   A . n 
A 1 222 PRO 222 242 ?   ?   ?   A . n 
A 1 223 ARG 223 243 ?   ?   ?   A . n 
A 1 224 GLU 224 244 ?   ?   ?   A . n 
A 1 225 VAL 225 245 ?   ?   ?   A . n 
A 1 226 THR 226 246 246 THR THR A . n 
A 1 227 ASN 227 247 247 ASN ASN A . n 
A 1 228 PHE 228 248 248 PHE PHE A . n 
A 1 229 LEU 229 249 249 LEU LEU A . n 
A 1 230 ARG 230 250 250 ARG ARG A . n 
A 1 231 LYS 231 251 251 LYS LYS A . n 
A 1 232 SER 232 252 252 SER SER A . n 
A 1 233 VAL 233 253 253 VAL VAL A . n 
A 1 234 LYS 234 254 254 LYS LYS A . n 
A 1 235 ARG 235 255 255 ARG ARG A . n 
A 1 236 MET 236 256 256 MET MET A . n 
A 1 237 LYS 237 257 257 LYS LYS A . n 
A 1 238 GLU 238 258 258 GLU GLU A . n 
A 1 239 SER 239 259 259 SER SER A . n 
A 1 240 ARG 240 260 ?   ?   ?   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 ?   ?   ?   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        A1A4S 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1A4S 
_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 A1A4S 1 602 700 A1A4S 420 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                     9COV 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     75.399 
_cell.length_a_esd                 ? 
_cell.length_b                     99.770 
_cell.length_b_esd                 ? 
_cell.length_c                     122.640 
_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                         9COV 
_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                   9COV 
_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             2.07 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          40.53 
_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, succinic acid' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     103 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      mirrors 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS 300K' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2018-01-13 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.98 
_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                        'SSRL BEAMLINE BL9-2' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.98 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL9-2 
_diffrn_source.pdbx_synchrotron_site       SSRL 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9COV 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.58 
_reflns.d_resolution_low                               77.39 
_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                                     14553 
_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                           98.0 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                3.9 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          11.0 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                0.022 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.999 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.038 
_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                                    2.58 
_reflns_shell.d_res_low                                     2.72 
_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                             2103 
_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                               1.078 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.331 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          99.2 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  1.940 
_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                                 9COV 
_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                            2.60 
_refine.ls_d_res_low                             49.88 
_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                     14198 
_refine.ls_number_reflns_R_free                  704 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    97.29 
_refine.ls_percent_reflns_R_free                 4.96 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2560 
_refine.ls_R_factor_R_free                       0.2742 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2503 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.34 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.10 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 43.58 
_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                            0.53 
_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                       2.60 
_refine_hist.d_res_low                        49.88 
_refine_hist.number_atoms_solvent             0 
_refine_hist.number_atoms_total               3539 
_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        3454 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         85 
_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  ? 3649 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.639  ? 4947 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 15.375 ? 1377 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.040  ? 541  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.005  ? 619  ? 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' 2.60 2.80  . . 146 2665 98.00 . . . . 0.4131 . . . . . . . . . . . 0.4240 
'X-RAY DIFFRACTION' 2.80 3.08  . . 143 2681 98.00 . . . . 0.3527 . . . . . . . . . . . 0.3994 
'X-RAY DIFFRACTION' 3.08 3.53  . . 121 2698 98.00 . . . . 0.3314 . . . . . . . . . . . 0.4367 
'X-RAY DIFFRACTION' 3.53 4.44  . . 133 2680 96.00 . . . . 0.2689 . . . . . . . . . . . 0.2842 
'X-RAY DIFFRACTION' 4.45 49.88 . . 161 2770 96.00 . . . . 0.2219 . . . . . . . . . . . 0.2465 
# 
_struct.entry_id                     9COV 
_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        9COV 
_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              9COV 
_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 9COV ?   A ?   ? UNP P08684 LEU 3  deletion         ?   1  
1 9COV ?   A ?   ? UNP P08684 ILE 4  deletion         ?   2  
1 9COV ?   A ?   ? UNP P08684 PRO 5  deletion         ?   3  
1 9COV ?   A ?   ? UNP P08684 ASP 6  deletion         ?   4  
1 9COV ?   A ?   ? UNP P08684 LEU 7  deletion         ?   5  
1 9COV ?   A ?   ? UNP P08684 ALA 8  deletion         ?   6  
1 9COV ?   A ?   ? UNP P08684 MET 9  deletion         ?   7  
1 9COV ?   A ?   ? UNP P08684 GLU 10 deletion         ?   8  
1 9COV ?   A ?   ? UNP P08684 THR 11 deletion         ?   9  
1 9COV ?   A ?   ? UNP P08684 TRP 12 deletion         ?   10 
1 9COV ?   A ?   ? UNP P08684 LEU 13 deletion         ?   11 
1 9COV ?   A ?   ? UNP P08684 LEU 14 deletion         ?   12 
1 9COV ?   A ?   ? UNP P08684 LEU 15 deletion         ?   13 
1 9COV ?   A ?   ? UNP P08684 ALA 16 deletion         ?   14 
1 9COV ?   A ?   ? UNP P08684 VAL 17 deletion         ?   15 
1 9COV ?   A ?   ? UNP P08684 SER 18 deletion         ?   16 
1 9COV ?   A ?   ? UNP P08684 LEU 19 deletion         ?   17 
1 9COV ?   A ?   ? UNP P08684 VAL 20 deletion         ?   18 
1 9COV ?   A ?   ? UNP P08684 LEU 21 deletion         ?   19 
1 9COV ?   A ?   ? UNP P08684 LEU 22 deletion         ?   20 
1 9COV HIS A 484 ? UNP P08684 ?   ?  'expression tag' 504 21 
1 9COV HIS A 485 ? UNP P08684 ?   ?  'expression tag' 505 22 
1 9COV HIS A 486 ? UNP P08684 ?   ?  'expression tag' 506 23 
1 9COV 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_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 
# 
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  ? LYS A 35  ? ASN A 49  LYS A 55  5 ? 7  
HELX_P HELX_P3  AA3 GLY A 36  ? GLY A 49  ? GLY A 56  GLY A 69  1 ? 14 
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 ? ALA A 130 ? THR A 138 ALA A 150 1 ? 13 
HELX_P HELX_P9  AA9 GLN A 131 ? THR A 146 ? GLN A 151 THR A 166 1 ? 16 
HELX_P HELX_P10 AB1 LEU A 152 ? SER A 168 ? LEU A 172 SER A 188 1 ? 17 
HELX_P HELX_P11 AB2 PHE A 199 ? PHE A 206 ? PHE A 219 PHE A 226 1 ? 8  
HELX_P HELX_P12 AB3 LEU A 209 ? GLU A 214 ? LEU A 229 GLU A 234 1 ? 6  
HELX_P HELX_P13 AB4 ASN A 227 ? VAL A 233 ? ASN A 247 VAL A 253 1 ? 7  
HELX_P HELX_P14 AB5 LEU A 252 ? ASP A 257 ? LEU A 272 ASP A 277 1 ? 6  
HELX_P HELX_P15 AB6 ASP A 272 ? HIS A 304 ? ASP A 292 HIS A 324 1 ? 33 
HELX_P HELX_P16 AB7 HIS A 304 ? LEU A 319 ? HIS A 324 LEU A 339 1 ? 16 
HELX_P HELX_P17 AB8 THR A 326 ? MET A 333 ? THR A 346 MET A 353 1 ? 8  
HELX_P HELX_P18 AB9 MET A 333 ? PHE A 347 ? MET A 353 PHE A 367 1 ? 15 
HELX_P HELX_P19 AC1 PRO A 377 ? ARG A 383 ? PRO A 397 ARG A 403 1 ? 7  
HELX_P HELX_P20 AC2 LEU A 395 ? SER A 400 ? LEU A 415 SER A 420 5 ? 6  
HELX_P HELX_P21 AC3 SER A 417 ? ASN A 421 ? SER A 437 ASN A 441 5 ? 5  
HELX_P HELX_P22 AC4 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 ? ? ? ? ? ? ? 2.354 ? ? 
metalc2 metalc ? ? B HEM .   FE ? ? ? 1_555 C A1A4S . N28 ? ? A HEM 601 A A1A4S 602 1_555 ? ? ? ? ? ? ? 2.058 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  SG ? A CYS 422 ? A CYS 442 ? 1_555 FE ? B HEM . ? A HEM 601 ? 1_555 NA  ? B HEM   . ? A HEM   601 ? 1_555 96.6  ? 
2  SG ? A CYS 422 ? A CYS 442 ? 1_555 FE ? B HEM . ? A HEM 601 ? 1_555 NB  ? B HEM   . ? A HEM   601 ? 1_555 81.4  ? 
3  NA ? B HEM .   ? A HEM 601 ? 1_555 FE ? B HEM . ? A HEM 601 ? 1_555 NB  ? B HEM   . ? A HEM   601 ? 1_555 88.8  ? 
4  SG ? A CYS 422 ? A CYS 442 ? 1_555 FE ? B HEM . ? A HEM 601 ? 1_555 NC  ? B HEM   . ? A HEM   601 ? 1_555 89.4  ? 
5  NA ? B HEM .   ? A HEM 601 ? 1_555 FE ? B HEM . ? A HEM 601 ? 1_555 NC  ? B HEM   . ? A HEM   601 ? 1_555 173.4 ? 
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 89.3  ? 
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_555 102.3 ? 
8  NA ? B HEM .   ? A HEM 601 ? 1_555 FE ? B HEM . ? A HEM 601 ? 1_555 ND  ? B HEM   . ? A HEM   601 ? 1_555 91.9  ? 
9  NB ? B HEM .   ? A HEM 601 ? 1_555 FE ? B HEM . ? A HEM 601 ? 1_555 ND  ? B HEM   . ? A HEM   601 ? 1_555 176.2 ? 
10 NC ? B HEM .   ? A HEM 601 ? 1_555 FE ? B HEM . ? A HEM 601 ? 1_555 ND  ? B HEM   . ? A HEM   601 ? 1_555 89.6  ? 
11 SG ? A CYS 422 ? A CYS 442 ? 1_555 FE ? B HEM . ? A HEM 601 ? 1_555 N28 ? C A1A4S . ? A A1A4S 602 ? 1_555 171.7 ? 
12 NA ? B HEM .   ? A HEM 601 ? 1_555 FE ? B HEM . ? A HEM 601 ? 1_555 N28 ? C A1A4S . ? A A1A4S 602 ? 1_555 88.7  ? 
13 NB ? B HEM .   ? A HEM 601 ? 1_555 FE ? B HEM . ? A HEM 601 ? 1_555 N28 ? C A1A4S . ? A A1A4S 602 ? 1_555 92.3  ? 
14 NC ? B HEM .   ? A HEM 601 ? 1_555 FE ? B HEM . ? A HEM 601 ? 1_555 N28 ? C A1A4S . ? A A1A4S 602 ? 1_555 85.1  ? 
15 ND ? B HEM .   ? A HEM 601 ? 1_555 FE ? B HEM . ? A HEM 601 ? 1_555 N28 ? C A1A4S . ? A A1A4S 602 ? 1_555 83.9  ? 
# 
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 0.51 
2 ILE 453 A . ? ILE 473 A PRO 454 A ? PRO 474 A 1 0.03 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 3 ? 
AA3 ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? parallel      
AA1 3 4 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA3 1 2 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 VAL A 51  ? ASP A 56  ? VAL A 71  ASP A 76  
AA1 2 GLN A 59  ? ILE A 64  ? GLN A 79  ILE A 84  
AA1 3 VAL A 373 ? ILE A 376 ? VAL A 393 ILE A 396 
AA1 4 LEU A 353 ? VAL A 356 ? LEU A 373 VAL A 376 
AA2 1 VAL A 150 ? THR A 151 ? VAL A 170 THR A 171 
AA2 2 VAL A 470 ? SER A 475 ? VAL A 490 SER A 495 
AA2 3 PHE A 443 ? PRO A 447 ? PHE A 463 PRO A 467 
AA3 1 VAL A 361 ? ILE A 363 ? VAL A 381 ILE A 383 
AA3 2 MET A 366 ? ILE A 368 ? MET A 386 ILE A 388 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N PHE A 54  ? N PHE A 74  O VAL A 61  ? O VAL A 81  
AA1 2 3 N LEU A 62  ? N LEU A 82  O MET A 375 ? O MET A 395 
AA1 3 4 O ILE A 376 ? O ILE A 396 N LEU A 353 ? N LEU A 373 
AA2 1 2 N VAL A 150 ? N VAL A 170 O LEU A 471 ? O LEU A 491 
AA2 2 3 O LYS A 472 ? O LYS A 492 N LYS A 446 ? N LYS A 466 
AA3 1 2 N VAL A 361 ? N VAL A 381 O ILE A 368 ? O ILE A 388 
# 
_pdbx_entry_details.entry_id                   9COV 
_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  ? ? 68.62   -51.36  
2  1 VAL A 95  ? ? -124.43 -59.95  
3  1 PHE A 102 ? ? -110.29 60.35   
4  1 ASP A 123 ? ? 48.55   -121.50 
5  1 PRO A 135 ? ? -69.14  8.00    
6  1 SER A 195 ? ? -88.12  39.38   
7  1 ASP A 201 ? ? -163.05 75.03   
8  1 PHE A 226 ? ? -119.17 59.49   
9  1 ARG A 255 ? ? -90.68  37.05   
10 1 ALA A 289 ? ? -103.17 -163.52 
11 1 TYR A 307 ? ? -92.40  -66.09  
12 1 MET A 371 ? ? 67.77   -52.78  
13 1 TYR A 407 ? ? -141.06 -37.67  
14 1 ASN A 426 ? ? -83.31  37.21   
# 
_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         -18.3678 
_pdbx_refine_tls.origin_y         -23.5078 
_pdbx_refine_tls.origin_z         -12.8602 
_pdbx_refine_tls.T[1][1]          0.6959 
_pdbx_refine_tls.T[1][1]_esd      ? 
_pdbx_refine_tls.T[1][2]          -0.0431 
_pdbx_refine_tls.T[1][2]_esd      ? 
_pdbx_refine_tls.T[1][3]          -0.0245 
_pdbx_refine_tls.T[1][3]_esd      ? 
_pdbx_refine_tls.T[2][2]          0.7482 
_pdbx_refine_tls.T[2][2]_esd      ? 
_pdbx_refine_tls.T[2][3]          -0.1834 
_pdbx_refine_tls.T[2][3]_esd      ? 
_pdbx_refine_tls.T[3][3]          0.7332 
_pdbx_refine_tls.T[3][3]_esd      ? 
_pdbx_refine_tls.L[1][1]          3.6533 
_pdbx_refine_tls.L[1][1]_esd      ? 
_pdbx_refine_tls.L[1][2]          -1.7280 
_pdbx_refine_tls.L[1][2]_esd      ? 
_pdbx_refine_tls.L[1][3]          -0.5769 
_pdbx_refine_tls.L[1][3]_esd      ? 
_pdbx_refine_tls.L[2][2]          5.7160 
_pdbx_refine_tls.L[2][2]_esd      ? 
_pdbx_refine_tls.L[2][3]          0.8931 
_pdbx_refine_tls.L[2][3]_esd      ? 
_pdbx_refine_tls.L[3][3]          3.4005 
_pdbx_refine_tls.L[3][3]_esd      ? 
_pdbx_refine_tls.S[1][1]          -0.0533 
_pdbx_refine_tls.S[1][1]_esd      ? 
_pdbx_refine_tls.S[1][2]          0.4187 
_pdbx_refine_tls.S[1][2]_esd      ? 
_pdbx_refine_tls.S[1][3]          -0.5515 
_pdbx_refine_tls.S[1][3]_esd      ? 
_pdbx_refine_tls.S[2][1]          0.2273 
_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]          -0.0610 
_pdbx_refine_tls.S[2][3]_esd      ? 
_pdbx_refine_tls.S[3][1]          0.7670 
_pdbx_refine_tls.S[3][1]_esd      ? 
_pdbx_refine_tls.S[3][2]          -0.1952 
_pdbx_refine_tls.S[3][2]_esd      ? 
_pdbx_refine_tls.S[3][3]          -0.0113 
_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 VAL 204 ? A VAL 184 
9  1 Y 1 A GLU 205 ? A GLU 185 
10 1 Y 1 A ASN 206 ? A ASN 186 
11 1 Y 1 A THR 207 ? A THR 187 
12 1 Y 1 A LYS 208 ? A LYS 188 
13 1 Y 1 A LYS 209 ? A LYS 189 
14 1 Y 1 A LEU 210 ? A LEU 190 
15 1 Y 1 A LEU 211 ? A LEU 191 
16 1 Y 1 A ARG 212 ? A ARG 192 
17 1 Y 1 A PHE 213 ? A PHE 193 
18 1 Y 1 A ASP 214 ? A ASP 194 
19 1 Y 1 A PHE 215 ? A PHE 195 
20 1 Y 1 A LEU 216 ? A LEU 196 
21 1 Y 1 A ASP 217 ? A ASP 197 
22 1 Y 1 A VAL 240 ? A VAL 220 
23 1 Y 1 A PHE 241 ? A PHE 221 
24 1 Y 1 A PRO 242 ? A PRO 222 
25 1 Y 1 A ARG 243 ? A ARG 223 
26 1 Y 1 A GLU 244 ? A GLU 224 
27 1 Y 1 A VAL 245 ? A VAL 225 
28 1 Y 1 A ARG 260 ? A ARG 240 
29 1 Y 1 A LEU 261 ? A LEU 241 
30 1 Y 1 A GLU 262 ? A GLU 242 
31 1 Y 1 A ASP 263 ? A ASP 243 
32 1 Y 1 A THR 264 ? A THR 244 
33 1 Y 1 A GLN 265 ? A GLN 245 
34 1 Y 1 A LYS 266 ? A LYS 246 
35 1 Y 1 A HIS 267 ? A HIS 247 
36 1 Y 1 A ARG 268 ? A ARG 248 
37 1 Y 1 A VAL 269 ? A VAL 249 
38 1 Y 1 A ASN 280 ? A ASN 260 
39 1 Y 1 A SER 281 ? A SER 261 
40 1 Y 1 A LYS 282 ? A LYS 262 
41 1 Y 1 A GLU 283 ? A GLU 263 
42 1 Y 1 A THR 284 ? A THR 264 
43 1 Y 1 A GLU 285 ? A GLU 265 
44 1 Y 1 A SER 286 ? A SER 266 
45 1 Y 1 A HIS 287 ? A HIS 267 
46 1 Y 1 A ASP 497 ? A ASP 477 
47 1 Y 1 A GLY 498 ? A GLY 478 
48 1 Y 1 A THR 499 ? A THR 479 
49 1 Y 1 A VAL 500 ? A VAL 480 
50 1 Y 1 A SER 501 ? A SER 481 
51 1 Y 1 A GLY 502 ? A GLY 482 
52 1 Y 1 A ALA 503 ? A ALA 483 
53 1 Y 1 A HIS 504 ? A HIS 484 
54 1 Y 1 A HIS 505 ? A HIS 485 
55 1 Y 1 A HIS 506 ? A HIS 486 
56 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 
A1A4S C11  C  N N 1   
A1A4S C13  C  N N 2   
A1A4S C14  C  Y N 3   
A1A4S C15  C  Y N 4   
A1A4S C16  C  Y N 5   
A1A4S C17  C  Y N 6   
A1A4S C18  C  Y N 7   
A1A4S C19  C  Y N 8   
A1A4S C20  C  N N 9   
A1A4S C23  C  Y N 10  
A1A4S C01  C  N N 11  
A1A4S C02  C  N N 12  
A1A4S C03  C  N N 13  
A1A4S C05  C  N N 14  
A1A4S C06  C  N R 15  
A1A4S C08  C  N N 16  
A1A4S C09  C  N S 17  
A1A4S C21  C  Y N 18  
A1A4S C24  C  Y N 19  
A1A4S C25  C  Y N 20  
A1A4S C26  C  Y N 21  
A1A4S C27  C  Y N 22  
A1A4S C29  C  Y N 23  
A1A4S C30  C  Y N 24  
A1A4S C32  C  Y N 25  
A1A4S C33  C  Y N 26  
A1A4S C34  C  Y N 27  
A1A4S C35  C  Y N 28  
A1A4S C36  C  Y N 29  
A1A4S C38  C  Y N 30  
A1A4S C39  C  Y N 31  
A1A4S C40  C  Y N 32  
A1A4S C41  C  Y N 33  
A1A4S C42  C  Y N 34  
A1A4S N04  N  N N 35  
A1A4S N10  N  N N 36  
A1A4S N28  N  Y N 37  
A1A4S N31  N  Y N 38  
A1A4S N37  N  Y N 39  
A1A4S O12  O  N N 40  
A1A4S O22  O  N N 41  
A1A4S S07  S  N N 42  
A1A4S H1   H  N N 43  
A1A4S H2   H  N N 44  
A1A4S H3   H  N N 45  
A1A4S H4   H  N N 46  
A1A4S H5   H  N N 47  
A1A4S H6   H  N N 48  
A1A4S H7   H  N N 49  
A1A4S H8   H  N N 50  
A1A4S H9   H  N N 51  
A1A4S H10  H  N N 52  
A1A4S H11  H  N N 53  
A1A4S H12  H  N N 54  
A1A4S H13  H  N N 55  
A1A4S H14  H  N N 56  
A1A4S H15  H  N N 57  
A1A4S H16  H  N N 58  
A1A4S H17  H  N N 59  
A1A4S H18  H  N N 60  
A1A4S H19  H  N N 61  
A1A4S H20  H  N N 62  
A1A4S H21  H  N N 63  
A1A4S H22  H  N N 64  
A1A4S H23  H  N N 65  
A1A4S H24  H  N N 66  
A1A4S H25  H  N N 67  
A1A4S H26  H  N N 68  
A1A4S H27  H  N N 69  
A1A4S H28  H  N N 70  
A1A4S H29  H  N N 71  
A1A4S H30  H  N N 72  
A1A4S H31  H  N N 73  
A1A4S H32  H  N N 74  
A1A4S H33  H  N N 75  
A1A4S H34  H  N N 76  
A1A4S H35  H  N N 77  
ALA   N    N  N N 78  
ALA   CA   C  N S 79  
ALA   C    C  N N 80  
ALA   O    O  N N 81  
ALA   CB   C  N N 82  
ALA   OXT  O  N N 83  
ALA   H    H  N N 84  
ALA   H2   H  N N 85  
ALA   HA   H  N N 86  
ALA   HB1  H  N N 87  
ALA   HB2  H  N N 88  
ALA   HB3  H  N N 89  
ALA   HXT  H  N N 90  
ARG   N    N  N N 91  
ARG   CA   C  N S 92  
ARG   C    C  N N 93  
ARG   O    O  N N 94  
ARG   CB   C  N N 95  
ARG   CG   C  N N 96  
ARG   CD   C  N N 97  
ARG   NE   N  N N 98  
ARG   CZ   C  N N 99  
ARG   NH1  N  N N 100 
ARG   NH2  N  N N 101 
ARG   OXT  O  N N 102 
ARG   H    H  N N 103 
ARG   H2   H  N N 104 
ARG   HA   H  N N 105 
ARG   HB2  H  N N 106 
ARG   HB3  H  N N 107 
ARG   HG2  H  N N 108 
ARG   HG3  H  N N 109 
ARG   HD2  H  N N 110 
ARG   HD3  H  N N 111 
ARG   HE   H  N N 112 
ARG   HH11 H  N N 113 
ARG   HH12 H  N N 114 
ARG   HH21 H  N N 115 
ARG   HH22 H  N N 116 
ARG   HXT  H  N N 117 
ASN   N    N  N N 118 
ASN   CA   C  N S 119 
ASN   C    C  N N 120 
ASN   O    O  N N 121 
ASN   CB   C  N N 122 
ASN   CG   C  N N 123 
ASN   OD1  O  N N 124 
ASN   ND2  N  N N 125 
ASN   OXT  O  N N 126 
ASN   H    H  N N 127 
ASN   H2   H  N N 128 
ASN   HA   H  N N 129 
ASN   HB2  H  N N 130 
ASN   HB3  H  N N 131 
ASN   HD21 H  N N 132 
ASN   HD22 H  N N 133 
ASN   HXT  H  N N 134 
ASP   N    N  N N 135 
ASP   CA   C  N S 136 
ASP   C    C  N N 137 
ASP   O    O  N N 138 
ASP   CB   C  N N 139 
ASP   CG   C  N N 140 
ASP   OD1  O  N N 141 
ASP   OD2  O  N N 142 
ASP   OXT  O  N N 143 
ASP   H    H  N N 144 
ASP   H2   H  N N 145 
ASP   HA   H  N N 146 
ASP   HB2  H  N N 147 
ASP   HB3  H  N N 148 
ASP   HD2  H  N N 149 
ASP   HXT  H  N N 150 
CYS   N    N  N N 151 
CYS   CA   C  N R 152 
CYS   C    C  N N 153 
CYS   O    O  N N 154 
CYS   CB   C  N N 155 
CYS   SG   S  N N 156 
CYS   OXT  O  N N 157 
CYS   H    H  N N 158 
CYS   H2   H  N N 159 
CYS   HA   H  N N 160 
CYS   HB2  H  N N 161 
CYS   HB3  H  N N 162 
CYS   HG   H  N N 163 
CYS   HXT  H  N N 164 
GLN   N    N  N N 165 
GLN   CA   C  N S 166 
GLN   C    C  N N 167 
GLN   O    O  N N 168 
GLN   CB   C  N N 169 
GLN   CG   C  N N 170 
GLN   CD   C  N N 171 
GLN   OE1  O  N N 172 
GLN   NE2  N  N N 173 
GLN   OXT  O  N N 174 
GLN   H    H  N N 175 
GLN   H2   H  N N 176 
GLN   HA   H  N N 177 
GLN   HB2  H  N N 178 
GLN   HB3  H  N N 179 
GLN   HG2  H  N N 180 
GLN   HG3  H  N N 181 
GLN   HE21 H  N N 182 
GLN   HE22 H  N N 183 
GLN   HXT  H  N N 184 
GLU   N    N  N N 185 
GLU   CA   C  N S 186 
GLU   C    C  N N 187 
GLU   O    O  N N 188 
GLU   CB   C  N N 189 
GLU   CG   C  N N 190 
GLU   CD   C  N N 191 
GLU   OE1  O  N N 192 
GLU   OE2  O  N N 193 
GLU   OXT  O  N N 194 
GLU   H    H  N N 195 
GLU   H2   H  N N 196 
GLU   HA   H  N N 197 
GLU   HB2  H  N N 198 
GLU   HB3  H  N N 199 
GLU   HG2  H  N N 200 
GLU   HG3  H  N N 201 
GLU   HE2  H  N N 202 
GLU   HXT  H  N N 203 
GLY   N    N  N N 204 
GLY   CA   C  N N 205 
GLY   C    C  N N 206 
GLY   O    O  N N 207 
GLY   OXT  O  N N 208 
GLY   H    H  N N 209 
GLY   H2   H  N N 210 
GLY   HA2  H  N N 211 
GLY   HA3  H  N N 212 
GLY   HXT  H  N N 213 
HEM   CHA  C  N N 214 
HEM   CHB  C  N N 215 
HEM   CHC  C  N N 216 
HEM   CHD  C  N N 217 
HEM   C1A  C  Y N 218 
HEM   C2A  C  Y N 219 
HEM   C3A  C  Y N 220 
HEM   C4A  C  Y N 221 
HEM   CMA  C  N N 222 
HEM   CAA  C  N N 223 
HEM   CBA  C  N N 224 
HEM   CGA  C  N N 225 
HEM   O1A  O  N N 226 
HEM   O2A  O  N N 227 
HEM   C1B  C  N N 228 
HEM   C2B  C  N N 229 
HEM   C3B  C  N N 230 
HEM   C4B  C  N N 231 
HEM   CMB  C  N N 232 
HEM   CAB  C  N N 233 
HEM   CBB  C  N N 234 
HEM   C1C  C  Y N 235 
HEM   C2C  C  Y N 236 
HEM   C3C  C  Y N 237 
HEM   C4C  C  Y N 238 
HEM   CMC  C  N N 239 
HEM   CAC  C  N N 240 
HEM   CBC  C  N N 241 
HEM   C1D  C  N N 242 
HEM   C2D  C  N N 243 
HEM   C3D  C  N N 244 
HEM   C4D  C  N N 245 
HEM   CMD  C  N N 246 
HEM   CAD  C  N N 247 
HEM   CBD  C  N N 248 
HEM   CGD  C  N N 249 
HEM   O1D  O  N N 250 
HEM   O2D  O  N N 251 
HEM   NA   N  Y N 252 
HEM   NB   N  N N 253 
HEM   NC   N  Y N 254 
HEM   ND   N  N N 255 
HEM   FE   FE N N 256 
HEM   HHB  H  N N 257 
HEM   HHC  H  N N 258 
HEM   HHD  H  N N 259 
HEM   HMA  H  N N 260 
HEM   HMAA H  N N 261 
HEM   HMAB H  N N 262 
HEM   HAA  H  N N 263 
HEM   HAAA H  N N 264 
HEM   HBA  H  N N 265 
HEM   HBAA H  N N 266 
HEM   HMB  H  N N 267 
HEM   HMBA H  N N 268 
HEM   HMBB H  N N 269 
HEM   HAB  H  N N 270 
HEM   HBB  H  N N 271 
HEM   HBBA H  N N 272 
HEM   HMC  H  N N 273 
HEM   HMCA H  N N 274 
HEM   HMCB H  N N 275 
HEM   HAC  H  N N 276 
HEM   HBC  H  N N 277 
HEM   HBCA H  N N 278 
HEM   HMD  H  N N 279 
HEM   HMDA H  N N 280 
HEM   HMDB H  N N 281 
HEM   HAD  H  N N 282 
HEM   HADA H  N N 283 
HEM   HBD  H  N N 284 
HEM   HBDA H  N N 285 
HEM   H2A  H  N N 286 
HEM   H2D  H  N N 287 
HEM   HHA  H  N N 288 
HIS   N    N  N N 289 
HIS   CA   C  N S 290 
HIS   C    C  N N 291 
HIS   O    O  N N 292 
HIS   CB   C  N N 293 
HIS   CG   C  Y N 294 
HIS   ND1  N  Y N 295 
HIS   CD2  C  Y N 296 
HIS   CE1  C  Y N 297 
HIS   NE2  N  Y N 298 
HIS   OXT  O  N N 299 
HIS   H    H  N N 300 
HIS   H2   H  N N 301 
HIS   HA   H  N N 302 
HIS   HB2  H  N N 303 
HIS   HB3  H  N N 304 
HIS   HD1  H  N N 305 
HIS   HD2  H  N N 306 
HIS   HE1  H  N N 307 
HIS   HE2  H  N N 308 
HIS   HXT  H  N N 309 
ILE   N    N  N N 310 
ILE   CA   C  N S 311 
ILE   C    C  N N 312 
ILE   O    O  N N 313 
ILE   CB   C  N S 314 
ILE   CG1  C  N N 315 
ILE   CG2  C  N N 316 
ILE   CD1  C  N N 317 
ILE   OXT  O  N N 318 
ILE   H    H  N N 319 
ILE   H2   H  N N 320 
ILE   HA   H  N N 321 
ILE   HB   H  N N 322 
ILE   HG12 H  N N 323 
ILE   HG13 H  N N 324 
ILE   HG21 H  N N 325 
ILE   HG22 H  N N 326 
ILE   HG23 H  N N 327 
ILE   HD11 H  N N 328 
ILE   HD12 H  N N 329 
ILE   HD13 H  N N 330 
ILE   HXT  H  N N 331 
LEU   N    N  N N 332 
LEU   CA   C  N S 333 
LEU   C    C  N N 334 
LEU   O    O  N N 335 
LEU   CB   C  N N 336 
LEU   CG   C  N N 337 
LEU   CD1  C  N N 338 
LEU   CD2  C  N N 339 
LEU   OXT  O  N N 340 
LEU   H    H  N N 341 
LEU   H2   H  N N 342 
LEU   HA   H  N N 343 
LEU   HB2  H  N N 344 
LEU   HB3  H  N N 345 
LEU   HG   H  N N 346 
LEU   HD11 H  N N 347 
LEU   HD12 H  N N 348 
LEU   HD13 H  N N 349 
LEU   HD21 H  N N 350 
LEU   HD22 H  N N 351 
LEU   HD23 H  N N 352 
LEU   HXT  H  N N 353 
LYS   N    N  N N 354 
LYS   CA   C  N S 355 
LYS   C    C  N N 356 
LYS   O    O  N N 357 
LYS   CB   C  N N 358 
LYS   CG   C  N N 359 
LYS   CD   C  N N 360 
LYS   CE   C  N N 361 
LYS   NZ   N  N N 362 
LYS   OXT  O  N N 363 
LYS   H    H  N N 364 
LYS   H2   H  N N 365 
LYS   HA   H  N N 366 
LYS   HB2  H  N N 367 
LYS   HB3  H  N N 368 
LYS   HG2  H  N N 369 
LYS   HG3  H  N N 370 
LYS   HD2  H  N N 371 
LYS   HD3  H  N N 372 
LYS   HE2  H  N N 373 
LYS   HE3  H  N N 374 
LYS   HZ1  H  N N 375 
LYS   HZ2  H  N N 376 
LYS   HZ3  H  N N 377 
LYS   HXT  H  N N 378 
MET   N    N  N N 379 
MET   CA   C  N S 380 
MET   C    C  N N 381 
MET   O    O  N N 382 
MET   CB   C  N N 383 
MET   CG   C  N N 384 
MET   SD   S  N N 385 
MET   CE   C  N N 386 
MET   OXT  O  N N 387 
MET   H    H  N N 388 
MET   H2   H  N N 389 
MET   HA   H  N N 390 
MET   HB2  H  N N 391 
MET   HB3  H  N N 392 
MET   HG2  H  N N 393 
MET   HG3  H  N N 394 
MET   HE1  H  N N 395 
MET   HE2  H  N N 396 
MET   HE3  H  N N 397 
MET   HXT  H  N N 398 
PHE   N    N  N N 399 
PHE   CA   C  N S 400 
PHE   C    C  N N 401 
PHE   O    O  N N 402 
PHE   CB   C  N N 403 
PHE   CG   C  Y N 404 
PHE   CD1  C  Y N 405 
PHE   CD2  C  Y N 406 
PHE   CE1  C  Y N 407 
PHE   CE2  C  Y N 408 
PHE   CZ   C  Y N 409 
PHE   OXT  O  N N 410 
PHE   H    H  N N 411 
PHE   H2   H  N N 412 
PHE   HA   H  N N 413 
PHE   HB2  H  N N 414 
PHE   HB3  H  N N 415 
PHE   HD1  H  N N 416 
PHE   HD2  H  N N 417 
PHE   HE1  H  N N 418 
PHE   HE2  H  N N 419 
PHE   HZ   H  N N 420 
PHE   HXT  H  N N 421 
PRO   N    N  N N 422 
PRO   CA   C  N S 423 
PRO   C    C  N N 424 
PRO   O    O  N N 425 
PRO   CB   C  N N 426 
PRO   CG   C  N N 427 
PRO   CD   C  N N 428 
PRO   OXT  O  N N 429 
PRO   H    H  N N 430 
PRO   HA   H  N N 431 
PRO   HB2  H  N N 432 
PRO   HB3  H  N N 433 
PRO   HG2  H  N N 434 
PRO   HG3  H  N N 435 
PRO   HD2  H  N N 436 
PRO   HD3  H  N N 437 
PRO   HXT  H  N N 438 
SER   N    N  N N 439 
SER   CA   C  N S 440 
SER   C    C  N N 441 
SER   O    O  N N 442 
SER   CB   C  N N 443 
SER   OG   O  N N 444 
SER   OXT  O  N N 445 
SER   H    H  N N 446 
SER   H2   H  N N 447 
SER   HA   H  N N 448 
SER   HB2  H  N N 449 
SER   HB3  H  N N 450 
SER   HG   H  N N 451 
SER   HXT  H  N N 452 
THR   N    N  N N 453 
THR   CA   C  N S 454 
THR   C    C  N N 455 
THR   O    O  N N 456 
THR   CB   C  N R 457 
THR   OG1  O  N N 458 
THR   CG2  C  N N 459 
THR   OXT  O  N N 460 
THR   H    H  N N 461 
THR   H2   H  N N 462 
THR   HA   H  N N 463 
THR   HB   H  N N 464 
THR   HG1  H  N N 465 
THR   HG21 H  N N 466 
THR   HG22 H  N N 467 
THR   HG23 H  N N 468 
THR   HXT  H  N N 469 
TRP   N    N  N N 470 
TRP   CA   C  N S 471 
TRP   C    C  N N 472 
TRP   O    O  N N 473 
TRP   CB   C  N N 474 
TRP   CG   C  Y N 475 
TRP   CD1  C  Y N 476 
TRP   CD2  C  Y N 477 
TRP   NE1  N  Y N 478 
TRP   CE2  C  Y N 479 
TRP   CE3  C  Y N 480 
TRP   CZ2  C  Y N 481 
TRP   CZ3  C  Y N 482 
TRP   CH2  C  Y N 483 
TRP   OXT  O  N N 484 
TRP   H    H  N N 485 
TRP   H2   H  N N 486 
TRP   HA   H  N N 487 
TRP   HB2  H  N N 488 
TRP   HB3  H  N N 489 
TRP   HD1  H  N N 490 
TRP   HE1  H  N N 491 
TRP   HE3  H  N N 492 
TRP   HZ2  H  N N 493 
TRP   HZ3  H  N N 494 
TRP   HH2  H  N N 495 
TRP   HXT  H  N N 496 
TYR   N    N  N N 497 
TYR   CA   C  N S 498 
TYR   C    C  N N 499 
TYR   O    O  N N 500 
TYR   CB   C  N N 501 
TYR   CG   C  Y N 502 
TYR   CD1  C  Y N 503 
TYR   CD2  C  Y N 504 
TYR   CE1  C  Y N 505 
TYR   CE2  C  Y N 506 
TYR   CZ   C  Y N 507 
TYR   OH   O  N N 508 
TYR   OXT  O  N N 509 
TYR   H    H  N N 510 
TYR   H2   H  N N 511 
TYR   HA   H  N N 512 
TYR   HB2  H  N N 513 
TYR   HB3  H  N N 514 
TYR   HD1  H  N N 515 
TYR   HD2  H  N N 516 
TYR   HE1  H  N N 517 
TYR   HE2  H  N N 518 
TYR   HH   H  N N 519 
TYR   HXT  H  N N 520 
VAL   N    N  N N 521 
VAL   CA   C  N S 522 
VAL   C    C  N N 523 
VAL   O    O  N N 524 
VAL   CB   C  N N 525 
VAL   CG1  C  N N 526 
VAL   CG2  C  N N 527 
VAL   OXT  O  N N 528 
VAL   H    H  N N 529 
VAL   H2   H  N N 530 
VAL   HA   H  N N 531 
VAL   HB   H  N N 532 
VAL   HG11 H  N N 533 
VAL   HG12 H  N N 534 
VAL   HG13 H  N N 535 
VAL   HG21 H  N N 536 
VAL   HG22 H  N N 537 
VAL   HG23 H  N N 538 
VAL   HXT  H  N N 539 
# 
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 
A1A4S N37 C36  sing Y N 1   
A1A4S N37 C38  sing Y N 2   
A1A4S C42 C36  doub Y N 3   
A1A4S C42 C41  sing Y N 4   
A1A4S C36 C35  sing Y N 5   
A1A4S C38 C21  doub Y N 6   
A1A4S C41 C40  doub Y N 7   
A1A4S C32 C33  doub Y N 8   
A1A4S C32 N31  sing Y N 9   
A1A4S C26 C27  doub Y N 10  
A1A4S C26 C25  sing Y N 11  
A1A4S C33 C34  sing Y N 12  
A1A4S C35 C21  sing Y N 13  
A1A4S C35 C39  doub Y N 14  
A1A4S C21 C20  sing N N 15  
A1A4S C27 N28  sing Y N 16  
A1A4S N31 C30  doub Y N 17  
A1A4S C34 C23  doub Y N 18  
A1A4S C40 C39  sing Y N 19  
A1A4S C30 C23  sing Y N 20  
A1A4S C23 C11  sing N N 21  
A1A4S C25 C24  doub Y N 22  
A1A4S O22 C11  doub N N 23  
A1A4S C20 C09  sing N N 24  
A1A4S N28 C29  doub Y N 25  
A1A4S C11 N10  sing N N 26  
A1A4S N10 C09  sing N N 27  
A1A4S C24 C29  sing Y N 28  
A1A4S C24 C01  sing N N 29  
A1A4S C09 C08  sing N N 30  
A1A4S C08 S07  sing N N 31  
A1A4S C01 C02  sing N N 32  
A1A4S N04 C03  sing N N 33  
A1A4S N04 C05  sing N N 34  
A1A4S C03 C02  sing N N 35  
A1A4S C15 C19  doub Y N 36  
A1A4S C15 C16  sing Y N 37  
A1A4S C19 C14  sing Y N 38  
A1A4S C06 C05  sing N N 39  
A1A4S C06 S07  sing N N 40  
A1A4S C06 C13  sing N N 41  
A1A4S C05 O12  doub N N 42  
A1A4S C16 C17  doub Y N 43  
A1A4S C14 C13  sing N N 44  
A1A4S C14 C18  doub Y N 45  
A1A4S C17 C18  sing Y N 46  
A1A4S C13 H1   sing N N 47  
A1A4S C13 H2   sing N N 48  
A1A4S C15 H3   sing N N 49  
A1A4S C16 H4   sing N N 50  
A1A4S C17 H5   sing N N 51  
A1A4S C18 H6   sing N N 52  
A1A4S C19 H7   sing N N 53  
A1A4S C20 H8   sing N N 54  
A1A4S C20 H9   sing N N 55  
A1A4S C01 H10  sing N N 56  
A1A4S C01 H11  sing N N 57  
A1A4S C02 H12  sing N N 58  
A1A4S C02 H13  sing N N 59  
A1A4S C03 H14  sing N N 60  
A1A4S C03 H15  sing N N 61  
A1A4S C06 H16  sing N N 62  
A1A4S C08 H17  sing N N 63  
A1A4S C08 H18  sing N N 64  
A1A4S C09 H19  sing N N 65  
A1A4S C25 H20  sing N N 66  
A1A4S C26 H21  sing N N 67  
A1A4S C27 H22  sing N N 68  
A1A4S C29 H23  sing N N 69  
A1A4S C30 H24  sing N N 70  
A1A4S C32 H25  sing N N 71  
A1A4S C33 H26  sing N N 72  
A1A4S C34 H27  sing N N 73  
A1A4S C38 H28  sing N N 74  
A1A4S C39 H29  sing N N 75  
A1A4S C40 H30  sing N N 76  
A1A4S C41 H31  sing N N 77  
A1A4S C42 H32  sing N N 78  
A1A4S N04 H33  sing N N 79  
A1A4S N10 H34  sing N N 80  
A1A4S N37 H35  sing N N 81  
ALA   N   CA   sing N N 82  
ALA   N   H    sing N N 83  
ALA   N   H2   sing N N 84  
ALA   CA  C    sing N N 85  
ALA   CA  CB   sing N N 86  
ALA   CA  HA   sing N N 87  
ALA   C   O    doub N N 88  
ALA   C   OXT  sing N N 89  
ALA   CB  HB1  sing N N 90  
ALA   CB  HB2  sing N N 91  
ALA   CB  HB3  sing N N 92  
ALA   OXT HXT  sing N N 93  
ARG   N   CA   sing N N 94  
ARG   N   H    sing N N 95  
ARG   N   H2   sing N N 96  
ARG   CA  C    sing N N 97  
ARG   CA  CB   sing N N 98  
ARG   CA  HA   sing N N 99  
ARG   C   O    doub N N 100 
ARG   C   OXT  sing N N 101 
ARG   CB  CG   sing N N 102 
ARG   CB  HB2  sing N N 103 
ARG   CB  HB3  sing N N 104 
ARG   CG  CD   sing N N 105 
ARG   CG  HG2  sing N N 106 
ARG   CG  HG3  sing N N 107 
ARG   CD  NE   sing N N 108 
ARG   CD  HD2  sing N N 109 
ARG   CD  HD3  sing N N 110 
ARG   NE  CZ   sing N N 111 
ARG   NE  HE   sing N N 112 
ARG   CZ  NH1  sing N N 113 
ARG   CZ  NH2  doub N N 114 
ARG   NH1 HH11 sing N N 115 
ARG   NH1 HH12 sing N N 116 
ARG   NH2 HH21 sing N N 117 
ARG   NH2 HH22 sing N N 118 
ARG   OXT HXT  sing N N 119 
ASN   N   CA   sing N N 120 
ASN   N   H    sing N N 121 
ASN   N   H2   sing N N 122 
ASN   CA  C    sing N N 123 
ASN   CA  CB   sing N N 124 
ASN   CA  HA   sing N N 125 
ASN   C   O    doub N N 126 
ASN   C   OXT  sing N N 127 
ASN   CB  CG   sing N N 128 
ASN   CB  HB2  sing N N 129 
ASN   CB  HB3  sing N N 130 
ASN   CG  OD1  doub N N 131 
ASN   CG  ND2  sing N N 132 
ASN   ND2 HD21 sing N N 133 
ASN   ND2 HD22 sing N N 134 
ASN   OXT HXT  sing N N 135 
ASP   N   CA   sing N N 136 
ASP   N   H    sing N N 137 
ASP   N   H2   sing N N 138 
ASP   CA  C    sing N N 139 
ASP   CA  CB   sing N N 140 
ASP   CA  HA   sing N N 141 
ASP   C   O    doub N N 142 
ASP   C   OXT  sing N N 143 
ASP   CB  CG   sing N N 144 
ASP   CB  HB2  sing N N 145 
ASP   CB  HB3  sing N N 146 
ASP   CG  OD1  doub N N 147 
ASP   CG  OD2  sing N N 148 
ASP   OD2 HD2  sing N N 149 
ASP   OXT HXT  sing N N 150 
CYS   N   CA   sing N N 151 
CYS   N   H    sing N N 152 
CYS   N   H2   sing N N 153 
CYS   CA  C    sing N N 154 
CYS   CA  CB   sing N N 155 
CYS   CA  HA   sing N N 156 
CYS   C   O    doub N N 157 
CYS   C   OXT  sing N N 158 
CYS   CB  SG   sing N N 159 
CYS   CB  HB2  sing N N 160 
CYS   CB  HB3  sing N N 161 
CYS   SG  HG   sing N N 162 
CYS   OXT HXT  sing N N 163 
GLN   N   CA   sing N N 164 
GLN   N   H    sing N N 165 
GLN   N   H2   sing N N 166 
GLN   CA  C    sing N N 167 
GLN   CA  CB   sing N N 168 
GLN   CA  HA   sing N N 169 
GLN   C   O    doub N N 170 
GLN   C   OXT  sing N N 171 
GLN   CB  CG   sing N N 172 
GLN   CB  HB2  sing N N 173 
GLN   CB  HB3  sing N N 174 
GLN   CG  CD   sing N N 175 
GLN   CG  HG2  sing N N 176 
GLN   CG  HG3  sing N N 177 
GLN   CD  OE1  doub N N 178 
GLN   CD  NE2  sing N N 179 
GLN   NE2 HE21 sing N N 180 
GLN   NE2 HE22 sing N N 181 
GLN   OXT HXT  sing N N 182 
GLU   N   CA   sing N N 183 
GLU   N   H    sing N N 184 
GLU   N   H2   sing N N 185 
GLU   CA  C    sing N N 186 
GLU   CA  CB   sing N N 187 
GLU   CA  HA   sing N N 188 
GLU   C   O    doub N N 189 
GLU   C   OXT  sing N N 190 
GLU   CB  CG   sing N N 191 
GLU   CB  HB2  sing N N 192 
GLU   CB  HB3  sing N N 193 
GLU   CG  CD   sing N N 194 
GLU   CG  HG2  sing N N 195 
GLU   CG  HG3  sing N N 196 
GLU   CD  OE1  doub N N 197 
GLU   CD  OE2  sing N N 198 
GLU   OE2 HE2  sing N N 199 
GLU   OXT HXT  sing N N 200 
GLY   N   CA   sing N N 201 
GLY   N   H    sing N N 202 
GLY   N   H2   sing N N 203 
GLY   CA  C    sing N N 204 
GLY   CA  HA2  sing N N 205 
GLY   CA  HA3  sing N N 206 
GLY   C   O    doub N N 207 
GLY   C   OXT  sing N N 208 
GLY   OXT HXT  sing N N 209 
HEM   CHA C1A  sing N N 210 
HEM   CHA C4D  doub N N 211 
HEM   CHA HHA  sing N N 212 
HEM   CHB C4A  sing N N 213 
HEM   CHB C1B  doub N N 214 
HEM   CHB HHB  sing N N 215 
HEM   CHC C4B  sing N N 216 
HEM   CHC C1C  doub N N 217 
HEM   CHC HHC  sing N N 218 
HEM   CHD C4C  doub N N 219 
HEM   CHD C1D  sing N N 220 
HEM   CHD HHD  sing N N 221 
HEM   C1A C2A  doub Y N 222 
HEM   C1A NA   sing Y N 223 
HEM   C2A C3A  sing Y N 224 
HEM   C2A CAA  sing N N 225 
HEM   C3A C4A  doub Y N 226 
HEM   C3A CMA  sing N N 227 
HEM   C4A NA   sing Y N 228 
HEM   CMA HMA  sing N N 229 
HEM   CMA HMAA sing N N 230 
HEM   CMA HMAB sing N N 231 
HEM   CAA CBA  sing N N 232 
HEM   CAA HAA  sing N N 233 
HEM   CAA HAAA sing N N 234 
HEM   CBA CGA  sing N N 235 
HEM   CBA HBA  sing N N 236 
HEM   CBA HBAA sing N N 237 
HEM   CGA O1A  doub N N 238 
HEM   CGA O2A  sing N N 239 
HEM   C1B C2B  sing N N 240 
HEM   C1B NB   sing N N 241 
HEM   C2B C3B  doub N N 242 
HEM   C2B CMB  sing N N 243 
HEM   C3B C4B  sing N N 244 
HEM   C3B CAB  sing N N 245 
HEM   C4B NB   doub N N 246 
HEM   CMB HMB  sing N N 247 
HEM   CMB HMBA sing N N 248 
HEM   CMB HMBB sing N N 249 
HEM   CAB CBB  doub N N 250 
HEM   CAB HAB  sing N N 251 
HEM   CBB HBB  sing N N 252 
HEM   CBB HBBA sing N N 253 
HEM   C1C C2C  sing Y N 254 
HEM   C1C NC   sing Y N 255 
HEM   C2C C3C  doub Y N 256 
HEM   C2C CMC  sing N N 257 
HEM   C3C C4C  sing Y N 258 
HEM   C3C CAC  sing N N 259 
HEM   C4C NC   sing Y N 260 
HEM   CMC HMC  sing N N 261 
HEM   CMC HMCA sing N N 262 
HEM   CMC HMCB sing N N 263 
HEM   CAC CBC  doub N N 264 
HEM   CAC HAC  sing N N 265 
HEM   CBC HBC  sing N N 266 
HEM   CBC HBCA sing N N 267 
HEM   C1D C2D  sing N N 268 
HEM   C1D ND   doub N N 269 
HEM   C2D C3D  doub N N 270 
HEM   C2D CMD  sing N N 271 
HEM   C3D C4D  sing N N 272 
HEM   C3D CAD  sing N N 273 
HEM   C4D ND   sing N N 274 
HEM   CMD HMD  sing N N 275 
HEM   CMD HMDA sing N N 276 
HEM   CMD HMDB sing N N 277 
HEM   CAD CBD  sing N N 278 
HEM   CAD HAD  sing N N 279 
HEM   CAD HADA sing N N 280 
HEM   CBD CGD  sing N N 281 
HEM   CBD HBD  sing N N 282 
HEM   CBD HBDA sing N N 283 
HEM   CGD O1D  doub N N 284 
HEM   CGD O2D  sing N N 285 
HEM   O2A H2A  sing N N 286 
HEM   O2D H2D  sing N N 287 
HEM   FE  NA   sing N N 288 
HEM   FE  NB   sing N N 289 
HEM   FE  NC   sing N N 290 
HEM   FE  ND   sing N N 291 
HIS   N   CA   sing N N 292 
HIS   N   H    sing N N 293 
HIS   N   H2   sing N N 294 
HIS   CA  C    sing N N 295 
HIS   CA  CB   sing N N 296 
HIS   CA  HA   sing N N 297 
HIS   C   O    doub N N 298 
HIS   C   OXT  sing N N 299 
HIS   CB  CG   sing N N 300 
HIS   CB  HB2  sing N N 301 
HIS   CB  HB3  sing N N 302 
HIS   CG  ND1  sing Y N 303 
HIS   CG  CD2  doub Y N 304 
HIS   ND1 CE1  doub Y N 305 
HIS   ND1 HD1  sing N N 306 
HIS   CD2 NE2  sing Y N 307 
HIS   CD2 HD2  sing N N 308 
HIS   CE1 NE2  sing Y N 309 
HIS   CE1 HE1  sing N N 310 
HIS   NE2 HE2  sing N N 311 
HIS   OXT HXT  sing N N 312 
ILE   N   CA   sing N N 313 
ILE   N   H    sing N N 314 
ILE   N   H2   sing N N 315 
ILE   CA  C    sing N N 316 
ILE   CA  CB   sing N N 317 
ILE   CA  HA   sing N N 318 
ILE   C   O    doub N N 319 
ILE   C   OXT  sing N N 320 
ILE   CB  CG1  sing N N 321 
ILE   CB  CG2  sing N N 322 
ILE   CB  HB   sing N N 323 
ILE   CG1 CD1  sing N N 324 
ILE   CG1 HG12 sing N N 325 
ILE   CG1 HG13 sing N N 326 
ILE   CG2 HG21 sing N N 327 
ILE   CG2 HG22 sing N N 328 
ILE   CG2 HG23 sing N N 329 
ILE   CD1 HD11 sing N N 330 
ILE   CD1 HD12 sing N N 331 
ILE   CD1 HD13 sing N N 332 
ILE   OXT HXT  sing N N 333 
LEU   N   CA   sing N N 334 
LEU   N   H    sing N N 335 
LEU   N   H2   sing N N 336 
LEU   CA  C    sing N N 337 
LEU   CA  CB   sing N N 338 
LEU   CA  HA   sing N N 339 
LEU   C   O    doub N N 340 
LEU   C   OXT  sing N N 341 
LEU   CB  CG   sing N N 342 
LEU   CB  HB2  sing N N 343 
LEU   CB  HB3  sing N N 344 
LEU   CG  CD1  sing N N 345 
LEU   CG  CD2  sing N N 346 
LEU   CG  HG   sing N N 347 
LEU   CD1 HD11 sing N N 348 
LEU   CD1 HD12 sing N N 349 
LEU   CD1 HD13 sing N N 350 
LEU   CD2 HD21 sing N N 351 
LEU   CD2 HD22 sing N N 352 
LEU   CD2 HD23 sing N N 353 
LEU   OXT HXT  sing N N 354 
LYS   N   CA   sing N N 355 
LYS   N   H    sing N N 356 
LYS   N   H2   sing N N 357 
LYS   CA  C    sing N N 358 
LYS   CA  CB   sing N N 359 
LYS   CA  HA   sing N N 360 
LYS   C   O    doub N N 361 
LYS   C   OXT  sing N N 362 
LYS   CB  CG   sing N N 363 
LYS   CB  HB2  sing N N 364 
LYS   CB  HB3  sing N N 365 
LYS   CG  CD   sing N N 366 
LYS   CG  HG2  sing N N 367 
LYS   CG  HG3  sing N N 368 
LYS   CD  CE   sing N N 369 
LYS   CD  HD2  sing N N 370 
LYS   CD  HD3  sing N N 371 
LYS   CE  NZ   sing N N 372 
LYS   CE  HE2  sing N N 373 
LYS   CE  HE3  sing N N 374 
LYS   NZ  HZ1  sing N N 375 
LYS   NZ  HZ2  sing N N 376 
LYS   NZ  HZ3  sing N N 377 
LYS   OXT HXT  sing N N 378 
MET   N   CA   sing N N 379 
MET   N   H    sing N N 380 
MET   N   H2   sing N N 381 
MET   CA  C    sing N N 382 
MET   CA  CB   sing N N 383 
MET   CA  HA   sing N N 384 
MET   C   O    doub N N 385 
MET   C   OXT  sing N N 386 
MET   CB  CG   sing N N 387 
MET   CB  HB2  sing N N 388 
MET   CB  HB3  sing N N 389 
MET   CG  SD   sing N N 390 
MET   CG  HG2  sing N N 391 
MET   CG  HG3  sing N N 392 
MET   SD  CE   sing N N 393 
MET   CE  HE1  sing N N 394 
MET   CE  HE2  sing N N 395 
MET   CE  HE3  sing N N 396 
MET   OXT HXT  sing N N 397 
PHE   N   CA   sing N N 398 
PHE   N   H    sing N N 399 
PHE   N   H2   sing N N 400 
PHE   CA  C    sing N N 401 
PHE   CA  CB   sing N N 402 
PHE   CA  HA   sing N N 403 
PHE   C   O    doub N N 404 
PHE   C   OXT  sing N N 405 
PHE   CB  CG   sing N N 406 
PHE   CB  HB2  sing N N 407 
PHE   CB  HB3  sing N N 408 
PHE   CG  CD1  doub Y N 409 
PHE   CG  CD2  sing Y N 410 
PHE   CD1 CE1  sing Y N 411 
PHE   CD1 HD1  sing N N 412 
PHE   CD2 CE2  doub Y N 413 
PHE   CD2 HD2  sing N N 414 
PHE   CE1 CZ   doub Y N 415 
PHE   CE1 HE1  sing N N 416 
PHE   CE2 CZ   sing Y N 417 
PHE   CE2 HE2  sing N N 418 
PHE   CZ  HZ   sing N N 419 
PHE   OXT HXT  sing N N 420 
PRO   N   CA   sing N N 421 
PRO   N   CD   sing N N 422 
PRO   N   H    sing N N 423 
PRO   CA  C    sing N N 424 
PRO   CA  CB   sing N N 425 
PRO   CA  HA   sing N N 426 
PRO   C   O    doub N N 427 
PRO   C   OXT  sing N N 428 
PRO   CB  CG   sing N N 429 
PRO   CB  HB2  sing N N 430 
PRO   CB  HB3  sing N N 431 
PRO   CG  CD   sing N N 432 
PRO   CG  HG2  sing N N 433 
PRO   CG  HG3  sing N N 434 
PRO   CD  HD2  sing N N 435 
PRO   CD  HD3  sing N N 436 
PRO   OXT HXT  sing N N 437 
SER   N   CA   sing N N 438 
SER   N   H    sing N N 439 
SER   N   H2   sing N N 440 
SER   CA  C    sing N N 441 
SER   CA  CB   sing N N 442 
SER   CA  HA   sing N N 443 
SER   C   O    doub N N 444 
SER   C   OXT  sing N N 445 
SER   CB  OG   sing N N 446 
SER   CB  HB2  sing N N 447 
SER   CB  HB3  sing N N 448 
SER   OG  HG   sing N N 449 
SER   OXT HXT  sing N N 450 
THR   N   CA   sing N N 451 
THR   N   H    sing N N 452 
THR   N   H2   sing N N 453 
THR   CA  C    sing N N 454 
THR   CA  CB   sing N N 455 
THR   CA  HA   sing N N 456 
THR   C   O    doub N N 457 
THR   C   OXT  sing N N 458 
THR   CB  OG1  sing N N 459 
THR   CB  CG2  sing N N 460 
THR   CB  HB   sing N N 461 
THR   OG1 HG1  sing N N 462 
THR   CG2 HG21 sing N N 463 
THR   CG2 HG22 sing N N 464 
THR   CG2 HG23 sing N N 465 
THR   OXT HXT  sing N N 466 
TRP   N   CA   sing N N 467 
TRP   N   H    sing N N 468 
TRP   N   H2   sing N N 469 
TRP   CA  C    sing N N 470 
TRP   CA  CB   sing N N 471 
TRP   CA  HA   sing N N 472 
TRP   C   O    doub N N 473 
TRP   C   OXT  sing N N 474 
TRP   CB  CG   sing N N 475 
TRP   CB  HB2  sing N N 476 
TRP   CB  HB3  sing N N 477 
TRP   CG  CD1  doub Y N 478 
TRP   CG  CD2  sing Y N 479 
TRP   CD1 NE1  sing Y N 480 
TRP   CD1 HD1  sing N N 481 
TRP   CD2 CE2  doub Y N 482 
TRP   CD2 CE3  sing Y N 483 
TRP   NE1 CE2  sing Y N 484 
TRP   NE1 HE1  sing N N 485 
TRP   CE2 CZ2  sing Y N 486 
TRP   CE3 CZ3  doub Y N 487 
TRP   CE3 HE3  sing N N 488 
TRP   CZ2 CH2  doub Y N 489 
TRP   CZ2 HZ2  sing N N 490 
TRP   CZ3 CH2  sing Y N 491 
TRP   CZ3 HZ3  sing N N 492 
TRP   CH2 HH2  sing N N 493 
TRP   OXT HXT  sing N N 494 
TYR   N   CA   sing N N 495 
TYR   N   H    sing N N 496 
TYR   N   H2   sing N N 497 
TYR   CA  C    sing N N 498 
TYR   CA  CB   sing N N 499 
TYR   CA  HA   sing N N 500 
TYR   C   O    doub N N 501 
TYR   C   OXT  sing N N 502 
TYR   CB  CG   sing N N 503 
TYR   CB  HB2  sing N N 504 
TYR   CB  HB3  sing N N 505 
TYR   CG  CD1  doub Y N 506 
TYR   CG  CD2  sing Y N 507 
TYR   CD1 CE1  sing Y N 508 
TYR   CD1 HD1  sing N N 509 
TYR   CD2 CE2  doub Y N 510 
TYR   CD2 HD2  sing N N 511 
TYR   CE1 CZ   doub Y N 512 
TYR   CE1 HE1  sing N N 513 
TYR   CE2 CZ   sing Y N 514 
TYR   CE2 HE2  sing N N 515 
TYR   CZ  OH   sing N N 516 
TYR   OH  HH   sing N N 517 
TYR   OXT HXT  sing N N 518 
VAL   N   CA   sing N N 519 
VAL   N   H    sing N N 520 
VAL   N   H2   sing N N 521 
VAL   CA  C    sing N N 522 
VAL   CA  CB   sing N N 523 
VAL   CA  HA   sing N N 524 
VAL   C   O    doub N N 525 
VAL   C   OXT  sing N N 526 
VAL   CB  CG1  sing N N 527 
VAL   CB  CG2  sing N N 528 
VAL   CB  HB   sing N N 529 
VAL   CG1 HG11 sing N N 530 
VAL   CG1 HG12 sing N N 531 
VAL   CG1 HG13 sing N N 532 
VAL   CG2 HG21 sing N N 533 
VAL   CG2 HG22 sing N N 534 
VAL   CG2 HG23 sing N N 535 
VAL   OXT HXT  sing N N 536 
# 
_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                    9COV 
_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]   0.013263 
_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]   0.010023 
_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]   0.008154 
_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   . HIS   A 1 8   ? -29.544 8.640   -14.834 1.00 184.96 ? 28  HIS   A N   1 
ATOM   2    C  CA  . HIS   A 1 8   ? -28.594 9.736   -14.644 1.00 192.04 ? 28  HIS   A CA  1 
ATOM   3    C  C   . HIS   A 1 8   ? -27.167 9.299   -14.944 1.00 182.57 ? 28  HIS   A C   1 
ATOM   4    O  O   . HIS   A 1 8   ? -26.412 9.998   -15.628 1.00 194.28 ? 28  HIS   A O   1 
ATOM   5    C  CB  . HIS   A 1 8   ? -28.670 10.291  -13.211 1.00 200.63 ? 28  HIS   A CB  1 
ATOM   6    C  CG  . HIS   A 1 8   ? -28.322 9.285   -12.156 1.00 196.29 ? 28  HIS   A CG  1 
ATOM   7    N  ND1 . HIS   A 1 8   ? -27.245 9.436   -11.312 1.00 202.03 ? 28  HIS   A ND1 1 
ATOM   8    C  CD2 . HIS   A 1 8   ? -28.910 8.117   -11.803 1.00 191.00 ? 28  HIS   A CD2 1 
ATOM   9    C  CE1 . HIS   A 1 8   ? -27.182 8.408   -10.484 1.00 196.21 ? 28  HIS   A CE1 1 
ATOM   10   N  NE2 . HIS   A 1 8   ? -28.181 7.592   -10.761 1.00 201.43 ? 28  HIS   A NE2 1 
ATOM   11   N  N   . SER   A 1 9   ? -26.797 8.137   -14.419 1.00 175.86 ? 29  SER   A N   1 
ATOM   12   C  CA  . SER   A 1 9   ? -25.480 7.563   -14.636 1.00 166.40 ? 29  SER   A CA  1 
ATOM   13   C  C   . SER   A 1 9   ? -25.403 6.757   -15.928 1.00 151.47 ? 29  SER   A C   1 
ATOM   14   O  O   . SER   A 1 9   ? -24.478 5.951   -16.088 1.00 137.17 ? 29  SER   A O   1 
ATOM   15   C  CB  . SER   A 1 9   ? -25.081 6.687   -13.441 1.00 158.24 ? 29  SER   A CB  1 
ATOM   16   O  OG  . SER   A 1 9   ? -26.011 5.639   -13.242 1.00 154.96 ? 29  SER   A OG  1 
ATOM   17   N  N   . HIS   A 1 10  ? -26.333 6.968   -16.860 1.00 140.94 ? 30  HIS   A N   1 
ATOM   18   C  CA  . HIS   A 1 10  ? -26.358 6.226   -18.117 1.00 136.83 ? 30  HIS   A CA  1 
ATOM   19   C  C   . HIS   A 1 10  ? -25.517 6.868   -19.219 1.00 142.55 ? 30  HIS   A C   1 
ATOM   20   O  O   . HIS   A 1 10  ? -25.653 6.483   -20.384 1.00 140.80 ? 30  HIS   A O   1 
ATOM   21   C  CB  . HIS   A 1 10  ? -27.804 6.053   -18.605 1.00 135.35 ? 30  HIS   A CB  1 
ATOM   22   C  CG  . HIS   A 1 10  ? -28.511 4.880   -17.997 1.00 139.46 ? 30  HIS   A CG  1 
ATOM   23   N  ND1 . HIS   A 1 10  ? -29.673 4.353   -18.519 1.00 140.54 ? 30  HIS   A ND1 1 
ATOM   24   C  CD2 . HIS   A 1 10  ? -28.214 4.130   -16.910 1.00 133.25 ? 30  HIS   A CD2 1 
ATOM   25   C  CE1 . HIS   A 1 10  ? -30.062 3.331   -17.777 1.00 136.78 ? 30  HIS   A CE1 1 
ATOM   26   N  NE2 . HIS   A 1 10  ? -29.194 3.175   -16.795 1.00 132.51 ? 30  HIS   A NE2 1 
ATOM   27   N  N   . GLY   A 1 11  ? -24.648 7.820   -18.882 1.00 133.40 ? 31  GLY   A N   1 
ATOM   28   C  CA  . GLY   A 1 11  ? -23.763 8.425   -19.857 1.00 143.44 ? 31  GLY   A CA  1 
ATOM   29   C  C   . GLY   A 1 11  ? -22.297 8.134   -19.637 1.00 134.34 ? 31  GLY   A C   1 
ATOM   30   O  O   . GLY   A 1 11  ? -21.449 8.739   -20.311 1.00 140.74 ? 31  GLY   A O   1 
ATOM   31   N  N   . LEU   A 1 12  ? -21.964 7.224   -18.714 1.00 127.34 ? 32  LEU   A N   1 
ATOM   32   C  CA  . LEU   A 1 12  ? -20.570 6.967   -18.380 1.00 125.45 ? 32  LEU   A CA  1 
ATOM   33   C  C   . LEU   A 1 12  ? -19.789 6.475   -19.591 1.00 128.87 ? 32  LEU   A C   1 
ATOM   34   O  O   . LEU   A 1 12  ? -18.645 6.890   -19.811 1.00 131.06 ? 32  LEU   A O   1 
ATOM   35   C  CB  . LEU   A 1 12  ? -20.496 5.962   -17.233 1.00 111.36 ? 32  LEU   A CB  1 
ATOM   36   C  CG  . LEU   A 1 12  ? -19.100 5.482   -16.815 1.00 123.32 ? 32  LEU   A CG  1 
ATOM   37   C  CD1 . LEU   A 1 12  ? -18.167 6.650   -16.500 1.00 124.64 ? 32  LEU   A CD1 1 
ATOM   38   C  CD2 . LEU   A 1 12  ? -19.175 4.516   -15.635 1.00 119.83 ? 32  LEU   A CD2 1 
ATOM   39   N  N   . PHE   A 1 13  ? -20.388 5.593   -20.393 1.00 121.68 ? 33  PHE   A N   1 
ATOM   40   C  CA  . PHE   A 1 13  ? -19.694 5.098   -21.575 1.00 127.23 ? 33  PHE   A CA  1 
ATOM   41   C  C   . PHE   A 1 13  ? -19.841 6.043   -22.760 1.00 128.92 ? 33  PHE   A C   1 
ATOM   42   O  O   . PHE   A 1 13  ? -18.957 6.084   -23.624 1.00 127.66 ? 33  PHE   A O   1 
ATOM   43   C  CB  . PHE   A 1 13  ? -20.195 3.700   -21.929 1.00 123.43 ? 33  PHE   A CB  1 
ATOM   44   C  CG  . PHE   A 1 13  ? -19.957 2.689   -20.845 1.00 116.54 ? 33  PHE   A CG  1 
ATOM   45   C  CD1 . PHE   A 1 13  ? -18.670 2.322   -20.492 1.00 112.62 ? 33  PHE   A CD1 1 
ATOM   46   C  CD2 . PHE   A 1 13  ? -21.020 2.109   -20.174 1.00 114.24 ? 33  PHE   A CD2 1 
ATOM   47   C  CE1 . PHE   A 1 13  ? -18.450 1.392   -19.490 1.00 111.60 ? 33  PHE   A CE1 1 
ATOM   48   C  CE2 . PHE   A 1 13  ? -20.805 1.178   -19.173 1.00 116.87 ? 33  PHE   A CE2 1 
ATOM   49   C  CZ  . PHE   A 1 13  ? -19.520 0.820   -18.831 1.00 106.69 ? 33  PHE   A CZ  1 
ATOM   50   N  N   . LYS   A 1 14  ? -20.939 6.801   -22.825 1.00 135.51 ? 34  LYS   A N   1 
ATOM   51   C  CA  . LYS   A 1 14  ? -21.007 7.904   -23.778 1.00 144.99 ? 34  LYS   A CA  1 
ATOM   52   C  C   . LYS   A 1 14  ? -19.903 8.919   -23.509 1.00 145.19 ? 34  LYS   A C   1 
ATOM   53   O  O   . LYS   A 1 14  ? -19.342 9.505   -24.443 1.00 151.05 ? 34  LYS   A O   1 
ATOM   54   C  CB  . LYS   A 1 14  ? -22.378 8.578   -23.714 1.00 153.85 ? 34  LYS   A CB  1 
ATOM   55   C  CG  . LYS   A 1 14  ? -23.529 7.736   -24.238 1.00 149.34 ? 34  LYS   A CG  1 
ATOM   56   C  CD  . LYS   A 1 14  ? -24.773 8.593   -24.425 1.00 160.68 ? 34  LYS   A CD  1 
ATOM   57   C  CE  . LYS   A 1 14  ? -25.925 7.797   -25.018 1.00 162.95 ? 34  LYS   A CE  1 
ATOM   58   N  NZ  . LYS   A 1 14  ? -27.113 8.661   -25.263 1.00 149.36 ? 34  LYS   A NZ  1 
ATOM   59   N  N   . LYS   A 1 15  ? -19.576 9.136   -22.234 1.00 135.65 ? 35  LYS   A N   1 
ATOM   60   C  CA  . LYS   A 1 15  ? -18.489 10.043  -21.882 1.00 136.39 ? 35  LYS   A CA  1 
ATOM   61   C  C   . LYS   A 1 15  ? -17.137 9.459   -22.276 1.00 140.03 ? 35  LYS   A C   1 
ATOM   62   O  O   . LYS   A 1 15  ? -16.361 10.088  -23.003 1.00 143.75 ? 35  LYS   A O   1 
ATOM   63   C  CB  . LYS   A 1 15  ? -18.526 10.343  -20.382 1.00 139.09 ? 35  LYS   A CB  1 
ATOM   64   C  CG  . LYS   A 1 15  ? -17.236 10.940  -19.846 1.00 149.52 ? 35  LYS   A CG  1 
ATOM   65   C  CD  . LYS   A 1 15  ? -17.001 10.548  -18.397 1.00 155.01 ? 35  LYS   A CD  1 
ATOM   66   C  CE  . LYS   A 1 15  ? -15.570 10.847  -17.977 1.00 156.46 ? 35  LYS   A CE  1 
ATOM   67   N  NZ  . LYS   A 1 15  ? -15.274 10.344  -16.609 1.00 164.44 ? 35  LYS   A NZ  1 
ATOM   68   N  N   . LEU   A 1 16  ? -16.841 8.246   -21.805 1.00 144.16 ? 36  LEU   A N   1 
ATOM   69   C  CA  . LEU   A 1 16  ? -15.540 7.621   -22.018 1.00 143.79 ? 36  LEU   A CA  1 
ATOM   70   C  C   . LEU   A 1 16  ? -15.264 7.271   -23.476 1.00 142.12 ? 36  LEU   A C   1 
ATOM   71   O  O   . LEU   A 1 16  ? -14.185 6.741   -23.762 1.00 142.83 ? 36  LEU   A O   1 
ATOM   72   C  CB  . LEU   A 1 16  ? -15.423 6.356   -21.163 1.00 136.93 ? 36  LEU   A CB  1 
ATOM   73   C  CG  . LEU   A 1 16  ? -15.291 6.535   -19.649 1.00 138.89 ? 36  LEU   A CG  1 
ATOM   74   C  CD1 . LEU   A 1 16  ? -15.172 5.184   -18.960 1.00 129.57 ? 36  LEU   A CD1 1 
ATOM   75   C  CD2 . LEU   A 1 16  ? -14.096 7.413   -19.318 1.00 137.52 ? 36  LEU   A CD2 1 
ATOM   76   N  N   . GLY   A 1 17  ? -16.189 7.545   -24.393 1.00 139.59 ? 37  GLY   A N   1 
ATOM   77   C  CA  . GLY   A 1 17  ? -16.018 7.125   -25.770 1.00 145.91 ? 37  GLY   A CA  1 
ATOM   78   C  C   . GLY   A 1 17  ? -15.974 5.627   -25.961 1.00 139.99 ? 37  GLY   A C   1 
ATOM   79   O  O   . GLY   A 1 17  ? -15.247 5.143   -26.833 1.00 143.72 ? 37  GLY   A O   1 
ATOM   80   N  N   . ILE   A 1 18  ? -16.728 4.879   -25.168 1.00 122.02 ? 38  ILE   A N   1 
ATOM   81   C  CA  . ILE   A 1 18  ? -16.757 3.421   -25.217 1.00 128.96 ? 38  ILE   A CA  1 
ATOM   82   C  C   . ILE   A 1 18  ? -18.111 3.000   -25.781 1.00 128.55 ? 38  ILE   A C   1 
ATOM   83   O  O   . ILE   A 1 18  ? -19.150 3.399   -25.236 1.00 118.25 ? 38  ILE   A O   1 
ATOM   84   C  CB  . ILE   A 1 18  ? -16.514 2.805   -23.829 1.00 128.59 ? 38  ILE   A CB  1 
ATOM   85   C  CG1 . ILE   A 1 18  ? -15.117 3.178   -23.323 1.00 124.23 ? 38  ILE   A CG1 1 
ATOM   86   C  CG2 . ILE   A 1 18  ? -16.683 1.292   -23.871 1.00 119.08 ? 38  ILE   A CG2 1 
ATOM   87   C  CD1 . ILE   A 1 18  ? -14.835 2.723   -21.908 1.00 133.39 ? 38  ILE   A CD1 1 
ATOM   88   N  N   . PRO   A 1 19  ? -18.155 2.211   -26.854 1.00 126.37 ? 39  PRO   A N   1 
ATOM   89   C  CA  . PRO   A 1 19  ? -19.443 1.887   -27.474 1.00 131.48 ? 39  PRO   A CA  1 
ATOM   90   C  C   . PRO   A 1 19  ? -20.238 0.900   -26.635 1.00 125.88 ? 39  PRO   A C   1 
ATOM   91   O  O   . PRO   A 1 19  ? -19.722 0.243   -25.729 1.00 117.47 ? 39  PRO   A O   1 
ATOM   92   C  CB  . PRO   A 1 19  ? -19.046 1.278   -28.822 1.00 129.15 ? 39  PRO   A CB  1 
ATOM   93   C  CG  . PRO   A 1 19  ? -17.704 0.683   -28.575 1.00 125.26 ? 39  PRO   A CG  1 
ATOM   94   C  CD  . PRO   A 1 19  ? -17.026 1.586   -27.566 1.00 124.42 ? 39  PRO   A CD  1 
ATOM   95   N  N   . GLY   A 1 20  ? -21.526 0.807   -26.952 1.00 124.39 ? 40  GLY   A N   1 
ATOM   96   C  CA  . GLY   A 1 20  ? -22.408 -0.106  -26.268 1.00 128.86 ? 40  GLY   A CA  1 
ATOM   97   C  C   . GLY   A 1 20  ? -23.865 0.164   -26.572 1.00 128.11 ? 40  GLY   A C   1 
ATOM   98   O  O   . GLY   A 1 20  ? -24.234 1.235   -27.063 1.00 133.58 ? 40  GLY   A O   1 
ATOM   99   N  N   . PRO   A 1 21  ? -24.726 -0.810  -26.283 1.00 128.45 ? 41  PRO   A N   1 
ATOM   100  C  CA  . PRO   A 1 21  ? -26.155 -0.625  -26.552 1.00 125.39 ? 41  PRO   A CA  1 
ATOM   101  C  C   . PRO   A 1 21  ? -26.735 0.503   -25.715 1.00 117.14 ? 41  PRO   A C   1 
ATOM   102  O  O   . PRO   A 1 21  ? -26.415 0.657   -24.534 1.00 107.70 ? 41  PRO   A O   1 
ATOM   103  C  CB  . PRO   A 1 21  ? -26.767 -1.979  -26.177 1.00 124.79 ? 41  PRO   A CB  1 
ATOM   104  C  CG  . PRO   A 1 21  ? -25.786 -2.586  -25.225 1.00 128.40 ? 41  PRO   A CG  1 
ATOM   105  C  CD  . PRO   A 1 21  ? -24.438 -2.129  -25.696 1.00 122.23 ? 41  PRO   A CD  1 
ATOM   106  N  N   . THR   A 1 22  ? -27.596 1.290   -26.345 1.00 123.96 ? 42  THR   A N   1 
ATOM   107  C  CA  . THR   A 1 22  ? -28.180 2.457   -25.700 1.00 115.62 ? 42  THR   A CA  1 
ATOM   108  C  C   . THR   A 1 22  ? -29.083 2.026   -24.555 1.00 105.63 ? 42  THR   A C   1 
ATOM   109  O  O   . THR   A 1 22  ? -30.073 1.319   -24.789 1.00 104.84 ? 42  THR   A O   1 
ATOM   110  C  CB  . THR   A 1 22  ? -28.976 3.284   -26.702 1.00 120.40 ? 42  THR   A CB  1 
ATOM   111  O  OG1 . THR   A 1 22  ? -28.135 3.635   -27.809 1.00 119.91 ? 42  THR   A OG1 1 
ATOM   112  C  CG2 . THR   A 1 22  ? -29.493 4.553   -26.041 1.00 114.14 ? 42  THR   A CG2 1 
ATOM   113  N  N   . PRO   A 1 23  ? -28.795 2.425   -23.320 1.00 101.94 ? 43  PRO   A N   1 
ATOM   114  C  CA  . PRO   A 1 23  ? -29.595 1.951   -22.188 1.00 107.42 ? 43  PRO   A CA  1 
ATOM   115  C  C   . PRO   A 1 23  ? -30.912 2.699   -22.065 1.00 117.48 ? 43  PRO   A C   1 
ATOM   116  O  O   . PRO   A 1 23  ? -30.978 3.920   -22.230 1.00 107.85 ? 43  PRO   A O   1 
ATOM   117  C  CB  . PRO   A 1 23  ? -28.689 2.228   -20.982 1.00 106.34 ? 43  PRO   A CB  1 
ATOM   118  C  CG  . PRO   A 1 23  ? -27.873 3.409   -21.407 1.00 111.95 ? 43  PRO   A CG  1 
ATOM   119  C  CD  . PRO   A 1 23  ? -27.634 3.223   -22.886 1.00 108.10 ? 43  PRO   A CD  1 
ATOM   120  N  N   . LEU   A 1 24  ? -31.968 1.944   -21.779 1.00 110.50 ? 44  LEU   A N   1 
ATOM   121  C  CA  . LEU   A 1 24  ? -33.231 2.540   -21.386 1.00 113.06 ? 44  LEU   A CA  1 
ATOM   122  C  C   . LEU   A 1 24  ? -33.150 2.992   -19.929 1.00 113.97 ? 44  LEU   A C   1 
ATOM   123  O  O   . LEU   A 1 24  ? -32.464 2.363   -19.119 1.00 114.36 ? 44  LEU   A O   1 
ATOM   124  C  CB  . LEU   A 1 24  ? -34.371 1.540   -21.552 1.00 114.18 ? 44  LEU   A CB  1 
ATOM   125  C  CG  . LEU   A 1 24  ? -34.681 1.004   -22.950 1.00 117.75 ? 44  LEU   A CG  1 
ATOM   126  C  CD1 . LEU   A 1 24  ? -35.691 -0.130  -22.864 1.00 118.01 ? 44  LEU   A CD1 1 
ATOM   127  C  CD2 . LEU   A 1 24  ? -35.202 2.115   -23.844 1.00 126.58 ? 44  LEU   A CD2 1 
ATOM   128  N  N   . PRO   A 1 25  ? -33.831 4.080   -19.573 1.00 128.46 ? 45  PRO   A N   1 
ATOM   129  C  CA  . PRO   A 1 25  ? -33.783 4.551   -18.183 1.00 121.88 ? 45  PRO   A CA  1 
ATOM   130  C  C   . PRO   A 1 25  ? -34.214 3.468   -17.205 1.00 116.79 ? 45  PRO   A C   1 
ATOM   131  O  O   . PRO   A 1 25  ? -35.108 2.667   -17.489 1.00 117.57 ? 45  PRO   A O   1 
ATOM   132  C  CB  . PRO   A 1 25  ? -34.755 5.735   -18.179 1.00 110.72 ? 45  PRO   A CB  1 
ATOM   133  C  CG  . PRO   A 1 25  ? -34.752 6.217   -19.593 1.00 119.01 ? 45  PRO   A CG  1 
ATOM   134  C  CD  . PRO   A 1 25  ? -34.607 4.985   -20.438 1.00 116.93 ? 45  PRO   A CD  1 
ATOM   135  N  N   . PHE   A 1 26  ? -33.542 3.444   -16.051 1.00 122.93 ? 46  PHE   A N   1 
ATOM   136  C  CA  . PHE   A 1 26  ? -33.781 2.493   -14.968 1.00 119.54 ? 46  PHE   A CA  1 
ATOM   137  C  C   . PHE   A 1 26  ? -33.371 1.074   -15.344 1.00 114.27 ? 46  PHE   A C   1 
ATOM   138  O  O   . PHE   A 1 26  ? -32.634 0.423   -14.599 1.00 113.58 ? 46  PHE   A O   1 
ATOM   139  C  CB  . PHE   A 1 26  ? -35.248 2.511   -14.528 1.00 118.23 ? 46  PHE   A CB  1 
ATOM   140  C  CG  . PHE   A 1 26  ? -35.678 3.809   -13.916 1.00 129.14 ? 46  PHE   A CG  1 
ATOM   141  C  CD1 . PHE   A 1 26  ? -35.401 4.087   -12.589 1.00 140.81 ? 46  PHE   A CD1 1 
ATOM   142  C  CD2 . PHE   A 1 26  ? -36.364 4.750   -14.666 1.00 124.39 ? 46  PHE   A CD2 1 
ATOM   143  C  CE1 . PHE   A 1 26  ? -35.799 5.282   -12.020 1.00 146.42 ? 46  PHE   A CE1 1 
ATOM   144  C  CE2 . PHE   A 1 26  ? -36.767 5.949   -14.105 1.00 132.59 ? 46  PHE   A CE2 1 
ATOM   145  C  CZ  . PHE   A 1 26  ? -36.484 6.216   -12.779 1.00 142.13 ? 46  PHE   A CZ  1 
ATOM   146  N  N   . LEU   A 1 27  ? -33.842 0.578   -16.489 1.00 106.85 ? 47  LEU   A N   1 
ATOM   147  C  CA  . LEU   A 1 27  ? -33.539 -0.794  -16.875 1.00 111.33 ? 47  LEU   A CA  1 
ATOM   148  C  C   . LEU   A 1 27  ? -32.103 -0.971  -17.349 1.00 107.33 ? 47  LEU   A C   1 
ATOM   149  O  O   . LEU   A 1 27  ? -31.570 -2.083  -17.264 1.00 108.36 ? 47  LEU   A O   1 
ATOM   150  C  CB  . LEU   A 1 27  ? -34.498 -1.254  -17.974 1.00 116.15 ? 47  LEU   A CB  1 
ATOM   151  C  CG  . LEU   A 1 27  ? -35.985 -1.351  -17.622 1.00 104.87 ? 47  LEU   A CG  1 
ATOM   152  C  CD1 . LEU   A 1 27  ? -36.769 -1.964  -18.776 1.00 101.74 ? 47  LEU   A CD1 1 
ATOM   153  C  CD2 . LEU   A 1 27  ? -36.197 -2.145  -16.342 1.00 113.56 ? 47  LEU   A CD2 1 
ATOM   154  N  N   . GLY   A 1 28  ? -31.468 0.082   -17.840 1.00 114.69 ? 48  GLY   A N   1 
ATOM   155  C  CA  . GLY   A 1 28  ? -30.195 -0.104  -18.511 1.00 110.17 ? 48  GLY   A CA  1 
ATOM   156  C  C   . GLY   A 1 28  ? -30.418 -0.889  -19.788 1.00 106.68 ? 48  GLY   A C   1 
ATOM   157  O  O   . GLY   A 1 28  ? -31.194 -0.486  -20.665 1.00 102.94 ? 48  GLY   A O   1 
ATOM   158  N  N   . ASN   A 1 29  ? -29.750 -2.040  -19.895 1.00 99.98  ? 49  ASN   A N   1 
ATOM   159  C  CA  . ASN   A 1 29  ? -29.852 -2.905  -21.065 1.00 91.33  ? 49  ASN   A CA  1 
ATOM   160  C  C   . ASN   A 1 29  ? -30.345 -4.301  -20.705 1.00 102.05 ? 49  ASN   A C   1 
ATOM   161  O  O   . ASN   A 1 29  ? -30.104 -5.250  -21.458 1.00 107.38 ? 49  ASN   A O   1 
ATOM   162  C  CB  . ASN   A 1 29  ? -28.503 -2.994  -21.781 1.00 102.26 ? 49  ASN   A CB  1 
ATOM   163  C  CG  . ASN   A 1 29  ? -27.812 -1.654  -21.886 1.00 103.29 ? 49  ASN   A CG  1 
ATOM   164  O  OD1 . ASN   A 1 29  ? -27.179 -1.198  -20.935 1.00 102.51 ? 49  ASN   A OD1 1 
ATOM   165  N  ND2 . ASN   A 1 29  ? -27.924 -1.015  -23.046 1.00 97.65  ? 49  ASN   A ND2 1 
ATOM   166  N  N   . ILE   A 1 30  ? -31.045 -4.446  -19.576 1.00 96.56  ? 50  ILE   A N   1 
ATOM   167  C  CA  . ILE   A 1 30  ? -31.429 -5.771  -19.104 1.00 97.60  ? 50  ILE   A CA  1 
ATOM   168  C  C   . ILE   A 1 30  ? -32.493 -6.411  -19.986 1.00 110.94 ? 50  ILE   A C   1 
ATOM   169  O  O   . ILE   A 1 30  ? -32.635 -7.640  -19.979 1.00 116.09 ? 50  ILE   A O   1 
ATOM   170  C  CB  . ILE   A 1 30  ? -31.915 -5.713  -17.642 1.00 98.83  ? 50  ILE   A CB  1 
ATOM   171  C  CG1 . ILE   A 1 30  ? -33.176 -4.855  -17.532 1.00 116.60 ? 50  ILE   A CG1 1 
ATOM   172  C  CG2 . ILE   A 1 30  ? -30.806 -5.197  -16.727 1.00 107.76 ? 50  ILE   A CG2 1 
ATOM   173  C  CD1 . ILE   A 1 30  ? -33.979 -5.125  -16.285 1.00 124.84 ? 50  ILE   A CD1 1 
ATOM   174  N  N   . LEU   A 1 31  ? -33.258 -5.614  -20.739 1.00 118.61 ? 51  LEU   A N   1 
ATOM   175  C  CA  . LEU   A 1 31  ? -34.219 -6.197  -21.670 1.00 110.37 ? 51  LEU   A CA  1 
ATOM   176  C  C   . LEU   A 1 31  ? -33.524 -7.032  -22.736 1.00 117.13 ? 51  LEU   A C   1 
ATOM   177  O  O   . LEU   A 1 31  ? -34.123 -7.962  -23.286 1.00 116.06 ? 51  LEU   A O   1 
ATOM   178  C  CB  . LEU   A 1 31  ? -35.063 -5.105  -22.329 1.00 111.51 ? 51  LEU   A CB  1 
ATOM   179  C  CG  . LEU   A 1 31  ? -36.171 -4.446  -21.510 1.00 113.06 ? 51  LEU   A CG  1 
ATOM   180  C  CD1 . LEU   A 1 31  ? -37.001 -3.550  -22.410 1.00 105.89 ? 51  LEU   A CD1 1 
ATOM   181  C  CD2 . LEU   A 1 31  ? -37.048 -5.487  -20.832 1.00 100.77 ? 51  LEU   A CD2 1 
ATOM   182  N  N   . SER   A 1 32  ? -32.261 -6.718  -23.032 1.00 113.69 ? 52  SER   A N   1 
ATOM   183  C  CA  . SER   A 1 32  ? -31.473 -7.474  -23.997 1.00 118.56 ? 52  SER   A CA  1 
ATOM   184  C  C   . SER   A 1 32  ? -31.114 -8.872  -23.510 1.00 122.36 ? 52  SER   A C   1 
ATOM   185  O  O   . SER   A 1 32  ? -30.707 -9.703  -24.328 1.00 125.21 ? 52  SER   A O   1 
ATOM   186  C  CB  . SER   A 1 32  ? -30.199 -6.703  -24.340 1.00 115.75 ? 52  SER   A CB  1 
ATOM   187  O  OG  . SER   A 1 32  ? -30.504 -5.450  -24.930 1.00 112.79 ? 52  SER   A OG  1 
ATOM   188  N  N   . TYR   A 1 33  ? -31.247 -9.152  -22.208 1.00 115.76 ? 53  TYR   A N   1 
ATOM   189  C  CA  . TYR   A 1 33  ? -31.007 -10.494 -21.674 1.00 112.95 ? 53  TYR   A CA  1 
ATOM   190  C  C   . TYR   A 1 33  ? -32.103 -11.487 -22.053 1.00 126.16 ? 53  TYR   A C   1 
ATOM   191  O  O   . TYR   A 1 33  ? -32.093 -12.619 -21.551 1.00 125.35 ? 53  TYR   A O   1 
ATOM   192  C  CB  . TYR   A 1 33  ? -30.865 -10.445 -20.150 1.00 106.33 ? 53  TYR   A CB  1 
ATOM   193  C  CG  . TYR   A 1 33  ? -29.585 -9.803  -19.658 1.00 115.34 ? 53  TYR   A CG  1 
ATOM   194  C  CD1 . TYR   A 1 33  ? -28.440 -9.803  -20.442 1.00 113.19 ? 53  TYR   A CD1 1 
ATOM   195  C  CD2 . TYR   A 1 33  ? -29.522 -9.197  -18.408 1.00 111.34 ? 53  TYR   A CD2 1 
ATOM   196  C  CE1 . TYR   A 1 33  ? -27.268 -9.218  -19.998 1.00 112.03 ? 53  TYR   A CE1 1 
ATOM   197  C  CE2 . TYR   A 1 33  ? -28.352 -8.608  -17.954 1.00 105.86 ? 53  TYR   A CE2 1 
ATOM   198  C  CZ  . TYR   A 1 33  ? -27.229 -8.621  -18.754 1.00 113.01 ? 53  TYR   A CZ  1 
ATOM   199  O  OH  . TYR   A 1 33  ? -26.064 -8.037  -18.310 1.00 104.91 ? 53  TYR   A OH  1 
ATOM   200  N  N   . HIS   A 1 34  ? -33.045 -11.113 -22.923 1.00 122.39 ? 54  HIS   A N   1 
ATOM   201  C  CA  . HIS   A 1 34  ? -34.153 -11.994 -23.275 1.00 129.58 ? 54  HIS   A CA  1 
ATOM   202  C  C   . HIS   A 1 34  ? -33.705 -13.238 -24.029 1.00 130.84 ? 54  HIS   A C   1 
ATOM   203  O  O   . HIS   A 1 34  ? -34.494 -14.181 -24.155 1.00 132.39 ? 54  HIS   A O   1 
ATOM   204  C  CB  . HIS   A 1 34  ? -35.187 -11.230 -24.103 1.00 133.39 ? 54  HIS   A CB  1 
ATOM   205  C  CG  . HIS   A 1 34  ? -34.785 -11.020 -25.530 1.00 134.56 ? 54  HIS   A CG  1 
ATOM   206  N  ND1 . HIS   A 1 34  ? -33.730 -10.213 -25.896 1.00 140.60 ? 54  HIS   A ND1 1 
ATOM   207  C  CD2 . HIS   A 1 34  ? -35.300 -11.511 -26.682 1.00 135.54 ? 54  HIS   A CD2 1 
ATOM   208  C  CE1 . HIS   A 1 34  ? -33.609 -10.219 -27.212 1.00 138.57 ? 54  HIS   A CE1 1 
ATOM   209  N  NE2 . HIS   A 1 34  ? -34.551 -10.999 -27.713 1.00 138.82 ? 54  HIS   A NE2 1 
ATOM   210  N  N   . LYS   A 1 35  ? -32.475 -13.261 -24.541 1.00 131.59 ? 55  LYS   A N   1 
ATOM   211  C  CA  . LYS   A 1 35  ? -31.906 -14.441 -25.177 1.00 138.83 ? 55  LYS   A CA  1 
ATOM   212  C  C   . LYS   A 1 35  ? -30.839 -15.099 -24.315 1.00 131.75 ? 55  LYS   A C   1 
ATOM   213  O  O   . LYS   A 1 35  ? -30.188 -16.049 -24.763 1.00 138.71 ? 55  LYS   A O   1 
ATOM   214  C  CB  . LYS   A 1 35  ? -31.329 -14.077 -26.548 1.00 137.33 ? 55  LYS   A CB  1 
ATOM   215  C  CG  . LYS   A 1 35  ? -32.378 -13.760 -27.597 1.00 138.67 ? 55  LYS   A CG  1 
ATOM   216  C  CD  . LYS   A 1 35  ? -31.736 -13.451 -28.937 1.00 140.40 ? 55  LYS   A CD  1 
ATOM   217  C  CE  . LYS   A 1 35  ? -32.776 -13.379 -30.040 1.00 151.10 ? 55  LYS   A CE  1 
ATOM   218  N  NZ  . LYS   A 1 35  ? -33.466 -14.687 -30.224 1.00 147.41 ? 55  LYS   A NZ  1 
ATOM   219  N  N   . GLY   A 1 36  ? -30.654 -14.625 -23.095 1.00 138.24 ? 56  GLY   A N   1 
ATOM   220  C  CA  . GLY   A 1 36  ? -29.612 -15.115 -22.217 1.00 132.15 ? 56  GLY   A CA  1 
ATOM   221  C  C   . GLY   A 1 36  ? -28.371 -14.242 -22.268 1.00 127.41 ? 56  GLY   A C   1 
ATOM   222  O  O   . GLY   A 1 36  ? -28.135 -13.496 -23.227 1.00 128.29 ? 56  GLY   A O   1 
ATOM   223  N  N   . PHE   A 1 37  ? -27.557 -14.340 -21.214 1.00 109.19 ? 57  PHE   A N   1 
ATOM   224  C  CA  . PHE   A 1 37  ? -26.328 -13.560 -21.139 1.00 121.02 ? 57  PHE   A CA  1 
ATOM   225  C  C   . PHE   A 1 37  ? -25.417 -13.856 -22.321 1.00 110.08 ? 57  PHE   A C   1 
ATOM   226  O  O   . PHE   A 1 37  ? -24.732 -12.962 -22.833 1.00 114.73 ? 57  PHE   A O   1 
ATOM   227  C  CB  . PHE   A 1 37  ? -25.589 -13.863 -19.833 1.00 117.18 ? 57  PHE   A CB  1 
ATOM   228  C  CG  . PHE   A 1 37  ? -26.418 -13.676 -18.590 1.00 125.34 ? 57  PHE   A CG  1 
ATOM   229  C  CD1 . PHE   A 1 37  ? -27.364 -14.616 -18.215 1.00 131.78 ? 57  PHE   A CD1 1 
ATOM   230  C  CD2 . PHE   A 1 37  ? -26.219 -12.573 -17.776 1.00 123.18 ? 57  PHE   A CD2 1 
ATOM   231  C  CE1 . PHE   A 1 37  ? -28.115 -14.445 -17.065 1.00 134.79 ? 57  PHE   A CE1 1 
ATOM   232  C  CE2 . PHE   A 1 37  ? -26.963 -12.398 -16.624 1.00 121.04 ? 57  PHE   A CE2 1 
ATOM   233  C  CZ  . PHE   A 1 37  ? -27.912 -13.333 -16.267 1.00 137.32 ? 57  PHE   A CZ  1 
ATOM   234  N  N   . CYS   A 1 38  ? -25.411 -15.111 -22.772 1.00 103.01 ? 58  CYS   A N   1 
ATOM   235  C  CA  . CYS   A 1 38  ? -24.438 -15.565 -23.759 1.00 110.65 ? 58  CYS   A CA  1 
ATOM   236  C  C   . CYS   A 1 38  ? -24.721 -14.978 -25.136 1.00 112.80 ? 58  CYS   A C   1 
ATOM   237  O  O   . CYS   A 1 38  ? -23.820 -14.433 -25.785 1.00 113.67 ? 58  CYS   A O   1 
ATOM   238  C  CB  . CYS   A 1 38  ? -24.438 -17.091 -23.805 1.00 110.36 ? 58  CYS   A CB  1 
ATOM   239  S  SG  . CYS   A 1 38  ? -23.964 -17.848 -22.233 1.00 104.30 ? 58  CYS   A SG  1 
ATOM   240  N  N   . MET   A 1 39  ? -25.967 -15.087 -25.604 1.00 111.61 ? 59  MET   A N   1 
ATOM   241  C  CA  . MET   A 1 39  ? -26.320 -14.502 -26.893 1.00 115.52 ? 59  MET   A CA  1 
ATOM   242  C  C   . MET   A 1 39  ? -26.164 -12.989 -26.872 1.00 114.65 ? 59  MET   A C   1 
ATOM   243  O  O   . MET   A 1 39  ? -25.915 -12.373 -27.916 1.00 112.23 ? 59  MET   A O   1 
ATOM   244  C  CB  . MET   A 1 39  ? -27.751 -14.884 -27.272 1.00 128.83 ? 59  MET   A CB  1 
ATOM   245  C  CG  . MET   A 1 39  ? -28.091 -16.354 -27.058 1.00 130.11 ? 59  MET   A CG  1 
ATOM   246  S  SD  . MET   A 1 39  ? -26.888 -17.487 -27.776 1.00 153.62 ? 59  MET   A SD  1 
ATOM   247  C  CE  . MET   A 1 39  ? -27.038 -17.087 -29.514 1.00 131.77 ? 59  MET   A CE  1 
ATOM   248  N  N   . PHE   A 1 40  ? -26.310 -12.374 -25.697 1.00 108.41 ? 60  PHE   A N   1 
ATOM   249  C  CA  . PHE   A 1 40  ? -26.059 -10.944 -25.564 1.00 111.33 ? 60  PHE   A CA  1 
ATOM   250  C  C   . PHE   A 1 40  ? -24.579 -10.630 -25.751 1.00 116.28 ? 60  PHE   A C   1 
ATOM   251  O  O   . PHE   A 1 40  ? -24.217 -9.741  -26.532 1.00 112.04 ? 60  PHE   A O   1 
ATOM   252  C  CB  . PHE   A 1 40  ? -26.552 -10.456 -24.200 1.00 111.17 ? 60  PHE   A CB  1 
ATOM   253  C  CG  . PHE   A 1 40  ? -26.282 -9.002  -23.938 1.00 109.63 ? 60  PHE   A CG  1 
ATOM   254  C  CD1 . PHE   A 1 40  ? -26.863 -8.025  -24.726 1.00 109.56 ? 60  PHE   A CD1 1 
ATOM   255  C  CD2 . PHE   A 1 40  ? -25.460 -8.612  -22.892 1.00 110.16 ? 60  PHE   A CD2 1 
ATOM   256  C  CE1 . PHE   A 1 40  ? -26.623 -6.686  -24.485 1.00 114.58 ? 60  PHE   A CE1 1 
ATOM   257  C  CE2 . PHE   A 1 40  ? -25.216 -7.274  -22.645 1.00 110.90 ? 60  PHE   A CE2 1 
ATOM   258  C  CZ  . PHE   A 1 40  ? -25.798 -6.310  -23.443 1.00 117.34 ? 60  PHE   A CZ  1 
ATOM   259  N  N   . ASP   A 1 41  ? -23.706 -11.358 -25.048 1.00 118.13 ? 61  ASP   A N   1 
ATOM   260  C  CA  . ASP   A 1 41  ? -22.273 -11.096 -25.148 1.00 115.19 ? 61  ASP   A CA  1 
ATOM   261  C  C   . ASP   A 1 41  ? -21.744 -11.427 -26.538 1.00 118.52 ? 61  ASP   A C   1 
ATOM   262  O  O   . ASP   A 1 41  ? -20.915 -10.686 -27.079 1.00 117.51 ? 61  ASP   A O   1 
ATOM   263  C  CB  . ASP   A 1 41  ? -21.516 -11.883 -24.078 1.00 106.68 ? 61  ASP   A CB  1 
ATOM   264  C  CG  . ASP   A 1 41  ? -22.012 -11.585 -22.677 1.00 104.11 ? 61  ASP   A CG  1 
ATOM   265  O  OD1 . ASP   A 1 41  ? -22.550 -10.478 -22.455 1.00 107.70 ? 61  ASP   A OD1 1 
ATOM   266  O  OD2 . ASP   A 1 41  ? -21.864 -12.462 -21.799 1.00 104.96 ? 61  ASP   A OD2 1 
ATOM   267  N  N   . MET   A 1 42  ? -22.210 -12.530 -27.133 1.00 115.58 ? 62  MET   A N   1 
ATOM   268  C  CA  A MET   A 1 42  ? -21.777 -12.884 -28.482 0.41 115.99 ? 62  MET   A CA  1 
ATOM   269  C  CA  B MET   A 1 42  ? -21.773 -12.882 -28.482 0.59 115.97 ? 62  MET   A CA  1 
ATOM   270  C  C   . MET   A 1 42  ? -22.123 -11.780 -29.473 1.00 117.93 ? 62  MET   A C   1 
ATOM   271  O  O   . MET   A 1 42  ? -21.271 -11.339 -30.255 1.00 123.29 ? 62  MET   A O   1 
ATOM   272  C  CB  A MET   A 1 42  ? -22.412 -14.209 -28.906 0.41 112.80 ? 62  MET   A CB  1 
ATOM   273  C  CB  B MET   A 1 42  ? -22.393 -14.211 -28.916 0.59 115.92 ? 62  MET   A CB  1 
ATOM   274  C  CG  A MET   A 1 42  ? -21.799 -15.437 -28.248 0.41 113.61 ? 62  MET   A CG  1 
ATOM   275  C  CG  B MET   A 1 42  ? -21.785 -15.438 -28.254 0.59 113.79 ? 62  MET   A CG  1 
ATOM   276  S  SD  A MET   A 1 42  ? -20.270 -15.965 -29.045 0.41 113.33 ? 62  MET   A SD  1 
ATOM   277  S  SD  B MET   A 1 42  ? -22.031 -16.935 -29.232 0.59 116.55 ? 62  MET   A SD  1 
ATOM   278  C  CE  A MET   A 1 42  ? -20.898 -16.611 -30.593 0.41 109.29 ? 62  MET   A CE  1 
ATOM   279  C  CE  B MET   A 1 42  ? -20.971 -16.597 -30.636 0.59 109.36 ? 62  MET   A CE  1 
ATOM   280  N  N   . GLU   A 1 43  ? -23.376 -11.321 -29.453 1.00 124.25 ? 63  GLU   A N   1 
ATOM   281  C  CA  . GLU   A 1 43  ? -23.785 -10.232 -30.335 1.00 124.80 ? 63  GLU   A CA  1 
ATOM   282  C  C   . GLU   A 1 43  ? -22.978 -8.972  -30.051 1.00 126.18 ? 63  GLU   A C   1 
ATOM   283  O  O   . GLU   A 1 43  ? -22.419 -8.358  -30.967 1.00 139.04 ? 63  GLU   A O   1 
ATOM   284  C  CB  . GLU   A 1 43  ? -25.278 -9.949  -30.170 1.00 129.92 ? 63  GLU   A CB  1 
ATOM   285  C  CG  . GLU   A 1 43  ? -26.203 -11.001 -30.744 1.00 135.39 ? 63  GLU   A CG  1 
ATOM   286  C  CD  . GLU   A 1 43  ? -27.660 -10.652 -30.516 1.00 154.14 ? 63  GLU   A CD  1 
ATOM   287  O  OE1 . GLU   A 1 43  ? -27.929 -9.531  -30.035 1.00 156.59 ? 63  GLU   A OE1 1 
ATOM   288  O  OE2 . GLU   A 1 43  ? -28.533 -11.494 -30.812 1.00 156.80 ? 63  GLU   A OE2 1 
ATOM   289  N  N   . CYS   A 1 44  ? -22.912 -8.572  -28.776 1.00 122.94 ? 64  CYS   A N   1 
ATOM   290  C  CA  . CYS   A 1 44  ? -22.162 -7.377  -28.398 1.00 121.86 ? 64  CYS   A CA  1 
ATOM   291  C  C   . CYS   A 1 44  ? -20.701 -7.488  -28.806 1.00 124.93 ? 64  CYS   A C   1 
ATOM   292  O  O   . CYS   A 1 44  ? -20.099 -6.508  -29.262 1.00 129.80 ? 64  CYS   A O   1 
ATOM   293  C  CB  . CYS   A 1 44  ? -22.277 -7.143  -26.895 1.00 119.22 ? 64  CYS   A CB  1 
ATOM   294  S  SG  . CYS   A 1 44  ? -23.789 -6.298  -26.389 1.00 121.51 ? 64  CYS   A SG  1 
ATOM   295  N  N   . HIS   A 1 45  ? -20.113 -8.675  -28.642 1.00 125.90 ? 65  HIS   A N   1 
ATOM   296  C  CA  . HIS   A 1 45  ? -18.750 -8.897  -29.107 1.00 122.18 ? 65  HIS   A CA  1 
ATOM   297  C  C   . HIS   A 1 45  ? -18.624 -8.598  -30.596 1.00 128.97 ? 65  HIS   A C   1 
ATOM   298  O  O   . HIS   A 1 45  ? -17.607 -8.059  -31.045 1.00 133.74 ? 65  HIS   A O   1 
ATOM   299  C  CB  . HIS   A 1 45  ? -18.327 -10.333 -28.799 1.00 123.66 ? 65  HIS   A CB  1 
ATOM   300  C  CG  . HIS   A 1 45  ? -16.870 -10.595 -29.008 1.00 126.71 ? 65  HIS   A CG  1 
ATOM   301  N  ND1 . HIS   A 1 45  ? -15.924 -9.592  -29.001 1.00 131.52 ? 65  HIS   A ND1 1 
ATOM   302  C  CD2 . HIS   A 1 45  ? -16.195 -11.747 -29.232 1.00 123.09 ? 65  HIS   A CD2 1 
ATOM   303  C  CE1 . HIS   A 1 45  ? -14.730 -10.116 -29.213 1.00 127.41 ? 65  HIS   A CE1 1 
ATOM   304  N  NE2 . HIS   A 1 45  ? -14.866 -11.422 -29.356 1.00 125.83 ? 65  HIS   A NE2 1 
ATOM   305  N  N   . LYS   A 1 46  ? -19.660 -8.921  -31.375 1.00 134.28 ? 66  LYS   A N   1 
ATOM   306  C  CA  . LYS   A 1 46  ? -19.640 -8.622  -32.804 1.00 137.25 ? 66  LYS   A CA  1 
ATOM   307  C  C   . LYS   A 1 46  ? -19.882 -7.141  -33.065 1.00 143.58 ? 66  LYS   A C   1 
ATOM   308  O  O   . LYS   A 1 46  ? -19.224 -6.538  -33.922 1.00 143.12 ? 66  LYS   A O   1 
ATOM   309  C  CB  . LYS   A 1 46  ? -20.694 -9.459  -33.528 1.00 136.48 ? 66  LYS   A CB  1 
ATOM   310  C  CG  . LYS   A 1 46  ? -20.196 -10.194 -34.761 1.00 148.79 ? 66  LYS   A CG  1 
ATOM   311  C  CD  . LYS   A 1 46  ? -21.346 -10.860 -35.502 1.00 157.25 ? 66  LYS   A CD  1 
ATOM   312  C  CE  . LYS   A 1 46  ? -22.204 -9.830  -36.215 1.00 163.55 ? 66  LYS   A CE  1 
ATOM   313  N  NZ  . LYS   A 1 46  ? -21.435 -9.163  -37.302 1.00 175.81 ? 66  LYS   A NZ  1 
ATOM   314  N  N   . LYS   A 1 47  ? -20.822 -6.540  -32.334 1.00 156.84 ? 67  LYS   A N   1 
ATOM   315  C  CA  . LYS   A 1 47  ? -21.269 -5.188  -32.653 1.00 161.54 ? 67  LYS   A CA  1 
ATOM   316  C  C   . LYS   A 1 47  ? -20.189 -4.151  -32.372 1.00 158.93 ? 67  LYS   A C   1 
ATOM   317  O  O   . LYS   A 1 47  ? -20.001 -3.218  -33.160 1.00 164.82 ? 67  LYS   A O   1 
ATOM   318  C  CB  . LYS   A 1 47  ? -22.538 -4.857  -31.866 1.00 160.47 ? 67  LYS   A CB  1 
ATOM   319  C  CG  . LYS   A 1 47  ? -23.778 -4.661  -32.725 1.00 168.17 ? 67  LYS   A CG  1 
ATOM   320  C  CD  . LYS   A 1 47  ? -24.986 -4.250  -31.892 1.00 172.98 ? 67  LYS   A CD  1 
ATOM   321  C  CE  . LYS   A 1 47  ? -25.553 -5.422  -31.102 1.00 171.26 ? 67  LYS   A CE  1 
ATOM   322  N  NZ  . LYS   A 1 47  ? -26.758 -5.030  -30.315 1.00 167.97 ? 67  LYS   A NZ  1 
ATOM   323  N  N   . TYR   A 1 48  ? -19.464 -4.296  -31.261 1.00 142.89 ? 68  TYR   A N   1 
ATOM   324  C  CA  . TYR   A 1 48  ? -18.635 -3.211  -30.756 1.00 137.88 ? 68  TYR   A CA  1 
ATOM   325  C  C   . TYR   A 1 48  ? -17.144 -3.511  -30.697 1.00 136.44 ? 68  TYR   A C   1 
ATOM   326  O  O   . TYR   A 1 48  ? -16.354 -2.565  -30.619 1.00 133.53 ? 68  TYR   A O   1 
ATOM   327  C  CB  . TYR   A 1 48  ? -19.118 -2.792  -29.361 1.00 129.69 ? 68  TYR   A CB  1 
ATOM   328  C  CG  . TYR   A 1 48  ? -20.609 -2.554  -29.312 1.00 140.72 ? 68  TYR   A CG  1 
ATOM   329  C  CD1 . TYR   A 1 48  ? -21.164 -1.402  -29.854 1.00 138.24 ? 68  TYR   A CD1 1 
ATOM   330  C  CD2 . TYR   A 1 48  ? -21.461 -3.486  -28.737 1.00 137.06 ? 68  TYR   A CD2 1 
ATOM   331  C  CE1 . TYR   A 1 48  ? -22.529 -1.182  -29.817 1.00 137.20 ? 68  TYR   A CE1 1 
ATOM   332  C  CE2 . TYR   A 1 48  ? -22.825 -3.275  -28.695 1.00 136.72 ? 68  TYR   A CE2 1 
ATOM   333  C  CZ  . TYR   A 1 48  ? -23.353 -2.122  -29.235 1.00 141.82 ? 68  TYR   A CZ  1 
ATOM   334  O  OH  . TYR   A 1 48  ? -24.713 -1.915  -29.192 1.00 138.41 ? 68  TYR   A OH  1 
ATOM   335  N  N   . GLY   A 1 49  ? -16.733 -4.776  -30.728 1.00 134.27 ? 69  GLY   A N   1 
ATOM   336  C  CA  . GLY   A 1 49  ? -15.320 -5.081  -30.847 1.00 130.82 ? 69  GLY   A CA  1 
ATOM   337  C  C   . GLY   A 1 49  ? -14.636 -5.521  -29.569 1.00 130.37 ? 69  GLY   A C   1 
ATOM   338  O  O   . GLY   A 1 49  ? -15.204 -6.280  -28.778 1.00 129.79 ? 69  GLY   A O   1 
ATOM   339  N  N   . LYS   A 1 50  ? -13.407 -5.043  -29.357 1.00 127.64 ? 70  LYS   A N   1 
ATOM   340  C  CA  . LYS   A 1 50  ? -12.597 -5.516  -28.241 1.00 130.22 ? 70  LYS   A CA  1 
ATOM   341  C  C   . LYS   A 1 50  ? -13.101 -5.019  -26.893 1.00 122.59 ? 70  LYS   A C   1 
ATOM   342  O  O   . LYS   A 1 50  ? -12.799 -5.640  -25.868 1.00 121.88 ? 70  LYS   A O   1 
ATOM   343  C  CB  . LYS   A 1 50  ? -11.138 -5.093  -28.436 1.00 135.54 ? 70  LYS   A CB  1 
ATOM   344  C  CG  . LYS   A 1 50  ? -10.825 -3.678  -27.970 1.00 146.02 ? 70  LYS   A CG  1 
ATOM   345  C  CD  . LYS   A 1 50  ? -9.819  -3.000  -28.886 1.00 157.57 ? 70  LYS   A CD  1 
ATOM   346  C  CE  . LYS   A 1 50  ? -9.348  -1.678  -28.300 1.00 162.22 ? 70  LYS   A CE  1 
ATOM   347  N  NZ  . LYS   A 1 50  ? -10.491 -0.813  -27.895 1.00 154.87 ? 70  LYS   A NZ  1 
ATOM   348  N  N   . VAL   A 1 51  ? -13.853 -3.920  -26.869 1.00 132.92 ? 71  VAL   A N   1 
ATOM   349  C  CA  . VAL   A 1 51  ? -14.313 -3.292  -25.635 1.00 123.87 ? 71  VAL   A CA  1 
ATOM   350  C  C   . VAL   A 1 51  ? -15.697 -2.708  -25.873 1.00 123.30 ? 71  VAL   A C   1 
ATOM   351  O  O   . VAL   A 1 51  ? -15.953 -2.097  -26.916 1.00 119.67 ? 71  VAL   A O   1 
ATOM   352  C  CB  . VAL   A 1 51  ? -13.336 -2.195  -25.156 1.00 117.37 ? 71  VAL   A CB  1 
ATOM   353  C  CG1 . VAL   A 1 51  ? -14.014 -1.259  -24.165 1.00 118.13 ? 71  VAL   A CG1 1 
ATOM   354  C  CG2 . VAL   A 1 51  ? -12.102 -2.817  -24.527 1.00 127.76 ? 71  VAL   A CG2 1 
ATOM   355  N  N   . TRP   A 1 52  ? -16.593 -2.905  -24.909 1.00 111.90 ? 72  TRP   A N   1 
ATOM   356  C  CA  . TRP   A 1 52  ? -17.901 -2.266  -24.948 1.00 108.09 ? 72  TRP   A CA  1 
ATOM   357  C  C   . TRP   A 1 52  ? -18.448 -2.178  -23.532 1.00 99.83  ? 72  TRP   A C   1 
ATOM   358  O  O   . TRP   A 1 52  ? -17.949 -2.824  -22.607 1.00 96.91  ? 72  TRP   A O   1 
ATOM   359  C  CB  . TRP   A 1 52  ? -18.873 -3.011  -25.870 1.00 115.45 ? 72  TRP   A CB  1 
ATOM   360  C  CG  . TRP   A 1 52  ? -19.372 -4.336  -25.360 1.00 110.82 ? 72  TRP   A CG  1 
ATOM   361  C  CD1 . TRP   A 1 52  ? -20.501 -4.561  -24.623 1.00 109.93 ? 72  TRP   A CD1 1 
ATOM   362  C  CD2 . TRP   A 1 52  ? -18.780 -5.621  -25.585 1.00 113.72 ? 72  TRP   A CD2 1 
ATOM   363  N  NE1 . TRP   A 1 52  ? -20.638 -5.904  -24.363 1.00 110.58 ? 72  TRP   A NE1 1 
ATOM   364  C  CE2 . TRP   A 1 52  ? -19.596 -6.576  -24.947 1.00 109.86 ? 72  TRP   A CE2 1 
ATOM   365  C  CE3 . TRP   A 1 52  ? -17.636 -6.054  -26.260 1.00 120.68 ? 72  TRP   A CE3 1 
ATOM   366  C  CZ2 . TRP   A 1 52  ? -19.301 -7.938  -24.961 1.00 113.68 ? 72  TRP   A CZ2 1 
ATOM   367  C  CZ3 . TRP   A 1 52  ? -17.345 -7.404  -26.273 1.00 121.09 ? 72  TRP   A CZ3 1 
ATOM   368  C  CH2 . TRP   A 1 52  ? -18.173 -8.331  -25.628 1.00 112.93 ? 72  TRP   A CH2 1 
ATOM   369  N  N   . GLY   A 1 53  ? -19.487 -1.363  -23.376 1.00 107.81 ? 73  GLY   A N   1 
ATOM   370  C  CA  . GLY   A 1 53  ? -20.076 -1.141  -22.074 1.00 100.61 ? 73  GLY   A CA  1 
ATOM   371  C  C   . GLY   A 1 53  ? -21.586 -1.065  -22.106 1.00 104.25 ? 73  GLY   A C   1 
ATOM   372  O  O   . GLY   A 1 53  ? -22.171 -0.471  -23.017 1.00 115.60 ? 73  GLY   A O   1 
ATOM   373  N  N   . PHE   A 1 54  ? -22.226 -1.668  -21.109 1.00 98.58  ? 74  PHE   A N   1 
ATOM   374  C  CA  . PHE   A 1 54  ? -23.675 -1.661  -20.985 1.00 96.31  ? 74  PHE   A CA  1 
ATOM   375  C  C   . PHE   A 1 54  ? -24.022 -1.410  -19.521 1.00 96.21  ? 74  PHE   A C   1 
ATOM   376  O  O   . PHE   A 1 54  ? -23.147 -1.136  -18.693 1.00 85.94  ? 74  PHE   A O   1 
ATOM   377  C  CB  . PHE   A 1 54  ? -24.273 -2.966  -21.528 1.00 101.21 ? 74  PHE   A CB  1 
ATOM   378  C  CG  . PHE   A 1 54  ? -23.717 -4.206  -20.888 1.00 101.41 ? 74  PHE   A CG  1 
ATOM   379  C  CD1 . PHE   A 1 54  ? -22.532 -4.772  -21.350 1.00 103.90 ? 74  PHE   A CD1 1 
ATOM   380  C  CD2 . PHE   A 1 54  ? -24.385 -4.815  -19.839 1.00 95.61  ? 74  PHE   A CD2 1 
ATOM   381  C  CE1 . PHE   A 1 54  ? -22.013 -5.917  -20.771 1.00 100.69 ? 74  PHE   A CE1 1 
ATOM   382  C  CE2 . PHE   A 1 54  ? -23.879 -5.959  -19.253 1.00 99.11  ? 74  PHE   A CE2 1 
ATOM   383  C  CZ  . PHE   A 1 54  ? -22.687 -6.515  -19.722 1.00 97.76  ? 74  PHE   A CZ  1 
ATOM   384  N  N   . TYR   A 1 55  ? -25.313 -1.498  -19.201 1.00 97.91  ? 75  TYR   A N   1 
ATOM   385  C  CA  . TYR   A 1 55  ? -25.809 -1.201  -17.862 1.00 96.27  ? 75  TYR   A CA  1 
ATOM   386  C  C   . TYR   A 1 55  ? -26.776 -2.289  -17.425 1.00 96.48  ? 75  TYR   A C   1 
ATOM   387  O  O   . TYR   A 1 55  ? -27.784 -2.532  -18.097 1.00 98.25  ? 75  TYR   A O   1 
ATOM   388  C  CB  . TYR   A 1 55  ? -26.502 0.166   -17.815 1.00 103.24 ? 75  TYR   A CB  1 
ATOM   389  C  CG  . TYR   A 1 55  ? -25.615 1.327   -18.204 1.00 108.72 ? 75  TYR   A CG  1 
ATOM   390  C  CD1 . TYR   A 1 55  ? -25.476 1.699   -19.534 1.00 105.91 ? 75  TYR   A CD1 1 
ATOM   391  C  CD2 . TYR   A 1 55  ? -24.918 2.051   -17.243 1.00 109.02 ? 75  TYR   A CD2 1 
ATOM   392  C  CE1 . TYR   A 1 55  ? -24.668 2.757   -19.899 1.00 106.95 ? 75  TYR   A CE1 1 
ATOM   393  C  CE2 . TYR   A 1 55  ? -24.104 3.115   -17.600 1.00 112.87 ? 75  TYR   A CE2 1 
ATOM   394  C  CZ  . TYR   A 1 55  ? -23.985 3.462   -18.932 1.00 115.03 ? 75  TYR   A CZ  1 
ATOM   395  O  OH  . TYR   A 1 55  ? -23.183 4.515   -19.310 1.00 115.50 ? 75  TYR   A OH  1 
ATOM   396  N  N   . ASP   A 1 56  ? -26.471 -2.936  -16.303 1.00 99.60  ? 76  ASP   A N   1 
ATOM   397  C  CA  . ASP   A 1 56  ? -27.429 -3.788  -15.603 1.00 99.41  ? 76  ASP   A CA  1 
ATOM   398  C  C   . ASP   A 1 56  ? -28.174 -2.900  -14.616 1.00 104.03 ? 76  ASP   A C   1 
ATOM   399  O  O   . ASP   A 1 56  ? -27.712 -2.674  -13.494 1.00 102.22 ? 76  ASP   A O   1 
ATOM   400  C  CB  . ASP   A 1 56  ? -26.726 -4.942  -14.899 1.00 104.10 ? 76  ASP   A CB  1 
ATOM   401  C  CG  . ASP   A 1 56  ? -26.176 -5.963  -15.864 1.00 99.72  ? 76  ASP   A CG  1 
ATOM   402  O  OD1 . ASP   A 1 56  ? -26.414 -5.814  -17.081 1.00 102.15 ? 76  ASP   A OD1 1 
ATOM   403  O  OD2 . ASP   A 1 56  ? -25.505 -6.913  -15.411 1.00 99.35  ? 76  ASP   A OD2 1 
ATOM   404  N  N   . GLY   A 1 57  ? -29.329 -2.390  -15.038 1.00 111.93 ? 77  GLY   A N   1 
ATOM   405  C  CA  . GLY   A 1 57  ? -30.027 -1.366  -14.289 1.00 112.05 ? 77  GLY   A CA  1 
ATOM   406  C  C   . GLY   A 1 57  ? -29.313 -0.032  -14.372 1.00 109.41 ? 77  GLY   A C   1 
ATOM   407  O  O   . GLY   A 1 57  ? -29.192 0.549   -15.455 1.00 104.67 ? 77  GLY   A O   1 
ATOM   408  N  N   . GLN   A 1 58  ? -28.837 0.465   -13.231 1.00 96.10  ? 78  GLN   A N   1 
ATOM   409  C  CA  . GLN   A 1 58  ? -27.998 1.653   -13.175 1.00 110.09 ? 78  GLN   A CA  1 
ATOM   410  C  C   . GLN   A 1 58  ? -26.524 1.305   -13.029 1.00 111.32 ? 78  GLN   A C   1 
ATOM   411  O  O   . GLN   A 1 58  ? -25.699 2.201   -12.822 1.00 100.25 ? 78  GLN   A O   1 
ATOM   412  C  CB  . GLN   A 1 58  ? -28.433 2.557   -12.020 1.00 114.89 ? 78  GLN   A CB  1 
ATOM   413  C  CG  . GLN   A 1 58  ? -29.849 3.095   -12.137 1.00 129.16 ? 78  GLN   A CG  1 
ATOM   414  C  CD  . GLN   A 1 58  ? -29.953 4.266   -13.093 1.00 136.04 ? 78  GLN   A CD  1 
ATOM   415  O  OE1 . GLN   A 1 58  ? -28.945 4.772   -13.588 1.00 146.13 ? 78  GLN   A OE1 1 
ATOM   416  N  NE2 . GLN   A 1 58  ? -31.178 4.706   -13.355 1.00 135.88 ? 78  GLN   A NE2 1 
ATOM   417  N  N   . GLN   A 1 59  ? -26.174 0.021   -13.146 1.00 97.92  ? 79  GLN   A N   1 
ATOM   418  C  CA  . GLN   A 1 59  ? -24.842 -0.464  -12.814 1.00 95.61  ? 79  GLN   A CA  1 
ATOM   419  C  C   . GLN   A 1 59  ? -24.011 -0.625  -14.078 1.00 91.66  ? 79  GLN   A C   1 
ATOM   420  O  O   . GLN   A 1 59  ? -24.271 -1.545  -14.867 1.00 84.45  ? 79  GLN   A O   1 
ATOM   421  C  CB  . GLN   A 1 59  ? -24.942 -1.787  -12.051 1.00 94.05  ? 79  GLN   A CB  1 
ATOM   422  C  CG  . GLN   A 1 59  ? -23.639 -2.544  -11.904 1.00 93.30  ? 79  GLN   A CG  1 
ATOM   423  C  CD  . GLN   A 1 59  ? -22.606 -1.782  -11.099 1.00 84.78  ? 79  GLN   A CD  1 
ATOM   424  O  OE1 . GLN   A 1 59  ? -22.727 -1.649  -9.882  1.00 78.94  ? 79  GLN   A OE1 1 
ATOM   425  N  NE2 . GLN   A 1 59  ? -21.584 -1.267  -11.779 1.00 82.84  ? 79  GLN   A NE2 1 
ATOM   426  N  N   . PRO   A 1 60  ? -23.020 0.234   -14.318 1.00 81.92  ? 80  PRO   A N   1 
ATOM   427  C  CA  . PRO   A 1 60  ? -22.217 0.106   -15.543 1.00 94.06  ? 80  PRO   A CA  1 
ATOM   428  C  C   . PRO   A 1 60  ? -21.365 -1.159  -15.533 1.00 90.63  ? 80  PRO   A C   1 
ATOM   429  O  O   . PRO   A 1 60  ? -20.674 -1.461  -14.557 1.00 75.26  ? 80  PRO   A O   1 
ATOM   430  C  CB  . PRO   A 1 60  ? -21.350 1.373   -15.536 1.00 98.49  ? 80  PRO   A CB  1 
ATOM   431  C  CG  . PRO   A 1 60  ? -21.253 1.752   -14.095 1.00 92.81  ? 80  PRO   A CG  1 
ATOM   432  C  CD  . PRO   A 1 60  ? -22.583 1.375   -13.488 1.00 86.23  ? 80  PRO   A CD  1 
ATOM   433  N  N   . VAL   A 1 61  ? -21.426 -1.905  -16.633 1.00 86.83  ? 81  VAL   A N   1 
ATOM   434  C  CA  . VAL   A 1 61  ? -20.576 -3.070  -16.849 1.00 92.67  ? 81  VAL   A CA  1 
ATOM   435  C  C   . VAL   A 1 61  ? -19.707 -2.793  -18.065 1.00 95.80  ? 81  VAL   A C   1 
ATOM   436  O  O   . VAL   A 1 61  ? -20.218 -2.402  -19.120 1.00 97.06  ? 81  VAL   A O   1 
ATOM   437  C  CB  . VAL   A 1 61  ? -21.398 -4.357  -17.047 1.00 88.59  ? 81  VAL   A CB  1 
ATOM   438  C  CG1 . VAL   A 1 61  ? -20.471 -5.555  -17.210 1.00 91.41  ? 81  VAL   A CG1 1 
ATOM   439  C  CG2 . VAL   A 1 61  ? -22.345 -4.568  -15.882 1.00 82.07  ? 81  VAL   A CG2 1 
ATOM   440  N  N   . LEU   A 1 62  ? -18.399 -2.979  -17.913 1.00 86.51  ? 82  LEU   A N   1 
ATOM   441  C  CA  . LEU   A 1 62  ? -17.453 -2.857  -19.014 1.00 90.48  ? 82  LEU   A CA  1 
ATOM   442  C  C   . LEU   A 1 62  ? -16.984 -4.247  -19.416 1.00 96.78  ? 82  LEU   A C   1 
ATOM   443  O  O   . LEU   A 1 62  ? -16.353 -4.947  -18.617 1.00 94.00  ? 82  LEU   A O   1 
ATOM   444  C  CB  . LEU   A 1 62  ? -16.256 -1.987  -18.634 1.00 94.22  ? 82  LEU   A CB  1 
ATOM   445  C  CG  . LEU   A 1 62  ? -15.211 -1.876  -19.748 1.00 97.62  ? 82  LEU   A CG  1 
ATOM   446  C  CD1 . LEU   A 1 62  ? -15.664 -0.905  -20.834 1.00 108.74 ? 82  LEU   A CD1 1 
ATOM   447  C  CD2 . LEU   A 1 62  ? -13.855 -1.481  -19.188 1.00 101.44 ? 82  LEU   A CD2 1 
ATOM   448  N  N   . ALA   A 1 63  ? -17.289 -4.641  -20.647 1.00 97.63  ? 83  ALA   A N   1 
ATOM   449  C  CA  . ALA   A 1 63  ? -16.828 -5.913  -21.180 1.00 96.09  ? 83  ALA   A CA  1 
ATOM   450  C  C   . ALA   A 1 63  ? -15.501 -5.713  -21.896 1.00 92.55  ? 83  ALA   A C   1 
ATOM   451  O  O   . ALA   A 1 63  ? -15.372 -4.825  -22.744 1.00 97.52  ? 83  ALA   A O   1 
ATOM   452  C  CB  . ALA   A 1 63  ? -17.860 -6.508  -22.134 1.00 98.22  ? 83  ALA   A CB  1 
ATOM   453  N  N   . ILE   A 1 64  ? -14.517 -6.535  -21.543 1.00 99.49  ? 84  ILE   A N   1 
ATOM   454  C  CA  . ILE   A 1 64  ? -13.205 -6.507  -22.173 1.00 102.87 ? 84  ILE   A CA  1 
ATOM   455  C  C   . ILE   A 1 64  ? -12.935 -7.872  -22.786 1.00 106.92 ? 84  ILE   A C   1 
ATOM   456  O  O   . ILE   A 1 64  ? -13.417 -8.901  -22.301 1.00 98.95  ? 84  ILE   A O   1 
ATOM   457  C  CB  . ILE   A 1 64  ? -12.092 -6.122  -21.174 1.00 98.82  ? 84  ILE   A CB  1 
ATOM   458  C  CG1 . ILE   A 1 64  ? -11.879 -7.236  -20.141 1.00 103.28 ? 84  ILE   A CG1 1 
ATOM   459  C  CG2 . ILE   A 1 64  ? -12.431 -4.798  -20.496 1.00 87.94  ? 84  ILE   A CG2 1 
ATOM   460  C  CD1 . ILE   A 1 64  ? -10.615 -7.077  -19.292 1.00 108.53 ? 84  ILE   A CD1 1 
ATOM   461  N  N   . THR   A 1 65  ? -12.172 -7.874  -23.880 1.00 113.45 ? 85  THR   A N   1 
ATOM   462  C  CA  . THR   A 1 65  ? -11.788 -9.107  -24.556 1.00 113.80 ? 85  THR   A CA  1 
ATOM   463  C  C   . THR   A 1 65  ? -10.298 -9.151  -24.871 1.00 124.36 ? 85  THR   A C   1 
ATOM   464  O  O   . THR   A 1 65  ? -9.852  -10.071 -25.566 1.00 125.68 ? 85  THR   A O   1 
ATOM   465  C  CB  . THR   A 1 65  ? -12.596 -9.301  -25.850 1.00 113.20 ? 85  THR   A CB  1 
ATOM   466  O  OG1 . THR   A 1 65  ? -12.303 -8.239  -26.765 1.00 117.30 ? 85  THR   A OG1 1 
ATOM   467  C  CG2 . THR   A 1 65  ? -14.093 -9.319  -25.562 1.00 103.76 ? 85  THR   A CG2 1 
ATOM   468  N  N   . ASP   A 1 66  ? -9.519  -8.194  -24.380 1.00 130.52 ? 86  ASP   A N   1 
ATOM   469  C  CA  . ASP   A 1 66  ? -8.103  -8.141  -24.714 1.00 128.67 ? 86  ASP   A CA  1 
ATOM   470  C  C   . ASP   A 1 66  ? -7.316  -9.057  -23.785 1.00 123.98 ? 86  ASP   A C   1 
ATOM   471  O  O   . ASP   A 1 66  ? -7.413  -8.908  -22.562 1.00 124.90 ? 86  ASP   A O   1 
ATOM   472  C  CB  . ASP   A 1 66  ? -7.585  -6.707  -24.622 1.00 130.36 ? 86  ASP   A CB  1 
ATOM   473  C  CG  . ASP   A 1 66  ? -6.244  -6.524  -25.305 1.00 136.97 ? 86  ASP   A CG  1 
ATOM   474  O  OD1 . ASP   A 1 66  ? -6.210  -6.448  -26.554 1.00 129.16 ? 86  ASP   A OD1 1 
ATOM   475  O  OD2 . ASP   A 1 66  ? -5.224  -6.460  -24.589 1.00 136.72 ? 86  ASP   A OD2 1 
ATOM   476  N  N   . PRO   A 1 67  ? -6.550  -10.018 -24.313 1.00 125.82 ? 87  PRO   A N   1 
ATOM   477  C  CA  . PRO   A 1 67  ? -5.823  -10.952 -23.432 1.00 125.48 ? 87  PRO   A CA  1 
ATOM   478  C  C   . PRO   A 1 67  ? -4.897  -10.275 -22.432 1.00 117.87 ? 87  PRO   A C   1 
ATOM   479  O  O   . PRO   A 1 67  ? -4.774  -10.750 -21.297 1.00 120.56 ? 87  PRO   A O   1 
ATOM   480  C  CB  . PRO   A 1 67  ? -5.043  -11.820 -24.429 1.00 113.13 ? 87  PRO   A CB  1 
ATOM   481  C  CG  . PRO   A 1 67  ? -5.881  -11.805 -25.658 1.00 111.59 ? 87  PRO   A CG  1 
ATOM   482  C  CD  . PRO   A 1 67  ? -6.463  -10.417 -25.729 1.00 126.05 ? 87  PRO   A CD  1 
ATOM   483  N  N   . ASP   A 1 68  ? -4.239  -9.182  -22.821 1.00 112.66 ? 88  ASP   A N   1 
ATOM   484  C  CA  . ASP   A 1 68  ? -3.386  -8.466  -21.877 1.00 116.76 ? 88  ASP   A CA  1 
ATOM   485  C  C   . ASP   A 1 68  ? -4.222  -7.720  -20.844 1.00 114.92 ? 88  ASP   A C   1 
ATOM   486  O  O   . ASP   A 1 68  ? -3.897  -7.728  -19.650 1.00 98.05  ? 88  ASP   A O   1 
ATOM   487  C  CB  . ASP   A 1 68  ? -2.462  -7.505  -22.624 1.00 118.90 ? 88  ASP   A CB  1 
ATOM   488  C  CG  . ASP   A 1 68  ? -1.303  -8.215  -23.301 1.00 125.53 ? 88  ASP   A CG  1 
ATOM   489  O  OD1 . ASP   A 1 68  ? -0.711  -9.125  -22.680 1.00 124.73 ? 88  ASP   A OD1 1 
ATOM   490  O  OD2 . ASP   A 1 68  ? -0.983  -7.861  -24.455 1.00 132.92 ? 88  ASP   A OD2 1 
ATOM   491  N  N   . MET   A 1 69  ? -5.301  -7.070  -21.287 1.00 116.93 ? 89  MET   A N   1 
ATOM   492  C  CA  . MET   A 1 69  ? -6.230  -6.435  -20.357 1.00 116.32 ? 89  MET   A CA  1 
ATOM   493  C  C   . MET   A 1 69  ? -6.824  -7.460  -19.397 1.00 107.87 ? 89  MET   A C   1 
ATOM   494  O  O   . MET   A 1 69  ? -6.942  -7.202  -18.192 1.00 102.05 ? 89  MET   A O   1 
ATOM   495  C  CB  . MET   A 1 69  ? -7.331  -5.720  -21.141 1.00 127.32 ? 89  MET   A CB  1 
ATOM   496  C  CG  . MET   A 1 69  ? -7.581  -4.277  -20.727 1.00 135.40 ? 89  MET   A CG  1 
ATOM   497  S  SD  . MET   A 1 69  ? -8.735  -3.429  -21.828 1.00 143.59 ? 89  MET   A SD  1 
ATOM   498  C  CE  . MET   A 1 69  ? -7.679  -3.061  -23.229 1.00 145.27 ? 89  MET   A CE  1 
ATOM   499  N  N   . ILE   A 1 70  ? -7.185  -8.637  -19.913 1.00 106.88 ? 90  ILE   A N   1 
ATOM   500  C  CA  . ILE   A 1 70  ? -7.707  -9.706  -19.068 1.00 109.27 ? 90  ILE   A CA  1 
ATOM   501  C  C   . ILE   A 1 70  ? -6.636  -10.198 -18.101 1.00 106.83 ? 90  ILE   A C   1 
ATOM   502  O  O   . ILE   A 1 70  ? -6.912  -10.439 -16.919 1.00 91.00  ? 90  ILE   A O   1 
ATOM   503  C  CB  . ILE   A 1 70  ? -8.261  -10.841 -19.949 1.00 122.65 ? 90  ILE   A CB  1 
ATOM   504  C  CG1 . ILE   A 1 70  ? -9.546  -10.384 -20.639 1.00 106.83 ? 90  ILE   A CG1 1 
ATOM   505  C  CG2 . ILE   A 1 70  ? -8.502  -12.111 -19.137 1.00 107.47 ? 90  ILE   A CG2 1 
ATOM   506  C  CD1 . ILE   A 1 70  ? -9.916  -11.207 -21.842 1.00 108.97 ? 90  ILE   A CD1 1 
ATOM   507  N  N   . LYS   A 1 71  ? -5.399  -10.346 -18.583 1.00 109.77 ? 91  LYS   A N   1 
ATOM   508  C  CA  . LYS   A 1 71  ? -4.294  -10.694 -17.694 1.00 101.73 ? 91  LYS   A CA  1 
ATOM   509  C  C   . LYS   A 1 71  ? -4.062  -9.600  -16.659 1.00 94.76  ? 91  LYS   A C   1 
ATOM   510  O  O   . LYS   A 1 71  ? -3.751  -9.887  -15.496 1.00 92.58  ? 91  LYS   A O   1 
ATOM   511  C  CB  . LYS   A 1 71  ? -3.026  -10.943 -18.512 1.00 114.21 ? 91  LYS   A CB  1 
ATOM   512  C  CG  . LYS   A 1 71  ? -1.825  -11.402 -17.706 1.00 112.76 ? 91  LYS   A CG  1 
ATOM   513  C  CD  . LYS   A 1 71  ? -0.605  -11.542 -18.600 1.00 128.84 ? 91  LYS   A CD  1 
ATOM   514  C  CE  . LYS   A 1 71  ? 0.618   -11.987 -17.820 1.00 137.47 ? 91  LYS   A CE  1 
ATOM   515  N  NZ  . LYS   A 1 71  ? 1.860   -11.876 -18.636 1.00 138.28 ? 91  LYS   A NZ  1 
ATOM   516  N  N   . THR   A 1 72  ? -4.215  -8.337  -17.066 1.00 95.57  ? 92  THR   A N   1 
ATOM   517  C  CA  . THR   A 1 72  ? -4.086  -7.225  -16.129 1.00 110.92 ? 92  THR   A CA  1 
ATOM   518  C  C   . THR   A 1 72  ? -5.145  -7.304  -15.038 1.00 113.42 ? 92  THR   A C   1 
ATOM   519  O  O   . THR   A 1 72  ? -4.832  -7.234  -13.843 1.00 112.83 ? 92  THR   A O   1 
ATOM   520  C  CB  . THR   A 1 72  ? -4.196  -5.896  -16.878 1.00 105.38 ? 92  THR   A CB  1 
ATOM   521  O  OG1 . THR   A 1 72  ? -3.229  -5.856  -17.935 1.00 112.12 ? 92  THR   A OG1 1 
ATOM   522  C  CG2 . THR   A 1 72  ? -3.964  -4.730  -15.930 1.00 90.99  ? 92  THR   A CG2 1 
ATOM   523  N  N   . VAL   A 1 73  ? -6.406  -7.472  -15.436 1.00 103.76 ? 93  VAL   A N   1 
ATOM   524  C  CA  . VAL   A 1 73  ? -7.512  -7.419  -14.484 1.00 107.96 ? 93  VAL   A CA  1 
ATOM   525  C  C   . VAL   A 1 73  ? -7.433  -8.581  -13.502 1.00 101.84 ? 93  VAL   A C   1 
ATOM   526  O  O   . VAL   A 1 73  ? -7.395  -8.384  -12.282 1.00 90.15  ? 93  VAL   A O   1 
ATOM   527  C  CB  . VAL   A 1 73  ? -8.860  -7.402  -15.225 1.00 118.47 ? 93  VAL   A CB  1 
ATOM   528  C  CG1 . VAL   A 1 73  ? -9.993  -7.742  -14.271 1.00 103.82 ? 93  VAL   A CG1 1 
ATOM   529  C  CG2 . VAL   A 1 73  ? -9.091  -6.044  -15.853 1.00 94.85  ? 93  VAL   A CG2 1 
ATOM   530  N  N   . LEU   A 1 74  ? -7.391  -9.808  -14.021 1.00 96.92  ? 94  LEU   A N   1 
ATOM   531  C  CA  . LEU   A 1 74  ? -7.551  -10.984 -13.177 1.00 93.23  ? 94  LEU   A CA  1 
ATOM   532  C  C   . LEU   A 1 74  ? -6.295  -11.339 -12.393 1.00 103.67 ? 94  LEU   A C   1 
ATOM   533  O  O   . LEU   A 1 74  ? -6.399  -12.020 -11.367 1.00 102.42 ? 94  LEU   A O   1 
ATOM   534  C  CB  . LEU   A 1 74  ? -7.974  -12.184 -14.028 1.00 106.38 ? 94  LEU   A CB  1 
ATOM   535  C  CG  . LEU   A 1 74  ? -9.251  -12.025 -14.856 1.00 115.46 ? 94  LEU   A CG  1 
ATOM   536  C  CD1 . LEU   A 1 74  ? -9.475  -13.237 -15.750 1.00 109.51 ? 94  LEU   A CD1 1 
ATOM   537  C  CD2 . LEU   A 1 74  ? -10.451 -11.797 -13.952 1.00 104.39 ? 94  LEU   A CD2 1 
ATOM   538  N  N   . VAL   A 1 75  ? -5.119  -10.900 -12.841 1.00 93.27  ? 95  VAL   A N   1 
ATOM   539  C  CA  . VAL   A 1 75  ? -3.869  -11.367 -12.253 1.00 113.51 ? 95  VAL   A CA  1 
ATOM   540  C  C   . VAL   A 1 75  ? -3.022  -10.197 -11.770 1.00 114.72 ? 95  VAL   A C   1 
ATOM   541  O  O   . VAL   A 1 75  ? -2.697  -10.103 -10.580 1.00 121.31 ? 95  VAL   A O   1 
ATOM   542  C  CB  . VAL   A 1 75  ? -3.078  -12.228 -13.256 1.00 119.74 ? 95  VAL   A CB  1 
ATOM   543  C  CG1 . VAL   A 1 75  ? -1.921  -12.921 -12.558 1.00 76.97  ? 95  VAL   A CG1 1 
ATOM   544  C  CG2 . VAL   A 1 75  ? -3.989  -13.246 -13.930 1.00 111.83 ? 95  VAL   A CG2 1 
ATOM   545  N  N   . LYS   A 1 76  ? -2.655  -9.303  -12.692 1.00 116.58 ? 96  LYS   A N   1 
ATOM   546  C  CA  . LYS   A 1 76  ? -1.683  -8.259  -12.379 1.00 115.10 ? 96  LYS   A CA  1 
ATOM   547  C  C   . LYS   A 1 76  ? -2.219  -7.297  -11.325 1.00 117.20 ? 96  LYS   A C   1 
ATOM   548  O  O   . LYS   A 1 76  ? -1.539  -7.004  -10.335 1.00 120.31 ? 96  LYS   A O   1 
ATOM   549  C  CB  . LYS   A 1 76  ? -1.292  -7.509  -13.655 1.00 119.55 ? 96  LYS   A CB  1 
ATOM   550  C  CG  . LYS   A 1 76  ? -0.492  -8.356  -14.628 1.00 130.00 ? 96  LYS   A CG  1 
ATOM   551  C  CD  . LYS   A 1 76  ? -0.297  -7.660  -15.962 1.00 134.89 ? 96  LYS   A CD  1 
ATOM   552  C  CE  . LYS   A 1 76  ? 0.572   -8.496  -16.889 1.00 146.86 ? 96  LYS   A CE  1 
ATOM   553  N  NZ  . LYS   A 1 76  ? 0.681   -7.898  -18.250 1.00 160.95 ? 96  LYS   A NZ  1 
ATOM   554  N  N   . GLU   A 1 77  ? -3.446  -6.807  -11.510 1.00 125.01 ? 97  GLU   A N   1 
ATOM   555  C  CA  . GLU   A 1 77  ? -4.046  -5.841  -10.597 1.00 121.00 ? 97  GLU   A CA  1 
ATOM   556  C  C   . GLU   A 1 77  ? -5.160  -6.459  -9.759  1.00 112.93 ? 97  GLU   A C   1 
ATOM   557  O  O   . GLU   A 1 77  ? -6.126  -5.781  -9.401  1.00 105.88 ? 97  GLU   A O   1 
ATOM   558  C  CB  . GLU   A 1 77  ? -4.570  -4.631  -11.367 1.00 110.82 ? 97  GLU   A CB  1 
ATOM   559  C  CG  . GLU   A 1 77  ? -3.560  -4.042  -12.336 1.00 119.43 ? 97  GLU   A CG  1 
ATOM   560  C  CD  . GLU   A 1 77  ? -2.257  -3.649  -11.666 1.00 129.78 ? 97  GLU   A CD  1 
ATOM   561  O  OE1 . GLU   A 1 77  ? -2.309  -3.069  -10.561 1.00 120.91 ? 97  GLU   A OE1 1 
ATOM   562  O  OE2 . GLU   A 1 77  ? -1.181  -3.919  -12.245 1.00 123.29 ? 97  GLU   A OE2 1 
ATOM   563  N  N   . CYS   A 1 78  ? -5.028  -7.744  -9.429  1.00 117.99 ? 98  CYS   A N   1 
ATOM   564  C  CA  . CYS   A 1 78  ? -6.052  -8.417  -8.639  1.00 99.36  ? 98  CYS   A CA  1 
ATOM   565  C  C   . CYS   A 1 78  ? -6.053  -7.911  -7.201  1.00 100.31 ? 98  CYS   A C   1 
ATOM   566  O  O   . CYS   A 1 78  ? -7.047  -7.349  -6.727  1.00 101.59 ? 98  CYS   A O   1 
ATOM   567  C  CB  . CYS   A 1 78  ? -5.836  -9.932  -8.683  1.00 91.41  ? 98  CYS   A CB  1 
ATOM   568  S  SG  . CYS   A 1 78  ? -6.937  -10.873 -7.600  1.00 93.58  ? 98  CYS   A SG  1 
ATOM   569  N  N   . TYR   A 1 79  ? -4.935  -8.095  -6.490  1.00 110.39 ? 99  TYR   A N   1 
ATOM   570  C  CA  . TYR   A 1 79  ? -4.876  -7.716  -5.081  1.00 112.04 ? 99  TYR   A CA  1 
ATOM   571  C  C   . TYR   A 1 79  ? -5.123  -6.228  -4.876  1.00 107.08 ? 99  TYR   A C   1 
ATOM   572  O  O   . TYR   A 1 79  ? -5.623  -5.824  -3.820  1.00 111.38 ? 99  TYR   A O   1 
ATOM   573  C  CB  . TYR   A 1 79  ? -3.520  -8.090  -4.487  1.00 117.64 ? 99  TYR   A CB  1 
ATOM   574  C  CG  . TYR   A 1 79  ? -3.335  -9.556  -4.188  1.00 132.16 ? 99  TYR   A CG  1 
ATOM   575  C  CD1 . TYR   A 1 79  ? -3.904  -10.128 -3.059  1.00 133.30 ? 99  TYR   A CD1 1 
ATOM   576  C  CD2 . TYR   A 1 79  ? -2.570  -10.363 -5.020  1.00 135.33 ? 99  TYR   A CD2 1 
ATOM   577  C  CE1 . TYR   A 1 79  ? -3.731  -11.463 -2.772  1.00 137.98 ? 99  TYR   A CE1 1 
ATOM   578  C  CE2 . TYR   A 1 79  ? -2.388  -11.702 -4.741  1.00 137.76 ? 99  TYR   A CE2 1 
ATOM   579  C  CZ  . TYR   A 1 79  ? -2.973  -12.246 -3.615  1.00 149.14 ? 99  TYR   A CZ  1 
ATOM   580  O  OH  . TYR   A 1 79  ? -2.804  -13.579 -3.321  1.00 162.42 ? 99  TYR   A OH  1 
ATOM   581  N  N   . SER   A 1 80  ? -4.786  -5.402  -5.865  1.00 102.56 ? 100 SER   A N   1 
ATOM   582  C  CA  . SER   A 1 80  ? -4.834  -3.953  -5.710  1.00 109.15 ? 100 SER   A CA  1 
ATOM   583  C  C   . SER   A 1 80  ? -6.204  -3.364  -6.038  1.00 117.35 ? 100 SER   A C   1 
ATOM   584  O  O   . SER   A 1 80  ? -6.786  -2.654  -5.212  1.00 112.47 ? 100 SER   A O   1 
ATOM   585  C  CB  . SER   A 1 80  ? -3.750  -3.308  -6.582  1.00 105.50 ? 100 SER   A CB  1 
ATOM   586  O  OG  . SER   A 1 80  ? -3.790  -3.803  -7.910  1.00 115.31 ? 100 SER   A OG  1 
ATOM   587  N  N   . VAL   A 1 81  ? -6.738  -3.645  -7.229  1.00 109.63 ? 101 VAL   A N   1 
ATOM   588  C  CA  . VAL   A 1 81  ? -7.909  -2.949  -7.745  1.00 107.84 ? 101 VAL   A CA  1 
ATOM   589  C  C   . VAL   A 1 81  ? -9.087  -3.887  -7.979  1.00 102.79 ? 101 VAL   A C   1 
ATOM   590  O  O   . VAL   A 1 81  ? -10.237 -3.521  -7.712  1.00 102.22 ? 101 VAL   A O   1 
ATOM   591  C  CB  . VAL   A 1 81  ? -7.569  -2.177  -9.039  1.00 106.93 ? 101 VAL   A CB  1 
ATOM   592  C  CG1 . VAL   A 1 81  ? -8.775  -1.376  -9.521  1.00 109.93 ? 101 VAL   A CG1 1 
ATOM   593  C  CG2 . VAL   A 1 81  ? -6.374  -1.267  -8.810  1.00 111.00 ? 101 VAL   A CG2 1 
ATOM   594  N  N   . PHE   A 1 82  ? -8.834  -5.094  -8.481  1.00 107.69 ? 102 PHE   A N   1 
ATOM   595  C  CA  . PHE   A 1 82  ? -9.925  -5.989  -8.852  1.00 87.80  ? 102 PHE   A CA  1 
ATOM   596  C  C   . PHE   A 1 82  ? -10.008 -7.178  -7.903  1.00 84.46  ? 102 PHE   A C   1 
ATOM   597  O  O   . PHE   A 1 82  ? -9.887  -8.332  -8.325  1.00 94.78  ? 102 PHE   A O   1 
ATOM   598  C  CB  . PHE   A 1 82  ? -9.748  -6.452  -10.298 1.00 93.79  ? 102 PHE   A CB  1 
ATOM   599  C  CG  . PHE   A 1 82  ? -9.496  -5.325  -11.259 1.00 102.83 ? 102 PHE   A CG  1 
ATOM   600  C  CD1 . PHE   A 1 82  ? -10.508 -4.439  -11.585 1.00 98.51  ? 102 PHE   A CD1 1 
ATOM   601  C  CD2 . PHE   A 1 82  ? -8.246  -5.144  -11.826 1.00 105.13 ? 102 PHE   A CD2 1 
ATOM   602  C  CE1 . PHE   A 1 82  ? -10.280 -3.397  -12.464 1.00 101.83 ? 102 PHE   A CE1 1 
ATOM   603  C  CE2 . PHE   A 1 82  ? -8.012  -4.104  -12.707 1.00 107.31 ? 102 PHE   A CE2 1 
ATOM   604  C  CZ  . PHE   A 1 82  ? -9.031  -3.229  -13.025 1.00 103.32 ? 102 PHE   A CZ  1 
ATOM   605  N  N   . THR   A 1 83  ? -10.225 -6.902  -6.617  1.00 94.00  ? 103 THR   A N   1 
ATOM   606  C  CA  . THR   A 1 83  ? -10.220 -7.963  -5.618  1.00 93.91  ? 103 THR   A CA  1 
ATOM   607  C  C   . THR   A 1 83  ? -11.557 -8.691  -5.538  1.00 76.82  ? 103 THR   A C   1 
ATOM   608  O  O   . THR   A 1 83  ? -11.585 -9.902  -5.293  1.00 78.90  ? 103 THR   A O   1 
ATOM   609  C  CB  . THR   A 1 83  ? -9.862  -7.385  -4.243  1.00 84.51  ? 103 THR   A CB  1 
ATOM   610  O  OG1 . THR   A 1 83  ? -8.645  -6.633  -4.333  1.00 94.23  ? 103 THR   A OG1 1 
ATOM   611  C  CG2 . THR   A 1 83  ? -9.688  -8.495  -3.219  1.00 97.13  ? 103 THR   A CG2 1 
ATOM   612  N  N   . ASN   A 1 84  ? -12.664 -7.985  -5.751  1.00 90.65  ? 104 ASN   A N   1 
ATOM   613  C  CA  . ASN   A 1 84  ? -13.977 -8.469  -5.357  1.00 81.27  ? 104 ASN   A CA  1 
ATOM   614  C  C   . ASN   A 1 84  ? -14.931 -8.524  -6.544  1.00 83.79  ? 104 ASN   A C   1 
ATOM   615  O  O   . ASN   A 1 84  ? -14.791 -7.774  -7.516  1.00 85.02  ? 104 ASN   A O   1 
ATOM   616  C  CB  . ASN   A 1 84  ? -14.568 -7.575  -4.257  1.00 83.09  ? 104 ASN   A CB  1 
ATOM   617  C  CG  . ASN   A 1 84  ? -13.572 -7.287  -3.143  1.00 89.11  ? 104 ASN   A CG  1 
ATOM   618  O  OD1 . ASN   A 1 84  ? -12.846 -8.177  -2.705  1.00 85.69  ? 104 ASN   A OD1 1 
ATOM   619  N  ND2 . ASN   A 1 84  ? -13.526 -6.036  -2.690  1.00 94.10  ? 104 ASN   A ND2 1 
ATOM   620  N  N   . ARG   A 1 85  ? -15.914 -9.416  -6.442  1.00 85.90  ? 105 ARG   A N   1 
ATOM   621  C  CA  . ARG   A 1 85  ? -16.959 -9.561  -7.440  1.00 72.62  ? 105 ARG   A CA  1 
ATOM   622  C  C   . ARG   A 1 85  ? -18.109 -8.604  -7.140  1.00 101.43 ? 105 ARG   A C   1 
ATOM   623  O  O   . ARG   A 1 85  ? -18.087 -7.844  -6.167  1.00 88.26  ? 105 ARG   A O   1 
ATOM   624  C  CB  . ARG   A 1 85  ? -17.451 -11.005 -7.487  1.00 89.18  ? 105 ARG   A CB  1 
ATOM   625  C  CG  . ARG   A 1 85  ? -16.351 -12.010 -7.770  1.00 94.15  ? 105 ARG   A CG  1 
ATOM   626  C  CD  . ARG   A 1 85  ? -16.901 -13.378 -8.119  1.00 95.57  ? 105 ARG   A CD  1 
ATOM   627  N  NE  . ARG   A 1 85  ? -15.860 -14.233 -8.676  1.00 113.89 ? 105 ARG   A NE  1 
ATOM   628  C  CZ  . ARG   A 1 85  ? -15.060 -15.005 -7.955  1.00 101.93 ? 105 ARG   A CZ  1 
ATOM   629  N  NH1 . ARG   A 1 85  ? -15.166 -15.070 -6.638  1.00 107.25 ? 105 ARG   A NH1 1 
ATOM   630  N  NH2 . ARG   A 1 85  ? -14.132 -15.732 -8.570  1.00 95.26  ? 105 ARG   A NH2 1 
ATOM   631  N  N   . ARG   A 1 86  ? -19.131 -8.648  -7.986  1.00 95.71  ? 106 ARG   A N   1 
ATOM   632  C  CA  . ARG   A 1 86  ? -20.283 -7.779  -7.806  1.00 98.99  ? 106 ARG   A CA  1 
ATOM   633  C  C   . ARG   A 1 86  ? -20.962 -8.089  -6.474  1.00 103.83 ? 106 ARG   A C   1 
ATOM   634  O  O   . ARG   A 1 86  ? -21.134 -9.267  -6.129  1.00 90.81  ? 106 ARG   A O   1 
ATOM   635  C  CB  . ARG   A 1 86  ? -21.269 -7.951  -8.962  1.00 104.47 ? 106 ARG   A CB  1 
ATOM   636  C  CG  . ARG   A 1 86  ? -22.349 -6.885  -9.031  1.00 114.11 ? 106 ARG   A CG  1 
ATOM   637  C  CD  . ARG   A 1 86  ? -23.282 -7.121  -10.207 1.00 113.90 ? 106 ARG   A CD  1 
ATOM   638  N  NE  . ARG   A 1 86  ? -22.555 -7.430  -11.433 1.00 102.18 ? 106 ARG   A NE  1 
ATOM   639  C  CZ  . ARG   A 1 86  ? -23.076 -7.353  -12.650 1.00 99.23  ? 106 ARG   A CZ  1 
ATOM   640  N  NH1 . ARG   A 1 86  ? -24.316 -6.935  -12.845 1.00 109.01 ? 106 ARG   A NH1 1 
ATOM   641  N  NH2 . ARG   A 1 86  ? -22.334 -7.701  -13.697 1.00 104.62 ? 106 ARG   A NH2 1 
ATOM   642  N  N   . PRO   A 1 87  ? -21.327 -7.076  -5.692  1.00 111.13 ? 107 PRO   A N   1 
ATOM   643  C  CA  . PRO   A 1 87  ? -22.039 -7.331  -4.434  1.00 114.89 ? 107 PRO   A CA  1 
ATOM   644  C  C   . PRO   A 1 87  ? -23.318 -8.121  -4.675  1.00 127.89 ? 107 PRO   A C   1 
ATOM   645  O  O   . PRO   A 1 87  ? -24.115 -7.799  -5.559  1.00 130.71 ? 107 PRO   A O   1 
ATOM   646  C  CB  . PRO   A 1 87  ? -22.323 -5.923  -3.892  1.00 109.00 ? 107 PRO   A CB  1 
ATOM   647  C  CG  . PRO   A 1 87  ? -22.100 -4.990  -5.057  1.00 115.03 ? 107 PRO   A CG  1 
ATOM   648  C  CD  . PRO   A 1 87  ? -21.058 -5.644  -5.901  1.00 108.12 ? 107 PRO   A CD  1 
ATOM   649  N  N   . PHE   A 1 88  ? -23.496 -9.174  -3.884  1.00 132.55 ? 108 PHE   A N   1 
ATOM   650  C  CA  . PHE   A 1 88  ? -24.582 -10.129 -4.059  1.00 144.63 ? 108 PHE   A CA  1 
ATOM   651  C  C   . PHE   A 1 88  ? -25.411 -10.161 -2.786  1.00 156.59 ? 108 PHE   A C   1 
ATOM   652  O  O   . PHE   A 1 88  ? -24.889 -10.468 -1.709  1.00 156.77 ? 108 PHE   A O   1 
ATOM   653  C  CB  . PHE   A 1 88  ? -24.027 -11.517 -4.387  1.00 146.88 ? 108 PHE   A CB  1 
ATOM   654  C  CG  . PHE   A 1 88  ? -25.070 -12.508 -4.811  1.00 150.17 ? 108 PHE   A CG  1 
ATOM   655  C  CD1 . PHE   A 1 88  ? -25.754 -12.342 -6.004  1.00 154.09 ? 108 PHE   A CD1 1 
ATOM   656  C  CD2 . PHE   A 1 88  ? -25.352 -13.617 -4.028  1.00 148.53 ? 108 PHE   A CD2 1 
ATOM   657  C  CE1 . PHE   A 1 88  ? -26.712 -13.255 -6.405  1.00 156.93 ? 108 PHE   A CE1 1 
ATOM   658  C  CE2 . PHE   A 1 88  ? -26.309 -14.537 -4.422  1.00 149.93 ? 108 PHE   A CE2 1 
ATOM   659  C  CZ  . PHE   A 1 88  ? -26.990 -14.355 -5.613  1.00 154.67 ? 108 PHE   A CZ  1 
ATOM   660  N  N   . GLY   A 1 89  ? -26.695 -9.842  -2.907  1.00 189.38 ? 109 GLY   A N   1 
ATOM   661  C  CA  . GLY   A 1 89  ? -27.575 -9.816  -1.765  1.00 191.05 ? 109 GLY   A CA  1 
ATOM   662  C  C   . GLY   A 1 89  ? -29.028 -9.991  -2.148  1.00 188.99 ? 109 GLY   A C   1 
ATOM   663  O  O   . GLY   A 1 89  ? -29.411 -9.845  -3.313  1.00 193.68 ? 109 GLY   A O   1 
ATOM   664  N  N   . PRO   A 1 90  ? -29.875 -10.312 -1.164  1.00 170.68 ? 110 PRO   A N   1 
ATOM   665  C  CA  . PRO   A 1 90  ? -29.562 -10.507 0.260   1.00 171.25 ? 110 PRO   A CA  1 
ATOM   666  C  C   . PRO   A 1 90  ? -28.920 -11.865 0.531   1.00 171.47 ? 110 PRO   A C   1 
ATOM   667  O  O   . PRO   A 1 90  ? -29.365 -12.886 0.013   1.00 163.05 ? 110 PRO   A O   1 
ATOM   668  C  CB  . PRO   A 1 90  ? -30.937 -10.381 0.923   1.00 165.50 ? 110 PRO   A CB  1 
ATOM   669  C  CG  . PRO   A 1 90  ? -31.878 -10.949 -0.107  1.00 161.87 ? 110 PRO   A CG  1 
ATOM   670  C  CD  . PRO   A 1 90  ? -31.305 -10.537 -1.445  1.00 170.05 ? 110 PRO   A CD  1 
ATOM   671  N  N   . VAL   A 1 91  ? -27.865 -11.903 1.347   1.00 163.01 ? 111 VAL   A N   1 
ATOM   672  C  CA  . VAL   A 1 91  ? -27.132 -13.127 1.631   1.00 156.43 ? 111 VAL   A CA  1 
ATOM   673  C  C   . VAL   A 1 91  ? -27.237 -13.527 3.097   1.00 162.51 ? 111 VAL   A C   1 
ATOM   674  O  O   . VAL   A 1 91  ? -27.345 -14.718 3.413   1.00 166.16 ? 111 VAL   A O   1 
ATOM   675  C  CB  . VAL   A 1 91  ? -25.652 -12.993 1.216   1.00 154.94 ? 111 VAL   A CB  1 
ATOM   676  C  CG1 . VAL   A 1 91  ? -25.490 -13.288 -0.264  1.00 150.40 ? 111 VAL   A CG1 1 
ATOM   677  C  CG2 . VAL   A 1 91  ? -25.141 -11.598 1.539   1.00 164.40 ? 111 VAL   A CG2 1 
ATOM   678  N  N   . GLY   A 1 92  ? -27.200 -12.558 4.008   1.00 185.49 ? 112 GLY   A N   1 
ATOM   679  C  CA  . GLY   A 1 92  ? -27.227 -12.854 5.428   1.00 180.89 ? 112 GLY   A CA  1 
ATOM   680  C  C   . GLY   A 1 92  ? -25.873 -13.275 5.958   1.00 174.39 ? 112 GLY   A C   1 
ATOM   681  O  O   . GLY   A 1 92  ? -24.859 -12.640 5.653   1.00 174.74 ? 112 GLY   A O   1 
ATOM   682  N  N   . PHE   A 1 93  ? -25.840 -14.348 6.754   1.00 159.32 ? 113 PHE   A N   1 
ATOM   683  C  CA  . PHE   A 1 93  ? -24.569 -14.869 7.242   1.00 158.15 ? 113 PHE   A CA  1 
ATOM   684  C  C   . PHE   A 1 93  ? -23.670 -15.338 6.106   1.00 159.59 ? 113 PHE   A C   1 
ATOM   685  O  O   . PHE   A 1 93  ? -22.450 -15.411 6.284   1.00 160.10 ? 113 PHE   A O   1 
ATOM   686  C  CB  . PHE   A 1 93  ? -24.809 -16.020 8.222   1.00 166.40 ? 113 PHE   A CB  1 
ATOM   687  C  CG  . PHE   A 1 93  ? -25.255 -17.292 7.561   1.00 177.81 ? 113 PHE   A CG  1 
ATOM   688  C  CD1 . PHE   A 1 93  ? -26.581 -17.472 7.205   1.00 182.32 ? 113 PHE   A CD1 1 
ATOM   689  C  CD2 . PHE   A 1 93  ? -24.347 -18.306 7.293   1.00 172.61 ? 113 PHE   A CD2 1 
ATOM   690  C  CE1 . PHE   A 1 93  ? -26.996 -18.638 6.592   1.00 187.45 ? 113 PHE   A CE1 1 
ATOM   691  C  CE2 . PHE   A 1 93  ? -24.755 -19.475 6.681   1.00 173.97 ? 113 PHE   A CE2 1 
ATOM   692  C  CZ  . PHE   A 1 93  ? -26.082 -19.642 6.330   1.00 186.05 ? 113 PHE   A CZ  1 
ATOM   693  N  N   . MET   A 1 94  ? -24.246 -15.650 4.941   1.00 159.24 ? 114 MET   A N   1 
ATOM   694  C  CA  . MET   A 1 94  ? -23.468 -16.087 3.787   1.00 158.46 ? 114 MET   A CA  1 
ATOM   695  C  C   . MET   A 1 94  ? -22.569 -14.993 3.227   1.00 154.37 ? 114 MET   A C   1 
ATOM   696  O  O   . MET   A 1 94  ? -21.789 -15.270 2.308   1.00 148.05 ? 114 MET   A O   1 
ATOM   697  C  CB  . MET   A 1 94  ? -24.401 -16.600 2.689   1.00 158.93 ? 114 MET   A CB  1 
ATOM   698  C  CG  . MET   A 1 94  ? -25.098 -17.908 3.029   1.00 157.98 ? 114 MET   A CG  1 
ATOM   699  S  SD  . MET   A 1 94  ? -23.945 -19.285 3.188   1.00 141.00 ? 114 MET   A SD  1 
ATOM   700  C  CE  . MET   A 1 94  ? -23.228 -19.317 1.547   1.00 131.27 ? 114 MET   A CE  1 
ATOM   701  N  N   . LYS   A 1 95  ? -22.661 -13.765 3.746   1.00 168.67 ? 115 LYS   A N   1 
ATOM   702  C  CA  . LYS   A 1 95  ? -21.703 -12.726 3.384   1.00 167.47 ? 115 LYS   A CA  1 
ATOM   703  C  C   . LYS   A 1 95  ? -20.274 -13.138 3.711   1.00 152.97 ? 115 LYS   A C   1 
ATOM   704  O  O   . LYS   A 1 95  ? -19.332 -12.598 3.120   1.00 156.19 ? 115 LYS   A O   1 
ATOM   705  C  CB  . LYS   A 1 95  ? -22.038 -11.423 4.112   1.00 171.16 ? 115 LYS   A CB  1 
ATOM   706  C  CG  . LYS   A 1 95  ? -21.502 -11.381 5.535   1.00 171.65 ? 115 LYS   A CG  1 
ATOM   707  C  CD  . LYS   A 1 95  ? -21.849 -10.096 6.256   1.00 175.42 ? 115 LYS   A CD  1 
ATOM   708  C  CE  . LYS   A 1 95  ? -21.142 -10.046 7.601   1.00 175.99 ? 115 LYS   A CE  1 
ATOM   709  N  NZ  . LYS   A 1 95  ? -21.218 -11.362 8.301   1.00 164.72 ? 115 LYS   A NZ  1 
ATOM   710  N  N   . SER   A 1 96  ? -20.100 -14.078 4.639   1.00 147.68 ? 116 SER   A N   1 
ATOM   711  C  CA  A SER   A 1 96  ? -18.791 -14.565 5.051   0.56 144.96 ? 116 SER   A CA  1 
ATOM   712  C  CA  B SER   A 1 96  ? -18.782 -14.552 5.038   0.44 144.50 ? 116 SER   A CA  1 
ATOM   713  C  C   . SER   A 1 96  ? -18.287 -15.715 4.190   1.00 135.25 ? 116 SER   A C   1 
ATOM   714  O  O   . SER   A 1 96  ? -17.161 -16.175 4.399   1.00 130.81 ? 116 SER   A O   1 
ATOM   715  C  CB  A SER   A 1 96  ? -18.833 -15.001 6.520   0.56 148.75 ? 116 SER   A CB  1 
ATOM   716  C  CB  B SER   A 1 96  ? -18.793 -14.966 6.512   0.44 148.22 ? 116 SER   A CB  1 
ATOM   717  O  OG  A SER   A 1 96  ? -19.888 -15.920 6.758   0.56 148.36 ? 116 SER   A OG  1 
ATOM   718  O  OG  B SER   A 1 96  ? -19.038 -13.851 7.350   0.44 151.35 ? 116 SER   A OG  1 
ATOM   719  N  N   . ALA   A 1 97  ? -19.095 -16.200 3.250   1.00 130.00 ? 117 ALA   A N   1 
ATOM   720  C  CA  . ALA   A 1 97  ? -18.635 -17.235 2.336   1.00 123.68 ? 117 ALA   A CA  1 
ATOM   721  C  C   . ALA   A 1 97  ? -17.498 -16.689 1.481   1.00 114.45 ? 117 ALA   A C   1 
ATOM   722  O  O   . ALA   A 1 97  ? -17.481 -15.506 1.130   1.00 114.61 ? 117 ALA   A O   1 
ATOM   723  C  CB  . ALA   A 1 97  ? -19.789 -17.720 1.458   1.00 123.10 ? 117 ALA   A CB  1 
ATOM   724  N  N   . ILE   A 1 98  ? -16.534 -17.557 1.158   1.00 102.72 ? 118 ILE   A N   1 
ATOM   725  C  CA  . ILE   A 1 98  ? -15.299 -17.100 0.520   1.00 107.42 ? 118 ILE   A CA  1 
ATOM   726  C  C   . ILE   A 1 98  ? -15.601 -16.430 -0.815  1.00 107.20 ? 118 ILE   A C   1 
ATOM   727  O  O   . ILE   A 1 98  ? -15.051 -15.370 -1.137  1.00 100.01 ? 118 ILE   A O   1 
ATOM   728  C  CB  . ILE   A 1 98  ? -14.308 -18.269 0.356   1.00 106.07 ? 118 ILE   A CB  1 
ATOM   729  C  CG1 . ILE   A 1 98  ? -13.074 -17.816 -0.428  1.00 105.07 ? 118 ILE   A CG1 1 
ATOM   730  C  CG2 . ILE   A 1 98  ? -14.968 -19.460 -0.326  1.00 98.60  ? 118 ILE   A CG2 1 
ATOM   731  C  CD1 . ILE   A 1 98  ? -12.005 -18.878 -0.553  1.00 107.05 ? 118 ILE   A CD1 1 
ATOM   732  N  N   . SER   A 1 99  ? -16.497 -17.027 -1.602  1.00 107.38 ? 119 SER   A N   1 
ATOM   733  C  CA  . SER   A 1 99  ? -16.805 -16.490 -2.921  1.00 103.21 ? 119 SER   A CA  1 
ATOM   734  C  C   . SER   A 1 99  ? -17.522 -15.150 -2.841  1.00 105.89 ? 119 SER   A C   1 
ATOM   735  O  O   . SER   A 1 99  ? -17.497 -14.384 -3.811  1.00 107.88 ? 119 SER   A O   1 
ATOM   736  C  CB  . SER   A 1 99  ? -17.643 -17.499 -3.704  1.00 101.70 ? 119 SER   A CB  1 
ATOM   737  O  OG  . SER   A 1 99  ? -18.797 -17.878 -2.972  1.00 103.95 ? 119 SER   A OG  1 
ATOM   738  N  N   . ILE   A 1 100 ? -18.139 -14.841 -1.703  1.00 101.68 ? 120 ILE   A N   1 
ATOM   739  C  CA  . ILE   A 1 100 ? -18.884 -13.599 -1.545  1.00 106.11 ? 120 ILE   A CA  1 
ATOM   740  C  C   . ILE   A 1 100 ? -18.123 -12.556 -0.726  1.00 103.78 ? 120 ILE   A C   1 
ATOM   741  O  O   . ILE   A 1 100 ? -18.395 -11.353 -0.874  1.00 86.40  ? 120 ILE   A O   1 
ATOM   742  C  CB  . ILE   A 1 100 ? -20.267 -13.889 -0.921  1.00 116.46 ? 120 ILE   A CB  1 
ATOM   743  C  CG1 . ILE   A 1 100 ? -20.984 -14.978 -1.720  1.00 117.52 ? 120 ILE   A CG1 1 
ATOM   744  C  CG2 . ILE   A 1 100 ? -21.139 -12.641 -0.885  1.00 125.10 ? 120 ILE   A CG2 1 
ATOM   745  C  CD1 . ILE   A 1 100 ? -22.346 -15.349 -1.172  1.00 131.11 ? 120 ILE   A CD1 1 
ATOM   746  N  N   . ALA   A 1 101 ? -17.166 -12.971 0.104   1.00 103.60 ? 121 ALA   A N   1 
ATOM   747  C  CA  . ALA   A 1 101 ? -16.420 -12.038 0.937   1.00 103.11 ? 121 ALA   A CA  1 
ATOM   748  C  C   . ALA   A 1 101 ? -15.481 -11.180 0.092   1.00 95.48  ? 121 ALA   A C   1 
ATOM   749  O  O   . ALA   A 1 101 ? -15.105 -11.533 -1.030  1.00 99.53  ? 121 ALA   A O   1 
ATOM   750  C  CB  . ALA   A 1 101 ? -15.621 -12.791 2.002   1.00 117.72 ? 121 ALA   A CB  1 
ATOM   751  N  N   . GLU   A 1 102 ? -15.078 -10.046 0.663   1.00 102.49 ? 122 GLU   A N   1 
ATOM   752  C  CA  . GLU   A 1 102 ? -14.338 -9.019  -0.053  1.00 100.31 ? 122 GLU   A CA  1 
ATOM   753  C  C   . GLU   A 1 102 ? -13.026 -8.681  0.648   1.00 99.07  ? 122 GLU   A C   1 
ATOM   754  O  O   . GLU   A 1 102 ? -12.862 -8.911  1.850   1.00 99.92  ? 122 GLU   A O   1 
ATOM   755  C  CB  . GLU   A 1 102 ? -15.181 -7.747  -0.190  1.00 95.88  ? 122 GLU   A CB  1 
ATOM   756  C  CG  . GLU   A 1 102 ? -16.413 -7.892  -1.059  1.00 96.46  ? 122 GLU   A CG  1 
ATOM   757  C  CD  . GLU   A 1 102 ? -17.320 -6.677  -0.974  1.00 108.10 ? 122 GLU   A CD  1 
ATOM   758  O  OE1 . GLU   A 1 102 ? -17.167 -5.880  -0.023  1.00 113.57 ? 122 GLU   A OE1 1 
ATOM   759  O  OE2 . GLU   A 1 102 ? -18.186 -6.515  -1.857  1.00 103.51 ? 122 GLU   A OE2 1 
ATOM   760  N  N   . ASP   A 1 103 ? -12.093 -8.130  -0.138  1.00 102.12 ? 123 ASP   A N   1 
ATOM   761  C  CA  . ASP   A 1 103 ? -10.854 -7.512  0.331   1.00 102.91 ? 123 ASP   A CA  1 
ATOM   762  C  C   . ASP   A 1 103 ? -10.089 -8.376  1.333   1.00 111.93 ? 123 ASP   A C   1 
ATOM   763  O  O   . ASP   A 1 103 ? -9.719  -9.518  1.033   1.00 107.95 ? 123 ASP   A O   1 
ATOM   764  C  CB  . ASP   A 1 103 ? -11.158 -6.135  0.925   1.00 103.97 ? 123 ASP   A CB  1 
ATOM   765  C  CG  . ASP   A 1 103 ? -11.544 -5.116  -0.134  1.00 106.72 ? 123 ASP   A CG  1 
ATOM   766  O  OD1 . ASP   A 1 103 ? -11.203 -5.333  -1.319  1.00 93.36  ? 123 ASP   A OD1 1 
ATOM   767  O  OD2 . ASP   A 1 103 ? -12.171 -4.092  0.237   1.00 102.24 ? 123 ASP   A OD2 1 
ATOM   768  N  N   . GLU   A 1 104 ? -9.857  -7.837  2.532   1.00 108.15 ? 124 GLU   A N   1 
ATOM   769  C  CA  . GLU   A 1 104 ? -9.002  -8.512  3.506   1.00 120.22 ? 124 GLU   A CA  1 
ATOM   770  C  C   . GLU   A 1 104 ? -9.658  -9.775  4.047   1.00 110.97 ? 124 GLU   A C   1 
ATOM   771  O  O   . GLU   A 1 104 ? -8.981  -10.788 4.260   1.00 108.57 ? 124 GLU   A O   1 
ATOM   772  C  CB  . GLU   A 1 104 ? -8.659  -7.554  4.646   1.00 124.20 ? 124 GLU   A CB  1 
ATOM   773  C  CG  . GLU   A 1 104 ? -7.891  -6.326  4.198   1.00 127.07 ? 124 GLU   A CG  1 
ATOM   774  C  CD  . GLU   A 1 104 ? -6.724  -6.679  3.304   1.00 145.57 ? 124 GLU   A CD  1 
ATOM   775  O  OE1 . GLU   A 1 104 ? -5.874  -7.492  3.722   1.00 143.77 ? 124 GLU   A OE1 1 
ATOM   776  O  OE2 . GLU   A 1 104 ? -6.672  -6.158  2.172   1.00 142.22 ? 124 GLU   A OE2 1 
ATOM   777  N  N   . GLU   A 1 105 ? -10.972 -9.735  4.280   1.00 111.57 ? 125 GLU   A N   1 
ATOM   778  C  CA  . GLU   A 1 105 ? -11.662 -10.924 4.766   1.00 120.49 ? 125 GLU   A CA  1 
ATOM   779  C  C   . GLU   A 1 105 ? -11.555 -12.074 3.775   1.00 113.43 ? 125 GLU   A C   1 
ATOM   780  O  O   . GLU   A 1 105 ? -11.489 -13.239 4.183   1.00 104.49 ? 125 GLU   A O   1 
ATOM   781  C  CB  . GLU   A 1 105 ? -13.132 -10.615 5.041   1.00 122.22 ? 125 GLU   A CB  1 
ATOM   782  C  CG  . GLU   A 1 105 ? -13.864 -11.717 5.791   1.00 129.77 ? 125 GLU   A CG  1 
ATOM   783  C  CD  . GLU   A 1 105 ? -15.370 -11.569 5.719   1.00 149.89 ? 125 GLU   A CD  1 
ATOM   784  O  OE1 . GLU   A 1 105 ? -15.861 -10.911 4.777   1.00 141.79 ? 125 GLU   A OE1 1 
ATOM   785  O  OE2 . GLU   A 1 105 ? -16.061 -12.110 6.608   1.00 155.56 ? 125 GLU   A OE2 1 
ATOM   786  N  N   . TRP   A 1 106 ? -11.546 -11.771 2.475   1.00 103.71 ? 126 TRP   A N   1 
ATOM   787  C  CA  . TRP   A 1 106 ? -11.423 -12.828 1.477   1.00 109.40 ? 126 TRP   A CA  1 
ATOM   788  C  C   . TRP   A 1 106 ? -10.003 -13.381 1.420   1.00 101.97 ? 126 TRP   A C   1 
ATOM   789  O  O   . TRP   A 1 106 ? -9.811  -14.586 1.217   1.00 91.35  ? 126 TRP   A O   1 
ATOM   790  C  CB  . TRP   A 1 106 ? -11.847 -12.313 0.102   1.00 99.18  ? 126 TRP   A CB  1 
ATOM   791  C  CG  . TRP   A 1 106 ? -11.312 -13.149 -1.017  1.00 99.37  ? 126 TRP   A CG  1 
ATOM   792  C  CD1 . TRP   A 1 106 ? -11.849 -14.303 -1.507  1.00 97.17  ? 126 TRP   A CD1 1 
ATOM   793  C  CD2 . TRP   A 1 106 ? -10.121 -12.906 -1.775  1.00 106.45 ? 126 TRP   A CD2 1 
ATOM   794  N  NE1 . TRP   A 1 106 ? -11.070 -14.790 -2.529  1.00 96.77  ? 126 TRP   A NE1 1 
ATOM   795  C  CE2 . TRP   A 1 106 ? -10.002 -13.951 -2.713  1.00 100.85 ? 126 TRP   A CE2 1 
ATOM   796  C  CE3 . TRP   A 1 106 ? -9.145  -11.905 -1.754  1.00 107.55 ? 126 TRP   A CE3 1 
ATOM   797  C  CZ2 . TRP   A 1 106 ? -8.950  -14.023 -3.621  1.00 110.15 ? 126 TRP   A CZ2 1 
ATOM   798  C  CZ3 . TRP   A 1 106 ? -8.100  -11.978 -2.656  1.00 107.41 ? 126 TRP   A CZ3 1 
ATOM   799  C  CH2 . TRP   A 1 106 ? -8.011  -13.030 -3.577  1.00 108.73 ? 126 TRP   A CH2 1 
ATOM   800  N  N   . LYS   A 1 107 ? -8.996  -12.518 1.576   1.00 109.99 ? 127 LYS   A N   1 
ATOM   801  C  CA  . LYS   A 1 107 ? -7.613  -12.989 1.586   1.00 112.55 ? 127 LYS   A CA  1 
ATOM   802  C  C   . LYS   A 1 107 ? -7.384  -14.002 2.701   1.00 118.54 ? 127 LYS   A C   1 
ATOM   803  O  O   . LYS   A 1 107 ? -6.730  -15.031 2.494   1.00 92.70  ? 127 LYS   A O   1 
ATOM   804  C  CB  . LYS   A 1 107 ? -6.659  -11.805 1.737   1.00 105.04 ? 127 LYS   A CB  1 
ATOM   805  C  CG  . LYS   A 1 107 ? -5.738  -11.581 0.552   1.00 119.14 ? 127 LYS   A CG  1 
ATOM   806  C  CD  . LYS   A 1 107 ? -6.038  -10.256 -0.124  1.00 128.59 ? 127 LYS   A CD  1 
ATOM   807  C  CE  . LYS   A 1 107 ? -5.852  -9.094  0.838   1.00 132.24 ? 127 LYS   A CE  1 
ATOM   808  N  NZ  . LYS   A 1 107 ? -6.328  -7.809  0.256   1.00 131.24 ? 127 LYS   A NZ  1 
ATOM   809  N  N   . ARG   A 1 108 ? -7.925  -13.728 3.889   1.00 103.60 ? 128 ARG   A N   1 
ATOM   810  C  CA  . ARG   A 1 108 ? -7.761  -14.646 5.011   1.00 115.29 ? 128 ARG   A CA  1 
ATOM   811  C  C   . ARG   A 1 108 ? -8.440  -15.982 4.736   1.00 115.84 ? 128 ARG   A C   1 
ATOM   812  O  O   . ARG   A 1 108 ? -7.876  -17.044 5.025   1.00 118.56 ? 128 ARG   A O   1 
ATOM   813  C  CB  . ARG   A 1 108 ? -8.309  -14.005 6.284   1.00 109.73 ? 128 ARG   A CB  1 
ATOM   814  C  CG  . ARG   A 1 108 ? -8.524  -14.963 7.437   1.00 124.53 ? 128 ARG   A CG  1 
ATOM   815  C  CD  . ARG   A 1 108 ? -9.051  -14.217 8.648   1.00 140.94 ? 128 ARG   A CD  1 
ATOM   816  N  NE  . ARG   A 1 108 ? -9.868  -15.064 9.506   1.00 149.69 ? 128 ARG   A NE  1 
ATOM   817  C  CZ  . ARG   A 1 108 ? -11.158 -15.297 9.307   1.00 152.49 ? 128 ARG   A CZ  1 
ATOM   818  N  NH1 . ARG   A 1 108 ? -11.805 -14.771 8.281   1.00 149.79 ? 128 ARG   A NH1 1 
ATOM   819  N  NH2 . ARG   A 1 108 ? -11.815 -16.081 10.157  1.00 150.20 ? 128 ARG   A NH2 1 
ATOM   820  N  N   . LEU   A 1 109 ? -9.642  -15.950 4.156   1.00 114.37 ? 129 LEU   A N   1 
ATOM   821  C  CA  . LEU   A 1 109 ? -10.355 -17.189 3.861   1.00 109.01 ? 129 LEU   A CA  1 
ATOM   822  C  C   . LEU   A 1 109 ? -9.666  -17.977 2.754   1.00 117.85 ? 129 LEU   A C   1 
ATOM   823  O  O   . LEU   A 1 109 ? -9.640  -19.213 2.790   1.00 119.19 ? 129 LEU   A O   1 
ATOM   824  C  CB  . LEU   A 1 109 ? -11.802 -16.882 3.478   1.00 107.10 ? 129 LEU   A CB  1 
ATOM   825  C  CG  . LEU   A 1 109 ? -12.650 -16.202 4.553   1.00 112.93 ? 129 LEU   A CG  1 
ATOM   826  C  CD1 . LEU   A 1 109 ? -14.050 -15.918 4.036   1.00 108.86 ? 129 LEU   A CD1 1 
ATOM   827  C  CD2 . LEU   A 1 109 ? -12.700 -17.042 5.821   1.00 122.60 ? 129 LEU   A CD2 1 
ATOM   828  N  N   . ARG   A 1 110 ? -9.109  -17.281 1.759   1.00 106.06 ? 130 ARG   A N   1 
ATOM   829  C  CA  . ARG   A 1 110 ? -8.413  -17.972 0.678   1.00 108.19 ? 130 ARG   A CA  1 
ATOM   830  C  C   . ARG   A 1 110 ? -7.198  -18.726 1.204   1.00 116.11 ? 130 ARG   A C   1 
ATOM   831  O  O   . ARG   A 1 110 ? -6.956  -19.875 0.817   1.00 116.98 ? 130 ARG   A O   1 
ATOM   832  C  CB  . ARG   A 1 110 ? -7.999  -16.975 -0.405  1.00 109.62 ? 130 ARG   A CB  1 
ATOM   833  C  CG  . ARG   A 1 110 ? -7.448  -17.623 -1.666  1.00 104.70 ? 130 ARG   A CG  1 
ATOM   834  C  CD  . ARG   A 1 110 ? -8.561  -18.196 -2.528  1.00 109.86 ? 130 ARG   A CD  1 
ATOM   835  N  NE  . ARG   A 1 110 ? -8.038  -19.010 -3.619  1.00 107.16 ? 130 ARG   A NE  1 
ATOM   836  C  CZ  . ARG   A 1 110 ? -8.728  -19.350 -4.700  1.00 100.77 ? 130 ARG   A CZ  1 
ATOM   837  N  NH1 . ARG   A 1 110 ? -9.962  -18.917 -4.897  1.00 100.37 ? 130 ARG   A NH1 1 
ATOM   838  N  NH2 . ARG   A 1 110 ? -8.163  -20.143 -5.606  1.00 84.87  ? 130 ARG   A NH2 1 
ATOM   839  N  N   . SER   A 1 111 ? -6.426  -18.097 2.092   1.00 115.73 ? 131 SER   A N   1 
ATOM   840  C  CA  . SER   A 1 111 ? -5.292  -18.784 2.701   1.00 114.34 ? 131 SER   A CA  1 
ATOM   841  C  C   . SER   A 1 111 ? -5.756  -19.935 3.585   1.00 125.89 ? 131 SER   A C   1 
ATOM   842  O  O   . SER   A 1 111 ? -5.156  -21.017 3.580   1.00 122.02 ? 131 SER   A O   1 
ATOM   843  C  CB  . SER   A 1 111 ? -4.454  -17.791 3.508   1.00 112.22 ? 131 SER   A CB  1 
ATOM   844  O  OG  . SER   A 1 111 ? -3.903  -16.786 2.674   1.00 118.54 ? 131 SER   A OG  1 
ATOM   845  N  N   . LEU   A 1 112 ? -6.833  -19.723 4.343   1.00 119.53 ? 132 LEU   A N   1 
ATOM   846  C  CA  . LEU   A 1 112 ? -7.285  -20.730 5.296   1.00 125.96 ? 132 LEU   A CA  1 
ATOM   847  C  C   . LEU   A 1 112 ? -7.842  -21.966 4.600   1.00 131.35 ? 132 LEU   A C   1 
ATOM   848  O  O   . LEU   A 1 112 ? -7.785  -23.068 5.159   1.00 115.47 ? 132 LEU   A O   1 
ATOM   849  C  CB  . LEU   A 1 112 ? -8.337  -20.126 6.222   1.00 132.11 ? 132 LEU   A CB  1 
ATOM   850  C  CG  . LEU   A 1 112 ? -8.840  -20.987 7.378   1.00 138.36 ? 132 LEU   A CG  1 
ATOM   851  C  CD1 . LEU   A 1 112 ? -8.123  -20.635 8.674   1.00 148.39 ? 132 LEU   A CD1 1 
ATOM   852  C  CD2 . LEU   A 1 112 ? -10.336 -20.815 7.519   1.00 142.63 ? 132 LEU   A CD2 1 
ATOM   853  N  N   . LEU   A 1 113 ? -8.380  -21.810 3.391   1.00 126.28 ? 133 LEU   A N   1 
ATOM   854  C  CA  . LEU   A 1 113 ? -8.981  -22.919 2.664   1.00 125.97 ? 133 LEU   A CA  1 
ATOM   855  C  C   . LEU   A 1 113 ? -8.133  -23.432 1.510   1.00 131.43 ? 133 LEU   A C   1 
ATOM   856  O  O   . LEU   A 1 113 ? -8.481  -24.463 0.925   1.00 125.52 ? 133 LEU   A O   1 
ATOM   857  C  CB  . LEU   A 1 113 ? -10.364 -22.515 2.132   1.00 123.73 ? 133 LEU   A CB  1 
ATOM   858  C  CG  . LEU   A 1 113 ? -11.415 -22.194 3.195   1.00 127.39 ? 133 LEU   A CG  1 
ATOM   859  C  CD1 . LEU   A 1 113 ? -12.748 -21.827 2.558   1.00 132.12 ? 133 LEU   A CD1 1 
ATOM   860  C  CD2 . LEU   A 1 113 ? -11.577 -23.365 4.153   1.00 138.42 ? 133 LEU   A CD2 1 
ATOM   861  N  N   . SER   A 1 114 ? -7.041  -22.748 1.164   1.00 129.70 ? 134 SER   A N   1 
ATOM   862  C  CA  . SER   A 1 114 ? -6.210  -23.201 0.048   1.00 135.75 ? 134 SER   A CA  1 
ATOM   863  C  C   . SER   A 1 114 ? -5.651  -24.606 0.242   1.00 138.35 ? 134 SER   A C   1 
ATOM   864  O  O   . SER   A 1 114 ? -5.739  -25.411 -0.702  1.00 137.19 ? 134 SER   A O   1 
ATOM   865  C  CB  . SER   A 1 114 ? -5.086  -22.187 -0.206  1.00 131.63 ? 134 SER   A CB  1 
ATOM   866  O  OG  . SER   A 1 114 ? -5.599  -20.981 -0.748  1.00 124.48 ? 134 SER   A OG  1 
ATOM   867  N  N   . PRO   A 1 115 ? -5.073  -24.982 1.407   1.00 136.34 ? 135 PRO   A N   1 
ATOM   868  C  CA  . PRO   A 1 115 ? -4.426  -26.302 1.499   1.00 151.00 ? 135 PRO   A CA  1 
ATOM   869  C  C   . PRO   A 1 115 ? -5.386  -27.482 1.456   1.00 147.11 ? 135 PRO   A C   1 
ATOM   870  O  O   . PRO   A 1 115 ? -4.972  -28.625 1.674   1.00 152.59 ? 135 PRO   A O   1 
ATOM   871  C  CB  . PRO   A 1 115 ? -3.694  -26.243 2.848   1.00 153.06 ? 135 PRO   A CB  1 
ATOM   872  C  CG  . PRO   A 1 115 ? -3.592  -24.797 3.175   1.00 143.69 ? 135 PRO   A CG  1 
ATOM   873  C  CD  . PRO   A 1 115 ? -4.844  -24.196 2.632   1.00 139.47 ? 135 PRO   A CD  1 
ATOM   874  N  N   . THR   A 1 116 ? -6.666  -27.228 1.179   1.00 151.64 ? 136 THR   A N   1 
ATOM   875  C  CA  . THR   A 1 116 ? -7.626  -28.318 1.052   1.00 150.20 ? 136 THR   A CA  1 
ATOM   876  C  C   . THR   A 1 116 ? -7.466  -29.064 -0.267  1.00 146.41 ? 136 THR   A C   1 
ATOM   877  O  O   . THR   A 1 116 ? -7.757  -30.264 -0.336  1.00 148.93 ? 136 THR   A O   1 
ATOM   878  C  CB  . THR   A 1 116 ? -9.053  -27.778 1.185   1.00 147.93 ? 136 THR   A CB  1 
ATOM   879  O  OG1 . THR   A 1 116 ? -9.159  -27.007 2.388   1.00 154.59 ? 136 THR   A OG1 1 
ATOM   880  C  CG2 . THR   A 1 116 ? -10.063 -28.917 1.238   1.00 151.94 ? 136 THR   A CG2 1 
ATOM   881  N  N   . PHE   A 1 117 ? -6.990  -28.390 -1.310  1.00 145.46 ? 137 PHE   A N   1 
ATOM   882  C  CA  . PHE   A 1 117 ? -6.877  -28.974 -2.640  1.00 149.45 ? 137 PHE   A CA  1 
ATOM   883  C  C   . PHE   A 1 117 ? -5.426  -29.053 -3.095  1.00 152.08 ? 137 PHE   A C   1 
ATOM   884  O  O   . PHE   A 1 117 ? -5.111  -28.836 -4.267  1.00 153.23 ? 137 PHE   A O   1 
ATOM   885  C  CB  . PHE   A 1 117 ? -7.712  -28.191 -3.647  1.00 145.30 ? 137 PHE   A CB  1 
ATOM   886  C  CG  . PHE   A 1 117 ? -9.132  -27.995 -3.220  1.00 143.87 ? 137 PHE   A CG  1 
ATOM   887  C  CD1 . PHE   A 1 117 ? -10.018 -29.060 -3.215  1.00 141.32 ? 137 PHE   A CD1 1 
ATOM   888  C  CD2 . PHE   A 1 117 ? -9.581  -26.748 -2.816  1.00 138.19 ? 137 PHE   A CD2 1 
ATOM   889  C  CE1 . PHE   A 1 117 ? -11.326 -28.885 -2.819  1.00 139.53 ? 137 PHE   A CE1 1 
ATOM   890  C  CE2 . PHE   A 1 117 ? -10.887 -26.564 -2.419  1.00 134.67 ? 137 PHE   A CE2 1 
ATOM   891  C  CZ  . PHE   A 1 117 ? -11.762 -27.635 -2.422  1.00 139.04 ? 137 PHE   A CZ  1 
ATOM   892  N  N   . THR   A 1 118 ? -4.523  -29.366 -2.171  1.00 158.15 ? 138 THR   A N   1 
ATOM   893  C  CA  . THR   A 1 118 ? -3.153  -29.648 -2.560  1.00 163.22 ? 138 THR   A CA  1 
ATOM   894  C  C   . THR   A 1 118 ? -3.091  -30.975 -3.308  1.00 163.94 ? 138 THR   A C   1 
ATOM   895  O  O   . THR   A 1 118 ? -4.022  -31.785 -3.272  1.00 162.49 ? 138 THR   A O   1 
ATOM   896  C  CB  . THR   A 1 118 ? -2.235  -29.692 -1.337  1.00 165.47 ? 138 THR   A CB  1 
ATOM   897  O  OG1 . THR   A 1 118 ? -2.673  -30.721 -0.442  1.00 166.56 ? 138 THR   A OG1 1 
ATOM   898  C  CG2 . THR   A 1 118 ? -2.245  -28.355 -0.613  1.00 150.89 ? 138 THR   A CG2 1 
ATOM   899  N  N   . SER   A 1 119 ? -1.972  -31.191 -4.002  1.00 165.64 ? 139 SER   A N   1 
ATOM   900  C  CA  . SER   A 1 119 ? -1.793  -32.435 -4.741  1.00 169.89 ? 139 SER   A CA  1 
ATOM   901  C  C   . SER   A 1 119 ? -1.838  -33.649 -3.821  1.00 174.87 ? 139 SER   A C   1 
ATOM   902  O  O   . SER   A 1 119 ? -2.168  -34.754 -4.267  1.00 169.97 ? 139 SER   A O   1 
ATOM   903  C  CB  . SER   A 1 119 ? -0.478  -32.393 -5.519  1.00 168.08 ? 139 SER   A CB  1 
ATOM   904  O  OG  . SER   A 1 119 ? 0.538   -31.745 -4.772  1.00 161.59 ? 139 SER   A OG  1 
ATOM   905  N  N   . GLY   A 1 120 ? -1.523  -33.465 -2.540  1.00 202.61 ? 140 GLY   A N   1 
ATOM   906  C  CA  . GLY   A 1 120 ? -1.590  -34.547 -1.578  1.00 201.87 ? 140 GLY   A CA  1 
ATOM   907  C  C   . GLY   A 1 120 ? -2.984  -34.784 -1.032  1.00 198.40 ? 140 GLY   A C   1 
ATOM   908  O  O   . GLY   A 1 120 ? -3.457  -35.925 -1.004  1.00 199.47 ? 140 GLY   A O   1 
ATOM   909  N  N   . LYS   A 1 121 ? -3.649  -33.714 -0.586  1.00 177.00 ? 141 LYS   A N   1 
ATOM   910  C  CA  . LYS   A 1 121 ? -5.010  -33.849 -0.072  1.00 174.87 ? 141 LYS   A CA  1 
ATOM   911  C  C   . LYS   A 1 121 ? -5.943  -34.429 -1.128  1.00 173.33 ? 141 LYS   A C   1 
ATOM   912  O  O   . LYS   A 1 121 ? -6.857  -35.196 -0.805  1.00 167.95 ? 141 LYS   A O   1 
ATOM   913  C  CB  . LYS   A 1 121 ? -5.525  -32.495 0.417   1.00 166.21 ? 141 LYS   A CB  1 
ATOM   914  C  CG  . LYS   A 1 121 ? -4.775  -31.937 1.617   1.00 161.09 ? 141 LYS   A CG  1 
ATOM   915  C  CD  . LYS   A 1 121 ? -5.128  -32.677 2.896   1.00 161.21 ? 141 LYS   A CD  1 
ATOM   916  C  CE  . LYS   A 1 121 ? -4.241  -32.227 4.045   1.00 158.54 ? 141 LYS   A CE  1 
ATOM   917  N  NZ  . LYS   A 1 121 ? -4.309  -30.754 4.258   1.00 157.12 ? 141 LYS   A NZ  1 
ATOM   918  N  N   . LEU   A 1 122 ? -5.728  -34.074 -2.397  1.00 166.77 ? 142 LEU   A N   1 
ATOM   919  C  CA  . LEU   A 1 122 ? -6.482  -34.701 -3.478  1.00 164.19 ? 142 LEU   A CA  1 
ATOM   920  C  C   . LEU   A 1 122 ? -6.145  -36.182 -3.586  1.00 162.78 ? 142 LEU   A C   1 
ATOM   921  O  O   . LEU   A 1 122 ? -7.034  -37.025 -3.755  1.00 160.82 ? 142 LEU   A O   1 
ATOM   922  C  CB  . LEU   A 1 122 ? -6.196  -33.991 -4.802  1.00 156.88 ? 142 LEU   A CB  1 
ATOM   923  C  CG  . LEU   A 1 122 ? -7.314  -33.153 -5.422  1.00 150.24 ? 142 LEU   A CG  1 
ATOM   924  C  CD1 . LEU   A 1 122 ? -7.748  -32.055 -4.470  1.00 152.46 ? 142 LEU   A CD1 1 
ATOM   925  C  CD2 . LEU   A 1 122 ? -6.859  -32.568 -6.750  1.00 145.85 ? 142 LEU   A CD2 1 
ATOM   926  N  N   . LYS   A 1 123 ? -4.855  -36.517 -3.487  1.00 167.40 ? 143 LYS   A N   1 
ATOM   927  C  CA  . LYS   A 1 123 ? -4.435  -37.910 -3.590  1.00 167.47 ? 143 LYS   A CA  1 
ATOM   928  C  C   . LYS   A 1 123 ? -4.998  -38.746 -2.449  1.00 165.43 ? 143 LYS   A C   1 
ATOM   929  O  O   . LYS   A 1 123 ? -5.221  -39.951 -2.613  1.00 166.77 ? 143 LYS   A O   1 
ATOM   930  C  CB  . LYS   A 1 123 ? -2.908  -37.990 -3.620  1.00 170.20 ? 143 LYS   A CB  1 
ATOM   931  C  CG  . LYS   A 1 123 ? -2.353  -39.326 -4.086  1.00 168.26 ? 143 LYS   A CG  1 
ATOM   932  C  CD  . LYS   A 1 123 ? -1.236  -39.126 -5.102  1.00 168.71 ? 143 LYS   A CD  1 
ATOM   933  C  CE  . LYS   A 1 123 ? -0.198  -38.130 -4.606  1.00 165.62 ? 143 LYS   A CE  1 
ATOM   934  N  NZ  . LYS   A 1 123 ? 0.848   -37.858 -5.632  1.00 165.49 ? 143 LYS   A NZ  1 
ATOM   935  N  N   . GLU   A 1 124 ? -5.241  -38.125 -1.292  1.00 167.97 ? 144 GLU   A N   1 
ATOM   936  C  CA  . GLU   A 1 124 ? -5.940  -38.812 -0.214  1.00 165.34 ? 144 GLU   A CA  1 
ATOM   937  C  C   . GLU   A 1 124 ? -7.381  -39.136 -0.581  1.00 166.57 ? 144 GLU   A C   1 
ATOM   938  O  O   . GLU   A 1 124 ? -7.969  -40.046 0.012   1.00 159.89 ? 144 GLU   A O   1 
ATOM   939  C  CB  . GLU   A 1 124 ? -5.921  -37.963 1.060   1.00 167.83 ? 144 GLU   A CB  1 
ATOM   940  C  CG  . GLU   A 1 124 ? -4.550  -37.763 1.683   1.00 170.41 ? 144 GLU   A CG  1 
ATOM   941  C  CD  . GLU   A 1 124 ? -4.624  -37.006 2.996   1.00 177.05 ? 144 GLU   A CD  1 
ATOM   942  O  OE1 . GLU   A 1 124 ? -5.645  -37.144 3.702   1.00 174.15 ? 144 GLU   A OE1 1 
ATOM   943  O  OE2 . GLU   A 1 124 ? -3.670  -36.267 3.319   1.00 178.54 ? 144 GLU   A OE2 1 
ATOM   944  N  N   . MET   A 1 125 ? -7.961  -38.420 -1.544  1.00 166.94 ? 145 MET   A N   1 
ATOM   945  C  CA  . MET   A 1 125 ? -9.371  -38.567 -1.880  1.00 166.70 ? 145 MET   A CA  1 
ATOM   946  C  C   . MET   A 1 125 ? -9.634  -39.588 -2.980  1.00 168.71 ? 145 MET   A C   1 
ATOM   947  O  O   . MET   A 1 125 ? -10.794 -39.966 -3.181  1.00 169.91 ? 145 MET   A O   1 
ATOM   948  C  CB  . MET   A 1 125 ? -9.957  -37.213 -2.302  1.00 160.72 ? 145 MET   A CB  1 
ATOM   949  C  CG  . MET   A 1 125 ? -9.897  -36.143 -1.223  1.00 167.60 ? 145 MET   A CG  1 
ATOM   950  S  SD  . MET   A 1 125 ? -10.563 -34.559 -1.770  1.00 169.59 ? 145 MET   A SD  1 
ATOM   951  C  CE  . MET   A 1 125 ? -10.276 -33.548 -0.319  1.00 165.02 ? 145 MET   A CE  1 
ATOM   952  N  N   . VAL   A 1 126 ? -8.607  -40.041 -3.693  1.00 169.23 ? 146 VAL   A N   1 
ATOM   953  C  CA  . VAL   A 1 126 ? -8.789  -41.006 -4.777  1.00 173.88 ? 146 VAL   A CA  1 
ATOM   954  C  C   . VAL   A 1 126 ? -9.264  -42.351 -4.228  1.00 178.63 ? 146 VAL   A C   1 
ATOM   955  O  O   . VAL   A 1 126 ? -10.210 -42.926 -4.786  1.00 178.57 ? 146 VAL   A O   1 
ATOM   956  C  CB  . VAL   A 1 126 ? -7.505  -41.161 -5.611  1.00 172.09 ? 146 VAL   A CB  1 
ATOM   957  C  CG1 . VAL   A 1 126 ? -7.673  -42.266 -6.643  1.00 165.80 ? 146 VAL   A CG1 1 
ATOM   958  C  CG2 . VAL   A 1 126 ? -7.157  -39.850 -6.288  1.00 159.31 ? 146 VAL   A CG2 1 
ATOM   959  N  N   . PRO   A 1 127 ? -8.664  -42.903 -3.163  1.00 177.62 ? 147 PRO   A N   1 
ATOM   960  C  CA  . PRO   A 1 127 ? -9.219  -44.149 -2.605  1.00 181.96 ? 147 PRO   A CA  1 
ATOM   961  C  C   . PRO   A 1 127 ? -10.645 -44.008 -2.102  1.00 182.41 ? 147 PRO   A C   1 
ATOM   962  O  O   . PRO   A 1 127 ? -11.388 -44.998 -2.091  1.00 189.49 ? 147 PRO   A O   1 
ATOM   963  C  CB  . PRO   A 1 127 ? -8.250  -44.482 -1.462  1.00 181.10 ? 147 PRO   A CB  1 
ATOM   964  C  CG  . PRO   A 1 127 ? -6.979  -43.846 -1.860  1.00 175.46 ? 147 PRO   A CG  1 
ATOM   965  C  CD  . PRO   A 1 127 ? -7.381  -42.562 -2.517  1.00 178.28 ? 147 PRO   A CD  1 
ATOM   966  N  N   . ILE   A 1 128 ? -11.054 -42.809 -1.688  1.00 179.64 ? 148 ILE   A N   1 
ATOM   967  C  CA  . ILE   A 1 128 ? -12.403 -42.629 -1.160  1.00 181.55 ? 148 ILE   A CA  1 
ATOM   968  C  C   . ILE   A 1 128 ? -13.409 -42.450 -2.292  1.00 186.20 ? 148 ILE   A C   1 
ATOM   969  O  O   . ILE   A 1 128 ? -14.514 -43.004 -2.247  1.00 187.81 ? 148 ILE   A O   1 
ATOM   970  C  CB  . ILE   A 1 128 ? -12.435 -41.447 -0.171  1.00 182.17 ? 148 ILE   A CB  1 
ATOM   971  C  CG1 . ILE   A 1 128 ? -11.837 -41.853 1.179   1.00 186.68 ? 148 ILE   A CG1 1 
ATOM   972  C  CG2 . ILE   A 1 128 ? -13.856 -40.939 0.024   1.00 184.06 ? 148 ILE   A CG2 1 
ATOM   973  C  CD1 . ILE   A 1 128 ? -10.329 -41.784 1.244   1.00 186.38 ? 148 ILE   A CD1 1 
ATOM   974  N  N   . ILE   A 1 129 ? -13.044 -41.688 -3.328  1.00 186.14 ? 149 ILE   A N   1 
ATOM   975  C  CA  . ILE   A 1 129 ? -13.954 -41.463 -4.449  1.00 183.74 ? 149 ILE   A CA  1 
ATOM   976  C  C   . ILE   A 1 129 ? -14.237 -42.764 -5.189  1.00 191.53 ? 149 ILE   A C   1 
ATOM   977  O  O   . ILE   A 1 129 ? -15.330 -42.951 -5.740  1.00 191.48 ? 149 ILE   A O   1 
ATOM   978  C  CB  . ILE   A 1 129 ? -13.379 -40.384 -5.391  1.00 171.71 ? 149 ILE   A CB  1 
ATOM   979  C  CG1 . ILE   A 1 129 ? -13.414 -39.013 -4.714  1.00 163.94 ? 149 ILE   A CG1 1 
ATOM   980  C  CG2 . ILE   A 1 129 ? -14.140 -40.341 -6.711  1.00 163.09 ? 149 ILE   A CG2 1 
ATOM   981  C  CD1 . ILE   A 1 129 ? -12.987 -37.878 -5.618  1.00 151.89 ? 149 ILE   A CD1 1 
ATOM   982  N  N   . ALA   A 1 130 ? -13.282 -43.697 -5.183  1.00 191.30 ? 150 ALA   A N   1 
ATOM   983  C  CA  . ALA   A 1 130 ? -13.437 -44.958 -5.900  1.00 190.40 ? 150 ALA   A CA  1 
ATOM   984  C  C   . ALA   A 1 130 ? -14.607 -45.799 -5.399  1.00 201.10 ? 150 ALA   A C   1 
ATOM   985  O  O   . ALA   A 1 130 ? -14.899 -46.837 -6.003  1.00 193.41 ? 150 ALA   A O   1 
ATOM   986  C  CB  . ALA   A 1 130 ? -12.143 -45.769 -5.804  1.00 191.93 ? 150 ALA   A CB  1 
ATOM   987  N  N   . GLN   A 1 131 ? -15.279 -45.387 -4.323  1.00 207.60 ? 151 GLN   A N   1 
ATOM   988  C  CA  . GLN   A 1 131 ? -16.425 -46.140 -3.823  1.00 206.03 ? 151 GLN   A CA  1 
ATOM   989  C  C   . GLN   A 1 131 ? -17.694 -45.809 -4.601  1.00 201.12 ? 151 GLN   A C   1 
ATOM   990  O  O   . GLN   A 1 131 ? -18.316 -46.692 -5.202  1.00 207.53 ? 151 GLN   A O   1 
ATOM   991  C  CB  . GLN   A 1 131 ? -16.629 -45.862 -2.331  1.00 210.02 ? 151 GLN   A CB  1 
ATOM   992  C  CG  . GLN   A 1 131 ? -18.008 -46.259 -1.815  1.00 211.83 ? 151 GLN   A CG  1 
ATOM   993  C  CD  . GLN   A 1 131 ? -18.233 -45.851 -0.373  1.00 220.02 ? 151 GLN   A CD  1 
ATOM   994  O  OE1 . GLN   A 1 131 ? -17.289 -45.760 0.411   1.00 231.30 ? 151 GLN   A OE1 1 
ATOM   995  N  NE2 . GLN   A 1 131 ? -19.488 -45.598 -0.017  1.00 215.51 ? 151 GLN   A NE2 1 
ATOM   996  N  N   . TYR   A 1 132 ? -18.092 -44.536 -4.600  1.00 197.61 ? 152 TYR   A N   1 
ATOM   997  C  CA  . TYR   A 1 132 ? -19.377 -44.140 -5.163  1.00 191.23 ? 152 TYR   A CA  1 
ATOM   998  C  C   . TYR   A 1 132 ? -19.422 -44.234 -6.681  1.00 188.96 ? 152 TYR   A C   1 
ATOM   999  O  O   . TYR   A 1 132 ? -20.518 -44.198 -7.250  1.00 180.68 ? 152 TYR   A O   1 
ATOM   1000 C  CB  . TYR   A 1 132 ? -19.722 -42.724 -4.710  1.00 184.39 ? 152 TYR   A CB  1 
ATOM   1001 C  CG  . TYR   A 1 132 ? -19.821 -42.607 -3.210  1.00 187.21 ? 152 TYR   A CG  1 
ATOM   1002 C  CD1 . TYR   A 1 132 ? -20.932 -43.090 -2.530  1.00 185.84 ? 152 TYR   A CD1 1 
ATOM   1003 C  CD2 . TYR   A 1 132 ? -18.797 -42.032 -2.471  1.00 185.68 ? 152 TYR   A CD2 1 
ATOM   1004 C  CE1 . TYR   A 1 132 ? -21.026 -42.989 -1.159  1.00 189.56 ? 152 TYR   A CE1 1 
ATOM   1005 C  CE2 . TYR   A 1 132 ? -18.881 -41.930 -1.102  1.00 186.83 ? 152 TYR   A CE2 1 
ATOM   1006 C  CZ  . TYR   A 1 132 ? -19.996 -42.409 -0.451  1.00 188.77 ? 152 TYR   A CZ  1 
ATOM   1007 O  OH  . TYR   A 1 132 ? -20.074 -42.305 0.915   1.00 192.08 ? 152 TYR   A OH  1 
ATOM   1008 N  N   . GLY   A 1 133 ? -18.274 -44.351 -7.347  1.00 184.31 ? 153 GLY   A N   1 
ATOM   1009 C  CA  . GLY   A 1 133 ? -18.295 -44.681 -8.760  1.00 178.33 ? 153 GLY   A CA  1 
ATOM   1010 C  C   . GLY   A 1 133 ? -18.862 -46.065 -9.007  1.00 183.46 ? 153 GLY   A C   1 
ATOM   1011 O  O   . GLY   A 1 133 ? -19.561 -46.294 -9.997  1.00 186.23 ? 153 GLY   A O   1 
ATOM   1012 N  N   . ASP   A 1 134 ? -18.574 -47.006 -8.105  1.00 187.95 ? 154 ASP   A N   1 
ATOM   1013 C  CA  . ASP   A 1 134 ? -19.156 -48.338 -8.214  1.00 184.43 ? 154 ASP   A CA  1 
ATOM   1014 C  C   . ASP   A 1 134 ? -20.631 -48.335 -7.838  1.00 180.32 ? 154 ASP   A C   1 
ATOM   1015 O  O   . ASP   A 1 134 ? -21.406 -49.139 -8.367  1.00 185.31 ? 154 ASP   A O   1 
ATOM   1016 C  CB  . ASP   A 1 134 ? -18.379 -49.322 -7.343  1.00 189.74 ? 154 ASP   A CB  1 
ATOM   1017 C  CG  . ASP   A 1 134 ? -16.933 -49.453 -7.771  1.00 196.80 ? 154 ASP   A CG  1 
ATOM   1018 O  OD1 . ASP   A 1 134 ? -16.656 -49.286 -8.978  1.00 197.86 ? 154 ASP   A OD1 1 
ATOM   1019 O  OD2 . ASP   A 1 134 ? -16.073 -49.718 -6.905  1.00 196.78 ? 154 ASP   A OD2 1 
ATOM   1020 N  N   . VAL   A 1 135 ? -21.034 -47.452 -6.921  1.00 183.39 ? 155 VAL   A N   1 
ATOM   1021 C  CA  . VAL   A 1 135 ? -22.458 -47.222 -6.708  1.00 183.71 ? 155 VAL   A CA  1 
ATOM   1022 C  C   . VAL   A 1 135 ? -23.061 -46.540 -7.927  1.00 183.88 ? 155 VAL   A C   1 
ATOM   1023 O  O   . VAL   A 1 135 ? -24.219 -46.790 -8.283  1.00 185.67 ? 155 VAL   A O   1 
ATOM   1024 C  CB  . VAL   A 1 135 ? -22.685 -46.396 -5.427  1.00 183.98 ? 155 VAL   A CB  1 
ATOM   1025 C  CG1 . VAL   A 1 135 ? -24.172 -46.192 -5.177  1.00 183.49 ? 155 VAL   A CG1 1 
ATOM   1026 C  CG2 . VAL   A 1 135 ? -22.026 -47.072 -4.234  1.00 182.01 ? 155 VAL   A CG2 1 
ATOM   1027 N  N   . LEU   A 1 136 ? -22.284 -45.680 -8.592  1.00 182.79 ? 156 LEU   A N   1 
ATOM   1028 C  CA  . LEU   A 1 136 ? -22.748 -45.027 -9.812  1.00 176.11 ? 156 LEU   A CA  1 
ATOM   1029 C  C   . LEU   A 1 136 ? -22.914 -46.030 -10.947 1.00 179.41 ? 156 LEU   A C   1 
ATOM   1030 O  O   . LEU   A 1 136 ? -23.856 -45.927 -11.741 1.00 185.98 ? 156 LEU   A O   1 
ATOM   1031 C  CB  . LEU   A 1 136 ? -21.771 -43.919 -10.204 1.00 171.17 ? 156 LEU   A CB  1 
ATOM   1032 C  CG  . LEU   A 1 136 ? -21.890 -43.237 -11.567 1.00 167.32 ? 156 LEU   A CG  1 
ATOM   1033 C  CD1 . LEU   A 1 136 ? -23.217 -42.522 -11.704 1.00 163.15 ? 156 LEU   A CD1 1 
ATOM   1034 C  CD2 . LEU   A 1 136 ? -20.740 -42.262 -11.750 1.00 155.41 ? 156 LEU   A CD2 1 
ATOM   1035 N  N   . VAL   A 1 137 ? -22.010 -47.006 -11.040 1.00 188.32 ? 157 VAL   A N   1 
ATOM   1036 C  CA  . VAL   A 1 137 ? -22.133 -48.036 -12.067 1.00 186.98 ? 157 VAL   A CA  1 
ATOM   1037 C  C   . VAL   A 1 137 ? -23.300 -48.964 -11.750 1.00 187.63 ? 157 VAL   A C   1 
ATOM   1038 O  O   . VAL   A 1 137 ? -24.129 -49.265 -12.617 1.00 191.89 ? 157 VAL   A O   1 
ATOM   1039 C  CB  . VAL   A 1 137 ? -20.814 -48.816 -12.209 1.00 180.31 ? 157 VAL   A CB  1 
ATOM   1040 C  CG1 . VAL   A 1 137 ? -21.009 -50.029 -13.104 1.00 181.93 ? 157 VAL   A CG1 1 
ATOM   1041 C  CG2 . VAL   A 1 137 ? -19.723 -47.915 -12.764 1.00 181.55 ? 157 VAL   A CG2 1 
ATOM   1042 N  N   . ARG   A 1 138 ? -23.384 -49.427 -10.501 1.00 183.52 ? 158 ARG   A N   1 
ATOM   1043 C  CA  . ARG   A 1 138 ? -24.450 -50.349 -10.125 1.00 184.68 ? 158 ARG   A CA  1 
ATOM   1044 C  C   . ARG   A 1 138 ? -25.821 -49.687 -10.199 1.00 190.47 ? 158 ARG   A C   1 
ATOM   1045 O  O   . ARG   A 1 138 ? -26.812 -50.356 -10.513 1.00 196.23 ? 158 ARG   A O   1 
ATOM   1046 C  CB  . ARG   A 1 138 ? -24.196 -50.899 -8.724  1.00 189.59 ? 158 ARG   A CB  1 
ATOM   1047 C  CG  . ARG   A 1 138 ? -23.784 -52.363 -8.690  1.00 192.07 ? 158 ARG   A CG  1 
ATOM   1048 C  CD  . ARG   A 1 138 ? -23.604 -52.851 -7.258  1.00 199.52 ? 158 ARG   A CD  1 
ATOM   1049 N  NE  . ARG   A 1 138 ? -24.447 -52.119 -6.319  1.00 198.99 ? 158 ARG   A NE  1 
ATOM   1050 C  CZ  . ARG   A 1 138 ? -24.001 -51.201 -5.472  1.00 203.58 ? 158 ARG   A CZ  1 
ATOM   1051 N  NH1 . ARG   A 1 138 ? -22.715 -50.896 -5.398  1.00 203.23 ? 158 ARG   A NH1 1 
ATOM   1052 N  NH2 . ARG   A 1 138 ? -24.866 -50.569 -4.684  1.00 204.78 ? 158 ARG   A NH2 1 
ATOM   1053 N  N   . ASN   A 1 139 ? -25.901 -48.385 -9.911  1.00 181.48 ? 159 ASN   A N   1 
ATOM   1054 C  CA  . ASN   A 1 139 ? -27.146 -47.662 -10.148 1.00 187.44 ? 159 ASN   A CA  1 
ATOM   1055 C  C   . ASN   A 1 139 ? -27.439 -47.535 -11.636 1.00 186.44 ? 159 ASN   A C   1 
ATOM   1056 O  O   . ASN   A 1 139 ? -28.609 -47.492 -12.034 1.00 190.95 ? 159 ASN   A O   1 
ATOM   1057 C  CB  . ASN   A 1 139 ? -27.091 -46.275 -9.502  1.00 181.62 ? 159 ASN   A CB  1 
ATOM   1058 C  CG  . ASN   A 1 139 ? -27.467 -46.300 -8.034  1.00 186.89 ? 159 ASN   A CG  1 
ATOM   1059 O  OD1 . ASN   A 1 139 ? -28.126 -47.230 -7.568  1.00 192.94 ? 159 ASN   A OD1 1 
ATOM   1060 N  ND2 . ASN   A 1 139 ? -27.061 -45.271 -7.299  1.00 182.99 ? 159 ASN   A ND2 1 
ATOM   1061 N  N   . LEU   A 1 140 ? -26.396 -47.478 -12.468 1.00 190.10 ? 160 LEU   A N   1 
ATOM   1062 C  CA  . LEU   A 1 140 ? -26.583 -47.396 -13.912 1.00 188.38 ? 160 LEU   A CA  1 
ATOM   1063 C  C   . LEU   A 1 140 ? -26.842 -48.757 -14.546 1.00 191.75 ? 160 LEU   A C   1 
ATOM   1064 O  O   . LEU   A 1 140 ? -27.582 -48.839 -15.532 1.00 196.26 ? 160 LEU   A O   1 
ATOM   1065 C  CB  . LEU   A 1 140 ? -25.361 -46.748 -14.565 1.00 182.24 ? 160 LEU   A CB  1 
ATOM   1066 C  CG  . LEU   A 1 140 ? -25.337 -45.220 -14.573 1.00 169.80 ? 160 LEU   A CG  1 
ATOM   1067 C  CD1 . LEU   A 1 140 ? -24.051 -44.712 -15.201 1.00 161.85 ? 160 LEU   A CD1 1 
ATOM   1068 C  CD2 . LEU   A 1 140 ? -26.550 -44.681 -15.313 1.00 161.92 ? 160 LEU   A CD2 1 
ATOM   1069 N  N   . ARG   A 1 141 ? -26.245 -49.827 -14.010 1.00 190.97 ? 161 ARG   A N   1 
ATOM   1070 C  CA  . ARG   A 1 141 ? -26.474 -51.162 -14.555 1.00 193.35 ? 161 ARG   A CA  1 
ATOM   1071 C  C   . ARG   A 1 141 ? -27.932 -51.582 -14.436 1.00 202.57 ? 161 ARG   A C   1 
ATOM   1072 O  O   . ARG   A 1 141 ? -28.387 -52.439 -15.201 1.00 211.09 ? 161 ARG   A O   1 
ATOM   1073 C  CB  . ARG   A 1 141 ? -25.566 -52.173 -13.847 1.00 195.90 ? 161 ARG   A CB  1 
ATOM   1074 C  CG  . ARG   A 1 141 ? -25.637 -53.602 -14.375 1.00 206.15 ? 161 ARG   A CG  1 
ATOM   1075 C  CD  . ARG   A 1 141 ? -24.291 -54.297 -14.232 1.00 209.68 ? 161 ARG   A CD  1 
ATOM   1076 N  NE  . ARG   A 1 141 ? -23.336 -53.820 -15.225 1.00 207.73 ? 161 ARG   A NE  1 
ATOM   1077 C  CZ  . ARG   A 1 141 ? -22.024 -54.005 -15.160 1.00 203.75 ? 161 ARG   A CZ  1 
ATOM   1078 N  NH1 . ARG   A 1 141 ? -21.462 -54.621 -14.133 1.00 209.92 ? 161 ARG   A NH1 1 
ATOM   1079 N  NH2 . ARG   A 1 141 ? -21.256 -53.557 -16.149 1.00 193.82 ? 161 ARG   A NH2 1 
ATOM   1080 N  N   . ARG   A 1 142 ? -28.674 -50.989 -13.501 1.00 202.54 ? 162 ARG   A N   1 
ATOM   1081 C  CA  . ARG   A 1 142 ? -30.085 -51.314 -13.339 1.00 205.39 ? 162 ARG   A CA  1 
ATOM   1082 C  C   . ARG   A 1 142 ? -30.931 -50.655 -14.422 1.00 207.54 ? 162 ARG   A C   1 
ATOM   1083 O  O   . ARG   A 1 142 ? -31.793 -51.301 -15.027 1.00 211.58 ? 162 ARG   A O   1 
ATOM   1084 C  CB  . ARG   A 1 142 ? -30.561 -50.891 -11.950 1.00 206.02 ? 162 ARG   A CB  1 
ATOM   1085 C  CG  . ARG   A 1 142 ? -29.874 -51.627 -10.817 1.00 209.12 ? 162 ARG   A CG  1 
ATOM   1086 C  CD  . ARG   A 1 142 ? -30.167 -50.968 -9.482  1.00 212.96 ? 162 ARG   A CD  1 
ATOM   1087 N  NE  . ARG   A 1 142 ? -29.780 -51.812 -8.359  1.00 221.36 ? 162 ARG   A NE  1 
ATOM   1088 C  CZ  . ARG   A 1 142 ? -29.842 -51.441 -7.087  1.00 226.53 ? 162 ARG   A CZ  1 
ATOM   1089 N  NH1 . ARG   A 1 142 ? -30.260 -50.236 -6.738  1.00 220.63 ? 162 ARG   A NH1 1 
ATOM   1090 N  NH2 . ARG   A 1 142 ? -29.474 -52.302 -6.142  1.00 225.98 ? 162 ARG   A NH2 1 
ATOM   1091 N  N   . GLU   A 1 143 ? -30.701 -49.368 -14.676 1.00 207.14 ? 163 GLU   A N   1 
ATOM   1092 C  CA  . GLU   A 1 143 ? -31.414 -48.658 -15.730 1.00 207.52 ? 163 GLU   A CA  1 
ATOM   1093 C  C   . GLU   A 1 143 ? -30.852 -48.936 -17.120 1.00 207.32 ? 163 GLU   A C   1 
ATOM   1094 O  O   . GLU   A 1 143 ? -31.337 -48.348 -18.093 1.00 203.47 ? 163 GLU   A O   1 
ATOM   1095 C  CB  . GLU   A 1 143 ? -31.399 -47.153 -15.452 1.00 203.87 ? 163 GLU   A CB  1 
ATOM   1096 C  CG  . GLU   A 1 143 ? -32.466 -46.678 -14.469 1.00 206.93 ? 163 GLU   A CG  1 
ATOM   1097 C  CD  . GLU   A 1 143 ? -32.224 -47.149 -13.046 1.00 208.46 ? 163 GLU   A CD  1 
ATOM   1098 O  OE1 . GLU   A 1 143 ? -32.394 -48.356 -12.772 1.00 207.40 ? 163 GLU   A OE1 1 
ATOM   1099 O  OE2 . GLU   A 1 143 ? -31.864 -46.307 -12.197 1.00 211.06 ? 163 GLU   A OE2 1 
ATOM   1100 N  N   . ALA   A 1 144 ? -29.847 -49.803 -17.234 1.00 208.46 ? 164 ALA   A N   1 
ATOM   1101 C  CA  . ALA   A 1 144 ? -29.319 -50.238 -18.522 1.00 211.88 ? 164 ALA   A CA  1 
ATOM   1102 C  C   . ALA   A 1 144 ? -29.799 -51.628 -18.912 1.00 216.96 ? 164 ALA   A C   1 
ATOM   1103 O  O   . ALA   A 1 144 ? -30.144 -51.856 -20.075 1.00 222.71 ? 164 ALA   A O   1 
ATOM   1104 C  CB  . ALA   A 1 144 ? -27.789 -50.217 -18.509 1.00 203.95 ? 164 ALA   A CB  1 
ATOM   1105 N  N   . GLU   A 1 145 ? -29.818 -52.567 -17.962 1.00 223.29 ? 165 GLU   A N   1 
ATOM   1106 C  CA  . GLU   A 1 145 ? -30.379 -53.887 -18.229 1.00 226.81 ? 165 GLU   A CA  1 
ATOM   1107 C  C   . GLU   A 1 145 ? -31.861 -53.802 -18.569 1.00 222.62 ? 165 GLU   A C   1 
ATOM   1108 O  O   . GLU   A 1 145 ? -32.385 -54.670 -19.277 1.00 229.82 ? 165 GLU   A O   1 
ATOM   1109 C  CB  . GLU   A 1 145 ? -30.149 -54.804 -17.027 1.00 225.12 ? 165 GLU   A CB  1 
ATOM   1110 C  CG  . GLU   A 1 145 ? -28.704 -55.243 -16.872 1.00 230.23 ? 165 GLU   A CG  1 
ATOM   1111 C  CD  . GLU   A 1 145 ? -28.495 -56.171 -15.696 1.00 230.91 ? 165 GLU   A CD  1 
ATOM   1112 O  OE1 . GLU   A 1 145 ? -29.339 -56.176 -14.773 1.00 232.85 ? 165 GLU   A OE1 1 
ATOM   1113 O  OE2 . GLU   A 1 145 ? -27.484 -56.900 -15.697 1.00 231.92 ? 165 GLU   A OE2 1 
ATOM   1114 N  N   . THR   A 1 146 ? -32.546 -52.774 -18.071 1.00 223.68 ? 166 THR   A N   1 
ATOM   1115 C  CA  . THR   A 1 146 ? -33.872 -52.406 -18.549 1.00 221.04 ? 166 THR   A CA  1 
ATOM   1116 C  C   . THR   A 1 146 ? -33.626 -51.364 -19.631 1.00 231.19 ? 166 THR   A C   1 
ATOM   1117 O  O   . THR   A 1 146 ? -32.899 -50.390 -19.404 1.00 225.66 ? 166 THR   A O   1 
ATOM   1118 C  CB  . THR   A 1 146 ? -34.754 -51.898 -17.410 1.00 217.55 ? 166 THR   A CB  1 
ATOM   1119 O  OG1 . THR   A 1 146 ? -34.453 -50.519 -17.162 1.00 209.42 ? 166 THR   A OG1 1 
ATOM   1120 C  CG2 . THR   A 1 146 ? -34.507 -52.706 -16.148 1.00 214.43 ? 166 THR   A CG2 1 
ATOM   1121 N  N   . GLY   A 1 147 ? -34.228 -51.569 -20.800 1.00 248.40 ? 167 GLY   A N   1 
ATOM   1122 C  CA  . GLY   A 1 147 ? -34.079 -50.643 -21.905 1.00 253.55 ? 167 GLY   A CA  1 
ATOM   1123 C  C   . GLY   A 1 147 ? -34.878 -49.382 -21.653 1.00 249.21 ? 167 GLY   A C   1 
ATOM   1124 O  O   . GLY   A 1 147 ? -35.875 -49.125 -22.335 1.00 248.54 ? 167 GLY   A O   1 
ATOM   1125 N  N   . LYS   A 1 148 ? -34.444 -48.584 -20.682 1.00 223.77 ? 168 LYS   A N   1 
ATOM   1126 C  CA  . LYS   A 1 148 ? -35.108 -47.335 -20.332 1.00 220.85 ? 168 LYS   A CA  1 
ATOM   1127 C  C   . LYS   A 1 148 ? -34.095 -46.200 -20.393 1.00 221.56 ? 168 LYS   A C   1 
ATOM   1128 O  O   . LYS   A 1 148 ? -33.036 -46.289 -19.746 1.00 205.39 ? 168 LYS   A O   1 
ATOM   1129 C  CB  . LYS   A 1 148 ? -35.732 -47.422 -18.938 1.00 212.85 ? 168 LYS   A CB  1 
ATOM   1130 C  CG  . LYS   A 1 148 ? -36.509 -46.181 -18.529 1.00 205.24 ? 168 LYS   A CG  1 
ATOM   1131 C  CD  . LYS   A 1 148 ? -37.115 -46.344 -17.147 1.00 192.93 ? 168 LYS   A CD  1 
ATOM   1132 C  CE  . LYS   A 1 148 ? -37.857 -45.089 -16.720 1.00 178.68 ? 168 LYS   A CE  1 
ATOM   1133 N  NZ  . LYS   A 1 148 ? -38.966 -44.738 -17.650 1.00 176.87 ? 168 LYS   A NZ  1 
ATOM   1134 N  N   . PRO   A 1 149 ? -34.359 -45.138 -21.159 1.00 230.00 ? 169 PRO   A N   1 
ATOM   1135 C  CA  . PRO   A 1 149 ? -33.420 -44.011 -21.219 1.00 225.12 ? 169 PRO   A CA  1 
ATOM   1136 C  C   . PRO   A 1 149 ? -33.178 -43.407 -19.845 1.00 223.18 ? 169 PRO   A C   1 
ATOM   1137 O  O   . PRO   A 1 149 ? -34.051 -43.412 -18.975 1.00 226.66 ? 169 PRO   A O   1 
ATOM   1138 C  CB  . PRO   A 1 149 ? -34.119 -43.019 -22.156 1.00 227.17 ? 169 PRO   A CB  1 
ATOM   1139 C  CG  . PRO   A 1 149 ? -35.000 -43.866 -23.001 1.00 223.65 ? 169 PRO   A CG  1 
ATOM   1140 C  CD  . PRO   A 1 149 ? -35.476 -44.977 -22.104 1.00 227.99 ? 169 PRO   A CD  1 
ATOM   1141 N  N   . VAL   A 1 150 ? -31.971 -42.879 -19.661 1.00 193.11 ? 170 VAL   A N   1 
ATOM   1142 C  CA  . VAL   A 1 150 ? -31.480 -42.452 -18.356 1.00 180.49 ? 170 VAL   A CA  1 
ATOM   1143 C  C   . VAL   A 1 150 ? -31.345 -40.936 -18.339 1.00 170.17 ? 170 VAL   A C   1 
ATOM   1144 O  O   . VAL   A 1 150 ? -30.782 -40.344 -19.269 1.00 168.61 ? 170 VAL   A O   1 
ATOM   1145 C  CB  . VAL   A 1 150 ? -30.138 -43.123 -18.020 1.00 178.26 ? 170 VAL   A CB  1 
ATOM   1146 C  CG1 . VAL   A 1 150 ? -29.547 -42.511 -16.764 1.00 161.49 ? 170 VAL   A CG1 1 
ATOM   1147 C  CG2 . VAL   A 1 150 ? -30.332 -44.622 -17.852 1.00 181.05 ? 170 VAL   A CG2 1 
ATOM   1148 N  N   . THR   A 1 151 ? -31.874 -40.308 -17.289 1.00 164.74 ? 171 THR   A N   1 
ATOM   1149 C  CA  . THR   A 1 151 ? -31.563 -38.915 -16.984 1.00 160.00 ? 171 THR   A CA  1 
ATOM   1150 C  C   . THR   A 1 151 ? -30.185 -38.873 -16.333 1.00 156.52 ? 171 THR   A C   1 
ATOM   1151 O  O   . THR   A 1 151 ? -30.007 -39.354 -15.209 1.00 158.31 ? 171 THR   A O   1 
ATOM   1152 C  CB  . THR   A 1 151 ? -32.622 -38.307 -16.067 1.00 161.38 ? 171 THR   A CB  1 
ATOM   1153 O  OG1 . THR   A 1 151 ? -32.771 -39.121 -14.897 1.00 161.65 ? 171 THR   A OG1 1 
ATOM   1154 C  CG2 . THR   A 1 151 ? -33.962 -38.202 -16.783 1.00 156.62 ? 171 THR   A CG2 1 
ATOM   1155 N  N   . LEU   A 1 152 ? -29.208 -38.300 -17.038 1.00 163.53 ? 172 LEU   A N   1 
ATOM   1156 C  CA  . LEU   A 1 152 ? -27.824 -38.351 -16.576 1.00 163.45 ? 172 LEU   A CA  1 
ATOM   1157 C  C   . LEU   A 1 152 ? -27.628 -37.542 -15.299 1.00 165.73 ? 172 LEU   A C   1 
ATOM   1158 O  O   . LEU   A 1 152 ? -27.001 -38.015 -14.344 1.00 167.80 ? 172 LEU   A O   1 
ATOM   1159 C  CB  . LEU   A 1 152 ? -26.888 -37.855 -17.678 1.00 155.82 ? 172 LEU   A CB  1 
ATOM   1160 C  CG  . LEU   A 1 152 ? -26.838 -38.738 -18.926 1.00 156.93 ? 172 LEU   A CG  1 
ATOM   1161 C  CD1 . LEU   A 1 152 ? -25.981 -38.102 -20.001 1.00 153.01 ? 172 LEU   A CD1 1 
ATOM   1162 C  CD2 . LEU   A 1 152 ? -26.321 -40.125 -18.577 1.00 156.31 ? 172 LEU   A CD2 1 
ATOM   1163 N  N   . LYS   A 1 153 ? -28.162 -36.318 -15.262 1.00 163.42 ? 173 LYS   A N   1 
ATOM   1164 C  CA  . LYS   A 1 153 ? -27.951 -35.444 -14.113 1.00 157.26 ? 173 LYS   A CA  1 
ATOM   1165 C  C   . LYS   A 1 153 ? -28.543 -36.017 -12.831 1.00 157.34 ? 173 LYS   A C   1 
ATOM   1166 O  O   . LYS   A 1 153 ? -28.103 -35.646 -11.738 1.00 154.26 ? 173 LYS   A O   1 
ATOM   1167 C  CB  . LYS   A 1 153 ? -28.542 -34.064 -14.399 1.00 154.83 ? 173 LYS   A CB  1 
ATOM   1168 C  CG  . LYS   A 1 153 ? -27.781 -32.911 -13.774 1.00 138.20 ? 173 LYS   A CG  1 
ATOM   1169 C  CD  . LYS   A 1 153 ? -28.186 -31.598 -14.422 1.00 142.27 ? 173 LYS   A CD  1 
ATOM   1170 C  CE  . LYS   A 1 153 ? -27.361 -30.440 -13.894 1.00 143.36 ? 173 LYS   A CE  1 
ATOM   1171 N  NZ  . LYS   A 1 153 ? -27.524 -29.214 -14.724 1.00 128.52 ? 173 LYS   A NZ  1 
ATOM   1172 N  N   . ASP   A 1 154 ? -29.526 -36.913 -12.941 1.00 152.99 ? 174 ASP   A N   1 
ATOM   1173 C  CA  . ASP   A 1 154 ? -30.053 -37.585 -11.758 1.00 155.45 ? 174 ASP   A CA  1 
ATOM   1174 C  C   . ASP   A 1 154 ? -29.022 -38.539 -11.166 1.00 155.54 ? 174 ASP   A C   1 
ATOM   1175 O  O   . ASP   A 1 154 ? -28.702 -38.462 -9.975  1.00 155.66 ? 174 ASP   A O   1 
ATOM   1176 C  CB  . ASP   A 1 154 ? -31.339 -38.334 -12.107 1.00 162.53 ? 174 ASP   A CB  1 
ATOM   1177 C  CG  . ASP   A 1 154 ? -32.537 -37.414 -12.223 1.00 164.96 ? 174 ASP   A CG  1 
ATOM   1178 O  OD1 . ASP   A 1 154 ? -32.408 -36.225 -11.863 1.00 146.06 ? 174 ASP   A OD1 1 
ATOM   1179 O  OD2 . ASP   A 1 154 ? -33.607 -37.879 -12.671 1.00 167.91 ? 174 ASP   A OD2 1 
ATOM   1180 N  N   . VAL   A 1 155 ? -28.491 -39.447 -11.988 1.00 168.80 ? 175 VAL   A N   1 
ATOM   1181 C  CA  . VAL   A 1 155 ? -27.524 -40.427 -11.503 1.00 164.39 ? 175 VAL   A CA  1 
ATOM   1182 C  C   . VAL   A 1 155 ? -26.129 -39.826 -11.356 1.00 172.90 ? 175 VAL   A C   1 
ATOM   1183 O  O   . VAL   A 1 155 ? -25.338 -40.309 -10.536 1.00 171.18 ? 175 VAL   A O   1 
ATOM   1184 C  CB  . VAL   A 1 155 ? -27.521 -41.658 -12.430 1.00 156.76 ? 175 VAL   A CB  1 
ATOM   1185 C  CG1 . VAL   A 1 155 ? -26.971 -41.306 -13.809 1.00 160.65 ? 175 VAL   A CG1 1 
ATOM   1186 C  CG2 . VAL   A 1 155 ? -26.758 -42.820 -11.802 1.00 163.70 ? 175 VAL   A CG2 1 
ATOM   1187 N  N   . PHE   A 1 156 ? -25.808 -38.774 -12.114 1.00 187.26 ? 176 PHE   A N   1 
ATOM   1188 C  CA  . PHE   A 1 156 ? -24.551 -38.062 -11.899 1.00 190.47 ? 176 PHE   A CA  1 
ATOM   1189 C  C   . PHE   A 1 156 ? -24.617 -37.211 -10.637 1.00 185.90 ? 176 PHE   A C   1 
ATOM   1190 O  O   . PHE   A 1 156 ? -23.687 -37.218 -9.822  1.00 186.07 ? 176 PHE   A O   1 
ATOM   1191 C  CB  . PHE   A 1 156 ? -24.217 -37.191 -13.111 1.00 183.83 ? 176 PHE   A CB  1 
ATOM   1192 C  CG  . PHE   A 1 156 ? -23.752 -37.968 -14.309 1.00 176.91 ? 176 PHE   A CG  1 
ATOM   1193 C  CD1 . PHE   A 1 156 ? -23.156 -39.211 -14.158 1.00 184.45 ? 176 PHE   A CD1 1 
ATOM   1194 C  CD2 . PHE   A 1 156 ? -23.906 -37.454 -15.587 1.00 174.32 ? 176 PHE   A CD2 1 
ATOM   1195 C  CE1 . PHE   A 1 156 ? -22.724 -39.928 -15.259 1.00 185.98 ? 176 PHE   A CE1 1 
ATOM   1196 C  CE2 . PHE   A 1 156 ? -23.477 -38.165 -16.693 1.00 180.19 ? 176 PHE   A CE2 1 
ATOM   1197 C  CZ  . PHE   A 1 156 ? -22.885 -39.404 -16.529 1.00 190.27 ? 176 PHE   A CZ  1 
ATOM   1198 N  N   . GLY   A 1 157 ? -25.707 -36.461 -10.466 1.00 173.46 ? 177 GLY   A N   1 
ATOM   1199 C  CA  . GLY   A 1 157 ? -25.872 -35.680 -9.251  1.00 169.71 ? 177 GLY   A CA  1 
ATOM   1200 C  C   . GLY   A 1 157 ? -25.959 -36.549 -8.013  1.00 169.10 ? 177 GLY   A C   1 
ATOM   1201 O  O   . GLY   A 1 157 ? -25.427 -36.199 -6.957  1.00 166.42 ? 177 GLY   A O   1 
ATOM   1202 N  N   . ALA   A 1 158 ? -26.637 -37.694 -8.126  1.00 167.42 ? 178 ALA   A N   1 
ATOM   1203 C  CA  . ALA   A 1 158 ? -26.629 -38.667 -7.040  1.00 171.14 ? 178 ALA   A CA  1 
ATOM   1204 C  C   . ALA   A 1 158 ? -25.209 -39.112 -6.722  1.00 167.43 ? 178 ALA   A C   1 
ATOM   1205 O  O   . ALA   A 1 158 ? -24.848 -39.284 -5.551  1.00 171.01 ? 178 ALA   A O   1 
ATOM   1206 C  CB  . ALA   A 1 158 ? -27.503 -39.867 -7.405  1.00 172.83 ? 178 ALA   A CB  1 
ATOM   1207 N  N   . TYR   A 1 159 ? -24.385 -39.294 -7.755  1.00 161.72 ? 179 TYR   A N   1 
ATOM   1208 C  CA  . TYR   A 1 159 ? -22.975 -39.597 -7.538  1.00 159.61 ? 179 TYR   A CA  1 
ATOM   1209 C  C   . TYR   A 1 159 ? -22.233 -38.389 -6.981  1.00 158.58 ? 179 TYR   A C   1 
ATOM   1210 O  O   . TYR   A 1 159 ? -21.519 -38.496 -5.977  1.00 158.72 ? 179 TYR   A O   1 
ATOM   1211 C  CB  . TYR   A 1 159 ? -22.331 -40.066 -8.844  1.00 162.11 ? 179 TYR   A CB  1 
ATOM   1212 C  CG  . TYR   A 1 159 ? -20.827 -39.909 -8.864  1.00 159.73 ? 179 TYR   A CG  1 
ATOM   1213 C  CD1 . TYR   A 1 159 ? -20.003 -40.853 -8.265  1.00 158.65 ? 179 TYR   A CD1 1 
ATOM   1214 C  CD2 . TYR   A 1 159 ? -20.232 -38.814 -9.477  1.00 154.74 ? 179 TYR   A CD2 1 
ATOM   1215 C  CE1 . TYR   A 1 159 ? -18.628 -40.710 -8.278  1.00 156.38 ? 179 TYR   A CE1 1 
ATOM   1216 C  CE2 . TYR   A 1 159 ? -18.862 -38.661 -9.491  1.00 148.46 ? 179 TYR   A CE2 1 
ATOM   1217 C  CZ  . TYR   A 1 159 ? -18.064 -39.612 -8.894  1.00 151.61 ? 179 TYR   A CZ  1 
ATOM   1218 O  OH  . TYR   A 1 159 ? -16.697 -39.456 -8.914  1.00 149.69 ? 179 TYR   A OH  1 
ATOM   1219 N  N   . SER   A 1 160 ? -22.390 -37.227 -7.625  1.00 152.12 ? 180 SER   A N   1 
ATOM   1220 C  CA  . SER   A 1 160 ? -21.638 -36.038 -7.231  1.00 157.36 ? 180 SER   A CA  1 
ATOM   1221 C  C   . SER   A 1 160 ? -21.910 -35.658 -5.781  1.00 155.64 ? 180 SER   A C   1 
ATOM   1222 O  O   . SER   A 1 160 ? -20.985 -35.306 -5.038  1.00 150.99 ? 180 SER   A O   1 
ATOM   1223 C  CB  . SER   A 1 160 ? -21.978 -34.874 -8.160  1.00 154.07 ? 180 SER   A CB  1 
ATOM   1224 O  OG  . SER   A 1 160 ? -21.788 -35.231 -9.518  1.00 153.19 ? 180 SER   A OG  1 
ATOM   1225 N  N   . MET   A 1 161 ? -23.176 -35.720 -5.362  1.00 160.12 ? 181 MET   A N   1 
ATOM   1226 C  CA  . MET   A 1 161 ? -23.513 -35.428 -3.972  1.00 162.20 ? 181 MET   A CA  1 
ATOM   1227 C  C   . MET   A 1 161 ? -22.820 -36.397 -3.023  1.00 162.38 ? 181 MET   A C   1 
ATOM   1228 O  O   . MET   A 1 161 ? -22.290 -35.986 -1.984  1.00 159.09 ? 181 MET   A O   1 
ATOM   1229 C  CB  . MET   A 1 161 ? -25.027 -35.478 -3.781  1.00 165.44 ? 181 MET   A CB  1 
ATOM   1230 C  CG  . MET   A 1 161 ? -25.478 -35.419 -2.331  1.00 165.14 ? 181 MET   A CG  1 
ATOM   1231 S  SD  . MET   A 1 161 ? -25.032 -33.867 -1.531  1.00 185.53 ? 181 MET   A SD  1 
ATOM   1232 C  CE  . MET   A 1 161 ? -25.731 -32.687 -2.682  1.00 170.27 ? 181 MET   A CE  1 
ATOM   1233 N  N   . ASP   A 1 162 ? -22.801 -37.687 -3.373  1.00 163.95 ? 182 ASP   A N   1 
ATOM   1234 C  CA  . ASP   A 1 162 ? -22.133 -38.675 -2.531  1.00 168.19 ? 182 ASP   A CA  1 
ATOM   1235 C  C   . ASP   A 1 162 ? -20.657 -38.347 -2.355  1.00 164.93 ? 182 ASP   A C   1 
ATOM   1236 O  O   . ASP   A 1 162 ? -20.079 -38.601 -1.292  1.00 166.19 ? 182 ASP   A O   1 
ATOM   1237 C  CB  . ASP   A 1 162 ? -22.295 -40.070 -3.132  1.00 175.62 ? 182 ASP   A CB  1 
ATOM   1238 C  CG  . ASP   A 1 162 ? -23.715 -40.576 -3.053  1.00 184.33 ? 182 ASP   A CG  1 
ATOM   1239 O  OD1 . ASP   A 1 162 ? -24.578 -39.833 -2.543  1.00 189.51 ? 182 ASP   A OD1 1 
ATOM   1240 O  OD2 . ASP   A 1 162 ? -23.970 -41.715 -3.498  1.00 189.14 ? 182 ASP   A OD2 1 
ATOM   1241 N  N   . VAL   A 1 163 ? -20.031 -37.783 -3.388  1.00 162.82 ? 183 VAL   A N   1 
ATOM   1242 C  CA  . VAL   A 1 163 ? -18.608 -37.473 -3.315  1.00 160.10 ? 183 VAL   A CA  1 
ATOM   1243 C  C   . VAL   A 1 163 ? -18.363 -36.303 -2.369  1.00 163.06 ? 183 VAL   A C   1 
ATOM   1244 O  O   . VAL   A 1 163 ? -17.462 -36.346 -1.525  1.00 166.02 ? 183 VAL   A O   1 
ATOM   1245 C  CB  . VAL   A 1 163 ? -18.048 -37.185 -4.719  1.00 158.24 ? 183 VAL   A CB  1 
ATOM   1246 C  CG1 . VAL   A 1 163 ? -16.555 -36.905 -4.649  1.00 154.65 ? 183 VAL   A CG1 1 
ATOM   1247 C  CG2 . VAL   A 1 163 ? -18.333 -38.346 -5.653  1.00 151.81 ? 183 VAL   A CG2 1 
ATOM   1248 N  N   . ILE   A 1 164 ? -19.169 -35.245 -2.488  1.00 163.30 ? 184 ILE   A N   1 
ATOM   1249 C  CA  . ILE   A 1 164 ? -18.860 -34.000 -1.791  1.00 162.05 ? 184 ILE   A CA  1 
ATOM   1250 C  C   . ILE   A 1 164 ? -19.120 -34.129 -0.293  1.00 164.32 ? 184 ILE   A C   1 
ATOM   1251 O  O   . ILE   A 1 164 ? -18.404 -33.538 0.524   1.00 165.23 ? 184 ILE   A O   1 
ATOM   1252 C  CB  . ILE   A 1 164 ? -19.642 -32.827 -2.416  1.00 155.44 ? 184 ILE   A CB  1 
ATOM   1253 C  CG1 . ILE   A 1 164 ? -18.675 -31.725 -2.846  1.00 149.19 ? 184 ILE   A CG1 1 
ATOM   1254 C  CG2 . ILE   A 1 164 ? -20.675 -32.259 -1.454  1.00 156.52 ? 184 ILE   A CG2 1 
ATOM   1255 C  CD1 . ILE   A 1 164 ? -17.595 -31.415 -1.833  1.00 152.94 ? 184 ILE   A CD1 1 
ATOM   1256 N  N   . THR   A 1 165 ? -20.134 -34.909 0.095   1.00 158.28 ? 185 THR   A N   1 
ATOM   1257 C  CA  . THR   A 1 165 ? -20.458 -35.023 1.514   1.00 161.29 ? 185 THR   A CA  1 
ATOM   1258 C  C   . THR   A 1 165 ? -19.362 -35.744 2.287   1.00 169.09 ? 185 THR   A C   1 
ATOM   1259 O  O   . THR   A 1 165 ? -19.172 -35.480 3.479   1.00 171.78 ? 185 THR   A O   1 
ATOM   1260 C  CB  . THR   A 1 165 ? -21.796 -35.742 1.700   1.00 166.62 ? 185 THR   A CB  1 
ATOM   1261 O  OG1 . THR   A 1 165 ? -21.767 -37.002 1.018   1.00 169.22 ? 185 THR   A OG1 1 
ATOM   1262 C  CG2 . THR   A 1 165 ? -22.939 -34.899 1.156   1.00 159.50 ? 185 THR   A CG2 1 
ATOM   1263 N  N   . SER   A 1 166 ? -18.629 -36.641 1.630   1.00 170.75 ? 186 SER   A N   1 
ATOM   1264 C  CA  . SER   A 1 166 ? -17.572 -37.399 2.288   1.00 177.51 ? 186 SER   A CA  1 
ATOM   1265 C  C   . SER   A 1 166 ? -16.197 -36.767 2.108   1.00 177.69 ? 186 SER   A C   1 
ATOM   1266 O  O   . SER   A 1 166 ? -15.392 -36.768 3.046   1.00 180.33 ? 186 SER   A O   1 
ATOM   1267 C  CB  . SER   A 1 166 ? -17.562 -38.838 1.766   1.00 183.90 ? 186 SER   A CB  1 
ATOM   1268 O  OG  . SER   A 1 166 ? -18.223 -38.924 0.516   1.00 185.96 ? 186 SER   A OG  1 
ATOM   1269 N  N   . THR   A 1 167 ? -15.910 -36.223 0.921   1.00 178.93 ? 187 THR   A N   1 
ATOM   1270 C  CA  . THR   A 1 167 ? -14.615 -35.596 0.678   1.00 173.90 ? 187 THR   A CA  1 
ATOM   1271 C  C   . THR   A 1 167 ? -14.368 -34.401 1.591   1.00 176.87 ? 187 THR   A C   1 
ATOM   1272 O  O   . THR   A 1 167 ? -13.210 -34.019 1.795   1.00 185.05 ? 187 THR   A O   1 
ATOM   1273 C  CB  . THR   A 1 167 ? -14.499 -35.152 -0.783  1.00 173.24 ? 187 THR   A CB  1 
ATOM   1274 O  OG1 . THR   A 1 167 ? -15.698 -34.474 -1.180  1.00 170.12 ? 187 THR   A OG1 1 
ATOM   1275 C  CG2 . THR   A 1 167 ? -14.263 -36.350 -1.695  1.00 172.18 ? 187 THR   A CG2 1 
ATOM   1276 N  N   . SER   A 1 168 ? -15.423 -33.804 2.145   1.00 182.34 ? 188 SER   A N   1 
ATOM   1277 C  CA  . SER   A 1 168 ? -15.291 -32.655 3.029   1.00 180.68 ? 188 SER   A CA  1 
ATOM   1278 C  C   . SER   A 1 168 ? -15.699 -32.937 4.466   1.00 174.81 ? 188 SER   A C   1 
ATOM   1279 O  O   . SER   A 1 168 ? -15.136 -32.331 5.381   1.00 180.26 ? 188 SER   A O   1 
ATOM   1280 C  CB  . SER   A 1 168 ? -16.124 -31.480 2.498   1.00 173.15 ? 188 SER   A CB  1 
ATOM   1281 O  OG  . SER   A 1 168 ? -15.680 -31.084 1.212   1.00 168.58 ? 188 SER   A OG  1 
ATOM   1282 N  N   . PHE   A 1 169 ? -16.654 -33.843 4.687   1.00 175.85 ? 189 PHE   A N   1 
ATOM   1283 C  CA  . PHE   A 1 169 ? -17.130 -34.172 6.027   1.00 169.50 ? 189 PHE   A CA  1 
ATOM   1284 C  C   . PHE   A 1 169 ? -16.914 -35.643 6.354   1.00 173.52 ? 189 PHE   A C   1 
ATOM   1285 O  O   . PHE   A 1 169 ? -16.138 -35.959 7.261   1.00 173.54 ? 189 PHE   A O   1 
ATOM   1286 C  CB  . PHE   A 1 169 ? -18.614 -33.801 6.169   1.00 163.62 ? 189 PHE   A CB  1 
ATOM   1287 C  CG  . PHE   A 1 169 ? -18.956 -32.442 5.629   1.00 151.79 ? 189 PHE   A CG  1 
ATOM   1288 C  CD1 . PHE   A 1 169 ? -19.281 -32.276 4.292   1.00 152.72 ? 189 PHE   A CD1 1 
ATOM   1289 C  CD2 . PHE   A 1 169 ? -18.964 -31.332 6.459   1.00 153.13 ? 189 PHE   A CD2 1 
ATOM   1290 C  CE1 . PHE   A 1 169 ? -19.599 -31.029 3.790   1.00 147.57 ? 189 PHE   A CE1 1 
ATOM   1291 C  CE2 . PHE   A 1 169 ? -19.283 -30.081 5.964   1.00 150.92 ? 189 PHE   A CE2 1 
ATOM   1292 C  CZ  . PHE   A 1 169 ? -19.601 -29.930 4.628   1.00 146.62 ? 189 PHE   A CZ  1 
ATOM   1293 N  N   . GLY   A 1 170 ? -17.573 -36.555 5.641   1.00 173.63 ? 190 GLY   A N   1 
ATOM   1294 C  CA  . GLY   A 1 170 ? -17.375 -37.975 5.866   1.00 180.56 ? 190 GLY   A CA  1 
ATOM   1295 C  C   . GLY   A 1 170 ? -18.656 -38.783 5.894   1.00 185.78 ? 190 GLY   A C   1 
ATOM   1296 O  O   . GLY   A 1 170 ? -18.628 -39.991 6.150   1.00 193.74 ? 190 GLY   A O   1 
ATOM   1297 N  N   . VAL   A 1 171 ? -19.785 -38.135 5.627   1.00 189.36 ? 191 VAL   A N   1 
ATOM   1298 C  CA  . VAL   A 1 171 ? -21.081 -38.799 5.700   1.00 198.11 ? 191 VAL   A CA  1 
ATOM   1299 C  C   . VAL   A 1 171 ? -21.302 -39.616 4.434   1.00 197.27 ? 191 VAL   A C   1 
ATOM   1300 O  O   . VAL   A 1 171 ? -21.144 -39.111 3.316   1.00 194.00 ? 191 VAL   A O   1 
ATOM   1301 C  CB  . VAL   A 1 171 ? -22.207 -37.775 5.909   1.00 200.56 ? 191 VAL   A CB  1 
ATOM   1302 C  CG1 . VAL   A 1 171 ? -23.551 -38.480 5.994   1.00 207.21 ? 191 VAL   A CG1 1 
ATOM   1303 C  CG2 . VAL   A 1 171 ? -21.948 -36.961 7.166   1.00 202.03 ? 191 VAL   A CG2 1 
ATOM   1304 N  N   . ASN   A 1 172 ? -21.676 -40.881 4.609   1.00 198.93 ? 192 ASN   A N   1 
ATOM   1305 C  CA  . ASN   A 1 172 ? -21.873 -41.816 3.508   1.00 204.28 ? 192 ASN   A CA  1 
ATOM   1306 C  C   . ASN   A 1 172 ? -23.361 -42.098 3.343   1.00 209.48 ? 192 ASN   A C   1 
ATOM   1307 O  O   . ASN   A 1 172 ? -24.012 -42.579 4.278   1.00 211.19 ? 192 ASN   A O   1 
ATOM   1308 C  CB  . ASN   A 1 172 ? -21.103 -43.113 3.753   1.00 204.22 ? 192 ASN   A CB  1 
ATOM   1309 C  CG  . ASN   A 1 172 ? -21.306 -43.652 5.151   1.00 205.87 ? 192 ASN   A CG  1 
ATOM   1310 O  OD1 . ASN   A 1 172 ? -20.524 -43.365 6.058   1.00 205.40 ? 192 ASN   A OD1 1 
ATOM   1311 N  ND2 . ASN   A 1 172 ? -22.363 -44.434 5.337   1.00 208.88 ? 192 ASN   A ND2 1 
ATOM   1312 N  N   . ILE   A 1 173 ? -23.888 -41.805 2.156   1.00 209.46 ? 193 ILE   A N   1 
ATOM   1313 C  CA  . ILE   A 1 173 ? -25.301 -41.999 1.840   1.00 212.23 ? 193 ILE   A CA  1 
ATOM   1314 C  C   . ILE   A 1 173 ? -25.419 -42.397 0.376   1.00 209.58 ? 193 ILE   A C   1 
ATOM   1315 O  O   . ILE   A 1 173 ? -24.871 -41.726 -0.505  1.00 204.63 ? 193 ILE   A O   1 
ATOM   1316 C  CB  . ILE   A 1 173 ? -26.133 -40.729 2.118   1.00 217.27 ? 193 ILE   A CB  1 
ATOM   1317 C  CG1 . ILE   A 1 173 ? -26.318 -40.515 3.620   1.00 216.28 ? 193 ILE   A CG1 1 
ATOM   1318 C  CG2 . ILE   A 1 173 ? -27.483 -40.800 1.416   1.00 221.08 ? 193 ILE   A CG2 1 
ATOM   1319 C  CD1 . ILE   A 1 173 ? -27.088 -39.266 3.958   1.00 218.25 ? 193 ILE   A CD1 1 
ATOM   1320 N  N   . ASP   A 1 174 ? -26.129 -43.494 0.116   1.00 216.44 ? 194 ASP   A N   1 
ATOM   1321 C  CA  . ASP   A 1 174 ? -26.513 -43.850 -1.248  1.00 211.14 ? 194 ASP   A CA  1 
ATOM   1322 C  C   . ASP   A 1 174 ? -27.504 -42.732 -1.544  1.00 215.87 ? 194 ASP   A C   1 
ATOM   1323 O  O   . ASP   A 1 174 ? -28.426 -42.486 -0.757  1.00 218.89 ? 194 ASP   A O   1 
ATOM   1324 C  CB  . ASP   A 1 174 ? -26.971 -45.305 -1.313  1.00 200.86 ? 194 ASP   A CB  1 
ATOM   1325 C  CG  . ASP   A 1 174 ? -27.241 -45.773 -2.737  1.00 198.65 ? 194 ASP   A CG  1 
ATOM   1326 O  OD1 . ASP   A 1 174 ? -26.928 -45.019 -3.684  1.00 196.94 ? 194 ASP   A OD1 1 
ATOM   1327 O  OD2 . ASP   A 1 174 ? -27.760 -46.894 -2.914  1.00 185.42 ? 194 ASP   A OD2 1 
ATOM   1328 N  N   . SER   A 1 175 ? -27.336 -42.069 -2.680  1.00 231.51 ? 195 SER   A N   1 
ATOM   1329 C  CA  . SER   A 1 175 ? -28.277 -41.033 -3.100  1.00 229.47 ? 195 SER   A CA  1 
ATOM   1330 C  C   . SER   A 1 175 ? -29.457 -41.548 -3.910  1.00 230.18 ? 195 SER   A C   1 
ATOM   1331 O  O   . SER   A 1 175 ? -29.877 -40.912 -4.876  1.00 223.75 ? 195 SER   A O   1 
ATOM   1332 C  CB  . SER   A 1 175 ? -27.524 -39.945 -3.856  1.00 221.52 ? 195 SER   A CB  1 
ATOM   1333 O  OG  . SER   A 1 175 ? -26.674 -39.239 -2.977  1.00 220.59 ? 195 SER   A OG  1 
ATOM   1334 N  N   . LEU   A 1 176 ? -30.000 -42.704 -3.539  1.00 217.45 ? 196 LEU   A N   1 
ATOM   1335 C  CA  . LEU   A 1 176 ? -31.305 -43.127 -4.017  1.00 210.40 ? 196 LEU   A CA  1 
ATOM   1336 C  C   . LEU   A 1 176 ? -32.342 -43.178 -2.909  1.00 218.26 ? 196 LEU   A C   1 
ATOM   1337 O  O   . LEU   A 1 176 ? -33.542 -43.187 -3.197  1.00 208.96 ? 196 LEU   A O   1 
ATOM   1338 C  CB  . LEU   A 1 176 ? -31.201 -44.500 -4.704  1.00 194.63 ? 196 LEU   A CB  1 
ATOM   1339 C  CG  . LEU   A 1 176 ? -32.423 -45.009 -5.477  1.00 183.20 ? 196 LEU   A CG  1 
ATOM   1340 C  CD1 . LEU   A 1 176 ? -32.876 -43.986 -6.510  1.00 172.17 ? 196 LEU   A CD1 1 
ATOM   1341 C  CD2 . LEU   A 1 176 ? -32.161 -46.366 -6.135  1.00 183.04 ? 196 LEU   A CD2 1 
ATOM   1342 N  N   . ASN   A 1 177 ? -31.901 -43.189 -1.656  1.00 230.57 ? 197 ASN   A N   1 
ATOM   1343 C  CA  . ASN   A 1 177 ? -32.776 -43.039 -0.505  1.00 229.82 ? 197 ASN   A CA  1 
ATOM   1344 C  C   . ASN   A 1 177 ? -32.873 -41.536 -0.246  1.00 231.69 ? 197 ASN   A C   1 
ATOM   1345 O  O   . ASN   A 1 177 ? -32.497 -40.728 -1.108  1.00 228.03 ? 197 ASN   A O   1 
ATOM   1346 C  CB  . ASN   A 1 177 ? -32.152 -43.696 0.730   1.00 231.87 ? 197 ASN   A CB  1 
ATOM   1347 C  CG  . ASN   A 1 177 ? -30.748 -43.172 1.044   1.00 230.85 ? 197 ASN   A CG  1 
ATOM   1348 O  OD1 . ASN   A 1 177 ? -30.520 -41.964 1.096   1.00 237.88 ? 197 ASN   A OD1 1 
ATOM   1349 N  ND2 . ASN   A 1 177 ? -29.807 -44.088 1.275   1.00 224.31 ? 197 ASN   A ND2 1 
ATOM   1350 N  N   . ASN   A 1 178 ? -33.372 -41.153 0.919   1.00 254.59 ? 198 ASN   A N   1 
ATOM   1351 C  CA  . ASN   A 1 178 ? -33.691 -39.765 1.237   1.00 252.27 ? 198 ASN   A CA  1 
ATOM   1352 C  C   . ASN   A 1 178 ? -32.429 -38.910 1.258   1.00 254.02 ? 198 ASN   A C   1 
ATOM   1353 O  O   . ASN   A 1 178 ? -31.591 -39.087 2.153   1.00 253.14 ? 198 ASN   A O   1 
ATOM   1354 C  CB  . ASN   A 1 178 ? -34.416 -39.685 2.590   1.00 247.02 ? 198 ASN   A CB  1 
ATOM   1355 C  CG  . ASN   A 1 178 ? -33.696 -40.450 3.693   1.00 251.19 ? 198 ASN   A CG  1 
ATOM   1356 O  OD1 . ASN   A 1 178 ? -33.039 -41.456 3.432   1.00 250.18 ? 198 ASN   A OD1 1 
ATOM   1357 N  ND2 . ASN   A 1 178 ? -33.817 -39.973 4.932   1.00 252.23 ? 198 ASN   A ND2 1 
ATOM   1358 N  N   . PRO   A 1 179 ? -32.243 -37.984 0.311   1.00 229.43 ? 199 PRO   A N   1 
ATOM   1359 C  CA  . PRO   A 1 179 ? -31.059 -37.117 0.354   1.00 219.52 ? 199 PRO   A CA  1 
ATOM   1360 C  C   . PRO   A 1 179 ? -31.331 -35.830 1.113   1.00 215.92 ? 199 PRO   A C   1 
ATOM   1361 O  O   . PRO   A 1 179 ? -32.073 -34.964 0.641   1.00 211.83 ? 199 PRO   A O   1 
ATOM   1362 C  CB  . PRO   A 1 179 ? -30.772 -36.854 -1.127  1.00 211.26 ? 199 PRO   A CB  1 
ATOM   1363 C  CG  . PRO   A 1 179 ? -32.143 -36.903 -1.781  1.00 210.84 ? 199 PRO   A CG  1 
ATOM   1364 C  CD  . PRO   A 1 179 ? -33.047 -37.755 -0.905  1.00 220.83 ? 199 PRO   A CD  1 
ATOM   1365 N  N   . GLN   A 1 180 ? -30.739 -35.696 2.297   1.00 209.21 ? 200 GLN   A N   1 
ATOM   1366 C  CA  . GLN   A 1 180 ? -30.946 -34.518 3.136   1.00 203.70 ? 200 GLN   A CA  1 
ATOM   1367 C  C   . GLN   A 1 180 ? -30.094 -33.362 2.616   1.00 201.91 ? 200 GLN   A C   1 
ATOM   1368 O  O   . GLN   A 1 180 ? -29.104 -32.956 3.224   1.00 203.92 ? 200 GLN   A O   1 
ATOM   1369 C  CB  . GLN   A 1 180 ? -30.612 -34.831 4.587   1.00 207.26 ? 200 GLN   A CB  1 
ATOM   1370 C  CG  . GLN   A 1 180 ? -29.660 -36.018 4.773   1.00 210.28 ? 200 GLN   A CG  1 
ATOM   1371 C  CD  . GLN   A 1 180 ? -28.298 -35.795 4.134   1.00 210.34 ? 200 GLN   A CD  1 
ATOM   1372 O  OE1 . GLN   A 1 180 ? -28.069 -36.173 2.985   1.00 208.94 ? 200 GLN   A OE1 1 
ATOM   1373 N  NE2 . GLN   A 1 180 ? -27.392 -35.170 4.876   1.00 210.67 ? 200 GLN   A NE2 1 
ATOM   1374 N  N   . ASP   A 1 181 ? -30.496 -32.833 1.457   1.00 199.07 ? 201 ASP   A N   1 
ATOM   1375 C  CA  . ASP   A 1 181 ? -29.794 -31.715 0.833   1.00 193.48 ? 201 ASP   A CA  1 
ATOM   1376 C  C   . ASP   A 1 181 ? -30.659 -31.040 -0.225  1.00 188.22 ? 201 ASP   A C   1 
ATOM   1377 O  O   . ASP   A 1 181 ? -30.424 -31.229 -1.424  1.00 186.97 ? 201 ASP   A O   1 
ATOM   1378 C  CB  . ASP   A 1 181 ? -28.483 -32.185 0.199   1.00 196.32 ? 201 ASP   A CB  1 
ATOM   1379 C  CG  . ASP   A 1 181 ? -28.619 -33.532 -0.485  1.00 195.05 ? 201 ASP   A CG  1 
ATOM   1380 O  OD1 . ASP   A 1 181 ? -28.681 -34.560 0.223   1.00 195.61 ? 201 ASP   A OD1 1 
ATOM   1381 O  OD2 . ASP   A 1 181 ? -28.679 -33.561 -1.731  1.00 190.36 ? 201 ASP   A OD2 1 
ATOM   1382 N  N   . PRO   A 1 182 ? -31.660 -30.254 0.164   1.00 192.46 ? 202 PRO   A N   1 
ATOM   1383 C  CA  . PRO   A 1 182 ? -32.396 -29.454 -0.817  1.00 185.63 ? 202 PRO   A CA  1 
ATOM   1384 C  C   . PRO   A 1 182 ? -31.802 -28.065 -0.993  1.00 186.96 ? 202 PRO   A C   1 
ATOM   1385 O  O   . PRO   A 1 182 ? -31.170 -27.505 -0.097  1.00 181.57 ? 202 PRO   A O   1 
ATOM   1386 C  CB  . PRO   A 1 182 ? -33.798 -29.380 -0.200  1.00 178.90 ? 202 PRO   A CB  1 
ATOM   1387 C  CG  . PRO   A 1 182 ? -33.525 -29.352 1.263   1.00 180.25 ? 202 PRO   A CG  1 
ATOM   1388 C  CD  . PRO   A 1 182 ? -32.293 -30.200 1.495   1.00 188.81 ? 202 PRO   A CD  1 
ATOM   1389 N  N   . PHE   A 1 183 ? -32.017 -27.516 -2.185  1.00 183.42 ? 203 PHE   A N   1 
ATOM   1390 C  CA  . PHE   A 1 183 ? -31.527 -26.181 -2.534  1.00 181.64 ? 203 PHE   A CA  1 
ATOM   1391 C  C   . PHE   A 1 183 ? -32.215 -25.643 -3.784  1.00 177.91 ? 203 PHE   A C   1 
ATOM   1392 O  O   . PHE   A 1 183 ? -33.436 -25.489 -3.811  1.00 176.83 ? 203 PHE   A O   1 
ATOM   1393 C  CB  . PHE   A 1 183 ? -30.011 -26.199 -2.736  1.00 182.89 ? 203 PHE   A CB  1 
ATOM   1394 C  CG  . PHE   A 1 183 ? -29.476 -27.531 -3.178  1.00 184.11 ? 203 PHE   A CG  1 
ATOM   1395 C  CD1 . PHE   A 1 183 ? -29.784 -28.042 -4.429  1.00 181.46 ? 203 PHE   A CD1 1 
ATOM   1396 C  CD2 . PHE   A 1 183 ? -28.658 -28.270 -2.343  1.00 184.70 ? 203 PHE   A CD2 1 
ATOM   1397 C  CE1 . PHE   A 1 183 ? -29.286 -29.269 -4.833  1.00 186.65 ? 203 PHE   A CE1 1 
ATOM   1398 C  CE2 . PHE   A 1 183 ? -28.157 -29.493 -2.742  1.00 185.50 ? 203 PHE   A CE2 1 
ATOM   1399 C  CZ  . PHE   A 1 183 ? -28.471 -29.993 -3.988  1.00 188.00 ? 203 PHE   A CZ  1 
ATOM   1400 N  N   . PRO   A 1 198 ? -36.808 -14.983 -12.635 1.00 169.37 ? 218 PRO   A N   1 
ATOM   1401 C  CA  . PRO   A 1 198 ? -37.120 -15.037 -11.206 1.00 181.25 ? 218 PRO   A CA  1 
ATOM   1402 C  C   . PRO   A 1 198 ? -37.256 -13.657 -10.580 1.00 196.49 ? 218 PRO   A C   1 
ATOM   1403 O  O   . PRO   A 1 198 ? -38.100 -12.861 -10.993 1.00 192.69 ? 218 PRO   A O   1 
ATOM   1404 C  CB  . PRO   A 1 198 ? -35.912 -15.774 -10.623 1.00 179.18 ? 218 PRO   A CB  1 
ATOM   1405 C  CG  . PRO   A 1 198 ? -34.772 -15.484 -11.598 1.00 178.83 ? 218 PRO   A CG  1 
ATOM   1406 C  CD  . PRO   A 1 198 ? -35.358 -14.861 -12.852 1.00 172.99 ? 218 PRO   A CD  1 
ATOM   1407 N  N   . PHE   A 1 199 ? -36.417 -13.383 -9.582  1.00 220.36 ? 219 PHE   A N   1 
ATOM   1408 C  CA  . PHE   A 1 199 ? -36.366 -12.076 -8.942  1.00 221.84 ? 219 PHE   A CA  1 
ATOM   1409 C  C   . PHE   A 1 199 ? -34.983 -11.442 -8.942  1.00 224.98 ? 219 PHE   A C   1 
ATOM   1410 O  O   . PHE   A 1 199 ? -34.894 -10.218 -8.771  1.00 225.95 ? 219 PHE   A O   1 
ATOM   1411 C  CB  . PHE   A 1 199 ? -36.873 -12.170 -7.495  1.00 219.05 ? 219 PHE   A CB  1 
ATOM   1412 C  CG  . PHE   A 1 199 ? -35.789 -12.336 -6.477  1.00 214.57 ? 219 PHE   A CG  1 
ATOM   1413 C  CD1 . PHE   A 1 199 ? -35.073 -13.515 -6.395  1.00 212.71 ? 219 PHE   A CD1 1 
ATOM   1414 C  CD2 . PHE   A 1 199 ? -35.502 -11.319 -5.583  1.00 214.62 ? 219 PHE   A CD2 1 
ATOM   1415 C  CE1 . PHE   A 1 199 ? -34.077 -13.670 -5.456  1.00 209.48 ? 219 PHE   A CE1 1 
ATOM   1416 C  CE2 . PHE   A 1 199 ? -34.510 -11.471 -4.639  1.00 211.94 ? 219 PHE   A CE2 1 
ATOM   1417 C  CZ  . PHE   A 1 199 ? -33.796 -12.648 -4.576  1.00 210.56 ? 219 PHE   A CZ  1 
ATOM   1418 N  N   . PHE   A 1 200 ? -33.909 -12.218 -9.134  1.00 202.11 ? 220 PHE   A N   1 
ATOM   1419 C  CA  . PHE   A 1 200 ? -32.567 -11.660 -9.246  1.00 201.19 ? 220 PHE   A CA  1 
ATOM   1420 C  C   . PHE   A 1 200 ? -32.469 -10.605 -10.341 1.00 195.27 ? 220 PHE   A C   1 
ATOM   1421 O  O   . PHE   A 1 200 ? -31.570 -9.759  -10.294 1.00 188.00 ? 220 PHE   A O   1 
ATOM   1422 C  CB  . PHE   A 1 200 ? -31.565 -12.791 -9.498  1.00 195.35 ? 220 PHE   A CB  1 
ATOM   1423 C  CG  . PHE   A 1 200 ? -31.706 -13.957 -8.547  1.00 195.40 ? 220 PHE   A CG  1 
ATOM   1424 C  CD1 . PHE   A 1 200 ? -30.971 -14.003 -7.373  1.00 193.44 ? 220 PHE   A CD1 1 
ATOM   1425 C  CD2 . PHE   A 1 200 ? -32.572 -15.003 -8.829  1.00 193.63 ? 220 PHE   A CD2 1 
ATOM   1426 C  CE1 . PHE   A 1 200 ? -31.101 -15.065 -6.500  1.00 196.25 ? 220 PHE   A CE1 1 
ATOM   1427 C  CE2 . PHE   A 1 200 ? -32.706 -16.065 -7.958  1.00 192.05 ? 220 PHE   A CE2 1 
ATOM   1428 C  CZ  . PHE   A 1 200 ? -31.969 -16.096 -6.793  1.00 197.90 ? 220 PHE   A CZ  1 
ATOM   1429 N  N   . LEU   A 1 201 ? -33.372 -10.643 -11.322 1.00 208.32 ? 221 LEU   A N   1 
ATOM   1430 C  CA  . LEU   A 1 201 ? -33.469 -9.553  -12.286 1.00 210.27 ? 221 LEU   A CA  1 
ATOM   1431 C  C   . LEU   A 1 201 ? -33.873 -8.257  -11.593 1.00 207.52 ? 221 LEU   A C   1 
ATOM   1432 O  O   . LEU   A 1 201 ? -33.212 -7.224  -11.749 1.00 203.93 ? 221 LEU   A O   1 
ATOM   1433 C  CB  . LEU   A 1 201 ? -34.463 -9.920  -13.393 1.00 215.08 ? 221 LEU   A CB  1 
ATOM   1434 C  CG  . LEU   A 1 201 ? -34.596 -9.010  -14.618 1.00 206.52 ? 221 LEU   A CG  1 
ATOM   1435 C  CD1 . LEU   A 1 201 ? -35.584 -7.868  -14.384 1.00 195.62 ? 221 LEU   A CD1 1 
ATOM   1436 C  CD2 . LEU   A 1 201 ? -33.230 -8.471  -15.016 1.00 200.41 ? 221 LEU   A CD2 1 
ATOM   1437 N  N   . SER   A 1 202 ? -34.962 -8.300  -10.816 1.00 195.90 ? 222 SER   A N   1 
ATOM   1438 C  CA  . SER   A 1 202 ? -35.403 -7.121  -10.074 1.00 193.67 ? 222 SER   A CA  1 
ATOM   1439 C  C   . SER   A 1 202 ? -34.320 -6.613  -9.131  1.00 187.60 ? 222 SER   A C   1 
ATOM   1440 O  O   . SER   A 1 202 ? -34.245 -5.408  -8.866  1.00 189.38 ? 222 SER   A O   1 
ATOM   1441 C  CB  . SER   A 1 202 ? -36.684 -7.434  -9.297  1.00 190.70 ? 222 SER   A CB  1 
ATOM   1442 O  OG  . SER   A 1 202 ? -37.126 -8.760  -9.532  1.00 189.00 ? 222 SER   A OG  1 
ATOM   1443 N  N   . ILE   A 1 203 ? -33.469 -7.513  -8.627  1.00 193.36 ? 223 ILE   A N   1 
ATOM   1444 C  CA  . ILE   A 1 203 ? -32.305 -7.107  -7.840  1.00 187.00 ? 223 ILE   A CA  1 
ATOM   1445 C  C   . ILE   A 1 203 ? -31.421 -6.147  -8.622  1.00 186.09 ? 223 ILE   A C   1 
ATOM   1446 O  O   . ILE   A 1 203 ? -30.817 -5.240  -8.041  1.00 182.11 ? 223 ILE   A O   1 
ATOM   1447 C  CB  . ILE   A 1 203 ? -31.500 -8.344  -7.390  1.00 185.06 ? 223 ILE   A CB  1 
ATOM   1448 C  CG1 . ILE   A 1 203 ? -32.308 -9.225  -6.442  1.00 193.02 ? 223 ILE   A CG1 1 
ATOM   1449 C  CG2 . ILE   A 1 203 ? -30.193 -7.940  -6.723  1.00 165.41 ? 223 ILE   A CG2 1 
ATOM   1450 C  CD1 . ILE   A 1 203 ? -31.499 -10.382 -5.904  1.00 196.87 ? 223 ILE   A CD1 1 
ATOM   1451 N  N   . THR   A 1 204 ? -31.313 -6.330  -9.939  1.00 179.37 ? 224 THR   A N   1 
ATOM   1452 C  CA  . THR   A 1 204 ? -30.433 -5.469  -10.721 1.00 165.23 ? 224 THR   A CA  1 
ATOM   1453 C  C   . THR   A 1 204 ? -31.057 -4.102  -10.988 1.00 166.48 ? 224 THR   A C   1 
ATOM   1454 O  O   . THR   A 1 204 ? -30.331 -3.104  -11.061 1.00 163.72 ? 224 THR   A O   1 
ATOM   1455 C  CB  . THR   A 1 204 ? -30.049 -6.157  -12.032 1.00 153.19 ? 224 THR   A CB  1 
ATOM   1456 O  OG1 . THR   A 1 204 ? -30.478 -7.524  -11.990 1.00 165.71 ? 224 THR   A OG1 1 
ATOM   1457 C  CG2 . THR   A 1 204 ? -28.540 -6.131  -12.211 1.00 145.21 ? 224 THR   A CG2 1 
ATOM   1458 N  N   . VAL   A 1 205 ? -32.383 -4.024  -11.126 1.00 171.15 ? 225 VAL   A N   1 
ATOM   1459 C  CA  . VAL   A 1 205 ? -33.019 -2.713  -11.213 1.00 178.28 ? 225 VAL   A CA  1 
ATOM   1460 C  C   . VAL   A 1 205 ? -33.170 -2.111  -9.822  1.00 192.13 ? 225 VAL   A C   1 
ATOM   1461 O  O   . VAL   A 1 205 ? -33.157 -0.884  -9.662  1.00 195.77 ? 225 VAL   A O   1 
ATOM   1462 C  CB  . VAL   A 1 205 ? -34.376 -2.808  -11.940 1.00 177.97 ? 225 VAL   A CB  1 
ATOM   1463 C  CG1 . VAL   A 1 205 ? -34.844 -1.423  -12.395 1.00 168.38 ? 225 VAL   A CG1 1 
ATOM   1464 C  CG2 . VAL   A 1 205 ? -34.267 -3.744  -13.112 1.00 163.24 ? 225 VAL   A CG2 1 
ATOM   1465 N  N   . PHE   A 1 206 ? -33.298 -2.958  -8.800  1.00 215.65 ? 226 PHE   A N   1 
ATOM   1466 C  CA  . PHE   A 1 206 ? -33.412 -2.535  -7.406  1.00 219.69 ? 226 PHE   A CA  1 
ATOM   1467 C  C   . PHE   A 1 206 ? -32.259 -3.089  -6.568  1.00 210.07 ? 226 PHE   A C   1 
ATOM   1468 O  O   . PHE   A 1 206 ? -32.489 -3.826  -5.603  1.00 206.98 ? 226 PHE   A O   1 
ATOM   1469 C  CB  . PHE   A 1 206 ? -34.741 -2.984  -6.801  1.00 232.99 ? 226 PHE   A CB  1 
ATOM   1470 C  CG  . PHE   A 1 206 ? -35.948 -2.770  -7.683  1.00 242.76 ? 226 PHE   A CG  1 
ATOM   1471 C  CD1 . PHE   A 1 206 ? -36.024 -1.714  -8.573  1.00 245.79 ? 226 PHE   A CD1 1 
ATOM   1472 C  CD2 . PHE   A 1 206 ? -37.030 -3.629  -7.587  1.00 244.82 ? 226 PHE   A CD2 1 
ATOM   1473 C  CE1 . PHE   A 1 206 ? -37.139 -1.534  -9.364  1.00 246.03 ? 226 PHE   A CE1 1 
ATOM   1474 C  CE2 . PHE   A 1 206 ? -38.150 -3.448  -8.369  1.00 246.42 ? 226 PHE   A CE2 1 
ATOM   1475 C  CZ  . PHE   A 1 206 ? -38.206 -2.400  -9.258  1.00 246.42 ? 226 PHE   A CZ  1 
ATOM   1476 N  N   . PRO   A 1 207 ? -31.002 -2.767  -6.901  1.00 179.96 ? 227 PRO   A N   1 
ATOM   1477 C  CA  . PRO   A 1 207 ? -29.910 -3.154  -5.995  1.00 172.31 ? 227 PRO   A CA  1 
ATOM   1478 C  C   . PRO   A 1 207 ? -29.957 -2.372  -4.708  1.00 165.01 ? 227 PRO   A C   1 
ATOM   1479 O  O   . PRO   A 1 207 ? -29.392 -2.805  -3.694  1.00 158.36 ? 227 PRO   A O   1 
ATOM   1480 C  CB  . PRO   A 1 207 ? -28.650 -2.844  -6.807  1.00 174.69 ? 227 PRO   A CB  1 
ATOM   1481 C  CG  . PRO   A 1 207 ? -29.058 -1.711  -7.664  1.00 179.38 ? 227 PRO   A CG  1 
ATOM   1482 C  CD  . PRO   A 1 207 ? -30.510 -1.917  -8.000  1.00 179.82 ? 227 PRO   A CD  1 
ATOM   1483 N  N   . PHE   A 1 208 ? -30.631 -1.225  -4.733  1.00 159.80 ? 228 PHE   A N   1 
ATOM   1484 C  CA  . PHE   A 1 208 ? -30.932 -0.481  -3.523  1.00 160.79 ? 228 PHE   A CA  1 
ATOM   1485 C  C   . PHE   A 1 208 ? -31.836 -1.261  -2.581  1.00 158.06 ? 228 PHE   A C   1 
ATOM   1486 O  O   . PHE   A 1 208 ? -31.918 -0.924  -1.394  1.00 156.02 ? 228 PHE   A O   1 
ATOM   1487 C  CB  . PHE   A 1 208 ? -31.564 0.857   -3.906  1.00 166.04 ? 228 PHE   A CB  1 
ATOM   1488 C  CG  . PHE   A 1 208 ? -32.751 0.743   -4.825  1.00 175.35 ? 228 PHE   A CG  1 
ATOM   1489 C  CD1 . PHE   A 1 208 ? -33.992 0.376   -4.332  1.00 173.09 ? 228 PHE   A CD1 1 
ATOM   1490 C  CD2 . PHE   A 1 208 ? -32.633 1.041   -6.178  1.00 182.03 ? 228 PHE   A CD2 1 
ATOM   1491 C  CE1 . PHE   A 1 208 ? -35.086 0.284   -5.167  1.00 182.81 ? 228 PHE   A CE1 1 
ATOM   1492 C  CE2 . PHE   A 1 208 ? -33.724 0.954   -7.024  1.00 194.52 ? 228 PHE   A CE2 1 
ATOM   1493 C  CZ  . PHE   A 1 208 ? -34.952 0.578   -6.517  1.00 200.83 ? 228 PHE   A CZ  1 
ATOM   1494 N  N   . LEU   A 1 209 ? -32.518 -2.287  -3.082  1.00 160.56 ? 229 LEU   A N   1 
ATOM   1495 C  CA  . LEU   A 1 209 ? -33.330 -3.166  -2.251  1.00 157.76 ? 229 LEU   A CA  1 
ATOM   1496 C  C   . LEU   A 1 209 ? -32.531 -4.267  -1.577  1.00 151.96 ? 229 LEU   A C   1 
ATOM   1497 O  O   . LEU   A 1 209 ? -33.062 -4.935  -0.690  1.00 153.82 ? 229 LEU   A O   1 
ATOM   1498 C  CB  . LEU   A 1 209 ? -34.445 -3.800  -3.084  1.00 167.25 ? 229 LEU   A CB  1 
ATOM   1499 C  CG  . LEU   A 1 209 ? -35.680 -2.935  -3.276  1.00 173.20 ? 229 LEU   A CG  1 
ATOM   1500 C  CD1 . LEU   A 1 209 ? -36.721 -3.704  -4.056  1.00 177.82 ? 229 LEU   A CD1 1 
ATOM   1501 C  CD2 . LEU   A 1 209 ? -36.216 -2.520  -1.922  1.00 166.15 ? 229 LEU   A CD2 1 
ATOM   1502 N  N   . ILE   A 1 210 ? -31.288 -4.485  -1.986  1.00 159.06 ? 230 ILE   A N   1 
ATOM   1503 C  CA  . ILE   A 1 210 ? -30.436 -5.495  -1.360  1.00 158.11 ? 230 ILE   A CA  1 
ATOM   1504 C  C   . ILE   A 1 210 ? -30.245 -5.156  0.116   1.00 162.78 ? 230 ILE   A C   1 
ATOM   1505 O  O   . ILE   A 1 210 ? -30.541 -6.005  0.969   1.00 160.86 ? 230 ILE   A O   1 
ATOM   1506 C  CB  . ILE   A 1 210 ? -29.083 -5.630  -2.084  1.00 154.82 ? 230 ILE   A CB  1 
ATOM   1507 C  CG1 . ILE   A 1 210 ? -29.242 -6.405  -3.394  1.00 158.02 ? 230 ILE   A CG1 1 
ATOM   1508 C  CG2 . ILE   A 1 210 ? -28.054 -6.308  -1.180  1.00 158.23 ? 230 ILE   A CG2 1 
ATOM   1509 C  CD1 . ILE   A 1 210 ? -27.989 -6.421  -4.260  1.00 161.85 ? 230 ILE   A CD1 1 
ATOM   1510 N  N   . PRO   A 1 211 ? -29.778 -3.951  0.481   1.00 150.53 ? 231 PRO   A N   1 
ATOM   1511 C  CA  . PRO   A 1 211 ? -29.651 -3.659  1.917   1.00 150.50 ? 231 PRO   A CA  1 
ATOM   1512 C  C   . PRO   A 1 211 ? -30.975 -3.719  2.638   1.00 151.15 ? 231 PRO   A C   1 
ATOM   1513 O  O   . PRO   A 1 211 ? -31.008 -3.974  3.848   1.00 154.60 ? 231 PRO   A O   1 
ATOM   1514 C  CB  . PRO   A 1 211 ? -29.064 -2.242  1.949   1.00 151.59 ? 231 PRO   A CB  1 
ATOM   1515 C  CG  . PRO   A 1 211 ? -28.517 -2.010  0.578   1.00 145.78 ? 231 PRO   A CG  1 
ATOM   1516 C  CD  . PRO   A 1 211 ? -29.418 -2.772  -0.330  1.00 151.47 ? 231 PRO   A CD  1 
ATOM   1517 N  N   . ILE   A 1 212 ? -32.070 -3.454  1.925   1.00 149.49 ? 232 ILE   A N   1 
ATOM   1518 C  CA  . ILE   A 1 212 ? -33.403 -3.569  2.505   1.00 149.72 ? 232 ILE   A CA  1 
ATOM   1519 C  C   . ILE   A 1 212 ? -33.623 -4.976  3.042   1.00 148.36 ? 232 ILE   A C   1 
ATOM   1520 O  O   . ILE   A 1 212 ? -33.857 -5.178  4.238   1.00 151.13 ? 232 ILE   A O   1 
ATOM   1521 C  CB  . ILE   A 1 212 ? -34.468 -3.194  1.462   1.00 149.99 ? 232 ILE   A CB  1 
ATOM   1522 C  CG1 . ILE   A 1 212 ? -34.364 -1.706  1.123   1.00 155.08 ? 232 ILE   A CG1 1 
ATOM   1523 C  CG2 . ILE   A 1 212 ? -35.850 -3.591  1.947   1.00 148.42 ? 232 ILE   A CG2 1 
ATOM   1524 C  CD1 . ILE   A 1 212 ? -35.639 -0.947  1.402   1.00 159.15 ? 232 ILE   A CD1 1 
ATOM   1525 N  N   . LEU   A 1 213 ? -33.531 -5.970  2.158   1.00 157.68 ? 233 LEU   A N   1 
ATOM   1526 C  CA  . LEU   A 1 213 ? -33.700 -7.368  2.533   1.00 154.77 ? 233 LEU   A CA  1 
ATOM   1527 C  C   . LEU   A 1 213 ? -32.615 -7.860  3.482   1.00 158.72 ? 233 LEU   A C   1 
ATOM   1528 O  O   . LEU   A 1 213 ? -32.776 -8.936  4.071   1.00 163.84 ? 233 LEU   A O   1 
ATOM   1529 C  CB  . LEU   A 1 213 ? -33.731 -8.234  1.276   1.00 152.89 ? 233 LEU   A CB  1 
ATOM   1530 C  CG  . LEU   A 1 213 ? -34.499 -7.649  0.089   1.00 152.85 ? 233 LEU   A CG  1 
ATOM   1531 C  CD1 . LEU   A 1 213 ? -33.810 -7.993  -1.220  1.00 156.49 ? 233 LEU   A CD1 1 
ATOM   1532 C  CD2 . LEU   A 1 213 ? -35.926 -8.145  0.079   1.00 153.58 ? 233 LEU   A CD2 1 
ATOM   1533 N  N   . GLU   A 1 214 ? -31.516 -7.102  3.645   1.00 151.53 ? 234 GLU   A N   1 
ATOM   1534 C  CA  . GLU   A 1 214 ? -30.430 -7.451  4.564   1.00 158.93 ? 234 GLU   A CA  1 
ATOM   1535 C  C   . GLU   A 1 214 ? -30.797 -7.232  6.005   1.00 163.76 ? 234 GLU   A C   1 
ATOM   1536 O  O   . GLU   A 1 214 ? -29.925 -7.415  6.867   1.00 170.29 ? 234 GLU   A O   1 
ATOM   1537 C  CB  . GLU   A 1 214 ? -29.166 -6.645  4.242   1.00 167.70 ? 234 GLU   A CB  1 
ATOM   1538 C  CG  . GLU   A 1 214 ? -28.441 -7.049  2.966   1.00 180.34 ? 234 GLU   A CG  1 
ATOM   1539 C  CD  . GLU   A 1 214 ? -27.727 -8.379  3.075   1.00 185.91 ? 234 GLU   A CD  1 
ATOM   1540 O  OE1 . GLU   A 1 214 ? -27.684 -8.952  4.183   1.00 197.60 ? 234 GLU   A OE1 1 
ATOM   1541 O  OE2 . GLU   A 1 214 ? -27.205 -8.850  2.043   1.00 172.40 ? 234 GLU   A OE2 1 
ATOM   1542 N  N   . VAL   A 1 215 ? -32.036 -6.856  6.320   1.00 164.31 ? 235 VAL   A N   1 
ATOM   1543 C  CA  . VAL   A 1 215 ? -32.419 -6.632  7.710   1.00 168.19 ? 235 VAL   A CA  1 
ATOM   1544 C  C   . VAL   A 1 215 ? -33.578 -7.550  8.077   1.00 174.86 ? 235 VAL   A C   1 
ATOM   1545 O  O   . VAL   A 1 215 ? -33.696 -7.985  9.228   1.00 177.66 ? 235 VAL   A O   1 
ATOM   1546 C  CB  . VAL   A 1 215 ? -32.761 -5.148  7.966   1.00 166.19 ? 235 VAL   A CB  1 
ATOM   1547 C  CG1 . VAL   A 1 215 ? -34.188 -4.978  8.457   1.00 172.96 ? 235 VAL   A CG1 1 
ATOM   1548 C  CG2 . VAL   A 1 215 ? -31.789 -4.550  8.980   1.00 163.41 ? 235 VAL   A CG2 1 
ATOM   1549 N  N   . LEU   A 1 216 ? -34.434 -7.865  7.104   1.00 175.25 ? 236 LEU   A N   1 
ATOM   1550 C  CA  . LEU   A 1 216 ? -35.516 -8.808  7.343   1.00 184.73 ? 236 LEU   A CA  1 
ATOM   1551 C  C   . LEU   A 1 216 ? -35.068 -10.248 7.186   1.00 191.54 ? 236 LEU   A C   1 
ATOM   1552 O  O   . LEU   A 1 216 ? -35.889 -11.105 6.858   1.00 193.57 ? 236 LEU   A O   1 
ATOM   1553 C  CB  . LEU   A 1 216 ? -36.716 -8.529  6.424   1.00 182.18 ? 236 LEU   A CB  1 
ATOM   1554 C  CG  . LEU   A 1 216 ? -36.786 -7.468  5.317   1.00 172.41 ? 236 LEU   A CG  1 
ATOM   1555 C  CD1 . LEU   A 1 216 ? -38.137 -7.549  4.603   1.00 169.81 ? 236 LEU   A CD1 1 
ATOM   1556 C  CD2 . LEU   A 1 216 ? -36.578 -6.063  5.848   1.00 174.73 ? 236 LEU   A CD2 1 
ATOM   1557 N  N   . ASN   A 1 217 ? -33.777 -10.519 7.378   1.00 204.97 ? 237 ASN   A N   1 
ATOM   1558 C  CA  . ASN   A 1 217 ? -33.231 -11.873 7.469   1.00 217.08 ? 237 ASN   A CA  1 
ATOM   1559 C  C   . ASN   A 1 217 ? -33.677 -12.775 6.318   1.00 222.03 ? 237 ASN   A C   1 
ATOM   1560 O  O   . ASN   A 1 217 ? -33.677 -14.003 6.450   1.00 228.94 ? 237 ASN   A O   1 
ATOM   1561 C  CB  . ASN   A 1 217 ? -33.585 -12.514 8.816   1.00 214.03 ? 237 ASN   A CB  1 
ATOM   1562 C  CG  . ASN   A 1 217 ? -32.507 -13.454 9.312   1.00 226.44 ? 237 ASN   A CG  1 
ATOM   1563 O  OD1 . ASN   A 1 217 ? -32.683 -14.671 9.321   1.00 230.73 ? 237 ASN   A OD1 1 
ATOM   1564 N  ND2 . ASN   A 1 217 ? -31.375 -12.890 9.720   1.00 232.05 ? 237 ASN   A ND2 1 
ATOM   1565 N  N   . ILE   A 1 218 ? -34.060 -12.198 5.180   1.00 192.19 ? 238 ILE   A N   1 
ATOM   1566 C  CA  . ILE   A 1 218 ? -34.370 -13.002 4.004   1.00 184.95 ? 238 ILE   A CA  1 
ATOM   1567 C  C   . ILE   A 1 218 ? -33.052 -13.438 3.384   1.00 184.40 ? 238 ILE   A C   1 
ATOM   1568 O  O   . ILE   A 1 218 ? -32.490 -12.740 2.533   1.00 175.05 ? 238 ILE   A O   1 
ATOM   1569 C  CB  . ILE   A 1 218 ? -35.238 -12.237 2.991   1.00 176.11 ? 238 ILE   A CB  1 
ATOM   1570 C  CG1 . ILE   A 1 218 ? -35.699 -10.905 3.577   1.00 172.97 ? 238 ILE   A CG1 1 
ATOM   1571 C  CG2 . ILE   A 1 218 ? -36.440 -13.075 2.593   1.00 177.45 ? 238 ILE   A CG2 1 
ATOM   1572 C  CD1 . ILE   A 1 218 ? -36.799 -10.263 2.782   1.00 166.47 ? 238 ILE   A CD1 1 
ATOM   1573 N  N   . CYS   A 1 219 ? -32.547 -14.588 3.815   1.00 183.06 ? 239 CYS   A N   1 
ATOM   1574 C  CA  . CYS   A 1 219 ? -31.223 -15.040 3.413   1.00 176.02 ? 239 CYS   A CA  1 
ATOM   1575 C  C   . CYS   A 1 219 ? -31.297 -16.304 2.563   1.00 167.22 ? 239 CYS   A C   1 
ATOM   1576 O  O   . CYS   A 1 219 ? -32.174 -16.441 1.710   1.00 163.12 ? 239 CYS   A O   1 
ATOM   1577 C  CB  . CYS   A 1 219 ? -30.355 -15.283 4.649   1.00 177.49 ? 239 CYS   A CB  1 
ATOM   1578 S  SG  . CYS   A 1 219 ? -30.497 -13.999 5.918   1.00 190.10 ? 239 CYS   A SG  1 
ATOM   1579 N  N   . THR   A 1 226 ? -33.403 -21.224 4.727   1.00 163.75 ? 246 THR   A N   1 
ATOM   1580 C  CA  . THR   A 1 226 ? -33.798 -22.193 5.741   1.00 178.33 ? 246 THR   A CA  1 
ATOM   1581 C  C   . THR   A 1 226 ? -32.677 -22.451 6.741   1.00 191.12 ? 246 THR   A C   1 
ATOM   1582 O  O   . THR   A 1 226 ? -31.499 -22.249 6.442   1.00 186.20 ? 246 THR   A O   1 
ATOM   1583 C  CB  . THR   A 1 226 ? -34.215 -23.534 5.112   1.00 181.01 ? 246 THR   A CB  1 
ATOM   1584 O  OG1 . THR   A 1 226 ? -34.525 -24.473 6.148   1.00 188.05 ? 246 THR   A OG1 1 
ATOM   1585 C  CG2 . THR   A 1 226 ? -33.091 -24.091 4.251   1.00 177.47 ? 246 THR   A CG2 1 
ATOM   1586 N  N   . ASN   A 1 227 ? -33.057 -22.894 7.936   1.00 193.58 ? 247 ASN   A N   1 
ATOM   1587 C  CA  . ASN   A 1 227 ? -32.101 -23.240 8.975   1.00 203.95 ? 247 ASN   A CA  1 
ATOM   1588 C  C   . ASN   A 1 227 ? -31.678 -24.698 8.911   1.00 209.24 ? 247 ASN   A C   1 
ATOM   1589 O  O   . ASN   A 1 227 ? -31.081 -25.196 9.870   1.00 223.15 ? 247 ASN   A O   1 
ATOM   1590 C  CB  . ASN   A 1 227 ? -32.675 -22.916 10.361  1.00 208.77 ? 247 ASN   A CB  1 
ATOM   1591 C  CG  . ASN   A 1 227 ? -34.071 -23.488 10.574  1.00 208.07 ? 247 ASN   A CG  1 
ATOM   1592 O  OD1 . ASN   A 1 227 ? -34.512 -24.379 9.849   1.00 206.06 ? 247 ASN   A OD1 1 
ATOM   1593 N  ND2 . ASN   A 1 227 ? -34.773 -22.973 11.581  1.00 206.38 ? 247 ASN   A ND2 1 
ATOM   1594 N  N   . PHE   A 1 228 ? -31.972 -25.379 7.801   1.00 204.36 ? 248 PHE   A N   1 
ATOM   1595 C  CA  . PHE   A 1 228 ? -31.742 -26.812 7.649   1.00 203.32 ? 248 PHE   A CA  1 
ATOM   1596 C  C   . PHE   A 1 228 ? -30.342 -27.265 8.042   1.00 211.88 ? 248 PHE   A C   1 
ATOM   1597 O  O   . PHE   A 1 228 ? -30.174 -27.996 9.023   1.00 220.89 ? 248 PHE   A O   1 
ATOM   1598 C  CB  . PHE   A 1 228 ? -32.002 -27.234 6.198   1.00 195.57 ? 248 PHE   A CB  1 
ATOM   1599 C  CG  . PHE   A 1 228 ? -31.533 -28.625 5.872   1.00 192.78 ? 248 PHE   A CG  1 
ATOM   1600 C  CD1 . PHE   A 1 228 ? -31.844 -29.691 6.697   1.00 193.07 ? 248 PHE   A CD1 1 
ATOM   1601 C  CD2 . PHE   A 1 228 ? -30.781 -28.864 4.731   1.00 189.75 ? 248 PHE   A CD2 1 
ATOM   1602 C  CE1 . PHE   A 1 228 ? -31.402 -30.969 6.399   1.00 195.66 ? 248 PHE   A CE1 1 
ATOM   1603 C  CE2 . PHE   A 1 228 ? -30.340 -30.138 4.426   1.00 189.15 ? 248 PHE   A CE2 1 
ATOM   1604 C  CZ  . PHE   A 1 228 ? -30.650 -31.191 5.260   1.00 192.75 ? 248 PHE   A CZ  1 
ATOM   1605 N  N   . LEU   A 1 229 ? -29.332 -26.826 7.298   1.00 206.21 ? 249 LEU   A N   1 
ATOM   1606 C  CA  . LEU   A 1 229 ? -27.945 -27.034 7.684   1.00 209.04 ? 249 LEU   A CA  1 
ATOM   1607 C  C   . LEU   A 1 229 ? -27.385 -25.884 8.509   1.00 219.93 ? 249 LEU   A C   1 
ATOM   1608 O  O   . LEU   A 1 229 ? -26.319 -26.038 9.116   1.00 221.50 ? 249 LEU   A O   1 
ATOM   1609 C  CB  . LEU   A 1 229 ? -27.080 -27.251 6.439   1.00 198.42 ? 249 LEU   A CB  1 
ATOM   1610 C  CG  . LEU   A 1 229 ? -27.402 -28.504 5.619   1.00 196.83 ? 249 LEU   A CG  1 
ATOM   1611 C  CD1 . LEU   A 1 229 ? -26.426 -28.668 4.462   1.00 185.72 ? 249 LEU   A CD1 1 
ATOM   1612 C  CD2 . LEU   A 1 229 ? -27.411 -29.748 6.499   1.00 197.69 ? 249 LEU   A CD2 1 
ATOM   1613 N  N   . ARG   A 1 230 ? -28.077 -24.742 8.544   1.00 224.91 ? 250 ARG   A N   1 
ATOM   1614 C  CA  . ARG   A 1 230 ? -27.701 -23.650 9.435   1.00 228.00 ? 250 ARG   A CA  1 
ATOM   1615 C  C   . ARG   A 1 230 ? -27.640 -24.094 10.889  1.00 244.24 ? 250 ARG   A C   1 
ATOM   1616 O  O   . ARG   A 1 230 ? -26.970 -23.443 11.698  1.00 247.66 ? 250 ARG   A O   1 
ATOM   1617 C  CB  . ARG   A 1 230 ? -28.690 -22.496 9.292   1.00 224.04 ? 250 ARG   A CB  1 
ATOM   1618 C  CG  . ARG   A 1 230 ? -28.108 -21.233 8.705   1.00 220.15 ? 250 ARG   A CG  1 
ATOM   1619 C  CD  . ARG   A 1 230 ? -28.754 -20.018 9.340   1.00 221.95 ? 250 ARG   A CD  1 
ATOM   1620 N  NE  . ARG   A 1 230 ? -28.405 -19.912 10.751  1.00 228.77 ? 250 ARG   A NE  1 
ATOM   1621 C  CZ  . ARG   A 1 230 ? -27.558 -19.021 11.249  1.00 233.98 ? 250 ARG   A CZ  1 
ATOM   1622 N  NH1 . ARG   A 1 230 ? -26.991 -18.103 10.483  1.00 234.22 ? 250 ARG   A NH1 1 
ATOM   1623 N  NH2 . ARG   A 1 230 ? -27.277 -19.049 12.549  1.00 234.50 ? 250 ARG   A NH2 1 
ATOM   1624 N  N   . LYS   A 1 231 ? -28.338 -25.172 11.239  1.00 286.72 ? 251 LYS   A N   1 
ATOM   1625 C  CA  . LYS   A 1 231 ? -28.209 -25.811 12.539  1.00 292.53 ? 251 LYS   A CA  1 
ATOM   1626 C  C   . LYS   A 1 231 ? -27.732 -27.254 12.461  1.00 289.03 ? 251 LYS   A C   1 
ATOM   1627 O  O   . LYS   A 1 231 ? -27.113 -27.727 13.413  1.00 295.86 ? 251 LYS   A O   1 
ATOM   1628 C  CB  . LYS   A 1 231 ? -29.545 -25.758 13.300  1.00 290.54 ? 251 LYS   A CB  1 
ATOM   1629 C  CG  . LYS   A 1 231 ? -30.665 -26.549 12.652  1.00 287.61 ? 251 LYS   A CG  1 
ATOM   1630 C  CD  . LYS   A 1 231 ? -32.014 -25.879 12.852  1.00 272.38 ? 251 LYS   A CD  1 
ATOM   1631 C  CE  . LYS   A 1 231 ? -33.128 -26.715 12.240  1.00 268.20 ? 251 LYS   A CE  1 
ATOM   1632 N  NZ  . LYS   A 1 231 ? -32.797 -27.160 10.856  1.00 274.28 ? 251 LYS   A NZ  1 
ATOM   1633 N  N   . SER   A 1 232 ? -27.991 -27.962 11.357  1.00 249.39 ? 252 SER   A N   1 
ATOM   1634 C  CA  . SER   A 1 232 ? -27.502 -29.332 11.214  1.00 237.95 ? 252 SER   A CA  1 
ATOM   1635 C  C   . SER   A 1 232 ? -26.003 -29.350 10.933  1.00 231.20 ? 252 SER   A C   1 
ATOM   1636 O  O   . SER   A 1 232 ? -25.233 -30.003 11.646  1.00 229.84 ? 252 SER   A O   1 
ATOM   1637 C  CB  . SER   A 1 232 ? -28.271 -30.056 10.107  1.00 223.85 ? 252 SER   A CB  1 
ATOM   1638 O  OG  . SER   A 1 232 ? -27.649 -31.281 9.764   1.00 210.27 ? 252 SER   A OG  1 
ATOM   1639 N  N   . VAL   A 1 233 ? -25.571 -28.641 9.886   1.00 216.57 ? 253 VAL   A N   1 
ATOM   1640 C  CA  . VAL   A 1 233 ? -24.139 -28.513 9.632   1.00 211.27 ? 253 VAL   A CA  1 
ATOM   1641 C  C   . VAL   A 1 233 ? -23.469 -27.732 10.757  1.00 213.98 ? 253 VAL   A C   1 
ATOM   1642 O  O   . VAL   A 1 233 ? -22.323 -28.019 11.125  1.00 209.66 ? 253 VAL   A O   1 
ATOM   1643 C  CB  . VAL   A 1 233 ? -23.896 -27.874 8.250   1.00 198.96 ? 253 VAL   A CB  1 
ATOM   1644 C  CG1 . VAL   A 1 233 ? -22.595 -27.085 8.228   1.00 180.74 ? 253 VAL   A CG1 1 
ATOM   1645 C  CG2 . VAL   A 1 233 ? -23.875 -28.950 7.174   1.00 191.57 ? 253 VAL   A CG2 1 
ATOM   1646 N  N   . LYS   A 1 234 ? -24.170 -26.753 11.335  1.00 218.13 ? 254 LYS   A N   1 
ATOM   1647 C  CA  . LYS   A 1 234 ? -23.670 -26.118 12.549  1.00 224.24 ? 254 LYS   A CA  1 
ATOM   1648 C  C   . LYS   A 1 234 ? -23.492 -27.133 13.667  1.00 229.80 ? 254 LYS   A C   1 
ATOM   1649 O  O   . LYS   A 1 234 ? -22.575 -27.003 14.486  1.00 224.00 ? 254 LYS   A O   1 
ATOM   1650 C  CB  . LYS   A 1 234 ? -24.617 -25.004 12.992  1.00 223.83 ? 254 LYS   A CB  1 
ATOM   1651 C  CG  . LYS   A 1 234 ? -24.119 -24.195 14.176  1.00 206.52 ? 254 LYS   A CG  1 
ATOM   1652 C  CD  . LYS   A 1 234 ? -22.728 -23.644 13.916  1.00 191.20 ? 254 LYS   A CD  1 
ATOM   1653 C  CE  . LYS   A 1 234 ? -22.660 -22.164 14.238  1.00 175.75 ? 254 LYS   A CE  1 
ATOM   1654 N  NZ  . LYS   A 1 234 ? -23.653 -21.404 13.434  1.00 177.29 ? 254 LYS   A NZ  1 
ATOM   1655 N  N   . ARG   A 1 235 ? -24.349 -28.151 13.716  1.00 251.07 ? 255 ARG   A N   1 
ATOM   1656 C  CA  . ARG   A 1 235 ? -24.174 -29.269 14.639  1.00 249.07 ? 255 ARG   A CA  1 
ATOM   1657 C  C   . ARG   A 1 235 ? -23.363 -30.400 14.026  1.00 240.48 ? 255 ARG   A C   1 
ATOM   1658 O  O   . ARG   A 1 235 ? -23.655 -31.579 14.250  1.00 241.02 ? 255 ARG   A O   1 
ATOM   1659 C  CB  . ARG   A 1 235 ? -25.532 -29.773 15.114  1.00 255.53 ? 255 ARG   A CB  1 
ATOM   1660 C  CG  . ARG   A 1 235 ? -26.173 -28.912 16.191  1.00 259.54 ? 255 ARG   A CG  1 
ATOM   1661 C  CD  . ARG   A 1 235 ? -27.572 -29.402 16.534  1.00 268.04 ? 255 ARG   A CD  1 
ATOM   1662 N  NE  . ARG   A 1 235 ? -28.541 -29.095 15.488  1.00 271.18 ? 255 ARG   A NE  1 
ATOM   1663 C  CZ  . ARG   A 1 235 ? -28.917 -29.940 14.537  1.00 265.57 ? 255 ARG   A CZ  1 
ATOM   1664 N  NH1 . ARG   A 1 235 ? -28.415 -31.161 14.459  1.00 259.41 ? 255 ARG   A NH1 1 
ATOM   1665 N  NH2 . ARG   A 1 235 ? -29.820 -29.550 13.643  1.00 264.01 ? 255 ARG   A NH2 1 
ATOM   1666 N  N   . MET   A 1 236 ? -22.351 -30.072 13.223  1.00 218.92 ? 256 MET   A N   1 
ATOM   1667 C  CA  . MET   A 1 236 ? -21.298 -31.026 12.887  1.00 213.46 ? 256 MET   A CA  1 
ATOM   1668 C  C   . MET   A 1 236 ? -20.304 -31.000 14.041  1.00 213.07 ? 256 MET   A C   1 
ATOM   1669 O  O   . MET   A 1 236 ? -19.230 -30.398 13.971  1.00 211.11 ? 256 MET   A O   1 
ATOM   1670 C  CB  . MET   A 1 236 ? -20.646 -30.684 11.555  1.00 207.49 ? 256 MET   A CB  1 
ATOM   1671 C  CG  . MET   A 1 236 ? -21.538 -30.977 10.368  1.00 205.24 ? 256 MET   A CG  1 
ATOM   1672 S  SD  . MET   A 1 236 ? -22.290 -32.613 10.465  1.00 202.09 ? 256 MET   A SD  1 
ATOM   1673 C  CE  . MET   A 1 236 ? -23.840 -32.314 9.617   1.00 204.58 ? 256 MET   A CE  1 
ATOM   1674 N  N   . LYS   A 1 237 ? -20.705 -31.636 15.146  1.00 214.24 ? 257 LYS   A N   1 
ATOM   1675 C  CA  . LYS   A 1 237 ? -19.882 -31.634 16.351  1.00 212.91 ? 257 LYS   A CA  1 
ATOM   1676 C  C   . LYS   A 1 237 ? -18.592 -32.426 16.150  1.00 217.69 ? 257 LYS   A C   1 
ATOM   1677 O  O   . LYS   A 1 237 ? -17.529 -32.016 16.632  1.00 214.99 ? 257 LYS   A O   1 
ATOM   1678 C  CB  . LYS   A 1 237 ? -20.685 -32.176 17.543  1.00 205.64 ? 257 LYS   A CB  1 
ATOM   1679 C  CG  . LYS   A 1 237 ? -20.996 -33.676 17.536  1.00 205.58 ? 257 LYS   A CG  1 
ATOM   1680 C  CD  . LYS   A 1 237 ? -22.173 -34.039 16.638  1.00 205.59 ? 257 LYS   A CD  1 
ATOM   1681 C  CE  . LYS   A 1 237 ? -21.706 -34.794 15.401  1.00 204.76 ? 257 LYS   A CE  1 
ATOM   1682 N  NZ  . LYS   A 1 237 ? -22.155 -34.139 14.141  1.00 210.29 ? 257 LYS   A NZ  1 
ATOM   1683 N  N   . GLU   A 1 238 ? -18.664 -33.548 15.422  1.00 230.11 ? 258 GLU   A N   1 
ATOM   1684 C  CA  . GLU   A 1 238 ? -17.519 -34.435 15.180  1.00 231.10 ? 258 GLU   A CA  1 
ATOM   1685 C  C   . GLU   A 1 238 ? -16.749 -34.707 16.469  1.00 230.21 ? 258 GLU   A C   1 
ATOM   1686 O  O   . GLU   A 1 238 ? -15.517 -34.678 16.498  1.00 231.03 ? 258 GLU   A O   1 
ATOM   1687 C  CB  . GLU   A 1 238 ? -16.599 -33.856 14.105  1.00 235.03 ? 258 GLU   A CB  1 
ATOM   1688 C  CG  . GLU   A 1 238 ? -17.307 -33.633 12.792  1.00 233.45 ? 258 GLU   A CG  1 
ATOM   1689 C  CD  . GLU   A 1 238 ? -17.741 -34.931 12.149  1.00 243.17 ? 258 GLU   A CD  1 
ATOM   1690 O  OE1 . GLU   A 1 238 ? -17.005 -35.932 12.289  1.00 252.73 ? 258 GLU   A OE1 1 
ATOM   1691 O  OE2 . GLU   A 1 238 ? -18.814 -34.953 11.510  1.00 242.14 ? 258 GLU   A OE2 1 
ATOM   1692 N  N   . SER   A 1 239 ? -17.486 -34.941 17.552  1.00 215.09 ? 259 SER   A N   1 
ATOM   1693 C  CA  . SER   A 1 239 ? -16.887 -35.131 18.867  1.00 210.80 ? 259 SER   A CA  1 
ATOM   1694 C  C   . SER   A 1 239 ? -17.776 -36.032 19.714  1.00 203.58 ? 259 SER   A C   1 
ATOM   1695 O  O   . SER   A 1 239 ? -19.002 -35.915 19.678  1.00 204.42 ? 259 SER   A O   1 
ATOM   1696 C  CB  . SER   A 1 239 ? -16.676 -33.786 19.572  1.00 205.02 ? 259 SER   A CB  1 
ATOM   1697 O  OG  . SER   A 1 239 ? -15.889 -32.912 18.783  1.00 213.50 ? 259 SER   A OG  1 
ATOM   1698 N  N   . ASP   A 1 250 ? -10.043 -33.956 6.500   1.00 193.92 ? 270 ASP   A N   1 
ATOM   1699 C  CA  . ASP   A 1 250 ? -11.094 -33.476 5.609   1.00 192.79 ? 270 ASP   A CA  1 
ATOM   1700 C  C   . ASP   A 1 250 ? -11.247 -31.960 5.681   1.00 197.70 ? 270 ASP   A C   1 
ATOM   1701 O  O   . ASP   A 1 250 ? -10.753 -31.322 6.608   1.00 199.37 ? 270 ASP   A O   1 
ATOM   1702 C  CB  . ASP   A 1 250 ? -12.430 -34.144 5.942   1.00 186.65 ? 270 ASP   A CB  1 
ATOM   1703 C  CG  . ASP   A 1 250 ? -12.403 -35.645 5.733   1.00 190.69 ? 270 ASP   A CG  1 
ATOM   1704 O  OD1 . ASP   A 1 250 ? -11.528 -36.129 4.985   1.00 197.26 ? 270 ASP   A OD1 1 
ATOM   1705 O  OD2 . ASP   A 1 250 ? -13.263 -36.341 6.312   1.00 198.47 ? 270 ASP   A OD2 1 
ATOM   1706 N  N   . PHE   A 1 251 ? -11.940 -31.402 4.686   1.00 215.48 ? 271 PHE   A N   1 
ATOM   1707 C  CA  . PHE   A 1 251 ? -12.235 -29.972 4.669   1.00 210.14 ? 271 PHE   A CA  1 
ATOM   1708 C  C   . PHE   A 1 251 ? -12.817 -29.514 6.002   1.00 215.29 ? 271 PHE   A C   1 
ATOM   1709 O  O   . PHE   A 1 251 ? -12.409 -28.487 6.555   1.00 219.33 ? 271 PHE   A O   1 
ATOM   1710 C  CB  . PHE   A 1 251 ? -13.192 -29.674 3.510   1.00 206.17 ? 271 PHE   A CB  1 
ATOM   1711 C  CG  . PHE   A 1 251 ? -13.848 -28.329 3.579   1.00 212.56 ? 271 PHE   A CG  1 
ATOM   1712 C  CD1 . PHE   A 1 251 ? -13.175 -27.191 3.169   1.00 203.06 ? 271 PHE   A CD1 1 
ATOM   1713 C  CD2 . PHE   A 1 251 ? -15.153 -28.206 4.028   1.00 208.11 ? 271 PHE   A CD2 1 
ATOM   1714 C  CE1 . PHE   A 1 251 ? -13.787 -25.951 3.223   1.00 191.06 ? 271 PHE   A CE1 1 
ATOM   1715 C  CE2 . PHE   A 1 251 ? -15.768 -26.971 4.085   1.00 194.03 ? 271 PHE   A CE2 1 
ATOM   1716 C  CZ  . PHE   A 1 251 ? -15.086 -25.843 3.679   1.00 190.20 ? 271 PHE   A CZ  1 
ATOM   1717 N  N   . LEU   A 1 252 ? -13.759 -30.286 6.546   1.00 205.34 ? 272 LEU   A N   1 
ATOM   1718 C  CA  . LEU   A 1 252 ? -14.298 -29.976 7.865   1.00 196.47 ? 272 LEU   A CA  1 
ATOM   1719 C  C   . LEU   A 1 252 ? -13.230 -30.119 8.945   1.00 201.88 ? 272 LEU   A C   1 
ATOM   1720 O  O   . LEU   A 1 252 ? -13.167 -29.309 9.878   1.00 201.76 ? 272 LEU   A O   1 
ATOM   1721 C  CB  . LEU   A 1 252 ? -15.492 -30.882 8.152   1.00 183.40 ? 272 LEU   A CB  1 
ATOM   1722 C  CG  . LEU   A 1 252 ? -16.074 -30.924 9.559   1.00 182.46 ? 272 LEU   A CG  1 
ATOM   1723 C  CD1 . LEU   A 1 252 ? -16.817 -29.640 9.884   1.00 175.31 ? 272 LEU   A CD1 1 
ATOM   1724 C  CD2 . LEU   A 1 252 ? -16.991 -32.121 9.639   1.00 184.03 ? 272 LEU   A CD2 1 
ATOM   1725 N  N   . GLN   A 1 253 ? -12.380 -31.143 8.831   1.00 198.76 ? 273 GLN   A N   1 
ATOM   1726 C  CA  . GLN   A 1 253 ? -11.272 -31.304 9.769   1.00 202.26 ? 273 GLN   A CA  1 
ATOM   1727 C  C   . GLN   A 1 253 ? -10.313 -30.122 9.688   1.00 200.53 ? 273 GLN   A C   1 
ATOM   1728 O  O   . GLN   A 1 253 ? -10.049 -29.456 10.693  1.00 205.39 ? 273 GLN   A O   1 
ATOM   1729 C  CB  . GLN   A 1 253 ? -10.542 -32.616 9.489   1.00 201.34 ? 273 GLN   A CB  1 
ATOM   1730 C  CG  . GLN   A 1 253 ? -9.370  -32.894 10.402  1.00 208.67 ? 273 GLN   A CG  1 
ATOM   1731 C  CD  . GLN   A 1 253 ? -9.748  -33.777 11.571  1.00 220.46 ? 273 GLN   A CD  1 
ATOM   1732 O  OE1 . GLN   A 1 253 ? -9.631  -34.999 11.498  1.00 220.09 ? 273 GLN   A OE1 1 
ATOM   1733 N  NE2 . GLN   A 1 253 ? -10.205 -33.164 12.657  1.00 220.52 ? 273 GLN   A NE2 1 
ATOM   1734 N  N   . LEU   A 1 254 ? -9.810  -29.826 8.487   1.00 206.25 ? 274 LEU   A N   1 
ATOM   1735 C  CA  . LEU   A 1 254 ? -8.857  -28.744 8.260   1.00 202.36 ? 274 LEU   A CA  1 
ATOM   1736 C  C   . LEU   A 1 254 ? -9.391  -27.357 8.630   1.00 205.21 ? 274 LEU   A C   1 
ATOM   1737 O  O   . LEU   A 1 254 ? -8.617  -26.399 8.533   1.00 202.50 ? 274 LEU   A O   1 
ATOM   1738 C  CB  . LEU   A 1 254 ? -8.408  -28.744 6.792   1.00 189.70 ? 274 LEU   A CB  1 
ATOM   1739 C  CG  . LEU   A 1 254 ? -7.987  -30.087 6.188   1.00 189.18 ? 274 LEU   A CG  1 
ATOM   1740 C  CD1 . LEU   A 1 254 ? -7.740  -29.946 4.698   1.00 179.90 ? 274 LEU   A CD1 1 
ATOM   1741 C  CD2 . LEU   A 1 254 ? -6.767  -30.649 6.902   1.00 177.58 ? 274 LEU   A CD2 1 
ATOM   1742 N  N   . MET   A 1 255 ? -10.656 -27.204 9.036   1.00 203.99 ? 275 MET   A N   1 
ATOM   1743 C  CA  . MET   A 1 255 ? -11.166 -25.885 9.403   1.00 207.17 ? 275 MET   A CA  1 
ATOM   1744 C  C   . MET   A 1 255 ? -11.055 -25.620 10.900  1.00 217.09 ? 275 MET   A C   1 
ATOM   1745 O  O   . MET   A 1 255 ? -10.554 -24.567 11.306  1.00 220.67 ? 275 MET   A O   1 
ATOM   1746 C  CB  . MET   A 1 255 ? -12.623 -25.719 8.952   1.00 201.15 ? 275 MET   A CB  1 
ATOM   1747 C  CG  . MET   A 1 255 ? -12.784 -25.481 7.459   1.00 194.68 ? 275 MET   A CG  1 
ATOM   1748 S  SD  . MET   A 1 255 ? -14.495 -25.239 6.948   1.00 171.40 ? 275 MET   A SD  1 
ATOM   1749 C  CE  . MET   A 1 255 ? -14.603 -23.455 6.968   1.00 167.63 ? 275 MET   A CE  1 
ATOM   1750 N  N   . ILE   A 1 256 ? -11.550 -26.542 11.732  1.00 232.48 ? 276 ILE   A N   1 
ATOM   1751 C  CA  . ILE   A 1 256 ? -11.365 -26.403 13.171  1.00 239.15 ? 276 ILE   A CA  1 
ATOM   1752 C  C   . ILE   A 1 256 ? -9.903  -26.577 13.558  1.00 241.71 ? 276 ILE   A C   1 
ATOM   1753 O  O   . ILE   A 1 256 ? -9.472  -26.057 14.594  1.00 239.59 ? 276 ILE   A O   1 
ATOM   1754 C  CB  . ILE   A 1 256 ? -12.242 -27.408 13.935  1.00 237.05 ? 276 ILE   A CB  1 
ATOM   1755 C  CG1 . ILE   A 1 256 ? -13.506 -27.745 13.142  1.00 227.24 ? 276 ILE   A CG1 1 
ATOM   1756 C  CG2 . ILE   A 1 256 ? -12.609 -26.849 15.296  1.00 231.93 ? 276 ILE   A CG2 1 
ATOM   1757 C  CD1 . ILE   A 1 256 ? -14.380 -28.776 13.814  1.00 220.03 ? 276 ILE   A CD1 1 
ATOM   1758 N  N   . ASP   A 1 257 ? -9.124  -27.302 12.750  1.00 224.07 ? 277 ASP   A N   1 
ATOM   1759 C  CA  . ASP   A 1 257 ? -7.701  -27.449 13.037  1.00 222.80 ? 277 ASP   A CA  1 
ATOM   1760 C  C   . ASP   A 1 257 ? -6.949  -26.145 12.816  1.00 219.61 ? 277 ASP   A C   1 
ATOM   1761 O  O   . ASP   A 1 257 ? -5.956  -25.883 13.504  1.00 218.35 ? 277 ASP   A O   1 
ATOM   1762 C  CB  . ASP   A 1 257 ? -7.096  -28.559 12.177  1.00 218.20 ? 277 ASP   A CB  1 
ATOM   1763 C  CG  . ASP   A 1 257 ? -7.735  -29.908 12.431  1.00 218.98 ? 277 ASP   A CG  1 
ATOM   1764 O  OD1 . ASP   A 1 257 ? -8.707  -29.964 13.213  1.00 226.04 ? 277 ASP   A OD1 1 
ATOM   1765 O  OD2 . ASP   A 1 257 ? -7.273  -30.908 11.844  1.00 218.42 ? 277 ASP   A OD2 1 
ATOM   1766 N  N   . SER   A 1 258 ? -7.388  -25.329 11.861  1.00 218.73 ? 278 SER   A N   1 
ATOM   1767 C  CA  . SER   A 1 258 ? -6.813  -24.009 11.645  1.00 214.48 ? 278 SER   A CA  1 
ATOM   1768 C  C   . SER   A 1 258 ? -7.579  -22.916 12.379  1.00 217.97 ? 278 SER   A C   1 
ATOM   1769 O  O   . SER   A 1 258 ? -7.287  -21.731 12.188  1.00 210.25 ? 278 SER   A O   1 
ATOM   1770 C  CB  . SER   A 1 258 ? -6.748  -23.701 10.146  1.00 203.46 ? 278 SER   A CB  1 
ATOM   1771 O  OG  . SER   A 1 258 ? -7.830  -24.296 9.452   1.00 196.67 ? 278 SER   A OG  1 
ATOM   1772 N  N   . GLN   A 1 259 ? -8.549  -23.289 13.209  1.00 224.67 ? 279 GLN   A N   1 
ATOM   1773 C  CA  . GLN   A 1 259 ? -9.251  -22.342 14.064  1.00 219.59 ? 279 GLN   A CA  1 
ATOM   1774 C  C   . GLN   A 1 259 ? -8.551  -22.228 15.415  1.00 221.44 ? 279 GLN   A C   1 
ATOM   1775 O  O   . GLN   A 1 259 ? -8.037  -21.170 15.774  1.00 217.57 ? 279 GLN   A O   1 
ATOM   1776 C  CB  . GLN   A 1 259 ? -10.707 -22.765 14.264  1.00 213.82 ? 279 GLN   A CB  1 
ATOM   1777 C  CG  . GLN   A 1 259 ? -11.361 -22.144 15.488  1.00 217.21 ? 279 GLN   A CG  1 
ATOM   1778 C  CD  . GLN   A 1 259 ? -12.713 -22.751 15.805  1.00 210.40 ? 279 GLN   A CD  1 
ATOM   1779 O  OE1 . GLN   A 1 259 ? -13.455 -23.151 14.908  1.00 201.85 ? 279 GLN   A OE1 1 
ATOM   1780 N  NE2 . GLN   A 1 259 ? -13.038 -22.828 17.091  1.00 208.54 ? 279 GLN   A NE2 1 
ATOM   1781 N  N   . LYS   A 1 268 ? -8.520  -13.499 14.069  1.00 203.09 ? 288 LYS   A N   1 
ATOM   1782 C  CA  . LYS   A 1 268 ? -7.717  -13.648 12.861  1.00 198.99 ? 288 LYS   A CA  1 
ATOM   1783 C  C   . LYS   A 1 268 ? -7.633  -15.123 12.475  1.00 195.35 ? 288 LYS   A C   1 
ATOM   1784 O  O   . LYS   A 1 268 ? -6.948  -15.496 11.521  1.00 189.30 ? 288 LYS   A O   1 
ATOM   1785 C  CB  . LYS   A 1 268 ? -6.322  -13.054 13.067  1.00 198.92 ? 288 LYS   A CB  1 
ATOM   1786 C  CG  . LYS   A 1 268 ? -5.621  -12.642 11.783  1.00 194.18 ? 288 LYS   A CG  1 
ATOM   1787 C  CD  . LYS   A 1 268 ? -4.223  -12.124 12.068  1.00 199.32 ? 288 LYS   A CD  1 
ATOM   1788 C  CE  . LYS   A 1 268 ? -3.446  -11.900 10.784  1.00 196.51 ? 288 LYS   A CE  1 
ATOM   1789 N  NZ  . LYS   A 1 268 ? -2.021  -11.567 11.056  1.00 180.95 ? 288 LYS   A NZ  1 
ATOM   1790 N  N   . ALA   A 1 269 ? -8.332  -15.957 13.236  1.00 195.73 ? 289 ALA   A N   1 
ATOM   1791 C  CA  . ALA   A 1 269 ? -8.537  -17.355 12.902  1.00 189.64 ? 289 ALA   A CA  1 
ATOM   1792 C  C   . ALA   A 1 269 ? -9.959  -17.523 12.360  1.00 189.66 ? 289 ALA   A C   1 
ATOM   1793 O  O   . ALA   A 1 269 ? -10.616 -16.542 11.996  1.00 193.96 ? 289 ALA   A O   1 
ATOM   1794 C  CB  . ALA   A 1 269 ? -8.255  -18.228 14.130  1.00 196.44 ? 289 ALA   A CB  1 
ATOM   1795 N  N   . LEU   A 1 270 ? -10.449 -18.758 12.316  1.00 179.00 ? 290 LEU   A N   1 
ATOM   1796 C  CA  . LEU   A 1 270 ? -11.733 -19.061 11.701  1.00 169.06 ? 290 LEU   A CA  1 
ATOM   1797 C  C   . LEU   A 1 270 ? -12.840 -19.154 12.747  1.00 174.03 ? 290 LEU   A C   1 
ATOM   1798 O  O   . LEU   A 1 270 ? -12.615 -19.576 13.884  1.00 184.89 ? 290 LEU   A O   1 
ATOM   1799 C  CB  . LEU   A 1 270 ? -11.656 -20.368 10.909  1.00 167.72 ? 290 LEU   A CB  1 
ATOM   1800 C  CG  . LEU   A 1 270 ? -12.950 -20.859 10.256  1.00 164.13 ? 290 LEU   A CG  1 
ATOM   1801 C  CD1 . LEU   A 1 270 ? -13.413 -19.916 9.149   1.00 154.58 ? 290 LEU   A CD1 1 
ATOM   1802 C  CD2 . LEU   A 1 270 ? -12.783 -22.272 9.740   1.00 169.78 ? 290 LEU   A CD2 1 
ATOM   1803 N  N   . SER   A 1 271 ? -14.047 -18.760 12.340  1.00 162.89 ? 291 SER   A N   1 
ATOM   1804 C  CA  . SER   A 1 271 ? -15.239 -18.798 13.169  1.00 161.96 ? 291 SER   A CA  1 
ATOM   1805 C  C   . SER   A 1 271 ? -16.042 -20.070 12.887  1.00 161.63 ? 291 SER   A C   1 
ATOM   1806 O  O   . SER   A 1 271 ? -15.597 -20.967 12.165  1.00 156.21 ? 291 SER   A O   1 
ATOM   1807 C  CB  . SER   A 1 271 ? -16.075 -17.541 12.927  1.00 156.58 ? 291 SER   A CB  1 
ATOM   1808 O  OG  . SER   A 1 271 ? -17.392 -17.709 13.419  1.00 154.04 ? 291 SER   A OG  1 
ATOM   1809 N  N   . ASP   A 1 272 ? -17.250 -20.146 13.449  1.00 158.17 ? 292 ASP   A N   1 
ATOM   1810 C  CA  . ASP   A 1 272 ? -18.110 -21.321 13.338  1.00 159.79 ? 292 ASP   A CA  1 
ATOM   1811 C  C   . ASP   A 1 272 ? -19.299 -21.117 12.412  1.00 153.01 ? 292 ASP   A C   1 
ATOM   1812 O  O   . ASP   A 1 272 ? -19.527 -21.936 11.517  1.00 149.66 ? 292 ASP   A O   1 
ATOM   1813 C  CB  . ASP   A 1 272 ? -18.608 -21.740 14.727  1.00 163.81 ? 292 ASP   A CB  1 
ATOM   1814 C  CG  . ASP   A 1 272 ? -17.510 -22.322 15.585  1.00 171.57 ? 292 ASP   A CG  1 
ATOM   1815 O  OD1 . ASP   A 1 272 ? -16.358 -22.386 15.102  1.00 168.53 ? 292 ASP   A OD1 1 
ATOM   1816 O  OD2 . ASP   A 1 272 ? -17.795 -22.719 16.735  1.00 177.59 ? 292 ASP   A OD2 1 
ATOM   1817 N  N   . LEU   A 1 273 ? -20.085 -20.057 12.611  1.00 156.30 ? 293 LEU   A N   1 
ATOM   1818 C  CA  . LEU   A 1 273 ? -21.115 -19.737 11.629  1.00 155.76 ? 293 LEU   A CA  1 
ATOM   1819 C  C   . LEU   A 1 273 ? -20.494 -19.404 10.281  1.00 153.77 ? 293 LEU   A C   1 
ATOM   1820 O  O   . LEU   A 1 273 ? -21.129 -19.596 9.237   1.00 153.14 ? 293 LEU   A O   1 
ATOM   1821 C  CB  . LEU   A 1 273 ? -21.988 -18.578 12.117  1.00 163.98 ? 293 LEU   A CB  1 
ATOM   1822 C  CG  . LEU   A 1 273 ? -23.162 -18.173 11.219  1.00 177.18 ? 293 LEU   A CG  1 
ATOM   1823 C  CD1 . LEU   A 1 273 ? -24.007 -19.386 10.858  1.00 177.77 ? 293 LEU   A CD1 1 
ATOM   1824 C  CD2 . LEU   A 1 273 ? -24.016 -17.101 11.881  1.00 178.87 ? 293 LEU   A CD2 1 
ATOM   1825 N  N   . GLU   A 1 274 ? -19.253 -18.914 10.281  1.00 151.09 ? 294 GLU   A N   1 
ATOM   1826 C  CA  . GLU   A 1 274 ? -18.516 -18.782 9.033   1.00 145.10 ? 294 GLU   A CA  1 
ATOM   1827 C  C   . GLU   A 1 274 ? -18.080 -20.140 8.499   1.00 138.04 ? 294 GLU   A C   1 
ATOM   1828 O  O   . GLU   A 1 274 ? -17.942 -20.308 7.283   1.00 134.12 ? 294 GLU   A O   1 
ATOM   1829 C  CB  . GLU   A 1 274 ? -17.305 -17.873 9.231   1.00 149.94 ? 294 GLU   A CB  1 
ATOM   1830 C  CG  . GLU   A 1 274 ? -17.662 -16.456 9.635   1.00 155.10 ? 294 GLU   A CG  1 
ATOM   1831 C  CD  . GLU   A 1 274 ? -16.453 -15.548 9.699   1.00 158.13 ? 294 GLU   A CD  1 
ATOM   1832 O  OE1 . GLU   A 1 274 ? -15.351 -16.041 10.023  1.00 153.26 ? 294 GLU   A OE1 1 
ATOM   1833 O  OE2 . GLU   A 1 274 ? -16.606 -14.341 9.420   1.00 155.46 ? 294 GLU   A OE2 1 
ATOM   1834 N  N   . LEU   A 1 275 ? -17.857 -21.113 9.388   1.00 144.61 ? 295 LEU   A N   1 
ATOM   1835 C  CA  . LEU   A 1 275 ? -17.522 -22.465 8.946   1.00 145.40 ? 295 LEU   A CA  1 
ATOM   1836 C  C   . LEU   A 1 275 ? -18.691 -23.100 8.205   1.00 139.76 ? 295 LEU   A C   1 
ATOM   1837 O  O   . LEU   A 1 275 ? -18.492 -23.821 7.220   1.00 136.75 ? 295 LEU   A O   1 
ATOM   1838 C  CB  . LEU   A 1 275 ? -17.107 -23.323 10.147  1.00 151.62 ? 295 LEU   A CB  1 
ATOM   1839 C  CG  . LEU   A 1 275 ? -16.465 -24.703 9.935   1.00 153.50 ? 295 LEU   A CG  1 
ATOM   1840 C  CD1 . LEU   A 1 275 ? -15.578 -25.057 11.121  1.00 170.73 ? 295 LEU   A CD1 1 
ATOM   1841 C  CD2 . LEU   A 1 275 ? -17.494 -25.809 9.707   1.00 152.43 ? 295 LEU   A CD2 1 
ATOM   1842 N  N   . VAL   A 1 276 ? -19.915 -22.847 8.670   1.00 142.38 ? 296 VAL   A N   1 
ATOM   1843 C  CA  . VAL   A 1 276 ? -21.098 -23.380 7.999   1.00 141.98 ? 296 VAL   A CA  1 
ATOM   1844 C  C   . VAL   A 1 276 ? -21.190 -22.835 6.580   1.00 136.94 ? 296 VAL   A C   1 
ATOM   1845 O  O   . VAL   A 1 276 ? -21.440 -23.578 5.623   1.00 135.70 ? 296 VAL   A O   1 
ATOM   1846 C  CB  . VAL   A 1 276 ? -22.368 -23.048 8.804   1.00 147.12 ? 296 VAL   A CB  1 
ATOM   1847 C  CG1 . VAL   A 1 276 ? -23.612 -23.478 8.041   1.00 161.36 ? 296 VAL   A CG1 1 
ATOM   1848 C  CG2 . VAL   A 1 276 ? -22.316 -23.704 10.172  1.00 166.05 ? 296 VAL   A CG2 1 
ATOM   1849 N  N   . ALA   A 1 277 ? -20.985 -21.524 6.428   1.00 136.04 ? 297 ALA   A N   1 
ATOM   1850 C  CA  . ALA   A 1 277 ? -21.157 -20.887 5.126   1.00 132.03 ? 297 ALA   A CA  1 
ATOM   1851 C  C   . ALA   A 1 277 ? -20.208 -21.474 4.088   1.00 122.83 ? 297 ALA   A C   1 
ATOM   1852 O  O   . ALA   A 1 277 ? -20.592 -21.670 2.929   1.00 121.90 ? 297 ALA   A O   1 
ATOM   1853 C  CB  . ALA   A 1 277 ? -20.951 -19.377 5.253   1.00 134.80 ? 297 ALA   A CB  1 
ATOM   1854 N  N   . GLN   A 1 278 ? -18.967 -21.767 4.486   1.00 120.39 ? 298 GLN   A N   1 
ATOM   1855 C  CA  . GLN   A 1 278 ? -18.014 -22.367 3.556   1.00 124.90 ? 298 GLN   A CA  1 
ATOM   1856 C  C   . GLN   A 1 278 ? -18.439 -23.775 3.161   1.00 123.64 ? 298 GLN   A C   1 
ATOM   1857 O  O   . GLN   A 1 278 ? -18.232 -24.193 2.016   1.00 128.96 ? 298 GLN   A O   1 
ATOM   1858 C  CB  . GLN   A 1 278 ? -16.616 -22.387 4.171   1.00 129.77 ? 298 GLN   A CB  1 
ATOM   1859 C  CG  . GLN   A 1 278 ? -16.185 -21.072 4.798   1.00 128.46 ? 298 GLN   A CG  1 
ATOM   1860 C  CD  . GLN   A 1 278 ? -16.138 -19.934 3.802   1.00 128.31 ? 298 GLN   A CD  1 
ATOM   1861 O  OE1 . GLN   A 1 278 ? -15.907 -20.144 2.613   1.00 128.82 ? 298 GLN   A OE1 1 
ATOM   1862 N  NE2 . GLN   A 1 278 ? -16.361 -18.716 4.284   1.00 127.39 ? 298 GLN   A NE2 1 
ATOM   1863 N  N   . SER   A 1 279 ? -19.032 -24.520 4.098   1.00 129.02 ? 299 SER   A N   1 
ATOM   1864 C  CA  . SER   A 1 279 ? -19.547 -25.847 3.777   1.00 132.43 ? 299 SER   A CA  1 
ATOM   1865 C  C   . SER   A 1 279 ? -20.648 -25.768 2.725   1.00 126.45 ? 299 SER   A C   1 
ATOM   1866 O  O   . SER   A 1 279 ? -20.713 -26.606 1.817   1.00 133.55 ? 299 SER   A O   1 
ATOM   1867 C  CB  . SER   A 1 279 ? -20.067 -26.525 5.046   1.00 136.76 ? 299 SER   A CB  1 
ATOM   1868 O  OG  . SER   A 1 279 ? -19.154 -26.390 6.124   1.00 143.30 ? 299 SER   A OG  1 
ATOM   1869 N  N   . ILE   A 1 280 ? -21.519 -24.758 2.827   1.00 120.34 ? 300 ILE   A N   1 
ATOM   1870 C  CA  . ILE   A 1 280 ? -22.616 -24.606 1.873   1.00 118.98 ? 300 ILE   A CA  1 
ATOM   1871 C  C   . ILE   A 1 280 ? -22.075 -24.318 0.478   1.00 118.76 ? 300 ILE   A C   1 
ATOM   1872 O  O   . ILE   A 1 280 ? -22.572 -24.857 -0.520  1.00 121.67 ? 300 ILE   A O   1 
ATOM   1873 C  CB  . ILE   A 1 280 ? -23.583 -23.505 2.350   1.00 117.75 ? 300 ILE   A CB  1 
ATOM   1874 C  CG1 . ILE   A 1 280 ? -24.132 -23.841 3.737   1.00 121.11 ? 300 ILE   A CG1 1 
ATOM   1875 C  CG2 . ILE   A 1 280 ? -24.725 -23.310 1.357   1.00 118.11 ? 300 ILE   A CG2 1 
ATOM   1876 C  CD1 . ILE   A 1 280 ? -25.081 -22.798 4.288   1.00 127.79 ? 300 ILE   A CD1 1 
ATOM   1877 N  N   . ILE   A 1 281 ? -21.051 -23.466 0.385   1.00 122.57 ? 301 ILE   A N   1 
ATOM   1878 C  CA  . ILE   A 1 281 ? -20.443 -23.163 -0.911  1.00 125.12 ? 301 ILE   A CA  1 
ATOM   1879 C  C   . ILE   A 1 281 ? -19.846 -24.422 -1.525  1.00 130.77 ? 301 ILE   A C   1 
ATOM   1880 O  O   . ILE   A 1 281 ? -20.088 -24.741 -2.696  1.00 127.51 ? 301 ILE   A O   1 
ATOM   1881 C  CB  . ILE   A 1 281 ? -19.384 -22.055 -0.763  1.00 118.06 ? 301 ILE   A CB  1 
ATOM   1882 C  CG1 . ILE   A 1 281 ? -20.045 -20.703 -0.493  1.00 115.59 ? 301 ILE   A CG1 1 
ATOM   1883 C  CG2 . ILE   A 1 281 ? -18.505 -21.979 -2.006  1.00 116.35 ? 301 ILE   A CG2 1 
ATOM   1884 C  CD1 . ILE   A 1 281 ? -20.911 -20.207 -1.627  1.00 114.94 ? 301 ILE   A CD1 1 
ATOM   1885 N  N   . PHE   A 1 282 ? -19.053 -25.156 -0.741  1.00 133.06 ? 302 PHE   A N   1 
ATOM   1886 C  CA  . PHE   A 1 282 ? -18.394 -26.354 -1.255  1.00 134.19 ? 302 PHE   A CA  1 
ATOM   1887 C  C   . PHE   A 1 282 ? -19.405 -27.424 -1.647  1.00 132.91 ? 302 PHE   A C   1 
ATOM   1888 O  O   . PHE   A 1 282 ? -19.219 -28.128 -2.646  1.00 133.92 ? 302 PHE   A O   1 
ATOM   1889 C  CB  . PHE   A 1 282 ? -17.416 -26.899 -0.212  1.00 137.49 ? 302 PHE   A CB  1 
ATOM   1890 C  CG  . PHE   A 1 282 ? -16.097 -26.180 -0.177  1.00 148.62 ? 302 PHE   A CG  1 
ATOM   1891 C  CD1 . PHE   A 1 282 ? -16.044 -24.798 -0.089  1.00 146.41 ? 302 PHE   A CD1 1 
ATOM   1892 C  CD2 . PHE   A 1 282 ? -14.908 -26.890 -0.216  1.00 158.86 ? 302 PHE   A CD2 1 
ATOM   1893 C  CE1 . PHE   A 1 282 ? -14.833 -24.137 -0.054  1.00 143.03 ? 302 PHE   A CE1 1 
ATOM   1894 C  CE2 . PHE   A 1 282 ? -13.692 -26.235 -0.179  1.00 158.99 ? 302 PHE   A CE2 1 
ATOM   1895 C  CZ  . PHE   A 1 282 ? -13.654 -24.858 -0.099  1.00 152.76 ? 302 PHE   A CZ  1 
ATOM   1896 N  N   . ILE   A 1 283 ? -20.483 -27.561 -0.871  1.00 127.67 ? 303 ILE   A N   1 
ATOM   1897 C  CA  . ILE   A 1 283 ? -21.472 -28.600 -1.144  1.00 127.74 ? 303 ILE   A CA  1 
ATOM   1898 C  C   . ILE   A 1 283 ? -22.207 -28.316 -2.451  1.00 130.19 ? 303 ILE   A C   1 
ATOM   1899 O  O   . ILE   A 1 283 ? -22.456 -29.231 -3.246  1.00 133.83 ? 303 ILE   A O   1 
ATOM   1900 C  CB  . ILE   A 1 283 ? -22.439 -28.737 0.048   1.00 129.58 ? 303 ILE   A CB  1 
ATOM   1901 C  CG1 . ILE   A 1 283 ? -21.768 -29.500 1.194   1.00 131.25 ? 303 ILE   A CG1 1 
ATOM   1902 C  CG2 . ILE   A 1 283 ? -23.724 -29.439 -0.362  1.00 135.04 ? 303 ILE   A CG2 1 
ATOM   1903 C  CD1 . ILE   A 1 283 ? -22.520 -29.416 2.512   1.00 124.46 ? 303 ILE   A CD1 1 
ATOM   1904 N  N   . PHE   A 1 284 ? -22.554 -27.052 -2.702  1.00 125.15 ? 304 PHE   A N   1 
ATOM   1905 C  CA  . PHE   A 1 284 ? -23.199 -26.699 -3.963  1.00 129.22 ? 304 PHE   A CA  1 
ATOM   1906 C  C   . PHE   A 1 284 ? -22.281 -26.985 -5.146  1.00 127.88 ? 304 PHE   A C   1 
ATOM   1907 O  O   . PHE   A 1 284 ? -22.652 -27.705 -6.080  1.00 133.59 ? 304 PHE   A O   1 
ATOM   1908 C  CB  . PHE   A 1 284 ? -23.620 -25.227 -3.954  1.00 125.16 ? 304 PHE   A CB  1 
ATOM   1909 C  CG  . PHE   A 1 284 ? -24.127 -24.738 -5.283  1.00 127.68 ? 304 PHE   A CG  1 
ATOM   1910 C  CD1 . PHE   A 1 284 ? -25.473 -24.828 -5.602  1.00 124.06 ? 304 PHE   A CD1 1 
ATOM   1911 C  CD2 . PHE   A 1 284 ? -23.254 -24.199 -6.218  1.00 129.98 ? 304 PHE   A CD2 1 
ATOM   1912 C  CE1 . PHE   A 1 284 ? -25.940 -24.383 -6.826  1.00 127.45 ? 304 PHE   A CE1 1 
ATOM   1913 C  CE2 . PHE   A 1 284 ? -23.709 -23.757 -7.444  1.00 121.32 ? 304 PHE   A CE2 1 
ATOM   1914 C  CZ  . PHE   A 1 284 ? -25.056 -23.848 -7.750  1.00 127.31 ? 304 PHE   A CZ  1 
ATOM   1915 N  N   . ALA   A 1 285 ? -21.071 -26.418 -5.116  1.00 127.84 ? 305 ALA   A N   1 
ATOM   1916 C  CA  . ALA   A 1 285 ? -20.132 -26.538 -6.227  1.00 129.02 ? 305 ALA   A CA  1 
ATOM   1917 C  C   . ALA   A 1 285 ? -19.867 -27.995 -6.589  1.00 133.47 ? 305 ALA   A C   1 
ATOM   1918 O  O   . ALA   A 1 285 ? -20.050 -28.410 -7.738  1.00 141.13 ? 305 ALA   A O   1 
ATOM   1919 C  CB  . ALA   A 1 285 ? -18.824 -25.831 -5.872  1.00 127.15 ? 305 ALA   A CB  1 
ATOM   1920 N  N   . GLY   A 1 286 ? -19.437 -28.790 -5.609  1.00 130.72 ? 306 GLY   A N   1 
ATOM   1921 C  CA  . GLY   A 1 286 ? -19.149 -30.187 -5.869  1.00 136.42 ? 306 GLY   A CA  1 
ATOM   1922 C  C   . GLY   A 1 286 ? -20.343 -30.991 -6.345  1.00 142.17 ? 306 GLY   A C   1 
ATOM   1923 O  O   . GLY   A 1 286 ? -20.161 -32.091 -6.875  1.00 141.45 ? 306 GLY   A O   1 
ATOM   1924 N  N   . TYR   A 1 287 ? -21.559 -30.476 -6.167  1.00 152.42 ? 307 TYR   A N   1 
ATOM   1925 C  CA  . TYR   A 1 287 ? -22.751 -31.157 -6.679  1.00 151.98 ? 307 TYR   A CA  1 
ATOM   1926 C  C   . TYR   A 1 287 ? -23.101 -30.651 -8.075  1.00 147.71 ? 307 TYR   A C   1 
ATOM   1927 O  O   . TYR   A 1 287 ? -23.016 -31.395 -9.056  1.00 154.58 ? 307 TYR   A O   1 
ATOM   1928 C  CB  . TYR   A 1 287 ? -23.936 -30.982 -5.724  1.00 155.70 ? 307 TYR   A CB  1 
ATOM   1929 C  CG  . TYR   A 1 287 ? -25.255 -31.389 -6.348  1.00 161.30 ? 307 TYR   A CG  1 
ATOM   1930 C  CD1 . TYR   A 1 287 ? -25.617 -32.726 -6.441  1.00 170.53 ? 307 TYR   A CD1 1 
ATOM   1931 C  CD2 . TYR   A 1 287 ? -26.131 -30.437 -6.863  1.00 166.77 ? 307 TYR   A CD2 1 
ATOM   1932 C  CE1 . TYR   A 1 287 ? -26.815 -33.106 -7.021  1.00 179.41 ? 307 TYR   A CE1 1 
ATOM   1933 C  CE2 . TYR   A 1 287 ? -27.330 -30.809 -7.449  1.00 173.58 ? 307 TYR   A CE2 1 
ATOM   1934 C  CZ  . TYR   A 1 287 ? -27.667 -32.145 -7.523  1.00 177.33 ? 307 TYR   A CZ  1 
ATOM   1935 O  OH  . TYR   A 1 287 ? -28.858 -32.525 -8.099  1.00 177.76 ? 307 TYR   A OH  1 
ATOM   1936 N  N   . GLU   A 1 288 ? -23.491 -29.377 -8.172  1.00 134.99 ? 308 GLU   A N   1 
ATOM   1937 C  CA  . GLU   A 1 288 ? -24.085 -28.875 -9.407  1.00 134.47 ? 308 GLU   A CA  1 
ATOM   1938 C  C   . GLU   A 1 288 ? -23.054 -28.763 -10.525 1.00 132.55 ? 308 GLU   A C   1 
ATOM   1939 O  O   . GLU   A 1 288 ? -23.318 -29.178 -11.659 1.00 136.84 ? 308 GLU   A O   1 
ATOM   1940 C  CB  . GLU   A 1 288 ? -24.759 -27.527 -9.148  1.00 135.13 ? 308 GLU   A CB  1 
ATOM   1941 C  CG  . GLU   A 1 288 ? -26.111 -27.350 -9.837  1.00 135.23 ? 308 GLU   A CG  1 
ATOM   1942 C  CD  . GLU   A 1 288 ? -25.999 -27.258 -11.348 1.00 135.02 ? 308 GLU   A CD  1 
ATOM   1943 O  OE1 . GLU   A 1 288 ? -24.945 -26.803 -11.838 1.00 123.87 ? 308 GLU   A OE1 1 
ATOM   1944 O  OE2 . GLU   A 1 288 ? -26.964 -27.640 -12.045 1.00 139.56 ? 308 GLU   A OE2 1 
ATOM   1945 N  N   . THR   A 1 289 ? -21.876 -28.205 -10.230 1.00 125.01 ? 309 THR   A N   1 
ATOM   1946 C  CA  . THR   A 1 289 ? -20.852 -28.063 -11.263 1.00 124.16 ? 309 THR   A CA  1 
ATOM   1947 C  C   . THR   A 1 289 ? -20.369 -29.423 -11.754 1.00 123.13 ? 309 THR   A C   1 
ATOM   1948 O  O   . THR   A 1 289 ? -20.196 -29.628 -12.961 1.00 116.18 ? 309 THR   A O   1 
ATOM   1949 C  CB  . THR   A 1 289 ? -19.672 -27.243 -10.739 1.00 119.96 ? 309 THR   A CB  1 
ATOM   1950 O  OG1 . THR   A 1 289 ? -18.822 -28.074 -9.939  1.00 130.18 ? 309 THR   A OG1 1 
ATOM   1951 C  CG2 . THR   A 1 289 ? -20.169 -26.071 -9.901  1.00 114.71 ? 309 THR   A CG2 1 
ATOM   1952 N  N   . THR   A 1 290 ? -20.151 -30.364 -10.833 1.00 134.20 ? 310 THR   A N   1 
ATOM   1953 C  CA  . THR   A 1 290 ? -19.696 -31.696 -11.222 1.00 134.58 ? 310 THR   A CA  1 
ATOM   1954 C  C   . THR   A 1 290 ? -20.748 -32.418 -12.057 1.00 131.16 ? 310 THR   A C   1 
ATOM   1955 O  O   . THR   A 1 290 ? -20.432 -33.007 -13.096 1.00 126.58 ? 310 THR   A O   1 
ATOM   1956 C  CB  . THR   A 1 290 ? -19.341 -32.514 -9.980  1.00 136.22 ? 310 THR   A CB  1 
ATOM   1957 O  OG1 . THR   A 1 290 ? -18.275 -31.873 -9.267  1.00 129.56 ? 310 THR   A OG1 1 
ATOM   1958 C  CG2 . THR   A 1 290 ? -18.909 -33.918 -10.371 1.00 138.26 ? 310 THR   A CG2 1 
ATOM   1959 N  N   . SER   A 1 291 ? -22.010 -32.380 -11.623 1.00 137.21 ? 311 SER   A N   1 
ATOM   1960 C  CA  . SER   A 1 291 ? -23.055 -33.106 -12.339 1.00 136.75 ? 311 SER   A CA  1 
ATOM   1961 C  C   . SER   A 1 291 ? -23.346 -32.468 -13.693 1.00 132.83 ? 311 SER   A C   1 
ATOM   1962 O  O   . SER   A 1 291 ? -23.448 -33.166 -14.709 1.00 132.95 ? 311 SER   A O   1 
ATOM   1963 C  CB  . SER   A 1 291 ? -24.328 -33.163 -11.498 1.00 141.10 ? 311 SER   A CB  1 
ATOM   1964 O  OG  . SER   A 1 291 ? -24.961 -31.897 -11.465 1.00 135.19 ? 311 SER   A OG  1 
ATOM   1965 N  N   . SER   A 1 292 ? -23.493 -31.139 -13.721 1.00 126.23 ? 312 SER   A N   1 
ATOM   1966 C  CA  . SER   A 1 292 ? -23.884 -30.454 -14.952 1.00 124.83 ? 312 SER   A CA  1 
ATOM   1967 C  C   . SER   A 1 292 ? -22.861 -30.660 -16.058 1.00 123.53 ? 312 SER   A C   1 
ATOM   1968 O  O   . SER   A 1 292 ? -23.227 -30.903 -17.214 1.00 119.73 ? 312 SER   A O   1 
ATOM   1969 C  CB  . SER   A 1 292 ? -24.076 -28.961 -14.692 1.00 117.97 ? 312 SER   A CB  1 
ATOM   1970 O  OG  . SER   A 1 292 ? -24.428 -28.285 -15.886 1.00 117.79 ? 312 SER   A OG  1 
ATOM   1971 N  N   . VAL   A 1 293 ? -21.575 -30.544 -15.731 1.00 122.14 ? 313 VAL   A N   1 
ATOM   1972 C  CA  . VAL   A 1 293 ? -20.542 -30.732 -16.744 1.00 120.99 ? 313 VAL   A CA  1 
ATOM   1973 C  C   . VAL   A 1 293 ? -20.508 -32.183 -17.205 1.00 120.98 ? 313 VAL   A C   1 
ATOM   1974 O  O   . VAL   A 1 293 ? -20.282 -32.470 -18.387 1.00 124.44 ? 313 VAL   A O   1 
ATOM   1975 C  CB  . VAL   A 1 293 ? -19.178 -30.269 -16.202 1.00 108.13 ? 313 VAL   A CB  1 
ATOM   1976 C  CG1 . VAL   A 1 293 ? -18.074 -30.579 -17.201 1.00 92.98  ? 313 VAL   A CG1 1 
ATOM   1977 C  CG2 . VAL   A 1 293 ? -19.221 -28.781 -15.903 1.00 116.49 ? 313 VAL   A CG2 1 
ATOM   1978 N  N   . LEU   A 1 294 ? -20.750 -33.120 -16.285 1.00 127.76 ? 314 LEU   A N   1 
ATOM   1979 C  CA  . LEU   A 1 294 ? -20.765 -34.531 -16.653 1.00 124.95 ? 314 LEU   A CA  1 
ATOM   1980 C  C   . LEU   A 1 294 ? -21.866 -34.825 -17.666 1.00 125.74 ? 314 LEU   A C   1 
ATOM   1981 O  O   . LEU   A 1 294 ? -21.653 -35.571 -18.629 1.00 127.81 ? 314 LEU   A O   1 
ATOM   1982 C  CB  . LEU   A 1 294 ? -20.921 -35.389 -15.399 1.00 130.90 ? 314 LEU   A CB  1 
ATOM   1983 C  CG  . LEU   A 1 294 ? -19.626 -35.666 -14.628 1.00 125.23 ? 314 LEU   A CG  1 
ATOM   1984 C  CD1 . LEU   A 1 294 ? -19.914 -36.454 -13.361 1.00 125.26 ? 314 LEU   A CD1 1 
ATOM   1985 C  CD2 . LEU   A 1 294 ? -18.620 -36.404 -15.503 1.00 121.11 ? 314 LEU   A CD2 1 
ATOM   1986 N  N   . SER   A 1 295 ? -23.046 -34.230 -17.476 1.00 124.49 ? 315 SER   A N   1 
ATOM   1987 C  CA  . SER   A 1 295 ? -24.103 -34.344 -18.474 1.00 128.35 ? 315 SER   A CA  1 
ATOM   1988 C  C   . SER   A 1 295 ? -23.676 -33.721 -19.797 1.00 124.11 ? 315 SER   A C   1 
ATOM   1989 O  O   . SER   A 1 295 ? -23.992 -34.244 -20.872 1.00 128.09 ? 315 SER   A O   1 
ATOM   1990 C  CB  . SER   A 1 295 ? -25.377 -33.676 -17.959 1.00 135.26 ? 315 SER   A CB  1 
ATOM   1991 O  OG  . SER   A 1 295 ? -25.592 -33.972 -16.590 1.00 137.45 ? 315 SER   A OG  1 
ATOM   1992 N  N   . PHE   A 1 296 ? -22.955 -32.598 -19.732 1.00 117.43 ? 316 PHE   A N   1 
ATOM   1993 C  CA  . PHE   A 1 296 ? -22.473 -31.937 -20.941 1.00 117.83 ? 316 PHE   A CA  1 
ATOM   1994 C  C   . PHE   A 1 296 ? -21.499 -32.825 -21.707 1.00 118.71 ? 316 PHE   A C   1 
ATOM   1995 O  O   . PHE   A 1 296 ? -21.582 -32.941 -22.936 1.00 115.81 ? 316 PHE   A O   1 
ATOM   1996 C  CB  . PHE   A 1 296 ? -21.814 -30.606 -20.576 1.00 116.65 ? 316 PHE   A CB  1 
ATOM   1997 C  CG  . PHE   A 1 296 ? -22.766 -29.446 -20.548 1.00 120.33 ? 316 PHE   A CG  1 
ATOM   1998 C  CD1 . PHE   A 1 296 ? -23.645 -29.237 -21.597 1.00 116.39 ? 316 PHE   A CD1 1 
ATOM   1999 C  CD2 . PHE   A 1 296 ? -22.786 -28.569 -19.473 1.00 118.23 ? 316 PHE   A CD2 1 
ATOM   2000 C  CE1 . PHE   A 1 296 ? -24.524 -28.173 -21.583 1.00 120.81 ? 316 PHE   A CE1 1 
ATOM   2001 C  CE2 . PHE   A 1 296 ? -23.665 -27.499 -19.450 1.00 118.53 ? 316 PHE   A CE2 1 
ATOM   2002 C  CZ  . PHE   A 1 296 ? -24.536 -27.300 -20.508 1.00 124.51 ? 316 PHE   A CZ  1 
ATOM   2003 N  N   . ILE   A 1 297 ? -20.561 -33.455 -20.996 1.00 120.68 ? 317 ILE   A N   1 
ATOM   2004 C  CA  . ILE   A 1 297 ? -19.574 -34.303 -21.659 1.00 118.72 ? 317 ILE   A CA  1 
ATOM   2005 C  C   . ILE   A 1 297 ? -20.250 -35.504 -22.307 1.00 126.47 ? 317 ILE   A C   1 
ATOM   2006 O  O   . ILE   A 1 297 ? -19.952 -35.859 -23.454 1.00 127.98 ? 317 ILE   A O   1 
ATOM   2007 C  CB  . ILE   A 1 297 ? -18.480 -34.740 -20.665 1.00 118.36 ? 317 ILE   A CB  1 
ATOM   2008 C  CG1 . ILE   A 1 297 ? -17.794 -33.522 -20.042 1.00 117.20 ? 317 ILE   A CG1 1 
ATOM   2009 C  CG2 . ILE   A 1 297 ? -17.455 -35.626 -21.362 1.00 114.09 ? 317 ILE   A CG2 1 
ATOM   2010 C  CD1 . ILE   A 1 297 ? -16.727 -33.868 -19.021 1.00 108.81 ? 317 ILE   A CD1 1 
ATOM   2011 N  N   . MET   A 1 298 ? -21.181 -36.141 -21.592 1.00 123.14 ? 318 MET   A N   1 
ATOM   2012 C  CA  . MET   A 1 298 ? -21.814 -37.344 -22.122 1.00 138.32 ? 318 MET   A CA  1 
ATOM   2013 C  C   . MET   A 1 298 ? -22.705 -37.036 -23.318 1.00 139.39 ? 318 MET   A C   1 
ATOM   2014 O  O   . MET   A 1 298 ? -22.857 -37.881 -24.209 1.00 130.27 ? 318 MET   A O   1 
ATOM   2015 C  CB  . MET   A 1 298 ? -22.612 -38.047 -21.024 1.00 140.46 ? 318 MET   A CB  1 
ATOM   2016 C  CG  . MET   A 1 298 ? -21.773 -38.488 -19.836 1.00 141.13 ? 318 MET   A CG  1 
ATOM   2017 S  SD  . MET   A 1 298 ? -20.174 -39.174 -20.314 1.00 150.90 ? 318 MET   A SD  1 
ATOM   2018 C  CE  . MET   A 1 298 ? -20.674 -40.614 -21.253 1.00 127.98 ? 318 MET   A CE  1 
ATOM   2019 N  N   . TYR   A 1 299 ? -23.303 -35.843 -23.360 1.00 122.80 ? 319 TYR   A N   1 
ATOM   2020 C  CA  . TYR   A 1 299 ? -24.052 -35.449 -24.547 1.00 126.23 ? 319 TYR   A CA  1 
ATOM   2021 C  C   . TYR   A 1 299 ? -23.137 -35.346 -25.760 1.00 130.78 ? 319 TYR   A C   1 
ATOM   2022 O  O   . TYR   A 1 299 ? -23.521 -35.729 -26.872 1.00 138.33 ? 319 TYR   A O   1 
ATOM   2023 C  CB  . TYR   A 1 299 ? -24.773 -34.120 -24.309 1.00 129.61 ? 319 TYR   A CB  1 
ATOM   2024 C  CG  . TYR   A 1 299 ? -25.312 -33.489 -25.578 1.00 133.65 ? 319 TYR   A CG  1 
ATOM   2025 C  CD1 . TYR   A 1 299 ? -26.530 -33.891 -26.113 1.00 137.78 ? 319 TYR   A CD1 1 
ATOM   2026 C  CD2 . TYR   A 1 299 ? -24.601 -32.493 -26.240 1.00 129.21 ? 319 TYR   A CD2 1 
ATOM   2027 C  CE1 . TYR   A 1 299 ? -27.023 -33.320 -27.272 1.00 140.82 ? 319 TYR   A CE1 1 
ATOM   2028 C  CE2 . TYR   A 1 299 ? -25.086 -31.919 -27.398 1.00 132.48 ? 319 TYR   A CE2 1 
ATOM   2029 C  CZ  . TYR   A 1 299 ? -26.295 -32.335 -27.908 1.00 141.83 ? 319 TYR   A CZ  1 
ATOM   2030 O  OH  . TYR   A 1 299 ? -26.769 -31.755 -29.061 1.00 150.99 ? 319 TYR   A OH  1 
ATOM   2031 N  N   . GLU   A 1 300 ? -21.921 -34.831 -25.567 1.00 135.93 ? 320 GLU   A N   1 
ATOM   2032 C  CA  . GLU   A 1 300 ? -21.003 -34.672 -26.689 1.00 134.42 ? 320 GLU   A CA  1 
ATOM   2033 C  C   . GLU   A 1 300 ? -20.427 -36.010 -27.132 1.00 144.47 ? 320 GLU   A C   1 
ATOM   2034 O  O   . GLU   A 1 300 ? -20.256 -36.250 -28.333 1.00 141.48 ? 320 GLU   A O   1 
ATOM   2035 C  CB  . GLU   A 1 300 ? -19.887 -33.695 -26.319 1.00 131.09 ? 320 GLU   A CB  1 
ATOM   2036 C  CG  . GLU   A 1 300 ? -20.357 -32.256 -26.160 1.00 129.83 ? 320 GLU   A CG  1 
ATOM   2037 C  CD  . GLU   A 1 300 ? -20.905 -31.669 -27.450 1.00 136.47 ? 320 GLU   A CD  1 
ATOM   2038 O  OE1 . GLU   A 1 300 ? -20.548 -32.174 -28.536 1.00 116.44 ? 320 GLU   A OE1 1 
ATOM   2039 O  OE2 . GLU   A 1 300 ? -21.693 -30.702 -27.377 1.00 135.36 ? 320 GLU   A OE2 1 
ATOM   2040 N  N   . LEU   A 1 301 ? -20.119 -36.895 -26.180 1.00 135.94 ? 321 LEU   A N   1 
ATOM   2041 C  CA  . LEU   A 1 301 ? -19.650 -38.227 -26.544 1.00 141.26 ? 321 LEU   A CA  1 
ATOM   2042 C  C   . LEU   A 1 301 ? -20.728 -39.011 -27.280 1.00 149.41 ? 321 LEU   A C   1 
ATOM   2043 O  O   . LEU   A 1 301 ? -20.415 -39.845 -28.138 1.00 153.02 ? 321 LEU   A O   1 
ATOM   2044 C  CB  . LEU   A 1 301 ? -19.202 -38.992 -25.298 1.00 137.84 ? 321 LEU   A CB  1 
ATOM   2045 C  CG  . LEU   A 1 301 ? -18.140 -38.350 -24.402 1.00 130.12 ? 321 LEU   A CG  1 
ATOM   2046 C  CD1 . LEU   A 1 301 ? -17.741 -39.295 -23.274 1.00 125.22 ? 321 LEU   A CD1 1 
ATOM   2047 C  CD2 . LEU   A 1 301 ? -16.923 -37.927 -25.209 1.00 132.61 ? 321 LEU   A CD2 1 
ATOM   2048 N  N   . ALA   A 1 302 ? -21.999 -38.759 -26.960 1.00 166.27 ? 322 ALA   A N   1 
ATOM   2049 C  CA  . ALA   A 1 302 ? -23.088 -39.477 -27.614 1.00 161.89 ? 322 ALA   A CA  1 
ATOM   2050 C  C   . ALA   A 1 302 ? -23.262 -39.020 -29.057 1.00 155.59 ? 322 ALA   A C   1 
ATOM   2051 O  O   . ALA   A 1 302 ? -23.335 -39.844 -29.975 1.00 158.56 ? 322 ALA   A O   1 
ATOM   2052 C  CB  . ALA   A 1 302 ? -24.385 -39.293 -26.826 1.00 164.17 ? 322 ALA   A CB  1 
ATOM   2053 N  N   . THR   A 1 303 ? -23.333 -37.708 -29.277 1.00 148.58 ? 323 THR   A N   1 
ATOM   2054 C  CA  . THR   A 1 303 ? -23.481 -37.168 -30.624 1.00 146.30 ? 323 THR   A CA  1 
ATOM   2055 C  C   . THR   A 1 303 ? -22.187 -37.214 -31.425 1.00 144.68 ? 323 THR   A C   1 
ATOM   2056 O  O   . THR   A 1 303 ? -22.195 -36.849 -32.606 1.00 148.34 ? 323 THR   A O   1 
ATOM   2057 C  CB  . THR   A 1 303 ? -23.997 -35.728 -30.565 1.00 148.32 ? 323 THR   A CB  1 
ATOM   2058 O  OG1 . THR   A 1 303 ? -23.006 -34.887 -29.960 1.00 146.94 ? 323 THR   A OG1 1 
ATOM   2059 C  CG2 . THR   A 1 303 ? -25.281 -35.656 -29.750 1.00 152.50 ? 323 THR   A CG2 1 
ATOM   2060 N  N   . HIS   A 1 304 ? -21.082 -37.639 -30.815 1.00 149.07 ? 324 HIS   A N   1 
ATOM   2061 C  CA  . HIS   A 1 304 ? -19.801 -37.821 -31.499 1.00 149.99 ? 324 HIS   A CA  1 
ATOM   2062 C  C   . HIS   A 1 304 ? -19.222 -39.166 -31.082 1.00 154.89 ? 324 HIS   A C   1 
ATOM   2063 O  O   . HIS   A 1 304 ? -18.279 -39.234 -30.284 1.00 154.04 ? 324 HIS   A O   1 
ATOM   2064 C  CB  . HIS   A 1 304 ? -18.832 -36.682 -31.181 1.00 143.82 ? 324 HIS   A CB  1 
ATOM   2065 C  CG  . HIS   A 1 304 ? -19.354 -35.328 -31.544 1.00 138.25 ? 324 HIS   A CG  1 
ATOM   2066 N  ND1 . HIS   A 1 304 ? -20.308 -34.674 -30.795 1.00 135.55 ? 324 HIS   A ND1 1 
ATOM   2067 C  CD2 . HIS   A 1 304 ? -19.061 -34.508 -32.581 1.00 141.73 ? 324 HIS   A CD2 1 
ATOM   2068 C  CE1 . HIS   A 1 304 ? -20.577 -33.507 -31.352 1.00 134.08 ? 324 HIS   A CE1 1 
ATOM   2069 N  NE2 . HIS   A 1 304 ? -19.834 -33.382 -32.437 1.00 135.29 ? 324 HIS   A NE2 1 
ATOM   2070 N  N   . PRO   A 1 305 ? -19.769 -40.263 -31.609 1.00 164.35 ? 325 PRO   A N   1 
ATOM   2071 C  CA  . PRO   A 1 305 ? -19.338 -41.593 -31.151 1.00 163.92 ? 325 PRO   A CA  1 
ATOM   2072 C  C   . PRO   A 1 305 ? -17.895 -41.919 -31.478 1.00 164.22 ? 325 PRO   A C   1 
ATOM   2073 O  O   . PRO   A 1 305 ? -17.319 -42.807 -30.837 1.00 164.04 ? 325 PRO   A O   1 
ATOM   2074 C  CB  . PRO   A 1 305 ? -20.305 -42.540 -31.876 1.00 163.67 ? 325 PRO   A CB  1 
ATOM   2075 C  CG  . PRO   A 1 305 ? -21.494 -41.686 -32.199 1.00 166.37 ? 325 PRO   A CG  1 
ATOM   2076 C  CD  . PRO   A 1 305 ? -20.915 -40.346 -32.529 1.00 169.80 ? 325 PRO   A CD  1 
ATOM   2077 N  N   . ASP   A 1 306 ? -17.292 -41.246 -32.458 1.00 156.93 ? 326 ASP   A N   1 
ATOM   2078 C  CA  . ASP   A 1 306 ? -15.880 -41.478 -32.733 1.00 151.63 ? 326 ASP   A CA  1 
ATOM   2079 C  C   . ASP   A 1 306 ? -15.015 -41.003 -31.574 1.00 155.05 ? 326 ASP   A C   1 
ATOM   2080 O  O   . ASP   A 1 306 ? -13.999 -41.629 -31.249 1.00 154.66 ? 326 ASP   A O   1 
ATOM   2081 C  CB  . ASP   A 1 306 ? -15.476 -40.781 -34.030 1.00 153.81 ? 326 ASP   A CB  1 
ATOM   2082 C  CG  . ASP   A 1 306 ? -15.643 -39.281 -33.957 1.00 161.84 ? 326 ASP   A CG  1 
ATOM   2083 O  OD1 . ASP   A 1 306 ? -16.639 -38.819 -33.361 1.00 164.44 ? 326 ASP   A OD1 1 
ATOM   2084 O  OD2 . ASP   A 1 306 ? -14.770 -38.564 -34.489 1.00 169.29 ? 326 ASP   A OD2 1 
ATOM   2085 N  N   . VAL   A 1 307 ? -15.411 -39.903 -30.931 1.00 158.11 ? 327 VAL   A N   1 
ATOM   2086 C  CA  . VAL   A 1 307 ? -14.681 -39.416 -29.767 1.00 152.20 ? 327 VAL   A CA  1 
ATOM   2087 C  C   . VAL   A 1 307 ? -14.956 -40.295 -28.554 1.00 149.53 ? 327 VAL   A C   1 
ATOM   2088 O  O   . VAL   A 1 307 ? -14.103 -40.427 -27.668 1.00 157.09 ? 327 VAL   A O   1 
ATOM   2089 C  CB  . VAL   A 1 307 ? -15.046 -37.945 -29.497 1.00 137.95 ? 327 VAL   A CB  1 
ATOM   2090 C  CG1 . VAL   A 1 307 ? -14.133 -37.350 -28.436 1.00 145.00 ? 327 VAL   A CG1 1 
ATOM   2091 C  CG2 . VAL   A 1 307 ? -14.973 -37.141 -30.786 1.00 140.08 ? 327 VAL   A CG2 1 
ATOM   2092 N  N   . GLN   A 1 308 ? -16.137 -40.915 -28.493 1.00 150.82 ? 328 GLN   A N   1 
ATOM   2093 C  CA  . GLN   A 1 308 ? -16.456 -41.776 -27.360 1.00 151.63 ? 328 GLN   A CA  1 
ATOM   2094 C  C   . GLN   A 1 308 ? -15.648 -43.067 -27.403 1.00 155.30 ? 328 GLN   A C   1 
ATOM   2095 O  O   . GLN   A 1 308 ? -15.118 -43.508 -26.376 1.00 154.22 ? 328 GLN   A O   1 
ATOM   2096 C  CB  . GLN   A 1 308 ? -17.956 -42.074 -27.335 1.00 149.80 ? 328 GLN   A CB  1 
ATOM   2097 C  CG  . GLN   A 1 308 ? -18.401 -42.926 -26.157 1.00 140.86 ? 328 GLN   A CG  1 
ATOM   2098 C  CD  . GLN   A 1 308 ? -19.909 -43.029 -26.052 1.00 143.28 ? 328 GLN   A CD  1 
ATOM   2099 O  OE1 . GLN   A 1 308 ? -20.437 -43.784 -25.235 1.00 147.52 ? 328 GLN   A OE1 1 
ATOM   2100 N  NE2 . GLN   A 1 308 ? -20.612 -42.265 -26.879 1.00 144.07 ? 328 GLN   A NE2 1 
ATOM   2101 N  N   . GLN   A 1 309 ? -15.532 -43.683 -28.582 1.00 149.48 ? 329 GLN   A N   1 
ATOM   2102 C  CA  . GLN   A 1 309 ? -14.746 -44.908 -28.696 1.00 156.09 ? 329 GLN   A CA  1 
ATOM   2103 C  C   . GLN   A 1 309 ? -13.256 -44.624 -28.550 1.00 156.79 ? 329 GLN   A C   1 
ATOM   2104 O  O   . GLN   A 1 309 ? -12.548 -45.356 -27.848 1.00 158.71 ? 329 GLN   A O   1 
ATOM   2105 C  CB  . GLN   A 1 309 ? -15.027 -45.603 -30.027 1.00 145.59 ? 329 GLN   A CB  1 
ATOM   2106 C  CG  . GLN   A 1 309 ? -14.250 -46.900 -30.199 1.00 149.90 ? 329 GLN   A CG  1 
ATOM   2107 C  CD  . GLN   A 1 309 ? -14.304 -47.439 -31.612 1.00 141.35 ? 329 GLN   A CD  1 
ATOM   2108 O  OE1 . GLN   A 1 309 ? -15.381 -47.644 -32.171 1.00 142.13 ? 329 GLN   A OE1 1 
ATOM   2109 N  NE2 . GLN   A 1 309 ? -13.136 -47.672 -32.200 1.00 141.31 ? 329 GLN   A NE2 1 
ATOM   2110 N  N   . LYS   A 1 310 ? -12.763 -43.566 -29.200 1.00 152.71 ? 330 LYS   A N   1 
ATOM   2111 C  CA  . LYS   A 1 310 ? -11.347 -43.226 -29.090 1.00 149.42 ? 330 LYS   A CA  1 
ATOM   2112 C  C   . LYS   A 1 310 ? -10.959 -42.913 -27.650 1.00 150.65 ? 330 LYS   A C   1 
ATOM   2113 O  O   . LYS   A 1 310 ? -9.801  -43.107 -27.263 1.00 148.99 ? 330 LYS   A O   1 
ATOM   2114 C  CB  . LYS   A 1 310 ? -11.017 -42.044 -30.003 1.00 148.56 ? 330 LYS   A CB  1 
ATOM   2115 C  CG  . LYS   A 1 310 ? -9.527  -41.785 -30.175 1.00 151.15 ? 330 LYS   A CG  1 
ATOM   2116 C  CD  . LYS   A 1 310 ? -9.260  -40.614 -31.107 1.00 149.99 ? 330 LYS   A CD  1 
ATOM   2117 C  CE  . LYS   A 1 310 ? -7.768  -40.391 -31.291 1.00 157.31 ? 330 LYS   A CE  1 
ATOM   2118 N  NZ  . LYS   A 1 310 ? -7.486  -39.221 -32.168 1.00 153.95 ? 330 LYS   A NZ  1 
ATOM   2119 N  N   . LEU   A 1 311 ? -11.909 -42.434 -26.843 1.00 151.67 ? 331 LEU   A N   1 
ATOM   2120 C  CA  . LEU   A 1 311 ? -11.642 -42.236 -25.423 1.00 151.13 ? 331 LEU   A CA  1 
ATOM   2121 C  C   . LEU   A 1 311 ? -11.717 -43.550 -24.655 1.00 153.33 ? 331 LEU   A C   1 
ATOM   2122 O  O   . LEU   A 1 311 ? -10.918 -43.783 -23.741 1.00 154.38 ? 331 LEU   A O   1 
ATOM   2123 C  CB  . LEU   A 1 311 ? -12.624 -41.220 -24.838 1.00 147.06 ? 331 LEU   A CB  1 
ATOM   2124 C  CG  . LEU   A 1 311 ? -12.502 -40.945 -23.339 1.00 141.95 ? 331 LEU   A CG  1 
ATOM   2125 C  CD1 . LEU   A 1 311 ? -11.087 -40.523 -22.989 1.00 143.90 ? 331 LEU   A CD1 1 
ATOM   2126 C  CD2 . LEU   A 1 311 ? -13.499 -39.878 -22.921 1.00 140.16 ? 331 LEU   A CD2 1 
ATOM   2127 N  N   . GLN   A 1 312 ? -12.674 -44.415 -25.008 1.00 154.77 ? 332 GLN   A N   1 
ATOM   2128 C  CA  . GLN   A 1 312 ? -12.766 -45.725 -24.371 1.00 157.41 ? 332 GLN   A CA  1 
ATOM   2129 C  C   . GLN   A 1 312 ? -11.521 -46.561 -24.635 1.00 165.30 ? 332 GLN   A C   1 
ATOM   2130 O  O   . GLN   A 1 312 ? -11.127 -47.377 -23.793 1.00 164.71 ? 332 GLN   A O   1 
ATOM   2131 C  CB  . GLN   A 1 312 ? -14.013 -46.465 -24.865 1.00 159.70 ? 332 GLN   A CB  1 
ATOM   2132 C  CG  . GLN   A 1 312 ? -15.328 -45.960 -24.293 1.00 153.24 ? 332 GLN   A CG  1 
ATOM   2133 C  CD  . GLN   A 1 312 ? -16.535 -46.633 -24.925 1.00 154.14 ? 332 GLN   A CD  1 
ATOM   2134 O  OE1 . GLN   A 1 312 ? -16.552 -46.908 -26.125 1.00 134.96 ? 332 GLN   A OE1 1 
ATOM   2135 N  NE2 . GLN   A 1 312 ? -17.550 -46.905 -24.114 1.00 155.12 ? 332 GLN   A NE2 1 
ATOM   2136 N  N   . GLU   A 1 313 ? -10.887 -46.367 -25.793 1.00 161.03 ? 333 GLU   A N   1 
ATOM   2137 C  CA  . GLU   A 1 313 ? -9.693  -47.136 -26.124 1.00 166.31 ? 333 GLU   A CA  1 
ATOM   2138 C  C   . GLU   A 1 313 ? -8.500  -46.716 -25.275 1.00 170.31 ? 333 GLU   A C   1 
ATOM   2139 O  O   . GLU   A 1 313 ? -7.635  -47.546 -24.974 1.00 176.15 ? 333 GLU   A O   1 
ATOM   2140 C  CB  . GLU   A 1 313 ? -9.375  -46.989 -27.612 1.00 158.68 ? 333 GLU   A CB  1 
ATOM   2141 C  CG  . GLU   A 1 313 ? -10.426 -47.599 -28.531 1.00 154.79 ? 333 GLU   A CG  1 
ATOM   2142 C  CD  . GLU   A 1 313 ? -10.309 -47.102 -29.956 1.00 157.10 ? 333 GLU   A CD  1 
ATOM   2143 O  OE1 . GLU   A 1 313 ? -9.463  -46.217 -30.201 1.00 155.27 ? 333 GLU   A OE1 1 
ATOM   2144 O  OE2 . GLU   A 1 313 ? -11.061 -47.590 -30.827 1.00 165.28 ? 333 GLU   A OE2 1 
ATOM   2145 N  N   . GLU   A 1 314 ? -8.436  -45.445 -24.874 1.00 185.99 ? 334 GLU   A N   1 
ATOM   2146 C  CA  . GLU   A 1 314 ? -7.348  -44.994 -24.013 1.00 187.18 ? 334 GLU   A CA  1 
ATOM   2147 C  C   . GLU   A 1 314 ? -7.536  -45.467 -22.578 1.00 191.49 ? 334 GLU   A C   1 
ATOM   2148 O  O   . GLU   A 1 314 ? -6.560  -45.799 -21.896 1.00 198.50 ? 334 GLU   A O   1 
ATOM   2149 C  CB  . GLU   A 1 314 ? -7.243  -43.470 -24.050 1.00 186.31 ? 334 GLU   A CB  1 
ATOM   2150 C  CG  . GLU   A 1 314 ? -6.069  -42.913 -23.264 1.00 196.92 ? 334 GLU   A CG  1 
ATOM   2151 C  CD  . GLU   A 1 314 ? -6.320  -41.504 -22.771 1.00 185.80 ? 334 GLU   A CD  1 
ATOM   2152 O  OE1 . GLU   A 1 314 ? -7.435  -41.241 -22.273 1.00 176.13 ? 334 GLU   A OE1 1 
ATOM   2153 O  OE2 . GLU   A 1 314 ? -5.408  -40.659 -22.887 1.00 180.27 ? 334 GLU   A OE2 1 
ATOM   2154 N  N   . ILE   A 1 315 ? -8.783  -45.496 -22.104 1.00 171.86 ? 335 ILE   A N   1 
ATOM   2155 C  CA  . ILE   A 1 315 ? -9.048  -45.870 -20.719 1.00 168.49 ? 335 ILE   A CA  1 
ATOM   2156 C  C   . ILE   A 1 315 ? -8.693  -47.332 -20.480 1.00 165.85 ? 335 ILE   A C   1 
ATOM   2157 O  O   . ILE   A 1 315 ? -8.102  -47.681 -19.450 1.00 165.58 ? 335 ILE   A O   1 
ATOM   2158 C  CB  . ILE   A 1 315 ? -10.515 -45.569 -20.366 1.00 162.29 ? 335 ILE   A CB  1 
ATOM   2159 C  CG1 . ILE   A 1 315 ? -10.782 -44.067 -20.468 1.00 164.56 ? 335 ILE   A CG1 1 
ATOM   2160 C  CG2 . ILE   A 1 315 ? -10.845 -46.073 -18.976 1.00 160.49 ? 335 ILE   A CG2 1 
ATOM   2161 C  CD1 . ILE   A 1 315 ? -12.227 -43.696 -20.258 1.00 152.24 ? 335 ILE   A CD1 1 
ATOM   2162 N  N   . ASP   A 1 316 ? -9.042  -48.210 -21.424 1.00 164.18 ? 336 ASP   A N   1 
ATOM   2163 C  CA  . ASP   A 1 316 ? -8.666  -49.613 -21.306 1.00 167.41 ? 336 ASP   A CA  1 
ATOM   2164 C  C   . ASP   A 1 316 ? -7.167  -49.826 -21.466 1.00 172.97 ? 336 ASP   A C   1 
ATOM   2165 O  O   . ASP   A 1 316 ? -6.640  -50.828 -20.971 1.00 171.82 ? 336 ASP   A O   1 
ATOM   2166 C  CB  . ASP   A 1 316 ? -9.423  -50.448 -22.340 1.00 167.79 ? 336 ASP   A CB  1 
ATOM   2167 C  CG  . ASP   A 1 316 ? -10.925 -50.393 -22.149 1.00 169.97 ? 336 ASP   A CG  1 
ATOM   2168 O  OD1 . ASP   A 1 316 ? -11.370 -50.137 -21.007 1.00 171.92 ? 336 ASP   A OD1 1 
ATOM   2169 O  OD2 . ASP   A 1 316 ? -11.659 -50.615 -23.137 1.00 139.44 ? 336 ASP   A OD2 1 
ATOM   2170 N  N   . ALA   A 1 317 ? -6.472  -48.912 -22.143 1.00 169.64 ? 337 ALA   A N   1 
ATOM   2171 C  CA  . ALA   A 1 317 ? -5.027  -49.038 -22.297 1.00 167.89 ? 337 ALA   A CA  1 
ATOM   2172 C  C   . ALA   A 1 317 ? -4.308  -48.730 -20.989 1.00 168.07 ? 337 ALA   A C   1 
ATOM   2173 O  O   . ALA   A 1 317 ? -3.544  -49.556 -20.477 1.00 162.97 ? 337 ALA   A O   1 
ATOM   2174 C  CB  . ALA   A 1 317 ? -4.532  -48.115 -23.413 1.00 166.19 ? 337 ALA   A CB  1 
ATOM   2175 N  N   . VAL   A 1 318 ? -4.539  -47.535 -20.438 1.00 165.01 ? 338 VAL   A N   1 
ATOM   2176 C  CA  . VAL   A 1 318 ? -3.898  -47.152 -19.181 1.00 168.65 ? 338 VAL   A CA  1 
ATOM   2177 C  C   . VAL   A 1 318 ? -4.354  -48.063 -18.049 1.00 164.07 ? 338 VAL   A C   1 
ATOM   2178 O  O   . VAL   A 1 318 ? -3.565  -48.432 -17.169 1.00 163.96 ? 338 VAL   A O   1 
ATOM   2179 C  CB  . VAL   A 1 318 ? -4.182  -45.671 -18.866 1.00 166.91 ? 338 VAL   A CB  1 
ATOM   2180 C  CG1 . VAL   A 1 318 ? -3.741  -45.331 -17.451 1.00 163.57 ? 338 VAL   A CG1 1 
ATOM   2181 C  CG2 . VAL   A 1 318 ? -3.480  -44.771 -19.871 1.00 170.43 ? 338 VAL   A CG2 1 
ATOM   2182 N  N   . LEU   A 1 319 ? -5.630  -48.453 -18.057 1.00 165.32 ? 339 LEU   A N   1 
ATOM   2183 C  CA  . LEU   A 1 319 ? -6.213  -49.299 -17.019 1.00 161.14 ? 339 LEU   A CA  1 
ATOM   2184 C  C   . LEU   A 1 319 ? -6.687  -50.601 -17.653 1.00 172.22 ? 339 LEU   A C   1 
ATOM   2185 O  O   . LEU   A 1 319 ? -7.880  -50.757 -17.957 1.00 174.02 ? 339 LEU   A O   1 
ATOM   2186 C  CB  . LEU   A 1 319 ? -7.361  -48.582 -16.309 1.00 164.82 ? 339 LEU   A CB  1 
ATOM   2187 C  CG  . LEU   A 1 319 ? -6.975  -47.274 -15.621 1.00 167.33 ? 339 LEU   A CG  1 
ATOM   2188 C  CD1 . LEU   A 1 319 ? -8.204  -46.607 -15.045 1.00 168.26 ? 339 LEU   A CD1 1 
ATOM   2189 C  CD2 . LEU   A 1 319 ? -5.938  -47.524 -14.538 1.00 164.43 ? 339 LEU   A CD2 1 
ATOM   2190 N  N   . PRO   A 1 320 ? -5.788  -51.559 -17.864 1.00 176.73 ? 340 PRO   A N   1 
ATOM   2191 C  CA  . PRO   A 1 320 ? -6.199  -52.833 -18.461 1.00 185.76 ? 340 PRO   A CA  1 
ATOM   2192 C  C   . PRO   A 1 320 ? -6.961  -53.692 -17.463 1.00 203.47 ? 340 PRO   A C   1 
ATOM   2193 O  O   . PRO   A 1 320 ? -6.829  -53.553 -16.245 1.00 200.48 ? 340 PRO   A O   1 
ATOM   2194 C  CB  . PRO   A 1 320 ? -4.871  -53.483 -18.858 1.00 181.49 ? 340 PRO   A CB  1 
ATOM   2195 C  CG  . PRO   A 1 320 ? -3.891  -52.923 -17.890 1.00 171.60 ? 340 PRO   A CG  1 
ATOM   2196 C  CD  . PRO   A 1 320 ? -4.340  -51.515 -17.596 1.00 168.75 ? 340 PRO   A CD  1 
ATOM   2197 N  N   . ASN   A 1 321 ? -7.773  -54.600 -18.012 1.00 223.35 ? 341 ASN   A N   1 
ATOM   2198 C  CA  . ASN   A 1 321 ? -8.656  -55.467 -17.227 1.00 232.54 ? 341 ASN   A CA  1 
ATOM   2199 C  C   . ASN   A 1 321 ? -9.627  -54.659 -16.371 1.00 231.45 ? 341 ASN   A C   1 
ATOM   2200 O  O   . ASN   A 1 321 ? -9.972  -55.068 -15.259 1.00 241.67 ? 341 ASN   A O   1 
ATOM   2201 C  CB  . ASN   A 1 321 ? -7.859  -56.436 -16.346 1.00 237.11 ? 341 ASN   A CB  1 
ATOM   2202 C  CG  . ASN   A 1 321 ? -7.053  -57.431 -17.152 1.00 239.48 ? 341 ASN   A CG  1 
ATOM   2203 O  OD1 . ASN   A 1 321 ? -7.397  -57.749 -18.290 1.00 242.34 ? 341 ASN   A OD1 1 
ATOM   2204 N  ND2 . ASN   A 1 321 ? -5.975  -57.935 -16.562 1.00 242.84 ? 341 ASN   A ND2 1 
ATOM   2205 N  N   . LYS   A 1 322 ? -10.078 -53.516 -16.891 1.00 207.03 ? 342 LYS   A N   1 
ATOM   2206 C  CA  . LYS   A 1 322 ? -10.929 -52.583 -16.149 1.00 196.69 ? 342 LYS   A CA  1 
ATOM   2207 C  C   . LYS   A 1 322 ? -10.305 -52.234 -14.800 1.00 195.50 ? 342 LYS   A C   1 
ATOM   2208 O  O   . LYS   A 1 322 ? -10.927 -52.363 -13.743 1.00 197.42 ? 342 LYS   A O   1 
ATOM   2209 C  CB  . LYS   A 1 322 ? -12.342 -53.143 -15.968 1.00 201.99 ? 342 LYS   A CB  1 
ATOM   2210 C  CG  . LYS   A 1 322 ? -13.177 -53.210 -17.236 1.00 197.47 ? 342 LYS   A CG  1 
ATOM   2211 C  CD  . LYS   A 1 322 ? -14.617 -53.569 -16.900 1.00 193.78 ? 342 LYS   A CD  1 
ATOM   2212 C  CE  . LYS   A 1 322 ? -15.469 -53.727 -18.147 1.00 183.26 ? 342 LYS   A CE  1 
ATOM   2213 N  NZ  . LYS   A 1 322 ? -16.902 -53.969 -17.813 1.00 183.39 ? 342 LYS   A NZ  1 
ATOM   2214 N  N   . ALA   A 1 323 ? -9.050  -51.794 -14.846 1.00 205.71 ? 343 ALA   A N   1 
ATOM   2215 C  CA  . ALA   A 1 323 ? -8.316  -51.506 -13.627 1.00 197.04 ? 343 ALA   A CA  1 
ATOM   2216 C  C   . ALA   A 1 323 ? -8.913  -50.296 -12.909 1.00 199.86 ? 343 ALA   A C   1 
ATOM   2217 O  O   . ALA   A 1 323 ? -9.435  -49.378 -13.548 1.00 200.42 ? 343 ALA   A O   1 
ATOM   2218 C  CB  . ALA   A 1 323 ? -6.843  -51.252 -13.936 1.00 194.66 ? 343 ALA   A CB  1 
ATOM   2219 N  N   . PRO   A 1 324 ? -8.857  -50.276 -11.580 1.00 187.77 ? 344 PRO   A N   1 
ATOM   2220 C  CA  . PRO   A 1 324 ? -9.373  -49.128 -10.830 1.00 186.61 ? 344 PRO   A CA  1 
ATOM   2221 C  C   . PRO   A 1 324 ? -8.509  -47.903 -11.061 1.00 182.65 ? 344 PRO   A C   1 
ATOM   2222 O  O   . PRO   A 1 324 ? -7.278  -47.966 -10.922 1.00 183.92 ? 344 PRO   A O   1 
ATOM   2223 C  CB  . PRO   A 1 324 ? -9.300  -49.595 -9.367  1.00 188.18 ? 344 PRO   A CB  1 
ATOM   2224 C  CG  . PRO   A 1 324 ? -9.153  -51.088 -9.433  1.00 191.84 ? 344 PRO   A CG  1 
ATOM   2225 C  CD  . PRO   A 1 324 ? -8.392  -51.352 -10.690 1.00 190.07 ? 344 PRO   A CD  1 
ATOM   2226 N  N   . PRO   A 1 325 ? -9.113  -46.770 -11.417 1.00 173.18 ? 345 PRO   A N   1 
ATOM   2227 C  CA  . PRO   A 1 325 ? -8.316  -45.561 -11.656 1.00 170.23 ? 345 PRO   A CA  1 
ATOM   2228 C  C   . PRO   A 1 325 ? -7.682  -45.040 -10.375 1.00 164.02 ? 345 PRO   A C   1 
ATOM   2229 O  O   . PRO   A 1 325 ? -8.300  -45.037 -9.307  1.00 164.53 ? 345 PRO   A O   1 
ATOM   2230 C  CB  . PRO   A 1 325 ? -9.340  -44.569 -12.222 1.00 169.37 ? 345 PRO   A CB  1 
ATOM   2231 C  CG  . PRO   A 1 325 ? -10.654 -45.046 -11.700 1.00 176.47 ? 345 PRO   A CG  1 
ATOM   2232 C  CD  . PRO   A 1 325 ? -10.549 -46.545 -11.656 1.00 177.77 ? 345 PRO   A CD  1 
ATOM   2233 N  N   . THR   A 1 326 ? -6.431  -44.610 -10.492 1.00 162.58 ? 346 THR   A N   1 
ATOM   2234 C  CA  . THR   A 1 326 ? -5.673  -44.021 -9.398  1.00 164.17 ? 346 THR   A CA  1 
ATOM   2235 C  C   . THR   A 1 326 ? -5.328  -42.575 -9.745  1.00 163.84 ? 346 THR   A C   1 
ATOM   2236 O  O   . THR   A 1 326 ? -5.613  -42.091 -10.842 1.00 159.34 ? 346 THR   A O   1 
ATOM   2237 C  CB  . THR   A 1 326 ? -4.408  -44.838 -9.103  1.00 158.23 ? 346 THR   A CB  1 
ATOM   2238 O  OG1 . THR   A 1 326 ? -3.637  -44.985 -10.301 1.00 161.29 ? 346 THR   A OG1 1 
ATOM   2239 C  CG2 . THR   A 1 326 ? -4.773  -46.216 -8.565  1.00 171.87 ? 346 THR   A CG2 1 
ATOM   2240 N  N   . TYR   A 1 327 ? -4.712  -41.883 -8.785  1.00 158.68 ? 347 TYR   A N   1 
ATOM   2241 C  CA  . TYR   A 1 327 ? -4.344  -40.485 -8.986  1.00 156.73 ? 347 TYR   A CA  1 
ATOM   2242 C  C   . TYR   A 1 327 ? -3.428  -40.323 -10.195 1.00 156.67 ? 347 TYR   A C   1 
ATOM   2243 O  O   . TYR   A 1 327 ? -3.614  -39.416 -11.015 1.00 161.28 ? 347 TYR   A O   1 
ATOM   2244 C  CB  . TYR   A 1 327 ? -3.671  -39.947 -7.722  1.00 162.48 ? 347 TYR   A CB  1 
ATOM   2245 C  CG  . TYR   A 1 327 ? -3.381  -38.464 -7.733  1.00 167.53 ? 347 TYR   A CG  1 
ATOM   2246 C  CD1 . TYR   A 1 327 ? -2.230  -37.964 -8.329  1.00 168.21 ? 347 TYR   A CD1 1 
ATOM   2247 C  CD2 . TYR   A 1 327 ? -4.246  -37.566 -7.125  1.00 159.21 ? 347 TYR   A CD2 1 
ATOM   2248 C  CE1 . TYR   A 1 327 ? -1.960  -36.612 -8.333  1.00 165.57 ? 347 TYR   A CE1 1 
ATOM   2249 C  CE2 . TYR   A 1 327 ? -3.984  -36.213 -7.124  1.00 165.26 ? 347 TYR   A CE2 1 
ATOM   2250 C  CZ  . TYR   A 1 327 ? -2.840  -35.742 -7.729  1.00 161.95 ? 347 TYR   A CZ  1 
ATOM   2251 O  OH  . TYR   A 1 327 ? -2.577  -34.393 -7.728  1.00 155.59 ? 347 TYR   A OH  1 
ATOM   2252 N  N   . ASP   A 1 328 ? -2.435  -41.204 -10.325 1.00 161.01 ? 348 ASP   A N   1 
ATOM   2253 C  CA  . ASP   A 1 328 ? -1.423  -41.046 -11.363 1.00 162.67 ? 348 ASP   A CA  1 
ATOM   2254 C  C   . ASP   A 1 328 ? -1.876  -41.593 -12.711 1.00 165.36 ? 348 ASP   A C   1 
ATOM   2255 O  O   . ASP   A 1 328 ? -1.418  -41.111 -13.753 1.00 169.53 ? 348 ASP   A O   1 
ATOM   2256 C  CB  . ASP   A 1 328 ? -0.125  -41.722 -10.920 1.00 164.68 ? 348 ASP   A CB  1 
ATOM   2257 C  CG  . ASP   A 1 328 ? 0.440   -41.116 -9.648  1.00 167.05 ? 348 ASP   A CG  1 
ATOM   2258 O  OD1 . ASP   A 1 328 ? 1.036   -40.020 -9.722  1.00 169.25 ? 348 ASP   A OD1 1 
ATOM   2259 O  OD2 . ASP   A 1 328 ? 0.269   -41.727 -8.572  1.00 165.31 ? 348 ASP   A OD2 1 
ATOM   2260 N  N   . THR   A 1 329 ? -2.763  -42.590 -12.719 1.00 161.20 ? 349 THR   A N   1 
ATOM   2261 C  CA  . THR   A 1 329 ? -3.293  -43.087 -13.983 1.00 160.78 ? 349 THR   A CA  1 
ATOM   2262 C  C   . THR   A 1 329 ? -4.292  -42.125 -14.611 1.00 163.53 ? 349 THR   A C   1 
ATOM   2263 O  O   . THR   A 1 329 ? -4.489  -42.164 -15.830 1.00 162.68 ? 349 THR   A O   1 
ATOM   2264 C  CB  . THR   A 1 329 ? -3.942  -44.458 -13.785 1.00 156.09 ? 349 THR   A CB  1 
ATOM   2265 O  OG1 . THR   A 1 329 ? -4.824  -44.413 -12.655 1.00 154.85 ? 349 THR   A OG1 1 
ATOM   2266 C  CG2 . THR   A 1 329 ? -2.878  -45.522 -13.556 1.00 150.86 ? 349 THR   A CG2 1 
ATOM   2267 N  N   . VAL   A 1 330 ? -4.923  -41.264 -13.810 1.00 161.65 ? 350 VAL   A N   1 
ATOM   2268 C  CA  . VAL   A 1 330 ? -5.826  -40.258 -14.362 1.00 157.91 ? 350 VAL   A CA  1 
ATOM   2269 C  C   . VAL   A 1 330 ? -5.033  -39.146 -15.034 1.00 165.60 ? 350 VAL   A C   1 
ATOM   2270 O  O   . VAL   A 1 330 ? -5.330  -38.743 -16.165 1.00 170.33 ? 350 VAL   A O   1 
ATOM   2271 C  CB  . VAL   A 1 330 ? -6.752  -39.702 -13.265 1.00 155.71 ? 350 VAL   A CB  1 
ATOM   2272 C  CG1 . VAL   A 1 330 ? -7.539  -38.514 -13.791 1.00 143.37 ? 350 VAL   A CG1 1 
ATOM   2273 C  CG2 . VAL   A 1 330 ? -7.690  -40.783 -12.773 1.00 147.75 ? 350 VAL   A CG2 1 
ATOM   2274 N  N   . LEU   A 1 331 ? -4.006  -38.637 -14.350 1.00 152.06 ? 351 LEU   A N   1 
ATOM   2275 C  CA  . LEU   A 1 331 ? -3.180  -37.573 -14.908 1.00 158.42 ? 351 LEU   A CA  1 
ATOM   2276 C  C   . LEU   A 1 331 ? -2.404  -38.010 -16.142 1.00 166.92 ? 351 LEU   A C   1 
ATOM   2277 O  O   . LEU   A 1 331 ? -1.885  -37.150 -16.862 1.00 165.41 ? 351 LEU   A O   1 
ATOM   2278 C  CB  . LEU   A 1 331 ? -2.209  -37.054 -13.848 1.00 159.60 ? 351 LEU   A CB  1 
ATOM   2279 C  CG  . LEU   A 1 331 ? -2.799  -36.159 -12.759 1.00 161.08 ? 351 LEU   A CG  1 
ATOM   2280 C  CD1 . LEU   A 1 331 ? -1.718  -35.759 -11.771 1.00 157.17 ? 351 LEU   A CD1 1 
ATOM   2281 C  CD2 . LEU   A 1 331 ? -3.449  -34.928 -13.372 1.00 162.19 ? 351 LEU   A CD2 1 
ATOM   2282 N  N   . GLN   A 1 332 ? -2.305  -39.315 -16.402 1.00 178.08 ? 352 GLN   A N   1 
ATOM   2283 C  CA  . GLN   A 1 332 ? -1.627  -39.788 -17.603 1.00 174.80 ? 352 GLN   A CA  1 
ATOM   2284 C  C   . GLN   A 1 332 ? -2.523  -39.704 -18.832 1.00 174.58 ? 352 GLN   A C   1 
ATOM   2285 O  O   . GLN   A 1 332 ? -2.031  -39.448 -19.937 1.00 177.68 ? 352 GLN   A O   1 
ATOM   2286 C  CB  . GLN   A 1 332 ? -1.143  -41.226 -17.401 1.00 176.27 ? 352 GLN   A CB  1 
ATOM   2287 C  CG  . GLN   A 1 332 ? -0.478  -41.845 -18.623 1.00 182.34 ? 352 GLN   A CG  1 
ATOM   2288 C  CD  . GLN   A 1 332 ? -0.027  -43.275 -18.387 1.00 188.70 ? 352 GLN   A CD  1 
ATOM   2289 O  OE1 . GLN   A 1 332 ? 0.021   -43.743 -17.250 1.00 194.89 ? 352 GLN   A OE1 1 
ATOM   2290 N  NE2 . GLN   A 1 332 ? 0.304   -43.977 -19.465 1.00 182.48 ? 352 GLN   A NE2 1 
ATOM   2291 N  N   . MET   A 1 333 ? -3.827  -39.904 -18.660 1.00 170.76 ? 353 MET   A N   1 
ATOM   2292 C  CA  . MET   A 1 333 ? -4.761  -39.909 -19.782 1.00 166.56 ? 353 MET   A CA  1 
ATOM   2293 C  C   . MET   A 1 333 ? -4.874  -38.505 -20.362 1.00 162.45 ? 353 MET   A C   1 
ATOM   2294 O  O   . MET   A 1 333 ? -5.447  -37.608 -19.734 1.00 165.54 ? 353 MET   A O   1 
ATOM   2295 C  CB  . MET   A 1 333 ? -6.120  -40.428 -19.325 1.00 160.88 ? 353 MET   A CB  1 
ATOM   2296 C  CG  . MET   A 1 333 ? -6.045  -41.782 -18.645 1.00 167.48 ? 353 MET   A CG  1 
ATOM   2297 S  SD  . MET   A 1 333 ? -7.623  -42.327 -17.976 1.00 170.70 ? 353 MET   A SD  1 
ATOM   2298 C  CE  . MET   A 1 333 ? -7.117  -43.814 -17.118 1.00 167.79 ? 353 MET   A CE  1 
ATOM   2299 N  N   . GLU   A 1 334 ? -4.329  -38.313 -21.563 1.00 156.09 ? 354 GLU   A N   1 
ATOM   2300 C  CA  . GLU   A 1 334 ? -4.326  -37.003 -22.202 1.00 150.15 ? 354 GLU   A CA  1 
ATOM   2301 C  C   . GLU   A 1 334 ? -5.571  -36.763 -23.047 1.00 138.29 ? 354 GLU   A C   1 
ATOM   2302 O  O   . GLU   A 1 334 ? -6.065  -35.632 -23.108 1.00 139.85 ? 354 GLU   A O   1 
ATOM   2303 C  CB  . GLU   A 1 334 ? -3.071  -36.838 -23.065 1.00 154.12 ? 354 GLU   A CB  1 
ATOM   2304 C  CG  . GLU   A 1 334 ? -1.766  -36.872 -22.282 1.00 171.54 ? 354 GLU   A CG  1 
ATOM   2305 C  CD  . GLU   A 1 334 ? -0.555  -36.607 -23.157 1.00 181.18 ? 354 GLU   A CD  1 
ATOM   2306 O  OE1 . GLU   A 1 334 ? -0.729  -36.027 -24.249 1.00 180.49 ? 354 GLU   A OE1 1 
ATOM   2307 O  OE2 . GLU   A 1 334 ? 0.569   -36.979 -22.756 1.00 180.61 ? 354 GLU   A OE2 1 
ATOM   2308 N  N   . TYR   A 1 335 ? -6.090  -37.801 -23.707 1.00 138.77 ? 355 TYR   A N   1 
ATOM   2309 C  CA  . TYR   A 1 335 ? -7.303  -37.624 -24.498 1.00 133.89 ? 355 TYR   A CA  1 
ATOM   2310 C  C   . TYR   A 1 335 ? -8.511  -37.345 -23.612 1.00 122.31 ? 355 TYR   A C   1 
ATOM   2311 O  O   . TYR   A 1 335 ? -9.412  -36.599 -24.013 1.00 122.78 ? 355 TYR   A O   1 
ATOM   2312 C  CB  . TYR   A 1 335 ? -7.548  -38.853 -25.371 1.00 139.97 ? 355 TYR   A CB  1 
ATOM   2313 C  CG  . TYR   A 1 335 ? -8.523  -38.619 -26.503 1.00 134.16 ? 355 TYR   A CG  1 
ATOM   2314 C  CD1 . TYR   A 1 335 ? -8.158  -37.868 -27.613 1.00 135.53 ? 355 TYR   A CD1 1 
ATOM   2315 C  CD2 . TYR   A 1 335 ? -9.801  -39.162 -26.469 1.00 136.32 ? 355 TYR   A CD2 1 
ATOM   2316 C  CE1 . TYR   A 1 335 ? -9.041  -37.656 -28.652 1.00 141.32 ? 355 TYR   A CE1 1 
ATOM   2317 C  CE2 . TYR   A 1 335 ? -10.691 -38.957 -27.505 1.00 137.82 ? 355 TYR   A CE2 1 
ATOM   2318 C  CZ  . TYR   A 1 335 ? -10.305 -38.204 -28.593 1.00 136.34 ? 355 TYR   A CZ  1 
ATOM   2319 O  OH  . TYR   A 1 335 ? -11.188 -37.997 -29.627 1.00 133.05 ? 355 TYR   A OH  1 
ATOM   2320 N  N   . LEU   A 1 336 ? -8.549  -37.930 -22.412 1.00 134.00 ? 356 LEU   A N   1 
ATOM   2321 C  CA  . LEU   A 1 336 ? -9.591  -37.584 -21.452 1.00 133.58 ? 356 LEU   A CA  1 
ATOM   2322 C  C   . LEU   A 1 336 ? -9.482  -36.123 -21.038 1.00 131.37 ? 356 LEU   A C   1 
ATOM   2323 O  O   . LEU   A 1 336 ? -10.495 -35.420 -20.929 1.00 128.45 ? 356 LEU   A O   1 
ATOM   2324 C  CB  . LEU   A 1 336 ? -9.500  -38.500 -20.234 1.00 136.40 ? 356 LEU   A CB  1 
ATOM   2325 C  CG  . LEU   A 1 336 ? -10.594 -38.346 -19.177 1.00 125.46 ? 356 LEU   A CG  1 
ATOM   2326 C  CD1 . LEU   A 1 336 ? -11.944 -38.770 -19.733 1.00 126.86 ? 356 LEU   A CD1 1 
ATOM   2327 C  CD2 . LEU   A 1 336 ? -10.250 -39.142 -17.932 1.00 128.01 ? 356 LEU   A CD2 1 
ATOM   2328 N  N   . ASP   A 1 337 ? -8.254  -35.647 -20.812 1.00 128.67 ? 357 ASP   A N   1 
ATOM   2329 C  CA  . ASP   A 1 337 ? -8.042  -34.235 -20.514 1.00 132.02 ? 357 ASP   A CA  1 
ATOM   2330 C  C   . ASP   A 1 337 ? -8.507  -33.357 -21.668 1.00 119.70 ? 357 ASP   A C   1 
ATOM   2331 O  O   . ASP   A 1 337 ? -9.058  -32.272 -21.450 1.00 101.11 ? 357 ASP   A O   1 
ATOM   2332 C  CB  . ASP   A 1 337 ? -6.564  -33.986 -20.209 1.00 126.07 ? 357 ASP   A CB  1 
ATOM   2333 C  CG  . ASP   A 1 337 ? -6.267  -32.536 -19.866 1.00 111.04 ? 357 ASP   A CG  1 
ATOM   2334 O  OD1 . ASP   A 1 337 ? -6.729  -32.078 -18.801 1.00 121.48 ? 357 ASP   A OD1 1 
ATOM   2335 O  OD2 . ASP   A 1 337 ? -5.564  -31.861 -20.651 1.00 108.09 ? 357 ASP   A OD2 1 
ATOM   2336 N  N   . MET   A 1 338 ? -8.299  -33.818 -22.905 1.00 118.91 ? 358 MET   A N   1 
ATOM   2337 C  CA  . MET   A 1 338 ? -8.737  -33.061 -24.074 1.00 123.23 ? 358 MET   A CA  1 
ATOM   2338 C  C   . MET   A 1 338 ? -10.257 -32.975 -24.137 1.00 117.11 ? 358 MET   A C   1 
ATOM   2339 O  O   . MET   A 1 338 ? -10.819 -31.890 -24.330 1.00 121.77 ? 358 MET   A O   1 
ATOM   2340 C  CB  . MET   A 1 338 ? -8.175  -33.696 -25.347 1.00 112.83 ? 358 MET   A CB  1 
ATOM   2341 C  CG  . MET   A 1 338 ? -6.673  -33.532 -25.503 1.00 122.57 ? 358 MET   A CG  1 
ATOM   2342 S  SD  . MET   A 1 338 ? -5.953  -34.727 -26.644 1.00 124.44 ? 358 MET   A SD  1 
ATOM   2343 C  CE  . MET   A 1 338 ? -6.875  -34.379 -28.139 1.00 130.01 ? 358 MET   A CE  1 
ATOM   2344 N  N   . VAL   A 1 339 ? -10.940 -34.111 -23.968 1.00 123.00 ? 359 VAL   A N   1 
ATOM   2345 C  CA  . VAL   A 1 339 ? -12.401 -34.127 -24.031 1.00 115.51 ? 359 VAL   A CA  1 
ATOM   2346 C  C   . VAL   A 1 339 ? -12.992 -33.229 -22.952 1.00 112.02 ? 359 VAL   A C   1 
ATOM   2347 O  O   . VAL   A 1 339 ? -13.959 -32.494 -23.194 1.00 108.32 ? 359 VAL   A O   1 
ATOM   2348 C  CB  . VAL   A 1 339 ? -12.926 -35.571 -23.912 1.00 109.87 ? 359 VAL   A CB  1 
ATOM   2349 C  CG1 . VAL   A 1 339 ? -14.433 -35.576 -23.717 1.00 112.08 ? 359 VAL   A CG1 1 
ATOM   2350 C  CG2 . VAL   A 1 339 ? -12.545 -36.381 -25.141 1.00 136.74 ? 359 VAL   A CG2 1 
ATOM   2351 N  N   . VAL   A 1 340 ? -12.419 -33.270 -21.748 1.00 108.74 ? 360 VAL   A N   1 
ATOM   2352 C  CA  . VAL   A 1 340 ? -12.896 -32.423 -20.657 1.00 107.17 ? 360 VAL   A CA  1 
ATOM   2353 C  C   . VAL   A 1 340 ? -12.738 -30.952 -21.018 1.00 109.40 ? 360 VAL   A C   1 
ATOM   2354 O  O   . VAL   A 1 340 ? -13.668 -30.151 -20.865 1.00 107.68 ? 360 VAL   A O   1 
ATOM   2355 C  CB  . VAL   A 1 340 ? -12.153 -32.761 -19.351 1.00 103.88 ? 360 VAL   A CB  1 
ATOM   2356 C  CG1 . VAL   A 1 340 ? -12.356 -31.658 -18.319 1.00 104.82 ? 360 VAL   A CG1 1 
ATOM   2357 C  CG2 . VAL   A 1 340 ? -12.620 -34.101 -18.804 1.00 101.51 ? 360 VAL   A CG2 1 
ATOM   2358 N  N   . ASN   A 1 341 ? -11.553 -30.576 -21.506 1.00 112.98 ? 361 ASN   A N   1 
ATOM   2359 C  CA  . ASN   A 1 341 ? -11.284 -29.177 -21.820 1.00 112.69 ? 361 ASN   A CA  1 
ATOM   2360 C  C   . ASN   A 1 341 ? -12.167 -28.675 -22.956 1.00 117.02 ? 361 ASN   A C   1 
ATOM   2361 O  O   . ASN   A 1 341 ? -12.668 -27.545 -22.904 1.00 107.04 ? 361 ASN   A O   1 
ATOM   2362 C  CB  . ASN   A 1 341 ? -9.807  -28.998 -22.165 1.00 111.37 ? 361 ASN   A CB  1 
ATOM   2363 C  CG  . ASN   A 1 341 ? -8.897  -29.295 -20.991 1.00 111.59 ? 361 ASN   A CG  1 
ATOM   2364 O  OD1 . ASN   A 1 341 ? -9.361  -29.611 -19.895 1.00 104.60 ? 361 ASN   A OD1 1 
ATOM   2365 N  ND2 . ASN   A 1 341 ? -7.593  -29.206 -21.217 1.00 102.88 ? 361 ASN   A ND2 1 
ATOM   2366 N  N   . GLU   A 1 342 ? -12.376 -29.497 -23.989 1.00 113.22 ? 362 GLU   A N   1 
ATOM   2367 C  CA  . GLU   A 1 342 ? -13.172 -29.049 -25.128 1.00 107.92 ? 362 GLU   A CA  1 
ATOM   2368 C  C   . GLU   A 1 342 ? -14.639 -28.881 -24.759 1.00 113.33 ? 362 GLU   A C   1 
ATOM   2369 O  O   . GLU   A 1 342 ? -15.306 -27.976 -25.275 1.00 118.18 ? 362 GLU   A O   1 
ATOM   2370 C  CB  . GLU   A 1 342 ? -13.020 -30.018 -26.305 1.00 111.82 ? 362 GLU   A CB  1 
ATOM   2371 C  CG  . GLU   A 1 342 ? -13.926 -29.725 -27.514 1.00 118.87 ? 362 GLU   A CG  1 
ATOM   2372 C  CD  . GLU   A 1 342 ? -13.525 -28.484 -28.310 1.00 118.25 ? 362 GLU   A CD  1 
ATOM   2373 O  OE1 . GLU   A 1 342 ? -12.880 -27.574 -27.747 1.00 108.48 ? 362 GLU   A OE1 1 
ATOM   2374 O  OE2 . GLU   A 1 342 ? -13.863 -28.421 -29.512 1.00 121.09 ? 362 GLU   A OE2 1 
ATOM   2375 N  N   . THR   A 1 343 ? -15.157 -29.733 -23.873 1.00 112.78 ? 363 THR   A N   1 
ATOM   2376 C  CA  . THR   A 1 343 ? -16.511 -29.532 -23.372 1.00 108.80 ? 363 THR   A CA  1 
ATOM   2377 C  C   . THR   A 1 343 ? -16.604 -28.247 -22.562 1.00 110.37 ? 363 THR   A C   1 
ATOM   2378 O  O   . THR   A 1 343 ? -17.580 -27.496 -22.682 1.00 102.51 ? 363 THR   A O   1 
ATOM   2379 C  CB  . THR   A 1 343 ? -16.945 -30.729 -22.526 1.00 100.63 ? 363 THR   A CB  1 
ATOM   2380 O  OG1 . THR   A 1 343 ? -16.886 -31.920 -23.319 1.00 121.62 ? 363 THR   A OG1 1 
ATOM   2381 C  CG2 . THR   A 1 343 ? -18.367 -30.531 -22.024 1.00 100.18 ? 363 THR   A CG2 1 
ATOM   2382 N  N   . LEU   A 1 344 ? -15.589 -27.970 -21.739 1.00 109.28 ? 364 LEU   A N   1 
ATOM   2383 C  CA  . LEU   A 1 344 ? -15.575 -26.732 -20.971 1.00 103.76 ? 364 LEU   A CA  1 
ATOM   2384 C  C   . LEU   A 1 344 ? -15.416 -25.504 -21.855 1.00 106.49 ? 364 LEU   A C   1 
ATOM   2385 O  O   . LEU   A 1 344 ? -15.757 -24.399 -21.420 1.00 95.46  ? 364 LEU   A O   1 
ATOM   2386 C  CB  . LEU   A 1 344 ? -14.465 -26.767 -19.922 1.00 96.64  ? 364 LEU   A CB  1 
ATOM   2387 C  CG  . LEU   A 1 344 ? -14.700 -27.743 -18.771 1.00 95.50  ? 364 LEU   A CG  1 
ATOM   2388 C  CD1 . LEU   A 1 344 ? -13.572 -27.637 -17.768 1.00 100.61 ? 364 LEU   A CD1 1 
ATOM   2389 C  CD2 . LEU   A 1 344 ? -16.043 -27.472 -18.108 1.00 93.46  ? 364 LEU   A CD2 1 
ATOM   2390 N  N   . ARG   A 1 345 ? -14.909 -25.664 -23.079 1.00 109.04 ? 365 ARG   A N   1 
ATOM   2391 C  CA  . ARG   A 1 345 ? -14.893 -24.539 -24.008 1.00 107.36 ? 365 ARG   A CA  1 
ATOM   2392 C  C   . ARG   A 1 345 ? -16.303 -24.215 -24.478 1.00 103.38 ? 365 ARG   A C   1 
ATOM   2393 O  O   . ARG   A 1 345 ? -16.727 -23.054 -24.462 1.00 103.95 ? 365 ARG   A O   1 
ATOM   2394 C  CB  . ARG   A 1 345 ? -13.988 -24.844 -25.203 1.00 110.73 ? 365 ARG   A CB  1 
ATOM   2395 C  CG  . ARG   A 1 345 ? -13.769 -23.652 -26.131 1.00 105.12 ? 365 ARG   A CG  1 
ATOM   2396 C  CD  . ARG   A 1 345 ? -13.040 -24.051 -27.406 1.00 113.12 ? 365 ARG   A CD  1 
ATOM   2397 N  NE  . ARG   A 1 345 ? -13.782 -25.048 -28.169 1.00 116.62 ? 365 ARG   A NE  1 
ATOM   2398 C  CZ  . ARG   A 1 345 ? -14.806 -24.774 -28.965 1.00 119.99 ? 365 ARG   A CZ  1 
ATOM   2399 N  NH1 . ARG   A 1 345 ? -15.251 -23.538 -29.120 1.00 116.36 ? 365 ARG   A NH1 1 
ATOM   2400 N  NH2 . ARG   A 1 345 ? -15.401 -25.767 -29.621 1.00 132.11 ? 365 ARG   A NH2 1 
ATOM   2401 N  N   . LEU   A 1 346 ? -17.049 -25.236 -24.890 1.00 105.26 ? 366 LEU   A N   1 
ATOM   2402 C  CA  . LEU   A 1 346 ? -18.402 -25.008 -25.377 1.00 109.17 ? 366 LEU   A CA  1 
ATOM   2403 C  C   . LEU   A 1 346 ? -19.357 -24.634 -24.250 1.00 105.15 ? 366 LEU   A C   1 
ATOM   2404 O  O   . LEU   A 1 346 ? -20.304 -23.872 -24.474 1.00 109.72 ? 366 LEU   A O   1 
ATOM   2405 C  CB  . LEU   A 1 346 ? -18.901 -26.249 -26.111 1.00 98.14  ? 366 LEU   A CB  1 
ATOM   2406 C  CG  . LEU   A 1 346 ? -18.314 -26.468 -27.506 1.00 109.72 ? 366 LEU   A CG  1 
ATOM   2407 C  CD1 . LEU   A 1 346 ? -18.916 -27.707 -28.146 1.00 121.21 ? 366 LEU   A CD1 1 
ATOM   2408 C  CD2 . LEU   A 1 346 ? -18.546 -25.244 -28.381 1.00 107.63 ? 366 LEU   A CD2 1 
ATOM   2409 N  N   . PHE   A 1 347 ? -19.126 -25.144 -23.042 1.00 103.78 ? 367 PHE   A N   1 
ATOM   2410 C  CA  . PHE   A 1 347 ? -20.031 -24.938 -21.912 1.00 104.59 ? 367 PHE   A CA  1 
ATOM   2411 C  C   . PHE   A 1 347 ? -19.260 -24.529 -20.661 1.00 104.19 ? 367 PHE   A C   1 
ATOM   2412 O  O   . PHE   A 1 347 ? -19.184 -25.285 -19.686 1.00 104.69 ? 367 PHE   A O   1 
ATOM   2413 C  CB  . PHE   A 1 347 ? -20.853 -26.200 -21.662 1.00 105.64 ? 367 PHE   A CB  1 
ATOM   2414 C  CG  . PHE   A 1 347 ? -21.452 -26.780 -22.908 1.00 113.06 ? 367 PHE   A CG  1 
ATOM   2415 C  CD1 . PHE   A 1 347 ? -22.547 -26.176 -23.507 1.00 118.47 ? 367 PHE   A CD1 1 
ATOM   2416 C  CD2 . PHE   A 1 347 ? -20.914 -27.920 -23.486 1.00 108.47 ? 367 PHE   A CD2 1 
ATOM   2417 C  CE1 . PHE   A 1 347 ? -23.104 -26.703 -24.655 1.00 114.17 ? 367 PHE   A CE1 1 
ATOM   2418 C  CE2 . PHE   A 1 347 ? -21.464 -28.456 -24.635 1.00 115.89 ? 367 PHE   A CE2 1 
ATOM   2419 C  CZ  . PHE   A 1 347 ? -22.563 -27.846 -25.222 1.00 126.86 ? 367 PHE   A CZ  1 
ATOM   2420 N  N   . PRO   A 1 348 ? -18.684 -23.318 -20.649 1.00 98.80  ? 368 PRO   A N   1 
ATOM   2421 C  CA  . PRO   A 1 348 ? -18.161 -22.780 -19.387 1.00 102.34 ? 368 PRO   A CA  1 
ATOM   2422 C  C   . PRO   A 1 348 ? -19.305 -22.368 -18.475 1.00 97.83  ? 368 PRO   A C   1 
ATOM   2423 O  O   . PRO   A 1 348 ? -19.926 -21.320 -18.682 1.00 117.09 ? 368 PRO   A O   1 
ATOM   2424 C  CB  . PRO   A 1 348 ? -17.319 -21.580 -19.837 1.00 105.69 ? 368 PRO   A CB  1 
ATOM   2425 C  CG  . PRO   A 1 348 ? -17.970 -21.130 -21.099 1.00 113.82 ? 368 PRO   A CG  1 
ATOM   2426 C  CD  . PRO   A 1 348 ? -18.481 -22.382 -21.771 1.00 107.55 ? 368 PRO   A CD  1 
ATOM   2427 N  N   . ILE   A 1 349 ? -19.590 -23.195 -17.464 1.00 103.14 ? 369 ILE   A N   1 
ATOM   2428 C  CA  . ILE   A 1 349 ? -20.771 -23.019 -16.622 1.00 109.40 ? 369 ILE   A CA  1 
ATOM   2429 C  C   . ILE   A 1 349 ? -20.841 -21.636 -15.990 1.00 103.45 ? 369 ILE   A C   1 
ATOM   2430 O  O   . ILE   A 1 349 ? -21.931 -21.175 -15.634 1.00 108.38 ? 369 ILE   A O   1 
ATOM   2431 C  CB  . ILE   A 1 349 ? -20.813 -24.110 -15.531 1.00 102.47 ? 369 ILE   A CB  1 
ATOM   2432 C  CG1 . ILE   A 1 349 ? -19.561 -24.040 -14.660 1.00 94.11  ? 369 ILE   A CG1 1 
ATOM   2433 C  CG2 . ILE   A 1 349 ? -20.955 -25.495 -16.148 1.00 115.10 ? 369 ILE   A CG2 1 
ATOM   2434 C  CD1 . ILE   A 1 349 ? -19.601 -24.983 -13.490 1.00 106.90 ? 369 ILE   A CD1 1 
ATOM   2435 N  N   . ALA   A 1 350 ? -19.698 -20.965 -15.829 1.00 94.85  ? 370 ALA   A N   1 
ATOM   2436 C  CA  . ALA   A 1 350 ? -19.682 -19.613 -15.282 1.00 98.98  ? 370 ALA   A CA  1 
ATOM   2437 C  C   . ALA   A 1 350 ? -20.155 -18.575 -16.290 1.00 99.24  ? 370 ALA   A C   1 
ATOM   2438 O  O   . ALA   A 1 350 ? -20.724 -17.553 -15.892 1.00 93.90  ? 370 ALA   A O   1 
ATOM   2439 C  CB  . ALA   A 1 350 ? -18.274 -19.255 -14.804 1.00 98.27  ? 370 ALA   A CB  1 
ATOM   2440 N  N   . MET   A 1 351 ? -19.910 -18.812 -17.582 1.00 89.98  ? 371 MET   A N   1 
ATOM   2441 C  CA  . MET   A 1 351 ? -20.280 -17.907 -18.669 1.00 102.25 ? 371 MET   A CA  1 
ATOM   2442 C  C   . MET   A 1 351 ? -19.454 -16.627 -18.588 1.00 94.97  ? 371 MET   A C   1 
ATOM   2443 O  O   . MET   A 1 351 ? -18.829 -16.224 -19.575 1.00 87.38  ? 371 MET   A O   1 
ATOM   2444 C  CB  . MET   A 1 351 ? -21.792 -17.649 -18.667 1.00 96.50  ? 371 MET   A CB  1 
ATOM   2445 C  CG  . MET   A 1 351 ? -22.641 -18.864 -19.010 1.00 112.11 ? 371 MET   A CG  1 
ATOM   2446 S  SD  . MET   A 1 351 ? -24.401 -18.597 -18.708 1.00 127.42 ? 371 MET   A SD  1 
ATOM   2447 C  CE  . MET   A 1 351 ? -24.417 -18.371 -16.930 1.00 104.55 ? 371 MET   A CE  1 
ATOM   2448 N  N   . ARG   A 1 352 ? -19.446 -15.975 -17.428 1.00 89.79  ? 372 ARG   A N   1 
ATOM   2449 C  CA  . ARG   A 1 352 ? -18.823 -14.670 -17.271 1.00 90.22  ? 372 ARG   A CA  1 
ATOM   2450 C  C   . ARG   A 1 352 ? -17.928 -14.659 -16.043 1.00 85.46  ? 372 ARG   A C   1 
ATOM   2451 O  O   . ARG   A 1 352 ? -18.265 -15.249 -15.012 1.00 85.55  ? 372 ARG   A O   1 
ATOM   2452 C  CB  . ARG   A 1 352 ? -19.871 -13.559 -17.137 1.00 95.55  ? 372 ARG   A CB  1 
ATOM   2453 C  CG  . ARG   A 1 352 ? -20.707 -13.301 -18.376 1.00 90.19  ? 372 ARG   A CG  1 
ATOM   2454 C  CD  . ARG   A 1 352 ? -21.934 -12.485 -17.999 1.00 100.62 ? 372 ARG   A CD  1 
ATOM   2455 N  NE  . ARG   A 1 352 ? -22.430 -11.668 -19.100 1.00 106.96 ? 372 ARG   A NE  1 
ATOM   2456 C  CZ  . ARG   A 1 352 ? -23.337 -10.710 -18.967 1.00 104.38 ? 372 ARG   A CZ  1 
ATOM   2457 N  NH1 . ARG   A 1 352 ? -23.856 -10.410 -17.787 1.00 104.00 ? 372 ARG   A NH1 1 
ATOM   2458 N  NH2 . ARG   A 1 352 ? -23.725 -10.030 -20.041 1.00 98.62  ? 372 ARG   A NH2 1 
ATOM   2459 N  N   . LEU   A 1 353 ? -16.793 -13.979 -16.164 1.00 90.46  ? 373 LEU   A N   1 
ATOM   2460 C  CA  . LEU   A 1 353 ? -15.943 -13.641 -15.033 1.00 86.92  ? 373 LEU   A CA  1 
ATOM   2461 C  C   . LEU   A 1 353 ? -16.110 -12.158 -14.726 1.00 85.16  ? 373 LEU   A C   1 
ATOM   2462 O  O   . LEU   A 1 353 ? -16.189 -11.335 -15.642 1.00 82.20  ? 373 LEU   A O   1 
ATOM   2463 C  CB  . LEU   A 1 353 ? -14.477 -13.953 -15.334 1.00 90.01  ? 373 LEU   A CB  1 
ATOM   2464 C  CG  . LEU   A 1 353 ? -14.150 -15.383 -15.763 1.00 87.69  ? 373 LEU   A CG  1 
ATOM   2465 C  CD1 . LEU   A 1 353 ? -12.684 -15.496 -16.138 1.00 94.42  ? 373 LEU   A CD1 1 
ATOM   2466 C  CD2 . LEU   A 1 353 ? -14.494 -16.352 -14.650 1.00 65.34  ? 373 LEU   A CD2 1 
ATOM   2467 N  N   . GLU   A 1 354 ? -16.171 -11.818 -13.439 1.00 80.06  ? 374 GLU   A N   1 
ATOM   2468 C  CA  . GLU   A 1 354 ? -16.462 -10.449 -13.033 1.00 84.11  ? 374 GLU   A CA  1 
ATOM   2469 C  C   . GLU   A 1 354 ? -15.507 -9.993  -11.940 1.00 87.56  ? 374 GLU   A C   1 
ATOM   2470 O  O   . GLU   A 1 354 ? -15.100 -10.778 -11.079 1.00 85.68  ? 374 GLU   A O   1 
ATOM   2471 C  CB  . GLU   A 1 354 ? -17.906 -10.298 -12.540 1.00 80.34  ? 374 GLU   A CB  1 
ATOM   2472 C  CG  . GLU   A 1 354 ? -18.949 -10.373 -13.637 1.00 91.81  ? 374 GLU   A CG  1 
ATOM   2473 C  CD  . GLU   A 1 354 ? -20.338 -10.049 -13.142 1.00 96.59  ? 374 GLU   A CD  1 
ATOM   2474 O  OE1 . GLU   A 1 354 ? -20.508 -9.886  -11.913 1.00 105.68 ? 374 GLU   A OE1 1 
ATOM   2475 O  OE2 . GLU   A 1 354 ? -21.255 -9.955  -13.985 1.00 92.21  ? 374 GLU   A OE2 1 
ATOM   2476 N  N   . ARG   A 1 355 ? -15.171 -8.703  -11.979 1.00 84.78  ? 375 ARG   A N   1 
ATOM   2477 C  CA  . ARG   A 1 355 ? -14.356 -8.058  -10.957 1.00 87.26  ? 375 ARG   A CA  1 
ATOM   2478 C  C   . ARG   A 1 355 ? -14.830 -6.620  -10.806 1.00 85.58  ? 375 ARG   A C   1 
ATOM   2479 O  O   . ARG   A 1 355 ? -14.965 -5.910  -11.806 1.00 95.72  ? 375 ARG   A O   1 
ATOM   2480 C  CB  . ARG   A 1 355 ? -12.866 -8.071  -11.321 1.00 88.10  ? 375 ARG   A CB  1 
ATOM   2481 C  CG  . ARG   A 1 355 ? -12.224 -9.438  -11.462 1.00 79.86  ? 375 ARG   A CG  1 
ATOM   2482 C  CD  . ARG   A 1 355 ? -12.096 -10.143 -10.126 1.00 68.05  ? 375 ARG   A CD  1 
ATOM   2483 N  NE  . ARG   A 1 355 ? -11.347 -11.386 -10.259 1.00 98.26  ? 375 ARG   A NE  1 
ATOM   2484 C  CZ  . ARG   A 1 355 ? -11.867 -12.531 -10.679 1.00 87.73  ? 375 ARG   A CZ  1 
ATOM   2485 N  NH1 . ARG   A 1 355 ? -13.145 -12.633 -11.004 1.00 79.41  ? 375 ARG   A NH1 1 
ATOM   2486 N  NH2 . ARG   A 1 355 ? -11.083 -13.601 -10.778 1.00 87.22  ? 375 ARG   A NH2 1 
ATOM   2487 N  N   . VAL   A 1 356 ? -15.066 -6.184  -9.573  1.00 88.64  ? 376 VAL   A N   1 
ATOM   2488 C  CA  . VAL   A 1 356 ? -15.402 -4.784  -9.334  1.00 93.43  ? 376 VAL   A CA  1 
ATOM   2489 C  C   . VAL   A 1 356 ? -14.114 -3.972  -9.298  1.00 93.97  ? 376 VAL   A C   1 
ATOM   2490 O  O   . VAL   A 1 356 ? -13.164 -4.325  -8.590  1.00 94.09  ? 376 VAL   A O   1 
ATOM   2491 C  CB  . VAL   A 1 356 ? -16.199 -4.619  -8.030  1.00 99.72  ? 376 VAL   A CB  1 
ATOM   2492 C  CG1 . VAL   A 1 356 ? -16.462 -3.148  -7.770  1.00 93.41  ? 376 VAL   A CG1 1 
ATOM   2493 C  CG2 . VAL   A 1 356 ? -17.511 -5.380  -8.103  1.00 96.87  ? 376 VAL   A CG2 1 
ATOM   2494 N  N   . CYS   A 1 357 ? -14.067 -2.890  -10.069 1.00 97.94  ? 377 CYS   A N   1 
ATOM   2495 C  CA  . CYS   A 1 357 ? -12.900 -2.013  -10.065 1.00 108.36 ? 377 CYS   A CA  1 
ATOM   2496 C  C   . CYS   A 1 357 ? -13.027 -1.066  -8.879  1.00 95.91  ? 377 CYS   A C   1 
ATOM   2497 O  O   . CYS   A 1 357 ? -13.916 -0.209  -8.856  1.00 104.68 ? 377 CYS   A O   1 
ATOM   2498 C  CB  . CYS   A 1 357 ? -12.795 -1.259  -11.389 1.00 98.15  ? 377 CYS   A CB  1 
ATOM   2499 S  SG  . CYS   A 1 357 ? -11.601 0.107   -11.454 1.00 105.47 ? 377 CYS   A SG  1 
ATOM   2500 N  N   . LYS   A 1 358 ? -12.151 -1.225  -7.884  1.00 95.08  ? 378 LYS   A N   1 
ATOM   2501 C  CA  . LYS   A 1 358 ? -12.312 -0.551  -6.599  1.00 106.77 ? 378 LYS   A CA  1 
ATOM   2502 C  C   . LYS   A 1 358 ? -11.666 0.830   -6.546  1.00 101.64 ? 378 LYS   A C   1 
ATOM   2503 O  O   . LYS   A 1 358 ? -11.758 1.493   -5.508  1.00 100.67 ? 378 LYS   A O   1 
ATOM   2504 C  CB  . LYS   A 1 358 ? -11.763 -1.426  -5.463  1.00 102.81 ? 378 LYS   A CB  1 
ATOM   2505 C  CG  . LYS   A 1 358 ? -10.250 -1.431  -5.329  1.00 105.41 ? 378 LYS   A CG  1 
ATOM   2506 C  CD  . LYS   A 1 358 ? -9.804  -2.045  -4.008  1.00 111.49 ? 378 LYS   A CD  1 
ATOM   2507 C  CE  . LYS   A 1 358 ? -9.826  -3.565  -4.041  1.00 111.07 ? 378 LYS   A CE  1 
ATOM   2508 N  NZ  . LYS   A 1 358 ? -9.032  -4.127  -2.909  1.00 109.23 ? 378 LYS   A NZ  1 
ATOM   2509 N  N   . LYS   A 1 359 ? -11.027 1.283   -7.624  1.00 102.03 ? 379 LYS   A N   1 
ATOM   2510 C  CA  . LYS   A 1 359 ? -10.511 2.648   -7.678  1.00 111.89 ? 379 LYS   A CA  1 
ATOM   2511 C  C   . LYS   A 1 359 ? -10.084 2.970   -9.102  1.00 114.22 ? 379 LYS   A C   1 
ATOM   2512 O  O   . LYS   A 1 359 ? -9.827  2.071   -9.909  1.00 115.39 ? 379 LYS   A O   1 
ATOM   2513 C  CB  . LYS   A 1 359 ? -9.339  2.856   -6.708  1.00 107.24 ? 379 LYS   A CB  1 
ATOM   2514 C  CG  . LYS   A 1 359 ? -8.115  2.003   -6.975  1.00 106.43 ? 379 LYS   A CG  1 
ATOM   2515 C  CD  . LYS   A 1 359 ? -7.073  2.223   -5.887  1.00 106.68 ? 379 LYS   A CD  1 
ATOM   2516 C  CE  . LYS   A 1 359 ? -5.799  1.435   -6.147  1.00 97.78  ? 379 LYS   A CE  1 
ATOM   2517 N  NZ  . LYS   A 1 359 ? -4.803  1.628   -5.054  1.00 103.27 ? 379 LYS   A NZ  1 
ATOM   2518 N  N   . ASP   A 1 360 ? -10.009 4.270   -9.395  1.00 107.64 ? 380 ASP   A N   1 
ATOM   2519 C  CA  . ASP   A 1 360 ? -9.622  4.737   -10.721 1.00 116.42 ? 380 ASP   A CA  1 
ATOM   2520 C  C   . ASP   A 1 360 ? -8.295  4.124   -11.146 1.00 117.29 ? 380 ASP   A C   1 
ATOM   2521 O  O   . ASP   A 1 360 ? -7.338  4.080   -10.369 1.00 116.87 ? 380 ASP   A O   1 
ATOM   2522 C  CB  . ASP   A 1 360 ? -9.511  6.265   -10.740 1.00 105.36 ? 380 ASP   A CB  1 
ATOM   2523 C  CG  . ASP   A 1 360 ? -10.849 6.961   -10.573 1.00 123.36 ? 380 ASP   A CG  1 
ATOM   2524 O  OD1 . ASP   A 1 360 ? -11.832 6.299   -10.178 1.00 125.50 ? 380 ASP   A OD1 1 
ATOM   2525 O  OD2 . ASP   A 1 360 ? -10.914 8.180   -10.840 1.00 129.60 ? 380 ASP   A OD2 1 
ATOM   2526 N  N   . VAL   A 1 361 ? -8.241  3.657   -12.392 1.00 127.37 ? 381 VAL   A N   1 
ATOM   2527 C  CA  . VAL   A 1 361 ? -7.048  3.035   -12.952 1.00 132.99 ? 381 VAL   A CA  1 
ATOM   2528 C  C   . VAL   A 1 361 ? -6.978  3.349   -14.441 1.00 142.36 ? 381 VAL   A C   1 
ATOM   2529 O  O   . VAL   A 1 361 ? -7.912  3.895   -15.032 1.00 143.79 ? 381 VAL   A O   1 
ATOM   2530 C  CB  . VAL   A 1 361 ? -7.022  1.507   -12.730 1.00 128.98 ? 381 VAL   A CB  1 
ATOM   2531 C  CG1 . VAL   A 1 361 ? -6.389  1.178   -11.394 1.00 129.68 ? 381 VAL   A CG1 1 
ATOM   2532 C  CG2 . VAL   A 1 361 ? -8.427  0.941   -12.811 1.00 125.14 ? 381 VAL   A CG2 1 
ATOM   2533 N  N   . GLU   A 1 362 ? -5.845  2.995   -15.047 1.00 172.68 ? 382 GLU   A N   1 
ATOM   2534 C  CA  . GLU   A 1 362 ? -5.608  3.157   -16.483 1.00 180.40 ? 382 GLU   A CA  1 
ATOM   2535 C  C   . GLU   A 1 362 ? -4.858  1.904   -16.934 1.00 174.52 ? 382 GLU   A C   1 
ATOM   2536 O  O   . GLU   A 1 362 ? -3.625  1.888   -16.991 1.00 184.03 ? 382 GLU   A O   1 
ATOM   2537 C  CB  . GLU   A 1 362 ? -4.830  4.433   -16.777 1.00 197.52 ? 382 GLU   A CB  1 
ATOM   2538 C  CG  . GLU   A 1 362 ? -4.533  4.673   -18.248 1.00 199.79 ? 382 GLU   A CG  1 
ATOM   2539 C  CD  . GLU   A 1 362 ? -3.832  5.995   -18.486 1.00 213.11 ? 382 GLU   A CD  1 
ATOM   2540 O  OE1 . GLU   A 1 362 ? -3.990  6.909   -17.650 1.00 215.97 ? 382 GLU   A OE1 1 
ATOM   2541 O  OE2 . GLU   A 1 362 ? -3.120  6.117   -19.505 1.00 220.73 ? 382 GLU   A OE2 1 
ATOM   2542 N  N   . ILE   A 1 363 ? -5.608  0.850   -17.240 1.00 154.23 ? 383 ILE   A N   1 
ATOM   2543 C  CA  . ILE   A 1 363 ? -5.032  -0.445  -17.577 1.00 149.16 ? 383 ILE   A CA  1 
ATOM   2544 C  C   . ILE   A 1 363 ? -4.913  -0.556  -19.093 1.00 147.43 ? 383 ILE   A C   1 
ATOM   2545 O  O   . ILE   A 1 363 ? -5.851  -0.218  -19.828 1.00 144.37 ? 383 ILE   A O   1 
ATOM   2546 C  CB  . ILE   A 1 363 ? -5.862  -1.597  -16.978 1.00 147.57 ? 383 ILE   A CB  1 
ATOM   2547 C  CG1 . ILE   A 1 363 ? -7.142  -1.857  -17.778 1.00 136.29 ? 383 ILE   A CG1 1 
ATOM   2548 C  CG2 . ILE   A 1 363 ? -6.227  -1.283  -15.532 1.00 141.38 ? 383 ILE   A CG2 1 
ATOM   2549 C  CD1 . ILE   A 1 363 ? -7.986  -2.985  -17.230 1.00 119.79 ? 383 ILE   A CD1 1 
ATOM   2550 N  N   . ASN   A 1 364 ? -3.737  -0.989  -19.558 1.00 146.91 ? 384 ASN   A N   1 
ATOM   2551 C  CA  . ASN   A 1 364 ? -3.461  -1.203  -20.983 1.00 140.77 ? 384 ASN   A CA  1 
ATOM   2552 C  C   . ASN   A 1 364 ? -3.881  -0.010  -21.844 1.00 138.39 ? 384 ASN   A C   1 
ATOM   2553 O  O   . ASN   A 1 364 ? -4.291  -0.171  -22.996 1.00 143.07 ? 384 ASN   A O   1 
ATOM   2554 C  CB  . ASN   A 1 364 ? -4.123  -2.488  -21.482 1.00 148.04 ? 384 ASN   A CB  1 
ATOM   2555 C  CG  . ASN   A 1 364 ? -3.336  -3.730  -21.111 1.00 139.90 ? 384 ASN   A CG  1 
ATOM   2556 O  OD1 . ASN   A 1 364 ? -3.528  -4.310  -20.042 1.00 133.33 ? 384 ASN   A OD1 1 
ATOM   2557 N  ND2 . ASN   A 1 364 ? -2.444  -4.148  -22.001 1.00 134.12 ? 384 ASN   A ND2 1 
ATOM   2558 N  N   . GLY   A 1 365 ? -3.780  1.195   -21.290 1.00 139.38 ? 385 GLY   A N   1 
ATOM   2559 C  CA  . GLY   A 1 365 ? -4.111  2.392   -22.037 1.00 146.24 ? 385 GLY   A CA  1 
ATOM   2560 C  C   . GLY   A 1 365 ? -5.581  2.740   -22.099 1.00 146.55 ? 385 GLY   A C   1 
ATOM   2561 O  O   . GLY   A 1 365 ? -6.015  3.376   -23.065 1.00 150.36 ? 385 GLY   A O   1 
ATOM   2562 N  N   . MET   A 1 366 ? -6.364  2.348   -21.095 1.00 149.63 ? 386 MET   A N   1 
ATOM   2563 C  CA  . MET   A 1 366 ? -7.787  2.667   -21.041 1.00 143.89 ? 386 MET   A CA  1 
ATOM   2564 C  C   . MET   A 1 366 ? -8.147  3.055   -19.617 1.00 140.71 ? 386 MET   A C   1 
ATOM   2565 O  O   . MET   A 1 366 ? -7.976  2.255   -18.692 1.00 128.21 ? 386 MET   A O   1 
ATOM   2566 C  CB  . MET   A 1 366 ? -8.644  1.485   -21.506 1.00 138.19 ? 386 MET   A CB  1 
ATOM   2567 C  CG  . MET   A 1 366 ? -10.142 1.718   -21.373 1.00 133.14 ? 386 MET   A CG  1 
ATOM   2568 S  SD  . MET   A 1 366 ? -11.105 0.341   -22.021 1.00 136.63 ? 386 MET   A SD  1 
ATOM   2569 C  CE  . MET   A 1 366 ? -10.379 0.197   -23.650 1.00 133.54 ? 386 MET   A CE  1 
ATOM   2570 N  N   . PHE   A 1 367 ? -8.641  4.277   -19.443 1.00 129.48 ? 387 PHE   A N   1 
ATOM   2571 C  CA  . PHE   A 1 367 ? -9.083  4.723   -18.131 1.00 128.89 ? 387 PHE   A CA  1 
ATOM   2572 C  C   . PHE   A 1 367 ? -10.353 3.986   -17.719 1.00 127.41 ? 387 PHE   A C   1 
ATOM   2573 O  O   . PHE   A 1 367 ? -11.285 3.830   -18.514 1.00 123.02 ? 387 PHE   A O   1 
ATOM   2574 C  CB  . PHE   A 1 367 ? -9.325  6.231   -18.142 1.00 128.20 ? 387 PHE   A CB  1 
ATOM   2575 C  CG  . PHE   A 1 367 ? -9.928  6.758   -16.874 1.00 138.79 ? 387 PHE   A CG  1 
ATOM   2576 C  CD1 . PHE   A 1 367 ? -9.134  7.011   -15.769 1.00 135.01 ? 387 PHE   A CD1 1 
ATOM   2577 C  CD2 . PHE   A 1 367 ? -11.288 7.008   -16.789 1.00 126.24 ? 387 PHE   A CD2 1 
ATOM   2578 C  CE1 . PHE   A 1 367 ? -9.683  7.498   -14.599 1.00 132.11 ? 387 PHE   A CE1 1 
ATOM   2579 C  CE2 . PHE   A 1 367 ? -11.845 7.495   -15.622 1.00 129.05 ? 387 PHE   A CE2 1 
ATOM   2580 C  CZ  . PHE   A 1 367 ? -11.040 7.741   -14.524 1.00 129.52 ? 387 PHE   A CZ  1 
ATOM   2581 N  N   . ILE   A 1 368 ? -10.389 3.532   -16.465 1.00 130.25 ? 388 ILE   A N   1 
ATOM   2582 C  CA  . ILE   A 1 368 ? -11.525 2.799   -15.928 1.00 125.13 ? 388 ILE   A CA  1 
ATOM   2583 C  C   . ILE   A 1 368 ? -11.932 3.424   -14.600 1.00 122.22 ? 388 ILE   A C   1 
ATOM   2584 O  O   . ILE   A 1 368 ? -11.132 3.448   -13.659 1.00 122.54 ? 388 ILE   A O   1 
ATOM   2585 C  CB  . ILE   A 1 368 ? -11.210 1.304   -15.745 1.00 125.16 ? 388 ILE   A CB  1 
ATOM   2586 C  CG1 . ILE   A 1 368 ? -10.954 0.654   -17.106 1.00 119.79 ? 388 ILE   A CG1 1 
ATOM   2587 C  CG2 . ILE   A 1 368 ? -12.342 0.595   -15.023 1.00 115.84 ? 388 ILE   A CG2 1 
ATOM   2588 C  CD1 . ILE   A 1 368 ? -10.882 -0.850  -17.054 1.00 96.99  ? 388 ILE   A CD1 1 
ATOM   2589 N  N   . PRO   A 1 369 ? -13.152 3.938   -14.465 1.00 121.75 ? 389 PRO   A N   1 
ATOM   2590 C  CA  . PRO   A 1 369 ? -13.520 4.650   -13.238 1.00 121.48 ? 389 PRO   A CA  1 
ATOM   2591 C  C   . PRO   A 1 369 ? -13.936 3.704   -12.123 1.00 117.45 ? 389 PRO   A C   1 
ATOM   2592 O  O   . PRO   A 1 369 ? -14.429 2.598   -12.358 1.00 113.93 ? 389 PRO   A O   1 
ATOM   2593 C  CB  . PRO   A 1 369 ? -14.696 5.538   -13.676 1.00 113.12 ? 389 PRO   A CB  1 
ATOM   2594 C  CG  . PRO   A 1 369 ? -14.951 5.216   -15.145 1.00 118.86 ? 389 PRO   A CG  1 
ATOM   2595 C  CD  . PRO   A 1 369 ? -14.254 3.928   -15.438 1.00 114.95 ? 389 PRO   A CD  1 
ATOM   2596 N  N   . LYS   A 1 370 ? -13.724 4.168   -10.891 1.00 112.26 ? 390 LYS   A N   1 
ATOM   2597 C  CA  . LYS   A 1 370 ? -14.062 3.385   -9.708  1.00 106.16 ? 390 LYS   A CA  1 
ATOM   2598 C  C   . LYS   A 1 370 ? -15.549 3.047   -9.689  1.00 106.78 ? 390 LYS   A C   1 
ATOM   2599 O  O   . LYS   A 1 370 ? -16.399 3.888   -9.994  1.00 97.95  ? 390 LYS   A O   1 
ATOM   2600 C  CB  . LYS   A 1 370 ? -13.679 4.161   -8.445  1.00 110.71 ? 390 LYS   A CB  1 
ATOM   2601 C  CG  . LYS   A 1 370 ? -14.196 3.564   -7.146  1.00 108.82 ? 390 LYS   A CG  1 
ATOM   2602 C  CD  . LYS   A 1 370 ? -13.771 4.400   -5.949  1.00 107.13 ? 390 LYS   A CD  1 
ATOM   2603 C  CE  . LYS   A 1 370 ? -14.332 3.838   -4.654  1.00 106.28 ? 390 LYS   A CE  1 
ATOM   2604 N  NZ  . LYS   A 1 370 ? -13.888 4.637   -3.481  1.00 127.29 ? 390 LYS   A NZ  1 
ATOM   2605 N  N   . GLY   A 1 371 ? -15.860 1.799   -9.336  1.00 107.90 ? 391 GLY   A N   1 
ATOM   2606 C  CA  . GLY   A 1 371 ? -17.221 1.327   -9.254  1.00 99.94  ? 391 GLY   A CA  1 
ATOM   2607 C  C   . GLY   A 1 371 ? -17.691 0.531   -10.454 1.00 94.64  ? 391 GLY   A C   1 
ATOM   2608 O  O   . GLY   A 1 371 ? -18.689 -0.193  -10.349 1.00 93.86  ? 391 GLY   A O   1 
ATOM   2609 N  N   . VAL   A 1 372 ? -17.005 0.653   -11.588 1.00 96.68  ? 392 VAL   A N   1 
ATOM   2610 C  CA  . VAL   A 1 372 ? -17.362 -0.117  -12.771 1.00 98.30  ? 392 VAL   A CA  1 
ATOM   2611 C  C   . VAL   A 1 372 ? -17.100 -1.595  -12.517 1.00 89.37  ? 392 VAL   A C   1 
ATOM   2612 O  O   . VAL   A 1 372 ? -16.090 -1.974  -11.907 1.00 99.69  ? 392 VAL   A O   1 
ATOM   2613 C  CB  . VAL   A 1 372 ? -16.578 0.398   -13.990 1.00 105.61 ? 392 VAL   A CB  1 
ATOM   2614 C  CG1 . VAL   A 1 372 ? -16.680 -0.568  -15.160 1.00 96.31  ? 392 VAL   A CG1 1 
ATOM   2615 C  CG2 . VAL   A 1 372 ? -17.092 1.766   -14.390 1.00 104.30 ? 392 VAL   A CG2 1 
ATOM   2616 N  N   . VAL   A 1 373 ? -18.032 -2.436  -12.956 1.00 89.38  ? 393 VAL   A N   1 
ATOM   2617 C  CA  . VAL   A 1 373 ? -17.864 -3.884  -12.922 1.00 88.58  ? 393 VAL   A CA  1 
ATOM   2618 C  C   . VAL   A 1 373 ? -17.256 -4.312  -14.252 1.00 89.03  ? 393 VAL   A C   1 
ATOM   2619 O  O   . VAL   A 1 373 ? -17.910 -4.244  -15.296 1.00 92.12  ? 393 VAL   A O   1 
ATOM   2620 C  CB  . VAL   A 1 373 ? -19.193 -4.602  -12.658 1.00 98.22  ? 393 VAL   A CB  1 
ATOM   2621 C  CG1 . VAL   A 1 373 ? -19.051 -6.097  -12.915 1.00 85.39  ? 393 VAL   A CG1 1 
ATOM   2622 C  CG2 . VAL   A 1 373 ? -19.650 -4.356  -11.232 1.00 88.21  ? 393 VAL   A CG2 1 
ATOM   2623 N  N   . VAL   A 1 374 ? -15.996 -4.734  -14.214 1.00 82.42  ? 394 VAL   A N   1 
ATOM   2624 C  CA  . VAL   A 1 374 ? -15.325 -5.291  -15.381 1.00 83.03  ? 394 VAL   A CA  1 
ATOM   2625 C  C   . VAL   A 1 374 ? -15.800 -6.721  -15.584 1.00 78.35  ? 394 VAL   A C   1 
ATOM   2626 O  O   . VAL   A 1 374 ? -16.011 -7.465  -14.620 1.00 81.37  ? 394 VAL   A O   1 
ATOM   2627 C  CB  . VAL   A 1 374 ? -13.797 -5.220  -15.208 1.00 94.16  ? 394 VAL   A CB  1 
ATOM   2628 C  CG1 . VAL   A 1 374 ? -13.090 -5.901  -16.370 1.00 89.57  ? 394 VAL   A CG1 1 
ATOM   2629 C  CG2 . VAL   A 1 374 ? -13.355 -3.774  -15.093 1.00 95.89  ? 394 VAL   A CG2 1 
ATOM   2630 N  N   . MET   A 1 375 ? -15.973 -7.114  -16.844 1.00 80.46  ? 395 MET   A N   1 
ATOM   2631 C  CA  A MET   A 1 375 ? -16.533 -8.412  -17.180 0.58 91.57  ? 395 MET   A CA  1 
ATOM   2632 C  CA  B MET   A 1 375 ? -16.529 -8.415  -17.176 0.42 90.23  ? 395 MET   A CA  1 
ATOM   2633 C  C   . MET   A 1 375 ? -15.737 -9.039  -18.312 1.00 84.34  ? 395 MET   A C   1 
ATOM   2634 O  O   . MET   A 1 375 ? -15.364 -8.356  -19.268 1.00 86.62  ? 395 MET   A O   1 
ATOM   2635 C  CB  A MET   A 1 375 ? -18.006 -8.283  -17.589 0.58 90.30  ? 395 MET   A CB  1 
ATOM   2636 C  CB  B MET   A 1 375 ? -18.003 -8.304  -17.581 0.42 89.23  ? 395 MET   A CB  1 
ATOM   2637 C  CG  A MET   A 1 375 ? -18.755 -9.600  -17.691 0.58 86.02  ? 395 MET   A CG  1 
ATOM   2638 C  CG  B MET   A 1 375 ? -18.713 -9.638  -17.751 0.42 89.84  ? 395 MET   A CG  1 
ATOM   2639 S  SD  A MET   A 1 375 ? -18.744 -10.309 -19.349 0.58 77.56  ? 395 MET   A SD  1 
ATOM   2640 S  SD  B MET   A 1 375 ? -20.268 -9.464  -18.643 0.42 100.25 ? 395 MET   A SD  1 
ATOM   2641 C  CE  A MET   A 1 375 ? -19.705 -9.098  -20.250 0.58 89.98  ? 395 MET   A CE  1 
ATOM   2642 C  CE  B MET   A 1 375 ? -19.675 -9.091  -20.290 0.42 92.58  ? 395 MET   A CE  1 
ATOM   2643 N  N   . ILE   A 1 376 ? -15.492 -10.340 -18.195 1.00 80.79  ? 396 ILE   A N   1 
ATOM   2644 C  CA  . ILE   A 1 376 ? -14.840 -11.165 -19.204 1.00 88.40  ? 396 ILE   A CA  1 
ATOM   2645 C  C   . ILE   A 1 376 ? -15.893 -12.124 -19.754 1.00 87.61  ? 396 ILE   A C   1 
ATOM   2646 O  O   . ILE   A 1 376 ? -16.307 -13.055 -19.048 1.00 87.55  ? 396 ILE   A O   1 
ATOM   2647 C  CB  . ILE   A 1 376 ? -13.642 -11.937 -18.631 1.00 102.56 ? 396 ILE   A CB  1 
ATOM   2648 C  CG1 . ILE   A 1 376 ? -12.466 -11.006 -18.305 1.00 87.67  ? 396 ILE   A CG1 1 
ATOM   2649 C  CG2 . ILE   A 1 376 ? -13.170 -12.997 -19.614 1.00 86.93  ? 396 ILE   A CG2 1 
ATOM   2650 C  CD1 . ILE   A 1 376 ? -12.520 -10.340 -16.922 1.00 88.92  ? 396 ILE   A CD1 1 
ATOM   2651 N  N   . PRO   A 1 377 ? -16.366 -11.937 -20.989 1.00 83.74  ? 397 PRO   A N   1 
ATOM   2652 C  CA  . PRO   A 1 377 ? -17.394 -12.829 -21.579 1.00 89.78  ? 397 PRO   A CA  1 
ATOM   2653 C  C   . PRO   A 1 377 ? -16.788 -14.171 -21.975 1.00 80.79  ? 397 PRO   A C   1 
ATOM   2654 O  O   . PRO   A 1 377 ? -16.515 -14.446 -23.141 1.00 87.02  ? 397 PRO   A O   1 
ATOM   2655 C  CB  . PRO   A 1 377 ? -17.877 -12.026 -22.791 1.00 94.41  ? 397 PRO   A CB  1 
ATOM   2656 C  CG  . PRO   A 1 377 ? -16.706 -11.233 -23.202 1.00 97.69  ? 397 PRO   A CG  1 
ATOM   2657 C  CD  . PRO   A 1 377 ? -15.953 -10.885 -21.941 1.00 90.40  ? 397 PRO   A CD  1 
ATOM   2658 N  N   . SER   A 1 378 ? -16.584 -15.007 -20.952 1.00 84.62  ? 398 SER   A N   1 
ATOM   2659 C  CA  . SER   A 1 378 ? -15.943 -16.306 -21.135 1.00 90.33  ? 398 SER   A CA  1 
ATOM   2660 C  C   . SER   A 1 378 ? -16.651 -17.140 -22.196 1.00 94.60  ? 398 SER   A C   1 
ATOM   2661 O  O   . SER   A 1 378 ? -15.997 -17.762 -23.042 1.00 94.30  ? 398 SER   A O   1 
ATOM   2662 C  CB  . SER   A 1 378 ? -15.895 -17.051 -19.801 1.00 87.28  ? 398 SER   A CB  1 
ATOM   2663 O  OG  . SER   A 1 378 ? -15.000 -16.401 -18.913 1.00 100.25 ? 398 SER   A OG  1 
ATOM   2664 N  N   . TYR   A 1 379 ? -17.986 -17.144 -22.191 1.00 92.28  ? 399 TYR   A N   1 
ATOM   2665 C  CA  . TYR   A 1 379 ? -18.714 -17.899 -23.205 1.00 95.22  ? 399 TYR   A CA  1 
ATOM   2666 C  C   . TYR   A 1 379 ? -18.436 -17.350 -24.598 1.00 99.82  ? 399 TYR   A C   1 
ATOM   2667 O  O   . TYR   A 1 379 ? -18.135 -18.107 -25.527 1.00 106.64 ? 399 TYR   A O   1 
ATOM   2668 C  CB  . TYR   A 1 379 ? -20.211 -17.870 -22.909 1.00 93.16  ? 399 TYR   A CB  1 
ATOM   2669 C  CG  . TYR   A 1 379 ? -21.034 -18.671 -23.892 1.00 93.43  ? 399 TYR   A CG  1 
ATOM   2670 C  CD1 . TYR   A 1 379 ? -21.461 -18.113 -25.093 1.00 111.60 ? 399 TYR   A CD1 1 
ATOM   2671 C  CD2 . TYR   A 1 379 ? -21.384 -19.988 -23.620 1.00 94.59  ? 399 TYR   A CD2 1 
ATOM   2672 C  CE1 . TYR   A 1 379 ? -22.209 -18.841 -25.991 1.00 118.89 ? 399 TYR   A CE1 1 
ATOM   2673 C  CE2 . TYR   A 1 379 ? -22.133 -20.724 -24.513 1.00 87.85  ? 399 TYR   A CE2 1 
ATOM   2674 C  CZ  . TYR   A 1 379 ? -22.543 -20.147 -25.695 1.00 99.80  ? 399 TYR   A CZ  1 
ATOM   2675 O  OH  . TYR   A 1 379 ? -23.290 -20.884 -26.583 1.00 95.66  ? 399 TYR   A OH  1 
ATOM   2676 N  N   . ALA   A 1 380 ? -18.546 -16.028 -24.765 1.00 93.94  ? 400 ALA   A N   1 
ATOM   2677 C  CA  . ALA   A 1 380 ? -18.377 -15.444 -26.091 1.00 103.55 ? 400 ALA   A CA  1 
ATOM   2678 C  C   . ALA   A 1 380 ? -16.935 -15.541 -26.562 1.00 99.96  ? 400 ALA   A C   1 
ATOM   2679 O  O   . ALA   A 1 380 ? -16.676 -15.540 -27.771 1.00 102.87 ? 400 ALA   A O   1 
ATOM   2680 C  CB  . ALA   A 1 380 ? -18.833 -13.984 -26.099 1.00 105.03 ? 400 ALA   A CB  1 
ATOM   2681 N  N   . LEU   A 1 381 ? -15.988 -15.614 -25.627 1.00 98.44  ? 401 LEU   A N   1 
ATOM   2682 C  CA  . LEU   A 1 381 ? -14.589 -15.755 -26.005 1.00 100.05 ? 401 LEU   A CA  1 
ATOM   2683 C  C   . LEU   A 1 381 ? -14.278 -17.179 -26.447 1.00 99.60  ? 401 LEU   A C   1 
ATOM   2684 O  O   . LEU   A 1 381 ? -13.498 -17.386 -27.383 1.00 109.88 ? 401 LEU   A O   1 
ATOM   2685 C  CB  . LEU   A 1 381 ? -13.689 -15.336 -24.844 1.00 97.19  ? 401 LEU   A CB  1 
ATOM   2686 C  CG  . LEU   A 1 381 ? -13.631 -13.838 -24.552 1.00 102.32 ? 401 LEU   A CG  1 
ATOM   2687 C  CD1 . LEU   A 1 381 ? -12.757 -13.613 -23.340 1.00 103.20 ? 401 LEU   A CD1 1 
ATOM   2688 C  CD2 . LEU   A 1 381 ? -13.098 -13.072 -25.754 1.00 106.74 ? 401 LEU   A CD2 1 
ATOM   2689 N  N   . HIS   A 1 382 ? -14.902 -18.170 -25.806 1.00 99.20  ? 402 HIS   A N   1 
ATOM   2690 C  CA  . HIS   A 1 382 ? -14.662 -19.563 -26.160 1.00 105.82 ? 402 HIS   A CA  1 
ATOM   2691 C  C   . HIS   A 1 382 ? -15.205 -19.916 -27.541 1.00 112.41 ? 402 HIS   A C   1 
ATOM   2692 O  O   . HIS   A 1 382 ? -14.812 -20.944 -28.104 1.00 113.39 ? 402 HIS   A O   1 
ATOM   2693 C  CB  . HIS   A 1 382 ? -15.285 -20.482 -25.109 1.00 95.58  ? 402 HIS   A CB  1 
ATOM   2694 C  CG  . HIS   A 1 382 ? -14.587 -20.457 -23.783 1.00 96.52  ? 402 HIS   A CG  1 
ATOM   2695 N  ND1 . HIS   A 1 382 ? -14.915 -21.314 -22.754 1.00 96.29  ? 402 HIS   A ND1 1 
ATOM   2696 C  CD2 . HIS   A 1 382 ? -13.577 -19.682 -23.318 1.00 98.60  ? 402 HIS   A CD2 1 
ATOM   2697 C  CE1 . HIS   A 1 382 ? -14.138 -21.069 -21.714 1.00 99.03  ? 402 HIS   A CE1 1 
ATOM   2698 N  NE2 . HIS   A 1 382 ? -13.318 -20.082 -22.030 1.00 100.98 ? 402 HIS   A NE2 1 
ATOM   2699 N  N   . ARG   A 1 383 ? -16.095 -19.092 -28.097 1.00 119.00 ? 403 ARG   A N   1 
ATOM   2700 C  CA  . ARG   A 1 383 ? -16.687 -19.344 -29.406 1.00 122.83 ? 403 ARG   A CA  1 
ATOM   2701 C  C   . ARG   A 1 383 ? -16.371 -18.227 -30.395 1.00 129.72 ? 403 ARG   A C   1 
ATOM   2702 O  O   . ARG   A 1 383 ? -17.026 -18.120 -31.437 1.00 133.78 ? 403 ARG   A O   1 
ATOM   2703 C  CB  . ARG   A 1 383 ? -18.201 -19.533 -29.278 1.00 113.61 ? 403 ARG   A CB  1 
ATOM   2704 C  CG  . ARG   A 1 383 ? -18.604 -20.788 -28.511 1.00 107.38 ? 403 ARG   A CG  1 
ATOM   2705 C  CD  . ARG   A 1 383 ? -20.095 -20.792 -28.185 1.00 114.04 ? 403 ARG   A CD  1 
ATOM   2706 N  NE  . ARG   A 1 383 ? -20.495 -21.957 -27.401 1.00 109.89 ? 403 ARG   A NE  1 
ATOM   2707 C  CZ  . ARG   A 1 383 ? -21.233 -22.959 -27.861 1.00 106.09 ? 403 ARG   A CZ  1 
ATOM   2708 N  NH1 . ARG   A 1 383 ? -21.697 -22.964 -29.100 1.00 112.06 ? 403 ARG   A NH1 1 
ATOM   2709 N  NH2 . ARG   A 1 383 ? -21.516 -23.980 -27.057 1.00 106.67 ? 403 ARG   A NH2 1 
ATOM   2710 N  N   . ASP   A 1 384 ? -15.390 -17.391 -30.083 1.00 132.17 ? 404 ASP   A N   1 
ATOM   2711 C  CA  . ASP   A 1 384 ? -14.988 -16.313 -30.976 1.00 141.64 ? 404 ASP   A CA  1 
ATOM   2712 C  C   . ASP   A 1 384 ? -14.259 -16.899 -32.178 1.00 145.82 ? 404 ASP   A C   1 
ATOM   2713 O  O   . ASP   A 1 384 ? -13.216 -17.544 -32.003 1.00 149.25 ? 404 ASP   A O   1 
ATOM   2714 C  CB  . ASP   A 1 384 ? -14.094 -15.321 -30.235 1.00 142.57 ? 404 ASP   A CB  1 
ATOM   2715 C  CG  . ASP   A 1 384 ? -13.723 -14.119 -31.082 1.00 153.98 ? 404 ASP   A CG  1 
ATOM   2716 O  OD1 . ASP   A 1 384 ? -14.265 -13.975 -32.197 1.00 159.53 ? 404 ASP   A OD1 1 
ATOM   2717 O  OD2 . ASP   A 1 384 ? -12.884 -13.313 -30.626 1.00 155.84 ? 404 ASP   A OD2 1 
ATOM   2718 N  N   . PRO   A 1 385 ? -14.766 -16.716 -33.401 1.00 154.26 ? 405 PRO   A N   1 
ATOM   2719 C  CA  . PRO   A 1 385 ? -14.068 -17.257 -34.576 1.00 158.18 ? 405 PRO   A CA  1 
ATOM   2720 C  C   . PRO   A 1 385 ? -12.737 -16.585 -34.868 1.00 168.65 ? 405 PRO   A C   1 
ATOM   2721 O  O   . PRO   A 1 385 ? -11.998 -17.084 -35.727 1.00 170.65 ? 405 PRO   A O   1 
ATOM   2722 C  CB  . PRO   A 1 385 ? -15.066 -17.022 -35.718 1.00 147.71 ? 405 PRO   A CB  1 
ATOM   2723 C  CG  . PRO   A 1 385 ? -16.396 -16.868 -35.041 1.00 160.84 ? 405 PRO   A CG  1 
ATOM   2724 C  CD  . PRO   A 1 385 ? -16.088 -16.172 -33.751 1.00 153.44 ? 405 PRO   A CD  1 
ATOM   2725 N  N   . LYS   A 1 386 ? -12.406 -15.474 -34.206 1.00 184.18 ? 406 LYS   A N   1 
ATOM   2726 C  CA  . LYS   A 1 386 ? -11.093 -14.859 -34.362 1.00 192.68 ? 406 LYS   A CA  1 
ATOM   2727 C  C   . LYS   A 1 386 ? -10.031 -15.526 -33.497 1.00 198.03 ? 406 LYS   A C   1 
ATOM   2728 O  O   . LYS   A 1 386 ? -8.936  -14.971 -33.342 1.00 198.15 ? 406 LYS   A O   1 
ATOM   2729 C  CB  . LYS   A 1 386 ? -11.158 -13.361 -34.036 1.00 196.72 ? 406 LYS   A CB  1 
ATOM   2730 C  CG  . LYS   A 1 386 ? -11.978 -12.551 -35.022 1.00 205.36 ? 406 LYS   A CG  1 
ATOM   2731 C  CD  . LYS   A 1 386 ? -11.331 -11.205 -35.308 1.00 209.17 ? 406 LYS   A CD  1 
ATOM   2732 C  CE  . LYS   A 1 386 ? -12.090 -10.467 -36.399 1.00 213.59 ? 406 LYS   A CE  1 
ATOM   2733 N  NZ  . LYS   A 1 386 ? -11.439 -9.186  -36.785 1.00 209.95 ? 406 LYS   A NZ  1 
ATOM   2734 N  N   . TYR   A 1 387 ? -10.344 -16.692 -32.933 1.00 168.23 ? 407 TYR   A N   1 
ATOM   2735 C  CA  . TYR   A 1 387 ? -9.396  -17.511 -32.188 1.00 161.88 ? 407 TYR   A CA  1 
ATOM   2736 C  C   . TYR   A 1 387 ? -9.607  -18.995 -32.476 1.00 151.63 ? 407 TYR   A C   1 
ATOM   2737 O  O   . TYR   A 1 387 ? -8.637  -19.750 -32.576 1.00 153.14 ? 407 TYR   A O   1 
ATOM   2738 C  CB  . TYR   A 1 387 ? -9.529  -17.254 -30.680 1.00 151.14 ? 407 TYR   A CB  1 
ATOM   2739 C  CG  . TYR   A 1 387 ? -8.750  -16.059 -30.181 1.00 158.28 ? 407 TYR   A CG  1 
ATOM   2740 C  CD1 . TYR   A 1 387 ? -7.401  -16.170 -29.860 1.00 148.26 ? 407 TYR   A CD1 1 
ATOM   2741 C  CD2 . TYR   A 1 387 ? -9.364  -14.825 -30.018 1.00 165.00 ? 407 TYR   A CD2 1 
ATOM   2742 C  CE1 . TYR   A 1 387 ? -6.686  -15.083 -29.397 1.00 149.89 ? 407 TYR   A CE1 1 
ATOM   2743 C  CE2 . TYR   A 1 387 ? -8.655  -13.732 -29.554 1.00 163.35 ? 407 TYR   A CE2 1 
ATOM   2744 C  CZ  . TYR   A 1 387 ? -7.316  -13.869 -29.246 1.00 156.92 ? 407 TYR   A CZ  1 
ATOM   2745 O  OH  . TYR   A 1 387 ? -6.600  -12.789 -28.784 1.00 165.18 ? 407 TYR   A OH  1 
ATOM   2746 N  N   . TRP   A 1 388 ? -10.861 -19.421 -32.623 1.00 152.34 ? 408 TRP   A N   1 
ATOM   2747 C  CA  . TRP   A 1 388 ? -11.208 -20.829 -32.776 1.00 150.54 ? 408 TRP   A CA  1 
ATOM   2748 C  C   . TRP   A 1 388 ? -11.700 -21.099 -34.190 1.00 158.49 ? 408 TRP   A C   1 
ATOM   2749 O  O   . TRP   A 1 388 ? -12.500 -20.328 -34.731 1.00 162.09 ? 408 TRP   A O   1 
ATOM   2750 C  CB  . TRP   A 1 388 ? -12.284 -21.240 -31.765 1.00 139.06 ? 408 TRP   A CB  1 
ATOM   2751 C  CG  . TRP   A 1 388 ? -11.994 -20.824 -30.354 1.00 133.04 ? 408 TRP   A CG  1 
ATOM   2752 C  CD1 . TRP   A 1 388 ? -12.467 -19.716 -29.712 1.00 130.07 ? 408 TRP   A CD1 1 
ATOM   2753 C  CD2 . TRP   A 1 388 ? -11.165 -21.510 -29.410 1.00 124.16 ? 408 TRP   A CD2 1 
ATOM   2754 N  NE1 . TRP   A 1 388 ? -11.984 -19.671 -28.427 1.00 118.99 ? 408 TRP   A NE1 1 
ATOM   2755 C  CE2 . TRP   A 1 388 ? -11.182 -20.761 -28.217 1.00 119.17 ? 408 TRP   A CE2 1 
ATOM   2756 C  CE3 . TRP   A 1 388 ? -10.409 -22.685 -29.459 1.00 124.30 ? 408 TRP   A CE3 1 
ATOM   2757 C  CZ2 . TRP   A 1 388 ? -10.473 -21.149 -27.083 1.00 110.64 ? 408 TRP   A CZ2 1 
ATOM   2758 C  CZ3 . TRP   A 1 388 ? -9.706  -23.069 -28.332 1.00 120.12 ? 408 TRP   A CZ3 1 
ATOM   2759 C  CH2 . TRP   A 1 388 ? -9.743  -22.303 -27.160 1.00 103.85 ? 408 TRP   A CH2 1 
ATOM   2760 N  N   . THR   A 1 389 ? -11.232 -22.197 -34.778 1.00 157.02 ? 409 THR   A N   1 
ATOM   2761 C  CA  . THR   A 1 389 ? -11.738 -22.644 -36.067 1.00 158.41 ? 409 THR   A CA  1 
ATOM   2762 C  C   . THR   A 1 389 ? -13.016 -23.449 -35.862 1.00 155.14 ? 409 THR   A C   1 
ATOM   2763 O  O   . THR   A 1 389 ? -13.074 -24.324 -34.991 1.00 154.82 ? 409 THR   A O   1 
ATOM   2764 C  CB  . THR   A 1 389 ? -10.694 -23.497 -36.790 1.00 161.17 ? 409 THR   A CB  1 
ATOM   2765 O  OG1 . THR   A 1 389 ? -10.597 -24.773 -36.148 1.00 167.21 ? 409 THR   A OG1 1 
ATOM   2766 C  CG2 . THR   A 1 389 ? -9.329  -22.824 -36.754 1.00 164.59 ? 409 THR   A CG2 1 
ATOM   2767 N  N   . GLU   A 1 390 ? -14.039 -23.153 -36.662 1.00 155.82 ? 410 GLU   A N   1 
ATOM   2768 C  CA  . GLU   A 1 390 ? -15.352 -23.791 -36.581 1.00 148.71 ? 410 GLU   A CA  1 
ATOM   2769 C  C   . GLU   A 1 390 ? -15.815 -23.870 -35.117 1.00 147.26 ? 410 GLU   A C   1 
ATOM   2770 O  O   . GLU   A 1 390 ? -16.070 -24.968 -34.610 1.00 143.70 ? 410 GLU   A O   1 
ATOM   2771 C  CB  . GLU   A 1 390 ? -15.328 -25.172 -37.222 1.00 156.77 ? 410 GLU   A CB  1 
ATOM   2772 C  CG  . GLU   A 1 390 ? -15.276 -25.164 -38.739 1.00 164.01 ? 410 GLU   A CG  1 
ATOM   2773 C  CD  . GLU   A 1 390 ? -15.166 -26.558 -39.335 1.00 164.32 ? 410 GLU   A CD  1 
ATOM   2774 O  OE1 . GLU   A 1 390 ? -14.335 -27.353 -38.845 1.00 161.63 ? 410 GLU   A OE1 1 
ATOM   2775 O  OE2 . GLU   A 1 390 ? -15.912 -26.861 -40.291 1.00 169.47 ? 410 GLU   A OE2 1 
ATOM   2776 N  N   . PRO   A 1 391 ? -15.944 -22.732 -34.432 1.00 145.36 ? 411 PRO   A N   1 
ATOM   2777 C  CA  . PRO   A 1 391 ? -16.039 -22.765 -32.960 1.00 138.70 ? 411 PRO   A CA  1 
ATOM   2778 C  C   . PRO   A 1 391 ? -17.293 -23.432 -32.422 1.00 138.22 ? 411 PRO   A C   1 
ATOM   2779 O  O   . PRO   A 1 391 ? -17.322 -23.767 -31.230 1.00 138.52 ? 411 PRO   A O   1 
ATOM   2780 C  CB  . PRO   A 1 391 ? -15.989 -21.282 -32.571 1.00 138.71 ? 411 PRO   A CB  1 
ATOM   2781 C  CG  . PRO   A 1 391 ? -16.511 -20.570 -33.769 1.00 145.01 ? 411 PRO   A CG  1 
ATOM   2782 C  CD  . PRO   A 1 391 ? -16.044 -21.360 -34.958 1.00 147.48 ? 411 PRO   A CD  1 
ATOM   2783 N  N   . GLU   A 1 392 ? -18.321 -23.638 -33.242 1.00 143.64 ? 412 GLU   A N   1 
ATOM   2784 C  CA  . GLU   A 1 392 ? -19.500 -24.359 -32.782 1.00 142.37 ? 412 GLU   A CA  1 
ATOM   2785 C  C   . GLU   A 1 392 ? -19.314 -25.869 -32.797 1.00 139.33 ? 412 GLU   A C   1 
ATOM   2786 O  O   . GLU   A 1 392 ? -20.150 -26.583 -32.234 1.00 133.16 ? 412 GLU   A O   1 
ATOM   2787 C  CB  . GLU   A 1 392 ? -20.719 -23.989 -33.632 1.00 142.73 ? 412 GLU   A CB  1 
ATOM   2788 C  CG  . GLU   A 1 392 ? -21.284 -22.609 -33.341 1.00 148.02 ? 412 GLU   A CG  1 
ATOM   2789 C  CD  . GLU   A 1 392 ? -20.458 -21.497 -33.952 1.00 155.03 ? 412 GLU   A CD  1 
ATOM   2790 O  OE1 . GLU   A 1 392 ? -19.847 -21.728 -35.017 1.00 159.30 ? 412 GLU   A OE1 1 
ATOM   2791 O  OE2 . GLU   A 1 392 ? -20.419 -20.394 -33.367 1.00 145.92 ? 412 GLU   A OE2 1 
ATOM   2792 N  N   . LYS   A 1 393 ? -18.246 -26.371 -33.411 1.00 144.59 ? 413 LYS   A N   1 
ATOM   2793 C  CA  . LYS   A 1 393 ? -18.040 -27.805 -33.535 1.00 139.63 ? 413 LYS   A CA  1 
ATOM   2794 C  C   . LYS   A 1 393 ? -17.261 -28.341 -32.340 1.00 136.23 ? 413 LYS   A C   1 
ATOM   2795 O  O   . LYS   A 1 393 ? -16.390 -27.661 -31.788 1.00 135.70 ? 413 LYS   A O   1 
ATOM   2796 C  CB  . LYS   A 1 393 ? -17.304 -28.137 -34.834 1.00 137.20 ? 413 LYS   A CB  1 
ATOM   2797 C  CG  . LYS   A 1 393 ? -17.872 -27.430 -36.053 1.00 143.94 ? 413 LYS   A CG  1 
ATOM   2798 C  CD  . LYS   A 1 393 ? -17.453 -28.111 -37.343 1.00 141.22 ? 413 LYS   A CD  1 
ATOM   2799 C  CE  . LYS   A 1 393 ? -18.248 -29.382 -37.585 1.00 146.99 ? 413 LYS   A CE  1 
ATOM   2800 N  NZ  . LYS   A 1 393 ? -18.003 -29.920 -38.953 1.00 137.59 ? 413 LYS   A NZ  1 
ATOM   2801 N  N   . PHE   A 1 394 ? -17.593 -29.566 -31.944 1.00 132.27 ? 414 PHE   A N   1 
ATOM   2802 C  CA  . PHE   A 1 394 ? -16.930 -30.248 -30.836 1.00 128.40 ? 414 PHE   A CA  1 
ATOM   2803 C  C   . PHE   A 1 394 ? -15.683 -30.933 -31.381 1.00 134.63 ? 414 PHE   A C   1 
ATOM   2804 O  O   . PHE   A 1 394 ? -15.768 -31.974 -32.036 1.00 136.30 ? 414 PHE   A O   1 
ATOM   2805 C  CB  . PHE   A 1 394 ? -17.890 -31.241 -30.185 1.00 123.47 ? 414 PHE   A CB  1 
ATOM   2806 C  CG  . PHE   A 1 394 ? -17.250 -32.129 -29.157 1.00 125.65 ? 414 PHE   A CG  1 
ATOM   2807 C  CD1 . PHE   A 1 394 ? -16.967 -31.654 -27.887 1.00 125.11 ? 414 PHE   A CD1 1 
ATOM   2808 C  CD2 . PHE   A 1 394 ? -16.954 -33.451 -29.455 1.00 128.44 ? 414 PHE   A CD2 1 
ATOM   2809 C  CE1 . PHE   A 1 394 ? -16.385 -32.479 -26.936 1.00 122.32 ? 414 PHE   A CE1 1 
ATOM   2810 C  CE2 . PHE   A 1 394 ? -16.373 -34.282 -28.512 1.00 120.59 ? 414 PHE   A CE2 1 
ATOM   2811 C  CZ  . PHE   A 1 394 ? -16.089 -33.796 -27.250 1.00 123.29 ? 414 PHE   A CZ  1 
ATOM   2812 N  N   . LEU   A 1 395 ? -14.516 -30.344 -31.115 1.00 130.78 ? 415 LEU   A N   1 
ATOM   2813 C  CA  . LEU   A 1 395 ? -13.243 -30.826 -31.650 1.00 130.27 ? 415 LEU   A CA  1 
ATOM   2814 C  C   . LEU   A 1 395 ? -12.228 -30.923 -30.520 1.00 130.42 ? 415 LEU   A C   1 
ATOM   2815 O  O   . LEU   A 1 395 ? -11.517 -29.953 -30.222 1.00 127.69 ? 415 LEU   A O   1 
ATOM   2816 C  CB  . LEU   A 1 395 ? -12.732 -29.916 -32.765 1.00 128.77 ? 415 LEU   A CB  1 
ATOM   2817 C  CG  . LEU   A 1 395 ? -13.445 -30.003 -34.114 1.00 136.69 ? 415 LEU   A CG  1 
ATOM   2818 C  CD1 . LEU   A 1 395 ? -12.886 -28.967 -35.074 1.00 146.98 ? 415 LEU   A CD1 1 
ATOM   2819 C  CD2 . LEU   A 1 395 ? -13.308 -31.401 -34.694 1.00 138.07 ? 415 LEU   A CD2 1 
ATOM   2820 N  N   . PRO   A 1 396 ? -12.134 -32.081 -29.863 1.00 133.69 ? 416 PRO   A N   1 
ATOM   2821 C  CA  . PRO   A 1 396 ? -11.134 -32.241 -28.795 1.00 133.17 ? 416 PRO   A CA  1 
ATOM   2822 C  C   . PRO   A 1 396 ? -9.698  -32.099 -29.267 1.00 126.50 ? 416 PRO   A C   1 
ATOM   2823 O  O   . PRO   A 1 396 ? -8.820  -31.829 -28.438 1.00 125.11 ? 416 PRO   A O   1 
ATOM   2824 C  CB  . PRO   A 1 396 ? -11.409 -33.655 -28.267 1.00 129.35 ? 416 PRO   A CB  1 
ATOM   2825 C  CG  . PRO   A 1 396 ? -12.837 -33.911 -28.609 1.00 126.20 ? 416 PRO   A CG  1 
ATOM   2826 C  CD  . PRO   A 1 396 ? -13.067 -33.220 -29.924 1.00 128.42 ? 416 PRO   A CD  1 
ATOM   2827 N  N   . GLU   A 1 397 ? -9.421  -32.268 -30.563 1.00 123.48 ? 417 GLU   A N   1 
ATOM   2828 C  CA  . GLU   A 1 397 ? -8.058  -32.095 -31.054 1.00 129.91 ? 417 GLU   A CA  1 
ATOM   2829 C  C   . GLU   A 1 397 ? -7.562  -30.660 -30.935 1.00 129.65 ? 417 GLU   A C   1 
ATOM   2830 O  O   . GLU   A 1 397 ? -6.387  -30.409 -31.225 1.00 130.02 ? 417 GLU   A O   1 
ATOM   2831 C  CB  . GLU   A 1 397 ? -7.952  -32.564 -32.506 1.00 132.57 ? 417 GLU   A CB  1 
ATOM   2832 C  CG  . GLU   A 1 397 ? -7.892  -34.075 -32.660 1.00 132.27 ? 417 GLU   A CG  1 
ATOM   2833 C  CD  . GLU   A 1 397 ? -6.619  -34.672 -32.088 1.00 146.08 ? 417 GLU   A CD  1 
ATOM   2834 O  OE1 . GLU   A 1 397 ? -5.591  -33.963 -32.050 1.00 149.43 ? 417 GLU   A OE1 1 
ATOM   2835 O  OE2 . GLU   A 1 397 ? -6.648  -35.851 -31.676 1.00 149.22 ? 417 GLU   A OE2 1 
ATOM   2836 N  N   . ARG   A 1 398 ? -8.418  -29.718 -30.526 1.00 129.50 ? 418 ARG   A N   1 
ATOM   2837 C  CA  . ARG   A 1 398 ? -7.935  -28.379 -30.203 1.00 123.75 ? 418 ARG   A CA  1 
ATOM   2838 C  C   . ARG   A 1 398 ? -6.903  -28.423 -29.086 1.00 126.06 ? 418 ARG   A C   1 
ATOM   2839 O  O   . ARG   A 1 398 ? -5.971  -27.611 -29.064 1.00 124.37 ? 418 ARG   A O   1 
ATOM   2840 C  CB  . ARG   A 1 398 ? -9.095  -27.472 -29.788 1.00 127.21 ? 418 ARG   A CB  1 
ATOM   2841 C  CG  . ARG   A 1 398 ? -10.135 -27.192 -30.856 1.00 132.15 ? 418 ARG   A CG  1 
ATOM   2842 C  CD  . ARG   A 1 398 ? -11.174 -26.218 -30.321 1.00 123.52 ? 418 ARG   A CD  1 
ATOM   2843 N  NE  . ARG   A 1 398 ? -12.458 -26.350 -30.998 1.00 129.41 ? 418 ARG   A NE  1 
ATOM   2844 C  CZ  . ARG   A 1 398 ? -12.769 -25.756 -32.142 1.00 139.13 ? 418 ARG   A CZ  1 
ATOM   2845 N  NH1 . ARG   A 1 398 ? -11.907 -24.977 -32.774 1.00 145.42 ? 418 ARG   A NH1 1 
ATOM   2846 N  NH2 . ARG   A 1 398 ? -13.975 -25.952 -32.666 1.00 141.03 ? 418 ARG   A NH2 1 
ATOM   2847 N  N   . PHE   A 1 399 ? -7.053  -29.363 -28.152 1.00 122.98 ? 419 PHE   A N   1 
ATOM   2848 C  CA  . PHE   A 1 399 ? -6.228  -29.421 -26.953 1.00 125.70 ? 419 PHE   A CA  1 
ATOM   2849 C  C   . PHE   A 1 399 ? -5.201  -30.545 -27.007 1.00 124.02 ? 419 PHE   A C   1 
ATOM   2850 O  O   . PHE   A 1 399 ? -4.717  -30.992 -25.963 1.00 133.39 ? 419 PHE   A O   1 
ATOM   2851 C  CB  . PHE   A 1 399 ? -7.114  -29.559 -25.715 1.00 120.61 ? 419 PHE   A CB  1 
ATOM   2852 C  CG  . PHE   A 1 399 ? -8.068  -28.414 -25.531 1.00 115.39 ? 419 PHE   A CG  1 
ATOM   2853 C  CD1 . PHE   A 1 399 ? -7.665  -27.264 -24.872 1.00 117.48 ? 419 PHE   A CD1 1 
ATOM   2854 C  CD2 . PHE   A 1 399 ? -9.363  -28.482 -26.027 1.00 123.64 ? 419 PHE   A CD2 1 
ATOM   2855 C  CE1 . PHE   A 1 399 ? -8.536  -26.204 -24.705 1.00 125.75 ? 419 PHE   A CE1 1 
ATOM   2856 C  CE2 . PHE   A 1 399 ? -10.241 -27.424 -25.865 1.00 120.63 ? 419 PHE   A CE2 1 
ATOM   2857 C  CZ  . PHE   A 1 399 ? -9.828  -26.284 -25.202 1.00 116.43 ? 419 PHE   A CZ  1 
ATOM   2858 N  N   . SER   A 1 400 ? -4.862  -31.012 -28.204 1.00 136.30 ? 420 SER   A N   1 
ATOM   2859 C  CA  . SER   A 1 400 ? -3.751  -31.938 -28.346 1.00 151.72 ? 420 SER   A CA  1 
ATOM   2860 C  C   . SER   A 1 400 ? -2.438  -31.199 -28.126 1.00 160.58 ? 420 SER   A C   1 
ATOM   2861 O  O   . SER   A 1 400 ? -2.325  -29.999 -28.390 1.00 150.63 ? 420 SER   A O   1 
ATOM   2862 C  CB  . SER   A 1 400 ? -3.767  -32.589 -29.728 1.00 155.78 ? 420 SER   A CB  1 
ATOM   2863 O  OG  . SER   A 1 400 ? -3.707  -31.610 -30.751 1.00 160.83 ? 420 SER   A OG  1 
ATOM   2864 N  N   . LYS   A 1 401 ? -1.436  -31.928 -27.630 1.00 156.35 ? 421 LYS   A N   1 
ATOM   2865 C  CA  . LYS   A 1 401 ? -0.138  -31.313 -27.375 1.00 162.28 ? 421 LYS   A CA  1 
ATOM   2866 C  C   . LYS   A 1 401 ? 0.531   -30.817 -28.648 1.00 159.69 ? 421 LYS   A C   1 
ATOM   2867 O  O   . LYS   A 1 401 ? 1.512   -30.069 -28.564 1.00 157.89 ? 421 LYS   A O   1 
ATOM   2868 C  CB  . LYS   A 1 401 ? 0.774   -32.295 -26.638 1.00 165.01 ? 421 LYS   A CB  1 
ATOM   2869 C  CG  . LYS   A 1 401 ? 1.195   -31.803 -25.261 1.00 171.85 ? 421 LYS   A CG  1 
ATOM   2870 C  CD  . LYS   A 1 401 ? 1.128   -32.911 -24.220 1.00 178.70 ? 421 LYS   A CD  1 
ATOM   2871 C  CE  . LYS   A 1 401 ? 2.126   -34.021 -24.509 1.00 178.92 ? 421 LYS   A CE  1 
ATOM   2872 N  NZ  . LYS   A 1 401 ? 2.171   -35.023 -23.406 1.00 183.02 ? 421 LYS   A NZ  1 
ATOM   2873 N  N   . LYS   A 1 402 ? 0.029   -31.213 -29.817 1.00 177.50 ? 422 LYS   A N   1 
ATOM   2874 C  CA  . LYS   A 1 402 ? 0.437   -30.604 -31.074 1.00 177.00 ? 422 LYS   A CA  1 
ATOM   2875 C  C   . LYS   A 1 402 ? -0.240  -29.257 -31.303 1.00 177.58 ? 422 LYS   A C   1 
ATOM   2876 O  O   . LYS   A 1 402 ? 0.318   -28.405 -32.005 1.00 181.27 ? 422 LYS   A O   1 
ATOM   2877 C  CB  . LYS   A 1 402 ? 0.132   -31.564 -32.229 1.00 182.60 ? 422 LYS   A CB  1 
ATOM   2878 C  CG  . LYS   A 1 402 ? 0.328   -30.991 -33.620 1.00 192.71 ? 422 LYS   A CG  1 
ATOM   2879 C  CD  . LYS   A 1 402 ? -0.153  -31.961 -34.687 1.00 200.30 ? 422 LYS   A CD  1 
ATOM   2880 C  CE  . LYS   A 1 402 ? -0.464  -31.233 -35.984 1.00 204.26 ? 422 LYS   A CE  1 
ATOM   2881 N  NZ  . LYS   A 1 402 ? -1.523  -30.204 -35.784 1.00 200.27 ? 422 LYS   A NZ  1 
ATOM   2882 N  N   . ASN   A 1 403 ? -1.412  -29.034 -30.701 1.00 173.39 ? 423 ASN   A N   1 
ATOM   2883 C  CA  . ASN   A 1 403 ? -2.159  -27.798 -30.885 1.00 161.96 ? 423 ASN   A CA  1 
ATOM   2884 C  C   . ASN   A 1 403 ? -2.465  -27.043 -29.598 1.00 161.41 ? 423 ASN   A C   1 
ATOM   2885 O  O   . ASN   A 1 403 ? -3.004  -25.933 -29.676 1.00 160.01 ? 423 ASN   A O   1 
ATOM   2886 C  CB  . ASN   A 1 403 ? -3.484  -28.077 -31.614 1.00 148.15 ? 423 ASN   A CB  1 
ATOM   2887 C  CG  . ASN   A 1 403 ? -3.278  -28.515 -33.049 1.00 165.45 ? 423 ASN   A CG  1 
ATOM   2888 O  OD1 . ASN   A 1 403 ? -2.243  -28.235 -33.653 1.00 175.26 ? 423 ASN   A OD1 1 
ATOM   2889 N  ND2 . ASN   A 1 403 ? -4.269  -29.202 -33.606 1.00 155.81 ? 423 ASN   A ND2 1 
ATOM   2890 N  N   . LYS   A 1 404 ? -2.140  -27.592 -28.423 1.00 151.53 ? 424 LYS   A N   1 
ATOM   2891 C  CA  . LYS   A 1 404 ? -2.487  -26.920 -27.172 1.00 151.52 ? 424 LYS   A CA  1 
ATOM   2892 C  C   . LYS   A 1 404 ? -1.656  -25.672 -26.914 1.00 156.86 ? 424 LYS   A C   1 
ATOM   2893 O  O   . LYS   A 1 404 ? -1.917  -24.975 -25.926 1.00 157.97 ? 424 LYS   A O   1 
ATOM   2894 C  CB  . LYS   A 1 404 ? -2.344  -27.878 -25.987 1.00 152.11 ? 424 LYS   A CB  1 
ATOM   2895 C  CG  . LYS   A 1 404 ? -0.906  -28.209 -25.623 1.00 158.88 ? 424 LYS   A CG  1 
ATOM   2896 C  CD  . LYS   A 1 404 ? -0.771  -28.552 -24.145 1.00 162.99 ? 424 LYS   A CD  1 
ATOM   2897 C  CE  . LYS   A 1 404 ? -1.662  -29.717 -23.749 1.00 163.22 ? 424 LYS   A CE  1 
ATOM   2898 N  NZ  . LYS   A 1 404 ? -1.553  -30.009 -22.293 1.00 155.55 ? 424 LYS   A NZ  1 
ATOM   2899 N  N   . ASP   A 1 405 ? -0.667  -25.377 -27.758 1.00 159.48 ? 425 ASP   A N   1 
ATOM   2900 C  CA  . ASP   A 1 405 ? 0.115   -24.157 -27.626 1.00 159.43 ? 425 ASP   A CA  1 
ATOM   2901 C  C   . ASP   A 1 405 ? -0.518  -22.972 -28.344 1.00 157.43 ? 425 ASP   A C   1 
ATOM   2902 O  O   . ASP   A 1 405 ? -0.261  -21.825 -27.964 1.00 152.38 ? 425 ASP   A O   1 
ATOM   2903 C  CB  . ASP   A 1 405 ? 1.535   -24.379 -28.160 1.00 166.04 ? 425 ASP   A CB  1 
ATOM   2904 C  CG  . ASP   A 1 405 ? 1.844   -25.845 -28.407 1.00 170.31 ? 425 ASP   A CG  1 
ATOM   2905 O  OD1 . ASP   A 1 405 ? 1.755   -26.647 -27.452 1.00 167.44 ? 425 ASP   A OD1 1 
ATOM   2906 O  OD2 . ASP   A 1 405 ? 2.164   -26.196 -29.562 1.00 167.38 ? 425 ASP   A OD2 1 
ATOM   2907 N  N   . ASN   A 1 406 ? -1.341  -23.219 -29.362 1.00 174.44 ? 426 ASN   A N   1 
ATOM   2908 C  CA  . ASN   A 1 406 ? -2.040  -22.154 -30.079 1.00 170.09 ? 426 ASN   A CA  1 
ATOM   2909 C  C   . ASN   A 1 406 ? -3.319  -21.731 -29.364 1.00 166.51 ? 426 ASN   A C   1 
ATOM   2910 O  O   . ASN   A 1 406 ? -4.328  -21.442 -30.011 1.00 171.87 ? 426 ASN   A O   1 
ATOM   2911 C  CB  . ASN   A 1 406 ? -2.356  -22.631 -31.495 1.00 173.89 ? 426 ASN   A CB  1 
ATOM   2912 C  CG  . ASN   A 1 406 ? -1.325  -23.610 -32.025 1.00 184.09 ? 426 ASN   A CG  1 
ATOM   2913 O  OD1 . ASN   A 1 406 ? -0.131  -23.476 -31.758 1.00 187.99 ? 426 ASN   A OD1 1 
ATOM   2914 N  ND2 . ASN   A 1 406 ? -1.784  -24.607 -32.772 1.00 186.89 ? 426 ASN   A ND2 1 
ATOM   2915 N  N   . ILE   A 1 407 ? -3.312  -21.701 -28.033 1.00 145.79 ? 427 ILE   A N   1 
ATOM   2916 C  CA  . ILE   A 1 407 ? -4.492  -21.359 -27.245 1.00 140.26 ? 427 ILE   A CA  1 
ATOM   2917 C  C   . ILE   A 1 407 ? -4.073  -20.392 -26.145 1.00 132.95 ? 427 ILE   A C   1 
ATOM   2918 O  O   . ILE   A 1 407 ? -3.233  -20.731 -25.304 1.00 133.69 ? 427 ILE   A O   1 
ATOM   2919 C  CB  . ILE   A 1 407 ? -5.170  -22.607 -26.652 1.00 138.21 ? 427 ILE   A CB  1 
ATOM   2920 C  CG1 . ILE   A 1 407 ? -5.861  -23.407 -27.757 1.00 138.13 ? 427 ILE   A CG1 1 
ATOM   2921 C  CG2 . ILE   A 1 407 ? -6.178  -22.223 -25.584 1.00 98.52  ? 427 ILE   A CG2 1 
ATOM   2922 C  CD1 . ILE   A 1 407 ? -6.619  -24.604 -27.255 1.00 132.61 ? 427 ILE   A CD1 1 
ATOM   2923 N  N   . ASP   A 1 408 ? -4.658  -19.198 -26.149 1.00 117.18 ? 428 ASP   A N   1 
ATOM   2924 C  CA  . ASP   A 1 408 ? -4.302  -18.177 -25.171 1.00 109.35 ? 428 ASP   A CA  1 
ATOM   2925 C  C   . ASP   A 1 408 ? -5.017  -18.463 -23.855 1.00 111.12 ? 428 ASP   A C   1 
ATOM   2926 O  O   . ASP   A 1 408 ? -6.248  -18.581 -23.845 1.00 106.61 ? 428 ASP   A O   1 
ATOM   2927 C  CB  . ASP   A 1 408 ? -4.661  -16.790 -25.699 1.00 116.90 ? 428 ASP   A CB  1 
ATOM   2928 C  CG  . ASP   A 1 408 ? -3.898  -15.681 -25.008 1.00 113.70 ? 428 ASP   A CG  1 
ATOM   2929 O  OD1 . ASP   A 1 408 ? -3.659  -15.795 -23.788 1.00 108.28 ? 428 ASP   A OD1 1 
ATOM   2930 O  OD2 . ASP   A 1 408 ? -3.549  -14.690 -25.684 1.00 116.19 ? 428 ASP   A OD2 1 
ATOM   2931 N  N   . PRO   A 1 409 ? -4.297  -18.593 -22.727 1.00 123.51 ? 429 PRO   A N   1 
ATOM   2932 C  CA  . PRO   A 1 409 ? -4.971  -18.984 -21.484 1.00 109.57 ? 429 PRO   A CA  1 
ATOM   2933 C  C   . PRO   A 1 409 ? -5.736  -17.837 -20.846 1.00 94.76  ? 429 PRO   A C   1 
ATOM   2934 O  O   . PRO   A 1 409 ? -6.277  -17.961 -19.740 1.00 90.81  ? 429 PRO   A O   1 
ATOM   2935 C  CB  . PRO   A 1 409 ? -3.822  -19.462 -20.592 1.00 103.96 ? 429 PRO   A CB  1 
ATOM   2936 C  CG  . PRO   A 1 409 ? -2.634  -18.739 -21.098 1.00 110.50 ? 429 PRO   A CG  1 
ATOM   2937 C  CD  . PRO   A 1 409 ? -2.834  -18.645 -22.596 1.00 116.27 ? 429 PRO   A CD  1 
ATOM   2938 N  N   . TYR   A 1 410 ? -5.777  -16.708 -21.538 1.00 100.74 ? 430 TYR   A N   1 
ATOM   2939 C  CA  . TYR   A 1 410 ? -6.631  -15.603 -21.150 1.00 113.00 ? 430 TYR   A CA  1 
ATOM   2940 C  C   . TYR   A 1 410 ? -7.795  -15.430 -22.109 1.00 105.65 ? 430 TYR   A C   1 
ATOM   2941 O  O   . TYR   A 1 410 ? -8.627  -14.539 -21.904 1.00 113.98 ? 430 TYR   A O   1 
ATOM   2942 C  CB  . TYR   A 1 410 ? -5.808  -14.317 -21.038 1.00 115.88 ? 430 TYR   A CB  1 
ATOM   2943 C  CG  . TYR   A 1 410 ? -4.763  -14.426 -19.954 1.00 112.51 ? 430 TYR   A CG  1 
ATOM   2944 C  CD1 . TYR   A 1 410 ? -5.128  -14.404 -18.615 1.00 103.51 ? 430 TYR   A CD1 1 
ATOM   2945 C  CD2 . TYR   A 1 410 ? -3.418  -14.579 -20.266 1.00 111.46 ? 430 TYR   A CD2 1 
ATOM   2946 C  CE1 . TYR   A 1 410 ? -4.183  -14.517 -17.617 1.00 124.34 ? 430 TYR   A CE1 1 
ATOM   2947 C  CE2 . TYR   A 1 410 ? -2.465  -14.692 -19.276 1.00 112.68 ? 430 TYR   A CE2 1 
ATOM   2948 C  CZ  . TYR   A 1 410 ? -2.851  -14.662 -17.955 1.00 123.77 ? 430 TYR   A CZ  1 
ATOM   2949 O  OH  . TYR   A 1 410 ? -1.891  -14.775 -16.979 1.00 128.27 ? 430 TYR   A OH  1 
ATOM   2950 N  N   . ILE   A 1 411 ? -7.870  -16.254 -23.149 1.00 115.59 ? 431 ILE   A N   1 
ATOM   2951 C  CA  . ILE   A 1 411 ? -9.106  -16.436 -23.901 1.00 112.41 ? 431 ILE   A CA  1 
ATOM   2952 C  C   . ILE   A 1 411 ? -9.874  -17.649 -23.394 1.00 98.46  ? 431 ILE   A C   1 
ATOM   2953 O  O   . ILE   A 1 411 ? -11.085 -17.583 -23.168 1.00 101.24 ? 431 ILE   A O   1 
ATOM   2954 C  CB  . ILE   A 1 411 ? -8.797  -16.555 -25.408 1.00 117.60 ? 431 ILE   A CB  1 
ATOM   2955 C  CG1 . ILE   A 1 411 ? -8.117  -15.279 -25.906 1.00 121.18 ? 431 ILE   A CG1 1 
ATOM   2956 C  CG2 . ILE   A 1 411 ? -10.071 -16.856 -26.188 1.00 113.47 ? 431 ILE   A CG2 1 
ATOM   2957 C  CD1 . ILE   A 1 411 ? -8.869  -14.016 -25.558 1.00 122.14 ? 431 ILE   A CD1 1 
ATOM   2958 N  N   . TYR   A 1 412 ? -9.175  -18.766 -23.198 1.00 100.27 ? 432 TYR   A N   1 
ATOM   2959 C  CA  . TYR   A 1 412 ? -9.756  -19.968 -22.603 1.00 105.92 ? 432 TYR   A CA  1 
ATOM   2960 C  C   . TYR   A 1 412 ? -9.591  -19.880 -21.091 1.00 104.71 ? 432 TYR   A C   1 
ATOM   2961 O  O   . TYR   A 1 412 ? -8.503  -20.114 -20.555 1.00 96.21  ? 432 TYR   A O   1 
ATOM   2962 C  CB  . TYR   A 1 412 ? -9.095  -21.223 -23.158 1.00 95.26  ? 432 TYR   A CB  1 
ATOM   2963 C  CG  . TYR   A 1 412 ? -9.754  -22.488 -22.669 1.00 97.98  ? 432 TYR   A CG  1 
ATOM   2964 C  CD1 . TYR   A 1 412 ? -11.035 -22.820 -23.084 1.00 103.56 ? 432 TYR   A CD1 1 
ATOM   2965 C  CD2 . TYR   A 1 412 ? -9.106  -23.346 -21.789 1.00 92.30  ? 432 TYR   A CD2 1 
ATOM   2966 C  CE1 . TYR   A 1 412 ? -11.653 -23.969 -22.641 1.00 105.36 ? 432 TYR   A CE1 1 
ATOM   2967 C  CE2 . TYR   A 1 412 ? -9.717  -24.504 -21.340 1.00 100.64 ? 432 TYR   A CE2 1 
ATOM   2968 C  CZ  . TYR   A 1 412 ? -10.992 -24.810 -21.769 1.00 101.26 ? 432 TYR   A CZ  1 
ATOM   2969 O  OH  . TYR   A 1 412 ? -11.610 -25.959 -21.326 1.00 96.64  ? 432 TYR   A OH  1 
ATOM   2970 N  N   . THR   A 1 413 ? -10.678 -19.544 -20.399 1.00 94.74  ? 433 THR   A N   1 
ATOM   2971 C  CA  . THR   A 1 413 ? -10.658 -19.337 -18.950 1.00 94.14  ? 433 THR   A CA  1 
ATOM   2972 C  C   . THR   A 1 413 ? -11.877 -19.991 -18.310 1.00 102.33 ? 433 THR   A C   1 
ATOM   2973 O  O   . THR   A 1 413 ? -12.741 -19.306 -17.759 1.00 99.96  ? 433 THR   A O   1 
ATOM   2974 C  CB  . THR   A 1 413 ? -10.630 -17.842 -18.630 1.00 112.96 ? 433 THR   A CB  1 
ATOM   2975 O  OG1 . THR   A 1 413 ? -11.706 -17.185 -19.315 1.00 94.46  ? 433 THR   A OG1 1 
ATOM   2976 C  CG2 . THR   A 1 413 ? -9.305  -17.221 -19.055 1.00 94.17  ? 433 THR   A CG2 1 
ATOM   2977 N  N   . PRO   A 1 414 ? -11.975 -21.327 -18.351 1.00 106.40 ? 434 PRO   A N   1 
ATOM   2978 C  CA  . PRO   A 1 414 ? -13.160 -21.992 -17.777 1.00 95.87  ? 434 PRO   A CA  1 
ATOM   2979 C  C   . PRO   A 1 414 ? -13.168 -22.016 -16.259 1.00 98.74  ? 434 PRO   A C   1 
ATOM   2980 O  O   . PRO   A 1 414 ? -14.219 -22.296 -15.660 1.00 96.39  ? 434 PRO   A O   1 
ATOM   2981 C  CB  . PRO   A 1 414 ? -13.076 -23.409 -18.347 1.00 104.86 ? 434 PRO   A CB  1 
ATOM   2982 C  CG  . PRO   A 1 414 ? -11.610 -23.637 -18.496 1.00 98.78  ? 434 PRO   A CG  1 
ATOM   2983 C  CD  . PRO   A 1 414 ? -11.011 -22.303 -18.887 1.00 103.00 ? 434 PRO   A CD  1 
ATOM   2984 N  N   . PHE   A 1 415 ? -12.029 -21.740 -15.623 1.00 100.18 ? 435 PHE   A N   1 
ATOM   2985 C  CA  . PHE   A 1 415 ? -11.908 -21.732 -14.171 1.00 99.45  ? 435 PHE   A CA  1 
ATOM   2986 C  C   . PHE   A 1 415 ? -11.460 -20.373 -13.645 1.00 91.80  ? 435 PHE   A C   1 
ATOM   2987 O  O   . PHE   A 1 415 ? -11.021 -20.273 -12.494 1.00 87.68  ? 435 PHE   A O   1 
ATOM   2988 C  CB  . PHE   A 1 415 ? -10.935 -22.822 -13.711 1.00 98.61  ? 435 PHE   A CB  1 
ATOM   2989 C  CG  . PHE   A 1 415 ? -11.421 -24.221 -13.973 1.00 101.53 ? 435 PHE   A CG  1 
ATOM   2990 C  CD1 . PHE   A 1 415 ? -12.260 -24.854 -13.069 1.00 108.03 ? 435 PHE   A CD1 1 
ATOM   2991 C  CD2 . PHE   A 1 415 ? -11.035 -24.908 -15.116 1.00 98.69  ? 435 PHE   A CD2 1 
ATOM   2992 C  CE1 . PHE   A 1 415 ? -12.713 -26.144 -13.296 1.00 113.20 ? 435 PHE   A CE1 1 
ATOM   2993 C  CE2 . PHE   A 1 415 ? -11.486 -26.202 -15.349 1.00 108.04 ? 435 PHE   A CE2 1 
ATOM   2994 C  CZ  . PHE   A 1 415 ? -12.328 -26.818 -14.435 1.00 111.64 ? 435 PHE   A CZ  1 
ATOM   2995 N  N   . GLY   A 1 416 ? -11.566 -19.324 -14.454 1.00 98.27  ? 436 GLY   A N   1 
ATOM   2996 C  CA  . GLY   A 1 416 ? -11.051 -18.065 -13.979 1.00 96.71  ? 436 GLY   A CA  1 
ATOM   2997 C  C   . GLY   A 1 416 ? -9.535  -18.056 -14.070 1.00 98.57  ? 436 GLY   A C   1 
ATOM   2998 O  O   . GLY   A 1 416 ? -8.907  -18.919 -14.696 1.00 90.21  ? 436 GLY   A O   1 
ATOM   2999 N  N   . SER   A 1 417 ? -8.945  -17.055 -13.425 1.00 99.44  ? 437 SER   A N   1 
ATOM   3000 C  CA  . SER   A 1 417 ? -7.497  -16.923 -13.425 1.00 103.15 ? 437 SER   A CA  1 
ATOM   3001 C  C   . SER   A 1 417 ? -7.081  -16.025 -12.271 1.00 107.77 ? 437 SER   A C   1 
ATOM   3002 O  O   . SER   A 1 417 ? -7.880  -15.249 -11.740 1.00 95.42  ? 437 SER   A O   1 
ATOM   3003 C  CB  . SER   A 1 417 ? -6.990  -16.364 -14.758 1.00 105.85 ? 437 SER   A CB  1 
ATOM   3004 O  OG  . SER   A 1 417 ? -5.691  -16.842 -15.058 1.00 95.63  ? 437 SER   A OG  1 
ATOM   3005 N  N   . GLY   A 1 418 ? -5.809  -16.137 -11.899 1.00 99.24  ? 438 GLY   A N   1 
ATOM   3006 C  CA  . GLY   A 1 418 ? -5.239  -15.296 -10.874 1.00 72.11  ? 438 GLY   A CA  1 
ATOM   3007 C  C   . GLY   A 1 418 ? -5.562  -15.786 -9.478  1.00 88.40  ? 438 GLY   A C   1 
ATOM   3008 O  O   . GLY   A 1 418 ? -6.077  -16.892 -9.289  1.00 66.01  ? 438 GLY   A O   1 
ATOM   3009 N  N   . PRO   A 1 419 ? -5.270  -14.960 -8.468  1.00 93.61  ? 439 PRO   A N   1 
ATOM   3010 C  CA  . PRO   A 1 419 ? -5.489  -15.390 -7.073  1.00 97.25  ? 439 PRO   A CA  1 
ATOM   3011 C  C   . PRO   A 1 419 ? -6.925  -15.799 -6.759  1.00 100.93 ? 439 PRO   A C   1 
ATOM   3012 O  O   . PRO   A 1 419 ? -7.140  -16.550 -5.798  1.00 95.12  ? 439 PRO   A O   1 
ATOM   3013 C  CB  . PRO   A 1 419 ? -5.067  -14.158 -6.257  1.00 102.12 ? 439 PRO   A CB  1 
ATOM   3014 C  CG  . PRO   A 1 419 ? -4.147  -13.399 -7.158  1.00 89.02  ? 439 PRO   A CG  1 
ATOM   3015 C  CD  . PRO   A 1 419 ? -4.664  -13.619 -8.548  1.00 72.63  ? 439 PRO   A CD  1 
ATOM   3016 N  N   . ARG   A 1 420 ? -7.912  -15.353 -7.533  1.00 100.44 ? 440 ARG   A N   1 
ATOM   3017 C  CA  . ARG   A 1 420 ? -9.310  -15.687 -7.282  1.00 100.26 ? 440 ARG   A CA  1 
ATOM   3018 C  C   . ARG   A 1 420 ? -9.893  -16.544 -8.401  1.00 98.62  ? 440 ARG   A C   1 
ATOM   3019 O  O   . ARG   A 1 420 ? -11.034 -16.353 -8.828  1.00 102.76 ? 440 ARG   A O   1 
ATOM   3020 C  CB  . ARG   A 1 420 ? -10.144 -14.426 -7.081  1.00 99.88  ? 440 ARG   A CB  1 
ATOM   3021 C  CG  . ARG   A 1 420 ? -11.431 -14.666 -6.301  1.00 111.56 ? 440 ARG   A CG  1 
ATOM   3022 C  CD  . ARG   A 1 420 ? -11.929 -13.410 -5.606  1.00 104.95 ? 440 ARG   A CD  1 
ATOM   3023 N  NE  . ARG   A 1 420 ? -12.975 -13.738 -4.646  1.00 66.36  ? 440 ARG   A NE  1 
ATOM   3024 C  CZ  . ARG   A 1 420 ? -13.575 -12.864 -3.849  1.00 107.15 ? 440 ARG   A CZ  1 
ATOM   3025 N  NH1 . ARG   A 1 420 ? -13.263 -11.578 -3.870  1.00 76.36  ? 440 ARG   A NH1 1 
ATOM   3026 N  NH2 . ARG   A 1 420 ? -14.511 -13.293 -3.007  1.00 64.66  ? 440 ARG   A NH2 1 
ATOM   3027 N  N   . ASN   A 1 421 ? -9.115  -17.505 -8.887  1.00 90.60  ? 441 ASN   A N   1 
ATOM   3028 C  CA  . ASN   A 1 421 ? -9.653  -18.490 -9.805  1.00 92.86  ? 441 ASN   A CA  1 
ATOM   3029 C  C   . ASN   A 1 421 ? -10.451 -19.527 -9.016  1.00 83.95  ? 441 ASN   A C   1 
ATOM   3030 O  O   . ASN   A 1 421 ? -10.585 -19.446 -7.791  1.00 79.00  ? 441 ASN   A O   1 
ATOM   3031 C  CB  . ASN   A 1 421 ? -8.526  -19.119 -10.623 1.00 92.32  ? 441 ASN   A CB  1 
ATOM   3032 C  CG  . ASN   A 1 421 ? -7.595  -19.975 -9.787  1.00 92.79  ? 441 ASN   A CG  1 
ATOM   3033 O  OD1 . ASN   A 1 421 ? -7.592  -19.903 -8.557  1.00 93.27  ? 441 ASN   A OD1 1 
ATOM   3034 N  ND2 . ASN   A 1 421 ? -6.789  -20.789 -10.457 1.00 89.31  ? 441 ASN   A ND2 1 
ATOM   3035 N  N   . CYS   A 1 422 ? -11.006 -20.506 -9.722  1.00 86.63  ? 442 CYS   A N   1 
ATOM   3036 C  CA  . CYS   A 1 422 ? -11.737 -21.575 -9.055  1.00 98.81  ? 442 CYS   A CA  1 
ATOM   3037 C  C   . CYS   A 1 422 ? -10.822 -22.305 -8.082  1.00 96.46  ? 442 CYS   A C   1 
ATOM   3038 O  O   . CYS   A 1 422 ? -9.820  -22.901 -8.488  1.00 84.33  ? 442 CYS   A O   1 
ATOM   3039 C  CB  . CYS   A 1 422 ? -12.302 -22.548 -10.086 1.00 92.01  ? 442 CYS   A CB  1 
ATOM   3040 S  SG  . CYS   A 1 422 ? -13.120 -23.995 -9.378  1.00 82.08  ? 442 CYS   A SG  1 
ATOM   3041 N  N   . ILE   A 1 423 ? -11.169 -22.259 -6.794  1.00 108.68 ? 443 ILE   A N   1 
ATOM   3042 C  CA  . ILE   A 1 423 ? -10.314 -22.877 -5.787  1.00 109.54 ? 443 ILE   A CA  1 
ATOM   3043 C  C   . ILE   A 1 423 ? -10.362 -24.397 -5.886  1.00 113.38 ? 443 ILE   A C   1 
ATOM   3044 O  O   . ILE   A 1 423 ? -9.383  -25.076 -5.554  1.00 113.35 ? 443 ILE   A O   1 
ATOM   3045 C  CB  . ILE   A 1 423 ? -10.709 -22.395 -4.380  1.00 103.86 ? 443 ILE   A CB  1 
ATOM   3046 C  CG1 . ILE   A 1 423 ? -9.624  -22.768 -3.372  1.00 107.98 ? 443 ILE   A CG1 1 
ATOM   3047 C  CG2 . ILE   A 1 423 ? -12.034 -22.999 -3.962  1.00 105.72 ? 443 ILE   A CG2 1 
ATOM   3048 C  CD1 . ILE   A 1 423 ? -10.009 -22.489 -1.944  1.00 116.16 ? 443 ILE   A CD1 1 
ATOM   3049 N  N   . GLY   A 1 424 ? -11.479 -24.957 -6.346  1.00 109.22 ? 444 GLY   A N   1 
ATOM   3050 C  CA  . GLY   A 1 424 ? -11.600 -26.395 -6.469  1.00 114.59 ? 444 GLY   A CA  1 
ATOM   3051 C  C   . GLY   A 1 424 ? -11.364 -26.891 -7.880  1.00 113.63 ? 444 GLY   A C   1 
ATOM   3052 O  O   . GLY   A 1 424 ? -11.873 -27.950 -8.263  1.00 113.69 ? 444 GLY   A O   1 
ATOM   3053 N  N   . MET   A 1 425 ? -10.588 -26.130 -8.659  1.00 114.82 ? 445 MET   A N   1 
ATOM   3054 C  CA  . MET   A 1 425 ? -10.315 -26.496 -10.047 1.00 109.80 ? 445 MET   A CA  1 
ATOM   3055 C  C   . MET   A 1 425 ? -9.693  -27.883 -10.148 1.00 115.29 ? 445 MET   A C   1 
ATOM   3056 O  O   . MET   A 1 425 ? -10.163 -28.733 -10.912 1.00 112.74 ? 445 MET   A O   1 
ATOM   3057 C  CB  . MET   A 1 425 ? -9.394  -25.461 -10.695 1.00 91.91  ? 445 MET   A CB  1 
ATOM   3058 C  CG  . MET   A 1 425 ? -8.916  -25.874 -12.083 1.00 101.86 ? 445 MET   A CG  1 
ATOM   3059 S  SD  . MET   A 1 425 ? -7.365  -25.097 -12.576 1.00 109.29 ? 445 MET   A SD  1 
ATOM   3060 C  CE  . MET   A 1 425 ? -6.671  -24.699 -10.973 1.00 117.89 ? 445 MET   A CE  1 
ATOM   3061 N  N   . ARG   A 1 426 ? -8.625  -28.126 -9.386  1.00 110.31 ? 446 ARG   A N   1 
ATOM   3062 C  CA  . ARG   A 1 426 ? -7.934  -29.409 -9.462  1.00 113.97 ? 446 ARG   A CA  1 
ATOM   3063 C  C   . ARG   A 1 426 ? -8.824  -30.549 -8.979  1.00 114.22 ? 446 ARG   A C   1 
ATOM   3064 O  O   . ARG   A 1 426 ? -8.879  -31.612 -9.608  1.00 114.17 ? 446 ARG   A O   1 
ATOM   3065 C  CB  . ARG   A 1 426 ? -6.637  -29.350 -8.656  1.00 123.22 ? 446 ARG   A CB  1 
ATOM   3066 C  CG  . ARG   A 1 426 ? -5.535  -28.565 -9.347  1.00 121.81 ? 446 ARG   A CG  1 
ATOM   3067 C  CD  . ARG   A 1 426 ? -4.449  -28.130 -8.379  1.00 124.43 ? 446 ARG   A CD  1 
ATOM   3068 N  NE  . ARG   A 1 426 ? -3.205  -28.867 -8.570  1.00 143.21 ? 446 ARG   A NE  1 
ATOM   3069 C  CZ  . ARG   A 1 426 ? -2.651  -29.653 -7.658  1.00 143.88 ? 446 ARG   A CZ  1 
ATOM   3070 N  NH1 . ARG   A 1 426 ? -3.205  -29.830 -6.470  1.00 152.60 ? 446 ARG   A NH1 1 
ATOM   3071 N  NH2 . ARG   A 1 426 ? -1.507  -30.269 -7.941  1.00 132.03 ? 446 ARG   A NH2 1 
ATOM   3072 N  N   . PHE   A 1 427 ? -9.529  -30.345 -7.863  1.00 116.16 ? 447 PHE   A N   1 
ATOM   3073 C  CA  . PHE   A 1 427 ? -10.407 -31.386 -7.334  1.00 120.03 ? 447 PHE   A CA  1 
ATOM   3074 C  C   . PHE   A 1 427 ? -11.497 -31.748 -8.334  1.00 118.62 ? 447 PHE   A C   1 
ATOM   3075 O  O   . PHE   A 1 427 ? -11.740 -32.929 -8.608  1.00 131.38 ? 447 PHE   A O   1 
ATOM   3076 C  CB  . PHE   A 1 427 ? -11.029 -30.932 -6.010  1.00 127.67 ? 447 PHE   A CB  1 
ATOM   3077 C  CG  . PHE   A 1 427 ? -12.237 -31.737 -5.592  1.00 132.48 ? 447 PHE   A CG  1 
ATOM   3078 C  CD1 . PHE   A 1 427 ? -13.521 -31.314 -5.916  1.00 134.32 ? 447 PHE   A CD1 1 
ATOM   3079 C  CD2 . PHE   A 1 427 ? -12.089 -32.912 -4.871  1.00 134.97 ? 447 PHE   A CD2 1 
ATOM   3080 C  CE1 . PHE   A 1 427 ? -14.633 -32.051 -5.537  1.00 139.55 ? 447 PHE   A CE1 1 
ATOM   3081 C  CE2 . PHE   A 1 427 ? -13.198 -33.653 -4.485  1.00 145.53 ? 447 PHE   A CE2 1 
ATOM   3082 C  CZ  . PHE   A 1 427 ? -14.471 -33.220 -4.819  1.00 147.81 ? 447 PHE   A CZ  1 
ATOM   3083 N  N   . ALA   A 1 428 ? -12.175 -30.736 -8.880  1.00 118.35 ? 448 ALA   A N   1 
ATOM   3084 C  CA  . ALA   A 1 428 ? -13.279 -30.983 -9.802  1.00 119.35 ? 448 ALA   A CA  1 
ATOM   3085 C  C   . ALA   A 1 428 ? -12.814 -31.744 -11.037 1.00 121.74 ? 448 ALA   A C   1 
ATOM   3086 O  O   . ALA   A 1 428 ? -13.494 -32.668 -11.497 1.00 131.19 ? 448 ALA   A O   1 
ATOM   3087 C  CB  . ALA   A 1 428 ? -13.930 -29.660 -10.198 1.00 105.50 ? 448 ALA   A CB  1 
ATOM   3088 N  N   . LEU   A 1 429 ? -11.660 -31.366 -11.591 1.00 115.37 ? 449 LEU   A N   1 
ATOM   3089 C  CA  . LEU   A 1 429 ? -11.102 -32.114 -12.712 1.00 117.28 ? 449 LEU   A CA  1 
ATOM   3090 C  C   . LEU   A 1 429 ? -10.886 -33.575 -12.341 1.00 127.32 ? 449 LEU   A C   1 
ATOM   3091 O  O   . LEU   A 1 429 ? -11.202 -34.479 -13.123 1.00 130.49 ? 449 LEU   A O   1 
ATOM   3092 C  CB  . LEU   A 1 429 ? -9.788  -31.480 -13.163 1.00 103.16 ? 449 LEU   A CB  1 
ATOM   3093 C  CG  . LEU   A 1 429 ? -9.844  -30.123 -13.864 1.00 118.89 ? 449 LEU   A CG  1 
ATOM   3094 C  CD1 . LEU   A 1 429 ? -8.438  -29.623 -14.158 1.00 119.00 ? 449 LEU   A CD1 1 
ATOM   3095 C  CD2 . LEU   A 1 429 ? -10.654 -30.221 -15.145 1.00 102.29 ? 449 LEU   A CD2 1 
ATOM   3096 N  N   . MET   A 1 430 ? -10.359 -33.823 -11.142 1.00 131.96 ? 450 MET   A N   1 
ATOM   3097 C  CA  . MET   A 1 430 ? -10.103 -35.193 -10.711 1.00 130.89 ? 450 MET   A CA  1 
ATOM   3098 C  C   . MET   A 1 430 ? -11.404 -35.943 -10.452 1.00 136.86 ? 450 MET   A C   1 
ATOM   3099 O  O   . MET   A 1 430 ? -11.554 -37.101 -10.858 1.00 130.33 ? 450 MET   A O   1 
ATOM   3100 C  CB  . MET   A 1 430 ? -9.222  -35.192 -9.463  1.00 137.70 ? 450 MET   A CB  1 
ATOM   3101 C  CG  . MET   A 1 430 ? -9.169  -36.523 -8.734  1.00 141.98 ? 450 MET   A CG  1 
ATOM   3102 S  SD  . MET   A 1 430 ? -7.502  -36.894 -8.170  1.00 145.87 ? 450 MET   A SD  1 
ATOM   3103 C  CE  . MET   A 1 430 ? -6.665  -37.100 -9.740  1.00 156.54 ? 450 MET   A CE  1 
ATOM   3104 N  N   . ASN   A 1 431 ? -12.360 -35.297 -9.778  1.00 130.63 ? 451 ASN   A N   1 
ATOM   3105 C  CA  . ASN   A 1 431 ? -13.622 -35.961 -9.465  1.00 133.40 ? 451 ASN   A CA  1 
ATOM   3106 C  C   . ASN   A 1 431 ? -14.382 -36.329 -10.735 1.00 132.01 ? 451 ASN   A C   1 
ATOM   3107 O  O   . ASN   A 1 431 ? -14.946 -37.425 -10.835 1.00 132.65 ? 451 ASN   A O   1 
ATOM   3108 C  CB  . ASN   A 1 431 ? -14.474 -35.067 -8.563  1.00 133.27 ? 451 ASN   A CB  1 
ATOM   3109 C  CG  . ASN   A 1 431 ? -15.778 -35.724 -8.155  1.00 140.99 ? 451 ASN   A CG  1 
ATOM   3110 O  OD1 . ASN   A 1 431 ? -15.850 -36.940 -7.990  1.00 149.73 ? 451 ASN   A OD1 1 
ATOM   3111 N  ND2 . ASN   A 1 431 ? -16.822 -34.916 -7.994  1.00 139.12 ? 451 ASN   A ND2 1 
ATOM   3112 N  N   . MET   A 1 432 ? -14.401 -35.429 -11.720 1.00 145.53 ? 452 MET   A N   1 
ATOM   3113 C  CA  . MET   A 1 432 ? -15.076 -35.727 -12.980 1.00 137.84 ? 452 MET   A CA  1 
ATOM   3114 C  C   . MET   A 1 432 ? -14.358 -36.836 -13.739 1.00 135.92 ? 452 MET   A C   1 
ATOM   3115 O  O   . MET   A 1 432 ? -14.992 -37.780 -14.225 1.00 134.87 ? 452 MET   A O   1 
ATOM   3116 C  CB  . MET   A 1 432 ? -15.173 -34.467 -13.841 1.00 108.26 ? 452 MET   A CB  1 
ATOM   3117 C  CG  . MET   A 1 432 ? -16.050 -33.373 -13.263 1.00 125.35 ? 452 MET   A CG  1 
ATOM   3118 S  SD  . MET   A 1 432 ? -16.244 -31.987 -14.399 1.00 116.16 ? 452 MET   A SD  1 
ATOM   3119 C  CE  . MET   A 1 432 ? -14.533 -31.542 -14.691 1.00 107.88 ? 452 MET   A CE  1 
ATOM   3120 N  N   . LYS   A 1 433 ? -13.032 -36.735 -13.854 1.00 120.47 ? 453 LYS   A N   1 
ATOM   3121 C  CA  . LYS   A 1 433 ? -12.275 -37.723 -14.618 1.00 125.54 ? 453 LYS   A CA  1 
ATOM   3122 C  C   . LYS   A 1 433 ? -12.376 -39.108 -13.992 1.00 138.43 ? 453 LYS   A C   1 
ATOM   3123 O  O   . LYS   A 1 433 ? -12.531 -40.107 -14.704 1.00 128.61 ? 453 LYS   A O   1 
ATOM   3124 C  CB  . LYS   A 1 433 ? -10.815 -37.288 -14.734 1.00 123.21 ? 453 LYS   A CB  1 
ATOM   3125 C  CG  . LYS   A 1 433 ? -10.575 -36.187 -15.755 1.00 113.57 ? 453 LYS   A CG  1 
ATOM   3126 C  CD  . LYS   A 1 433 ? -9.127  -35.726 -15.745 1.00 120.25 ? 453 LYS   A CD  1 
ATOM   3127 C  CE  . LYS   A 1 433 ? -8.850  -34.753 -16.880 1.00 118.29 ? 453 LYS   A CE  1 
ATOM   3128 N  NZ  . LYS   A 1 433 ? -7.477  -34.184 -16.793 1.00 120.33 ? 453 LYS   A NZ  1 
ATOM   3129 N  N   . LEU   A 1 434 ? -12.281 -39.191 -12.661 1.00 141.51 ? 454 LEU   A N   1 
ATOM   3130 C  CA  . LEU   A 1 434 ? -12.472 -40.473 -11.989 1.00 130.83 ? 454 LEU   A CA  1 
ATOM   3131 C  C   . LEU   A 1 434 ? -13.854 -41.042 -12.282 1.00 134.37 ? 454 LEU   A C   1 
ATOM   3132 O  O   . LEU   A 1 434 ? -14.016 -42.261 -12.420 1.00 144.93 ? 454 LEU   A O   1 
ATOM   3133 C  CB  . LEU   A 1 434 ? -12.265 -40.318 -10.482 1.00 132.65 ? 454 LEU   A CB  1 
ATOM   3134 C  CG  . LEU   A 1 434 ? -10.823 -40.317 -9.973  1.00 137.06 ? 454 LEU   A CG  1 
ATOM   3135 C  CD1 . LEU   A 1 434 ? -10.787 -40.060 -8.477  1.00 143.61 ? 454 LEU   A CD1 1 
ATOM   3136 C  CD2 . LEU   A 1 434 ? -10.153 -41.636 -10.298 1.00 152.40 ? 454 LEU   A CD2 1 
ATOM   3137 N  N   . ALA   A 1 435 ? -14.861 -40.172 -12.392 1.00 141.09 ? 455 ALA   A N   1 
ATOM   3138 C  CA  . ALA   A 1 435 ? -16.206 -40.627 -12.727 1.00 140.06 ? 455 ALA   A CA  1 
ATOM   3139 C  C   . ALA   A 1 435 ? -16.296 -41.063 -14.184 1.00 142.74 ? 455 ALA   A C   1 
ATOM   3140 O  O   . ALA   A 1 435 ? -16.922 -42.084 -14.494 1.00 151.01 ? 455 ALA   A O   1 
ATOM   3141 C  CB  . ALA   A 1 435 ? -17.221 -39.523 -12.437 1.00 136.98 ? 455 ALA   A CB  1 
ATOM   3142 N  N   . LEU   A 1 436 ? -15.677 -40.303 -15.091 1.00 135.76 ? 456 LEU   A N   1 
ATOM   3143 C  CA  . LEU   A 1 436 ? -15.739 -40.638 -16.510 1.00 131.97 ? 456 LEU   A CA  1 
ATOM   3144 C  C   . LEU   A 1 436 ? -15.063 -41.968 -16.813 1.00 145.09 ? 456 LEU   A C   1 
ATOM   3145 O  O   . LEU   A 1 436 ? -15.504 -42.696 -17.710 1.00 147.52 ? 456 LEU   A O   1 
ATOM   3146 C  CB  . LEU   A 1 436 ? -15.103 -39.523 -17.340 1.00 129.39 ? 456 LEU   A CB  1 
ATOM   3147 C  CG  . LEU   A 1 436 ? -15.936 -38.259 -17.544 1.00 130.28 ? 456 LEU   A CG  1 
ATOM   3148 C  CD1 . LEU   A 1 436 ? -15.177 -37.270 -18.410 1.00 125.59 ? 456 LEU   A CD1 1 
ATOM   3149 C  CD2 . LEU   A 1 436 ? -17.277 -38.605 -18.171 1.00 134.86 ? 456 LEU   A CD2 1 
ATOM   3150 N  N   . ILE   A 1 437 ? -13.998 -42.301 -16.084 1.00 147.24 ? 457 ILE   A N   1 
ATOM   3151 C  CA  . ILE   A 1 437 ? -13.290 -43.556 -16.325 1.00 148.81 ? 457 ILE   A CA  1 
ATOM   3152 C  C   . ILE   A 1 437 ? -14.177 -44.745 -15.977 1.00 156.13 ? 457 ILE   A C   1 
ATOM   3153 O  O   . ILE   A 1 437 ? -14.369 -45.656 -16.791 1.00 160.41 ? 457 ILE   A O   1 
ATOM   3154 C  CB  . ILE   A 1 437 ? -11.975 -43.590 -15.528 1.00 150.82 ? 457 ILE   A CB  1 
ATOM   3155 C  CG1 . ILE   A 1 437 ? -10.999 -42.545 -16.069 1.00 149.11 ? 457 ILE   A CG1 1 
ATOM   3156 C  CG2 . ILE   A 1 437 ? -11.371 -44.985 -15.564 1.00 165.41 ? 457 ILE   A CG2 1 
ATOM   3157 C  CD1 . ILE   A 1 437 ? -9.815  -42.315 -15.177 1.00 146.87 ? 457 ILE   A CD1 1 
ATOM   3158 N  N   . ARG   A 1 438 ? -14.732 -44.749 -14.763 1.00 167.28 ? 458 ARG   A N   1 
ATOM   3159 C  CA  . ARG   A 1 438 ? -15.519 -45.890 -14.304 1.00 171.54 ? 458 ARG   A CA  1 
ATOM   3160 C  C   . ARG   A 1 438 ? -16.778 -46.080 -15.140 1.00 168.12 ? 458 ARG   A C   1 
ATOM   3161 O  O   . ARG   A 1 438 ? -17.228 -47.215 -15.336 1.00 175.47 ? 458 ARG   A O   1 
ATOM   3162 C  CB  . ARG   A 1 438 ? -15.877 -45.708 -12.828 1.00 181.33 ? 458 ARG   A CB  1 
ATOM   3163 C  CG  . ARG   A 1 438 ? -15.531 -46.894 -11.947 1.00 188.59 ? 458 ARG   A CG  1 
ATOM   3164 C  CD  . ARG   A 1 438 ? -14.129 -47.404 -12.235 1.00 192.50 ? 458 ARG   A CD  1 
ATOM   3165 N  NE  . ARG   A 1 438 ? -13.745 -48.487 -11.337 1.00 203.17 ? 458 ARG   A NE  1 
ATOM   3166 C  CZ  . ARG   A 1 438 ? -12.836 -49.409 -11.624 1.00 200.22 ? 458 ARG   A CZ  1 
ATOM   3167 N  NH1 . ARG   A 1 438 ? -12.212 -49.426 -12.790 1.00 195.19 ? 458 ARG   A NH1 1 
ATOM   3168 N  NH2 . ARG   A 1 438 ? -12.554 -50.344 -10.721 1.00 200.69 ? 458 ARG   A NH2 1 
ATOM   3169 N  N   . VAL   A 1 439 ? -17.356 -44.990 -15.642 1.00 159.63 ? 459 VAL   A N   1 
ATOM   3170 C  CA  . VAL   A 1 439 ? -18.592 -45.091 -16.409 1.00 155.17 ? 459 VAL   A CA  1 
ATOM   3171 C  C   . VAL   A 1 439 ? -18.319 -45.626 -17.809 1.00 160.82 ? 459 VAL   A C   1 
ATOM   3172 O  O   . VAL   A 1 439 ? -18.960 -46.582 -18.261 1.00 161.90 ? 459 VAL   A O   1 
ATOM   3173 C  CB  . VAL   A 1 439 ? -19.302 -43.726 -16.454 1.00 148.87 ? 459 VAL   A CB  1 
ATOM   3174 C  CG1 . VAL   A 1 439 ? -20.413 -43.742 -17.488 1.00 151.30 ? 459 VAL   A CG1 1 
ATOM   3175 C  CG2 . VAL   A 1 439 ? -19.858 -43.377 -15.086 1.00 156.46 ? 459 VAL   A CG2 1 
ATOM   3176 N  N   . LEU   A 1 440 ? -17.363 -45.019 -18.516 1.00 152.46 ? 460 LEU   A N   1 
ATOM   3177 C  CA  . LEU   A 1 440 ? -17.054 -45.445 -19.876 1.00 155.95 ? 460 LEU   A CA  1 
ATOM   3178 C  C   . LEU   A 1 440 ? -16.344 -46.792 -19.917 1.00 161.62 ? 460 LEU   A C   1 
ATOM   3179 O  O   . LEU   A 1 440 ? -16.349 -47.447 -20.966 1.00 159.08 ? 460 LEU   A O   1 
ATOM   3180 C  CB  . LEU   A 1 440 ? -16.212 -44.379 -20.574 1.00 147.79 ? 460 LEU   A CB  1 
ATOM   3181 C  CG  . LEU   A 1 440 ? -16.934 -43.047 -20.787 1.00 143.58 ? 460 LEU   A CG  1 
ATOM   3182 C  CD1 . LEU   A 1 440 ? -15.950 -41.969 -21.197 1.00 115.96 ? 460 LEU   A CD1 1 
ATOM   3183 C  CD2 . LEU   A 1 440 ? -18.037 -43.194 -21.826 1.00 148.47 ? 460 LEU   A CD2 1 
ATOM   3184 N  N   . GLN   A 1 441 ? -15.734 -47.219 -18.809 1.00 166.24 ? 461 GLN   A N   1 
ATOM   3185 C  CA  . GLN   A 1 441 ? -15.182 -48.568 -18.737 1.00 169.21 ? 461 GLN   A CA  1 
ATOM   3186 C  C   . GLN   A 1 441 ? -16.260 -49.635 -18.852 1.00 176.30 ? 461 GLN   A C   1 
ATOM   3187 O  O   . GLN   A 1 441 ? -15.954 -50.770 -19.233 1.00 171.90 ? 461 GLN   A O   1 
ATOM   3188 C  CB  . GLN   A 1 441 ? -14.418 -48.764 -17.425 1.00 170.49 ? 461 GLN   A CB  1 
ATOM   3189 C  CG  . GLN   A 1 441 ? -12.907 -48.695 -17.551 1.00 169.15 ? 461 GLN   A CG  1 
ATOM   3190 C  CD  . GLN   A 1 441 ? -12.207 -48.837 -16.212 1.00 172.67 ? 461 GLN   A CD  1 
ATOM   3191 O  OE1 . GLN   A 1 441 ? -12.851 -48.865 -15.163 1.00 176.22 ? 461 GLN   A OE1 1 
ATOM   3192 N  NE2 . GLN   A 1 441 ? -10.882 -48.926 -16.242 1.00 170.06 ? 461 GLN   A NE2 1 
ATOM   3193 N  N   . ASN   A 1 442 ? -17.508 -49.302 -18.533 1.00 175.87 ? 462 ASN   A N   1 
ATOM   3194 C  CA  . ASN   A 1 442 ? -18.584 -50.281 -18.477 1.00 179.32 ? 462 ASN   A CA  1 
ATOM   3195 C  C   . ASN   A 1 442 ? -19.712 -50.030 -19.466 1.00 179.13 ? 462 ASN   A C   1 
ATOM   3196 O  O   . ASN   A 1 442 ? -20.353 -50.992 -19.895 1.00 189.76 ? 462 ASN   A O   1 
ATOM   3197 C  CB  . ASN   A 1 442 ? -19.182 -50.336 -17.060 1.00 183.46 ? 462 ASN   A CB  1 
ATOM   3198 C  CG  . ASN   A 1 442 ? -18.285 -51.061 -16.071 1.00 189.37 ? 462 ASN   A CG  1 
ATOM   3199 O  OD1 . ASN   A 1 442 ? -18.560 -52.197 -15.682 1.00 197.54 ? 462 ASN   A OD1 1 
ATOM   3200 N  ND2 . ASN   A 1 442 ? -17.207 -50.404 -15.657 1.00 188.08 ? 462 ASN   A ND2 1 
ATOM   3201 N  N   . PHE   A 1 443 ? -19.978 -48.779 -19.839 1.00 164.80 ? 463 PHE   A N   1 
ATOM   3202 C  CA  . PHE   A 1 443 ? -21.129 -48.456 -20.666 1.00 167.90 ? 463 PHE   A CA  1 
ATOM   3203 C  C   . PHE   A 1 443 ? -20.728 -47.574 -21.839 1.00 163.71 ? 463 PHE   A C   1 
ATOM   3204 O  O   . PHE   A 1 443 ? -19.812 -46.753 -21.742 1.00 159.42 ? 463 PHE   A O   1 
ATOM   3205 C  CB  . PHE   A 1 443 ? -22.226 -47.739 -19.861 1.00 165.79 ? 463 PHE   A CB  1 
ATOM   3206 C  CG  . PHE   A 1 443 ? -22.650 -48.469 -18.621 1.00 171.01 ? 463 PHE   A CG  1 
ATOM   3207 C  CD1 . PHE   A 1 443 ? -23.491 -49.568 -18.697 1.00 181.27 ? 463 PHE   A CD1 1 
ATOM   3208 C  CD2 . PHE   A 1 443 ? -22.221 -48.043 -17.374 1.00 166.58 ? 463 PHE   A CD2 1 
ATOM   3209 C  CE1 . PHE   A 1 443 ? -23.886 -50.237 -17.552 1.00 184.69 ? 463 PHE   A CE1 1 
ATOM   3210 C  CE2 . PHE   A 1 443 ? -22.611 -48.704 -16.226 1.00 171.61 ? 463 PHE   A CE2 1 
ATOM   3211 C  CZ  . PHE   A 1 443 ? -23.445 -49.803 -16.314 1.00 183.66 ? 463 PHE   A CZ  1 
ATOM   3212 N  N   . SER   A 1 444 ? -21.430 -47.762 -22.950 1.00 162.30 ? 464 SER   A N   1 
ATOM   3213 C  CA  . SER   A 1 444 ? -21.424 -46.834 -24.068 1.00 157.57 ? 464 SER   A CA  1 
ATOM   3214 C  C   . SER   A 1 444 ? -22.726 -46.042 -24.067 1.00 162.16 ? 464 SER   A C   1 
ATOM   3215 O  O   . SER   A 1 444 ? -23.714 -46.430 -23.439 1.00 170.01 ? 464 SER   A O   1 
ATOM   3216 C  CB  . SER   A 1 444 ? -21.244 -47.573 -25.397 1.00 146.13 ? 464 SER   A CB  1 
ATOM   3217 O  OG  . SER   A 1 444 ? -19.920 -48.062 -25.531 1.00 149.65 ? 464 SER   A OG  1 
ATOM   3218 N  N   . PHE   A 1 445 ? -22.717 -44.913 -24.770 1.00 156.87 ? 465 PHE   A N   1 
ATOM   3219 C  CA  . PHE   A 1 445 ? -23.844 -43.991 -24.751 1.00 156.50 ? 465 PHE   A CA  1 
ATOM   3220 C  C   . PHE   A 1 445 ? -24.230 -43.615 -26.173 1.00 154.30 ? 465 PHE   A C   1 
ATOM   3221 O  O   . PHE   A 1 445 ? -23.369 -43.248 -26.978 1.00 149.57 ? 465 PHE   A O   1 
ATOM   3222 C  CB  . PHE   A 1 445 ? -23.508 -42.741 -23.934 1.00 144.49 ? 465 PHE   A CB  1 
ATOM   3223 C  CG  . PHE   A 1 445 ? -23.411 -42.996 -22.457 1.00 152.01 ? 465 PHE   A CG  1 
ATOM   3224 C  CD1 . PHE   A 1 445 ? -22.299 -43.622 -21.918 1.00 151.00 ? 465 PHE   A CD1 1 
ATOM   3225 C  CD2 . PHE   A 1 445 ? -24.435 -42.613 -21.609 1.00 160.16 ? 465 PHE   A CD2 1 
ATOM   3226 C  CE1 . PHE   A 1 445 ? -22.210 -43.861 -20.562 1.00 151.50 ? 465 PHE   A CE1 1 
ATOM   3227 C  CE2 . PHE   A 1 445 ? -24.351 -42.848 -20.250 1.00 154.14 ? 465 PHE   A CE2 1 
ATOM   3228 C  CZ  . PHE   A 1 445 ? -23.237 -43.473 -19.726 1.00 147.51 ? 465 PHE   A CZ  1 
ATOM   3229 N  N   . LYS   A 1 446 ? -25.524 -43.709 -26.474 1.00 157.13 ? 466 LYS   A N   1 
ATOM   3230 C  CA  . LYS   A 1 446 ? -26.080 -43.391 -27.779 1.00 162.07 ? 466 LYS   A CA  1 
ATOM   3231 C  C   . LYS   A 1 446 ? -27.239 -42.419 -27.627 1.00 158.66 ? 466 LYS   A C   1 
ATOM   3232 O  O   . LYS   A 1 446 ? -27.878 -42.372 -26.570 1.00 157.00 ? 466 LYS   A O   1 
ATOM   3233 C  CB  . LYS   A 1 446 ? -26.576 -44.656 -28.498 1.00 161.99 ? 466 LYS   A CB  1 
ATOM   3234 C  CG  . LYS   A 1 446 ? -25.583 -45.805 -28.519 1.00 163.04 ? 466 LYS   A CG  1 
ATOM   3235 C  CD  . LYS   A 1 446 ? -24.335 -45.443 -29.300 1.00 163.12 ? 466 LYS   A CD  1 
ATOM   3236 C  CE  . LYS   A 1 446 ? -23.372 -46.618 -29.379 1.00 164.99 ? 466 LYS   A CE  1 
ATOM   3237 N  NZ  . LYS   A 1 446 ? -23.946 -47.774 -30.125 1.00 164.78 ? 466 LYS   A NZ  1 
ATOM   3238 N  N   . PRO   A 1 447 ? -27.531 -41.628 -28.659 1.00 160.58 ? 467 PRO   A N   1 
ATOM   3239 C  CA  . PRO   A 1 447 ? -28.692 -40.735 -28.591 1.00 162.56 ? 467 PRO   A CA  1 
ATOM   3240 C  C   . PRO   A 1 447 ? -29.999 -41.510 -28.574 1.00 170.80 ? 467 PRO   A C   1 
ATOM   3241 O  O   . PRO   A 1 447 ? -30.103 -42.622 -29.098 1.00 164.24 ? 467 PRO   A O   1 
ATOM   3242 C  CB  . PRO   A 1 447 ? -28.568 -39.889 -29.864 1.00 162.27 ? 467 PRO   A CB  1 
ATOM   3243 C  CG  . PRO   A 1 447 ? -27.136 -39.993 -30.258 1.00 155.98 ? 467 PRO   A CG  1 
ATOM   3244 C  CD  . PRO   A 1 447 ? -26.717 -41.376 -29.860 1.00 156.42 ? 467 PRO   A CD  1 
ATOM   3245 N  N   . CYS   A 1 448 ? -31.007 -40.902 -27.963 1.00 171.39 ? 468 CYS   A N   1 
ATOM   3246 C  CA  . CYS   A 1 448 ? -32.339 -41.480 -27.866 1.00 174.25 ? 468 CYS   A CA  1 
ATOM   3247 C  C   . CYS   A 1 448 ? -33.308 -40.729 -28.775 1.00 179.85 ? 468 CYS   A C   1 
ATOM   3248 O  O   . CYS   A 1 448 ? -32.953 -39.756 -29.447 1.00 176.73 ? 468 CYS   A O   1 
ATOM   3249 C  CB  . CYS   A 1 448 ? -32.826 -41.466 -26.416 1.00 174.20 ? 468 CYS   A CB  1 
ATOM   3250 S  SG  . CYS   A 1 448 ? -32.552 -43.001 -25.509 1.00 183.16 ? 468 CYS   A SG  1 
ATOM   3251 N  N   . LYS   A 1 449 ? -34.554 -41.204 -28.790 1.00 190.62 ? 469 LYS   A N   1 
ATOM   3252 C  CA  . LYS   A 1 449 ? -35.599 -40.534 -29.559 1.00 194.27 ? 469 LYS   A CA  1 
ATOM   3253 C  C   . LYS   A 1 449 ? -35.924 -39.164 -28.974 1.00 192.07 ? 469 LYS   A C   1 
ATOM   3254 O  O   . LYS   A 1 449 ? -36.098 -38.191 -29.717 1.00 193.60 ? 469 LYS   A O   1 
ATOM   3255 C  CB  . LYS   A 1 449 ? -36.845 -41.419 -29.610 1.00 203.30 ? 469 LYS   A CB  1 
ATOM   3256 C  CG  . LYS   A 1 449 ? -38.171 -40.674 -29.607 1.00 207.78 ? 469 LYS   A CG  1 
ATOM   3257 C  CD  . LYS   A 1 449 ? -39.332 -41.652 -29.499 1.00 218.18 ? 469 LYS   A CD  1 
ATOM   3258 C  CE  . LYS   A 1 449 ? -40.644 -40.948 -29.190 1.00 228.05 ? 469 LYS   A CE  1 
ATOM   3259 N  NZ  . LYS   A 1 449 ? -41.742 -41.932 -28.971 1.00 237.03 ? 469 LYS   A NZ  1 
ATOM   3260 N  N   . GLU   A 1 450 ? -35.998 -39.066 -27.649 1.00 183.79 ? 470 GLU   A N   1 
ATOM   3261 C  CA  . GLU   A 1 450 ? -36.299 -37.814 -26.970 1.00 185.51 ? 470 GLU   A CA  1 
ATOM   3262 C  C   . GLU   A 1 450 ? -35.049 -37.013 -26.626 1.00 181.11 ? 470 GLU   A C   1 
ATOM   3263 O  O   . GLU   A 1 450 ? -35.143 -36.034 -25.879 1.00 166.28 ? 470 GLU   A O   1 
ATOM   3264 C  CB  . GLU   A 1 450 ? -37.107 -38.086 -25.699 1.00 186.78 ? 470 GLU   A CB  1 
ATOM   3265 C  CG  . GLU   A 1 450 ? -36.461 -39.088 -24.759 1.00 191.39 ? 470 GLU   A CG  1 
ATOM   3266 C  CD  . GLU   A 1 450 ? -37.381 -39.501 -23.628 1.00 200.48 ? 470 GLU   A CD  1 
ATOM   3267 O  OE1 . GLU   A 1 450 ? -38.379 -38.791 -23.381 1.00 202.11 ? 470 GLU   A OE1 1 
ATOM   3268 O  OE2 . GLU   A 1 450 ? -37.110 -40.541 -22.991 1.00 205.28 ? 470 GLU   A OE2 1 
ATOM   3269 N  N   . THR   A 1 451 ? -33.889 -37.405 -27.144 1.00 176.63 ? 471 THR   A N   1 
ATOM   3270 C  CA  . THR   A 1 451 ? -32.666 -36.651 -26.904 1.00 169.34 ? 471 THR   A CA  1 
ATOM   3271 C  C   . THR   A 1 451 ? -32.674 -35.371 -27.733 1.00 160.15 ? 471 THR   A C   1 
ATOM   3272 O  O   . THR   A 1 451 ? -32.825 -35.415 -28.959 1.00 154.46 ? 471 THR   A O   1 
ATOM   3273 C  CB  . THR   A 1 451 ? -31.441 -37.498 -27.239 1.00 166.69 ? 471 THR   A CB  1 
ATOM   3274 O  OG1 . THR   A 1 451 ? -31.315 -38.563 -26.289 1.00 169.80 ? 471 THR   A OG1 1 
ATOM   3275 C  CG2 . THR   A 1 451 ? -30.182 -36.646 -27.207 1.00 154.33 ? 471 THR   A CG2 1 
ATOM   3276 N  N   . GLN   A 1 452 ? -32.506 -34.233 -27.064 1.00 154.80 ? 472 GLN   A N   1 
ATOM   3277 C  CA  . GLN   A 1 452 ? -32.527 -32.934 -27.731 1.00 151.06 ? 472 GLN   A CA  1 
ATOM   3278 C  C   . GLN   A 1 452 ? -31.255 -32.760 -28.553 1.00 157.68 ? 472 GLN   A C   1 
ATOM   3279 O  O   . GLN   A 1 452 ? -30.172 -32.541 -28.001 1.00 159.66 ? 472 GLN   A O   1 
ATOM   3280 C  CB  . GLN   A 1 452 ? -32.672 -31.822 -26.697 1.00 136.88 ? 472 GLN   A CB  1 
ATOM   3281 C  CG  . GLN   A 1 452 ? -32.917 -30.440 -27.282 1.00 131.52 ? 472 GLN   A CG  1 
ATOM   3282 C  CD  . GLN   A 1 452 ? -33.092 -29.383 -26.208 1.00 150.11 ? 472 GLN   A CD  1 
ATOM   3283 O  OE1 . GLN   A 1 452 ? -32.383 -29.383 -25.201 1.00 146.27 ? 472 GLN   A OE1 1 
ATOM   3284 N  NE2 . GLN   A 1 452 ? -34.046 -28.482 -26.411 1.00 150.49 ? 472 GLN   A NE2 1 
ATOM   3285 N  N   . ILE   A 1 453 ? -31.383 -32.860 -29.877 1.00 146.48 ? 473 ILE   A N   1 
ATOM   3286 C  CA  . ILE   A 1 453 ? -30.268 -32.689 -30.793 1.00 150.92 ? 473 ILE   A CA  1 
ATOM   3287 C  C   . ILE   A 1 453 ? -30.688 -31.701 -31.880 1.00 152.52 ? 473 ILE   A C   1 
ATOM   3288 O  O   . ILE   A 1 453 ? -31.629 -31.982 -32.629 1.00 164.46 ? 473 ILE   A O   1 
ATOM   3289 C  CB  . ILE   A 1 453 ? -29.811 -34.012 -31.428 1.00 155.73 ? 473 ILE   A CB  1 
ATOM   3290 C  CG1 . ILE   A 1 453 ? -29.400 -35.008 -30.344 1.00 154.64 ? 473 ILE   A CG1 1 
ATOM   3291 C  CG2 . ILE   A 1 453 ? -28.662 -33.769 -32.400 1.00 148.72 ? 473 ILE   A CG2 1 
ATOM   3292 C  CD1 . ILE   A 1 453 ? -28.945 -36.341 -30.886 1.00 158.14 ? 473 ILE   A CD1 1 
ATOM   3293 N  N   . PRO   A 1 454 ? -30.029 -30.548 -32.010 1.00 156.22 ? 474 PRO   A N   1 
ATOM   3294 C  CA  . PRO   A 1 454 ? -28.893 -30.073 -31.208 1.00 146.47 ? 474 PRO   A CA  1 
ATOM   3295 C  C   . PRO   A 1 454 ? -29.342 -29.576 -29.839 1.00 140.28 ? 474 PRO   A C   1 
ATOM   3296 O  O   . PRO   A 1 454 ? -30.481 -29.146 -29.677 1.00 135.35 ? 474 PRO   A O   1 
ATOM   3297 C  CB  . PRO   A 1 454 ? -28.316 -28.947 -32.073 1.00 141.65 ? 474 PRO   A CB  1 
ATOM   3298 C  CG  . PRO   A 1 454 ? -29.521 -28.383 -32.771 1.00 152.66 ? 474 PRO   A CG  1 
ATOM   3299 C  CD  . PRO   A 1 454 ? -30.399 -29.579 -33.059 1.00 153.42 ? 474 PRO   A CD  1 
ATOM   3300 N  N   . LEU   A 1 455 ? -28.473 -29.630 -28.835 1.00 145.47 ? 475 LEU   A N   1 
ATOM   3301 C  CA  . LEU   A 1 455 ? -28.849 -29.188 -27.500 1.00 139.03 ? 475 LEU   A CA  1 
ATOM   3302 C  C   . LEU   A 1 455 ? -29.069 -27.681 -27.480 1.00 137.31 ? 475 LEU   A C   1 
ATOM   3303 O  O   . LEU   A 1 455 ? -28.215 -26.911 -27.929 1.00 134.10 ? 475 LEU   A O   1 
ATOM   3304 C  CB  . LEU   A 1 455 ? -27.771 -29.579 -26.490 1.00 138.49 ? 475 LEU   A CB  1 
ATOM   3305 C  CG  . LEU   A 1 455 ? -27.958 -29.103 -25.048 1.00 132.55 ? 475 LEU   A CG  1 
ATOM   3306 C  CD1 . LEU   A 1 455 ? -27.616 -30.224 -24.085 1.00 127.69 ? 475 LEU   A CD1 1 
ATOM   3307 C  CD2 . LEU   A 1 455 ? -27.099 -27.877 -24.763 1.00 125.79 ? 475 LEU   A CD2 1 
ATOM   3308 N  N   . LYS   A 1 456 ? -30.221 -27.262 -26.965 1.00 135.61 ? 476 LYS   A N   1 
ATOM   3309 C  CA  . LYS   A 1 456 ? -30.465 -25.857 -26.680 1.00 135.63 ? 476 LYS   A CA  1 
ATOM   3310 C  C   . LYS   A 1 456 ? -29.965 -25.526 -25.282 1.00 130.88 ? 476 LYS   A C   1 
ATOM   3311 O  O   . LYS   A 1 456 ? -30.207 -26.272 -24.329 1.00 128.75 ? 476 LYS   A O   1 
ATOM   3312 C  CB  . LYS   A 1 456 ? -31.953 -25.518 -26.787 1.00 142.66 ? 476 LYS   A CB  1 
ATOM   3313 C  CG  . LYS   A 1 456 ? -32.466 -25.325 -28.202 1.00 152.75 ? 476 LYS   A CG  1 
ATOM   3314 C  CD  . LYS   A 1 456 ? -33.785 -24.570 -28.184 1.00 162.92 ? 476 LYS   A CD  1 
ATOM   3315 C  CE  . LYS   A 1 456 ? -34.953 -25.463 -28.558 1.00 169.21 ? 476 LYS   A CE  1 
ATOM   3316 N  NZ  . LYS   A 1 456 ? -35.196 -25.463 -30.026 1.00 170.06 ? 476 LYS   A NZ  1 
ATOM   3317 N  N   . LEU   A 1 457 ? -29.257 -24.409 -25.165 1.00 135.80 ? 477 LEU   A N   1 
ATOM   3318 C  CA  . LEU   A 1 457 ? -28.872 -23.918 -23.853 1.00 137.89 ? 477 LEU   A CA  1 
ATOM   3319 C  C   . LEU   A 1 457 ? -30.068 -23.264 -23.177 1.00 149.32 ? 477 LEU   A C   1 
ATOM   3320 O  O   . LEU   A 1 457 ? -30.994 -22.785 -23.836 1.00 155.47 ? 477 LEU   A O   1 
ATOM   3321 C  CB  . LEU   A 1 457 ? -27.718 -22.922 -23.961 1.00 128.13 ? 477 LEU   A CB  1 
ATOM   3322 C  CG  . LEU   A 1 457 ? -26.342 -23.541 -24.208 1.00 123.14 ? 477 LEU   A CG  1 
ATOM   3323 C  CD1 . LEU   A 1 457 ? -25.279 -22.466 -24.377 1.00 125.10 ? 477 LEU   A CD1 1 
ATOM   3324 C  CD2 . LEU   A 1 457 ? -25.982 -24.482 -23.069 1.00 126.24 ? 477 LEU   A CD2 1 
ATOM   3325 N  N   . SER   A 1 458 ? -30.053 -23.266 -21.845 1.00 159.96 ? 478 SER   A N   1 
ATOM   3326 C  CA  . SER   A 1 458 ? -31.101 -22.579 -21.104 1.00 159.36 ? 478 SER   A CA  1 
ATOM   3327 C  C   . SER   A 1 458 ? -31.070 -21.094 -21.436 1.00 169.47 ? 478 SER   A C   1 
ATOM   3328 O  O   . SER   A 1 458 ? -30.155 -20.378 -21.018 1.00 161.43 ? 478 SER   A O   1 
ATOM   3329 C  CB  . SER   A 1 458 ? -30.942 -22.796 -19.597 1.00 151.05 ? 478 SER   A CB  1 
ATOM   3330 O  OG  . SER   A 1 458 ? -31.883 -22.025 -18.871 1.00 153.02 ? 478 SER   A OG  1 
ATOM   3331 N  N   . LEU   A 1 459 ? -32.063 -20.623 -22.191 1.00 212.51 ? 479 LEU   A N   1 
ATOM   3332 C  CA  . LEU   A 1 459 ? -32.169 -19.206 -22.522 1.00 210.74 ? 479 LEU   A CA  1 
ATOM   3333 C  C   . LEU   A 1 459 ? -32.385 -18.365 -21.268 1.00 207.61 ? 479 LEU   A C   1 
ATOM   3334 O  O   . LEU   A 1 459 ? -32.416 -17.132 -21.340 1.00 209.73 ? 479 LEU   A O   1 
ATOM   3335 C  CB  . LEU   A 1 459 ? -33.303 -18.965 -23.523 1.00 213.89 ? 479 LEU   A CB  1 
ATOM   3336 C  CG  . LEU   A 1 459 ? -33.009 -19.112 -25.020 1.00 214.65 ? 479 LEU   A CG  1 
ATOM   3337 C  CD1 . LEU   A 1 459 ? -32.595 -20.528 -25.378 1.00 209.70 ? 479 LEU   A CD1 1 
ATOM   3338 C  CD2 . LEU   A 1 459 ? -34.220 -18.692 -25.834 1.00 224.82 ? 479 LEU   A CD2 1 
ATOM   3339 N  N   . GLY   A 1 460 ? -32.536 -19.021 -20.117 1.00 177.02 ? 480 GLY   A N   1 
ATOM   3340 C  CA  . GLY   A 1 460 ? -32.690 -18.344 -18.843 1.00 159.08 ? 480 GLY   A CA  1 
ATOM   3341 C  C   . GLY   A 1 460 ? -31.388 -17.851 -18.240 1.00 168.93 ? 480 GLY   A C   1 
ATOM   3342 O  O   . GLY   A 1 460 ? -30.547 -17.287 -18.946 1.00 168.00 ? 480 GLY   A O   1 
ATOM   3343 N  N   . GLY   A 1 461 ? -31.201 -18.069 -16.939 1.00 163.25 ? 481 GLY   A N   1 
ATOM   3344 C  CA  . GLY   A 1 461 ? -30.104 -17.451 -16.217 1.00 153.99 ? 481 GLY   A CA  1 
ATOM   3345 C  C   . GLY   A 1 461 ? -28.791 -18.210 -16.185 1.00 160.24 ? 481 GLY   A C   1 
ATOM   3346 O  O   . GLY   A 1 461 ? -27.759 -17.690 -16.621 1.00 160.07 ? 481 GLY   A O   1 
ATOM   3347 N  N   . LEU   A 1 462 ? -28.810 -19.429 -15.657 1.00 183.44 ? 482 LEU   A N   1 
ATOM   3348 C  CA  . LEU   A 1 462 ? -27.607 -20.224 -15.462 1.00 178.23 ? 482 LEU   A CA  1 
ATOM   3349 C  C   . LEU   A 1 462 ? -27.389 -21.171 -16.637 1.00 186.16 ? 482 LEU   A C   1 
ATOM   3350 O  O   . LEU   A 1 462 ? -28.329 -21.557 -17.337 1.00 189.63 ? 482 LEU   A O   1 
ATOM   3351 C  CB  . LEU   A 1 462 ? -27.683 -21.016 -14.151 1.00 181.54 ? 482 LEU   A CB  1 
ATOM   3352 C  CG  . LEU   A 1 462 ? -28.929 -21.851 -13.834 1.00 183.59 ? 482 LEU   A CG  1 
ATOM   3353 C  CD1 . LEU   A 1 462 ? -28.563 -22.991 -12.903 1.00 186.15 ? 482 LEU   A CD1 1 
ATOM   3354 C  CD2 . LEU   A 1 462 ? -30.026 -21.001 -13.204 1.00 179.93 ? 482 LEU   A CD2 1 
ATOM   3355 N  N   . LEU   A 1 463 ? -26.128 -21.545 -16.846 1.00 148.86 ? 483 LEU   A N   1 
ATOM   3356 C  CA  . LEU   A 1 463 ? -25.753 -22.366 -17.996 1.00 142.45 ? 483 LEU   A CA  1 
ATOM   3357 C  C   . LEU   A 1 463 ? -26.176 -23.806 -17.741 1.00 142.05 ? 483 LEU   A C   1 
ATOM   3358 O  O   . LEU   A 1 463 ? -25.474 -24.571 -17.075 1.00 138.36 ? 483 LEU   A O   1 
ATOM   3359 C  CB  . LEU   A 1 463 ? -24.258 -22.275 -18.274 1.00 126.66 ? 483 LEU   A CB  1 
ATOM   3360 C  CG  . LEU   A 1 463 ? -23.915 -22.823 -19.660 1.00 124.50 ? 483 LEU   A CG  1 
ATOM   3361 C  CD1 . LEU   A 1 463 ? -24.560 -21.955 -20.727 1.00 113.93 ? 483 LEU   A CD1 1 
ATOM   3362 C  CD2 . LEU   A 1 463 ? -22.419 -22.908 -19.871 1.00 120.17 ? 483 LEU   A CD2 1 
ATOM   3363 N  N   . GLN   A 1 464 ? -27.332 -24.172 -18.277 1.00 138.17 ? 484 GLN   A N   1 
ATOM   3364 C  CA  . GLN   A 1 464 ? -27.865 -25.525 -18.228 1.00 133.19 ? 484 GLN   A CA  1 
ATOM   3365 C  C   . GLN   A 1 464 ? -28.567 -25.802 -19.551 1.00 136.38 ? 484 GLN   A C   1 
ATOM   3366 O  O   . GLN   A 1 464 ? -28.773 -24.873 -20.341 1.00 141.80 ? 484 GLN   A O   1 
ATOM   3367 C  CB  . GLN   A 1 464 ? -28.829 -25.687 -17.050 1.00 133.52 ? 484 GLN   A CB  1 
ATOM   3368 C  CG  . GLN   A 1 464 ? -28.152 -25.890 -15.706 1.00 142.67 ? 484 GLN   A CG  1 
ATOM   3369 C  CD  . GLN   A 1 464 ? -29.146 -25.934 -14.564 1.00 144.36 ? 484 GLN   A CD  1 
ATOM   3370 O  OE1 . GLN   A 1 464 ? -30.289 -25.502 -14.707 1.00 144.13 ? 484 GLN   A OE1 1 
ATOM   3371 N  NE2 . GLN   A 1 464 ? -28.715 -26.457 -13.421 1.00 137.17 ? 484 GLN   A NE2 1 
ATOM   3372 N  N   . PRO   A 1 465 ? -28.918 -27.047 -19.852 1.00 134.42 ? 485 PRO   A N   1 
ATOM   3373 C  CA  . PRO   A 1 465 ? -29.749 -27.305 -21.031 1.00 145.79 ? 485 PRO   A CA  1 
ATOM   3374 C  C   . PRO   A 1 465 ? -31.207 -26.963 -20.770 1.00 148.81 ? 485 PRO   A C   1 
ATOM   3375 O  O   . PRO   A 1 465 ? -31.681 -26.976 -19.632 1.00 129.59 ? 485 PRO   A O   1 
ATOM   3376 C  CB  . PRO   A 1 465 ? -29.573 -28.811 -21.270 1.00 141.57 ? 485 PRO   A CB  1 
ATOM   3377 C  CG  . PRO   A 1 465 ? -28.367 -29.204 -20.473 1.00 133.84 ? 485 PRO   A CG  1 
ATOM   3378 C  CD  . PRO   A 1 465 ? -28.348 -28.286 -19.299 1.00 130.27 ? 485 PRO   A CD  1 
ATOM   3379 N  N   . GLU   A 1 466 ? -31.918 -26.642 -21.853 1.00 154.70 ? 486 GLU   A N   1 
ATOM   3380 C  CA  . GLU   A 1 466 ? -33.359 -26.432 -21.769 1.00 155.79 ? 486 GLU   A CA  1 
ATOM   3381 C  C   . GLU   A 1 466 ? -34.031 -27.697 -21.255 1.00 157.20 ? 486 GLU   A C   1 
ATOM   3382 O  O   . GLU   A 1 466 ? -34.597 -27.708 -20.157 1.00 159.14 ? 486 GLU   A O   1 
ATOM   3383 C  CB  . GLU   A 1 466 ? -33.942 -26.042 -23.128 1.00 160.73 ? 486 GLU   A CB  1 
ATOM   3384 C  CG  . GLU   A 1 466 ? -33.894 -24.558 -23.442 1.00 163.95 ? 486 GLU   A CG  1 
ATOM   3385 C  CD  . GLU   A 1 466 ? -34.689 -24.210 -24.686 1.00 170.33 ? 486 GLU   A CD  1 
ATOM   3386 O  OE1 . GLU   A 1 466 ? -35.355 -25.112 -25.237 1.00 173.30 ? 486 GLU   A OE1 1 
ATOM   3387 O  OE2 . GLU   A 1 466 ? -34.651 -23.038 -25.115 1.00 182.83 ? 486 GLU   A OE2 1 
ATOM   3388 N  N   . LYS   A 1 467 ? -33.972 -28.773 -22.052 1.00 155.39 ? 487 LYS   A N   1 
ATOM   3389 C  CA  . LYS   A 1 467 ? -34.444 -30.085 -21.645 1.00 151.46 ? 487 LYS   A CA  1 
ATOM   3390 C  C   . LYS   A 1 467 ? -33.309 -30.871 -20.999 1.00 149.26 ? 487 LYS   A C   1 
ATOM   3391 O  O   . LYS   A 1 467 ? -32.145 -30.715 -21.381 1.00 131.23 ? 487 LYS   A O   1 
ATOM   3392 C  CB  . LYS   A 1 467 ? -34.978 -30.860 -22.847 1.00 143.14 ? 487 LYS   A CB  1 
ATOM   3393 C  CG  . LYS   A 1 467 ? -36.128 -30.182 -23.568 1.00 144.99 ? 487 LYS   A CG  1 
ATOM   3394 C  CD  . LYS   A 1 467 ? -36.448 -30.888 -24.878 1.00 146.35 ? 487 LYS   A CD  1 
ATOM   3395 C  CE  . LYS   A 1 467 ? -37.278 -32.146 -24.665 1.00 134.07 ? 487 LYS   A CE  1 
ATOM   3396 N  NZ  . LYS   A 1 467 ? -38.721 -31.844 -24.437 1.00 157.46 ? 487 LYS   A NZ  1 
ATOM   3397 N  N   . PRO   A 1 468 ? -33.618 -31.707 -20.010 1.00 150.06 ? 488 PRO   A N   1 
ATOM   3398 C  CA  . PRO   A 1 468 ? -32.577 -32.538 -19.398 1.00 143.90 ? 488 PRO   A CA  1 
ATOM   3399 C  C   . PRO   A 1 468 ? -31.948 -33.475 -20.417 1.00 145.76 ? 488 PRO   A C   1 
ATOM   3400 O  O   . PRO   A 1 468 ? -32.531 -33.796 -21.455 1.00 144.25 ? 488 PRO   A O   1 
ATOM   3401 C  CB  . PRO   A 1 468 ? -33.331 -33.314 -18.311 1.00 141.29 ? 488 PRO   A CB  1 
ATOM   3402 C  CG  . PRO   A 1 468 ? -34.521 -32.467 -18.002 1.00 139.72 ? 488 PRO   A CG  1 
ATOM   3403 C  CD  . PRO   A 1 468 ? -34.904 -31.814 -19.300 1.00 147.28 ? 488 PRO   A CD  1 
ATOM   3404 N  N   . VAL   A 1 469 ? -30.730 -33.908 -20.111 1.00 144.42 ? 489 VAL   A N   1 
ATOM   3405 C  CA  . VAL   A 1 469 ? -29.956 -34.756 -21.010 1.00 150.85 ? 489 VAL   A CA  1 
ATOM   3406 C  C   . VAL   A 1 469 ? -30.347 -36.206 -20.751 1.00 148.57 ? 489 VAL   A C   1 
ATOM   3407 O  O   . VAL   A 1 469 ? -30.056 -36.756 -19.686 1.00 150.44 ? 489 VAL   A O   1 
ATOM   3408 C  CB  . VAL   A 1 469 ? -28.450 -34.545 -20.826 1.00 142.47 ? 489 VAL   A CB  1 
ATOM   3409 C  CG1 . VAL   A 1 469 ? -27.682 -35.440 -21.778 1.00 139.07 ? 489 VAL   A CG1 1 
ATOM   3410 C  CG2 . VAL   A 1 469 ? -28.087 -33.084 -21.047 1.00 122.59 ? 489 VAL   A CG2 1 
ATOM   3411 N  N   . VAL   A 1 470 ? -31.007 -36.825 -21.727 1.00 147.35 ? 490 VAL   A N   1 
ATOM   3412 C  CA  . VAL   A 1 470 ? -31.417 -38.221 -21.651 1.00 160.58 ? 490 VAL   A CA  1 
ATOM   3413 C  C   . VAL   A 1 470 ? -30.756 -38.978 -22.794 1.00 166.73 ? 490 VAL   A C   1 
ATOM   3414 O  O   . VAL   A 1 470 ? -30.855 -38.570 -23.958 1.00 157.23 ? 490 VAL   A O   1 
ATOM   3415 C  CB  . VAL   A 1 470 ? -32.950 -38.370 -21.699 1.00 167.65 ? 490 VAL   A CB  1 
ATOM   3416 C  CG1 . VAL   A 1 470 ? -33.558 -37.968 -20.367 1.00 159.79 ? 490 VAL   A CG1 1 
ATOM   3417 C  CG2 . VAL   A 1 470 ? -33.537 -37.526 -22.820 1.00 171.48 ? 490 VAL   A CG2 1 
ATOM   3418 N  N   . LEU   A 1 471 ? -30.075 -40.072 -22.460 1.00 174.51 ? 491 LEU   A N   1 
ATOM   3419 C  CA  . LEU   A 1 471 ? -29.361 -40.877 -23.440 1.00 178.37 ? 491 LEU   A CA  1 
ATOM   3420 C  C   . LEU   A 1 471 ? -29.577 -42.352 -23.140 1.00 177.64 ? 491 LEU   A C   1 
ATOM   3421 O  O   . LEU   A 1 471 ? -29.822 -42.738 -21.994 1.00 179.89 ? 491 LEU   A O   1 
ATOM   3422 C  CB  . LEU   A 1 471 ? -27.857 -40.567 -23.440 1.00 165.78 ? 491 LEU   A CB  1 
ATOM   3423 C  CG  . LEU   A 1 471 ? -27.411 -39.143 -23.774 1.00 157.96 ? 491 LEU   A CG  1 
ATOM   3424 C  CD1 . LEU   A 1 471 ? -25.924 -38.993 -23.510 1.00 154.49 ? 491 LEU   A CD1 1 
ATOM   3425 C  CD2 . LEU   A 1 471 ? -27.732 -38.810 -25.220 1.00 159.68 ? 491 LEU   A CD2 1 
ATOM   3426 N  N   . LYS   A 1 472 ? -29.483 -43.174 -24.182 1.00 181.15 ? 492 LYS   A N   1 
ATOM   3427 C  CA  . LYS   A 1 472 ? -29.562 -44.617 -24.008 1.00 171.96 ? 492 LYS   A CA  1 
ATOM   3428 C  C   . LYS   A 1 472 ? -28.223 -45.150 -23.517 1.00 169.21 ? 492 LYS   A C   1 
ATOM   3429 O  O   . LYS   A 1 472 ? -27.160 -44.677 -23.928 1.00 161.42 ? 492 LYS   A O   1 
ATOM   3430 C  CB  . LYS   A 1 472 ? -29.954 -45.303 -25.317 1.00 163.26 ? 492 LYS   A CB  1 
ATOM   3431 C  CG  . LYS   A 1 472 ? -30.866 -46.510 -25.130 1.00 161.61 ? 492 LYS   A CG  1 
ATOM   3432 C  CD  . LYS   A 1 472 ? -31.164 -47.203 -26.450 1.00 156.13 ? 492 LYS   A CD  1 
ATOM   3433 C  CE  . LYS   A 1 472 ? -29.920 -47.864 -27.021 1.00 158.93 ? 492 LYS   A CE  1 
ATOM   3434 N  NZ  . LYS   A 1 472 ? -30.219 -48.631 -28.262 1.00 169.47 ? 492 LYS   A NZ  1 
ATOM   3435 N  N   . VAL   A 1 473 ? -28.279 -46.137 -22.629 1.00 174.67 ? 493 VAL   A N   1 
ATOM   3436 C  CA  . VAL   A 1 473 ? -27.092 -46.704 -22.000 1.00 172.48 ? 493 VAL   A CA  1 
ATOM   3437 C  C   . VAL   A 1 473 ? -27.053 -48.194 -22.305 1.00 177.01 ? 493 VAL   A C   1 
ATOM   3438 O  O   . VAL   A 1 473 ? -28.013 -48.918 -22.012 1.00 188.27 ? 493 VAL   A O   1 
ATOM   3439 C  CB  . VAL   A 1 473 ? -27.075 -46.451 -20.484 1.00 169.78 ? 493 VAL   A CB  1 
ATOM   3440 C  CG1 . VAL   A 1 473 ? -25.781 -46.961 -19.877 1.00 167.85 ? 493 VAL   A CG1 1 
ATOM   3441 C  CG2 . VAL   A 1 473 ? -27.263 -44.969 -20.190 1.00 167.72 ? 493 VAL   A CG2 1 
ATOM   3442 N  N   . GLU   A 1 474 ? -25.949 -48.647 -22.890 1.00 173.70 ? 494 GLU   A N   1 
ATOM   3443 C  CA  . GLU   A 1 474 ? -25.731 -50.051 -23.197 1.00 185.04 ? 494 GLU   A CA  1 
ATOM   3444 C  C   . GLU   A 1 474 ? -24.524 -50.556 -22.416 1.00 182.87 ? 494 GLU   A C   1 
ATOM   3445 O  O   . GLU   A 1 474 ? -23.642 -49.784 -22.033 1.00 173.19 ? 494 GLU   A O   1 
ATOM   3446 C  CB  . GLU   A 1 474 ? -25.529 -50.262 -24.703 1.00 183.10 ? 494 GLU   A CB  1 
ATOM   3447 C  CG  . GLU   A 1 474 ? -26.740 -49.873 -25.537 1.00 184.60 ? 494 GLU   A CG  1 
ATOM   3448 C  CD  . GLU   A 1 474 ? -26.456 -49.884 -27.025 1.00 190.84 ? 494 GLU   A CD  1 
ATOM   3449 O  OE1 . GLU   A 1 474 ? -25.292 -49.641 -27.409 1.00 188.30 ? 494 GLU   A OE1 1 
ATOM   3450 O  OE2 . GLU   A 1 474 ? -27.394 -50.139 -27.809 1.00 191.28 ? 494 GLU   A OE2 1 
ATOM   3451 N  N   . SER   A 1 475 ? -24.493 -51.865 -22.178 1.00 183.16 ? 495 SER   A N   1 
ATOM   3452 C  CA  . SER   A 1 475 ? -23.484 -52.489 -21.331 1.00 184.24 ? 495 SER   A CA  1 
ATOM   3453 C  C   . SER   A 1 475 ? -22.464 -53.228 -22.186 1.00 185.35 ? 495 SER   A C   1 
ATOM   3454 O  O   . SER   A 1 475 ? -22.835 -54.021 -23.058 1.00 194.73 ? 495 SER   A O   1 
ATOM   3455 C  CB  . SER   A 1 475 ? -24.131 -53.450 -20.330 1.00 189.07 ? 495 SER   A CB  1 
ATOM   3456 O  OG  . SER   A 1 475 ? -23.187 -53.903 -19.374 1.00 188.67 ? 495 SER   A OG  1 
ATOM   3457 N  N   . ARG   A 1 476 ? -21.184 -52.975 -21.926 1.00 182.25 ? 496 ARG   A N   1 
ATOM   3458 C  CA  . ARG   A 1 476 ? -20.101 -53.614 -22.667 1.00 184.66 ? 496 ARG   A CA  1 
ATOM   3459 C  C   . ARG   A 1 476 ? -19.804 -55.008 -22.122 1.00 176.08 ? 496 ARG   A C   1 
ATOM   3460 O  O   . ARG   A 1 476 ? -20.454 -55.984 -22.496 1.00 173.20 ? 496 ARG   A O   1 
ATOM   3461 C  CB  . ARG   A 1 476 ? -18.835 -52.756 -22.615 1.00 176.98 ? 496 ARG   A CB  1 
ATOM   3462 C  CG  . ARG   A 1 476 ? -19.071 -51.282 -22.902 1.00 175.30 ? 496 ARG   A CG  1 
ATOM   3463 C  CD  . ARG   A 1 476 ? -17.794 -50.478 -22.723 1.00 169.60 ? 496 ARG   A CD  1 
ATOM   3464 N  NE  . ARG   A 1 476 ? -16.870 -50.662 -23.836 1.00 166.62 ? 496 ARG   A NE  1 
ATOM   3465 C  CZ  . ARG   A 1 476 ? -15.595 -50.301 -23.817 1.00 163.10 ? 496 ARG   A CZ  1 
ATOM   3466 N  NH1 . ARG   A 1 476 ? -15.048 -49.749 -22.746 1.00 156.23 ? 496 ARG   A NH1 1 
ATOM   3467 N  NH2 . ARG   A 1 476 ? -14.847 -50.505 -24.898 1.00 160.43 ? 496 ARG   A NH2 1 
HETATM 3468 C  CHA . HEM   B 2 .   ? -14.890 -19.897 -8.494  1.00 98.46  ? 601 HEM   A CHA 1 
HETATM 3469 C  CHB . HEM   B 2 .   ? -15.398 -22.692 -12.442 1.00 100.55 ? 601 HEM   A CHB 1 
HETATM 3470 C  CHC . HEM   B 2 .   ? -16.045 -26.558 -9.580  1.00 104.69 ? 601 HEM   A CHC 1 
HETATM 3471 C  CHD . HEM   B 2 .   ? -15.299 -23.817 -5.642  1.00 109.26 ? 601 HEM   A CHD 1 
HETATM 3472 C  C1A . HEM   B 2 .   ? -14.976 -20.301 -9.812  1.00 95.47  ? 601 HEM   A C1A 1 
HETATM 3473 C  C2A . HEM   B 2 .   ? -14.853 -19.456 -10.983 1.00 100.06 ? 601 HEM   A C2A 1 
HETATM 3474 C  C3A . HEM   B 2 .   ? -14.993 -20.228 -12.069 1.00 91.45  ? 601 HEM   A C3A 1 
HETATM 3475 C  C4A . HEM   B 2 .   ? -15.208 -21.591 -11.632 1.00 97.67  ? 601 HEM   A C4A 1 
HETATM 3476 C  CMA . HEM   B 2 .   ? -14.937 -19.767 -13.540 1.00 85.01  ? 601 HEM   A CMA 1 
HETATM 3477 C  CAA . HEM   B 2 .   ? -14.603 -17.931 -10.968 1.00 90.11  ? 601 HEM   A CAA 1 
HETATM 3478 C  CBA . HEM   B 2 .   ? -13.111 -17.657 -11.144 1.00 71.57  ? 601 HEM   A CBA 1 
HETATM 3479 C  CGA . HEM   B 2 .   ? -12.875 -16.189 -11.398 1.00 89.90  ? 601 HEM   A CGA 1 
HETATM 3480 O  O1A . HEM   B 2 .   ? -11.745 -15.815 -11.809 1.00 100.93 ? 601 HEM   A O1A 1 
HETATM 3481 O  O2A . HEM   B 2 .   ? -13.821 -15.387 -11.193 1.00 79.42  ? 601 HEM   A O2A 1 
HETATM 3482 C  C1B . HEM   B 2 .   ? -15.633 -23.982 -12.013 1.00 103.80 ? 601 HEM   A C1B 1 
HETATM 3483 C  C2B . HEM   B 2 .   ? -15.893 -25.129 -12.864 1.00 104.98 ? 601 HEM   A C2B 1 
HETATM 3484 C  C3B . HEM   B 2 .   ? -16.078 -26.197 -12.066 1.00 98.44  ? 601 HEM   A C3B 1 
HETATM 3485 C  C4B . HEM   B 2 .   ? -15.931 -25.753 -10.694 1.00 97.10  ? 601 HEM   A C4B 1 
HETATM 3486 C  CMB . HEM   B 2 .   ? -15.943 -25.051 -14.410 1.00 107.70 ? 601 HEM   A CMB 1 
HETATM 3487 C  CAB . HEM   B 2 .   ? -16.376 -27.674 -12.435 1.00 110.05 ? 601 HEM   A CAB 1 
HETATM 3488 C  CBB . HEM   B 2 .   ? -16.368 -28.148 -13.685 1.00 106.12 ? 601 HEM   A CBB 1 
HETATM 3489 C  C1C . HEM   B 2 .   ? -15.831 -26.178 -8.273  1.00 112.34 ? 601 HEM   A C1C 1 
HETATM 3490 C  C2C . HEM   B 2 .   ? -15.724 -27.066 -7.134  1.00 113.18 ? 601 HEM   A C2C 1 
HETATM 3491 C  C3C . HEM   B 2 .   ? -15.511 -26.327 -6.042  1.00 107.55 ? 601 HEM   A C3C 1 
HETATM 3492 C  C4C . HEM   B 2 .   ? -15.485 -24.925 -6.449  1.00 107.09 ? 601 HEM   A C4C 1 
HETATM 3493 C  CMC . HEM   B 2 .   ? -15.829 -28.606 -7.182  1.00 116.46 ? 601 HEM   A CMC 1 
HETATM 3494 C  CAC . HEM   B 2 .   ? -15.348 -26.929 -4.622  1.00 109.27 ? 601 HEM   A CAC 1 
HETATM 3495 C  CBC . HEM   B 2 .   ? -15.021 -26.199 -3.550  1.00 122.38 ? 601 HEM   A CBC 1 
HETATM 3496 C  C1D . HEM   B 2 .   ? -15.170 -22.505 -6.052  1.00 104.41 ? 601 HEM   A C1D 1 
HETATM 3497 C  C2D . HEM   B 2 .   ? -15.074 -21.334 -5.203  1.00 103.55 ? 601 HEM   A C2D 1 
HETATM 3498 C  C3D . HEM   B 2 .   ? -14.969 -20.260 -5.999  1.00 103.71 ? 601 HEM   A C3D 1 
HETATM 3499 C  C4D . HEM   B 2 .   ? -14.982 -20.703 -7.376  1.00 94.79  ? 601 HEM   A C4D 1 
HETATM 3500 C  CMD . HEM   B 2 .   ? -15.104 -21.343 -3.658  1.00 102.98 ? 601 HEM   A CMD 1 
HETATM 3501 C  CAD . HEM   B 2 .   ? -14.824 -18.789 -5.569  1.00 90.89  ? 601 HEM   A CAD 1 
HETATM 3502 C  CBD . HEM   B 2 .   ? -13.335 -18.575 -5.332  1.00 93.90  ? 601 HEM   A CBD 1 
HETATM 3503 C  CGD . HEM   B 2 .   ? -13.069 -17.215 -4.750  1.00 100.58 ? 601 HEM   A CGD 1 
HETATM 3504 O  O1D . HEM   B 2 .   ? -11.959 -17.036 -4.188  1.00 92.14  ? 601 HEM   A O1D 1 
HETATM 3505 O  O2D . HEM   B 2 .   ? -13.953 -16.323 -4.842  1.00 85.39  ? 601 HEM   A O2D 1 
HETATM 3506 N  NA  . HEM   B 2 .   ? -15.190 -21.594 -10.250 1.00 100.19 ? 601 HEM   A NA  1 
HETATM 3507 N  NB  . HEM   B 2 .   ? -15.663 -24.397 -10.695 1.00 100.64 ? 601 HEM   A NB  1 
HETATM 3508 N  NC  . HEM   B 2 .   ? -15.681 -24.881 -7.819  1.00 104.98 ? 601 HEM   A NC  1 
HETATM 3509 N  ND  . HEM   B 2 .   ? -15.109 -22.077 -7.365  1.00 101.02 ? 601 HEM   A ND  1 
HETATM 3510 FE FE  . HEM   B 2 .   ? -15.316 -23.224 -9.026  1.00 108.23 ? 601 HEM   A FE  1 
HETATM 3511 C  C11 . A1A4S C 3 .   ? -23.253 -16.670 -8.749  1.00 130.84 ? 602 A1A4S A C11 1 
HETATM 3512 C  C13 . A1A4S C 3 .   ? -23.358 -17.743 -4.036  1.00 126.13 ? 602 A1A4S A C13 1 
HETATM 3513 C  C14 . A1A4S C 3 .   ? -24.011 -19.127 -4.228  1.00 121.16 ? 602 A1A4S A C14 1 
HETATM 3514 C  C15 . A1A4S C 3 .   ? -25.572 -20.569 -5.396  1.00 128.32 ? 602 A1A4S A C15 1 
HETATM 3515 C  C16 . A1A4S C 3 .   ? -25.198 -21.641 -4.577  1.00 120.53 ? 602 A1A4S A C16 1 
HETATM 3516 C  C17 . A1A4S C 3 .   ? -24.230 -21.457 -3.583  1.00 119.54 ? 602 A1A4S A C17 1 
HETATM 3517 C  C18 . A1A4S C 3 .   ? -23.640 -20.200 -3.409  1.00 123.23 ? 602 A1A4S A C18 1 
HETATM 3518 C  C19 . A1A4S C 3 .   ? -24.979 -19.313 -5.222  1.00 125.76 ? 602 A1A4S A C19 1 
HETATM 3519 C  C20 . A1A4S C 3 .   ? -20.688 -14.485 -8.858  1.00 114.66 ? 602 A1A4S A C20 1 
HETATM 3520 C  C23 . A1A4S C 3 .   ? -24.263 -15.599 -9.254  1.00 144.01 ? 602 A1A4S A C23 1 
HETATM 3521 C  C01 . A1A4S C 3 .   ? -20.270 -22.590 -6.446  1.00 111.78 ? 602 A1A4S A C01 1 
HETATM 3522 C  C02 . A1A4S C 3 .   ? -20.044 -21.368 -5.535  1.00 112.37 ? 602 A1A4S A C02 1 
HETATM 3523 C  C03 . A1A4S C 3 .   ? -19.731 -20.074 -6.308  1.00 107.94 ? 602 A1A4S A C03 1 
HETATM 3524 C  C05 . A1A4S C 3 .   ? -21.235 -18.335 -5.196  1.00 122.28 ? 602 A1A4S A C05 1 
HETATM 3525 C  C06 . A1A4S C 3 .   ? -22.428 -17.355 -5.202  1.00 126.64 ? 602 A1A4S A C06 1 
HETATM 3526 C  C08 . A1A4S C 3 .   ? -21.622 -14.624 -6.496  1.00 133.75 ? 602 A1A4S A C08 1 
HETATM 3527 C  C09 . A1A4S C 3 .   ? -21.043 -15.423 -7.688  1.00 124.69 ? 602 A1A4S A C09 1 
HETATM 3528 C  C21 . A1A4S C 3 .   ? -19.947 -15.140 -10.040 1.00 116.50 ? 602 A1A4S A C21 1 
HETATM 3529 C  C24 . A1A4S C 3 .   ? -19.422 -22.585 -7.730  1.00 95.39  ? 602 A1A4S A C24 1 
HETATM 3530 C  C25 . A1A4S C 3 .   ? -20.034 -22.336 -8.965  1.00 89.91  ? 602 A1A4S A C25 1 
HETATM 3531 C  C26 . A1A4S C 3 .   ? -19.229 -22.340 -10.110 1.00 104.15 ? 602 A1A4S A C26 1 
HETATM 3532 C  C27 . A1A4S C 3 .   ? -17.859 -22.592 -9.987  1.00 109.88 ? 602 A1A4S A C27 1 
HETATM 3533 C  C29 . A1A4S C 3 .   ? -18.049 -22.834 -7.663  1.00 105.92 ? 602 A1A4S A C29 1 
HETATM 3534 C  C30 . A1A4S C 3 .   ? -23.992 -14.231 -9.399  1.00 142.33 ? 602 A1A4S A C30 1 
HETATM 3535 C  C32 . A1A4S C 3 .   ? -26.161 -13.824 -10.212 1.00 141.48 ? 602 A1A4S A C32 1 
HETATM 3536 C  C33 . A1A4S C 3 .   ? -26.509 -15.175 -10.104 1.00 145.16 ? 602 A1A4S A C33 1 
HETATM 3537 C  C34 . A1A4S C 3 .   ? -25.541 -16.065 -9.623  1.00 146.68 ? 602 A1A4S A C34 1 
HETATM 3538 C  C35 . A1A4S C 3 .   ? -19.281 -16.380 -10.102 1.00 109.46 ? 602 A1A4S A C35 1 
HETATM 3539 C  C36 . A1A4S C 3 .   ? -18.779 -16.498 -11.399 1.00 113.51 ? 602 A1A4S A C36 1 
HETATM 3540 C  C38 . A1A4S C 3 .   ? -19.816 -14.558 -11.305 1.00 106.94 ? 602 A1A4S A C38 1 
HETATM 3541 C  C39 . A1A4S C 3 .   ? -19.052 -17.419 -9.185  1.00 106.98 ? 602 A1A4S A C39 1 
HETATM 3542 C  C40 . A1A4S C 3 .   ? -18.342 -18.566 -9.535  1.00 108.14 ? 602 A1A4S A C40 1 
HETATM 3543 C  C41 . A1A4S C 3 .   ? -17.849 -18.678 -10.834 1.00 113.42 ? 602 A1A4S A C41 1 
HETATM 3544 C  C42 . A1A4S C 3 .   ? -18.062 -17.646 -11.755 1.00 119.02 ? 602 A1A4S A C42 1 
HETATM 3545 N  N04 . A1A4S C 3 .   ? -20.886 -19.159 -6.367  1.00 119.08 ? 602 A1A4S A N04 1 
HETATM 3546 N  N10 . A1A4S C 3 .   ? -21.907 -16.554 -8.112  1.00 129.21 ? 602 A1A4S A N10 1 
HETATM 3547 N  N28 . A1A4S C 3 .   ? -17.321 -22.827 -8.784  1.00 102.92 ? 602 A1A4S A N28 1 
HETATM 3548 N  N31 . A1A4S C 3 .   ? -24.936 -13.398 -9.863  1.00 140.73 ? 602 A1A4S A N31 1 
HETATM 3549 N  N37 . A1A4S C 3 .   ? -19.119 -15.393 -12.080 1.00 115.99 ? 602 A1A4S A N37 1 
HETATM 3550 O  O12 . A1A4S C 3 .   ? -20.575 -18.442 -4.204  1.00 119.98 ? 602 A1A4S A O12 1 
HETATM 3551 O  O22 . A1A4S C 3 .   ? -23.635 -17.790 -8.931  1.00 128.09 ? 602 A1A4S A O22 1 
HETATM 3552 S  S07 . A1A4S C 3 .   ? -21.859 -15.631 -4.980  1.00 144.91 ? 602 A1A4S A S07 1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N  N   . HIS   A 8   ? 2.2720 2.3353 2.4204 0.3052  0.0605  0.1238  28  HIS   A N   
2    C  CA  . HIS   A 8   ? 2.3858 2.3738 2.5370 0.2998  0.0774  0.1329  28  HIS   A CA  
3    C  C   . HIS   A 8   ? 2.2722 2.2417 2.4231 0.2660  0.0861  0.1348  28  HIS   A C   
4    O  O   . HIS   A 8   ? 2.4376 2.3608 2.5833 0.2647  0.1023  0.1583  28  HIS   A O   
5    C  CB  . HIS   A 8   ? 2.4982 2.4549 2.6700 0.2974  0.0803  0.1067  28  HIS   A CB  
6    C  CG  . HIS   A 8   ? 2.4322 2.4130 2.6128 0.2689  0.0733  0.0742  28  HIS   A CG  
7    N  ND1 . HIS   A 8   ? 2.5158 2.4545 2.7061 0.2442  0.0760  0.0551  28  HIS   A ND1 
8    C  CD2 . HIS   A 8   ? 2.3458 2.3855 2.5259 0.2622  0.0634  0.0578  28  HIS   A CD2 
9    C  CE1 . HIS   A 8   ? 2.4325 2.4014 2.6212 0.2267  0.0669  0.0301  28  HIS   A CE1 
10   N  NE2 . HIS   A 8   ? 2.4811 2.5089 2.6634 0.2361  0.0616  0.0324  28  HIS   A NE2 
11   N  N   . SER   A 9   ? 2.1728 2.1775 2.3315 0.2393  0.0774  0.1107  29  SER   A N   
12   C  CA  . SER   A 9   ? 2.0536 2.0511 2.2178 0.2085  0.0832  0.1083  29  SER   A CA  
13   C  C   . SER   A 9   ? 1.8606 1.8939 2.0005 0.2088  0.0830  0.1261  29  SER   A C   
14   O  O   . SER   A 9   ? 1.6747 1.7186 1.8186 0.1846  0.0855  0.1194  29  SER   A O   
15   C  CB  . SER   A 9   ? 1.9397 1.9531 2.1195 0.1833  0.0724  0.0743  29  SER   A CB  
16   O  OG  . SER   A 9   ? 1.8832 1.9519 2.0527 0.1869  0.0591  0.0621  29  SER   A OG  
17   N  N   . HIS   A 10  ? 1.7301 1.7813 1.8437 0.2379  0.0790  0.1473  30  HIS   A N   
18   C  CA  . HIS   A 10  ? 1.6777 1.7618 1.7593 0.2427  0.0754  0.1617  30  HIS   A CA  
19   C  C   . HIS   A 10  ? 1.7730 1.8133 1.8299 0.2475  0.0981  0.1946  30  HIS   A C   
20   O  O   . HIS   A 10  ? 1.7579 1.8167 1.7753 0.2607  0.0967  0.2116  30  HIS   A O   
21   C  CB  . HIS   A 10  ? 1.6495 1.7800 1.7134 0.2734  0.0546  0.1652  30  HIS   A CB  
22   C  CG  . HIS   A 10  ? 1.6749 1.8664 1.7576 0.2619  0.0349  0.1349  30  HIS   A CG  
23   N  ND1 . HIS   A 10  ? 1.6718 1.9196 1.7486 0.2800  0.0137  0.1312  30  HIS   A ND1 
24   C  CD2 . HIS   A 10  ? 1.5840 1.7867 1.6920 0.2341  0.0339  0.1073  30  HIS   A CD2 
25   C  CE1 . HIS   A 10  ? 1.6014 1.8916 1.7040 0.2609  0.0040  0.1032  30  HIS   A CE1 
26   N  NE2 . HIS   A 10  ? 1.5523 1.8135 1.6691 0.2343  0.0168  0.0900  30  HIS   A NE2 
27   N  N   . GLY   A 11  ? 1.6694 1.6512 1.7480 0.2367  0.1199  0.2031  31  GLY   A N   
28   C  CA  . GLY   A 11  ? 1.8170 1.7536 1.8795 0.2365  0.1485  0.2352  31  GLY   A CA  
29   C  C   . GLY   A 11  ? 1.6952 1.6169 1.7923 0.1996  0.1672  0.2259  31  GLY   A C   
30   O  O   . GLY   A 11  ? 1.7902 1.6700 1.8872 0.1947  0.1974  0.2515  31  GLY   A O   
31   N  N   . LEU   A 12  ? 1.5851 1.5397 1.7136 0.1744  0.1514  0.1908  32  LEU   A N   
32   C  CA  . LEU   A 12  ? 1.5506 1.4949 1.7210 0.1412  0.1642  0.1780  32  LEU   A CA  
33   C  C   . LEU   A 12  ? 1.5972 1.5497 1.7495 0.1358  0.1866  0.1977  32  LEU   A C   
34   O  O   . LEU   A 12  ? 1.6243 1.5474 1.8081 0.1179  0.2138  0.2074  32  LEU   A O   
35   C  CB  . LEU   A 12  ? 1.3520 1.3327 1.5465 0.1223  0.1388  0.1387  32  LEU   A CB  
36   C  CG  . LEU   A 12  ? 1.4884 1.4699 1.7272 0.0910  0.1435  0.1202  32  LEU   A CG  
37   C  CD1 . LEU   A 12  ? 1.5061 1.4362 1.7932 0.0766  0.1613  0.1233  32  LEU   A CD1 
38   C  CD2 . LEU   A 12  ? 1.4304 1.4419 1.6809 0.0791  0.1154  0.0840  32  LEU   A CD2 
39   N  N   . PHE   A 13  ? 1.5089 1.5014 1.6129 0.1509  0.1767  0.2024  33  PHE   A N   
40   C  CA  . PHE   A 13  ? 1.5862 1.5848 1.6632 0.1495  0.1987  0.2196  33  PHE   A CA  
41   C  C   . PHE   A 13  ? 1.6365 1.5953 1.6668 0.1747  0.2250  0.2626  33  PHE   A C   
42   O  O   . PHE   A 13  ? 1.6304 1.5712 1.6490 0.1701  0.2579  0.2834  33  PHE   A O   
43   C  CB  . PHE   A 13  ? 1.5308 1.5850 1.5738 0.1539  0.1759  0.2023  33  PHE   A CB  
44   C  CG  . PHE   A 13  ? 1.4194 1.5063 1.5023 0.1295  0.1547  0.1643  33  PHE   A CG  
45   C  CD1 . PHE   A 13  ? 1.3563 1.4402 1.4824 0.1032  0.1673  0.1514  33  PHE   A CD1 
46   C  CD2 . PHE   A 13  ? 1.3807 1.5007 1.4593 0.1342  0.1234  0.1424  33  PHE   A CD2 
47   C  CE1 . PHE   A 13  ? 1.3249 1.4344 1.4811 0.0849  0.1460  0.1185  33  PHE   A CE1 
48   C  CE2 . PHE   A 13  ? 1.3967 1.5394 1.5043 0.1136  0.1069  0.1111  33  PHE   A CE2 
49   C  CZ  . PHE   A 13  ? 1.2586 1.3941 1.4011 0.0904  0.1168  0.0998  33  PHE   A CZ  
50   N  N   . LYS   A 14  ? 1.7345 1.6781 1.7363 0.2035  0.2129  0.2773  34  LYS   A N   
51   C  CA  . LYS   A 14  ? 1.8855 1.7768 1.8468 0.2286  0.2394  0.3209  34  LYS   A CA  
52   C  C   . LYS   A 14  ? 1.8920 1.7229 1.9017 0.2069  0.2768  0.3352  34  LYS   A C   
53   O  O   . LYS   A 14  ? 1.9887 1.7764 1.9741 0.2128  0.3147  0.3715  34  LYS   A O   
54   C  CB  . LYS   A 14  ? 2.0089 1.8943 1.9423 0.2642  0.2162  0.3305  34  LYS   A CB  
55   C  CG  . LYS   A 14  ? 1.9490 1.8918 1.8335 0.2904  0.1814  0.3226  34  LYS   A CG  
56   C  CD  . LYS   A 14  ? 2.1059 2.0371 1.9621 0.3316  0.1645  0.3407  34  LYS   A CD  
57   C  CE  . LYS   A 14  ? 2.1281 2.1206 1.9427 0.3585  0.1274  0.3316  34  LYS   A CE  
58   N  NZ  . LYS   A 14  ? 1.9666 1.9511 1.7573 0.4024  0.1095  0.3503  34  LYS   A NZ  
59   N  N   . LYS   A 15  ? 1.7500 1.5759 1.8282 0.1815  0.2672  0.3063  35  LYS   A N   
60   C  CA  . LYS   A 15  ? 1.7573 1.5307 1.8943 0.1563  0.2976  0.3119  35  LYS   A CA  
61   C  C   . LYS   A 15  ? 1.7887 1.5747 1.9571 0.1273  0.3249  0.3104  35  LYS   A C   
62   O  O   . LYS   A 15  ? 1.8474 1.5920 2.0224 0.1213  0.3677  0.3408  35  LYS   A O   
63   C  CB  . LYS   A 15  ? 1.7731 1.5418 1.9699 0.1390  0.2735  0.2752  35  LYS   A CB  
64   C  CG  . LYS   A 15  ? 1.8920 1.6242 2.1650 0.1041  0.2948  0.2655  35  LYS   A CG  
65   C  CD  . LYS   A 15  ? 1.9360 1.6917 2.2619 0.0817  0.2622  0.2168  35  LYS   A CD  
66   C  CE  . LYS   A 15  ? 1.9338 1.6706 2.3405 0.0448  0.2778  0.2017  35  LYS   A CE  
67   N  NZ  . LYS   A 15  ? 2.0117 1.7747 2.4616 0.0260  0.2416  0.1533  35  LYS   A NZ  
68   N  N   . LEU   A 16  ? 1.8154 1.6575 2.0046 0.1099  0.3028  0.2762  36  LEU   A N   
69   C  CA  . LEU   A 16  ? 1.7909 1.6515 2.0210 0.0828  0.3244  0.2683  36  LEU   A CA  
70   C  C   . LEU   A 16  ? 1.7869 1.6501 1.9628 0.0959  0.3577  0.2999  36  LEU   A C   
71   O  O   . LEU   A 16  ? 1.7798 1.6594 1.9877 0.0763  0.3808  0.2955  36  LEU   A O   
72   C  CB  . LEU   A 16  ? 1.6766 1.5940 1.9321 0.0675  0.2889  0.2250  36  LEU   A CB  
73   C  CG  . LEU   A 16  ? 1.6817 1.5981 1.9974 0.0487  0.2603  0.1890  36  LEU   A CG  
74   C  CD1 . LEU   A 16  ? 1.5429 1.5115 1.8688 0.0381  0.2290  0.1527  36  LEU   A CD1 
75   C  CD2 . LEU   A 16  ? 1.6503 1.5310 2.0437 0.0223  0.2837  0.1877  36  LEU   A CD2 
76   N  N   . GLY   A 17  ? 1.7872 1.6350 1.8815 0.1302  0.3603  0.3304  37  GLY   A N   
77   C  CA  . GLY   A 17  ? 1.8886 1.7393 1.9161 0.1473  0.3869  0.3574  37  GLY   A CA  
78   C  C   . GLY   A 17  ? 1.7999 1.7115 1.8076 0.1448  0.3671  0.3301  37  GLY   A C   
79   O  O   . GLY   A 17  ? 1.8522 1.7694 1.8390 0.1435  0.3973  0.3406  37  GLY   A O   
80   N  N   . ILE   A 18  ? 1.5560 1.5104 1.5699 0.1441  0.3198  0.2956  38  ILE   A N   
81   C  CA  . ILE   A 18  ? 1.6303 1.6388 1.6307 0.1398  0.2975  0.2664  38  ILE   A CA  
82   C  C   . ILE   A 18  ? 1.6429 1.6743 1.5670 0.1709  0.2664  0.2675  38  ILE   A C   
83   O  O   . ILE   A 18  ? 1.5121 1.5459 1.4351 0.1827  0.2380  0.2633  38  ILE   A O   
84   C  CB  . ILE   A 18  ? 1.5925 1.6306 1.6628 0.1125  0.2691  0.2251  38  ILE   A CB  
85   C  CG1 . ILE   A 18  ? 1.5163 1.5375 1.6663 0.0829  0.2952  0.2204  38  ILE   A CG1 
86   C  CG2 . ILE   A 18  ? 1.4619 1.5495 1.5132 0.1105  0.2449  0.1968  38  ILE   A CG2 
87   C  CD1 . ILE   A 18  ? 1.6036 1.6465 1.8181 0.0598  0.2649  0.1814  38  ILE   A CD1 
88   N  N   . PRO   A 19  ? 1.6298 1.6798 1.4920 0.1858  0.2696  0.2708  39  PRO   A N   
89   C  CA  . PRO   A 19  ? 1.7109 1.7826 1.5020 0.2168  0.2373  0.2709  39  PRO   A CA  
90   C  C   . PRO   A 19  ? 1.6145 1.7371 1.4313 0.2071  0.1914  0.2305  39  PRO   A C   
91   O  O   . PRO   A 19  ? 1.4831 1.6240 1.3563 0.1789  0.1857  0.2027  39  PRO   A O   
92   C  CB  . PRO   A 19  ? 1.7045 1.7776 1.4250 0.2318  0.2569  0.2816  39  PRO   A CB  
93   C  CG  . PRO   A 19  ? 1.6365 1.7149 1.4077 0.2014  0.2847  0.2675  39  PRO   A CG  
94   C  CD  . PRO   A 19  ? 1.6065 1.6591 1.4618 0.1762  0.3028  0.2726  39  PRO   A CD  
95   N  N   . GLY   A 20  ? 1.6021 1.7470 1.3772 0.2322  0.1584  0.2281  40  GLY   A N   
96   C  CA  . GLY   A 20  ? 1.6346 1.8283 1.4330 0.2244  0.1178  0.1925  40  GLY   A CA  
97   C  C   . GLY   A 20  ? 1.6284 1.8437 1.3956 0.2542  0.0849  0.1953  40  GLY   A C   
98   O  O   . GLY   A 20  ? 1.7174 1.9053 1.4529 0.2818  0.0908  0.2256  40  GLY   A O   
99   N  N   . PRO   A 21  ? 1.6119 1.8771 1.3915 0.2496  0.0496  0.1635  41  PRO   A N   
100  C  CA  . PRO   A 21  ? 1.5683 1.8647 1.3312 0.2769  0.0151  0.1615  41  PRO   A CA  
101  C  C   . PRO   A 21  ? 1.4554 1.7388 1.2566 0.2856  0.0141  0.1738  41  PRO   A C   
102  O  O   . PRO   A 21  ? 1.3206 1.5940 1.1774 0.2619  0.0242  0.1641  41  PRO   A O   
103  C  CB  . PRO   A 21  ? 1.5333 1.8844 1.3237 0.2588  -0.0156 0.1208  41  PRO   A CB  
104  C  CG  . PRO   A 21  ? 1.5672 1.9080 1.4033 0.2216  0.0030  0.1044  41  PRO   A CG  
105  C  CD  . PRO   A 21  ? 1.5119 1.8067 1.3255 0.2194  0.0402  0.1281  41  PRO   A CD  
106  N  N   . THR   A 22  ? 1.5536 1.8355 1.3209 0.3225  0.0005  0.1942  42  THR   A N   
107  C  CA  . THR   A 22  ? 1.4440 1.7086 1.2405 0.3379  0.0008  0.2087  42  THR   A CA  
108  C  C   . THR   A 22  ? 1.2803 1.5922 1.1411 0.3245  -0.0224 0.1768  42  THR   A C   
109  O  O   . THR   A 22  ? 1.2503 1.6180 1.1152 0.3324  -0.0545 0.1563  42  THR   A O   
110  C  CB  . THR   A 22  ? 1.5251 1.7816 1.2678 0.3853  -0.0129 0.2368  42  THR   A CB  
111  O  OG1 . THR   A 22  ? 1.5581 1.7666 1.2312 0.3989  0.0128  0.2691  42  THR   A OG1 
112  C  CG2 . THR   A 22  ? 1.4446 1.6749 1.2175 0.4031  -0.0087 0.2535  42  THR   A CG2 
113  N  N   . PRO   A 23  ? 1.2235 1.5150 1.1349 0.3047  -0.0070 0.1707  43  PRO   A N   
114  C  CA  . PRO   A 23  ? 1.2607 1.5935 1.2273 0.2911  -0.0232 0.1411  43  PRO   A CA  
115  C  C   . PRO   A 23  ? 1.3755 1.7302 1.3582 0.3231  -0.0406 0.1456  43  PRO   A C   
116  O  O   . PRO   A 23  ? 1.2710 1.5868 1.2400 0.3490  -0.0313 0.1717  43  PRO   A O   
117  C  CB  . PRO   A 23  ? 1.2485 1.5419 1.2501 0.2634  0.0010  0.1355  43  PRO   A CB  
118  C  CG  . PRO   A 23  ? 1.3480 1.5790 1.3267 0.2743  0.0259  0.1673  43  PRO   A CG  
119  C  CD  . PRO   A 23  ? 1.3188 1.5484 1.2399 0.2904  0.0269  0.1875  43  PRO   A CD  
120  N  N   . LEU   A 24  ? 1.2551 1.6723 1.2711 0.3212  -0.0650 0.1198  44  LEU   A N   
121  C  CA  . LEU   A 24  ? 1.2658 1.7131 1.3169 0.3464  -0.0790 0.1174  44  LEU   A CA  
122  C  C   . LEU   A 24  ? 1.2706 1.6948 1.3650 0.3319  -0.0581 0.1092  44  LEU   A C   
123  O  O   . LEU   A 24  ? 1.2744 1.6874 1.3832 0.2976  -0.0443 0.0931  44  LEU   A O   
124  C  CB  . LEU   A 24  ? 1.2431 1.7694 1.3259 0.3458  -0.1096 0.0903  44  LEU   A CB  
125  C  CG  . LEU   A 24  ? 1.2901 1.8499 1.3339 0.3626  -0.1394 0.0896  44  LEU   A CG  
126  C  CD1 . LEU   A 24  ? 1.2514 1.8887 1.3437 0.3497  -0.1672 0.0545  44  LEU   A CD1 
127  C  CD2 . LEU   A 24  ? 1.4170 1.9672 1.4250 0.4121  -0.1539 0.1174  44  LEU   A CD2 
128  N  N   . PRO   A 25  ? 1.4516 1.8660 1.5634 0.3600  -0.0562 0.1193  45  PRO   A N   
129  C  CA  . PRO   A 25  ? 1.3652 1.7542 1.5113 0.3495  -0.0364 0.1091  45  PRO   A CA  
130  C  C   . PRO   A 25  ? 1.2716 1.7069 1.4591 0.3221  -0.0374 0.0773  45  PRO   A C   
131  O  O   . PRO   A 25  ? 1.2519 1.7518 1.4633 0.3224  -0.0560 0.0628  45  PRO   A O   
132  C  CB  . PRO   A 25  ? 1.2199 1.6073 1.3795 0.3913  -0.0405 0.1220  45  PRO   A CB  
133  C  CG  . PRO   A 25  ? 1.3439 1.7197 1.4582 0.4220  -0.0536 0.1508  45  PRO   A CG  
134  C  CD  . PRO   A 25  ? 1.3099 1.7285 1.4042 0.4059  -0.0716 0.1415  45  PRO   A CD  
135  N  N   . PHE   A 26  ? 1.3590 1.7581 1.5538 0.2980  -0.0174 0.0665  46  PHE   A N   
136  C  CA  . PHE   A 26  ? 1.2978 1.7234 1.5208 0.2719  -0.0117 0.0403  46  PHE   A CA  
137  C  C   . PHE   A 26  ? 1.2245 1.6764 1.4407 0.2422  -0.0201 0.0284  46  PHE   A C   
138  O  O   . PHE   A 26  ? 1.2242 1.6554 1.4360 0.2141  -0.0096 0.0166  46  PHE   A O   
139  C  CB  . PHE   A 26  ? 1.2482 1.7282 1.5159 0.2887  -0.0151 0.0285  46  PHE   A CB  
140  C  CG  . PHE   A 26  ? 1.3920 1.8448 1.6700 0.3171  -0.0031 0.0349  46  PHE   A CG  
141  C  CD1 . PHE   A 26  ? 1.5519 1.9671 1.8313 0.3077  0.0182  0.0234  46  PHE   A CD1 
142  C  CD2 . PHE   A 26  ? 1.3272 1.7894 1.6097 0.3558  -0.0144 0.0517  46  PHE   A CD2 
143  C  CE1 . PHE   A 26  ? 1.6300 2.0167 1.9165 0.3349  0.0295  0.0263  46  PHE   A CE1 
144  C  CE2 . PHE   A 26  ? 1.4373 1.8707 1.7299 0.3840  -0.0027 0.0569  46  PHE   A CE2 
145  C  CZ  . PHE   A 26  ? 1.5699 1.9652 1.8654 0.3728  0.0200  0.0431  46  PHE   A CZ  
146  N  N   . LEU   A 27  ? 1.1171 1.6125 1.3301 0.2499  -0.0407 0.0301  47  LEU   A N   
147  C  CA  . LEU   A 27  ? 1.1675 1.6875 1.3752 0.2231  -0.0497 0.0155  47  LEU   A CA  
148  C  C   . LEU   A 27  ? 1.1465 1.6203 1.3113 0.2088  -0.0426 0.0251  47  LEU   A C   
149  O  O   . LEU   A 27  ? 1.1596 1.6367 1.3208 0.1820  -0.0422 0.0111  47  LEU   A O   
150  C  CB  . LEU   A 27  ? 1.2053 1.7858 1.4220 0.2370  -0.0773 0.0100  47  LEU   A CB  
151  C  CG  . LEU   A 27  ? 1.0221 1.6658 1.2967 0.2469  -0.0878 -0.0050 47  LEU   A CG  
152  C  CD1 . LEU   A 27  ? 0.9586 1.6634 1.2434 0.2560  -0.1210 -0.0157 47  LEU   A CD1 
153  C  CD2 . LEU   A 27  ? 1.1155 1.7700 1.4291 0.2166  -0.0692 -0.0253 47  LEU   A CD2 
154  N  N   . GLY   A 28  ? 1.2640 1.6942 1.3996 0.2258  -0.0349 0.0487  48  GLY   A N   
155  C  CA  . GLY   A 28  ? 1.2301 1.6260 1.3298 0.2146  -0.0267 0.0591  48  GLY   A CA  
156  C  C   . GLY   A 28  ? 1.1832 1.6138 1.2564 0.2199  -0.0448 0.0574  48  GLY   A C   
157  O  O   . GLY   A 28  ? 1.1336 1.5862 1.1912 0.2484  -0.0611 0.0677  48  GLY   A O   
158  N  N   . ASN   A 29  ? 1.0994 1.5343 1.1652 0.1944  -0.0442 0.0425  49  ASN   A N   
159  C  CA  . ASN   A 29  ? 0.9901 1.4530 1.0270 0.1967  -0.0609 0.0356  49  ASN   A CA  
160  C  C   . ASN   A 29  ? 1.1027 1.6066 1.1681 0.1727  -0.0748 0.0044  49  ASN   A C   
161  O  O   . ASN   A 29  ? 1.1734 1.6894 1.2170 0.1647  -0.0845 -0.0077 49  ASN   A O   
162  C  CB  . ASN   A 29  ? 1.1553 1.5797 1.1503 0.1914  -0.0442 0.0481  49  ASN   A CB  
163  C  CG  . ASN   A 29  ? 1.1905 1.5649 1.1693 0.2056  -0.0217 0.0787  49  ASN   A CG  
164  O  OD1 . ASN   A 29  ? 1.1824 1.5250 1.1878 0.1915  -0.0040 0.0808  49  ASN   A OD1 
165  N  ND2 . ASN   A 29  ? 1.1376 1.5018 1.0709 0.2340  -0.0224 0.1022  49  ASN   A ND2 
166  N  N   . ILE   A 30  ? 1.0114 1.5339 1.1236 0.1616  -0.0737 -0.0088 50  ILE   A N   
167  C  CA  . ILE   A 30  ? 1.0050 1.5567 1.1466 0.1351  -0.0797 -0.0356 50  ILE   A CA  
168  C  C   . ILE   A 30  ? 1.1513 1.7594 1.3046 0.1408  -0.1078 -0.0524 50  ILE   A C   
169  O  O   . ILE   A 30  ? 1.2051 1.8324 1.3736 0.1177  -0.1150 -0.0753 50  ILE   A O   
170  C  CB  . ILE   A 30  ? 1.0059 1.5589 1.1901 0.1232  -0.0659 -0.0426 50  ILE   A CB  
171  C  CG1 . ILE   A 30  ? 1.2089 1.7968 1.4245 0.1468  -0.0728 -0.0385 50  ILE   A CG1 
172  C  CG2 . ILE   A 30  ? 1.1427 1.6391 1.3127 0.1162  -0.0435 -0.0319 50  ILE   A CG2 
173  C  CD1 . ILE   A 30  ? 1.2908 1.8985 1.5539 0.1344  -0.0606 -0.0516 50  ILE   A CD1 
174  N  N   . LEU   A 31  ? 1.2415 1.8755 1.3896 0.1718  -0.1258 -0.0427 51  LEU   A N   
175  C  CA  . LEU   A 31  ? 1.1155 1.8051 1.2727 0.1801  -0.1588 -0.0612 51  LEU   A CA  
176  C  C   . LEU   A 31  ? 1.2216 1.9005 1.3285 0.1743  -0.1697 -0.0702 51  LEU   A C   
177  O  O   . LEU   A 31  ? 1.1906 1.9096 1.3095 0.1671  -0.1953 -0.0964 51  LEU   A O   
178  C  CB  . LEU   A 31  ? 1.1233 1.8379 1.2756 0.2207  -0.1789 -0.0465 51  LEU   A CB  
179  C  CG  . LEU   A 31  ? 1.1111 1.8594 1.3251 0.2320  -0.1784 -0.0466 51  LEU   A CG  
180  C  CD1 . LEU   A 31  ? 1.0137 1.7912 1.2184 0.2759  -0.2061 -0.0349 51  LEU   A CD1 
181  C  CD2 . LEU   A 31  ? 0.9141 1.7152 1.1997 0.2039  -0.1827 -0.0775 51  LEU   A CD2 
182  N  N   . SER   A 32  ? 1.2135 1.8390 1.2673 0.1771  -0.1497 -0.0506 52  SER   A N   
183  C  CA  . SER   A 32  ? 1.2973 1.9071 1.3002 0.1730  -0.1529 -0.0577 52  SER   A CA  
184  C  C   . SER   A 32  ? 1.3381 1.9473 1.3635 0.1371  -0.1484 -0.0848 52  SER   A C   
185  O  O   . SER   A 32  ? 1.3868 1.9926 1.3779 0.1331  -0.1566 -0.0993 52  SER   A O   
186  C  CB  . SER   A 32  ? 1.2975 1.8516 1.2488 0.1843  -0.1258 -0.0278 52  SER   A CB  
187  O  OG  . SER   A 32  ? 1.2724 1.8192 1.1940 0.2193  -0.1288 -0.0004 52  SER   A OG  
188  N  N   . TYR   A 33  ? 1.2379 1.8458 1.3148 0.1129  -0.1345 -0.0916 53  TYR   A N   
189  C  CA  . TYR   A 33  ? 1.1965 1.8001 1.2951 0.0803  -0.1299 -0.1152 53  TYR   A CA  
190  C  C   . TYR   A 33  ? 1.3373 1.9892 1.4672 0.0692  -0.1565 -0.1460 53  TYR   A C   
191  O  O   . TYR   A 33  ? 1.3195 1.9681 1.4752 0.0406  -0.1522 -0.1661 53  TYR   A O   
192  C  CB  . TYR   A 33  ? 1.1070 1.6904 1.2426 0.0615  -0.1065 -0.1104 53  TYR   A CB  
193  C  CG  . TYR   A 33  ? 1.2465 1.7783 1.3574 0.0637  -0.0825 -0.0893 53  TYR   A CG  
194  C  CD1 . TYR   A 33  ? 1.2430 1.7465 1.3112 0.0694  -0.0765 -0.0814 53  TYR   A CD1 
195  C  CD2 . TYR   A 33  ? 1.1950 1.7075 1.3278 0.0602  -0.0657 -0.0791 53  TYR   A CD2 
196  C  CE1 . TYR   A 33  ? 1.2456 1.7074 1.3036 0.0693  -0.0552 -0.0644 53  TYR   A CE1 
197  C  CE2 . TYR   A 33  ? 1.1462 1.6138 1.2622 0.0612  -0.0482 -0.0641 53  TYR   A CE2 
198  C  CZ  . TYR   A 33  ? 1.2551 1.6998 1.3389 0.0645  -0.0434 -0.0569 53  TYR   A CZ  
199  O  OH  . TYR   A 33  ? 1.1672 1.5727 1.2463 0.0634  -0.0266 -0.0441 53  TYR   A OH  
200  N  N   . HIS   A 34  ? 1.2748 1.9703 1.4051 0.0911  -0.1851 -0.1512 54  HIS   A N   
201  C  CA  . HIS   A 34  ? 1.3346 2.0827 1.5061 0.0800  -0.2145 -0.1840 54  HIS   A CA  
202  C  C   . HIS   A 34  ? 1.3637 2.1012 1.5065 0.0650  -0.2269 -0.2104 54  HIS   A C   
203  O  O   . HIS   A 34  ? 1.3578 2.1301 1.5422 0.0465  -0.2475 -0.2424 54  HIS   A O   
204  C  CB  . HIS   A 34  ? 1.3652 2.1631 1.5398 0.1125  -0.2475 -0.1838 54  HIS   A CB  
205  C  CG  . HIS   A 34  ? 1.4093 2.1973 1.5060 0.1415  -0.2688 -0.1802 54  HIS   A CG  
206  N  ND1 . HIS   A 34  ? 1.5257 2.2633 1.5530 0.1625  -0.2483 -0.1483 54  HIS   A ND1 
207  C  CD2 . HIS   A 34  ? 1.4182 2.2386 1.4929 0.1537  -0.3079 -0.2050 54  HIS   A CD2 
208  C  CE1 . HIS   A 34  ? 1.5223 2.2592 1.4834 0.1874  -0.2700 -0.1507 54  HIS   A CE1 
209  N  NE2 . HIS   A 34  ? 1.5012 2.2876 1.4857 0.1840  -0.3085 -0.1859 54  HIS   A NE2 
210  N  N   . LYS   A 35  ? 1.4108 2.1014 1.4876 0.0725  -0.2137 -0.1993 55  LYS   A N   
211  C  CA  . LYS   A 35  ? 1.5190 2.1913 1.5647 0.0597  -0.2196 -0.2237 55  LYS   A CA  
212  C  C   . LYS   A 35  ? 1.4441 2.0680 1.4939 0.0345  -0.1875 -0.2206 55  LYS   A C   
213  O  O   . LYS   A 35  ? 1.5492 2.1494 1.5716 0.0256  -0.1867 -0.2380 55  LYS   A O   
214  C  CB  . LYS   A 35  ? 1.5322 2.1902 1.4956 0.0907  -0.2289 -0.2166 55  LYS   A CB  
215  C  CG  . LYS   A 35  ? 1.5395 2.2433 1.4862 0.1171  -0.2698 -0.2283 55  LYS   A CG  
216  C  CD  . LYS   A 35  ? 1.6009 2.2815 1.4523 0.1497  -0.2749 -0.2191 55  LYS   A CD  
217  C  CE  . LYS   A 35  ? 1.7300 2.4547 1.5562 0.1766  -0.3228 -0.2382 55  LYS   A CE  
218  N  NZ  . LYS   A 35  ? 1.6599 2.4176 1.5235 0.1531  -0.3556 -0.2880 55  LYS   A NZ  
219  N  N   . GLY   A 36  ? 1.5210 2.1292 1.6023 0.0254  -0.1629 -0.2005 56  GLY   A N   
220  C  CA  . GLY   A 36  ? 1.4591 2.0210 1.5409 0.0069  -0.1356 -0.1948 56  GLY   A CA  
221  C  C   . GLY   A 36  ? 1.4245 1.9499 1.4665 0.0236  -0.1145 -0.1669 56  GLY   A C   
222  O  O   . GLY   A 36  ? 1.4487 1.9759 1.4500 0.0480  -0.1179 -0.1539 56  GLY   A O   
223  N  N   . PHE   A 37  ? 1.2012 1.6918 1.2558 0.0107  -0.0922 -0.1576 57  PHE   A N   
224  C  CA  . PHE   A 37  ? 1.3697 1.8276 1.4009 0.0221  -0.0721 -0.1346 57  PHE   A CA  
225  C  C   . PHE   A 37  ? 1.2505 1.6951 1.2370 0.0327  -0.0688 -0.1370 57  PHE   A C   
226  O  O   . PHE   A 37  ? 1.3222 1.7545 1.2825 0.0500  -0.0557 -0.1162 57  PHE   A O   
227  C  CB  . PHE   A 37  ? 1.3247 1.7499 1.3779 0.0057  -0.0554 -0.1317 57  PHE   A CB  
228  C  CG  . PHE   A 37  ? 1.4140 1.8456 1.5027 -0.0044 -0.0540 -0.1298 57  PHE   A CG  
229  C  CD1 . PHE   A 37  ? 1.4818 1.9291 1.5962 -0.0220 -0.0610 -0.1478 57  PHE   A CD1 
230  C  CD2 . PHE   A 37  ? 1.3884 1.8069 1.4850 0.0031  -0.0431 -0.1108 57  PHE   A CD2 
231  C  CE1 . PHE   A 37  ? 1.5080 1.9600 1.6532 -0.0305 -0.0536 -0.1444 57  PHE   A CE1 
232  C  CE2 . PHE   A 37  ? 1.3516 1.7731 1.4742 -0.0035 -0.0389 -0.1099 57  PHE   A CE2 
233  C  CZ  . PHE   A 37  ? 1.5442 1.9832 1.6900 -0.0198 -0.0424 -0.1255 57  PHE   A CZ  
234  N  N   . CYS   A 38  ? 1.1641 1.6085 1.1413 0.0226  -0.0780 -0.1628 58  CYS   A N   
235  C  CA  . CYS   A 38  ? 1.2810 1.7074 1.2158 0.0317  -0.0704 -0.1687 58  CYS   A CA  
236  C  C   . CYS   A 38  ? 1.3194 1.7623 1.2042 0.0572  -0.0796 -0.1635 58  CYS   A C   
237  O  O   . CYS   A 38  ? 1.3486 1.7739 1.1964 0.0740  -0.0604 -0.1460 58  CYS   A O   
238  C  CB  . CYS   A 38  ? 1.2789 1.6965 1.2179 0.0145  -0.0789 -0.2002 58  CYS   A CB  
239  S  SG  . CYS   A 38  ? 1.1972 1.5842 1.1814 -0.0104 -0.0658 -0.2023 58  CYS   A SG  
240  N  N   . MET   A 39  ? 1.2937 1.7705 1.1767 0.0613  -0.1084 -0.1785 59  MET   A N   
241  C  CA  . MET   A 39  ? 1.3561 1.8483 1.1848 0.0900  -0.1223 -0.1732 59  MET   A CA  
242  C  C   . MET   A 39  ? 1.3511 1.8372 1.1680 0.1108  -0.1073 -0.1349 59  MET   A C   
243  O  O   . MET   A 39  ? 1.3424 1.8206 1.1012 0.1374  -0.1032 -0.1189 59  MET   A O   
244  C  CB  . MET   A 39  ? 1.5061 2.0417 1.3471 0.0903  -0.1617 -0.1991 59  MET   A CB  
245  C  CG  . MET   A 39  ? 1.5100 2.0517 1.3821 0.0629  -0.1766 -0.2382 59  MET   A CG  
246  S  SD  . MET   A 39  ? 1.8379 2.3395 1.6597 0.0611  -0.1640 -0.2583 59  MET   A SD  
247  C  CE  . MET   A 39  ? 1.5869 2.0992 1.3205 0.0989  -0.1834 -0.2621 59  MET   A CE  
248  N  N   . PHE   A 40  ? 1.2554 1.7408 1.1229 0.1000  -0.0979 -0.1197 60  PHE   A N   
249  C  CA  . PHE   A 40  ? 1.2989 1.7703 1.1607 0.1169  -0.0809 -0.0847 60  PHE   A CA  
250  C  C   . PHE   A 40  ? 1.3825 1.8141 1.2217 0.1191  -0.0469 -0.0655 60  PHE   A C   
251  O  O   . PHE   A 40  ? 1.3475 1.7639 1.1458 0.1412  -0.0328 -0.0406 60  PHE   A O   
252  C  CB  . PHE   A 40  ? 1.2752 1.7526 1.1960 0.1040  -0.0792 -0.0785 60  PHE   A CB  
253  C  CG  . PHE   A 40  ? 1.2624 1.7200 1.1832 0.1190  -0.0618 -0.0460 60  PHE   A CG  
254  C  CD1 . PHE   A 40  ? 1.2689 1.7346 1.1592 0.1478  -0.0701 -0.0273 60  PHE   A CD1 
255  C  CD2 . PHE   A 40  ? 1.2688 1.6972 1.2195 0.1053  -0.0393 -0.0354 60  PHE   A CD2 
256  C  CE1 . PHE   A 40  ? 1.3405 1.7814 1.2315 0.1613  -0.0527 0.0029  60  PHE   A CE1 
257  C  CE2 . PHE   A 40  ? 1.2843 1.6911 1.2385 0.1172  -0.0243 -0.0088 60  PHE   A CE2 
258  C  CZ  . PHE   A 40  ? 1.3740 1.7851 1.2992 0.1445  -0.0292 0.0110  60  PHE   A CZ  
259  N  N   . ASP   A 41  ? 1.4022 1.8165 1.2697 0.0972  -0.0326 -0.0763 61  ASP   A N   
260  C  CA  . ASP   A 41  ? 1.3773 1.7608 1.2386 0.0976  -0.0009 -0.0611 61  ASP   A CA  
261  C  C   . ASP   A 41  ? 1.4415 1.8181 1.2435 0.1142  0.0094  -0.0622 61  ASP   A C   
262  O  O   . ASP   A 41  ? 1.4429 1.7994 1.2224 0.1268  0.0376  -0.0381 61  ASP   A O   
263  C  CB  . ASP   A 41  ? 1.2589 1.6295 1.1650 0.0738  0.0063  -0.0753 61  ASP   A CB  
264  C  CG  . ASP   A 41  ? 1.2097 1.5823 1.1637 0.0597  -0.0021 -0.0743 61  ASP   A CG  
265  O  OD1 . ASP   A 41  ? 1.2518 1.6283 1.2121 0.0684  -0.0031 -0.0566 61  ASP   A OD1 
266  O  OD2 . ASP   A 41  ? 1.2134 1.5802 1.1944 0.0420  -0.0065 -0.0909 61  ASP   A OD2 
267  N  N   . MET   A 42  ? 1.4084 1.7991 1.1839 0.1144  -0.0111 -0.0906 62  MET   A N   
268  C  CA  A MET   A 42  ? 1.4384 1.8208 1.1479 0.1331  -0.0031 -0.0954 62  MET   A CA  
269  C  CA  B MET   A 42  ? 1.4382 1.8205 1.1477 0.1331  -0.0029 -0.0953 62  MET   A CA  
270  C  C   . MET   A 42  ? 1.4827 1.8638 1.1342 0.1632  -0.0005 -0.0687 62  MET   A C   
271  O  O   . MET   A 42  ? 1.5731 1.9310 1.1806 0.1796  0.0302  -0.0482 62  MET   A O   
272  C  CB  A MET   A 42  ? 1.3987 1.7966 1.0907 0.1282  -0.0325 -0.1348 62  MET   A CB  
273  C  CB  B MET   A 42  ? 1.4385 1.8360 1.1300 0.1283  -0.0321 -0.1347 62  MET   A CB  
274  C  CG  A MET   A 42  ? 1.4005 1.7862 1.1298 0.1044  -0.0273 -0.1595 62  MET   A CG  
275  C  CG  B MET   A 42  ? 1.4030 1.7884 1.1320 0.1045  -0.0270 -0.1595 62  MET   A CG  
276  S  SD  A MET   A 42  ? 1.4192 1.7760 1.1106 0.1149  0.0076  -0.1624 62  MET   A SD  
277  S  SD  B MET   A 42  ? 1.4526 1.8382 1.1375 0.1064  -0.0475 -0.2032 62  MET   A SD  
278  C  CE  A MET   A 42  ? 1.3942 1.7573 1.0011 0.1366  -0.0144 -0.1892 62  MET   A CE  
279  C  CE  B MET   A 42  ? 1.3956 1.7599 0.9998 0.1375  -0.0163 -0.1897 62  MET   A CE  
280  N  N   . GLU   A 43  ? 1.5548 1.9600 1.2061 0.1722  -0.0310 -0.0675 63  GLU   A N   
281  C  CA  . GLU   A 43  ? 1.5816 1.9833 1.1769 0.2046  -0.0324 -0.0401 63  GLU   A CA  
282  C  C   . GLU   A 43  ? 1.6063 1.9761 1.2117 0.2088  0.0063  0.0010  63  GLU   A C   
283  O  O   . GLU   A 43  ? 1.7971 2.1407 1.3449 0.2308  0.0322  0.0271  63  GLU   A O   
284  C  CB  . GLU   A 43  ? 1.6291 2.0670 1.2403 0.2126  -0.0736 -0.0473 63  GLU   A CB  
285  C  CG  . GLU   A 43  ? 1.6928 2.1647 1.2865 0.2145  -0.1155 -0.0863 63  GLU   A CG  
286  C  CD  . GLU   A 43  ? 1.9056 2.4201 1.5309 0.2216  -0.1546 -0.0931 63  GLU   A CD  
287  O  OE1 . GLU   A 43  ? 1.9297 2.4427 1.5773 0.2307  -0.1474 -0.0646 63  GLU   A OE1 
288  O  OE2 . GLU   A 43  ? 1.9251 2.4749 1.5575 0.2179  -0.1922 -0.1283 63  GLU   A OE2 
289  N  N   . CYS   A 44  ? 1.5415 1.9108 1.2190 0.1876  0.0117  0.0066  64  CYS   A N   
290  C  CA  . CYS   A 44  ? 1.5314 1.8698 1.2291 0.1878  0.0452  0.0406  64  CYS   A CA  
291  C  C   . CYS   A 44  ? 1.5828 1.8936 1.2703 0.1833  0.0862  0.0505  64  CYS   A C   
292  O  O   . CYS   A 44  ? 1.6605 1.9426 1.3285 0.1953  0.1186  0.0831  64  CYS   A O   
293  C  CB  . CYS   A 44  ? 1.4707 1.8132 1.2460 0.1640  0.0404  0.0359  64  CYS   A CB  
294  S  SG  . CYS   A 44  ? 1.4870 1.8498 1.2799 0.1761  0.0114  0.0425  64  CYS   A SG  
295  N  N   . HIS   A 45  ? 1.5870 1.9053 1.2913 0.1664  0.0875  0.0232  65  HIS   A N   
296  C  CA  . HIS   A 45  ? 1.5488 1.8474 1.2461 0.1648  0.1261  0.0289  65  HIS   A CA  
297  C  C   . HIS   A 45  ? 1.6686 1.9516 1.2798 0.1943  0.1460  0.0474  65  HIS   A C   
298  O  O   . HIS   A 45  ? 1.7402 1.9988 1.3426 0.1993  0.1896  0.0719  65  HIS   A O   
299  C  CB  . HIS   A 45  ? 1.5559 1.8662 1.2762 0.1478  0.1181  -0.0067 65  HIS   A CB  
300  C  CG  . HIS   A 45  ? 1.5944 1.8901 1.3298 0.1434  0.1570  -0.0042 65  HIS   A CG  
301  N  ND1 . HIS   A 45  ? 1.6529 1.9309 1.4133 0.1429  0.1957  0.0253  65  HIS   A ND1 
302  C  CD2 . HIS   A 45  ? 1.5483 1.8458 1.2829 0.1397  0.1641  -0.0285 65  HIS   A CD2 
303  C  CE1 . HIS   A 45  ? 1.5958 1.8705 1.3747 0.1387  0.2253  0.0188  65  HIS   A CE1 
304  N  NE2 . HIS   A 45  ? 1.5780 1.8636 1.3393 0.1384  0.2067  -0.0134 65  HIS   A NE2 
305  N  N   . LYS   A 46  ? 1.7529 2.0495 1.2997 0.2148  0.1148  0.0361  66  LYS   A N   
306  C  CA  . LYS   A 46  ? 1.8285 2.1073 1.2791 0.2480  0.1290  0.0536  66  LYS   A CA  
307  C  C   . LYS   A 46  ? 1.9248 2.1804 1.3500 0.2684  0.1436  0.0977  66  LYS   A C   
308  O  O   . LYS   A 46  ? 1.9478 2.1708 1.3193 0.2872  0.1834  0.1287  66  LYS   A O   
309  C  CB  . LYS   A 46  ? 1.8310 2.1330 1.2215 0.2647  0.0840  0.0230  66  LYS   A CB  
310  C  CG  . LYS   A 46  ? 2.0190 2.3080 1.3264 0.2840  0.0977  0.0103  66  LYS   A CG  
311  C  CD  . LYS   A 46  ? 2.1395 2.4505 1.3849 0.3029  0.0467  -0.0208 66  LYS   A CD  
312  C  CE  . LYS   A 46  ? 2.2427 2.5504 1.4212 0.3383  0.0292  0.0063  66  LYS   A CE  
313  N  NZ  . LYS   A 46  ? 2.4424 2.7076 1.5299 0.3692  0.0739  0.0428  66  LYS   A NZ  
314  N  N   . LYS   A 47  ? 2.0757 2.3448 1.5386 0.2658  0.1147  0.1020  67  LYS   A N   
315  C  CA  . LYS   A 47  ? 2.1534 2.4001 1.5844 0.2907  0.1205  0.1411  67  LYS   A CA  
316  C  C   . LYS   A 47  ? 2.1233 2.3293 1.5862 0.2815  0.1724  0.1776  67  LYS   A C   
317  O  O   . LYS   A 47  ? 2.2286 2.3979 1.6359 0.3056  0.2005  0.2159  67  LYS   A O   
318  C  CB  . LYS   A 47  ? 2.1166 2.3909 1.5895 0.2900  0.0775  0.1328  67  LYS   A CB  
319  C  CG  . LYS   A 47  ? 2.2314 2.5216 1.6367 0.3266  0.0391  0.1346  67  LYS   A CG  
320  C  CD  . LYS   A 47  ? 2.2641 2.5847 1.7237 0.3260  0.0020  0.1280  67  LYS   A CD  
321  C  CE  . LYS   A 47  ? 2.2053 2.5743 1.7274 0.2978  -0.0317 0.0821  67  LYS   A CE  
322  N  NZ  . LYS   A 47  ? 2.1347 2.5363 1.7112 0.2982  -0.0632 0.0758  67  LYS   A NZ  
323  N  N   . TYR   A 48  ? 1.8892 2.0991 1.4411 0.2471  0.1854  0.1663  68  TYR   A N   
324  C  CA  . TYR   A 48  ? 1.8198 1.9970 1.4220 0.2343  0.2239  0.1953  68  TYR   A CA  
325  C  C   . TYR   A 48  ? 1.7913 1.9586 1.4342 0.2129  0.2672  0.1943  68  TYR   A C   
326  O  O   . TYR   A 48  ? 1.7545 1.8910 1.4282 0.2059  0.3068  0.2223  68  TYR   A O   
327  C  CB  . TYR   A 48  ? 1.6868 1.8742 1.3668 0.2150  0.1996  0.1858  68  TYR   A CB  
328  C  CG  . TYR   A 48  ? 1.8288 2.0341 1.4837 0.2348  0.1573  0.1830  68  TYR   A CG  
329  C  CD1 . TYR   A 48  ? 1.8206 1.9998 1.4320 0.2637  0.1610  0.2171  68  TYR   A CD1 
330  C  CD2 . TYR   A 48  ? 1.7606 2.0086 1.4383 0.2254  0.1150  0.1471  68  TYR   A CD2 
331  C  CE1 . TYR   A 48  ? 1.8059 2.0064 1.4008 0.2845  0.1208  0.2134  68  TYR   A CE1 
332  C  CE2 . TYR   A 48  ? 1.7526 2.0235 1.4185 0.2428  0.0778  0.1431  68  TYR   A CE2 
333  C  CZ  . TYR   A 48  ? 1.8375 2.0872 1.4637 0.2732  0.0794  0.1753  68  TYR   A CZ  
334  O  OH  . TYR   A 48  ? 1.7867 2.0643 1.4080 0.2929  0.0408  0.1699  68  TYR   A OH  
335  N  N   . GLY   A 49  ? 1.7535 1.9454 1.4028 0.2024  0.2616  0.1627  69  GLY   A N   
336  C  CA  . GLY   A 49  ? 1.7008 1.8863 1.3837 0.1883  0.3043  0.1625  69  GLY   A CA  
337  C  C   . GLY   A 49  ? 1.6555 1.8592 1.4388 0.1558  0.2978  0.1378  69  GLY   A C   
338  O  O   . GLY   A 49  ? 1.6322 1.8599 1.4393 0.1449  0.2573  0.1077  69  GLY   A O   
339  N  N   . LYS   A 50  ? 1.6049 1.7966 1.4484 0.1405  0.3379  0.1505  70  LYS   A N   
340  C  CA  . LYS   A 50  ? 1.6002 1.8105 1.5369 0.1133  0.3318  0.1257  70  LYS   A CA  
341  C  C   . LYS   A 50  ? 1.4848 1.6964 1.4768 0.0971  0.2982  0.1181  70  LYS   A C   
342  O  O   . LYS   A 50  ? 1.4509 1.6802 1.5000 0.0795  0.2765  0.0912  70  LYS   A O   
343  C  CB  . LYS   A 50  ? 1.6514 1.8535 1.6449 0.1021  0.3831  0.1400  70  LYS   A CB  
344  C  CG  . LYS   A 50  ? 1.7740 1.9516 1.8226 0.0891  0.4027  0.1655  70  LYS   A CG  
345  C  CD  . LYS   A 50  ? 1.9252 2.0814 1.9803 0.0907  0.4661  0.1969  70  LYS   A CD  
346  C  CE  . LYS   A 50  ? 1.9672 2.0991 2.0975 0.0712  0.4860  0.2165  70  LYS   A CE  
347  N  NZ  . LYS   A 50  ? 1.8924 1.9991 1.9930 0.0782  0.4568  0.2292  70  LYS   A NZ  
348  N  N   . VAL   A 51  ? 1.6291 1.8198 1.6016 0.1053  0.2940  0.1411  71  VAL   A N   
349  C  CA  . VAL   A 51  ? 1.4997 1.6861 1.5208 0.0927  0.2679  0.1359  71  VAL   A CA  
350  C  C   . VAL   A 51  ? 1.5141 1.6919 1.4788 0.1133  0.2468  0.1503  71  VAL   A C   
351  O  O   . VAL   A 51  ? 1.4941 1.6515 1.4013 0.1347  0.2662  0.1791  71  VAL   A O   
352  C  CB  . VAL   A 51  ? 1.4017 1.5640 1.4937 0.0757  0.2966  0.1510  71  VAL   A CB  
353  C  CG1 . VAL   A 51  ? 1.4084 1.5541 1.5258 0.0714  0.2738  0.1527  71  VAL   A CG1 
354  C  CG2 . VAL   A 51  ? 1.5015 1.6828 1.6698 0.0533  0.3020  0.1273  71  VAL   A CG2 
355  N  N   . TRP   A 52  ? 1.3593 1.5526 1.3397 0.1087  0.2079  0.1308  72  TRP   A N   
356  C  CA  . TRP   A 52  ? 1.3240 1.5137 1.2694 0.1272  0.1868  0.1422  72  TRP   A CA  
357  C  C   . TRP   A 52  ? 1.2005 1.3987 1.1938 0.1141  0.1582  0.1229  72  TRP   A C   
358  O  O   . TRP   A 52  ? 1.1449 1.3541 1.1832 0.0934  0.1490  0.0987  72  TRP   A O   
359  C  CB  . TRP   A 52  ? 1.4324 1.6462 1.3081 0.1485  0.1656  0.1363  72  TRP   A CB  
360  C  CG  . TRP   A 52  ? 1.3582 1.6086 1.2440 0.1373  0.1324  0.0998  72  TRP   A CG  
361  C  CD1 . TRP   A 52  ? 1.3349 1.6077 1.2343 0.1355  0.0984  0.0830  72  TRP   A CD1 
362  C  CD2 . TRP   A 52  ? 1.3905 1.6565 1.2738 0.1271  0.1331  0.0767  72  TRP   A CD2 
363  N  NE1 . TRP   A 52  ? 1.3322 1.6308 1.2385 0.1226  0.0794  0.0523  72  TRP   A NE1 
364  C  CE2 . TRP   A 52  ? 1.3287 1.6219 1.2237 0.1180  0.0986  0.0474  72  TRP   A CE2 
365  C  CE3 . TRP   A 52  ? 1.4842 1.7425 1.3586 0.1253  0.1622  0.0779  72  TRP   A CE3 
366  C  CZ2 . TRP   A 52  ? 1.3720 1.6796 1.2678 0.1072  0.0907  0.0201  72  TRP   A CZ2 
367  C  CZ3 . TRP   A 52  ? 1.4832 1.7592 1.3586 0.1167  0.1532  0.0492  72  TRP   A CZ3 
368  C  CH2 . TRP   A 52  ? 1.3694 1.6673 1.2542 0.1078  0.1169  0.0209  72  TRP   A CH2 
369  N  N   . GLY   A 53  ? 1.3086 1.4998 1.2881 0.1292  0.1449  0.1344  73  GLY   A N   
370  C  CA  . GLY   A 53  ? 1.2030 1.3984 1.2214 0.1209  0.1226  0.1188  73  GLY   A CA  
371  C  C   . GLY   A 53  ? 1.2510 1.4674 1.2426 0.1405  0.0962  0.1176  73  GLY   A C   
372  O  O   . GLY   A 53  ? 1.4106 1.6213 1.3605 0.1656  0.0978  0.1397  73  GLY   A O   
373  N  N   . PHE   A 54  ? 1.1628 1.4038 1.1790 0.1304  0.0725  0.0923  74  PHE   A N   
374  C  CA  . PHE   A 54  ? 1.1279 1.3964 1.1349 0.1456  0.0485  0.0870  74  PHE   A CA  
375  C  C   . PHE   A 54  ? 1.1138 1.3791 1.1625 0.1352  0.0410  0.0727  74  PHE   A C   
376  O  O   . PHE   A 54  ? 0.9834 1.2214 1.0605 0.1194  0.0516  0.0683  74  PHE   A O   
377  C  CB  . PHE   A 54  ? 1.1829 1.4938 1.1687 0.1450  0.0281  0.0679  74  PHE   A CB  
378  C  CG  . PHE   A 54  ? 1.1749 1.4955 1.1829 0.1185  0.0252  0.0420  74  PHE   A CG  
379  C  CD1 . PHE   A 54  ? 1.2131 1.5218 1.2129 0.1083  0.0402  0.0403  74  PHE   A CD1 
380  C  CD2 . PHE   A 54  ? 1.0856 1.4254 1.1218 0.1058  0.0097  0.0206  74  PHE   A CD2 
381  C  CE1 . PHE   A 54  ? 1.1639 1.4787 1.1833 0.0876  0.0363  0.0173  74  PHE   A CE1 
382  C  CE2 . PHE   A 54  ? 1.1243 1.4662 1.1751 0.0841  0.0077  -0.0002 74  PHE   A CE2 
383  C  CZ  . PHE   A 54  ? 1.1143 1.4434 1.1567 0.0758  0.0192  -0.0021 74  PHE   A CZ  
384  N  N   . TYR   A 55  ? 1.1243 1.4186 1.1771 0.1452  0.0225  0.0642  75  TYR   A N   
385  C  CA  . TYR   A 55  ? 1.0939 1.3855 1.1786 0.1405  0.0186  0.0522  75  TYR   A CA  
386  C  C   . TYR   A 55  ? 1.0781 1.4133 1.1743 0.1329  0.0018  0.0297  75  TYR   A C   
387  O  O   . TYR   A 55  ? 1.0904 1.4630 1.1798 0.1460  -0.0123 0.0289  75  TYR   A O   
388  C  CB  . TYR   A 55  ? 1.1867 1.4629 1.2731 0.1651  0.0210  0.0693  75  TYR   A CB  
389  C  CG  . TYR   A 55  ? 1.2754 1.5015 1.3540 0.1716  0.0406  0.0933  75  TYR   A CG  
390  C  CD1 . TYR   A 55  ? 1.2543 1.4717 1.2982 0.1889  0.0481  0.1185  75  TYR   A CD1 
391  C  CD2 . TYR   A 55  ? 1.2843 1.4691 1.3890 0.1606  0.0523  0.0903  75  TYR   A CD2 
392  C  CE1 . TYR   A 55  ? 1.2859 1.4534 1.3243 0.1933  0.0713  0.1432  75  TYR   A CE1 
393  C  CE2 . TYR   A 55  ? 1.3482 1.4860 1.4545 0.1632  0.0720  0.1111  75  TYR   A CE2 
394  C  CZ  . TYR   A 55  ? 1.3892 1.5177 1.4637 0.1787  0.0838  0.1391  75  TYR   A CZ  
395  O  OH  . TYR   A 55  ? 1.4112 1.4890 1.4881 0.1799  0.1087  0.1628  75  TYR   A OH  
396  N  N   . ASP   A 56  ? 1.1135 1.4429 1.2278 0.1122  0.0032  0.0116  76  ASP   A N   
397  C  CA  . ASP   A 56  ? 1.0954 1.4561 1.2257 0.1039  -0.0055 -0.0070 76  ASP   A CA  
398  C  C   . ASP   A 56  ? 1.1501 1.5047 1.2978 0.1152  -0.0009 -0.0064 76  ASP   A C   
399  O  O   . ASP   A 56  ? 1.1362 1.4597 1.2879 0.1077  0.0071  -0.0126 76  ASP   A O   
400  C  CB  . ASP   A 56  ? 1.1576 1.5080 1.2899 0.0794  -0.0039 -0.0236 76  ASP   A CB  
401  C  CG  . ASP   A 56  ? 1.1033 1.4645 1.2210 0.0699  -0.0086 -0.0282 76  ASP   A CG  
402  O  OD1 . ASP   A 56  ? 1.1334 1.5123 1.2354 0.0822  -0.0138 -0.0199 76  ASP   A OD1 
403  O  OD2 . ASP   A 56  ? 1.1024 1.4520 1.2204 0.0525  -0.0075 -0.0403 76  ASP   A OD2 
404  N  N   . GLY   A 57  ? 1.2373 1.6217 1.3939 0.1356  -0.0071 -0.0004 77  GLY   A N   
405  C  CA  . GLY   A 57  ? 1.2360 1.6131 1.4082 0.1527  -0.0009 0.0027  77  GLY   A CA  
406  C  C   . GLY   A 57  ? 1.2232 1.5510 1.3830 0.1662  0.0079  0.0200  77  GLY   A C   
407  O  O   . GLY   A 57  ? 1.1701 1.4923 1.3146 0.1819  0.0058  0.0390  77  GLY   A O   
408  N  N   . GLN   A 58  ? 1.0662 1.3547 1.2303 0.1606  0.0180  0.0132  78  GLN   A N   
409  C  CA  . GLN   A 58  ? 1.2627 1.4983 1.4218 0.1665  0.0267  0.0247  78  GLN   A CA  
410  C  C   . GLN   A 58  ? 1.2895 1.4948 1.4452 0.1428  0.0299  0.0199  78  GLN   A C   
411  O  O   . GLN   A 58  ? 1.1622 1.3234 1.3235 0.1414  0.0371  0.0244  78  GLN   A O   
412  C  CB  . GLN   A 58  ? 1.3291 1.5386 1.4975 0.1783  0.0330  0.0166  78  GLN   A CB  
413  C  CG  . GLN   A 58  ? 1.4971 1.7342 1.6763 0.2060  0.0325  0.0219  78  GLN   A CG  
414  C  CD  . GLN   A 58  ? 1.5925 1.8100 1.7666 0.2313  0.0336  0.0463  78  GLN   A CD  
415  O  OE1 . GLN   A 58  ? 1.7377 1.9142 1.9003 0.2264  0.0394  0.0602  78  GLN   A OE1 
416  N  NE2 . GLN   A 58  ? 1.5773 1.8234 1.7620 0.2595  0.0293  0.0526  78  GLN   A NE2 
417  N  N   . GLN   A 59  ? 1.1135 1.3421 1.2650 0.1242  0.0242  0.0099  79  GLN   A N   
418  C  CA  . GLN   A 59  ? 1.0909 1.2971 1.2447 0.1031  0.0249  0.0010  79  GLN   A CA  
419  C  C   . GLN   A 59  ? 1.0419 1.2497 1.1910 0.0988  0.0301  0.0151  79  GLN   A C   
420  O  O   . GLN   A 59  ? 0.9443 1.1842 1.0804 0.0970  0.0256  0.0155  79  GLN   A O   
421  C  CB  . GLN   A 59  ? 1.0667 1.2904 1.2166 0.0879  0.0175  -0.0185 79  GLN   A CB  
422  C  CG  . GLN   A 59  ? 1.0612 1.2712 1.2125 0.0693  0.0145  -0.0274 79  GLN   A CG  
423  C  CD  . GLN   A 59  ? 0.9628 1.1319 1.1266 0.0652  0.0139  -0.0339 79  GLN   A CD  
424  O  OE1 . GLN   A 59  ? 0.8969 1.0471 1.0553 0.0660  0.0086  -0.0479 79  GLN   A OE1 
425  N  NE2 . GLN   A 59  ? 0.9373 1.0921 1.1183 0.0609  0.0201  -0.0248 79  GLN   A NE2 
426  N  N   . PRO   A 60  ? 0.9265 1.0997 1.0863 0.0968  0.0411  0.0258  80  PRO   A N   
427  C  CA  . PRO   A 60  ? 1.0821 1.2557 1.2361 0.0936  0.0526  0.0414  80  PRO   A CA  
428  C  C   . PRO   A 60  ? 1.0319 1.2210 1.1907 0.0747  0.0492  0.0266  80  PRO   A C   
429  O  O   . PRO   A 60  ? 0.8341 1.0119 1.0136 0.0604  0.0433  0.0090  80  PRO   A O   
430  C  CB  . PRO   A 60  ? 1.1458 1.2750 1.3215 0.0922  0.0687  0.0539  80  PRO   A CB  
431  C  CG  . PRO   A 60  ? 1.0737 1.1808 1.2719 0.0852  0.0591  0.0334  80  PRO   A CG  
432  C  CD  . PRO   A 60  ? 0.9888 1.1194 1.1682 0.0966  0.0456  0.0231  80  PRO   A CD  
433  N  N   . VAL   A 61  ? 0.9829 1.1965 1.1196 0.0772  0.0514  0.0327  81  VAL   A N   
434  C  CA  . VAL   A 61  ? 1.0521 1.2777 1.1911 0.0627  0.0516  0.0208  81  VAL   A CA  
435  C  C   . VAL   A 61  ? 1.0966 1.3141 1.2293 0.0654  0.0728  0.0389  81  VAL   A C   
436  O  O   . VAL   A 61  ? 1.1220 1.3429 1.2228 0.0819  0.0801  0.0579  81  VAL   A O   
437  C  CB  . VAL   A 61  ? 0.9965 1.2560 1.1136 0.0621  0.0367  0.0073  81  VAL   A CB  
438  C  CG1 . VAL   A 61  ? 1.0295 1.2944 1.1491 0.0485  0.0375  -0.0060 81  VAL   A CG1 
439  C  CG2 . VAL   A 61  ? 0.9092 1.1760 1.0333 0.0597  0.0225  -0.0067 81  VAL   A CG2 
440  N  N   . LEU   A 62  ? 0.9724 1.1795 1.1350 0.0511  0.0835  0.0334  82  LEU   A N   
441  C  CA  . LEU   A 62  ? 1.0245 1.2265 1.1870 0.0513  0.1093  0.0488  82  LEU   A CA  
442  C  C   . LEU   A 62  ? 1.0995 1.3247 1.2530 0.0457  0.1075  0.0339  82  LEU   A C   
443  O  O   . LEU   A 62  ? 1.0526 1.2822 1.2366 0.0326  0.0975  0.0135  82  LEU   A O   
444  C  CB  . LEU   A 62  ? 1.0628 1.2391 1.2779 0.0386  0.1267  0.0531  82  LEU   A CB  
445  C  CG  . LEU   A 62  ? 1.1046 1.2770 1.3276 0.0368  0.1603  0.0700  82  LEU   A CG  
446  C  CD1 . LEU   A 62  ? 1.2654 1.4170 1.4494 0.0538  0.1837  0.1034  82  LEU   A CD1 
447  C  CD2 . LEU   A 62  ? 1.1327 1.2942 1.4274 0.0175  0.1721  0.0625  82  LEU   A CD2 
448  N  N   . ALA   A 63  ? 1.1212 1.3584 1.2298 0.0581  0.1159  0.0432  83  ALA   A N   
449  C  CA  . ALA   A 63  ? 1.1004 1.3550 1.1956 0.0553  0.1173  0.0288  83  ALA   A CA  
450  C  C   . ALA   A 63  ? 1.0531 1.2986 1.1647 0.0534  0.1507  0.0402  83  ALA   A C   
451  O  O   . ALA   A 63  ? 1.1271 1.3575 1.2205 0.0634  0.1760  0.0659  83  ALA   A O   
452  C  CB  . ALA   A 63  ? 1.1411 1.4136 1.1771 0.0702  0.1064  0.0277  83  ALA   A CB  
453  N  N   . ILE   A 64  ? 1.1263 1.3802 1.2737 0.0418  0.1524  0.0220  84  ILE   A N   
454  C  CA  . ILE   A 64  ? 1.1605 1.4135 1.3345 0.0391  0.1853  0.0285  84  ILE   A CA  
455  C  C   . ILE   A 64  ? 1.2146 1.4844 1.3635 0.0442  0.1866  0.0119  84  ILE   A C   
456  O  O   . ILE   A 64  ? 1.1141 1.3936 1.2518 0.0420  0.1587  -0.0103 84  ILE   A O   
457  C  CB  . ILE   A 64  ? 1.0833 1.3331 1.3384 0.0220  0.1874  0.0202  84  ILE   A CB  
458  C  CG1 . ILE   A 64  ? 1.1273 1.3902 1.4067 0.0146  0.1570  -0.0098 84  ILE   A CG1 
459  C  CG2 . ILE   A 64  ? 0.9451 1.1737 1.2224 0.0168  0.1825  0.0318  84  ILE   A CG2 
460  C  CD1 . ILE   A 64  ? 1.1663 1.4324 1.5248 0.0016  0.1555  -0.0224 84  ILE   A CD1 
461  N  N   . THR   A 65  ? 1.3010 1.5707 1.4390 0.0515  0.2219  0.0232  85  THR   A N   
462  C  CA  . THR   A 65  ? 1.3094 1.5915 1.4231 0.0586  0.2286  0.0068  85  THR   A CA  
463  C  C   . THR   A 65  ? 1.4244 1.7123 1.5884 0.0553  0.2655  0.0084  85  THR   A C   
464  O  O   . THR   A 65  ? 1.4450 1.7412 1.5889 0.0642  0.2795  -0.0029 85  THR   A O   
465  C  CB  . THR   A 65  ? 1.3324 1.6113 1.3575 0.0786  0.2341  0.0150  85  THR   A CB  
466  O  OG1 . THR   A 65  ? 1.3970 1.6602 1.3997 0.0890  0.2718  0.0469  85  THR   A OG1 
467  C  CG2 . THR   A 65  ? 1.2250 1.5064 1.2111 0.0820  0.1956  0.0103  85  THR   A CG2 
468  N  N   . ASP   A 66  ? 1.4806 1.7654 1.7133 0.0426  0.2819  0.0199  86  ASP   A N   
469  C  CA  . ASP   A 66  ? 1.4336 1.7290 1.7263 0.0380  0.3203  0.0222  86  ASP   A CA  
470  C  C   . ASP   A 66  ? 1.3447 1.6619 1.7041 0.0296  0.2986  -0.0082 86  ASP   A C   
471  O  O   . ASP   A 66  ? 1.3427 1.6599 1.7428 0.0183  0.2646  -0.0204 86  ASP   A O   
472  C  CB  . ASP   A 66  ? 1.4413 1.7242 1.7877 0.0258  0.3479  0.0463  86  ASP   A CB  
473  C  CG  . ASP   A 66  ? 1.5038 1.7969 1.9036 0.0223  0.4000  0.0559  86  ASP   A CG  
474  O  OD1 . ASP   A 66  ? 1.4265 1.7097 1.7712 0.0364  0.4409  0.0769  86  ASP   A OD1 
475  O  OD2 . ASP   A 66  ? 1.4617 1.7739 1.9590 0.0065  0.4002  0.0418  86  ASP   A OD2 
476  N  N   . PRO   A 67  ? 1.3599 1.6933 1.7273 0.0377  0.3162  -0.0213 87  PRO   A N   
477  C  CA  . PRO   A 67  ? 1.3294 1.6814 1.7569 0.0343  0.2926  -0.0500 87  PRO   A CA  
478  C  C   . PRO   A 67  ? 1.1943 1.5598 1.7244 0.0184  0.2861  -0.0546 87  PRO   A C   
479  O  O   . PRO   A 67  ? 1.2155 1.5862 1.7790 0.0150  0.2467  -0.0759 87  PRO   A O   
480  C  CB  . PRO   A 67  ? 1.1701 1.5360 1.5925 0.0483  0.3263  -0.0572 87  PRO   A CB  
481  C  CG  . PRO   A 67  ? 1.1897 1.5380 1.5124 0.0620  0.3458  -0.0420 87  PRO   A CG  
482  C  CD  . PRO   A 67  ? 1.3834 1.7150 1.6907 0.0548  0.3535  -0.0128 87  PRO   A CD  
483  N  N   . ASP   A 68  ? 1.1105 1.4794 1.6907 0.0089  0.3234  -0.0356 88  ASP   A N   
484  C  CA  . ASP   A 68  ? 1.1235 1.5055 1.8074 -0.0087 0.3145  -0.0432 88  ASP   A CA  
485  C  C   . ASP   A 68  ? 1.1115 1.4709 1.7842 -0.0185 0.2756  -0.0429 88  ASP   A C   
486  O  O   . ASP   A 68  ? 0.8775 1.2440 1.6038 -0.0262 0.2389  -0.0637 88  ASP   A O   
487  C  CB  . ASP   A 68  ? 1.1272 1.5171 1.8734 -0.0189 0.3697  -0.0229 88  ASP   A CB  
488  C  CG  . ASP   A 68  ? 1.1842 1.6066 1.9789 -0.0119 0.4061  -0.0306 88  ASP   A CG  
489  O  OD1 . ASP   A 68  ? 1.1493 1.5981 1.9916 -0.0074 0.3796  -0.0589 88  ASP   A OD1 
490  O  OD2 . ASP   A 68  ? 1.2826 1.7023 2.0653 -0.0088 0.4627  -0.0077 88  ASP   A OD2 
491  N  N   . MET   A 69  ? 1.1702 1.5018 1.7710 -0.0158 0.2826  -0.0202 89  MET   A N   
492  C  CA  . MET   A 69  ? 1.1765 1.4860 1.7572 -0.0213 0.2473  -0.0205 89  MET   A CA  
493  C  C   . MET   A 69  ? 1.0790 1.3906 1.6289 -0.0154 0.1988  -0.0447 89  MET   A C   
494  O  O   . MET   A 69  ? 0.9998 1.3043 1.5734 -0.0221 0.1646  -0.0583 89  MET   A O   
495  C  CB  . MET   A 69  ? 1.3502 1.6334 1.8541 -0.0137 0.2639  0.0081  89  MET   A CB  
496  C  CG  . MET   A 69  ? 1.4535 1.7110 1.9802 -0.0240 0.2658  0.0232  89  MET   A CG  
497  S  SD  . MET   A 69  ? 1.5971 1.8232 2.0353 -0.0094 0.2903  0.0608  89  MET   A SD  
498  C  CE  . MET   A 69  ? 1.6136 1.8377 2.0684 -0.0089 0.3560  0.0879  89  MET   A CE  
499  N  N   . ILE   A 70  ? 1.0828 1.4005 1.5778 -0.0026 0.1966  -0.0508 90  ILE   A N   
500  C  CA  . ILE   A 70  ? 1.1232 1.4387 1.5900 0.0021  0.1563  -0.0720 90  ILE   A CA  
501  C  C   . ILE   A 70  ? 1.0647 1.3938 1.6005 -0.0005 0.1352  -0.0948 90  ILE   A C   
502  O  O   . ILE   A 70  ? 0.8681 1.1873 1.4020 -0.0011 0.0976  -0.1088 90  ILE   A O   
503  C  CB  . ILE   A 70  ? 1.3150 1.6314 1.7139 0.0146  0.1621  -0.0746 90  ILE   A CB  
504  C  CG1 . ILE   A 70  ? 1.1431 1.4466 1.4693 0.0190  0.1673  -0.0567 90  ILE   A CG1 
505  C  CG2 . ILE   A 70  ? 1.1289 1.4414 1.5130 0.0182  0.1276  -0.0974 90  ILE   A CG2 
506  C  CD1 . ILE   A 70  ? 1.1900 1.4963 1.4539 0.0317  0.1813  -0.0572 90  ILE   A CD1 
507  N  N   . LYS   A 71  ? 1.0737 1.4262 1.6708 0.0001  0.1594  -0.0989 91  LYS   A N   
508  C  CA  . LYS   A 71  ? 0.9397 1.3110 1.6147 -0.0006 0.1377  -0.1212 91  LYS   A CA  
509  C  C   . LYS   A 71  ? 0.8346 1.2021 1.5639 -0.0140 0.1159  -0.1257 91  LYS   A C   
510  O  O   . LYS   A 71  ? 0.7977 1.1662 1.5537 -0.0118 0.0760  -0.1463 91  LYS   A O   
511  C  CB  . LYS   A 71  ? 1.0656 1.4683 1.8055 0.0025  0.1734  -0.1236 91  LYS   A CB  
512  C  CG  . LYS   A 71  ? 1.0089 1.4387 1.8368 0.0056  0.1505  -0.1485 91  LYS   A CG  
513  C  CD  . LYS   A 71  ? 1.1765 1.6422 2.0765 0.0082  0.1928  -0.1494 91  LYS   A CD  
514  C  CE  . LYS   A 71  ? 1.2420 1.7415 2.2399 0.0135  0.1679  -0.1757 91  LYS   A CE  
515  N  NZ  . LYS   A 71  ? 1.2077 1.7490 2.2973 0.0123  0.2134  -0.1762 91  LYS   A NZ  
516  N  N   . THR   A 72  ? 0.8434 1.2026 1.5853 -0.0265 0.1409  -0.1070 92  THR   A N   
517  C  CA  . THR   A 72  ? 1.0254 1.3747 1.8144 -0.0400 0.1211  -0.1125 92  THR   A CA  
518  C  C   . THR   A 72  ? 1.0867 1.4087 1.8140 -0.0353 0.0782  -0.1205 92  THR   A C   
519  O  O   . THR   A 72  ? 1.0702 1.3896 1.8274 -0.0364 0.0405  -0.1416 92  THR   A O   
520  C  CB  . THR   A 72  ? 0.9555 1.2915 1.7571 -0.0526 0.1603  -0.0872 92  THR   A CB  
521  O  OG1 . THR   A 72  ? 1.0160 1.3749 1.8693 -0.0565 0.2071  -0.0768 92  THR   A OG1 
522  C  CG2 . THR   A 72  ? 0.7584 1.0814 1.6174 -0.0681 0.1410  -0.0964 92  THR   A CG2 
523  N  N   . VAL   A 73  ? 0.9997 1.3023 1.6404 -0.0286 0.0834  -0.1049 93  VAL   A N   
524  C  CA  . VAL   A 73  ? 1.0800 1.3576 1.6645 -0.0252 0.0514  -0.1090 93  VAL   A CA  
525  C  C   . VAL   A 73  ? 1.0077 1.2847 1.5769 -0.0159 0.0149  -0.1305 93  VAL   A C   
526  O  O   . VAL   A 73  ? 0.8618 1.1258 1.4377 -0.0153 -0.0179 -0.1455 93  VAL   A O   
527  C  CB  . VAL   A 73  ? 1.2436 1.5085 1.7492 -0.0196 0.0665  -0.0885 93  VAL   A CB  
528  C  CG1 . VAL   A 73  ? 1.0828 1.3296 1.5323 -0.0144 0.0359  -0.0955 93  VAL   A CG1 
529  C  CG2 . VAL   A 73  ? 0.9460 1.1996 1.4580 -0.0254 0.0935  -0.0664 93  VAL   A CG2 
530  N  N   . LEU   A 74  ? 0.9504 1.2373 1.4949 -0.0070 0.0205  -0.1324 94  LEU   A N   
531  C  CA  . LEU   A 74  ? 0.9176 1.1940 1.4307 0.0034  -0.0103 -0.1475 94  LEU   A CA  
532  C  C   . LEU   A 74  ? 1.0259 1.3138 1.5993 0.0092  -0.0350 -0.1682 94  LEU   A C   
533  O  O   . LEU   A 74  ? 1.0246 1.2952 1.5718 0.0192  -0.0675 -0.1801 94  LEU   A O   
534  C  CB  . LEU   A 74  ? 1.0993 1.3771 1.5655 0.0107  0.0039  -0.1438 94  LEU   A CB  
535  C  CG  . LEU   A 74  ? 1.2372 1.5080 1.6418 0.0078  0.0224  -0.1273 94  LEU   A CG  
536  C  CD1 . LEU   A 74  ? 1.1730 1.4471 1.5407 0.0145  0.0342  -0.1297 94  LEU   A CD1 
537  C  CD2 . LEU   A 74  ? 1.1195 1.3682 1.4787 0.0056  0.0017  -0.1252 94  LEU   A CD2 
538  N  N   . VAL   A 75  ? 0.8578 1.1743 1.5118 0.0043  -0.0201 -0.1724 95  VAL   A N   
539  C  CA  . VAL   A 75  ? 1.0852 1.4220 1.8059 0.0123  -0.0433 -0.1939 95  VAL   A CA  
540  C  C   . VAL   A 75  ? 1.0667 1.4197 1.8727 0.0004  -0.0533 -0.2049 95  VAL   A C   
541  O  O   . VAL   A 75  ? 1.1461 1.4933 1.9697 0.0054  -0.0955 -0.2245 95  VAL   A O   
542  C  CB  . VAL   A 75  ? 1.1438 1.5085 1.8973 0.0200  -0.0167 -0.1949 95  VAL   A CB  
543  C  CG1 . VAL   A 75  ? 0.5753 0.9597 1.3894 0.0341  -0.0466 -0.2182 95  VAL   A CG1 
544  C  CG2 . VAL   A 75  ? 1.0779 1.4241 1.7469 0.0283  -0.0021 -0.1847 95  VAL   A CG2 
545  N  N   . LYS   A 76  ? 1.0670 1.4378 1.9249 -0.0149 -0.0145 -0.1929 96  LYS   A N   
546  C  CA  . LYS   A 76  ? 1.0084 1.3986 1.9662 -0.0295 -0.0181 -0.2049 96  LYS   A CA  
547  C  C   . LYS   A 76  ? 1.0507 1.4110 1.9914 -0.0368 -0.0494 -0.2125 96  LYS   A C   
548  O  O   . LYS   A 76  ? 1.0696 1.4370 2.0648 -0.0378 -0.0871 -0.2379 96  LYS   A O   
549  C  CB  . LYS   A 76  ? 1.0427 1.4498 2.0500 -0.0453 0.0381  -0.1851 96  LYS   A CB  
550  C  CG  . LYS   A 76  ? 1.1517 1.5933 2.1942 -0.0377 0.0706  -0.1829 96  LYS   A CG  
551  C  CD  . LYS   A 76  ? 1.2035 1.6526 2.2691 -0.0501 0.1327  -0.1576 96  LYS   A CD  
552  C  CE  . LYS   A 76  ? 1.3310 1.8152 2.4336 -0.0407 0.1675  -0.1580 96  LYS   A CE  
553  N  NZ  . LYS   A 76  ? 1.5083 1.9936 2.6136 -0.0490 0.2328  -0.1299 96  LYS   A NZ  
554  N  N   . GLU   A 77  ? 1.1859 1.5132 2.0505 -0.0400 -0.0362 -0.1927 97  GLU   A N   
555  C  CA  . GLU   A 77  ? 1.1529 1.4487 1.9960 -0.0453 -0.0597 -0.1984 97  GLU   A CA  
556  C  C   . GLU   A 77  ? 1.0936 1.3592 1.8379 -0.0297 -0.0884 -0.2002 97  GLU   A C   
557  O  O   . GLU   A 77  ? 1.0306 1.2665 1.7259 -0.0312 -0.0907 -0.1935 97  GLU   A O   
558  C  CB  . GLU   A 77  ? 1.0300 1.3094 1.8714 -0.0597 -0.0217 -0.1748 97  GLU   A CB  
559  C  CG  . GLU   A 77  ? 1.1012 1.4048 2.0318 -0.0758 0.0179  -0.1661 97  GLU   A CG  
560  C  CD  . GLU   A 77  ? 1.1879 1.5143 2.2289 -0.0875 -0.0042 -0.1948 97  GLU   A CD  
561  O  OE1 . GLU   A 77  ? 1.0786 1.3865 2.1287 -0.0903 -0.0426 -0.2161 97  GLU   A OE1 
562  O  OE2 . GLU   A 77  ? 1.0666 1.4309 2.1870 -0.0931 0.0163  -0.1977 97  GLU   A OE2 
563  N  N   . CYS   A 78  ? 1.1652 1.4364 1.8816 -0.0142 -0.1082 -0.2087 98  CYS   A N   
564  C  CA  . CYS   A 78  ? 0.9702 1.2104 1.5946 -0.0005 -0.1302 -0.2082 98  CYS   A CA  
565  C  C   . CYS   A 78  ? 0.9941 1.2100 1.6073 0.0050  -0.1718 -0.2284 98  CYS   A C   
566  O  O   . CYS   A 78  ? 1.0383 1.2248 1.5969 0.0047  -0.1736 -0.2234 98  CYS   A O   
567  C  CB  . CYS   A 78  ? 0.8756 1.1218 1.4757 0.0146  -0.1380 -0.2109 98  CYS   A CB  
568  S  SG  . CYS   A 78  ? 0.9524 1.1563 1.4471 0.0307  -0.1636 -0.2103 98  CYS   A SG  
569  N  N   . TYR   A 79  ? 1.1004 1.3291 1.7649 0.0120  -0.2065 -0.2531 99  TYR   A N   
570  C  CA  . TYR   A 79  ? 1.1361 1.3398 1.7811 0.0214  -0.2517 -0.2759 99  TYR   A CA  
571  C  C   . TYR   A 79  ? 1.0712 1.2605 1.7368 0.0064  -0.2492 -0.2812 99  TYR   A C   
572  O  O   . TYR   A 79  ? 1.1540 1.3096 1.7686 0.0145  -0.2754 -0.2931 99  TYR   A O   
573  C  CB  . TYR   A 79  ? 1.1776 1.4048 1.8874 0.0320  -0.2920 -0.3037 99  TYR   A CB  
574  C  CG  . TYR   A 79  ? 1.3757 1.6005 2.0453 0.0556  -0.3103 -0.3039 99  TYR   A CG  
575  C  CD1 . TYR   A 79  ? 1.4349 1.6180 2.0117 0.0768  -0.3409 -0.3069 99  TYR   A CD1 
576  C  CD2 . TYR   A 79  ? 1.3862 1.6466 2.1093 0.0581  -0.2951 -0.3007 99  TYR   A CD2 
577  C  CE1 . TYR   A 79  ? 1.5105 1.6839 2.0483 0.0992  -0.3560 -0.3047 99  TYR   A CE1 
578  C  CE2 . TYR   A 79  ? 1.4314 1.6844 2.1185 0.0813  -0.3119 -0.3011 99  TYR   A CE2 
579  C  CZ  . TYR   A 79  ? 1.6217 1.8293 2.2159 0.1014  -0.3427 -0.3022 99  TYR   A CZ  
580  O  OH  . TYR   A 79  ? 1.8081 2.0004 2.3626 0.1253  -0.3578 -0.3001 99  TYR   A OH  
581  N  N   . SER   A 80  ? 0.9837 1.1935 1.7196 -0.0142 -0.2161 -0.2720 100 SER   A N   
582  C  CA  . SER   A 80  ? 1.0609 1.2550 1.8314 -0.0297 -0.2132 -0.2784 100 SER   A CA  
583  C  C   . SER   A 80  ? 1.1983 1.3609 1.8994 -0.0320 -0.1842 -0.2539 100 SER   A C   
584  O  O   . SER   A 80  ? 1.1601 1.2890 1.8244 -0.0285 -0.2008 -0.2638 100 SER   A O   
585  C  CB  . SER   A 80  ? 0.9653 1.1925 1.8506 -0.0513 -0.1890 -0.2790 100 SER   A CB  
586  O  OG  . SER   A 80  ? 1.0804 1.3303 1.9704 -0.0553 -0.1429 -0.2507 100 SER   A OG  
587  N  N   . VAL   A 81  ? 1.1035 1.2768 1.7850 -0.0355 -0.1423 -0.2237 101 VAL   A N   
588  C  CA  . VAL   A 81  ? 1.1039 1.2551 1.7385 -0.0380 -0.1130 -0.1997 101 VAL   A CA  
589  C  C   . VAL   A 81  ? 1.0699 1.2178 1.6178 -0.0251 -0.1032 -0.1816 101 VAL   A C   
590  O  O   . VAL   A 81  ? 1.0895 1.2142 1.5803 -0.0193 -0.0999 -0.1732 101 VAL   A O   
591  C  CB  . VAL   A 81  ? 1.0701 1.2329 1.7600 -0.0540 -0.0703 -0.1785 101 VAL   A CB  
592  C  CG1 . VAL   A 81  ? 1.1334 1.2700 1.7733 -0.0524 -0.0447 -0.1537 101 VAL   A CG1 
593  C  CG2 . VAL   A 81  ? 1.0875 1.2546 1.8753 -0.0708 -0.0768 -0.1972 101 VAL   A CG2 
594  N  N   . PHE   A 82  ? 1.1265 1.2976 1.6675 -0.0205 -0.0979 -0.1767 102 PHE   A N   
595  C  CA  . PHE   A 82  ? 0.8992 1.0685 1.3681 -0.0121 -0.0860 -0.1606 102 PHE   A CA  
596  C  C   . PHE   A 82  ? 0.8743 1.0345 1.3001 0.0007  -0.1142 -0.1737 102 PHE   A C   
597  O  O   . PHE   A 82  ? 1.0050 1.1775 1.4186 0.0050  -0.1097 -0.1703 102 PHE   A O   
598  C  CB  . PHE   A 82  ? 0.9618 1.1573 1.4443 -0.0161 -0.0532 -0.1429 102 PHE   A CB  
599  C  CG  . PHE   A 82  ? 1.0608 1.2617 1.5847 -0.0269 -0.0223 -0.1273 102 PHE   A CG  
600  C  CD1 . PHE   A 82  ? 1.0227 1.2063 1.5138 -0.0269 -0.0065 -0.1095 102 PHE   A CD1 
601  C  CD2 . PHE   A 82  ? 1.0584 1.2803 1.6557 -0.0359 -0.0072 -0.1293 102 PHE   A CD2 
602  C  CE1 . PHE   A 82  ? 1.0550 1.2359 1.5780 -0.0346 0.0233  -0.0919 102 PHE   A CE1 
603  C  CE2 . PHE   A 82  ? 1.0744 1.2954 1.7073 -0.0463 0.0264  -0.1117 102 PHE   A CE2 
604  C  CZ  . PHE   A 82  ? 1.0454 1.2427 1.6373 -0.0452 0.0414  -0.0919 102 PHE   A CZ  
605  N  N   . THR   A 83  ? 1.0135 1.1470 1.4111 0.0082  -0.1421 -0.1882 103 THR   A N   
606  C  CA  . THR   A 83  ? 1.0332 1.1504 1.3847 0.0228  -0.1691 -0.1991 103 THR   A CA  
607  C  C   . THR   A 83  ? 0.8477 0.9487 1.1224 0.0280  -0.1558 -0.1840 103 THR   A C   
608  O  O   . THR   A 83  ? 0.8874 0.9812 1.1293 0.0361  -0.1625 -0.1834 103 THR   A O   
609  C  CB  . THR   A 83  ? 0.9247 1.0168 1.2696 0.0315  -0.2054 -0.2221 103 THR   A CB  
610  O  OG1 . THR   A 83  ? 1.0139 1.1242 1.4421 0.0233  -0.2187 -0.2391 103 THR   A OG1 
611  C  CG2 . THR   A 83  ? 1.1079 1.1799 1.4027 0.0504  -0.2349 -0.2319 103 THR   A CG2 
612  N  N   . ASN   A 84  ? 1.0328 1.1282 1.2831 0.0236  -0.1364 -0.1718 104 ASN   A N   
613  C  CA  . ASN   A 84  ? 0.9415 1.0207 1.1256 0.0288  -0.1278 -0.1623 104 ASN   A CA  
614  C  C   . ASN   A 84  ? 0.9670 1.0684 1.1483 0.0206  -0.0978 -0.1431 104 ASN   A C   
615  O  O   . ASN   A 84  ? 0.9643 1.0844 1.1818 0.0138  -0.0829 -0.1351 104 ASN   A O   
616  C  CB  . ASN   A 84  ? 0.9851 1.0357 1.1361 0.0364  -0.1367 -0.1696 104 ASN   A CB  
617  C  CG  . ASN   A 84  ? 1.0669 1.0959 1.2229 0.0454  -0.1709 -0.1926 104 ASN   A CG  
618  O  OD1 . ASN   A 84  ? 1.0276 1.0515 1.1768 0.0532  -0.1917 -0.2012 104 ASN   A OD1 
619  N  ND2 . ASN   A 84  ? 1.1308 1.1456 1.2991 0.0459  -0.1791 -0.2042 104 ASN   A ND2 
620  N  N   . ARG   A 85  ? 1.0096 1.1072 1.1469 0.0219  -0.0895 -0.1360 105 ARG   A N   
621  C  CA  . ARG   A 85  ? 0.8361 0.9559 0.9674 0.0155  -0.0669 -0.1219 105 ARG   A CA  
622  C  C   . ARG   A 85  ? 1.2072 1.3241 1.3224 0.0186  -0.0577 -0.1159 105 ARG   A C   
623  O  O   . ARG   A 85  ? 1.0512 1.1456 1.1565 0.0255  -0.0665 -0.1231 105 ARG   A O   
624  C  CB  . ARG   A 85  ? 1.0557 1.1745 1.1582 0.0129  -0.0629 -0.1202 105 ARG   A CB  
625  C  CG  . ARG   A 85  ? 1.1144 1.2325 1.2305 0.0131  -0.0715 -0.1267 105 ARG   A CG  
626  C  CD  . ARG   A 85  ? 1.1403 1.2573 1.2335 0.0083  -0.0634 -0.1245 105 ARG   A CD  
627  N  NE  . ARG   A 85  ? 1.3650 1.4854 1.4769 0.0097  -0.0678 -0.1306 105 ARG   A NE  
628  C  CZ  . ARG   A 85  ? 1.2240 1.3205 1.3283 0.0183  -0.0834 -0.1379 105 ARG   A CZ  
629  N  NH1 . ARG   A 85  ? 1.3132 1.3774 1.3843 0.0267  -0.0969 -0.1392 105 ARG   A NH1 
630  N  NH2 . ARG   A 85  ? 1.1294 1.2333 1.2569 0.0214  -0.0852 -0.1439 105 ARG   A NH2 
631  N  N   . ARG   A 86  ? 1.1277 1.2682 1.2406 0.0154  -0.0412 -0.1045 106 ARG   A N   
632  C  CA  . ARG   A 86  ? 1.1711 1.3149 1.2750 0.0207  -0.0317 -0.0984 106 ARG   A CA  
633  C  C   . ARG   A 86  ? 1.2519 1.3736 1.3195 0.0256  -0.0324 -0.1042 106 ARG   A C   
634  O  O   . ARG   A 86  ? 1.0963 1.2120 1.1421 0.0215  -0.0317 -0.1058 106 ARG   A O   
635  C  CB  . ARG   A 86  ? 1.2272 1.4054 1.3367 0.0181  -0.0186 -0.0873 106 ARG   A CB  
636  C  CG  . ARG   A 86  ? 1.3451 1.5335 1.4569 0.0271  -0.0100 -0.0795 106 ARG   A CG  
637  C  CD  . ARG   A 86  ? 1.3277 1.5539 1.4460 0.0270  -0.0033 -0.0707 106 ARG   A CD  
638  N  NE  . ARG   A 86  ? 1.1725 1.4111 1.2989 0.0230  -0.0041 -0.0664 106 ARG   A NE  
639  C  CZ  . ARG   A 86  ? 1.1255 1.3918 1.2530 0.0272  -0.0012 -0.0580 106 ARG   A CZ  
640  N  NH1 . ARG   A 86  ? 1.2418 1.5302 1.3700 0.0358  -0.0002 -0.0531 106 ARG   A NH1 
641  N  NH2 . ARG   A 86  ? 1.1920 1.4644 1.3186 0.0249  0.0003  -0.0552 106 ARG   A NH2 
642  N  N   . PRO   A 87  ? 1.3535 1.4580 1.4107 0.0353  -0.0319 -0.1073 107 PRO   A N   
643  C  CA  . PRO   A 87  ? 1.4224 1.5044 1.4383 0.0424  -0.0273 -0.1117 107 PRO   A CA  
644  C  C   . PRO   A 87  ? 1.5812 1.6869 1.5913 0.0367  -0.0078 -0.1029 107 PRO   A C   
645  O  O   . PRO   A 87  ? 1.5966 1.7368 1.6329 0.0347  0.0023  -0.0954 107 PRO   A O   
646  C  CB  . PRO   A 87  ? 1.3538 1.4204 1.3674 0.0547  -0.0263 -0.1164 107 PRO   A CB  
647  C  CG  . PRO   A 87  ? 1.4088 1.4957 1.4660 0.0524  -0.0251 -0.1091 107 PRO   A CG  
648  C  CD  . PRO   A 87  ? 1.3093 1.4088 1.3899 0.0408  -0.0335 -0.1072 107 PRO   A CD  
649  N  N   . PHE   A 88  ? 1.6577 1.7440 1.6346 0.0343  -0.0032 -0.1040 108 PHE   A N   
650  C  CA  . PHE   A 88  ? 1.8042 1.9094 1.7818 0.0242  0.0161  -0.0974 108 PHE   A CA  
651  C  C   . PHE   A 88  ? 1.9758 2.0576 1.9161 0.0315  0.0345  -0.0962 108 PHE   A C   
652  O  O   . PHE   A 88  ? 2.0085 2.0463 1.9017 0.0394  0.0300  -0.0991 108 PHE   A O   
653  C  CB  . PHE   A 88  ? 1.8361 1.9345 1.8100 0.0122  0.0107  -0.0973 108 PHE   A CB  
654  C  CG  . PHE   A 88  ? 1.8660 1.9867 1.8532 -0.0027 0.0282  -0.0931 108 PHE   A CG  
655  C  CD1 . PHE   A 88  ? 1.8857 2.0544 1.9145 -0.0104 0.0308  -0.0927 108 PHE   A CD1 
656  C  CD2 . PHE   A 88  ? 1.8645 1.9561 1.8227 -0.0088 0.0412  -0.0901 108 PHE   A CD2 
657  C  CE1 . PHE   A 88  ? 1.9074 2.0997 1.9555 -0.0256 0.0430  -0.0932 108 PHE   A CE1 
658  C  CE2 . PHE   A 88  ? 1.8689 1.9800 1.8480 -0.0261 0.0583  -0.0880 108 PHE   A CE2 
659  C  CZ  . PHE   A 88  ? 1.8950 2.0590 1.9227 -0.0354 0.0576  -0.0917 108 PHE   A CZ  
660  N  N   . GLY   A 89  ? 2.3747 2.4862 2.3349 0.0309  0.0554  -0.0920 109 GLY   A N   
661  C  CA  . GLY   A 89  ? 2.4115 2.5060 2.3417 0.0383  0.0796  -0.0902 109 GLY   A CA  
662  C  C   . GLY   A 89  ? 2.3567 2.4970 2.3271 0.0299  0.1049  -0.0852 109 GLY   A C   
663  O  O   . GLY   A 89  ? 2.3834 2.5711 2.4043 0.0230  0.0987  -0.0849 109 GLY   A O   
664  N  N   . PRO   A 90  ? 2.1361 2.2638 2.0852 0.0314  0.1345  -0.0814 110 PRO   A N   
665  C  CA  . PRO   A 90  ? 2.1866 2.2552 2.0649 0.0430  0.1457  -0.0800 110 PRO   A CA  
666  C  C   . PRO   A 90  ? 2.2133 2.2447 2.0570 0.0317  0.1428  -0.0743 110 PRO   A C   
667  O  O   . PRO   A 90  ? 2.0904 2.1407 1.9642 0.0114  0.1547  -0.0688 110 PRO   A O   
668  C  CB  . PRO   A 90  ? 2.1080 2.1900 1.9903 0.0466  0.1860  -0.0754 110 PRO   A CB  
669  C  CG  . PRO   A 90  ? 2.0167 2.1598 1.9737 0.0248  0.1970  -0.0725 110 PRO   A CG  
670  C  CD  . PRO   A 90  ? 2.0956 2.2718 2.0937 0.0217  0.1615  -0.0782 110 PRO   A CD  
671  N  N   . VAL   A 91  ? 2.1452 2.1220 1.9265 0.0459  0.1253  -0.0768 111 VAL   A N   
672  C  CA  . VAL   A 91  ? 2.0877 2.0241 1.8319 0.0410  0.1179  -0.0711 111 VAL   A CA  
673  C  C   . VAL   A 91  ? 2.2125 2.0879 1.8741 0.0560  0.1372  -0.0630 111 VAL   A C   
674  O  O   . VAL   A 91  ? 2.2776 2.1231 1.9128 0.0480  0.1539  -0.0504 111 VAL   A O   
675  C  CB  . VAL   A 91  ? 2.0718 1.9983 1.8168 0.0466  0.0754  -0.0808 111 VAL   A CB  
676  C  CG1 . VAL   A 91  ? 1.9761 1.9497 1.7887 0.0277  0.0645  -0.0826 111 VAL   A CG1 
677  C  CG2 . VAL   A 91  ? 2.1961 2.1181 1.9325 0.0650  0.0546  -0.0937 111 VAL   A CG2 
678  N  N   . GLY   A 92  ? 2.5271 2.3784 2.1424 0.0789  0.1358  -0.0699 112 GLY   A N   
679  C  CA  . GLY   A 92  ? 2.5205 2.3087 2.0436 0.0982  0.1516  -0.0634 112 GLY   A CA  
680  C  C   . GLY   A 92  ? 2.4760 2.2116 1.9384 0.1139  0.1144  -0.0672 112 GLY   A C   
681  O  O   . GLY   A 92  ? 2.4723 2.2155 1.9515 0.1209  0.0728  -0.0837 112 GLY   A O   
682  N  N   . PHE   A 93  ? 2.3258 2.0075 1.7200 0.1202  0.1295  -0.0516 113 PHE   A N   
683  C  CA  . PHE   A 93  ? 2.3468 1.9787 1.6836 0.1380  0.0920  -0.0537 113 PHE   A CA  
684  C  C   . PHE   A 93  ? 2.3326 1.9951 1.7360 0.1226  0.0596  -0.0592 113 PHE   A C   
685  O  O   . PHE   A 93  ? 2.3529 1.9941 1.7360 0.1380  0.0181  -0.0689 113 PHE   A O   
686  C  CB  . PHE   A 93  ? 2.5023 2.0674 1.7527 0.1478  0.1193  -0.0310 113 PHE   A CB  
687  C  CG  . PHE   A 93  ? 2.6311 2.2030 1.9219 0.1206  0.1465  -0.0121 113 PHE   A CG  
688  C  CD1 . PHE   A 93  ? 2.6613 2.2658 2.0002 0.0955  0.1953  -0.0015 113 PHE   A CD1 
689  C  CD2 . PHE   A 93  ? 2.5756 2.1220 1.8608 0.1204  0.1222  -0.0072 113 PHE   A CD2 
690  C  CE1 . PHE   A 93  ? 2.7103 2.3205 2.0914 0.0683  0.2180  0.0119  113 PHE   A CE1 
691  C  CE2 . PHE   A 93  ? 2.5802 2.1278 1.9023 0.0951  0.1466  0.0074  113 PHE   A CE2 
692  C  CZ  . PHE   A 93  ? 2.7067 2.2854 2.0768 0.0678  0.1940  0.0161  113 PHE   A CZ  
693  N  N   . MET   A 94  ? 2.2846 1.9980 1.7679 0.0940  0.0768  -0.0549 114 MET   A N   
694  C  CA  . MET   A 94  ? 2.2442 1.9878 1.7888 0.0798  0.0509  -0.0607 114 MET   A CA  
695  C  C   . MET   A 94  ? 2.1668 1.9444 1.7542 0.0853  0.0129  -0.0806 114 MET   A C   
696  O  O   . MET   A 94  ? 2.0630 1.8642 1.6980 0.0767  -0.0086 -0.0862 114 MET   A O   
697  C  CB  . MET   A 94  ? 2.2118 2.0014 1.8255 0.0496  0.0780  -0.0543 114 MET   A CB  
698  C  CG  . MET   A 94  ? 2.2188 1.9753 1.8083 0.0375  0.1129  -0.0361 114 MET   A CG  
699  S  SD  . MET   A 94  ? 2.0364 1.7353 1.5855 0.0450  0.0921  -0.0292 114 MET   A SD  
700  C  CE  . MET   A 94  ? 1.8647 1.6216 1.5013 0.0290  0.0619  -0.0459 114 MET   A CE  
701  N  N   . LYS   A 95  ? 2.3524 2.1309 1.9254 0.0988  0.0069  -0.0914 115 LYS   A N   
702  C  CA  . LYS   A 95  ? 2.3185 2.1175 1.9272 0.1046  -0.0293 -0.1104 115 LYS   A CA  
703  C  C   . LYS   A 95  ? 2.1506 1.9221 1.7395 0.1184  -0.0695 -0.1197 115 LYS   A C   
704  O  O   . LYS   A 95  ? 2.1656 1.9629 1.8060 0.1162  -0.0983 -0.1339 115 LYS   A O   
705  C  CB  . LYS   A 95  ? 2.3767 2.1663 1.9604 0.1196  -0.0291 -0.1221 115 LYS   A CB  
706  C  CG  . LYS   A 95  ? 2.4319 2.1618 1.9284 0.1472  -0.0484 -0.1308 115 LYS   A CG  
707  C  CD  . LYS   A 95  ? 2.4934 2.2102 1.9615 0.1630  -0.0480 -0.1458 115 LYS   A CD  
708  C  CE  . LYS   A 95  ? 2.5500 2.2074 1.9293 0.1923  -0.0766 -0.1595 115 LYS   A CE  
709  N  NZ  . LYS   A 95  ? 2.4474 2.0600 1.7513 0.2027  -0.0647 -0.1406 115 LYS   A NZ  
710  N  N   . SER   A 96  ? 2.1247 1.8445 1.6419 0.1336  -0.0710 -0.1112 116 SER   A N   
711  C  CA  A SER   A 96  ? 2.1080 1.7991 1.6006 0.1518  -0.1112 -0.1192 116 SER   A CA  
712  C  CA  B SER   A 96  ? 2.1016 1.7934 1.5954 0.1517  -0.1115 -0.1195 116 SER   A CA  
713  C  C   . SER   A 96  ? 1.9678 1.6710 1.5001 0.1402  -0.1142 -0.1111 116 SER   A C   
714  O  O   . SER   A 96  ? 1.9199 1.6060 1.4442 0.1557  -0.1479 -0.1178 116 SER   A O   
715  C  CB  A SER   A 96  ? 2.2152 1.8373 1.5993 0.1798  -0.1134 -0.1127 116 SER   A CB  
716  C  CB  B SER   A 96  ? 2.2076 1.8307 1.5933 0.1801  -0.1151 -0.1137 116 SER   A CB  
717  O  OG  A SER   A 96  ? 2.2331 1.8280 1.5758 0.1728  -0.0683 -0.0873 116 SER   A OG  
718  O  OG  B SER   A 96  ? 2.2660 1.8744 1.6103 0.1957  -0.1200 -0.1272 116 SER   A OG  
719  N  N   . ALA   A 97  ? 1.8778 1.6095 1.4522 0.1151  -0.0816 -0.0988 117 ALA   A N   
720  C  CA  . ALA   A 97  ? 1.7802 1.5243 1.3947 0.1035  -0.0841 -0.0949 117 ALA   A CA  
721  C  C   . ALA   A 97  ? 1.6264 1.4129 1.3093 0.1022  -0.1152 -0.1125 117 ALA   A C   
722  O  O   . ALA   A 97  ? 1.6036 1.4254 1.3258 0.0969  -0.1203 -0.1231 117 ALA   A O   
723  C  CB  . ALA   A 97  ? 1.7523 1.5229 1.4020 0.0760  -0.0459 -0.0835 117 ALA   A CB  
724  N  N   . ILE   A 98  ? 1.4747 1.2555 1.1728 0.1078  -0.1337 -0.1147 118 ILE   A N   
725  C  CA  . ILE   A 98  ? 1.5011 1.3182 1.2621 0.1104  -0.1630 -0.1317 118 ILE   A CA  
726  C  C   . ILE   A 98  ? 1.4554 1.3297 1.2878 0.0868  -0.1460 -0.1345 118 ILE   A C   
727  O  O   . ILE   A 98  ? 1.3389 1.2442 1.2168 0.0853  -0.1593 -0.1464 118 ILE   A O   
728  C  CB  . ILE   A 98  ? 1.4868 1.2892 1.2541 0.1218  -0.1805 -0.1326 118 ILE   A CB  
729  C  CG1 . ILE   A 98  ? 1.4329 1.2812 1.2780 0.1219  -0.2038 -0.1500 118 ILE   A CG1 
730  C  CG2 . ILE   A 98  ? 1.3957 1.1894 1.1611 0.1066  -0.1507 -0.1186 118 ILE   A CG2 
731  C  CD1 . ILE   A 98  ? 1.4568 1.2953 1.3153 0.1373  -0.2232 -0.1538 118 ILE   A CD1 
732  N  N   . SER   A 99  ? 1.4504 1.3372 1.2922 0.0684  -0.1165 -0.1236 119 SER   A N   
733  C  CA  . SER   A 99  ? 1.3610 1.2993 1.2611 0.0497  -0.1022 -0.1253 119 SER   A CA  
734  C  C   . SER   A 99  ? 1.3859 1.3442 1.2933 0.0452  -0.0937 -0.1253 119 SER   A C   
735  O  O   . SER   A 99  ? 1.3823 1.3798 1.3368 0.0361  -0.0894 -0.1275 119 SER   A O   
736  C  CB  . SER   A 99  ? 1.3387 1.2833 1.2423 0.0329  -0.0777 -0.1172 119 SER   A CB  
737  O  OG  . SER   A 99  ? 1.3904 1.3081 1.2509 0.0286  -0.0574 -0.1063 119 SER   A OG  
738  N  N   . ILE   A 100 ? 1.3588 1.2875 1.2170 0.0538  -0.0898 -0.1221 120 ILE   A N   
739  C  CA  . ILE   A 100 ? 1.4089 1.3520 1.2706 0.0526  -0.0799 -0.1228 120 ILE   A CA  
740  C  C   . ILE   A 100 ? 1.3880 1.3150 1.2401 0.0684  -0.1055 -0.1366 120 ILE   A C   
741  O  O   . ILE   A 100 ? 1.1552 1.0987 1.0289 0.0667  -0.1027 -0.1411 120 ILE   A O   
742  C  CB  . ILE   A 100 ? 1.5597 1.4861 1.3790 0.0502  -0.0514 -0.1113 120 ILE   A CB  
743  C  CG1 . ILE   A 100 ? 1.5619 1.5044 1.3991 0.0319  -0.0293 -0.1015 120 ILE   A CG1 
744  C  CG2 . ILE   A 100 ? 1.6589 1.6057 1.4889 0.0501  -0.0381 -0.1121 120 ILE   A CG2 
745  C  CD1 . ILE   A 100 ? 1.7468 1.6782 1.5567 0.0256  0.0022  -0.0904 120 ILE   A CD1 
746  N  N   . ALA   A 101 ? 1.4065 1.3011 1.2288 0.0844  -0.1324 -0.1448 121 ALA   A N   
747  C  CA  . ALA   A 101 ? 1.4087 1.2873 1.2219 0.0999  -0.1622 -0.1626 121 ALA   A CA  
748  C  C   . ALA   A 101 ? 1.2731 1.1896 1.1650 0.0910  -0.1780 -0.1754 121 ALA   A C   
749  O  O   . ALA   A 101 ? 1.2960 1.2451 1.2405 0.0784  -0.1710 -0.1707 121 ALA   A O   
750  C  CB  . ALA   A 101 ? 1.6252 1.4617 1.3861 0.1220  -0.1914 -0.1688 121 ALA   A CB  
751  N  N   . GLU   A 102 ? 1.3624 1.2710 1.2607 0.0981  -0.1982 -0.1926 122 GLU   A N   
752  C  CA  . GLU   A 102 ? 1.2991 1.2385 1.2736 0.0872  -0.2071 -0.2038 122 GLU   A CA  
753  C  C   . GLU   A 102 ? 1.2800 1.2099 1.2743 0.0982  -0.2496 -0.2291 122 GLU   A C   
754  O  O   . GLU   A 102 ? 1.3222 1.2162 1.2582 0.1179  -0.2751 -0.2407 122 GLU   A O   
755  C  CB  . GLU   A 102 ? 1.2400 1.1821 1.2209 0.0811  -0.1885 -0.2023 122 GLU   A CB  
756  C  CG  . GLU   A 102 ? 1.2404 1.2036 1.2210 0.0700  -0.1504 -0.1799 122 GLU   A CG  
757  C  CD  . GLU   A 102 ? 1.3902 1.3501 1.3671 0.0709  -0.1348 -0.1789 122 GLU   A CD  
758  O  OE1 . GLU   A 102 ? 1.4761 1.4074 1.4316 0.0820  -0.1506 -0.1955 122 GLU   A OE1 
759  O  OE2 . GLU   A 102 ? 1.3176 1.3029 1.3123 0.0624  -0.1086 -0.1631 122 GLU   A OE2 
760  N  N   . ASP   A 103 ? 1.2795 1.2426 1.3579 0.0855  -0.2564 -0.2378 123 ASP   A N   
761  C  CA  . ASP   A 103 ? 1.2730 1.2387 1.3983 0.0893  -0.2944 -0.2652 123 ASP   A CA  
762  C  C   . ASP   A 103 ? 1.4051 1.3515 1.4962 0.1116  -0.3348 -0.2801 123 ASP   A C   
763  O  O   . ASP   A 103 ? 1.3507 1.3069 1.4438 0.1165  -0.3354 -0.2711 123 ASP   A O   
764  C  CB  . ASP   A 103 ? 1.2957 1.2402 1.4146 0.0891  -0.3016 -0.2808 123 ASP   A CB  
765  C  CG  . ASP   A 103 ? 1.3052 1.2705 1.4790 0.0682  -0.2690 -0.2694 123 ASP   A CG  
766  O  OD1 . ASP   A 103 ? 1.1050 1.1054 1.3368 0.0534  -0.2489 -0.2554 123 ASP   A OD1 
767  O  OD2 . ASP   A 103 ? 1.2622 1.2052 1.4171 0.0692  -0.2636 -0.2745 123 ASP   A OD2 
768  N  N   . GLU   A 104 ? 1.3794 1.2953 1.4347 0.1277  -0.3699 -0.3037 124 GLU   A N   
769  C  CA  . GLU   A 104 ? 1.5482 1.4462 1.5734 0.1526  -0.4162 -0.3213 124 GLU   A CA  
770  C  C   . GLU   A 104 ? 1.4763 1.3375 1.4024 0.1721  -0.4072 -0.3004 124 GLU   A C   
771  O  O   . GLU   A 104 ? 1.4503 1.3077 1.3672 0.1883  -0.4294 -0.3002 124 GLU   A O   
772  C  CB  . GLU   A 104 ? 1.6144 1.4861 1.6186 0.1662  -0.4577 -0.3542 124 GLU   A CB  
773  C  CG  . GLU   A 104 ? 1.6049 1.5086 1.7146 0.1458  -0.4704 -0.3784 124 GLU   A CG  
774  C  CD  . GLU   A 104 ? 1.7858 1.7419 2.0034 0.1329  -0.4768 -0.3813 124 GLU   A CD  
775  O  OE1 . GLU   A 104 ? 1.7597 1.7224 1.9805 0.1514  -0.5128 -0.3926 124 GLU   A OE1 
776  O  OE2 . GLU   A 104 ? 1.7057 1.6955 2.0026 0.1065  -0.4440 -0.3709 124 GLU   A OE2 
777  N  N   . GLU   A 105 ? 1.5173 1.3500 1.3719 0.1713  -0.3733 -0.2821 125 GLU   A N   
778  C  CA  . GLU   A 105 ? 1.6724 1.4680 1.4378 0.1860  -0.3574 -0.2598 125 GLU   A CA  
779  C  C   . GLU   A 105 ? 1.5635 1.3826 1.3639 0.1750  -0.3369 -0.2393 125 GLU   A C   
780  O  O   . GLU   A 105 ? 1.4773 1.2671 1.2256 0.1911  -0.3413 -0.2281 125 GLU   A O   
781  C  CB  . GLU   A 105 ? 1.7233 1.4948 1.4259 0.1822  -0.3176 -0.2439 125 GLU   A CB  
782  C  CG  . GLU   A 105 ? 1.8675 1.5919 1.4710 0.1984  -0.3002 -0.2228 125 GLU   A CG  
783  C  CD  . GLU   A 105 ? 2.1359 1.8535 1.7059 0.1871  -0.2501 -0.2031 125 GLU   A CD  
784  O  OE1 . GLU   A 105 ? 1.9987 1.7567 1.6318 0.1645  -0.2265 -0.2001 125 GLU   A OE1 
785  O  OE2 . GLU   A 105 ? 2.2524 1.9246 1.7337 0.2021  -0.2337 -0.1901 125 GLU   A OE2 
786  N  N   . TRP   A 106 ? 1.3970 1.2637 1.2798 0.1495  -0.3135 -0.2341 126 TRP   A N   
787  C  CA  . TRP   A 106 ? 1.4511 1.3397 1.3660 0.1399  -0.2945 -0.2183 126 TRP   A CA  
788  C  C   . TRP   A 106 ? 1.3369 1.2401 1.2974 0.1520  -0.3286 -0.2321 126 TRP   A C   
789  O  O   . TRP   A 106 ? 1.2092 1.1042 1.1574 0.1594  -0.3257 -0.2217 126 TRP   A O   
790  C  CB  . TRP   A 106 ? 1.2854 1.2181 1.2649 0.1126  -0.2599 -0.2091 126 TRP   A CB  
791  C  CG  . TRP   A 106 ? 1.2607 1.2236 1.2914 0.1042  -0.2495 -0.2026 126 TRP   A CG  
792  C  CD1 . TRP   A 106 ? 1.2431 1.1996 1.2495 0.1005  -0.2267 -0.1861 126 TRP   A CD1 
793  C  CD2 . TRP   A 106 ? 1.3087 1.3116 1.4244 0.0988  -0.2598 -0.2144 126 TRP   A CD2 
794  N  NE1 . TRP   A 106 ? 1.2078 1.1958 1.2730 0.0952  -0.2234 -0.1879 126 TRP   A NE1 
795  C  CE2 . TRP   A 106 ? 1.2269 1.2451 1.3599 0.0945  -0.2415 -0.2040 126 TRP   A CE2 
796  C  CE3 . TRP   A 106 ? 1.2923 1.3192 1.4748 0.0963  -0.2809 -0.2336 126 TRP   A CE3 
797  C  CZ2 . TRP   A 106 ? 1.3061 1.3631 1.5159 0.0902  -0.2411 -0.2110 126 TRP   A CZ2 
798  C  CZ3 . TRP   A 106 ? 1.2490 1.3169 1.5151 0.0894  -0.2794 -0.2394 126 TRP   A CZ3 
799  C  CH2 . TRP   A 106 ? 1.2571 1.3400 1.5340 0.0876  -0.2584 -0.2275 126 TRP   A CH2 
800  N  N   . LYS   A 107 ? 1.4112 1.3372 1.4307 0.1540  -0.3607 -0.2566 127 LYS   A N   
801  C  CA  . LYS   A 107 ? 1.4190 1.3653 1.4920 0.1672  -0.3960 -0.2728 127 LYS   A CA  
802  C  C   . LYS   A 107 ? 1.5361 1.4370 1.5307 0.2001  -0.4278 -0.2730 127 LYS   A C   
803  O  O   . LYS   A 107 ? 1.2025 1.1076 1.2121 0.2129  -0.4378 -0.2701 127 LYS   A O   
804  C  CB  . LYS   A 107 ? 1.2884 1.2644 1.4383 0.1627  -0.4273 -0.3022 127 LYS   A CB  
805  C  CG  . LYS   A 107 ? 1.4078 1.4425 1.6764 0.1439  -0.4170 -0.3078 127 LYS   A CG  
806  C  CD  . LYS   A 107 ? 1.5025 1.5591 1.8243 0.1159  -0.3906 -0.3080 127 LYS   A CD  
807  C  CE  . LYS   A 107 ? 1.5535 1.5944 1.8765 0.1185  -0.4237 -0.3341 127 LYS   A CE  
808  N  NZ  . LYS   A 107 ? 1.5259 1.5751 1.8857 0.0933  -0.3945 -0.3308 127 LYS   A NZ  
809  N  N   . ARG   A 108 ? 1.3924 1.2460 1.2980 0.2165  -0.4422 -0.2757 128 ARG   A N   
810  C  CA  . ARG   A 108 ? 1.5877 1.3893 1.4034 0.2511  -0.4708 -0.2728 128 ARG   A CA  
811  C  C   . ARG   A 108 ? 1.6222 1.3939 1.3852 0.2524  -0.4357 -0.2411 128 ARG   A C   
812  O  O   . ARG   A 108 ? 1.6724 1.4216 1.4110 0.2757  -0.4551 -0.2363 128 ARG   A O   
813  C  CB  . ARG   A 108 ? 1.5640 1.3182 1.2869 0.2677  -0.4859 -0.2807 128 ARG   A CB  
814  C  CG  . ARG   A 108 ? 1.8144 1.5013 1.4158 0.3026  -0.4993 -0.2677 128 ARG   A CG  
815  C  CD  . ARG   A 108 ? 2.0683 1.7100 1.5769 0.3196  -0.5114 -0.2778 128 ARG   A CD  
816  N  NE  . ARG   A 108 ? 2.2451 1.8175 1.6251 0.3414  -0.4910 -0.2513 128 ARG   A NE  
817  C  CZ  . ARG   A 108 ? 2.3001 1.8538 1.6401 0.3243  -0.4331 -0.2233 128 ARG   A CZ  
818  N  NH1 . ARG   A 108 ? 2.2265 1.8254 1.6393 0.2882  -0.3938 -0.2183 128 ARG   A NH1 
819  N  NH2 . ARG   A 108 ? 2.3313 1.8193 1.5565 0.3448  -0.4140 -0.1993 128 ARG   A NH2 
820  N  N   . LEU   A 109 ? 1.6081 1.3796 1.3580 0.2275  -0.3850 -0.2205 129 LEU   A N   
821  C  CA  . LEU   A 109 ? 1.5633 1.3072 1.2714 0.2240  -0.3501 -0.1931 129 LEU   A CA  
822  C  C   . LEU   A 109 ? 1.6398 1.4172 1.4207 0.2165  -0.3462 -0.1919 129 LEU   A C   
823  O  O   . LEU   A 109 ? 1.6786 1.4240 1.4262 0.2279  -0.3410 -0.1779 129 LEU   A O   
824  C  CB  . LEU   A 109 ? 1.5450 1.2896 1.2348 0.1981  -0.3005 -0.1759 129 LEU   A CB  
825  C  CG  . LEU   A 109 ? 1.6565 1.3651 1.2691 0.2062  -0.2945 -0.1743 129 LEU   A CG  
826  C  CD1 . LEU   A 109 ? 1.6006 1.3214 1.2142 0.1802  -0.2446 -0.1585 129 LEU   A CD1 
827  C  CD2 . LEU   A 109 ? 1.8378 1.4770 1.3433 0.2369  -0.3056 -0.1633 129 LEU   A CD2 
828  N  N   . ARG   A 110 ? 1.4379 1.2757 1.3161 0.1982  -0.3457 -0.2058 130 ARG   A N   
829  C  CA  . ARG   A 110 ? 1.4307 1.3021 1.3780 0.1928  -0.3391 -0.2065 130 ARG   A CA  
830  C  C   . ARG   A 110 ? 1.5328 1.3930 1.4857 0.2241  -0.3802 -0.2171 130 ARG   A C   
831  O  O   . ARG   A 110 ? 1.5475 1.3965 1.5006 0.2324  -0.3732 -0.2086 130 ARG   A O   
832  C  CB  . ARG   A 110 ? 1.3947 1.3298 1.4404 0.1695  -0.3289 -0.2184 130 ARG   A CB  
833  C  CG  . ARG   A 110 ? 1.2986 1.2694 1.4102 0.1614  -0.3111 -0.2171 130 ARG   A CG  
834  C  CD  . ARG   A 110 ? 1.3753 1.3388 1.4599 0.1424  -0.2672 -0.1977 130 ARG   A CD  
835  N  NE  . ARG   A 110 ? 1.3185 1.3046 1.4485 0.1402  -0.2528 -0.1982 130 ARG   A NE  
836  C  CZ  . ARG   A 110 ? 1.2334 1.2299 1.3656 0.1217  -0.2175 -0.1887 130 ARG   A CZ  
837  N  NH1 . ARG   A 110 ? 1.2397 1.2330 1.3410 0.1025  -0.1937 -0.1775 130 ARG   A NH1 
838  N  NH2 . ARG   A 110 ? 1.0154 1.0271 1.1822 0.1241  -0.2073 -0.1924 130 ARG   A NH2 
839  N  N   . SER   A 111 ? 1.5256 1.3880 1.4837 0.2433  -0.4254 -0.2375 131 SER   A N   
840  C  CA  . SER   A 111 ? 1.5107 1.3629 1.4708 0.2779  -0.4711 -0.2491 131 SER   A CA  
841  C  C   . SER   A 111 ? 1.7195 1.4972 1.5665 0.3050  -0.4741 -0.2283 131 SER   A C   
842  O  O   . SER   A 111 ? 1.6767 1.4382 1.5212 0.3276  -0.4872 -0.2239 131 SER   A O   
843  C  CB  . SER   A 111 ? 1.4684 1.3392 1.4562 0.2920  -0.5227 -0.2787 131 SER   A CB  
844  O  OG  . SER   A 111 ? 1.4881 1.4257 1.5903 0.2664  -0.5186 -0.2973 131 SER   A OG  
845  N  N   . LEU   A 112 ? 1.6865 1.4158 1.4392 0.3038  -0.4587 -0.2142 132 LEU   A N   
846  C  CA  . LEU   A 112 ? 1.8320 1.4841 1.4701 0.3302  -0.4585 -0.1924 132 LEU   A CA  
847  C  C   . LEU   A 112 ? 1.9119 1.5401 1.5387 0.3189  -0.4161 -0.1668 132 LEU   A C   
848  O  O   . LEU   A 112 ? 1.7532 1.3220 1.3122 0.3444  -0.4211 -0.1502 132 LEU   A O   
849  C  CB  . LEU   A 112 ? 1.9546 1.5649 1.5002 0.3293  -0.4449 -0.1838 132 LEU   A CB  
850  C  CG  . LEU   A 112 ? 2.1062 1.6304 1.5205 0.3584  -0.4420 -0.1601 132 LEU   A CG  
851  C  CD1 . LEU   A 112 ? 2.2646 1.7584 1.6150 0.3997  -0.4989 -0.1767 132 LEU   A CD1 
852  C  CD2 . LEU   A 112 ? 2.1894 1.6853 1.5447 0.3361  -0.3882 -0.1384 132 LEU   A CD2 
853  N  N   . LEU   A 113 ? 1.8130 1.4828 1.5024 0.2822  -0.3756 -0.1637 133 LEU   A N   
854  C  CA  . LEU   A 113 ? 1.8177 1.4675 1.5009 0.2676  -0.3360 -0.1442 133 LEU   A CA  
855  C  C   . LEU   A 113 ? 1.8441 1.5357 1.6140 0.2640  -0.3370 -0.1547 133 LEU   A C   
856  O  O   . LEU   A 113 ? 1.7783 1.4485 1.5424 0.2564  -0.3100 -0.1425 133 LEU   A O   
857  C  CB  . LEU   A 113 ? 1.7869 1.4476 1.4665 0.2306  -0.2879 -0.1327 133 LEU   A CB  
858  C  CG  . LEU   A 113 ? 1.8780 1.4931 1.4691 0.2321  -0.2735 -0.1182 133 LEU   A CG  
859  C  CD1 . LEU   A 113 ? 1.9262 1.5626 1.5311 0.1960  -0.2268 -0.1090 133 LEU   A CD1 
860  C  CD2 . LEU   A 113 ? 2.0762 1.6103 1.5727 0.2568  -0.2719 -0.0968 133 LEU   A CD2 
861  N  N   . SER   A 114 ? 1.7756 1.5252 1.6273 0.2687  -0.3651 -0.1780 134 SER   A N   
862  C  CA  . SER   A 114 ? 1.8097 1.6020 1.7461 0.2664  -0.3612 -0.1883 134 SER   A CA  
863  C  C   . SER   A 114 ? 1.8648 1.6147 1.7772 0.2963  -0.3736 -0.1822 134 SER   A C   
864  O  O   . SER   A 114 ? 1.8418 1.5929 1.7779 0.2867  -0.3462 -0.1781 134 SER   A O   
865  C  CB  . SER   A 114 ? 1.7032 1.5636 1.7344 0.2676  -0.3887 -0.2139 134 SER   A CB  
866  O  OG  . SER   A 114 ? 1.5872 1.4882 1.6541 0.2356  -0.3667 -0.2175 134 SER   A OG  
867  N  N   . PRO   A 115 ? 1.8697 1.5784 1.7324 0.3346  -0.4147 -0.1817 135 PRO   A N   
868  C  CA  . PRO   A 115 ? 2.0723 1.7433 1.9216 0.3665  -0.4283 -0.1763 135 PRO   A CA  
869  C  C   . PRO   A 115 ? 2.0723 1.6708 1.8463 0.3611  -0.3912 -0.1496 135 PRO   A C   
870  O  O   . PRO   A 115 ? 2.1671 1.7174 1.9131 0.3894  -0.4006 -0.1412 135 PRO   A O   
871  C  CB  . PRO   A 115 ? 2.1230 1.7659 1.9266 0.4099  -0.4844 -0.1814 135 PRO   A CB  
872  C  CG  . PRO   A 115 ? 1.9787 1.6691 1.8118 0.3982  -0.5051 -0.2004 135 PRO   A CG  
873  C  CD  . PRO   A 115 ? 1.9260 1.6244 1.7490 0.3543  -0.4554 -0.1897 135 PRO   A CD  
874  N  N   . THR   A 116 ? 2.1424 1.7318 1.8873 0.3252  -0.3492 -0.1367 136 THR   A N   
875  C  CA  . THR   A 116 ? 2.1639 1.6906 1.8524 0.3135  -0.3109 -0.1142 136 THR   A CA  
876  C  C   . THR   A 116 ? 2.0886 1.6356 1.8388 0.2992  -0.2875 -0.1220 136 THR   A C   
877  O  O   . THR   A 116 ? 2.1519 1.6401 1.8666 0.3031  -0.2698 -0.1091 136 THR   A O   
878  C  CB  . THR   A 116 ? 2.1515 1.6697 1.7995 0.2799  -0.2749 -0.1008 136 THR   A CB  
879  O  OG1 . THR   A 116 ? 2.2606 1.7621 1.8510 0.2951  -0.2959 -0.0968 136 THR   A OG1 
880  C  CG2 . THR   A 116 ? 2.2447 1.6936 1.8346 0.2678  -0.2365 -0.0772 136 THR   A CG2 
881  N  N   . PHE   A 117 ? 2.0210 1.6457 1.8599 0.2838  -0.2859 -0.1430 137 PHE   A N   
882  C  CA  . PHE   A 117 ? 2.0455 1.6938 1.9389 0.2697  -0.2610 -0.1528 137 PHE   A CA  
883  C  C   . PHE   A 117 ? 2.0392 1.7314 2.0079 0.2947  -0.2849 -0.1728 137 PHE   A C   
884  O  O   . PHE   A 117 ? 2.0125 1.7594 2.0501 0.2805  -0.2680 -0.1878 137 PHE   A O   
885  C  CB  . PHE   A 117 ? 1.9648 1.6640 1.8920 0.2285  -0.2287 -0.1578 137 PHE   A CB  
886  C  CG  . PHE   A 117 ? 1.9765 1.6453 1.8444 0.2038  -0.2058 -0.1407 137 PHE   A CG  
887  C  CD1 . PHE   A 117 ? 1.9795 1.5898 1.8001 0.1930  -0.1802 -0.1271 137 PHE   A CD1 
888  C  CD2 . PHE   A 117 ? 1.8962 1.5944 1.7600 0.1913  -0.2084 -0.1392 137 PHE   A CD2 
889  C  CE1 . PHE   A 117 ? 1.9793 1.5668 1.7553 0.1693  -0.1563 -0.1120 137 PHE   A CE1 
890  C  CE2 . PHE   A 117 ? 1.8762 1.5502 1.6905 0.1706  -0.1852 -0.1242 137 PHE   A CE2 
891  C  CZ  . PHE   A 117 ? 1.9629 1.5843 1.7359 0.1593  -0.1584 -0.1104 137 PHE   A CZ  
892  N  N   . THR   A 118 ? 2.1279 1.7972 2.0839 0.3342  -0.3242 -0.1734 138 THR   A N   
893  C  CA  . THR   A 118 ? 2.1549 1.8616 2.1852 0.3619  -0.3465 -0.1921 138 THR   A CA  
894  C  C   . THR   A 118 ? 2.1753 1.8474 2.2061 0.3691  -0.3237 -0.1912 138 THR   A C   
895  O  O   . THR   A 118 ? 2.2009 1.8073 2.1657 0.3583  -0.2992 -0.1749 138 THR   A O   
896  C  CB  . THR   A 118 ? 2.1940 1.8842 2.2089 0.4059  -0.3996 -0.1941 138 THR   A CB  
897  O  OG1 . THR   A 118 ? 2.2726 1.8689 2.1870 0.4288  -0.4048 -0.1711 138 THR   A OG1 
898  C  CG2 . THR   A 118 ? 1.9973 1.7217 2.0140 0.3991  -0.4251 -0.2004 138 THR   A CG2 
899  N  N   . SER   A 119 ? 2.1552 1.8725 2.2658 0.3871  -0.3303 -0.2107 139 SER   A N   
900  C  CA  . SER   A 119 ? 2.2179 1.9037 2.3335 0.3982  -0.3101 -0.2141 139 SER   A CA  
901  C  C   . SER   A 119 ? 2.3375 1.9296 2.3771 0.4310  -0.3264 -0.1967 139 SER   A C   
902  O  O   . SER   A 119 ? 2.3025 1.8404 2.3153 0.4312  -0.3027 -0.1926 139 SER   A O   
903  C  CB  . SER   A 119 ? 2.1386 1.8922 2.3556 0.4177  -0.3159 -0.2384 139 SER   A CB  
904  O  OG  . SER   A 119 ? 2.0260 1.8229 2.2909 0.4435  -0.3594 -0.2473 139 SER   A OG  
905  N  N   . GLY   A 120 ? 2.7101 2.2778 2.7102 0.4595  -0.3666 -0.1865 140 GLY   A N   
906  C  CA  . GLY   A 120 ? 2.7608 2.2330 2.6764 0.4935  -0.3822 -0.1653 140 GLY   A CA  
907  C  C   . GLY   A 120 ? 2.7760 2.1718 2.5905 0.4689  -0.3555 -0.1376 140 GLY   A C   
908  O  O   . GLY   A 120 ? 2.8343 2.1495 2.5951 0.4722  -0.3343 -0.1214 140 GLY   A O   
909  N  N   . LYS   A 121 ? 2.5049 1.9241 2.2960 0.4441  -0.3544 -0.1322 141 LYS   A N   
910  C  CA  . LYS   A 121 ? 2.5285 1.8840 2.2318 0.4191  -0.3248 -0.1067 141 LYS   A CA  
911  C  C   . LYS   A 121 ? 2.5097 1.8519 2.2240 0.3793  -0.2749 -0.1061 141 LYS   A C   
912  O  O   . LYS   A 121 ? 2.4892 1.7548 2.1373 0.3681  -0.2484 -0.0847 141 LYS   A O   
913  C  CB  . LYS   A 121 ? 2.4091 1.8053 2.1008 0.3984  -0.3296 -0.1065 141 LYS   A CB  
914  C  CG  . LYS   A 121 ? 2.3536 1.7501 2.0169 0.4364  -0.3804 -0.1074 141 LYS   A CG  
915  C  CD  . LYS   A 121 ? 2.4286 1.7232 1.9732 0.4657  -0.3877 -0.0779 141 LYS   A CD  
916  C  CE  . LYS   A 121 ? 2.4056 1.6991 1.9191 0.5112  -0.4460 -0.0827 141 LYS   A CE  
917  N  NZ  . LYS   A 121 ? 2.3566 1.7164 1.8967 0.4938  -0.4617 -0.1001 141 LYS   A NZ  
918  N  N   . LEU   A 122 ? 2.3749 1.7897 2.1720 0.3576  -0.2613 -0.1301 142 LEU   A N   
919  C  CA  . LEU   A 122 ? 2.3420 1.7454 2.1512 0.3253  -0.2207 -0.1352 142 LEU   A CA  
920  C  C   . LEU   A 122 ? 2.3546 1.6854 2.1448 0.3489  -0.2164 -0.1325 142 LEU   A C   
921  O  O   . LEU   A 122 ? 2.3630 1.6319 2.1157 0.3287  -0.1867 -0.1231 142 LEU   A O   
922  C  CB  . LEU   A 122 ? 2.1909 1.6852 2.0844 0.3044  -0.2099 -0.1614 142 LEU   A CB  
923  C  CG  . LEU   A 122 ? 2.0901 1.6265 1.9917 0.2580  -0.1822 -0.1634 142 LEU   A CG  
924  C  CD1 . LEU   A 122 ? 2.1226 1.6738 1.9965 0.2508  -0.1941 -0.1500 142 LEU   A CD1 
925  C  CD2 . LEU   A 122 ? 1.9825 1.5993 1.9597 0.2461  -0.1725 -0.1872 142 LEU   A CD2 
926  N  N   . LYS   A 123 ? 2.4009 1.7383 2.2213 0.3922  -0.2462 -0.1418 143 LYS   A N   
927  C  CA  . LYS   A 123 ? 2.4299 1.6976 2.2354 0.4203  -0.2443 -0.1403 143 LYS   A CA  
928  C  C   . LYS   A 123 ? 2.4733 1.6309 2.1815 0.4338  -0.2430 -0.1079 143 LYS   A C   
929  O  O   . LYS   A 123 ? 2.5255 1.6056 2.2055 0.4381  -0.2241 -0.1011 143 LYS   A O   
930  C  CB  . LYS   A 123 ? 2.4330 1.7379 2.2961 0.4680  -0.2798 -0.1566 143 LYS   A CB  
931  C  CG  . LYS   A 123 ? 2.4223 1.6762 2.2947 0.4965  -0.2741 -0.1639 143 LYS   A CG  
932  C  CD  . LYS   A 123 ? 2.3671 1.7039 2.3393 0.5113  -0.2787 -0.1957 143 LYS   A CD  
933  C  CE  . LYS   A 123 ? 2.2831 1.6988 2.3110 0.5362  -0.3194 -0.2037 143 LYS   A CE  
934  N  NZ  . LYS   A 123 ? 2.2170 1.7199 2.3510 0.5456  -0.3165 -0.2338 143 LYS   A NZ  
935  N  N   . GLU   A 124 ? 2.5279 1.6731 2.1810 0.4409  -0.2606 -0.0875 144 GLU   A N   
936  C  CA  . GLU   A 124 ? 2.5637 1.6033 2.1150 0.4486  -0.2504 -0.0530 144 GLU   A CA  
937  C  C   . GLU   A 124 ? 2.5998 1.6023 2.1268 0.3973  -0.1992 -0.0427 144 GLU   A C   
938  O  O   . GLU   A 124 ? 2.5713 1.4755 2.0281 0.3988  -0.1785 -0.0160 144 GLU   A O   
939  C  CB  . GLU   A 124 ? 2.6141 1.6544 2.1083 0.4666  -0.2786 -0.0364 144 GLU   A CB  
940  C  CG  . GLU   A 124 ? 2.6367 1.6975 2.1405 0.5222  -0.3356 -0.0439 144 GLU   A CG  
941  C  CD  . GLU   A 124 ? 2.7486 1.7974 2.1812 0.5407  -0.3642 -0.0286 144 GLU   A CD  
942  O  OE1 . GLU   A 124 ? 2.7642 1.7452 2.1077 0.5274  -0.3381 -0.0004 144 GLU   A OE1 
943  O  OE2 . GLU   A 124 ? 2.7362 1.8439 2.2036 0.5681  -0.4118 -0.0463 144 GLU   A OE2 
944  N  N   . MET   A 125 ? 2.5599 1.6379 2.1450 0.3527  -0.1785 -0.0628 145 MET   A N   
945  C  CA  . MET   A 125 ? 2.5679 1.6262 2.1399 0.3027  -0.1350 -0.0565 145 MET   A CA  
946  C  C   . MET   A 125 ? 2.5906 1.6238 2.1956 0.2825  -0.1089 -0.0730 145 MET   A C   
947  O  O   . MET   A 125 ? 2.6207 1.6217 2.2133 0.2435  -0.0743 -0.0677 145 MET   A O   
948  C  CB  . MET   A 125 ? 2.4479 1.5990 2.0597 0.2667  -0.1287 -0.0690 145 MET   A CB  
949  C  CG  . MET   A 125 ? 2.5396 1.7120 2.1163 0.2800  -0.1500 -0.0551 145 MET   A CG  
950  S  SD  . MET   A 125 ? 2.5135 1.7898 2.1402 0.2400  -0.1416 -0.0702 145 MET   A SD  
951  C  CE  . MET   A 125 ? 2.4730 1.7504 2.0465 0.2670  -0.1722 -0.0552 145 MET   A CE  
952  N  N   . VAL   A 126 ? 2.5775 1.6257 2.2268 0.3078  -0.1241 -0.0947 146 VAL   A N   
953  C  CA  . VAL   A 126 ? 2.6351 1.6585 2.3132 0.2919  -0.1013 -0.1150 146 VAL   A CA  
954  C  C   . VAL   A 126 ? 2.7554 1.6570 2.3747 0.2948  -0.0817 -0.0934 146 VAL   A C   
955  O  O   . VAL   A 126 ? 2.7637 1.6337 2.3876 0.2563  -0.0501 -0.1004 146 VAL   A O   
956  C  CB  . VAL   A 126 ? 2.5785 1.6451 2.3150 0.3236  -0.1203 -0.1431 146 VAL   A CB  
957  C  CG1 . VAL   A 126 ? 2.5063 1.5330 2.2603 0.3125  -0.0972 -0.1648 146 VAL   A CG1 
958  C  CG2 . VAL   A 126 ? 2.3567 1.5407 2.1557 0.3129  -0.1301 -0.1640 146 VAL   A CG2 
959  N  N   . PRO   A 127 ? 2.7857 1.6135 2.3496 0.3388  -0.0989 -0.0673 147 PRO   A N   
960  C  CA  . PRO   A 127 ? 2.9030 1.6062 2.4046 0.3386  -0.0743 -0.0415 147 PRO   A CA  
961  C  C   . PRO   A 127 ? 2.9325 1.6037 2.3947 0.2933  -0.0387 -0.0186 147 PRO   A C   
962  O  O   . PRO   A 127 ? 3.0579 1.6442 2.4976 0.2713  -0.0054 -0.0077 147 PRO   A O   
963  C  CB  . PRO   A 127 ? 2.9313 1.5753 2.3744 0.4000  -0.1059 -0.0150 147 PRO   A CB  
964  C  CG  . PRO   A 127 ? 2.8098 1.5441 2.3126 0.4340  -0.1466 -0.0409 147 PRO   A CG  
965  C  CD  . PRO   A 127 ? 2.7885 1.6371 2.3481 0.3937  -0.1425 -0.0628 147 PRO   A CD  
966  N  N   . ILE   A 128 ? 2.8772 1.6134 2.3348 0.2783  -0.0429 -0.0118 148 ILE   A N   
967  C  CA  . ILE   A 128 ? 2.9213 1.6322 2.3447 0.2381  -0.0072 0.0104  148 ILE   A CA  
968  C  C   . ILE   A 128 ? 2.9396 1.7059 2.4294 0.1806  0.0199  -0.0165 148 ILE   A C   
969  O  O   . ILE   A 128 ? 2.9789 1.6963 2.4608 0.1431  0.0574  -0.0069 148 ILE   A O   
970  C  CB  . ILE   A 128 ? 2.9292 1.6792 2.3134 0.2502  -0.0227 0.0288  148 ILE   A CB  
971  C  CG1 . ILE   A 128 ? 3.0455 1.7094 2.3380 0.3015  -0.0399 0.0636  148 ILE   A CG1 
972  C  CG2 . ILE   A 128 ? 2.9501 1.7147 2.3285 0.2019  0.0147  0.0395  148 ILE   A CG2 
973  C  CD1 . ILE   A 128 ? 3.0313 1.7170 2.3333 0.3570  -0.0915 0.0519  148 ILE   A CD1 
974  N  N   . ILE   A 129 ? 2.8827 1.7505 2.4394 0.1733  0.0016  -0.0506 149 ILE   A N   
975  C  CA  . ILE   A 129 ? 2.8140 1.7385 2.4288 0.1238  0.0215  -0.0778 149 ILE   A CA  
976  C  C   . ILE   A 129 ? 2.9275 1.7904 2.5595 0.1064  0.0412  -0.0944 149 ILE   A C   
977  O  O   . ILE   A 129 ? 2.9153 1.7842 2.5758 0.0604  0.0658  -0.1073 149 ILE   A O   
978  C  CB  . ILE   A 129 ? 2.6045 1.6427 2.2771 0.1266  -0.0025 -0.1076 149 ILE   A CB  
979  C  CG1 . ILE   A 129 ? 2.4888 1.5888 2.1516 0.1306  -0.0158 -0.0936 149 ILE   A CG1 
980  C  CG2 . ILE   A 129 ? 2.4606 1.5488 2.1874 0.0845  0.0129  -0.1393 149 ILE   A CG2 
981  C  CD1 . ILE   A 129 ? 2.2811 1.4889 2.0013 0.1278  -0.0334 -0.1192 149 ILE   A CD1 
982  N  N   . ALA   A 130 ? 2.9503 1.7512 2.5670 0.1433  0.0298  -0.0956 150 ALA   A N   
983  C  CA  . ALA   A 130 ? 2.9553 1.6917 2.5874 0.1312  0.0463  -0.1145 150 ALA   A CA  
984  C  C   . ALA   A 130 ? 3.1297 1.7757 2.7354 0.0958  0.0838  -0.0944 150 ALA   A C   
985  O  O   . ALA   A 130 ? 3.0451 1.6350 2.6687 0.0776  0.1001  -0.1124 150 ALA   A O   
986  C  CB  . ALA   A 130 ? 2.9991 1.6794 2.6138 0.1846  0.0268  -0.1144 150 ALA   A CB  
987  N  N   . GLN   A 131 ? 3.2312 1.8601 2.7966 0.0852  0.0997  -0.0588 151 GLN   A N   
988  C  CA  . GLN   A 131 ? 3.2454 1.7917 2.7912 0.0490  0.1417  -0.0373 151 GLN   A CA  
989  C  C   . GLN   A 131 ? 3.1411 1.7497 2.7509 -0.0120 0.1626  -0.0625 151 GLN   A C   
990  O  O   . GLN   A 131 ? 3.2244 1.7928 2.8681 -0.0461 0.1831  -0.0816 151 GLN   A O   
991  C  CB  . GLN   A 131 ? 3.3367 1.8355 2.8077 0.0652  0.1547  0.0124  151 GLN   A CB  
992  C  CG  . GLN   A 131 ? 3.3810 1.8247 2.8427 0.0192  0.2049  0.0355  151 GLN   A CG  
993  C  CD  . GLN   A 131 ? 3.5240 1.9293 2.9064 0.0365  0.2205  0.0836  151 GLN   A CD  
994  O  OE1 . GLN   A 131 ? 3.7007 2.0726 3.0151 0.0893  0.1960  0.1064  151 GLN   A OE1 
995  N  NE2 . GLN   A 131 ? 3.4619 1.8736 2.8530 -0.0064 0.2608  0.0977  151 GLN   A NE2 
996  N  N   . TYR   A 132 ? 3.0576 1.7642 2.6865 -0.0252 0.1556  -0.0645 152 TYR   A N   
997  C  CA  . TYR   A 132 ? 2.9377 1.7047 2.6236 -0.0796 0.1748  -0.0830 152 TYR   A CA  
998  C  C   . TYR   A 132 ? 2.8674 1.6928 2.6193 -0.1001 0.1593  -0.1333 152 TYR   A C   
999  O  O   . TYR   A 132 ? 2.7340 1.5947 2.5365 -0.1461 0.1734  -0.1536 152 TYR   A O   
1000 C  CB  . TYR   A 132 ? 2.8236 1.6755 2.5070 -0.0816 0.1699  -0.0700 152 TYR   A CB  
1001 C  CG  . TYR   A 132 ? 2.9023 1.6962 2.5148 -0.0639 0.1880  -0.0226 152 TYR   A CG  
1002 C  CD1 . TYR   A 132 ? 2.9083 1.6440 2.5088 -0.0957 0.2329  0.0021  152 TYR   A CD1 
1003 C  CD2 . TYR   A 132 ? 2.9008 1.6964 2.4579 -0.0148 0.1609  -0.0036 152 TYR   A CD2 
1004 C  CE1 . TYR   A 132 ? 2.9995 1.6777 2.5254 -0.0770 0.2529  0.0466  152 TYR   A CE1 
1005 C  CE2 . TYR   A 132 ? 2.9591 1.6984 2.4414 0.0048  0.1749  0.0378  152 TYR   A CE2 
1006 C  CZ  . TYR   A 132 ? 3.0105 1.6892 2.4725 -0.0253 0.2222  0.0639  152 TYR   A CZ  
1007 O  OH  . TYR   A 132 ? 3.1006 1.7193 2.4783 -0.0030 0.2392  0.1064  152 TYR   A OH  
1008 N  N   . GLY   A 133 ? 2.8040 1.6419 2.5570 -0.0660 0.1308  -0.1547 153 GLY   A N   
1009 C  CA  . GLY   A 133 ? 2.7011 1.5716 2.5032 -0.0821 0.1209  -0.2020 153 GLY   A CA  
1010 C  C   . GLY   A 133 ? 2.7918 1.5726 2.6061 -0.1096 0.1432  -0.2153 153 GLY   A C   
1011 O  O   . GLY   A 133 ? 2.8021 1.6097 2.6641 -0.1456 0.1447  -0.2528 153 GLY   A O   
1012 N  N   . ASP   A 134 ? 2.9004 1.5705 2.6703 -0.0923 0.1596  -0.1853 154 ASP   A N   
1013 C  CA  . ASP   A 134 ? 2.8847 1.4572 2.6655 -0.1207 0.1856  -0.1932 154 ASP   A CA  
1014 C  C   . ASP   A 134 ? 2.8242 1.3931 2.6339 -0.1763 0.2193  -0.1824 154 ASP   A C   
1015 O  O   . ASP   A 134 ? 2.8844 1.4188 2.7376 -0.2177 0.2359  -0.2075 154 ASP   A O   
1016 C  CB  . ASP   A 134 ? 3.0130 1.4629 2.7335 -0.0819 0.1943  -0.1605 154 ASP   A CB  
1017 C  CG  . ASP   A 134 ? 3.1069 1.5594 2.8111 -0.0270 0.1619  -0.1754 154 ASP   A CG  
1018 O  OD1 . ASP   A 134 ? 3.0854 1.6014 2.8308 -0.0290 0.1428  -0.2201 154 ASP   A OD1 
1019 O  OD2 . ASP   A 134 ? 3.1449 1.5370 2.7948 0.0196  0.1557  -0.1426 154 ASP   A OD2 
1020 N  N   . VAL   A 135 ? 2.8583 1.4622 2.6476 -0.1781 0.2303  -0.1470 155 VAL   A N   
1021 C  CA  . VAL   A 135 ? 2.8401 1.4694 2.6708 -0.2309 0.2607  -0.1423 155 VAL   A CA  
1022 C  C   . VAL   A 135 ? 2.7794 1.5239 2.6832 -0.2622 0.2405  -0.1893 155 VAL   A C   
1023 O  O   . VAL   A 135 ? 2.7774 1.5364 2.7411 -0.3123 0.2581  -0.2084 155 VAL   A O   
1024 C  CB  . VAL   A 135 ? 2.8553 1.4947 2.6403 -0.2195 0.2778  -0.0941 155 VAL   A CB  
1025 C  CG1 . VAL   A 135 ? 2.8245 1.4901 2.6571 -0.2730 0.3144  -0.0885 155 VAL   A CG1 
1026 C  CG2 . VAL   A 135 ? 2.8976 1.4197 2.5981 -0.1820 0.2933  -0.0475 155 VAL   A CG2 
1027 N  N   . LEU   A 136 ? 2.7391 1.5661 2.6402 -0.2327 0.2032  -0.2086 156 LEU   A N   
1028 C  CA  . LEU   A 136 ? 2.6005 1.5318 2.5589 -0.2552 0.1814  -0.2519 156 LEU   A CA  
1029 C  C   . LEU   A 136 ? 2.6388 1.5431 2.6348 -0.2766 0.1746  -0.2994 156 LEU   A C   
1030 O  O   . LEU   A 136 ? 2.6851 1.6433 2.7380 -0.3152 0.1699  -0.3336 156 LEU   A O   
1031 C  CB  . LEU   A 136 ? 2.5174 1.5299 2.4564 -0.2152 0.1481  -0.2563 156 LEU   A CB  
1032 C  CG  . LEU   A 136 ? 2.4221 1.5342 2.4012 -0.2233 0.1215  -0.2990 156 LEU   A CG  
1033 C  CD1 . LEU   A 136 ? 2.3292 1.5144 2.3555 -0.2634 0.1273  -0.3051 156 LEU   A CD1 
1034 C  CD2 . LEU   A 136 ? 2.2608 1.4306 2.2135 -0.1795 0.0967  -0.2939 156 LEU   A CD2 
1035 N  N   . VAL   A 137 ? 2.7898 1.6108 2.7548 -0.2502 0.1718  -0.3042 157 VAL   A N   
1036 C  CA  . VAL   A 137 ? 2.7755 1.5584 2.7706 -0.2685 0.1666  -0.3508 157 VAL   A CA  
1037 C  C   . VAL   A 137 ? 2.7935 1.5087 2.8269 -0.3200 0.1982  -0.3517 157 VAL   A C   
1038 O  O   . VAL   A 137 ? 2.8201 1.5598 2.9110 -0.3605 0.1931  -0.3951 157 VAL   A O   
1039 C  CB  . VAL   A 137 ? 2.7299 1.4395 2.6817 -0.2225 0.1571  -0.3547 157 VAL   A CB  
1040 C  CG1 . VAL   A 137 ? 2.7623 1.4104 2.7399 -0.2426 0.1576  -0.4006 157 VAL   A CG1 
1041 C  CG2 . VAL   A 137 ? 2.7253 1.5147 2.6580 -0.1781 0.1265  -0.3641 157 VAL   A CG2 
1042 N  N   . ARG   A 138 ? 2.7806 1.4092 2.7830 -0.3191 0.2316  -0.3041 158 ARG   A N   
1043 C  CA  . ARG   A 138 ? 2.8074 1.3625 2.8470 -0.3685 0.2690  -0.2998 158 ARG   A CA  
1044 C  C   . ARG   A 138 ? 2.8295 1.4699 2.9375 -0.4194 0.2798  -0.3085 158 ARG   A C   
1045 O  O   . ARG   A 138 ? 2.8802 1.5264 3.0493 -0.4609 0.2869  -0.3259 158 ARG   A O   
1046 C  CB  . ARG   A 138 ? 2.9270 1.3698 2.9066 -0.3510 0.3054  -0.2406 158 ARG   A CB  
1047 C  CG  . ARG   A 138 ? 2.9982 1.3401 2.9597 -0.3373 0.3087  -0.2364 158 ARG   A CG  
1048 C  CD  . ARG   A 138 ? 3.1462 1.3902 3.0443 -0.3166 0.3419  -0.1727 158 ARG   A CD  
1049 N  NE  . ARG   A 138 ? 3.1316 1.4018 3.0274 -0.3389 0.3740  -0.1352 158 ARG   A NE  
1050 C  CZ  . ARG   A 138 ? 3.2105 1.4819 3.0426 -0.3078 0.3788  -0.0988 158 ARG   A CZ  
1051 N  NH1 . ARG   A 138 ? 3.2286 1.4940 2.9993 -0.2500 0.3474  -0.0921 158 ARG   A NH1 
1052 N  NH2 . ARG   A 138 ? 3.2161 1.5144 3.0503 -0.3309 0.4100  -0.0685 158 ARG   A NH2 
1053 N  N   . ASN   A 139 ? 2.6868 1.4224 2.7863 -0.4068 0.2705  -0.2897 159 ASN   A N   
1054 C  CA  . ASN   A 139 ? 2.7071 1.5382 2.8764 -0.4494 0.2739  -0.3041 159 ASN   A CA  
1055 C  C   . ASN   A 139 ? 2.6494 1.5590 2.8755 -0.4673 0.2359  -0.3668 159 ASN   A C   
1056 O  O   . ASN   A 139 ? 2.6645 1.6244 2.9665 -0.5135 0.2384  -0.3931 159 ASN   A O   
1057 C  CB  . ASN   A 139 ? 2.6167 1.5261 2.7578 -0.4265 0.2714  -0.2701 159 ASN   A CB  
1058 C  CG  . ASN   A 139 ? 2.7126 1.5656 2.8229 -0.4303 0.3171  -0.2144 159 ASN   A CG  
1059 O  OD1 . ASN   A 139 ? 2.8077 1.5837 2.9395 -0.4634 0.3562  -0.2028 159 ASN   A OD1 
1060 N  ND2 . ASN   A 139 ? 2.6685 1.5573 2.7269 -0.3966 0.3139  -0.1801 159 ASN   A ND2 
1061 N  N   . LEU   A 140 ? 2.7035 1.6252 2.8940 -0.4300 0.2008  -0.3918 160 LEU   A N   
1062 C  CA  . LEU   A 140 ? 2.6474 1.6346 2.8756 -0.4408 0.1646  -0.4511 160 LEU   A CA  
1063 C  C   . LEU   A 140 ? 2.7020 1.6263 2.9573 -0.4628 0.1613  -0.4869 160 LEU   A C   
1064 O  O   . LEU   A 140 ? 2.7228 1.7088 3.0252 -0.4859 0.1356  -0.5271 160 LEU   A O   
1065 C  CB  . LEU   A 140 ? 2.5725 1.6038 2.7480 -0.3890 0.1317  -0.4599 160 LEU   A CB  
1066 C  CG  . LEU   A 140 ? 2.3806 1.5222 2.5486 -0.3714 0.1159  -0.4441 160 LEU   A CG  
1067 C  CD1 . LEU   A 140 ? 2.2861 1.4581 2.4056 -0.3220 0.0896  -0.4515 160 LEU   A CD1 
1068 C  CD2 . LEU   A 140 ? 2.2293 1.4623 2.4607 -0.4084 0.1008  -0.4765 160 LEU   A CD2 
1069 N  N   . ARG   A 141 ? 2.7413 1.5547 2.9599 -0.4477 0.1800  -0.4661 161 ARG   A N   
1070 C  CA  . ARG   A 141 ? 2.7836 1.5420 3.0209 -0.4621 0.1735  -0.4911 161 ARG   A CA  
1071 C  C   . ARG   A 141 ? 2.8698 1.6473 3.1796 -0.5154 0.1868  -0.4934 161 ARG   A C   
1072 O  O   . ARG   A 141 ? 2.9700 1.7378 3.3128 -0.5361 0.1708  -0.5287 161 ARG   A O   
1073 C  CB  . ARG   A 141 ? 2.8756 1.5091 3.0586 -0.4331 0.1937  -0.4611 161 ARG   A CB  
1074 C  CG  . ARG   A 141 ? 3.0251 1.5884 3.2193 -0.4425 0.1874  -0.4861 161 ARG   A CG  
1075 C  CD  . ARG   A 141 ? 3.1224 1.5925 3.2520 -0.3932 0.1864  -0.4763 161 ARG   A CD  
1076 N  NE  . ARG   A 141 ? 3.0923 1.6068 3.1937 -0.3559 0.1541  -0.5126 161 ARG   A NE  
1077 C  CZ  . ARG   A 141 ? 3.0761 1.5419 3.1238 -0.3043 0.1499  -0.5057 161 ARG   A CZ  
1078 N  NH1 . ARG   A 141 ? 3.1979 1.5688 3.2091 -0.2801 0.1714  -0.4628 161 ARG   A NH1 
1079 N  NH2 . ARG   A 141 ? 2.9393 1.4557 2.9693 -0.2740 0.1236  -0.5418 161 ARG   A NH2 
1080 N  N   . ARG   A 142 ? 2.8515 1.6571 3.1871 -0.5373 0.2162  -0.4574 162 ARG   A N   
1081 C  CA  . ARG   A 142 ? 2.8529 1.6860 3.2650 -0.5868 0.2325  -0.4581 162 ARG   A CA  
1082 C  C   . ARG   A 142 ? 2.8188 1.7728 3.2938 -0.6087 0.1962  -0.5041 162 ARG   A C   
1083 O  O   . ARG   A 142 ? 2.8450 1.8158 3.3782 -0.6404 0.1837  -0.5350 162 ARG   A O   
1084 C  CB  . ARG   A 142 ? 2.8640 1.6863 3.2775 -0.5980 0.2798  -0.4023 162 ARG   A CB  
1085 C  CG  . ARG   A 142 ? 2.9667 1.6649 3.3142 -0.5766 0.3168  -0.3523 162 ARG   A CG  
1086 C  CD  . ARG   A 142 ? 3.0239 1.7177 3.3500 -0.5766 0.3596  -0.2965 162 ARG   A CD  
1087 N  NE  . ARG   A 142 ? 3.1897 1.7642 3.4568 -0.5611 0.3978  -0.2461 162 ARG   A NE  
1088 C  CZ  . ARG   A 142 ? 3.2805 1.8236 3.5031 -0.5511 0.4373  -0.1912 162 ARG   A CZ  
1089 N  NH1 . ARG   A 142 ? 3.1775 1.7962 3.4092 -0.5560 0.4461  -0.1792 162 ARG   A NH1 
1090 N  NH2 . ARG   A 142 ? 3.3304 1.7623 3.4934 -0.5334 0.4678  -0.1471 162 ARG   A NH2 
1091 N  N   . GLU   A 143 ? 2.7900 1.8278 3.2525 -0.5906 0.1774  -0.5090 163 GLU   A N   
1092 C  CA  . GLU   A 143 ? 2.7402 1.8936 3.2509 -0.6029 0.1390  -0.5500 163 GLU   A CA  
1093 C  C   . GLU   A 143 ? 2.7433 1.9073 3.2268 -0.5824 0.0931  -0.6001 163 GLU   A C   
1094 O  O   . GLU   A 143 ? 2.6558 1.9109 3.1640 -0.5853 0.0571  -0.6345 163 GLU   A O   
1095 C  CB  . GLU   A 143 ? 2.6678 1.9052 3.1731 -0.5900 0.1376  -0.5337 163 GLU   A CB  
1096 C  CG  . GLU   A 143 ? 2.6765 1.9504 3.2354 -0.6192 0.1720  -0.5003 163 GLU   A CG  
1097 C  CD  . GLU   A 143 ? 2.7389 1.9153 3.2665 -0.6203 0.2254  -0.4468 163 GLU   A CD  
1098 O  OE1 . GLU   A 143 ? 2.7493 1.8463 3.2847 -0.6358 0.2454  -0.4397 163 GLU   A OE1 
1099 O  OE2 . GLU   A 143 ? 2.7843 1.9605 3.2746 -0.6040 0.2471  -0.4107 163 GLU   A OE2 
1100 N  N   . ALA   A 144 ? 2.8061 1.8788 3.2355 -0.5588 0.0941  -0.6038 164 ALA   A N   
1101 C  CA  . ALA   A 144 ? 2.8603 1.9300 3.2601 -0.5393 0.0564  -0.6509 164 ALA   A CA  
1102 C  C   . ALA   A 144 ? 2.9362 1.9446 3.3628 -0.5646 0.0528  -0.6760 164 ALA   A C   
1103 O  O   . ALA   A 144 ? 2.9934 2.0369 3.4316 -0.5707 0.0176  -0.7225 164 ALA   A O   
1104 C  CB  . ALA   A 144 ? 2.8042 1.8200 3.1249 -0.4902 0.0573  -0.6432 164 ALA   A CB  
1105 N  N   . GLU   A 145 ? 3.0460 1.9597 3.4782 -0.5782 0.0887  -0.6454 165 GLU   A N   
1106 C  CA  . GLU   A 145 ? 3.0994 1.9532 3.5651 -0.6075 0.0891  -0.6664 165 GLU   A CA  
1107 C  C   . GLU   A 145 ? 2.9922 1.9220 3.5443 -0.6543 0.0785  -0.6884 165 GLU   A C   
1108 O  O   . GLU   A 145 ? 3.0783 1.9920 3.6618 -0.6772 0.0603  -0.7257 165 GLU   A O   
1109 C  CB  . GLU   A 145 ? 3.1199 1.8597 3.5738 -0.6117 0.1338  -0.6216 165 GLU   A CB  
1110 C  CG  . GLU   A 145 ? 3.2417 1.8913 3.6145 -0.5642 0.1372  -0.6091 165 GLU   A CG  
1111 C  CD  . GLU   A 145 ? 3.2944 1.8288 3.6501 -0.5645 0.1786  -0.5627 165 GLU   A CD  
1112 O  OE1 . GLU   A 145 ? 3.3072 1.8383 3.7016 -0.5959 0.2127  -0.5280 165 GLU   A OE1 
1113 O  OE2 . GLU   A 145 ? 3.3542 1.8016 3.6560 -0.5309 0.1777  -0.5601 165 GLU   A OE2 
1114 N  N   . THR   A 146 ? 2.9648 1.9768 3.5571 -0.6679 0.0893  -0.6669 166 THR   A N   
1115 C  CA  . THR   A 146 ? 2.8724 1.9813 3.5449 -0.7023 0.0706  -0.6918 166 THR   A CA  
1116 C  C   . THR   A 146 ? 2.9750 2.1829 3.6261 -0.6772 0.0248  -0.7231 166 THR   A C   
1117 O  O   . THR   A 146 ? 2.9064 2.1494 3.5182 -0.6489 0.0276  -0.7014 166 THR   A O   
1118 C  CB  . THR   A 146 ? 2.7973 1.9415 3.5272 -0.7287 0.1101  -0.6501 166 THR   A CB  
1119 O  OG1 . THR   A 146 ? 2.6793 1.8934 3.3844 -0.7044 0.1083  -0.6303 166 THR   A OG1 
1120 C  CG2 . THR   A 146 ? 2.7993 1.8344 3.5136 -0.7362 0.1636  -0.6027 166 THR   A CG2 
1121 N  N   . GLY   A 147 ? 3.1715 2.4213 3.8452 -0.6868 -0.0169 -0.7730 167 GLY   A N   
1122 C  CA  . GLY   A 147 ? 3.2178 2.5536 3.8622 -0.6604 -0.0619 -0.8037 167 GLY   A CA  
1123 C  C   . GLY   A 147 ? 3.1117 2.5583 3.7986 -0.6647 -0.0670 -0.7897 167 GLY   A C   
1124 O  O   . GLY   A 147 ? 3.0621 2.5893 3.7918 -0.6760 -0.1008 -0.8196 167 GLY   A O   
1125 N  N   . LYS   A 148 ? 2.7931 2.2428 3.4664 -0.6538 -0.0347 -0.7446 168 LYS   A N   
1126 C  CA  . LYS   A 148 ? 2.7108 2.2574 3.4229 -0.6570 -0.0330 -0.7260 168 LYS   A CA  
1127 C  C   . LYS   A 148 ? 2.7335 2.3087 3.3759 -0.6152 -0.0407 -0.7121 168 LYS   A C   
1128 O  O   . LYS   A 148 ? 2.5700 2.0766 3.1572 -0.5956 -0.0150 -0.6857 168 LYS   A O   
1129 C  CB  . LYS   A 148 ? 2.5980 2.1251 3.3642 -0.6865 0.0180  -0.6826 168 LYS   A CB  
1130 C  CG  . LYS   A 148 ? 2.4532 2.0793 3.2655 -0.6913 0.0232  -0.6638 168 LYS   A CG  
1131 C  CD  . LYS   A 148 ? 2.2904 1.8903 3.1496 -0.7190 0.0787  -0.6205 168 LYS   A CD  
1132 C  CE  . LYS   A 148 ? 2.0632 1.7602 2.9656 -0.7206 0.0861  -0.6018 168 LYS   A CE  
1133 N  NZ  . LYS   A 148 ? 1.9829 1.7824 2.9548 -0.7320 0.0458  -0.6385 168 LYS   A NZ  
1134 N  N   . PRO   A 149 ? 2.8087 2.4804 3.4497 -0.5989 -0.0757 -0.7286 169 PRO   A N   
1135 C  CA  . PRO   A 149 ? 2.7582 2.4598 3.3356 -0.5602 -0.0817 -0.7146 169 PRO   A CA  
1136 C  C   . PRO   A 149 ? 2.7369 2.4258 3.3169 -0.5617 -0.0394 -0.6664 169 PRO   A C   
1137 O  O   . PRO   A 149 ? 2.7575 2.4563 3.3980 -0.5910 -0.0117 -0.6438 169 PRO   A O   
1138 C  CB  . PRO   A 149 ? 2.7419 2.5533 3.3362 -0.5509 -0.1229 -0.7360 169 PRO   A CB  
1139 C  CG  . PRO   A 149 ? 2.6811 2.5001 3.3164 -0.5728 -0.1505 -0.7752 169 PRO   A CG  
1140 C  CD  . PRO   A 149 ? 2.7393 2.4922 3.4310 -0.6121 -0.1147 -0.7633 169 PRO   A CD  
1141 N  N   . VAL   A 150 ? 2.3864 2.0526 2.8981 -0.5287 -0.0335 -0.6513 170 VAL   A N   
1142 C  CA  . VAL   A 150 ? 2.2437 1.8748 2.7393 -0.5253 0.0064  -0.6071 170 VAL   A CA  
1143 C  C   . VAL   A 150 ? 2.0912 1.8068 2.5676 -0.5005 -0.0045 -0.5891 170 VAL   A C   
1144 O  O   . VAL   A 150 ? 2.0721 1.8296 2.5046 -0.4686 -0.0360 -0.6053 170 VAL   A O   
1145 C  CB  . VAL   A 150 ? 2.2721 1.8004 2.7004 -0.5018 0.0237  -0.5960 170 VAL   A CB  
1146 C  CG1 . VAL   A 150 ? 2.0807 1.5899 2.4651 -0.4766 0.0541  -0.5336 170 VAL   A CG1 
1147 C  CG2 . VAL   A 150 ? 2.3320 1.7714 2.7758 -0.5229 0.0394  -0.6005 170 VAL   A CG2 
1148 N  N   . THR   A 151 ? 2.0058 1.7459 2.5077 -0.5094 0.0229  -0.5488 171 THR   A N   
1149 C  CA  . THR   A 151 ? 1.9375 1.7376 2.4040 -0.4765 0.0204  -0.5144 171 THR   A CA  
1150 C  C   . THR   A 151 ? 1.9422 1.6779 2.3268 -0.4389 0.0367  -0.4767 171 THR   A C   
1151 O  O   . THR   A 151 ? 1.9921 1.6590 2.3641 -0.4437 0.0712  -0.4436 171 THR   A O   
1152 C  CB  . THR   A 151 ? 1.9218 1.7664 2.4435 -0.4982 0.0453  -0.4877 171 THR   A CB  
1153 O  OG1 . THR   A 151 ? 1.9480 1.7138 2.4802 -0.5205 0.0906  -0.4599 171 THR   A OG1 
1154 C  CG2 . THR   A 151 ? 1.8051 1.7301 2.4156 -0.5306 0.0234  -0.5269 171 THR   A CG2 
1155 N  N   . LEU   A 152 ? 2.0419 1.7999 2.3715 -0.4004 0.0122  -0.4815 172 LEU   A N   
1156 C  CA  . LEU   A 152 ? 2.0826 1.7838 2.3440 -0.3642 0.0223  -0.4539 172 LEU   A CA  
1157 C  C   . LEU   A 152 ? 2.1179 1.8202 2.3588 -0.3499 0.0451  -0.4030 172 LEU   A C   
1158 O  O   . LEU   A 152 ? 2.1794 1.8096 2.3867 -0.3392 0.0669  -0.3743 172 LEU   A O   
1159 C  CB  . LEU   A 152 ? 1.9896 1.7238 2.2072 -0.3288 -0.0060 -0.4720 172 LEU   A CB  
1160 C  CG  . LEU   A 152 ? 2.0089 1.7272 2.2265 -0.3341 -0.0276 -0.5228 172 LEU   A CG  
1161 C  CD1 . LEU   A 152 ? 1.9620 1.7196 2.1321 -0.2974 -0.0503 -0.5366 172 LEU   A CD1 
1162 C  CD2 . LEU   A 152 ? 2.0386 1.6557 2.2446 -0.3389 -0.0107 -0.5277 172 LEU   A CD2 
1163 N  N   . LYS   A 153 ? 2.0570 1.8379 2.3145 -0.3474 0.0388  -0.3922 173 LYS   A N   
1164 C  CA  . LYS   A 153 ? 1.9854 1.7706 2.2191 -0.3309 0.0572  -0.3481 173 LYS   A CA  
1165 C  C   . LYS   A 153 ? 2.0000 1.7309 2.2474 -0.3537 0.0943  -0.3217 173 LYS   A C   
1166 O  O   . LYS   A 153 ? 1.9839 1.6857 2.1914 -0.3353 0.1124  -0.2842 173 LYS   A O   
1167 C  CB  . LYS   A 153 ? 1.9165 1.7949 2.1716 -0.3262 0.0437  -0.3459 173 LYS   A CB  
1168 C  CG  . LYS   A 153 ? 1.7157 1.6084 1.9270 -0.2929 0.0457  -0.3121 173 LYS   A CG  
1169 C  CD  . LYS   A 153 ? 1.7327 1.7133 1.9597 -0.2835 0.0260  -0.3171 173 LYS   A CD  
1170 C  CE  . LYS   A 153 ? 1.7563 1.7481 1.9427 -0.2514 0.0264  -0.2873 173 LYS   A CE  
1171 N  NZ  . LYS   A 153 ? 1.5412 1.6078 1.7341 -0.2375 0.0056  -0.2933 173 LYS   A NZ  
1172 N  N   . ASP   A 154 ? 1.9320 1.6470 2.2340 -0.3931 0.1068  -0.3409 174 ASP   A N   
1173 C  CA  . ASP   A 154 ? 1.9802 1.6328 2.2936 -0.4163 0.1485  -0.3144 174 ASP   A CA  
1174 C  C   . ASP   A 154 ? 2.0370 1.5828 2.2899 -0.3991 0.1629  -0.2952 174 ASP   A C   
1175 O  O   . ASP   A 154 ? 2.0698 1.5669 2.2776 -0.3841 0.1881  -0.2545 174 ASP   A O   
1176 C  CB  . ASP   A 154 ? 2.0382 1.7017 2.4357 -0.4657 0.1586  -0.3429 174 ASP   A CB  
1177 C  CG  . ASP   A 154 ? 2.0141 1.7757 2.4779 -0.4839 0.1564  -0.3495 174 ASP   A CG  
1178 O  OD1 . ASP   A 154 ? 1.7672 1.5764 2.2061 -0.4588 0.1541  -0.3263 174 ASP   A OD1 
1179 O  OD2 . ASP   A 154 ? 2.0147 1.8058 2.5592 -0.5229 0.1561  -0.3795 174 ASP   A OD2 
1180 N  N   . VAL   A 155 ? 2.2197 1.7264 2.4676 -0.3982 0.1459  -0.3248 175 VAL   A N   
1181 C  CA  . VAL   A 155 ? 2.2158 1.6192 2.4110 -0.3800 0.1577  -0.3094 175 VAL   A CA  
1182 C  C   . VAL   A 155 ? 2.3466 1.7487 2.4741 -0.3291 0.1396  -0.2912 175 VAL   A C   
1183 O  O   . VAL   A 155 ? 2.3674 1.6926 2.4440 -0.3060 0.1520  -0.2637 175 VAL   A O   
1184 C  CB  . VAL   A 155 ? 2.1260 1.4848 2.3454 -0.3984 0.1482  -0.3506 175 VAL   A CB  
1185 C  CG1 . VAL   A 155 ? 2.1578 1.5737 2.3726 -0.3792 0.1072  -0.3903 175 VAL   A CG1 
1186 C  CG2 . VAL   A 155 ? 2.2684 1.5086 2.4429 -0.3856 0.1677  -0.3322 175 VAL   A CG2 
1187 N  N   . PHE   A 156 ? 2.5009 1.9858 2.6283 -0.3104 0.1109  -0.3051 176 PHE   A N   
1188 C  CA  . PHE   A 156 ? 2.5562 2.0492 2.6317 -0.2658 0.0967  -0.2863 176 PHE   A CA  
1189 C  C   . PHE   A 156 ? 2.5045 2.0037 2.5552 -0.2545 0.1116  -0.2449 176 PHE   A C   
1190 O  O   . PHE   A 156 ? 2.5386 1.9920 2.5391 -0.2240 0.1135  -0.2185 176 PHE   A O   
1191 C  CB  . PHE   A 156 ? 2.4418 2.0171 2.5257 -0.2514 0.0664  -0.3122 176 PHE   A CB  
1192 C  CG  . PHE   A 156 ? 2.3587 1.9195 2.4436 -0.2477 0.0499  -0.3505 176 PHE   A CG  
1193 C  CD1 . PHE   A 156 ? 2.4894 1.9637 2.5549 -0.2415 0.0578  -0.3547 176 PHE   A CD1 
1194 C  CD2 . PHE   A 156 ? 2.2980 1.9277 2.3976 -0.2475 0.0267  -0.3822 176 PHE   A CD2 
1195 C  CE1 . PHE   A 156 ? 2.5147 1.9730 2.5788 -0.2361 0.0438  -0.3924 176 PHE   A CE1 
1196 C  CE2 . PHE   A 156 ? 2.3800 1.9939 2.4724 -0.2416 0.0127  -0.4191 176 PHE   A CE2 
1197 C  CZ  . PHE   A 156 ? 2.5415 2.0702 2.6176 -0.2363 0.0216  -0.4254 176 PHE   A CZ  
1198 N  N   . GLY   A 157 ? 2.3162 1.8732 2.4014 -0.2765 0.1206  -0.2406 177 GLY   A N   
1199 C  CA  . GLY   A 157 ? 2.2761 1.8356 2.3363 -0.2668 0.1378  -0.2038 177 GLY   A CA  
1200 C  C   . GLY   A 157 ? 2.3103 1.7773 2.3373 -0.2707 0.1710  -0.1733 177 GLY   A C   
1201 O  O   . GLY   A 157 ? 2.3054 1.7404 2.2774 -0.2443 0.1778  -0.1413 177 GLY   A O   
1202 N  N   . ALA   A 158 ? 2.2944 1.7144 2.3523 -0.3034 0.1918  -0.1831 178 ALA   A N   
1203 C  CA  . ALA   A 158 ? 2.3879 1.7059 2.4088 -0.3058 0.2257  -0.1529 178 ALA   A CA  
1204 C  C   . ALA   A 158 ? 2.3872 1.6356 2.3388 -0.2637 0.2110  -0.1392 178 ALA   A C   
1205 O  O   . ALA   A 158 ? 2.4748 1.6568 2.3658 -0.2427 0.2279  -0.1027 178 ALA   A O   
1206 C  CB  . ALA   A 158 ? 2.4048 1.6827 2.4791 -0.3497 0.2479  -0.1713 178 ALA   A CB  
1207 N  N   . TYR   A 159 ? 2.3075 1.5714 2.2658 -0.2484 0.1793  -0.1686 179 TYR   A N   
1208 C  CA  . TYR   A 159 ? 2.3158 1.5296 2.2191 -0.2049 0.1617  -0.1591 179 TYR   A CA  
1209 C  C   . TYR   A 159 ? 2.3008 1.5573 2.1672 -0.1686 0.1434  -0.1393 179 TYR   A C   
1210 O  O   . TYR   A 159 ? 2.3402 1.5415 2.1491 -0.1375 0.1439  -0.1106 179 TYR   A O   
1211 C  CB  . TYR   A 159 ? 2.3360 1.5618 2.2617 -0.1985 0.1365  -0.1981 179 TYR   A CB  
1212 C  CG  . TYR   A 159 ? 2.3212 1.5395 2.2085 -0.1502 0.1114  -0.1947 179 TYR   A CG  
1213 C  CD1 . TYR   A 159 ? 2.3520 1.4793 2.1965 -0.1233 0.1145  -0.1785 179 TYR   A CD1 
1214 C  CD2 . TYR   A 159 ? 2.2266 1.5289 2.1240 -0.1311 0.0857  -0.2072 179 TYR   A CD2 
1215 C  CE1 . TYR   A 159 ? 2.3317 1.4590 2.1509 -0.0781 0.0900  -0.1774 179 TYR   A CE1 
1216 C  CE2 . TYR   A 159 ? 2.1553 1.4563 2.0293 -0.0894 0.0650  -0.2053 179 TYR   A CE2 
1217 C  CZ  . TYR   A 159 ? 2.2352 1.4521 2.0734 -0.0628 0.0660  -0.1917 179 TYR   A CZ  
1218 O  OH  . TYR   A 159 ? 2.2135 1.4361 2.0381 -0.0203 0.0438  -0.1920 179 TYR   A OH  
1219 N  N   . SER   A 160 ? 2.1765 1.5290 2.0745 -0.1714 0.1256  -0.1552 180 SER   A N   
1220 C  CA  . SER   A 160 ? 2.2372 1.6331 2.1089 -0.1392 0.1061  -0.1418 180 SER   A CA  
1221 C  C   . SER   A 160 ? 2.2408 1.6053 2.0675 -0.1309 0.1238  -0.1051 180 SER   A C   
1222 O  O   . SER   A 160 ? 2.2043 1.5492 1.9836 -0.0954 0.1094  -0.0874 180 SER   A O   
1223 C  CB  . SER   A 160 ? 2.1472 1.6446 2.0623 -0.1490 0.0906  -0.1626 180 SER   A CB  
1224 O  OG  . SER   A 160 ? 2.1163 1.6401 2.0641 -0.1555 0.0758  -0.1966 180 SER   A OG  
1225 N  N   . MET   A 161 ? 2.2939 1.6546 2.1355 -0.1624 0.1551  -0.0949 181 MET   A N   
1226 C  CA  . MET   A 161 ? 2.3485 1.6732 2.1411 -0.1547 0.1784  -0.0595 181 MET   A CA  
1227 C  C   . MET   A 161 ? 2.4092 1.6283 2.1323 -0.1296 0.1866  -0.0330 181 MET   A C   
1228 O  O   . MET   A 161 ? 2.3981 1.5893 2.0574 -0.0975 0.1815  -0.0081 181 MET   A O   
1229 C  CB  . MET   A 161 ? 2.3726 1.7104 2.2031 -0.1956 0.2166  -0.0549 181 MET   A CB  
1230 C  CG  . MET   A 161 ? 2.4044 1.6900 2.1803 -0.1903 0.2517  -0.0168 181 MET   A CG  
1231 S  SD  . MET   A 161 ? 2.6648 1.9936 2.3911 -0.1540 0.2337  -0.0021 181 MET   A SD  
1232 C  CE  . MET   A 161 ? 2.4010 1.8549 2.2137 -0.1767 0.2182  -0.0337 181 MET   A CE  
1233 N  N   . ASP   A 162 ? 2.4469 1.6035 2.1788 -0.1417 0.1972  -0.0390 182 ASP   A N   
1234 C  CA  . ASP   A 162 ? 2.5587 1.6082 2.2235 -0.1153 0.2046  -0.0129 182 ASP   A CA  
1235 C  C   . ASP   A 162 ? 2.5319 1.5804 2.1543 -0.0644 0.1639  -0.0114 182 ASP   A C   
1236 O  O   . ASP   A 162 ? 2.5948 1.5748 2.1449 -0.0306 0.1623  0.0175  182 ASP   A O   
1237 C  CB  . ASP   A 162 ? 2.6647 1.6523 2.3559 -0.1367 0.2187  -0.0259 182 ASP   A CB  
1238 C  CG  . ASP   A 162 ? 2.7686 1.7371 2.4981 -0.1865 0.2631  -0.0222 182 ASP   A CG  
1239 O  OD1 . ASP   A 162 ? 2.8186 1.8264 2.5555 -0.2028 0.2842  -0.0088 182 ASP   A OD1 
1240 O  OD2 . ASP   A 162 ? 2.8384 1.7532 2.5947 -0.2095 0.2776  -0.0339 182 ASP   A OD2 
1241 N  N   . VAL   A 163 ? 2.4651 1.5892 2.1320 -0.0573 0.1308  -0.0423 183 VAL   A N   
1242 C  CA  . VAL   A 163 ? 2.4358 1.5681 2.0793 -0.0119 0.0931  -0.0446 183 VAL   A CA  
1243 C  C   . VAL   A 163 ? 2.4762 1.6376 2.0819 0.0111  0.0797  -0.0266 183 VAL   A C   
1244 O  O   . VAL   A 163 ? 2.5452 1.6659 2.0969 0.0508  0.0604  -0.0100 183 VAL   A O   
1245 C  CB  . VAL   A 163 ? 2.3675 1.5730 2.0721 -0.0132 0.0685  -0.0818 183 VAL   A CB  
1246 C  CG1 . VAL   A 163 ? 2.3224 1.5391 2.0144 0.0322  0.0333  -0.0848 183 VAL   A CG1 
1247 C  CG2 . VAL   A 163 ? 2.2861 1.4596 2.0225 -0.0353 0.0807  -0.1035 183 VAL   A CG2 
1248 N  N   . ILE   A 164 ? 2.4469 1.6778 2.0800 -0.0118 0.0877  -0.0311 184 ILE   A N   
1249 C  CA  . ILE   A 164 ? 2.4268 1.6961 2.0341 0.0097  0.0702  -0.0223 184 ILE   A CA  
1250 C  C   . ILE   A 164 ? 2.5062 1.7045 2.0328 0.0257  0.0871  0.0121  184 ILE   A C   
1251 O  O   . ILE   A 164 ? 2.5356 1.7278 2.0144 0.0602  0.0632  0.0217  184 ILE   A O   
1252 C  CB  . ILE   A 164 ? 2.2946 1.6562 1.9554 -0.0172 0.0740  -0.0378 184 ILE   A CB  
1253 C  CG1 . ILE   A 164 ? 2.1848 1.6148 1.8689 0.0040  0.0376  -0.0543 184 ILE   A CG1 
1254 C  CG2 . ILE   A 164 ? 2.3193 1.6768 1.9510 -0.0283 0.1008  -0.0170 184 ILE   A CG2 
1255 C  CD1 . ILE   A 164 ? 2.2590 1.6607 1.8912 0.0453  0.0110  -0.0418 184 ILE   A CD1 
1256 N  N   . THR   A 165 ? 2.4544 1.5961 1.9634 0.0016  0.1289  0.0305  185 THR   A N   
1257 C  CA  . THR   A 165 ? 2.5440 1.6149 1.9695 0.0166  0.1522  0.0660  185 THR   A CA  
1258 C  C   . THR   A 165 ? 2.6967 1.6823 2.0454 0.0619  0.1321  0.0850  185 THR   A C   
1259 O  O   . THR   A 165 ? 2.7726 1.7148 2.0395 0.0919  0.1299  0.1093  185 THR   A O   
1260 C  CB  . THR   A 165 ? 2.6230 1.6522 2.0555 -0.0224 0.2073  0.0822  185 THR   A CB  
1261 O  OG1 . THR   A 165 ? 2.6603 1.6454 2.1239 -0.0393 0.2163  0.0745  185 THR   A OG1 
1262 C  CG2 . THR   A 165 ? 2.4802 1.5970 1.9831 -0.0614 0.2256  0.0661  185 THR   A CG2 
1263 N  N   . SER   A 166 ? 2.7188 1.6792 2.0897 0.0704  0.1156  0.0733  186 SER   A N   
1264 C  CA  . SER   A 166 ? 2.8534 1.7331 2.1580 0.1160  0.0943  0.0903  186 SER   A CA  
1265 C  C   . SER   A 166 ? 2.8347 1.7651 2.1515 0.1553  0.0385  0.0707  186 SER   A C   
1266 O  O   . SER   A 166 ? 2.9046 1.7928 2.1544 0.2000  0.0122  0.0863  186 SER   A O   
1267 C  CB  . SER   A 166 ? 2.9522 1.7637 2.2716 0.1060  0.1114  0.0904  186 SER   A CB  
1268 O  OG  . SER   A 166 ? 2.9303 1.7973 2.3382 0.0602  0.1263  0.0615  186 SER   A OG  
1269 N  N   . THR   A 167 ? 2.7922 1.8126 2.1938 0.1401  0.0202  0.0366  187 THR   A N   
1270 C  CA  . THR   A 167 ? 2.7019 1.7767 2.1287 0.1729  -0.0277 0.0170  187 THR   A CA  
1271 C  C   . THR   A 167 ? 2.7415 1.8462 2.1326 0.1940  -0.0509 0.0230  187 THR   A C   
1272 O  O   . THR   A 167 ? 2.8373 1.9635 2.2302 0.2295  -0.0932 0.0133  187 THR   A O   
1273 C  CB  . THR   A 167 ? 2.6321 1.7973 2.1528 0.1485  -0.0339 -0.0176 187 THR   A CB  
1274 O  OG1 . THR   A 167 ? 2.5656 1.7812 2.1171 0.1064  -0.0075 -0.0226 187 THR   A OG1 
1275 C  CG2 . THR   A 167 ? 2.6181 1.7533 2.1705 0.1432  -0.0262 -0.0308 187 THR   A CG2 
1276 N  N   . SER   A 168 ? 2.8195 1.9269 2.1818 0.1734  -0.0245 0.0366  188 SER   A N   
1277 C  CA  . SER   A 168 ? 2.8035 1.9343 2.1271 0.1923  -0.0437 0.0402  188 SER   A CA  
1278 C  C   . SER   A 168 ? 2.7938 1.8388 2.0095 0.2126  -0.0275 0.0736  188 SER   A C   
1279 O  O   . SER   A 168 ? 2.8839 1.9210 2.0443 0.2472  -0.0577 0.0770  188 SER   A O   
1280 C  CB  . SER   A 168 ? 2.6624 1.8763 2.0401 0.1570  -0.0290 0.0254  188 SER   A CB  
1281 O  OG  . SER   A 168 ? 2.5484 1.8412 2.0156 0.1431  -0.0458 -0.0038 188 SER   A OG  
1282 N  N   . PHE   A 169 ? 2.8395 1.8186 2.0234 0.1921  0.0200  0.0978  189 PHE   A N   
1283 C  CA  . PHE   A 169 ? 2.8243 1.7151 1.9010 0.2094  0.0456  0.1338  189 PHE   A CA  
1284 C  C   . PHE   A 169 ? 2.9282 1.7131 1.9516 0.2257  0.0597  0.1597  189 PHE   A C   
1285 O  O   . PHE   A 169 ? 2.9783 1.6981 1.9172 0.2734  0.0343  0.1774  189 PHE   A O   
1286 C  CB  . PHE   A 169 ? 2.7436 1.6475 1.8258 0.1690  0.0997  0.1446  189 PHE   A CB  
1287 C  CG  . PHE   A 169 ? 2.5362 1.5457 1.6856 0.1476  0.0907  0.1180  189 PHE   A CG  
1288 C  CD1 . PHE   A 169 ? 2.4871 1.5732 1.7422 0.1099  0.0940  0.0918  189 PHE   A CD1 
1289 C  CD2 . PHE   A 169 ? 2.5629 1.5903 1.6649 0.1671  0.0787  0.1189  189 PHE   A CD2 
1290 C  CE1 . PHE   A 169 ? 2.3726 1.5499 1.6844 0.0932  0.0861  0.0703  189 PHE   A CE1 
1291 C  CE2 . PHE   A 169 ? 2.4842 1.6024 1.6476 0.1486  0.0717  0.0955  189 PHE   A CE2 
1292 C  CZ  . PHE   A 169 ? 2.3700 1.5625 1.6382 0.1121  0.0759  0.0729  189 PHE   A CZ  
1293 N  N   . GLY   A 170 ? 2.9213 1.6847 1.9913 0.1889  0.0975  0.1616  190 GLY   A N   
1294 C  CA  . GLY   A 170 ? 3.0582 1.7172 2.0850 0.2019  0.1128  0.1848  190 GLY   A CA  
1295 C  C   . GLY   A 170 ? 3.1431 1.7451 2.1705 0.1593  0.1782  0.2064  190 GLY   A C   
1296 O  O   . GLY   A 170 ? 3.2899 1.7934 2.2777 0.1660  0.1994  0.2297  190 GLY   A O   
1297 N  N   . VAL   A 171 ? 3.1516 1.8145 2.2287 0.1154  0.2109  0.1986  191 VAL   A N   
1298 C  CA  . VAL   A 171 ? 3.2726 1.8924 2.3622 0.0716  0.2751  0.2173  191 VAL   A CA  
1299 C  C   . VAL   A 171 ? 3.2254 1.8593 2.4105 0.0330  0.2824  0.1922  191 VAL   A C   
1300 O  O   . VAL   A 171 ? 3.1245 1.8515 2.3951 0.0165  0.2545  0.1539  191 VAL   A O   
1301 C  CB  . VAL   A 171 ? 3.2740 1.9594 2.3869 0.0419  0.3057  0.2164  191 VAL   A CB  
1302 C  CG1 . VAL   A 171 ? 3.3632 2.0092 2.5005 -0.0047 0.3740  0.2348  191 VAL   A CG1 
1303 C  CG2 . VAL   A 171 ? 3.3325 1.9995 2.3442 0.0830  0.2968  0.2377  191 VAL   A CG2 
1304 N  N   . ASN   A 172 ? 3.2847 1.8220 2.4520 0.0190  0.3208  0.2138  192 ASN   A N   
1305 C  CA  . ASN   A 172 ? 3.3277 1.8587 2.5753 -0.0156 0.3289  0.1904  192 ASN   A CA  
1306 C  C   . ASN   A 172 ? 3.3735 1.9073 2.6785 -0.0753 0.3868  0.1928  192 ASN   A C   
1307 O  O   . ASN   A 172 ? 3.4390 1.8927 2.6925 -0.0830 0.4372  0.2308  192 ASN   A O   
1308 C  CB  . ASN   A 172 ? 3.3838 1.7983 2.5773 0.0137  0.3259  0.2089  192 ASN   A CB  
1309 C  CG  . ASN   A 172 ? 3.4812 1.7768 2.5641 0.0355  0.3638  0.2625  192 ASN   A CG  
1310 O  OD1 . ASN   A 172 ? 3.5179 1.7794 2.5071 0.0884  0.3385  0.2849  192 ASN   A OD1 
1311 N  ND2 . ASN   A 172 ? 3.5375 1.7686 2.6303 -0.0050 0.4249  0.2829  192 ASN   A ND2 
1312 N  N   . ILE   A 173 ? 3.3069 1.9329 2.7188 -0.1164 0.3796  0.1523  193 ILE   A N   
1313 C  CA  . ILE   A 173 ? 3.3090 1.9581 2.7966 -0.1753 0.4260  0.1455  193 ILE   A CA  
1314 C  C   . ILE   A 173 ? 3.2252 1.9244 2.8136 -0.2087 0.4061  0.0984  193 ILE   A C   
1315 O  O   . ILE   A 173 ? 3.1224 1.9061 2.7465 -0.1979 0.3599  0.0647  193 ILE   A O   
1316 C  CB  . ILE   A 173 ? 3.3353 2.0748 2.8453 -0.1894 0.4387  0.1455  193 ILE   A CB  
1317 C  CG1 . ILE   A 173 ? 3.3769 2.0531 2.7878 -0.1656 0.4741  0.1931  193 ILE   A CG1 
1318 C  CG2 . ILE   A 173 ? 3.3278 2.1255 2.9468 -0.2501 0.4701  0.1231  193 ILE   A CG2 
1319 C  CD1 . ILE   A 173 ? 3.3692 2.1278 2.7954 -0.1744 0.4878  0.1931  193 ILE   A CD1 
1320 N  N   . ASP   A 174 ? 3.3160 1.9598 2.9481 -0.2490 0.4418  0.0956  194 ASP   A N   
1321 C  CA  . ASP   A 174 ? 3.1980 1.8929 2.9313 -0.2884 0.4278  0.0475  194 ASP   A CA  
1322 C  C   . ASP   A 174 ? 3.1920 2.0024 3.0078 -0.3266 0.4337  0.0253  194 ASP   A C   
1323 O  O   . ASP   A 174 ? 3.2223 2.0278 3.0666 -0.3609 0.4809  0.0417  194 ASP   A O   
1324 C  CB  . ASP   A 174 ? 3.0929 1.6888 2.8502 -0.3216 0.4646  0.0502  194 ASP   A CB  
1325 C  CG  . ASP   A 174 ? 3.0191 1.6568 2.8718 -0.3577 0.4438  -0.0042 194 ASP   A CG  
1326 O  OD1 . ASP   A 174 ? 2.9529 1.6894 2.8404 -0.3499 0.3987  -0.0412 194 ASP   A OD1 
1327 O  OD2 . ASP   A 174 ? 2.8617 1.4309 2.7524 -0.3932 0.4725  -0.0105 194 ASP   A OD2 
1328 N  N   . SER   A 175 ? 3.3422 2.2556 3.1986 -0.3202 0.3878  -0.0113 195 SER   A N   
1329 C  CA  . SER   A 175 ? 3.2554 2.2825 3.1808 -0.3464 0.3860  -0.0307 195 SER   A CA  
1330 C  C   . SER   A 175 ? 3.2191 2.2784 3.2483 -0.4027 0.4017  -0.0629 195 SER   A C   
1331 O  O   . SER   A 175 ? 3.0824 2.2403 3.1787 -0.4182 0.3740  -0.0999 195 SER   A O   
1332 C  CB  . SER   A 175 ? 3.1241 2.2422 3.0503 -0.3174 0.3327  -0.0554 195 SER   A CB  
1333 O  OG  . SER   A 175 ? 3.1438 2.2490 2.9887 -0.2716 0.3215  -0.0264 195 SER   A OG  
1334 N  N   . LEU   A 176 ? 3.0808 2.0563 3.1251 -0.4335 0.4448  -0.0500 196 LEU   A N   
1335 C  CA  . LEU   A 176 ? 2.9460 1.9527 3.0957 -0.4919 0.4692  -0.0749 196 LEU   A CA  
1336 C  C   . LEU   A 176 ? 3.0506 2.0310 3.2115 -0.5179 0.5329  -0.0379 196 LEU   A C   
1337 O  O   . LEU   A 176 ? 2.8819 1.9165 3.1412 -0.5650 0.5548  -0.0562 196 LEU   A O   
1338 C  CB  . LEU   A 176 ? 2.7588 1.6949 2.9414 -0.5162 0.4671  -0.1012 196 LEU   A CB  
1339 C  CG  . LEU   A 176 ? 2.5609 1.5355 2.8644 -0.5778 0.4780  -0.1411 196 LEU   A CG  
1340 C  CD1 . LEU   A 176 ? 2.3514 1.4664 2.7240 -0.5860 0.4353  -0.1841 196 LEU   A CD1 
1341 C  CD2 . LEU   A 176 ? 2.5760 1.4832 2.8957 -0.5890 0.4655  -0.1668 196 LEU   A CD2 
1342 N  N   . ASN   A 177 ? 3.2657 2.1670 3.3278 -0.4864 0.5625  0.0130  197 ASN   A N   
1343 C  CA  . ASN   A 177 ? 3.2671 2.1462 3.3189 -0.5007 0.6246  0.0532  197 ASN   A CA  
1344 C  C   . ASN   A 177 ? 3.2544 2.2404 3.3085 -0.4845 0.6132  0.0535  197 ASN   A C   
1345 O  O   . ASN   A 177 ? 3.1563 2.2459 3.2619 -0.4831 0.5656  0.0152  197 ASN   A O   
1346 C  CB  . ASN   A 177 ? 3.3782 2.1210 3.3108 -0.4693 0.6589  0.1071  197 ASN   A CB  
1347 C  CG  . ASN   A 177 ? 3.4090 2.1331 3.2293 -0.4036 0.6123  0.1206  197 ASN   A CG  
1348 O  OD1 . ASN   A 177 ? 3.4774 2.2816 3.2794 -0.3778 0.5838  0.1158  197 ASN   A OD1 
1349 N  ND2 . ASN   A 177 ? 3.3860 2.0027 3.1341 -0.3761 0.6048  0.1374  197 ASN   A ND2 
1350 N  N   . ASN   A 178 ? 3.5735 2.5313 3.5686 -0.4707 0.6572  0.0961  198 ASN   A N   
1351 C  CA  . ASN   A 178 ? 3.5155 2.5630 3.5067 -0.4538 0.6526  0.0989  198 ASN   A CA  
1352 C  C   . ASN   A 178 ? 3.5612 2.6244 3.4659 -0.3973 0.5963  0.0985  198 ASN   A C   
1353 O  O   . ASN   A 178 ? 3.6157 2.5936 3.4089 -0.3577 0.5990  0.1320  198 ASN   A O   
1354 C  CB  . ASN   A 178 ? 3.4778 2.4806 3.4270 -0.4561 0.7229  0.1446  198 ASN   A CB  
1355 C  CG  . ASN   A 178 ? 3.6204 2.4824 3.4412 -0.4250 0.7504  0.1925  198 ASN   A CG  
1356 O  OD1 . ASN   A 178 ? 3.6416 2.4254 3.4389 -0.4222 0.7372  0.1928  198 ASN   A OD1 
1357 N  ND2 . ASN   A 178 ? 3.6744 2.5015 3.4075 -0.3988 0.7881  0.2329  198 ASN   A ND2 
1358 N  N   . PRO   A 179 ? 3.1994 2.3670 3.1507 -0.3908 0.5447  0.0622  199 PRO   A N   
1359 C  CA  . PRO   A 179 ? 3.0927 2.2776 2.9704 -0.3400 0.4950  0.0621  199 PRO   A CA  
1360 C  C   . PRO   A 179 ? 3.0423 2.2747 2.8872 -0.3188 0.5036  0.0779  199 PRO   A C   
1361 O  O   . PRO   A 179 ? 2.9345 2.2639 2.8502 -0.3347 0.4992  0.0575  199 PRO   A O   
1362 C  CB  . PRO   A 179 ? 2.9372 2.2042 2.8856 -0.3477 0.4411  0.0154  199 PRO   A CB  
1363 C  CG  . PRO   A 179 ? 2.8702 2.2071 2.9335 -0.3980 0.4607  -0.0093 199 PRO   A CG  
1364 C  CD  . PRO   A 179 ? 3.0157 2.2857 3.0891 -0.4289 0.5266  0.0182  199 PRO   A CD  
1365 N  N   . GLN   A 180 ? 3.0172 2.1795 2.7523 -0.2807 0.5146  0.1131  200 GLN   A N   
1366 C  CA  . GLN   A 180 ? 2.9520 2.1455 2.6420 -0.2569 0.5242  0.1282  200 GLN   A CA  
1367 C  C   . GLN   A 180 ? 2.9079 2.1719 2.5918 -0.2260 0.4626  0.1044  200 GLN   A C   
1368 O  O   . GLN   A 180 ? 2.9734 2.2043 2.5704 -0.1834 0.4368  0.1162  200 GLN   A O   
1369 C  CB  . GLN   A 180 ? 3.0734 2.1612 2.6403 -0.2255 0.5559  0.1724  200 GLN   A CB  
1370 C  CG  . GLN   A 180 ? 3.1692 2.1505 2.6699 -0.2078 0.5460  0.1889  200 GLN   A CG  
1371 C  CD  . GLN   A 180 ? 3.1695 2.1687 2.6537 -0.1753 0.4757  0.1661  200 GLN   A CD  
1372 O  OE1 . GLN   A 180 ? 3.1172 2.1496 2.6721 -0.1934 0.4479  0.1363  200 GLN   A OE1 
1373 N  NE2 . GLN   A 180 ? 3.2111 2.1898 2.6036 -0.1270 0.4471  0.1784  200 GLN   A NE2 
1374 N  N   . ASP   A 181 ? 2.8071 2.1694 2.5872 -0.2482 0.4387  0.0697  201 ASP   A N   
1375 C  CA  . ASP   A 181 ? 2.7106 2.1438 2.4968 -0.2242 0.3855  0.0471  201 ASP   A CA  
1376 C  C   . ASP   A 181 ? 2.5739 2.1144 2.4632 -0.2512 0.3759  0.0169  201 ASP   A C   
1377 O  O   . ASP   A 181 ? 2.5271 2.1070 2.4698 -0.2628 0.3432  -0.0114 201 ASP   A O   
1378 C  CB  . ASP   A 181 ? 2.7624 2.1696 2.5271 -0.2051 0.3394  0.0341  201 ASP   A CB  
1379 C  CG  . ASP   A 181 ? 2.7444 2.1156 2.5510 -0.2340 0.3474  0.0235  201 ASP   A CG  
1380 O  OD1 . ASP   A 181 ? 2.7948 2.0765 2.5611 -0.2379 0.3798  0.0476  201 ASP   A OD1 
1381 O  OD2 . ASP   A 181 ? 2.6423 2.0712 2.5192 -0.2520 0.3218  -0.0091 201 ASP   A OD2 
1382 N  N   . PRO   A 182 ? 2.6020 2.1912 2.5193 -0.2592 0.4029  0.0215  202 PRO   A N   
1383 C  CA  . PRO   A 182 ? 2.4498 2.1446 2.4585 -0.2760 0.3865  -0.0066 202 PRO   A CA  
1384 C  C   . PRO   A 182 ? 2.4573 2.2031 2.4433 -0.2433 0.3482  -0.0145 202 PRO   A C   
1385 O  O   . PRO   A 182 ? 2.4269 2.1373 2.3347 -0.2112 0.3458  0.0030  202 PRO   A O   
1386 C  CB  . PRO   A 182 ? 2.3429 2.0588 2.3958 -0.2997 0.4406  0.0047  202 PRO   A CB  
1387 C  CG  . PRO   A 182 ? 2.4194 2.0572 2.3721 -0.2747 0.4742  0.0405  202 PRO   A CG  
1388 C  CD  . PRO   A 182 ? 2.5852 2.1319 2.4567 -0.2558 0.4557  0.0528  202 PRO   A CD  
1389 N  N   . PHE   A 183 ? 2.3622 2.1898 2.4172 -0.2518 0.3172  -0.0421 203 PHE   A N   
1390 C  CA  . PHE   A 183 ? 2.3254 2.2051 2.3710 -0.2249 0.2820  -0.0509 203 PHE   A CA  
1391 C  C   . PHE   A 183 ? 2.2187 2.1910 2.3499 -0.2398 0.2613  -0.0774 203 PHE   A C   
1392 O  O   . PHE   A 183 ? 2.1685 2.1884 2.3618 -0.2594 0.2838  -0.0819 203 PHE   A O   
1393 C  CB  . PHE   A 183 ? 2.3724 2.2160 2.3606 -0.1983 0.2437  -0.0524 203 PHE   A CB  
1394 C  CG  . PHE   A 183 ? 2.4049 2.2000 2.3902 -0.2099 0.2371  -0.0580 203 PHE   A CG  
1395 C  CD1 . PHE   A 183 ? 2.3371 2.1700 2.3875 -0.2340 0.2229  -0.0835 203 PHE   A CD1 
1396 C  CD2 . PHE   A 183 ? 2.4648 2.1740 2.3788 -0.1941 0.2432  -0.0388 203 PHE   A CD2 
1397 C  CE1 . PHE   A 183 ? 2.4205 2.2046 2.4665 -0.2435 0.2174  -0.0911 203 PHE   A CE1 
1398 C  CE2 . PHE   A 183 ? 2.4921 2.1528 2.4033 -0.2020 0.2376  -0.0439 203 PHE   A CE2 
1399 C  CZ  . PHE   A 183 ? 2.4892 2.1866 2.4674 -0.2275 0.2258  -0.0706 203 PHE   A CZ  
1400 N  N   . PRO   A 198 ? 1.7547 2.4323 2.2482 -0.0991 0.0139  -0.1786 218 PRO   A N   
1401 C  CA  . PRO   A 198 ? 1.9103 2.5647 2.4116 -0.1076 0.0535  -0.1673 218 PRO   A CA  
1402 C  C   . PRO   A 198 ? 2.1068 2.7630 2.5958 -0.0790 0.0652  -0.1509 218 PRO   A C   
1403 O  O   . PRO   A 198 ? 2.0264 2.7377 2.5572 -0.0621 0.0549  -0.1538 218 PRO   A O   
1404 C  CB  . PRO   A 198 ? 1.9305 2.5084 2.3693 -0.1187 0.0658  -0.1589 218 PRO   A CB  
1405 C  CG  . PRO   A 198 ? 1.9483 2.5080 2.3386 -0.1036 0.0354  -0.1585 218 PRO   A CG  
1406 C  CD  . PRO   A 198 ? 1.8441 2.4650 2.2639 -0.0889 0.0054  -0.1681 218 PRO   A CD  
1407 N  N   . PHE   A 199 ? 2.4491 3.0433 2.8802 -0.0721 0.0848  -0.1351 219 PHE   A N   
1408 C  CA  . PHE   A 199 ? 2.4790 3.0618 2.8880 -0.0449 0.0946  -0.1218 219 PHE   A CA  
1409 C  C   . PHE   A 199 ? 2.5594 3.0880 2.9008 -0.0286 0.0816  -0.1111 219 PHE   A C   
1410 O  O   . PHE   A 199 ? 2.5778 3.1016 2.9058 -0.0044 0.0804  -0.1029 219 PHE   A O   
1411 C  CB  . PHE   A 199 ? 2.4505 3.0131 2.8593 -0.0491 0.1353  -0.1154 219 PHE   A CB  
1412 C  CG  . PHE   A 199 ? 2.4443 2.9297 2.7789 -0.0481 0.1489  -0.1046 219 PHE   A CG  
1413 C  CD1 . PHE   A 199 ? 2.4439 2.8883 2.7497 -0.0685 0.1485  -0.1051 219 PHE   A CD1 
1414 C  CD2 . PHE   A 199 ? 2.4694 2.9221 2.7630 -0.0250 0.1601  -0.0957 219 PHE   A CD2 
1415 C  CE1 . PHE   A 199 ? 2.4487 2.8241 2.6864 -0.0640 0.1567  -0.0957 219 PHE   A CE1 
1416 C  CE2 . PHE   A 199 ? 2.4814 2.8652 2.7061 -0.0222 0.1673  -0.0888 219 PHE   A CE2 
1417 C  CZ  . PHE   A 199 ? 2.4856 2.8323 2.6826 -0.0408 0.1646  -0.0881 219 PHE   A CZ  
1418 N  N   . PHE   A 200 ? 2.2957 2.7841 2.5996 -0.0410 0.0724  -0.1119 220 PHE   A N   
1419 C  CA  . PHE   A 200 ? 2.3154 2.7606 2.5681 -0.0276 0.0588  -0.1040 220 PHE   A CA  
1420 C  C   . PHE   A 200 ? 2.2297 2.7015 2.4882 -0.0076 0.0371  -0.1005 220 PHE   A C   
1421 O  O   . PHE   A 200 ? 2.1586 2.5990 2.3855 0.0071  0.0321  -0.0915 220 PHE   A O   
1422 C  CB  . PHE   A 200 ? 2.2615 2.6732 2.4877 -0.0440 0.0508  -0.1083 220 PHE   A CB  
1423 C  CG  . PHE   A 200 ? 2.2744 2.6563 2.4936 -0.0636 0.0717  -0.1099 220 PHE   A CG  
1424 C  CD1 . PHE   A 200 ? 2.2843 2.6094 2.4561 -0.0590 0.0840  -0.1014 220 PHE   A CD1 
1425 C  CD2 . PHE   A 200 ? 2.2299 2.6381 2.4889 -0.0860 0.0784  -0.1202 220 PHE   A CD2 
1426 C  CE1 . PHE   A 200 ? 2.3363 2.6275 2.4930 -0.0738 0.1047  -0.0993 220 PHE   A CE1 
1427 C  CE2 . PHE   A 200 ? 2.2237 2.5980 2.4754 -0.1044 0.1017  -0.1186 220 PHE   A CE2 
1428 C  CZ  . PHE   A 200 ? 2.3364 2.6500 2.5329 -0.0971 0.1159  -0.1063 220 PHE   A CZ  
1429 N  N   . LEU   A 201 ? 2.3633 2.8906 2.6614 -0.0063 0.0236  -0.1076 221 LEU   A N   
1430 C  CA  . LEU   A 201 ? 2.3795 2.9310 2.6790 0.0179  0.0051  -0.1010 221 LEU   A CA  
1431 C  C   . LEU   A 201 ? 2.3440 2.8924 2.6482 0.0403  0.0171  -0.0905 221 LEU   A C   
1432 O  O   . LEU   A 201 ? 2.3168 2.8380 2.5934 0.0588  0.0128  -0.0785 221 LEU   A O   
1433 C  CB  . LEU   A 201 ? 2.4061 3.0199 2.7462 0.0172  -0.0153 -0.1132 221 LEU   A CB  
1434 C  CG  . LEU   A 201 ? 2.2911 2.9310 2.6246 0.0440  -0.0398 -0.1068 221 LEU   A CG  
1435 C  CD1 . LEU   A 201 ? 2.1322 2.8034 2.4970 0.0689  -0.0376 -0.0996 221 LEU   A CD1 
1436 C  CD2 . LEU   A 201 ? 2.2493 2.8394 2.5262 0.0543  -0.0419 -0.0917 221 LEU   A CD2 
1437 N  N   . SER   A 202 ? 2.1759 2.7503 2.5172 0.0387  0.0348  -0.0953 222 SER   A N   
1438 C  CA  . SER   A 202 ? 2.1477 2.7177 2.4932 0.0613  0.0494  -0.0878 222 SER   A CA  
1439 C  C   . SER   A 202 ? 2.1114 2.6132 2.4036 0.0659  0.0609  -0.0803 222 SER   A C   
1440 O  O   . SER   A 202 ? 2.1435 2.6273 2.4246 0.0883  0.0633  -0.0734 222 SER   A O   
1441 C  CB  . SER   A 202 ? 2.0815 2.6887 2.4755 0.0558  0.0730  -0.0954 222 SER   A CB  
1442 O  OG  . SER   A 202 ? 2.0389 2.6758 2.4664 0.0280  0.0737  -0.1072 222 SER   A OG  
1443 N  N   . ILE   A 203 ? 2.2082 2.6705 2.4682 0.0461  0.0657  -0.0828 223 ILE   A N   
1444 C  CA  . ILE   A 203 ? 2.1649 2.5650 2.3752 0.0505  0.0684  -0.0788 223 ILE   A CA  
1445 C  C   . ILE   A 203 ? 2.1633 2.5474 2.3598 0.0641  0.0499  -0.0714 223 ILE   A C   
1446 O  O   . ILE   A 203 ? 2.1337 2.4784 2.3072 0.0759  0.0517  -0.0686 223 ILE   A O   
1447 C  CB  . ILE   A 203 ? 2.1614 2.5274 2.3428 0.0291  0.0704  -0.0827 223 ILE   A CB  
1448 C  CG1 . ILE   A 203 ? 2.2598 2.6273 2.4465 0.0163  0.0953  -0.0862 223 ILE   A CG1 
1449 C  CG2 . ILE   A 203 ? 1.9473 2.2552 2.0825 0.0351  0.0649  -0.0811 223 ILE   A CG2 
1450 C  CD1 . ILE   A 203 ? 2.3355 2.6591 2.4858 -0.0003 0.0981  -0.0870 223 ILE   A CD1 
1451 N  N   . THR   A 204 ? 2.0652 2.4763 2.2738 0.0624  0.0330  -0.0686 224 THR   A N   
1452 C  CA  . THR   A 204 ? 1.8977 2.2897 2.0905 0.0742  0.0211  -0.0583 224 THR   A CA  
1453 C  C   . THR   A 204 ? 1.9061 2.3081 2.1112 0.1001  0.0209  -0.0485 224 THR   A C   
1454 O  O   . THR   A 204 ? 1.8881 2.2550 2.0777 0.1113  0.0204  -0.0392 224 THR   A O   
1455 C  CB  . THR   A 204 ? 1.7396 2.1509 1.9300 0.0661  0.0062  -0.0578 224 THR   A CB  
1456 O  OG1 . THR   A 204 ? 1.8867 2.3205 2.0890 0.0462  0.0058  -0.0707 224 THR   A OG1 
1457 C  CG2 . THR   A 204 ? 1.6611 2.0312 1.8250 0.0605  0.0039  -0.0535 224 THR   A CG2 
1458 N  N   . VAL   A 205 ? 1.9390 2.3876 2.1762 0.1103  0.0218  -0.0507 225 VAL   A N   
1459 C  CA  . VAL   A 205 ? 2.0231 2.4778 2.2728 0.1386  0.0229  -0.0418 225 VAL   A CA  
1460 C  C   . VAL   A 205 ? 2.2103 2.6343 2.4556 0.1456  0.0425  -0.0463 225 VAL   A C   
1461 O  O   . VAL   A 205 ? 2.2663 2.6657 2.5064 0.1673  0.0456  -0.0395 225 VAL   A O   
1462 C  CB  . VAL   A 205 ? 1.9834 2.5045 2.2742 0.1509  0.0128  -0.0437 225 VAL   A CB  
1463 C  CG1 . VAL   A 205 ? 1.8589 2.3830 2.1558 0.1855  0.0073  -0.0302 225 VAL   A CG1 
1464 C  CG2 . VAL   A 205 ? 1.7867 2.3381 2.0774 0.1385  -0.0072 -0.0471 225 VAL   A CG2 
1465 N  N   . PHE   A 206 ? 2.5106 2.9305 2.7528 0.1287  0.0570  -0.0577 226 PHE   A N   
1466 C  CA  . PHE   A 206 ? 2.5782 2.9650 2.8041 0.1354  0.0772  -0.0637 226 PHE   A CA  
1467 C  C   . PHE   A 206 ? 2.4886 2.8227 2.6704 0.1185  0.0790  -0.0694 226 PHE   A C   
1468 O  O   . PHE   A 206 ? 2.4569 2.7826 2.6250 0.1087  0.0948  -0.0762 226 PHE   A O   
1469 C  CB  . PHE   A 206 ? 2.7223 3.1501 2.9802 0.1356  0.0981  -0.0706 226 PHE   A CB  
1470 C  CG  . PHE   A 206 ? 2.8050 3.2998 3.1189 0.1483  0.0921  -0.0687 226 PHE   A CG  
1471 C  CD1 . PHE   A 206 ? 2.8377 3.3407 3.1604 0.1727  0.0750  -0.0593 226 PHE   A CD1 
1472 C  CD2 . PHE   A 206 ? 2.7975 3.3467 3.1577 0.1367  0.1037  -0.0766 226 PHE   A CD2 
1473 C  CE1 . PHE   A 206 ? 2.8035 3.3691 3.1754 0.1882  0.0651  -0.0583 226 PHE   A CE1 
1474 C  CE2 . PHE   A 206 ? 2.7758 3.3924 3.1947 0.1490  0.0940  -0.0783 226 PHE   A CE2 
1475 C  CZ  . PHE   A 206 ? 2.7715 3.3972 3.1942 0.1766  0.0727  -0.0694 226 PHE   A CZ  
1476 N  N   . PRO   A 207 ? 2.1268 2.4243 2.2865 0.1156  0.0636  -0.0663 227 PRO   A N   
1477 C  CA  . PRO   A 207 ? 2.0588 2.3074 2.1807 0.1044  0.0618  -0.0741 227 PRO   A CA  
1478 C  C   . PRO   A 207 ? 1.9887 2.1972 2.0840 0.1191  0.0719  -0.0828 227 PRO   A C   
1479 O  O   . PRO   A 207 ? 1.9289 2.1008 1.9870 0.1138  0.0728  -0.0918 227 PRO   A O   
1480 C  CB  . PRO   A 207 ? 2.0959 2.3254 2.2162 0.0994  0.0437  -0.0691 227 PRO   A CB  
1481 C  CG  . PRO   A 207 ? 2.1436 2.3865 2.2857 0.1166  0.0422  -0.0581 227 PRO   A CG  
1482 C  CD  . PRO   A 207 ? 2.1232 2.4180 2.2910 0.1249  0.0495  -0.0552 227 PRO   A CD  
1483 N  N   . PHE   A 208 ? 1.9162 2.1289 2.0264 0.1401  0.0787  -0.0809 228 PHE   A N   
1484 C  CA  . PHE   A 208 ? 1.9481 2.1273 2.0341 0.1574  0.0921  -0.0914 228 PHE   A CA  
1485 C  C   . PHE   A 208 ? 1.9133 2.1058 1.9866 0.1564  0.1162  -0.0964 228 PHE   A C   
1486 O  O   . PHE   A 208 ? 1.9119 2.0682 1.9480 0.1685  0.1293  -0.1068 228 PHE   A O   
1487 C  CB  . PHE   A 208 ? 2.0043 2.1893 2.1153 0.1818  0.0955  -0.0870 228 PHE   A CB  
1488 C  CG  . PHE   A 208 ? 2.0857 2.3340 2.2429 0.1890  0.1007  -0.0758 228 PHE   A CG  
1489 C  CD1 . PHE   A 208 ? 2.0381 2.3243 2.2144 0.1950  0.1219  -0.0798 228 PHE   A CD1 
1490 C  CD2 . PHE   A 208 ? 2.1546 2.4249 2.3367 0.1914  0.0844  -0.0619 228 PHE   A CD2 
1491 C  CE1 . PHE   A 208 ? 2.1228 2.4729 2.3504 0.2020  0.1226  -0.0729 228 PHE   A CE1 
1492 C  CE2 . PHE   A 208 ? 2.2798 2.6093 2.5016 0.2012  0.0834  -0.0540 228 PHE   A CE2 
1493 C  CZ  . PHE   A 208 ? 2.3366 2.7086 2.5855 0.2062  0.1003  -0.0610 228 PHE   A CZ  
1494 N  N   . LEU   A 209 ? 1.9187 2.1602 2.0215 0.1421  0.1237  -0.0901 229 LEU   A N   
1495 C  CA  . LEU   A 209 ? 1.8811 2.1350 1.9781 0.1356  0.1507  -0.0925 229 LEU   A CA  
1496 C  C   . LEU   A 209 ? 1.8362 2.0520 1.8858 0.1179  0.1504  -0.0944 229 LEU   A C   
1497 O  O   . LEU   A 209 ? 1.8688 2.0775 1.8982 0.1145  0.1763  -0.0946 229 LEU   A O   
1498 C  CB  . LEU   A 209 ? 1.9574 2.2814 2.1159 0.1258  0.1584  -0.0871 229 LEU   A CB  
1499 C  CG  . LEU   A 209 ? 2.0022 2.3705 2.2082 0.1475  0.1708  -0.0870 229 LEU   A CG  
1500 C  CD1 . LEU   A 209 ? 2.0146 2.4557 2.2859 0.1349  0.1737  -0.0855 229 LEU   A CD1 
1501 C  CD2 . LEU   A 209 ? 1.9292 2.2732 2.1104 0.1639  0.2029  -0.0933 229 LEU   A CD2 
1502 N  N   . ILE   A 210 ? 1.9397 2.1311 1.9727 0.1077  0.1238  -0.0946 230 ILE   A N   
1503 C  CA  . ILE   A 210 ? 1.9555 2.1085 1.9434 0.0951  0.1190  -0.0966 230 ILE   A CA  
1504 C  C   . ILE   A 210 ? 2.0535 2.1524 1.9790 0.1110  0.1287  -0.1050 230 ILE   A C   
1505 O  O   . ILE   A 210 ? 2.0473 2.1279 1.9366 0.1079  0.1487  -0.1026 230 ILE   A O   
1506 C  CB  . ILE   A 210 ? 1.9178 2.0579 1.9067 0.0853  0.0878  -0.0972 230 ILE   A CB  
1507 C  CG1 . ILE   A 210 ? 1.9286 2.1145 1.9609 0.0675  0.0819  -0.0898 230 ILE   A CG1 
1508 C  CG2 . ILE   A 210 ? 1.9954 2.0854 1.9312 0.0821  0.0778  -0.1029 230 ILE   A CG2 
1509 C  CD1 . ILE   A 210 ? 1.9771 2.1564 2.0160 0.0605  0.0564  -0.0894 230 ILE   A CD1 
1510 N  N   . PRO   A 211 ? 1.9147 1.9828 1.8222 0.1289  0.1162  -0.1153 231 PRO   A N   
1511 C  CA  . PRO   A 211 ? 1.9541 1.9691 1.7950 0.1462  0.1238  -0.1269 231 PRO   A CA  
1512 C  C   . PRO   A 211 ? 1.9629 1.9878 1.7922 0.1572  0.1639  -0.1240 231 PRO   A C   
1513 O  O   . PRO   A 211 ? 2.0425 2.0253 1.8063 0.1678  0.1792  -0.1284 231 PRO   A O   
1514 C  CB  . PRO   A 211 ? 1.9768 1.9653 1.8178 0.1616  0.1031  -0.1407 231 PRO   A CB  
1515 C  CG  . PRO   A 211 ? 1.8742 1.8920 1.7729 0.1482  0.0817  -0.1335 231 PRO   A CG  
1516 C  CD  . PRO   A 211 ? 1.9123 1.9877 1.8551 0.1356  0.0975  -0.1174 231 PRO   A CD  
1517 N  N   . ILE   A 212 ? 1.9031 1.9830 1.7940 0.1570  0.1815  -0.1168 232 ILE   A N   
1518 C  CA  . ILE   A 212 ? 1.8964 1.9981 1.7940 0.1653  0.2231  -0.1138 232 ILE   A CA  
1519 C  C   . ILE   A 212 ? 1.8898 1.9852 1.7619 0.1485  0.2465  -0.1045 232 ILE   A C   
1520 O  O   . ILE   A 212 ? 1.9575 2.0148 1.7702 0.1592  0.2737  -0.1053 232 ILE   A O   
1521 C  CB  . ILE   A 212 ? 1.8482 2.0205 1.8303 0.1655  0.2305  -0.1080 232 ILE   A CB  
1522 C  CG1 . ILE   A 212 ? 1.9096 2.0764 1.9063 0.1883  0.2144  -0.1149 232 ILE   A CG1 
1523 C  CG2 . ILE   A 212 ? 1.8080 2.0162 1.8152 0.1673  0.2746  -0.1043 232 ILE   A CG2 
1524 C  CD1 . ILE   A 212 ? 1.9419 2.1368 1.9682 0.2116  0.2435  -0.1175 232 ILE   A CD1 
1525 N  N   . LEU   A 213 ? 1.9837 2.1114 1.8961 0.1227  0.2372  -0.0955 233 LEU   A N   
1526 C  CA  . LEU   A 213 ? 1.9555 2.0743 1.8508 0.1035  0.2583  -0.0857 233 LEU   A CA  
1527 C  C   . LEU   A 213 ? 2.0593 2.1053 1.8660 0.1079  0.2482  -0.0858 233 LEU   A C   
1528 O  O   . LEU   A 213 ? 2.1430 2.1653 1.9167 0.0984  0.2714  -0.0757 233 LEU   A O   
1529 C  CB  . LEU   A 213 ? 1.8949 2.0605 1.8537 0.0763  0.2439  -0.0804 233 LEU   A CB  
1530 C  CG  . LEU   A 213 ? 1.8428 2.0796 1.8852 0.0753  0.2360  -0.0828 233 LEU   A CG  
1531 C  CD1 . LEU   A 213 ? 1.8717 2.1298 1.9443 0.0598  0.1999  -0.0828 233 LEU   A CD1 
1532 C  CD2 . LEU   A 213 ? 1.8152 2.1047 1.9156 0.0649  0.2711  -0.0798 233 LEU   A CD2 
1533 N  N   . GLU   A 214 ? 1.9929 2.0021 1.7623 0.1224  0.2134  -0.0972 234 GLU   A N   
1534 C  CA  . GLU   A 214 ? 2.1363 2.0790 1.8233 0.1310  0.1959  -0.1012 234 GLU   A CA  
1535 C  C   . GLU   A 214 ? 2.2402 2.1342 1.8475 0.1541  0.2225  -0.1042 234 GLU   A C   
1536 O  O   . GLU   A 214 ? 2.3687 2.2040 1.8977 0.1670  0.2049  -0.1096 234 GLU   A O   
1537 C  CB  . GLU   A 214 ? 2.2531 2.1793 1.9394 0.1378  0.1491  -0.1160 234 GLU   A CB  
1538 C  CG  . GLU   A 214 ? 2.3840 2.3416 2.1267 0.1169  0.1209  -0.1124 234 GLU   A CG  
1539 C  CD  . GLU   A 214 ? 2.4714 2.4061 2.1863 0.1051  0.1112  -0.1056 234 GLU   A CD  
1540 O  OE1 . GLU   A 214 ? 2.6580 2.5463 2.3036 0.1146  0.1223  -0.1027 234 GLU   A OE1 
1541 O  OE2 . GLU   A 214 ? 2.2772 2.2374 2.0359 0.0883  0.0932  -0.1026 234 GLU   A OE2 
1542 N  N   . VAL   A 215 ? 2.2354 2.1509 1.8569 0.1621  0.2635  -0.1015 235 VAL   A N   
1543 C  CA  . VAL   A 215 ? 2.3280 2.1950 1.8673 0.1867  0.2942  -0.1044 235 VAL   A CA  
1544 C  C   . VAL   A 215 ? 2.4061 2.2875 1.9503 0.1767  0.3509  -0.0855 235 VAL   A C   
1545 O  O   . VAL   A 215 ? 2.4869 2.3160 1.9472 0.1895  0.3800  -0.0785 235 VAL   A O   
1546 C  CB  . VAL   A 215 ? 2.3019 2.1698 1.8427 0.2121  0.2954  -0.1224 235 VAL   A CB  
1547 C  CG1 . VAL   A 215 ? 2.3769 2.2669 1.9280 0.2227  0.3522  -0.1170 235 VAL   A CG1 
1548 C  CG2 . VAL   A 215 ? 2.3223 2.1180 1.7684 0.2376  0.2681  -0.1417 235 VAL   A CG2 
1549 N  N   . LEU   A 216 ? 2.3553 2.3064 1.9972 0.1538  0.3671  -0.0772 236 LEU   A N   
1550 C  CA  . LEU   A 216 ? 2.4608 2.4321 2.1260 0.1380  0.4199  -0.0606 236 LEU   A CA  
1551 C  C   . LEU   A 216 ? 2.5579 2.5083 2.2113 0.1125  0.4174  -0.0454 236 LEU   A C   
1552 O  O   . LEU   A 216 ? 2.5531 2.5382 2.2636 0.0877  0.4492  -0.0337 236 LEU   A O   
1553 C  CB  . LEU   A 216 ? 2.3605 2.4195 2.1421 0.1254  0.4376  -0.0617 236 LEU   A CB  
1554 C  CG  . LEU   A 216 ? 2.1926 2.3082 2.0499 0.1306  0.4034  -0.0747 236 LEU   A CG  
1555 C  CD1 . LEU   A 216 ? 2.0955 2.2957 2.0608 0.1179  0.4287  -0.0724 236 LEU   A CD1 
1556 C  CD2 . LEU   A 216 ? 2.2451 2.3329 2.0609 0.1646  0.3944  -0.0890 236 LEU   A CD2 
1557 N  N   . ASN   A 217 ? 2.7683 2.6643 2.3555 0.1179  0.3786  -0.0472 237 ASN   A N   
1558 C  CA  . ASN   A 217 ? 2.9453 2.8034 2.4993 0.1017  0.3766  -0.0324 237 ASN   A CA  
1559 C  C   . ASN   A 217 ? 2.9582 2.8709 2.6070 0.0658  0.3807  -0.0255 237 ASN   A C   
1560 O  O   . ASN   A 217 ? 3.0589 2.9454 2.6943 0.0484  0.3981  -0.0106 237 ASN   A O   
1561 C  CB  . ASN   A 217 ? 2.9579 2.7527 2.4215 0.1130  0.4236  -0.0153 237 ASN   A CB  
1562 C  CG  . ASN   A 217 ? 3.1676 2.8901 2.5460 0.1176  0.4030  -0.0050 237 ASN   A CG  
1563 O  OD1 . ASN   A 217 ? 3.2288 2.9324 2.6057 0.0987  0.4266  0.0142  237 ASN   A OD1 
1564 N  ND2 . ASN   A 217 ? 3.2749 2.9563 2.5857 0.1431  0.3572  -0.0188 237 ASN   A ND2 
1565 N  N   . ILE   A 218 ? 2.5252 2.5101 2.2671 0.0554  0.3641  -0.0366 238 ILE   A N   
1566 C  CA  . ILE   A 218 ? 2.3880 2.4241 2.2150 0.0237  0.3581  -0.0351 238 ILE   A CA  
1567 C  C   . ILE   A 218 ? 2.3943 2.4077 2.2043 0.0181  0.3106  -0.0385 238 ILE   A C   
1568 O  O   . ILE   A 218 ? 2.2567 2.2978 2.0965 0.0222  0.2719  -0.0502 238 ILE   A O   
1569 C  CB  . ILE   A 218 ? 2.2153 2.3355 2.1406 0.0189  0.3536  -0.0458 238 ILE   A CB  
1570 C  CG1 . ILE   A 218 ? 2.1777 2.3044 2.0901 0.0477  0.3664  -0.0521 238 ILE   A CG1 
1571 C  CG2 . ILE   A 218 ? 2.1886 2.3600 2.1938 -0.0090 0.3869  -0.0415 238 ILE   A CG2 
1572 C  CD1 . ILE   A 218 ? 2.0365 2.2441 2.0447 0.0462  0.3727  -0.0592 238 ILE   A CD1 
1573 N  N   . CYS   A 219 ? 2.4110 2.3717 2.1727 0.0101  0.3158  -0.0273 239 CYS   A N   
1574 C  CA  . CYS   A 219 ? 2.3397 2.2714 2.0767 0.0097  0.2732  -0.0304 239 CYS   A CA  
1575 C  C   . CYS   A 219 ? 2.2076 2.1534 1.9924 -0.0200 0.2738  -0.0265 239 CYS   A C   
1576 O  O   . CYS   A 219 ? 2.1094 2.1141 1.9742 -0.0414 0.2842  -0.0311 239 CYS   A O   
1577 C  CB  . CYS   A 219 ? 2.4209 2.2710 2.0518 0.0325  0.2688  -0.0230 239 CYS   A CB  
1578 S  SG  . CYS   A 219 ? 2.6146 2.4350 2.1735 0.0676  0.2788  -0.0284 239 CYS   A SG  
1579 N  N   . THR   A 226 ? 2.2383 2.0210 1.9624 -0.0901 0.4444  0.0458  246 THR   A N   
1580 C  CA  . THR   A 226 ? 2.4639 2.1770 2.1348 -0.0958 0.4969  0.0722  246 THR   A CA  
1581 C  C   . THR   A 226 ? 2.7004 2.3187 2.2426 -0.0629 0.4836  0.0885  246 THR   A C   
1582 O  O   . THR   A 226 ? 2.6515 2.2588 2.1646 -0.0449 0.4298  0.0776  246 THR   A O   
1583 C  CB  . THR   A 226 ? 2.4769 2.1881 2.2127 -0.1355 0.5155  0.0759  246 THR   A CB  
1584 O  OG1 . THR   A 226 ? 2.6119 2.2444 2.2887 -0.1397 0.5694  0.1054  246 THR   A OG1 
1585 C  CG2 . THR   A 226 ? 2.4361 2.1336 2.1732 -0.1374 0.4627  0.0644  246 THR   A CG2 
1586 N  N   . ASN   A 227 ? 2.7794 2.3303 2.2453 -0.0540 0.5337  0.1149  247 ASN   A N   
1587 C  CA  . ASN   A 227 ? 2.9868 2.4410 2.3212 -0.0203 0.5244  0.1332  247 ASN   A CA  
1588 C  C   . ASN   A 227 ? 3.0829 2.4714 2.3960 -0.0330 0.5294  0.1516  247 ASN   A C   
1589 O  O   . ASN   A 227 ? 3.3264 2.6250 2.5273 -0.0062 0.5335  0.1737  247 ASN   A O   
1590 C  CB  . ASN   A 227 ? 3.0946 2.5001 2.3377 0.0029  0.5758  0.1538  247 ASN   A CB  
1591 C  CG  . ASN   A 227 ? 3.0673 2.4800 2.3584 -0.0280 0.6532  0.1729  247 ASN   A CG  
1592 O  OD1 . ASN   A 227 ? 3.0069 2.4394 2.3831 -0.0666 0.6692  0.1750  247 ASN   A OD1 
1593 N  ND2 . ASN   A 227 ? 3.0686 2.4653 2.3075 -0.0111 0.7028  0.1852  247 ASN   A ND2 
1594 N  N   . PHE   A 228 ? 2.9734 2.4025 2.3887 -0.0711 0.5271  0.1418  248 PHE   A N   
1595 C  CA  . PHE   A 228 ? 2.9818 2.3508 2.3927 -0.0889 0.5380  0.1570  248 PHE   A CA  
1596 C  C   . PHE   A 228 ? 3.1502 2.4415 2.4587 -0.0528 0.4968  0.1658  248 PHE   A C   
1597 O  O   . PHE   A 228 ? 3.3289 2.5283 2.5357 -0.0329 0.5226  0.1954  248 PHE   A O   
1598 C  CB  . PHE   A 228 ? 2.8196 2.2553 2.3558 -0.1286 0.5200  0.1329  248 PHE   A CB  
1599 C  CG  . PHE   A 228 ? 2.8052 2.1809 2.3389 -0.1433 0.5170  0.1407  248 PHE   A CG  
1600 C  CD1 . PHE   A 228 ? 2.8554 2.1428 2.3374 -0.1499 0.5678  0.1727  248 PHE   A CD1 
1601 C  CD2 . PHE   A 228 ? 2.7413 2.1456 2.3227 -0.1493 0.4657  0.1165  248 PHE   A CD2 
1602 C  CE1 . PHE   A 228 ? 2.9097 2.1356 2.3888 -0.1619 0.5650  0.1799  248 PHE   A CE1 
1603 C  CE2 . PHE   A 228 ? 2.7539 2.1005 2.3325 -0.1604 0.4629  0.1214  248 PHE   A CE2 
1604 C  CZ  . PHE   A 228 ? 2.8461 2.1027 2.3748 -0.1668 0.5114  0.1528  248 PHE   A CZ  
1605 N  N   . LEU   A 229 ? 3.0580 2.3854 2.3916 -0.0423 0.4336  0.1411  249 LEU   A N   
1606 C  CA  . LEU   A 229 ? 3.1417 2.4099 2.3909 -0.0053 0.3881  0.1446  249 LEU   A CA  
1607 C  C   . LEU   A 229 ? 3.3065 2.5709 2.4790 0.0357  0.3605  0.1395  249 LEU   A C   
1608 O  O   . LEU   A 229 ? 3.3738 2.5808 2.4614 0.0713  0.3269  0.1450  249 LEU   A O   
1609 C  CB  . LEU   A 229 ? 2.9712 2.2792 2.2884 -0.0136 0.3363  0.1200  249 LEU   A CB  
1610 C  CG  . LEU   A 229 ? 2.9332 2.2318 2.3138 -0.0488 0.3539  0.1210  249 LEU   A CG  
1611 C  CD1 . LEU   A 229 ? 2.7643 2.0962 2.1959 -0.0493 0.3016  0.0959  249 LEU   A CD1 
1612 C  CD2 . LEU   A 229 ? 3.0051 2.1971 2.3091 -0.0432 0.3892  0.1543  249 LEU   A CD2 
1613 N  N   . ARG   A 230 ? 3.3399 2.6635 2.5422 0.0325  0.3720  0.1274  250 ARG   A N   
1614 C  CA  . ARG   A 230 ? 3.4084 2.7208 2.5337 0.0700  0.3533  0.1219  250 ARG   A CA  
1615 C  C   . ARG   A 230 ? 3.6920 2.9056 2.6825 0.1011  0.3800  0.1506  250 ARG   A C   
1616 O  O   . ARG   A 230 ? 3.7743 2.9575 2.6779 0.1400  0.3502  0.1453  250 ARG   A O   
1617 C  CB  . ARG   A 230 ? 3.3167 2.6997 2.4962 0.0592  0.3753  0.1084  250 ARG   A CB  
1618 C  CG  . ARG   A 230 ? 3.2321 2.6790 2.4538 0.0694  0.3231  0.0776  250 ARG   A CG  
1619 C  CD  . ARG   A 230 ? 3.2556 2.7221 2.4555 0.0845  0.3416  0.0709  250 ARG   A CD  
1620 N  NE  . ARG   A 230 ? 3.4115 2.7997 2.4810 0.1226  0.3461  0.0821  250 ARG   A NE  
1621 C  CZ  . ARG   A 230 ? 3.5014 2.8753 2.5136 0.1556  0.3018  0.0645  250 ARG   A CZ  
1622 N  NH1 . ARG   A 230 ? 3.4635 2.8952 2.5404 0.1539  0.2546  0.0367  250 ARG   A NH1 
1623 N  NH2 . ARG   A 230 ? 3.5756 2.8731 2.4613 0.1914  0.3054  0.0747  250 ARG   A NH2 
1624 N  N   . LYS   A 231 ? 4.2542 3.4155 3.2243 0.0850  0.4359  0.1803  251 LYS   A N   
1625 C  CA  . LYS   A 231 ? 4.4082 3.4631 3.2435 0.1148  0.4635  0.2133  251 LYS   A CA  
1626 C  C   . LYS   A 231 ? 4.3959 3.3792 3.2068 0.1111  0.4652  0.2359  251 LYS   A C   
1627 O  O   . LYS   A 231 ? 4.5531 3.4456 3.2427 0.1480  0.4591  0.2581  251 LYS   A O   
1628 C  CB  . LYS   A 231 ? 4.3972 3.4350 3.2070 0.1048  0.5426  0.2361  251 LYS   A CB  
1629 C  CG  . LYS   A 231 ? 4.3163 3.3814 3.2301 0.0533  0.5998  0.2472  251 LYS   A CG  
1630 C  CD  . LYS   A 231 ? 4.0905 3.2077 3.0513 0.0354  0.6581  0.2468  251 LYS   A CD  
1631 C  CE  . LYS   A 231 ? 3.9908 3.1370 3.0626 -0.0170 0.7135  0.2559  251 LYS   A CE  
1632 N  NZ  . LYS   A 231 ? 4.0129 3.2120 3.1964 -0.0486 0.6702  0.2329  251 LYS   A NZ  
1633 N  N   . SER   A 232 ? 3.8459 2.8647 2.7651 0.0700  0.4712  0.2298  252 SER   A N   
1634 C  CA  . SER   A 232 ? 3.7301 2.6794 2.6315 0.0666  0.4705  0.2481  252 SER   A CA  
1635 C  C   . SER   A 232 ? 3.6551 2.5964 2.5332 0.0982  0.3954  0.2317  252 SER   A C   
1636 O  O   . SER   A 232 ? 3.6995 2.5542 2.4789 0.1327  0.3810  0.2520  252 SER   A O   
1637 C  CB  . SER   A 232 ? 3.4959 2.4865 2.5227 0.0124  0.4989  0.2416  252 SER   A CB  
1638 O  OG  . SER   A 232 ? 3.3444 2.2773 2.3677 0.0095  0.4864  0.2503  252 SER   A OG  
1639 N  N   . VAL   A 233 ? 3.4092 2.4405 2.3790 0.0880  0.3477  0.1956  253 VAL   A N   
1640 C  CA  . VAL   A 233 ? 3.3453 2.3796 2.3024 0.1180  0.2782  0.1776  253 VAL   A CA  
1641 C  C   . VAL   A 233 ? 3.4253 2.4282 2.2766 0.1666  0.2472  0.1780  253 VAL   A C   
1642 O  O   . VAL   A 233 ? 3.4051 2.3642 2.1968 0.2030  0.2019  0.1786  253 VAL   A O   
1643 C  CB  . VAL   A 233 ? 3.1142 2.2520 2.1934 0.0945  0.2420  0.1409  253 VAL   A CB  
1644 C  CG1 . VAL   A 233 ? 2.8790 2.0423 1.9458 0.1280  0.1756  0.1180  253 VAL   A CG1 
1645 C  CG2 . VAL   A 233 ? 2.9939 2.1368 2.1480 0.0649  0.2457  0.1371  253 VAL   A CG2 
1646 N  N   . LYS   A 234 ? 3.4796 2.5030 2.3053 0.1697  0.2696  0.1762  254 LYS   A N   
1647 C  CA  . LYS   A 234 ? 3.6110 2.5896 2.3196 0.2166  0.2472  0.1782  254 LYS   A CA  
1648 C  C   . LYS   A 234 ? 3.7636 2.6270 2.3409 0.2478  0.2668  0.2150  254 LYS   A C   
1649 O  O   . LYS   A 234 ? 3.7395 2.5537 2.2178 0.2946  0.2242  0.2150  254 LYS   A O   
1650 C  CB  . LYS   A 234 ? 3.5971 2.6095 2.2981 0.2129  0.2792  0.1721  254 LYS   A CB  
1651 C  CG  . LYS   A 234 ? 3.4297 2.4030 2.0140 0.2608  0.2521  0.1662  254 LYS   A CG  
1652 C  CD  . LYS   A 234 ? 3.2220 2.2228 1.8200 0.2849  0.1698  0.1348  254 LYS   A CD  
1653 C  CE  . LYS   A 234 ? 3.0152 2.0565 1.6058 0.3002  0.1441  0.1052  254 LYS   A CE  
1654 N  NZ  . LYS   A 234 ? 2.9721 2.0951 1.6690 0.2617  0.1764  0.0925  254 LYS   A NZ  
1655 N  N   . ARG   A 235 ? 4.0490 2.8664 2.6240 0.2233  0.3298  0.2465  255 ARG   A N   
1656 C  CA  . ARG   A 235 ? 4.1020 2.8026 2.5589 0.2496  0.3528  0.2861  255 ARG   A CA  
1657 C  C   . ARG   A 235 ? 3.9940 2.6640 2.4793 0.2488  0.3244  0.2905  255 ARG   A C   
1658 O  O   . ARG   A 235 ? 4.0388 2.6300 2.4888 0.2425  0.3655  0.3239  255 ARG   A O   
1659 C  CB  . ARG   A 235 ? 4.2055 2.8632 2.6403 0.2244  0.4423  0.3208  255 ARG   A CB  
1660 C  CG  . ARG   A 235 ? 4.2903 2.9335 2.6376 0.2451  0.4764  0.3290  255 ARG   A CG  
1661 C  CD  . ARG   A 235 ? 4.4072 3.0212 2.7559 0.2143  0.5712  0.3617  255 ARG   A CD  
1662 N  NE  . ARG   A 235 ? 4.3609 3.0762 2.8666 0.1588  0.5991  0.3414  255 ARG   A NE  
1663 C  CZ  . ARG   A 235 ? 4.2461 2.9836 2.8607 0.1131  0.6179  0.3423  255 ARG   A CZ  
1664 N  NH1 . ARG   A 235 ? 4.2007 2.8653 2.7902 0.1136  0.6150  0.3626  255 ARG   A NH1 
1665 N  NH2 . ARG   A 235 ? 4.1487 2.9826 2.8998 0.0674  0.6383  0.3209  255 ARG   A NH2 
1666 N  N   . MET   A 236 ? 3.6782 2.4084 2.2314 0.2542  0.2574  0.2571  256 MET   A N   
1667 C  CA  . MET   A 236 ? 3.6217 2.3141 2.1748 0.2713  0.2183  0.2592  256 MET   A CA  
1668 C  C   . MET   A 236 ? 3.6848 2.3062 2.1046 0.3340  0.1745  0.2694  256 MET   A C   
1669 O  O   . MET   A 236 ? 3.6446 2.3039 2.0725 0.3621  0.1066  0.2414  256 MET   A O   
1670 C  CB  . MET   A 236 ? 3.4714 2.2592 2.1532 0.2520  0.1701  0.2198  256 MET   A CB  
1671 C  CG  . MET   A 236 ? 3.3839 2.2274 2.1869 0.1947  0.2085  0.2114  256 MET   A CG  
1672 S  SD  . MET   A 236 ? 3.3819 2.1317 2.1651 0.1711  0.2730  0.2497  256 MET   A SD  
1673 C  CE  . MET   A 236 ? 3.3470 2.1764 2.2496 0.1056  0.3294  0.2385  256 MET   A CE  
1674 N  N   . LYS   A 237 ? 3.7764 2.2931 2.0705 0.3564  0.2157  0.3104  257 LYS   A N   
1675 C  CA  . LYS   A 237 ? 3.8339 2.2734 1.9822 0.4200  0.1775  0.3235  257 LYS   A CA  
1676 C  C   . LYS   A 237 ? 3.9075 2.3143 2.0493 0.4527  0.1187  0.3217  257 LYS   A C   
1677 O  O   . LYS   A 237 ? 3.8913 2.2965 1.9807 0.5005  0.0512  0.3053  257 LYS   A O   
1678 C  CB  . LYS   A 237 ? 3.8063 2.1593 1.8479 0.4307  0.2406  0.3616  257 LYS   A CB  
1679 C  CG  . LYS   A 237 ? 3.8312 2.1098 1.8702 0.4165  0.2879  0.3965  257 LYS   A CG  
1680 C  CD  . LYS   A 237 ? 3.7949 2.0905 1.9259 0.3529  0.3582  0.4100  257 LYS   A CD  
1681 C  CE  . LYS   A 237 ? 3.7491 2.0558 1.9748 0.3290  0.3376  0.4021  257 LYS   A CE  
1682 N  NZ  . LYS   A 237 ? 3.7241 2.1563 2.1096 0.2762  0.3351  0.3622  257 LYS   A NZ  
1683 N  N   . GLU   A 238 ? 4.0529 2.4364 2.2536 0.4278  0.1417  0.3354  258 GLU   A N   
1684 C  CA  . GLU   A 238 ? 4.0783 2.4247 2.2777 0.4579  0.0943  0.3363  258 GLU   A CA  
1685 C  C   . GLU   A 238 ? 4.1313 2.4096 2.2060 0.5198  0.0599  0.3483  258 GLU   A C   
1686 O  O   . GLU   A 238 ? 4.1352 2.4302 2.2128 0.5583  -0.0105 0.3271  258 GLU   A O   
1687 C  CB  . GLU   A 238 ? 4.0496 2.5052 2.3754 0.4505  0.0304  0.2878  258 GLU   A CB  
1688 C  CG  . GLU   A 238 ? 3.9511 2.4965 2.4225 0.3866  0.0611  0.2655  258 GLU   A CG  
1689 C  CD  . GLU   A 238 ? 4.0753 2.5759 2.5883 0.3560  0.1048  0.2845  258 GLU   A CD  
1690 O  OE1 . GLU   A 238 ? 4.2331 2.6631 2.7064 0.3862  0.0862  0.2996  258 GLU   A OE1 
1691 O  OE2 . GLU   A 238 ? 4.0261 2.5613 2.6130 0.3028  0.1558  0.2828  258 GLU   A OE2 
1692 N  N   . SER   A 239 ? 3.9855 2.2102 1.9768 0.5244  0.1100  0.3726  259 SER   A N   
1693 C  CA  . SER   A 239 ? 3.9823 2.1585 1.8685 0.5774  0.0833  0.3763  259 SER   A CA  
1694 C  C   . SER   A 239 ? 3.9435 2.0351 1.7566 0.5728  0.1566  0.4166  259 SER   A C   
1695 O  O   . SER   A 239 ? 3.9490 2.0409 1.7772 0.5334  0.2259  0.4324  259 SER   A O   
1696 C  CB  . SER   A 239 ? 3.9068 2.1291 1.7539 0.6020  0.0456  0.3472  259 SER   A CB  
1697 O  OG  . SER   A 239 ? 3.9614 2.2660 1.8846 0.6028  -0.0199 0.3088  259 SER   A OG  
1698 N  N   . ASP   A 250 ? 3.1071 2.0563 2.2048 0.4293  -0.2437 0.0609  270 ASP   A N   
1699 C  CA  . ASP   A 250 ? 3.0535 2.0576 2.2142 0.3723  -0.1998 0.0520  270 ASP   A CA  
1700 C  C   . ASP   A 250 ? 3.0801 2.1632 2.2685 0.3587  -0.2131 0.0329  270 ASP   A C   
1701 O  O   . ASP   A 250 ? 3.1182 2.1984 2.2588 0.3904  -0.2491 0.0307  270 ASP   A O   
1702 C  CB  . ASP   A 250 ? 3.0204 1.9512 2.1204 0.3461  -0.1412 0.0835  270 ASP   A CB  
1703 C  CG  . ASP   A 250 ? 3.1037 1.9544 2.1873 0.3508  -0.1209 0.1010  270 ASP   A CG  
1704 O  OD1 . ASP   A 250 ? 3.1616 2.0308 2.3028 0.3628  -0.1443 0.0830  270 ASP   A OD1 
1705 O  OD2 . ASP   A 250 ? 3.2529 2.0205 2.2676 0.3422  -0.0789 0.1326  270 ASP   A OD2 
1706 N  N   . PHE   A 251 ? 3.2574 2.4081 2.5218 0.3127  -0.1851 0.0184  271 PHE   A N   
1707 C  CA  . PHE   A 251 ? 3.1568 2.3778 2.4498 0.2959  -0.1904 0.0026  271 PHE   A CA  
1708 C  C   . PHE   A 251 ? 3.2703 2.4449 2.4648 0.3100  -0.1845 0.0211  271 PHE   A C   
1709 O  O   . PHE   A 251 ? 3.3162 2.5192 2.4983 0.3272  -0.2168 0.0076  271 PHE   A O   
1710 C  CB  . PHE   A 251 ? 3.0631 2.3408 2.4296 0.2453  -0.1511 -0.0063 271 PHE   A CB  
1711 C  CG  . PHE   A 251 ? 3.1211 2.4532 2.5021 0.2253  -0.1434 -0.0143 271 PHE   A CG  
1712 C  CD1 . PHE   A 251 ? 2.9557 2.3622 2.3976 0.2266  -0.1742 -0.0396 271 PHE   A CD1 
1713 C  CD2 . PHE   A 251 ? 3.0867 2.3950 2.4255 0.2044  -0.1024 0.0035  271 PHE   A CD2 
1714 C  CE1 . PHE   A 251 ? 2.7847 2.2353 2.2393 0.2094  -0.1663 -0.0466 271 PHE   A CE1 
1715 C  CE2 . PHE   A 251 ? 2.8871 2.2446 2.2407 0.1887  -0.0947 -0.0045 271 PHE   A CE2 
1716 C  CZ  . PHE   A 251 ? 2.7971 2.2233 2.2064 0.1918  -0.1275 -0.0294 271 PHE   A CZ  
1717 N  N   . LEU   A 252 ? 3.1933 2.2928 2.3158 0.3034  -0.1419 0.0516  272 LEU   A N   
1718 C  CA  . LEU   A 252 ? 3.1347 2.1794 2.1510 0.3211  -0.1307 0.0726  272 LEU   A CA  
1719 C  C   . LEU   A 252 ? 3.2483 2.2412 2.1810 0.3780  -0.1805 0.0769  272 LEU   A C   
1720 O  O   . LEU   A 252 ? 3.2695 2.2565 2.1398 0.4005  -0.2008 0.0741  272 LEU   A O   
1721 C  CB  . LEU   A 252 ? 3.0102 1.9834 1.9746 0.3007  -0.0689 0.1062  272 LEU   A CB  
1722 C  CG  . LEU   A 252 ? 3.0671 1.9600 1.9055 0.3223  -0.0452 0.1370  272 LEU   A CG  
1723 C  CD1 . LEU   A 252 ? 2.9622 1.9020 1.7968 0.3080  -0.0312 0.1279  272 LEU   A CD1 
1724 C  CD2 . LEU   A 252 ? 3.1227 1.9403 1.9293 0.3018  0.0147  0.1707  272 LEU   A CD2 
1725 N  N   . GLN   A 253 ? 3.2225 2.1771 2.1524 0.4039  -0.2030 0.0821  273 GLN   A N   
1726 C  CA  . GLN   A 253 ? 3.3038 2.2167 2.1646 0.4617  -0.2581 0.0833  273 GLN   A CA  
1727 C  C   . GLN   A 253 ? 3.2341 2.2312 2.1538 0.4753  -0.3167 0.0451  273 GLN   A C   
1728 O  O   . GLN   A 253 ? 3.3224 2.3068 2.1747 0.5054  -0.3498 0.0401  273 GLN   A O   
1729 C  CB  . GLN   A 253 ? 3.3063 2.1718 2.1719 0.4851  -0.2701 0.0933  273 GLN   A CB  
1730 C  CG  . GLN   A 253 ? 3.4356 2.2582 2.2348 0.5488  -0.3302 0.0950  273 GLN   A CG  
1731 C  CD  . GLN   A 253 ? 3.6751 2.3731 2.3282 0.5822  -0.3120 0.1380  273 GLN   A CD  
1732 O  OE1 . GLN   A 253 ? 3.7021 2.3300 2.3304 0.5956  -0.2980 0.1610  273 GLN   A OE1 
1733 N  NE2 . GLN   A 253 ? 3.7205 2.3857 2.2725 0.5969  -0.3100 0.1496  273 GLN   A NE2 
1734 N  N   . LEU   A 254 ? 3.2362 2.3187 2.2817 0.4520  -0.3280 0.0170  274 LEU   A N   
1735 C  CA  . LEU   A 254 ? 3.1337 2.3003 2.2547 0.4593  -0.3784 -0.0196 274 LEU   A CA  
1736 C  C   . LEU   A 254 ? 3.1599 2.3642 2.2728 0.4429  -0.3773 -0.0326 274 LEU   A C   
1737 O  O   . LEU   A 254 ? 3.0844 2.3525 2.2570 0.4482  -0.4192 -0.0633 274 LEU   A O   
1738 C  CB  . LEU   A 254 ? 2.9025 2.1481 2.1571 0.4313  -0.3744 -0.0417 274 LEU   A CB  
1739 C  CG  . LEU   A 254 ? 2.8979 2.1140 2.1759 0.4403  -0.3670 -0.0330 274 LEU   A CG  
1740 C  CD1 . LEU   A 254 ? 2.7125 2.0086 2.1143 0.4081  -0.3540 -0.0556 274 LEU   A CD1 
1741 C  CD2 . LEU   A 254 ? 2.7733 1.9548 2.0190 0.4968  -0.4211 -0.0343 274 LEU   A CD2 
1742 N  N   . MET   A 255 ? 3.1780 2.3466 2.2260 0.4233  -0.3306 -0.0118 275 MET   A N   
1743 C  CA  . MET   A 255 ? 3.2103 2.4119 2.2494 0.4110  -0.3288 -0.0251 275 MET   A CA  
1744 C  C   . MET   A 255 ? 3.3977 2.5377 2.3131 0.4534  -0.3557 -0.0197 275 MET   A C   
1745 O  O   . MET   A 255 ? 3.4300 2.6034 2.3512 0.4669  -0.3973 -0.0468 275 MET   A O   
1746 C  CB  . MET   A 255 ? 3.1277 2.3378 2.1774 0.3660  -0.2632 -0.0103 275 MET   A CB  
1747 C  CG  . MET   A 255 ? 2.9771 2.2673 2.1526 0.3228  -0.2446 -0.0255 275 MET   A CG  
1748 S  SD  . MET   A 255 ? 2.6709 1.9780 1.8637 0.2737  -0.1756 -0.0116 275 MET   A SD  
1749 C  CE  . MET   A 255 ? 2.5881 1.9636 1.8174 0.2649  -0.1911 -0.0376 275 MET   A CE  
1750 N  N   . ILE   A 256 ? 3.6620 2.7091 2.4621 0.4742  -0.3306 0.0150  276 ILE   A N   
1751 C  CA  . ILE   A 256 ? 3.8132 2.7927 2.4809 0.5213  -0.3581 0.0222  276 ILE   A CA  
1752 C  C   . ILE   A 256 ? 3.8484 2.8256 2.5098 0.5698  -0.4345 0.0037  276 ILE   A C   
1753 O  O   . ILE   A 256 ? 3.8554 2.8092 2.4386 0.6085  -0.4793 -0.0085 276 ILE   A O   
1754 C  CB  . ILE   A 256 ? 3.8631 2.7379 2.4059 0.5325  -0.3071 0.0682  276 ILE   A CB  
1755 C  CG1 . ILE   A 256 ? 3.7187 2.6037 2.3118 0.4785  -0.2307 0.0878  276 ILE   A CG1 
1756 C  CG2 . ILE   A 256 ? 3.8617 2.6809 2.2695 0.5638  -0.3092 0.0753  276 ILE   A CG2 
1757 C  CD1 . ILE   A 256 ? 3.6963 2.4806 2.1833 0.4833  -0.1742 0.1335  276 ILE   A CD1 
1758 N  N   . ASP   A 257 ? 3.5894 2.5915 2.3328 0.5701  -0.4517 -0.0008 277 ASP   A N   
1759 C  CA  . ASP   A 257 ? 3.5656 2.5777 2.3222 0.6158  -0.5254 -0.0213 277 ASP   A CA  
1760 C  C   . ASP   A 257 ? 3.4635 2.5683 2.3126 0.6102  -0.5757 -0.0679 277 ASP   A C   
1761 O  O   . ASP   A 257 ? 3.4494 2.5605 2.2864 0.6481  -0.6379 -0.0910 277 ASP   A O   
1762 C  CB  . ASP   A 257 ? 3.4818 2.4993 2.3094 0.6171  -0.5254 -0.0149 277 ASP   A CB  
1763 C  CG  . ASP   A 257 ? 3.5550 2.4725 2.2927 0.6251  -0.4799 0.0300  277 ASP   A CG  
1764 O  OD1 . ASP   A 257 ? 3.7040 2.5530 2.3313 0.6249  -0.4421 0.0580  277 ASP   A OD1 
1765 O  OD2 . ASP   A 257 ? 3.5380 2.4438 2.3173 0.6312  -0.4793 0.0373  277 ASP   A OD2 
1766 N  N   . SER   A 258 ? 3.3933 2.5729 2.3446 0.5599  -0.5459 -0.0839 278 SER   A N   
1767 C  CA  . SER   A 258 ? 3.2835 2.5446 2.3213 0.5489  -0.5839 -0.1251 278 SER   A CA  
1768 C  C   . SER   A 258 ? 3.3532 2.6026 2.3261 0.5423  -0.5751 -0.1319 278 SER   A C   
1769 O  O   . SER   A 258 ? 3.2118 2.5229 2.2539 0.5274  -0.5982 -0.1650 278 SER   A O   
1770 C  CB  . SER   A 258 ? 3.0652 2.4133 2.2520 0.5016  -0.5586 -0.1388 278 SER   A CB  
1771 O  OG  . SER   A 258 ? 2.9855 2.3165 2.1706 0.4673  -0.4914 -0.1103 278 SER   A OG  
1772 N  N   . GLN   A 259 ? 3.5080 2.6774 2.3510 0.5533  -0.5396 -0.1014 279 GLN   A N   
1773 C  CA  . GLN   A 259 ? 3.4780 2.6249 2.2407 0.5562  -0.5316 -0.1069 279 GLN   A CA  
1774 C  C   . GLN   A 259 ? 3.5444 2.6483 2.2209 0.6048  -0.5818 -0.1207 279 GLN   A C   
1775 O  O   . GLN   A 259 ? 3.4685 2.6128 2.1852 0.6066  -0.6170 -0.1577 279 GLN   A O   
1776 C  CB  . GLN   A 259 ? 3.4506 2.5410 2.1328 0.5380  -0.4555 -0.0678 279 GLN   A CB  
1777 C  CG  . GLN   A 259 ? 3.5537 2.5905 2.1087 0.5593  -0.4475 -0.0652 279 GLN   A CG  
1778 C  CD  . GLN   A 259 ? 3.5175 2.4902 1.9864 0.5477  -0.3708 -0.0225 279 GLN   A CD  
1779 O  OE1 . GLN   A 259 ? 3.3788 2.3748 1.9156 0.5060  -0.3162 -0.0046 279 GLN   A OE1 
1780 N  NE2 . GLN   A 259 ? 3.5648 2.4618 1.8970 0.5815  -0.3626 -0.0079 279 GLN   A NE2 
1781 N  N   . LYS   A 268 ? 3.0549 2.4905 2.1709 0.4604  -0.6429 -0.3273 288 LYS   A N   
1782 C  CA  . LYS   A 268 ? 2.9369 2.4398 2.1841 0.4377  -0.6590 -0.3370 288 LYS   A CA  
1783 C  C   . LYS   A 268 ? 2.9044 2.3915 2.1266 0.4491  -0.6522 -0.3077 288 LYS   A C   
1784 O  O   . LYS   A 268 ? 2.7753 2.3138 2.1033 0.4341  -0.6573 -0.3089 288 LYS   A O   
1785 C  CB  . LYS   A 268 ? 2.8901 2.4349 2.2329 0.4434  -0.7111 -0.3727 288 LYS   A CB  
1786 C  CG  . LYS   A 268 ? 2.7514 2.3759 2.2507 0.4095  -0.7169 -0.3894 288 LYS   A CG  
1787 C  CD  . LYS   A 268 ? 2.7736 2.4353 2.3644 0.4162  -0.7641 -0.4232 288 LYS   A CD  
1788 C  CE  . LYS   A 268 ? 2.6602 2.3993 2.4068 0.3847  -0.7633 -0.4348 288 LYS   A CE  
1789 N  NZ  . LYS   A 268 ? 2.4211 2.1959 2.2581 0.3927  -0.8062 -0.4658 288 LYS   A NZ  
1790 N  N   . ALA   A 269 ? 2.9771 2.3918 2.0679 0.4733  -0.6297 -0.2774 289 ALA   A N   
1791 C  CA  . ALA   A 269 ? 2.9172 2.3055 1.9828 0.4768  -0.6000 -0.2399 289 ALA   A CA  
1792 C  C   . ALA   A 269 ? 2.9242 2.3040 1.9778 0.4425  -0.5209 -0.2070 289 ALA   A C   
1793 O  O   . ALA   A 269 ? 2.9552 2.3665 2.0478 0.4139  -0.4939 -0.2154 289 ALA   A O   
1794 C  CB  . ALA   A 269 ? 3.0706 2.3824 2.0107 0.5260  -0.6248 -0.2263 289 ALA   A CB  
1795 N  N   . LEU   A 270 ? 2.8209 2.1573 1.8231 0.4457  -0.4845 -0.1703 290 LEU   A N   
1796 C  CA  . LEU   A 270 ? 2.6934 2.0285 1.7017 0.4108  -0.4123 -0.1409 290 LEU   A CA  
1797 C  C   . LEU   A 270 ? 2.8236 2.0878 1.7012 0.4243  -0.3744 -0.1178 290 LEU   A C   
1798 O  O   . LEU   A 270 ? 3.0227 2.2183 1.7841 0.4649  -0.3951 -0.1099 290 LEU   A O   
1799 C  CB  . LEU   A 270 ? 2.6649 1.9978 1.7098 0.3999  -0.3900 -0.1166 290 LEU   A CB  
1800 C  CG  . LEU   A 270 ? 2.6171 1.9469 1.6721 0.3637  -0.3191 -0.0877 290 LEU   A CG  
1801 C  CD1 . LEU   A 270 ? 2.4345 1.8420 1.5968 0.3217  -0.2965 -0.1019 290 LEU   A CD1 
1802 C  CD2 . LEU   A 270 ? 2.6924 1.9995 1.7591 0.3618  -0.3046 -0.0657 290 LEU   A CD2 
1803 N  N   . SER   A 271 ? 2.6698 1.9519 1.5673 0.3913  -0.3175 -0.1065 291 SER   A N   
1804 C  CA  . SER   A 271 ? 2.7109 1.9379 1.5051 0.3968  -0.2689 -0.0839 291 SER   A CA  
1805 C  C   . SER   A 271 ? 2.7235 1.9175 1.5000 0.3808  -0.2121 -0.0440 291 SER   A C   
1806 O  O   . SER   A 271 ? 2.6340 1.8379 1.4632 0.3712  -0.2165 -0.0354 291 SER   A O   
1807 C  CB  . SER   A 271 ? 2.6148 1.8851 1.4495 0.3725  -0.2425 -0.0985 291 SER   A CB  
1808 O  OG  . SER   A 271 ? 2.6183 1.8509 1.3835 0.3680  -0.1810 -0.0727 291 SER   A OG  
1809 N  N   . ASP   A 272 ? 2.7163 1.8710 1.4225 0.3767  -0.1559 -0.0208 292 ASP   A N   
1810 C  CA  . ASP   A 272 ? 2.7573 1.8731 1.4409 0.3606  -0.0971 0.0172  292 ASP   A CA  
1811 C  C   . ASP   A 272 ? 2.6231 1.7942 1.3964 0.3129  -0.0411 0.0229  292 ASP   A C   
1812 O  O   . ASP   A 272 ? 2.5525 1.7415 1.3925 0.2845  -0.0189 0.0352  292 ASP   A O   
1813 C  CB  . ASP   A 272 ? 2.8897 1.9119 1.4223 0.3928  -0.0689 0.0444  292 ASP   A CB  
1814 C  CG  . ASP   A 272 ? 3.0433 1.9980 1.4776 0.4417  -0.1194 0.0480  292 ASP   A CG  
1815 O  OD1 . ASP   A 272 ? 2.9745 1.9611 1.4678 0.4496  -0.1772 0.0274  292 ASP   A OD1 
1816 O  OD2 . ASP   A 272 ? 3.1930 2.0632 1.4914 0.4738  -0.1009 0.0720  292 ASP   A OD2 
1817 N  N   . LEU   A 273 ? 2.6552 1.8528 1.4307 0.3051  -0.0188 0.0129  293 LEU   A N   
1818 C  CA  . LEU   A 273 ? 2.5935 1.8562 1.4684 0.2625  0.0238  0.0130  293 LEU   A CA  
1819 C  C   . LEU   A 273 ? 2.5011 1.8411 1.5004 0.2389  -0.0096 -0.0096 293 LEU   A C   
1820 O  O   . LEU   A 273 ? 2.4483 1.8367 1.5337 0.2037  0.0185  -0.0056 293 LEU   A O   
1821 C  CB  . LEU   A 273 ? 2.6994 1.9768 1.5545 0.2643  0.0491  0.0042  293 LEU   A CB  
1822 C  CG  . LEU   A 273 ? 2.8120 2.1563 1.7639 0.2256  0.0936  0.0047  293 LEU   A CG  
1823 C  CD1 . LEU   A 273 ? 2.8153 2.1497 1.7893 0.1986  0.1455  0.0336  293 LEU   A CD1 
1824 C  CD2 . LEU   A 273 ? 2.8435 2.1910 1.7617 0.2350  0.1208  -0.0020 293 LEU   A CD2 
1825 N  N   . GLU   A 274 ? 2.4592 1.8119 1.4697 0.2582  -0.0691 -0.0339 294 GLU   A N   
1826 C  CA  . GLU   A 274 ? 2.3248 1.7419 1.4464 0.2387  -0.0983 -0.0514 294 GLU   A CA  
1827 C  C   . GLU   A 274 ? 2.2341 1.6360 1.3747 0.2333  -0.0989 -0.0368 294 GLU   A C   
1828 O  O   . GLU   A 274 ? 2.1362 1.5899 1.3698 0.2077  -0.0984 -0.0428 294 GLU   A O   
1829 C  CB  . GLU   A 274 ? 2.3754 1.8109 1.5108 0.2595  -0.1585 -0.0822 294 GLU   A CB  
1830 C  CG  . GLU   A 274 ? 2.4375 1.8895 1.5660 0.2626  -0.1612 -0.1015 294 GLU   A CG  
1831 C  CD  . GLU   A 274 ? 2.4573 1.9323 1.6184 0.2767  -0.2206 -0.1349 294 GLU   A CD  
1832 O  OE1 . GLU   A 274 ? 2.4081 1.8637 1.5515 0.2990  -0.2644 -0.1424 294 GLU   A OE1 
1833 O  OE2 . GLU   A 274 ? 2.3951 1.9077 1.6040 0.2653  -0.2234 -0.1541 294 GLU   A OE2 
1834 N  N   . LEU   A 275 ? 2.3726 1.7002 1.4218 0.2591  -0.0997 -0.0175 295 LEU   A N   
1835 C  CA  . LEU   A 275 ? 2.3872 1.6896 1.4477 0.2557  -0.0960 -0.0015 295 LEU   A CA  
1836 C  C   . LEU   A 275 ? 2.2973 1.6111 1.4019 0.2167  -0.0388 0.0164  295 LEU   A C   
1837 O  O   . LEU   A 275 ? 2.2305 1.5648 1.4005 0.1977  -0.0373 0.0159  295 LEU   A O   
1838 C  CB  . LEU   A 275 ? 2.5357 1.7471 1.4782 0.2953  -0.1069 0.0186  295 LEU   A CB  
1839 C  CG  . LEU   A 275 ? 2.5756 1.7452 1.5115 0.3058  -0.1164 0.0336  295 LEU   A CG  
1840 C  CD1 . LEU   A 275 ? 2.8532 1.9518 1.6821 0.3578  -0.1568 0.0401  295 LEU   A CD1 
1841 C  CD2 . LEU   A 275 ? 2.5781 1.7080 1.5056 0.2801  -0.0557 0.0643  295 LEU   A CD2 
1842 N  N   . VAL   A 276 ? 2.3454 1.6473 1.4173 0.2051  0.0082  0.0303  296 VAL   A N   
1843 C  CA  . VAL   A 276 ? 2.3171 1.6369 1.4406 0.1663  0.0616  0.0441  296 VAL   A CA  
1844 C  C   . VAL   A 276 ? 2.1836 1.5930 1.4267 0.1350  0.0534  0.0219  296 VAL   A C   
1845 O  O   . VAL   A 276 ? 2.1408 1.5698 1.4455 0.1084  0.0677  0.0236  296 VAL   A O   
1846 C  CB  . VAL   A 276 ? 2.4051 1.7049 1.4796 0.1619  0.1129  0.0601  296 VAL   A CB  
1847 C  CG1 . VAL   A 276 ? 2.5499 1.8833 1.6978 0.1191  0.1645  0.0690  296 VAL   A CG1 
1848 C  CG2 . VAL   A 276 ? 2.7199 1.9228 1.6663 0.1933  0.1278  0.0865  296 VAL   A CG2 
1849 N  N   . ALA   A 277 ? 2.1449 1.6056 1.4183 0.1391  0.0299  0.0005  297 ALA   A N   
1850 C  CA  . ALA   A 277 ? 2.0326 1.5742 1.4097 0.1121  0.0259  -0.0173 297 ALA   A CA  
1851 C  C   . ALA   A 277 ? 1.8894 1.4531 1.3245 0.1058  -0.0019 -0.0271 297 ALA   A C   
1852 O  O   . ALA   A 277 ? 1.8383 1.4474 1.3457 0.0785  0.0106  -0.0318 297 ALA   A O   
1853 C  CB  . ALA   A 277 ? 2.0506 1.6301 1.4409 0.1221  0.0035  -0.0367 297 ALA   A CB  
1854 N  N   . GLN   A 278 ? 1.8792 1.4120 1.2829 0.1328  -0.0403 -0.0316 298 GLN   A N   
1855 C  CA  . GLN   A 278 ? 1.9119 1.4639 1.3700 0.1305  -0.0645 -0.0412 298 GLN   A CA  
1856 C  C   . GLN   A 278 ? 1.9062 1.4266 1.3651 0.1152  -0.0367 -0.0258 298 GLN   A C   
1857 O  O   . GLN   A 278 ? 1.9410 1.4943 1.4645 0.0982  -0.0381 -0.0350 298 GLN   A O   
1858 C  CB  . GLN   A 278 ? 1.9923 1.5191 1.4195 0.1658  -0.1122 -0.0499 298 GLN   A CB  
1859 C  CG  . GLN   A 278 ? 1.9738 1.5181 1.3888 0.1831  -0.1423 -0.0667 298 GLN   A CG  
1860 C  CD  . GLN   A 278 ? 1.9172 1.5372 1.4209 0.1621  -0.1472 -0.0861 298 GLN   A CD  
1861 O  OE1 . GLN   A 278 ? 1.8851 1.5477 1.4618 0.1438  -0.1444 -0.0917 298 GLN   A OE1 
1862 N  NE2 . GLN   A 278 ? 1.9047 1.5376 1.3981 0.1662  -0.1532 -0.0963 298 GLN   A NE2 
1863 N  N   . SER   A 279 ? 2.0214 1.4742 1.4067 0.1213  -0.0097 -0.0026 299 SER   A N   
1864 C  CA  . SER   A 279 ? 2.0759 1.4923 1.4637 0.1031  0.0217  0.0127  299 SER   A CA  
1865 C  C   . SER   A 279 ? 1.9561 1.4279 1.4207 0.0617  0.0535  0.0063  299 SER   A C   
1866 O  O   . SER   A 279 ? 2.0286 1.5065 1.5392 0.0420  0.0606  0.0018  299 SER   A O   
1867 C  CB  . SER   A 279 ? 2.1908 1.5222 1.4832 0.1161  0.0514  0.0418  299 SER   A CB  
1868 O  OG  . SER   A 279 ? 2.3172 1.6002 1.5274 0.1587  0.0189  0.0466  299 SER   A OG  
1869 N  N   . ILE   A 280 ? 1.8602 1.3727 1.3393 0.0501  0.0706  0.0038  300 ILE   A N   
1870 C  CA  . ILE   A 280 ? 1.7993 1.3692 1.3520 0.0142  0.0970  -0.0032 300 ILE   A CA  
1871 C  C   . ILE   A 280 ? 1.7499 1.3836 1.3789 0.0040  0.0697  -0.0261 300 ILE   A C   
1872 O  O   . ILE   A 280 ? 1.7599 1.4199 1.4429 -0.0219 0.0817  -0.0333 300 ILE   A O   
1873 C  CB  . ILE   A 280 ? 1.7746 1.3745 1.3247 0.0107  0.1181  -0.0012 300 ILE   A CB  
1874 C  CG1 . ILE   A 280 ? 1.8668 1.3998 1.3349 0.0221  0.1511  0.0227  300 ILE   A CG1 
1875 C  CG2 . ILE   A 280 ? 1.7306 1.3955 1.3617 -0.0230 0.1409  -0.0097 300 ILE   A CG2 
1876 C  CD1 . ILE   A 280 ? 1.9457 1.5037 1.4061 0.0221  0.1758  0.0243  300 ILE   A CD1 
1877 N  N   . ILE   A 281 ? 1.7883 1.4464 1.4224 0.0242  0.0335  -0.0387 301 ILE   A N   
1878 C  CA  . ILE   A 281 ? 1.7795 1.4939 1.4805 0.0171  0.0114  -0.0579 301 ILE   A CA  
1879 C  C   . ILE   A 281 ? 1.8546 1.5461 1.5679 0.0150  0.0056  -0.0611 301 ILE   A C   
1880 O  O   . ILE   A 281 ? 1.7849 1.5104 1.5494 -0.0050 0.0109  -0.0721 301 ILE   A O   
1881 C  CB  . ILE   A 281 ? 1.6809 1.4185 1.3862 0.0390  -0.0231 -0.0692 301 ILE   A CB  
1882 C  CG1 . ILE   A 281 ? 1.6373 1.4075 1.3471 0.0367  -0.0166 -0.0710 301 ILE   A CG1 
1883 C  CG2 . ILE   A 281 ? 1.6244 1.4059 1.3906 0.0359  -0.0432 -0.0854 301 ILE   A CG2 
1884 C  CD1 . ILE   A 281 ? 1.5883 1.4193 1.3596 0.0122  -0.0007 -0.0770 301 ILE   A CD1 
1885 N  N   . PHE   A 282 ? 1.9205 1.5517 1.5834 0.0382  -0.0069 -0.0524 302 PHE   A N   
1886 C  CA  . PHE   A 282 ? 1.9411 1.5446 1.6130 0.0413  -0.0138 -0.0556 302 PHE   A CA  
1887 C  C   . PHE   A 282 ? 1.9296 1.5095 1.6108 0.0135  0.0198  -0.0498 302 PHE   A C   
1888 O  O   . PHE   A 282 ? 1.9268 1.5152 1.6462 0.0023  0.0186  -0.0624 302 PHE   A O   
1889 C  CB  . PHE   A 282 ? 2.0247 1.5639 1.6353 0.0759  -0.0347 -0.0450 302 PHE   A CB  
1890 C  CG  . PHE   A 282 ? 2.1509 1.7188 1.7770 0.1025  -0.0764 -0.0593 302 PHE   A CG  
1891 C  CD1 . PHE   A 282 ? 2.1005 1.7173 1.7451 0.1032  -0.0892 -0.0688 302 PHE   A CD1 
1892 C  CD2 . PHE   A 282 ? 2.2880 1.8333 1.9147 0.1269  -0.1023 -0.0641 302 PHE   A CD2 
1893 C  CE1 . PHE   A 282 ? 2.0410 1.6846 1.7090 0.1242  -0.1265 -0.0836 302 PHE   A CE1 
1894 C  CE2 . PHE   A 282 ? 2.2703 1.8477 1.9228 0.1498  -0.1403 -0.0790 302 PHE   A CE2 
1895 C  CZ  . PHE   A 282 ? 2.1674 1.7943 1.8426 0.1468  -0.1522 -0.0892 302 PHE   A CZ  
1896 N  N   . ILE   A 283 ? 1.8842 1.4340 1.5327 0.0017  0.0512  -0.0324 303 ILE   A N   
1897 C  CA  . ILE   A 283 ? 1.8885 1.4131 1.5519 -0.0275 0.0853  -0.0269 303 ILE   A CA  
1898 C  C   . ILE   A 283 ? 1.8695 1.4664 1.6108 -0.0590 0.0907  -0.0478 303 ILE   A C   
1899 O  O   . ILE   A 283 ? 1.9062 1.4979 1.6808 -0.0791 0.0982  -0.0583 303 ILE   A O   
1900 C  CB  . ILE   A 283 ? 1.9440 1.4219 1.5574 -0.0323 0.1221  -0.0017 303 ILE   A CB  
1901 C  CG1 . ILE   A 283 ? 2.0242 1.4104 1.5523 -0.0027 0.1209  0.0212  303 ILE   A CG1 
1902 C  CG2 . ILE   A 283 ? 1.9985 1.4779 1.6544 -0.0716 0.1613  -0.0006 303 ILE   A CG2 
1903 C  CD1 . ILE   A 283 ? 1.9773 1.3145 1.4370 0.0024  0.1547  0.0482  303 ILE   A CD1 
1904 N  N   . PHE   A 284 ? 1.7745 1.4372 1.5435 -0.0618 0.0850  -0.0553 304 PHE   A N   
1905 C  CA  . PHE   A 284 ? 1.7801 1.5126 1.6169 -0.0859 0.0850  -0.0746 304 PHE   A CA  
1906 C  C   . PHE   A 284 ? 1.7469 1.4996 1.6123 -0.0817 0.0597  -0.0943 304 PHE   A C   
1907 O  O   . PHE   A 284 ? 1.8046 1.5670 1.7041 -0.1016 0.0641  -0.1088 304 PHE   A O   
1908 C  CB  . PHE   A 284 ? 1.7032 1.4953 1.5570 -0.0832 0.0815  -0.0762 304 PHE   A CB  
1909 C  CG  . PHE   A 284 ? 1.6906 1.5548 1.6059 -0.0989 0.0734  -0.0951 304 PHE   A CG  
1910 C  CD1 . PHE   A 284 ? 1.6201 1.5163 1.5772 -0.1255 0.0925  -0.1006 304 PHE   A CD1 
1911 C  CD2 . PHE   A 284 ? 1.7024 1.6022 1.6341 -0.0860 0.0469  -0.1071 304 PHE   A CD2 
1912 C  CE1 . PHE   A 284 ? 1.6248 1.5859 1.6318 -0.1359 0.0806  -0.1184 304 PHE   A CE1 
1913 C  CE2 . PHE   A 284 ? 1.5577 1.5174 1.5345 -0.0969 0.0403  -0.1219 304 PHE   A CE2 
1914 C  CZ  . PHE   A 284 ? 1.6120 1.6019 1.6231 -0.1203 0.0547  -0.1278 304 PHE   A CZ  
1915 N  N   . ALA   A 285 ? 1.7481 1.5078 1.6013 -0.0556 0.0336  -0.0967 305 ALA   A N   
1916 C  CA  . ALA   A 285 ? 1.7450 1.5297 1.6273 -0.0488 0.0132  -0.1145 305 ALA   A CA  
1917 C  C   . ALA   A 285 ? 1.8176 1.5567 1.6969 -0.0527 0.0169  -0.1210 305 ALA   A C   
1918 O  O   . ALA   A 285 ? 1.8960 1.6579 1.8084 -0.0671 0.0176  -0.1392 305 ALA   A O   
1919 C  CB  . ALA   A 285 ? 1.7233 1.5130 1.5947 -0.0198 -0.0119 -0.1135 305 ALA   A CB  
1920 N  N   . GLY   A 286 ? 1.8204 1.4907 1.6558 -0.0378 0.0187  -0.1065 306 GLY   A N   
1921 C  CA  . GLY   A 286 ? 1.9121 1.5297 1.7415 -0.0385 0.0229  -0.1110 306 GLY   A CA  
1922 C  C   . GLY   A 286 ? 1.9812 1.5880 1.8325 -0.0729 0.0477  -0.1175 306 GLY   A C   
1923 O  O   . GLY   A 286 ? 1.9811 1.5537 1.8397 -0.0781 0.0499  -0.1288 306 GLY   A O   
1924 N  N   . TYR   A 287 ? 2.0963 1.7321 1.9628 -0.0963 0.0661  -0.1126 307 TYR   A N   
1925 C  CA  . TYR   A 287 ? 2.0780 1.7160 1.9804 -0.1320 0.0874  -0.1228 307 TYR   A CA  
1926 C  C   . TYR   A 287 ? 1.9806 1.6954 1.9362 -0.1465 0.0737  -0.1503 307 TYR   A C   
1927 O  O   . TYR   A 287 ? 2.0609 1.7742 2.0383 -0.1562 0.0673  -0.1728 307 TYR   A O   
1928 C  CB  . TYR   A 287 ? 2.1302 1.7587 2.0272 -0.1498 0.1178  -0.1033 307 TYR   A CB  
1929 C  CG  . TYR   A 287 ? 2.1728 1.8287 2.1273 -0.1892 0.1365  -0.1181 307 TYR   A CG  
1930 C  CD1 . TYR   A 287 ? 2.3038 1.9059 2.2698 -0.2114 0.1543  -0.1226 307 TYR   A CD1 
1931 C  CD2 . TYR   A 287 ? 2.2000 1.9356 2.2011 -0.2035 0.1346  -0.1293 307 TYR   A CD2 
1932 C  CE1 . TYR   A 287 ? 2.3862 2.0167 2.4138 -0.2495 0.1685  -0.1403 307 TYR   A CE1 
1933 C  CE2 . TYR   A 287 ? 2.2559 2.0228 2.3166 -0.2382 0.1469  -0.1460 307 TYR   A CE2 
1934 C  CZ  . TYR   A 287 ? 2.3151 2.0310 2.3915 -0.2624 0.1632  -0.1528 307 TYR   A CZ  
1935 O  OH  . TYR   A 287 ? 2.2868 2.0365 2.4308 -0.2990 0.1729  -0.1730 307 TYR   A OH  
1936 N  N   . GLU   A 288 ? 1.7929 1.5715 1.7647 -0.1457 0.0687  -0.1489 308 GLU   A N   
1937 C  CA  . GLU   A 288 ? 1.7474 1.5966 1.7653 -0.1602 0.0588  -0.1711 308 GLU   A CA  
1938 C  C   . GLU   A 288 ? 1.7153 1.5864 1.7347 -0.1435 0.0352  -0.1889 308 GLU   A C   
1939 O  O   . GLU   A 288 ? 1.7546 1.6471 1.7977 -0.1555 0.0282  -0.2128 308 GLU   A O   
1940 C  CB  . GLU   A 288 ? 1.7326 1.6377 1.7639 -0.1598 0.0609  -0.1618 308 GLU   A CB  
1941 C  CG  . GLU   A 288 ? 1.6983 1.6588 1.7808 -0.1855 0.0654  -0.1765 308 GLU   A CG  
1942 C  CD  . GLU   A 288 ? 1.6723 1.6793 1.7787 -0.1862 0.0422  -0.2026 308 GLU   A CD  
1943 O  OE1 . GLU   A 288 ? 1.5354 1.5500 1.6212 -0.1639 0.0259  -0.2041 308 GLU   A OE1 
1944 O  OE2 . GLU   A 288 ? 1.7070 1.7430 1.8528 -0.2087 0.0405  -0.2223 308 GLU   A OE2 
1945 N  N   . THR   A 289 ? 1.6293 1.4960 1.6246 -0.1157 0.0234  -0.1791 309 THR   A N   
1946 C  CA  . THR   A 289 ? 1.6091 1.4983 1.6101 -0.0995 0.0068  -0.1941 309 THR   A CA  
1947 C  C   . THR   A 289 ? 1.6122 1.4576 1.6084 -0.0994 0.0063  -0.2102 309 THR   A C   
1948 O  O   . THR   A 289 ? 1.5123 1.3806 1.5213 -0.1002 -0.0005 -0.2323 309 THR   A O   
1949 C  CB  . THR   A 289 ? 1.5596 1.4522 1.5462 -0.0720 -0.0041 -0.1810 309 THR   A CB  
1950 O  OG1 . THR   A 289 ? 1.7176 1.5504 1.6784 -0.0559 -0.0065 -0.1734 309 THR   A OG1 
1951 C  CG2 . THR   A 289 ? 1.4873 1.4015 1.4696 -0.0716 -0.0016 -0.1636 309 THR   A CG2 
1952 N  N   . THR   A 290 ? 1.7825 1.5608 1.7556 -0.0962 0.0142  -0.1992 310 THR   A N   
1953 C  CA  . THR   A 290 ? 1.8060 1.5338 1.7736 -0.0943 0.0149  -0.2135 310 THR   A CA  
1954 C  C   . THR   A 290 ? 1.7536 1.4841 1.7457 -0.1249 0.0221  -0.2364 310 THR   A C   
1955 O  O   . THR   A 290 ? 1.6934 1.4231 1.6929 -0.1239 0.0150  -0.2619 310 THR   A O   
1956 C  CB  . THR   A 290 ? 1.8643 1.5138 1.7975 -0.0832 0.0228  -0.1927 310 THR   A CB  
1957 O  OG1 . THR   A 290 ? 1.7870 1.4369 1.6989 -0.0518 0.0091  -0.1766 310 THR   A OG1 
1958 C  CG2 . THR   A 290 ? 1.9115 1.5022 1.8395 -0.0803 0.0246  -0.2069 310 THR   A CG2 
1959 N  N   . SER   A 291 ? 1.8235 1.5589 1.8310 -0.1521 0.0360  -0.2300 311 SER   A N   
1960 C  CA  . SER   A 291 ? 1.8055 1.5446 1.8460 -0.1839 0.0409  -0.2543 311 SER   A CA  
1961 C  C   . SER   A 291 ? 1.7231 1.5358 1.7881 -0.1875 0.0225  -0.2806 311 SER   A C   
1962 O  O   . SER   A 291 ? 1.7214 1.5324 1.7975 -0.1964 0.0137  -0.3108 311 SER   A O   
1963 C  CB  . SER   A 291 ? 1.8560 1.5888 1.9164 -0.2122 0.0629  -0.2401 311 SER   A CB  
1964 O  OG  . SER   A 291 ? 1.7517 1.5542 1.8304 -0.2145 0.0603  -0.2331 311 SER   A OG  
1965 N  N   . SER   A 292 ? 1.6176 1.4915 1.6871 -0.1790 0.0160  -0.2697 312 SER   A N   
1966 C  CA  . SER   A 292 ? 1.5714 1.5132 1.6586 -0.1806 -0.0005 -0.2900 312 SER   A CA  
1967 C  C   . SER   A 292 ? 1.5614 1.5040 1.6283 -0.1605 -0.0136 -0.3094 312 SER   A C   
1968 O  O   . SER   A 292 ? 1.5031 1.4696 1.5766 -0.1671 -0.0257 -0.3377 312 SER   A O   
1969 C  CB  . SER   A 292 ? 1.4652 1.4617 1.5553 -0.1703 -0.0028 -0.2703 312 SER   A CB  
1970 O  OG  . SER   A 292 ? 1.4394 1.4963 1.5400 -0.1678 -0.0189 -0.2866 312 SER   A OG  
1971 N  N   . VAL   A 293 ? 1.5598 1.4787 1.6022 -0.1344 -0.0117 -0.2957 313 VAL   A N   
1972 C  CA  . VAL   A 293 ? 1.5497 1.4706 1.5766 -0.1137 -0.0187 -0.3127 313 VAL   A CA  
1973 C  C   . VAL   A 293 ? 1.5675 1.4387 1.5904 -0.1213 -0.0183 -0.3394 313 VAL   A C   
1974 O  O   . VAL   A 293 ? 1.6107 1.4928 1.6247 -0.1152 -0.0255 -0.3663 313 VAL   A O   
1975 C  CB  . VAL   A 293 ? 1.3941 1.3058 1.4086 -0.0851 -0.0163 -0.2925 313 VAL   A CB  
1976 C  CG1 . VAL   A 293 ? 1.2055 1.1171 1.2104 -0.0635 -0.0179 -0.3101 313 VAL   A CG1 
1977 C  CG2 . VAL   A 293 ? 1.4813 1.4426 1.5020 -0.0790 -0.0181 -0.2712 313 VAL   A CG2 
1978 N  N   . LEU   A 294 ? 1.6722 1.4842 1.6979 -0.1341 -0.0084 -0.3325 314 LEU   A N   
1979 C  CA  . LEU   A 294 ? 1.6557 1.4118 1.6800 -0.1432 -0.0064 -0.3574 314 LEU   A CA  
1980 C  C   . LEU   A 294 ? 1.6500 1.4325 1.6951 -0.1697 -0.0159 -0.3911 314 LEU   A C   
1981 O  O   . LEU   A 294 ? 1.6845 1.4503 1.7214 -0.1676 -0.0235 -0.4235 314 LEU   A O   
1982 C  CB  . LEU   A 294 ? 1.7559 1.4399 1.7779 -0.1532 0.0091  -0.3381 314 LEU   A CB  
1983 C  CG  . LEU   A 294 ? 1.7101 1.3444 1.7038 -0.1214 0.0126  -0.3172 314 LEU   A CG  
1984 C  CD1 . LEU   A 294 ? 1.7391 1.2991 1.7210 -0.1302 0.0285  -0.2942 314 LEU   A CD1 
1985 C  CD2 . LEU   A 294 ? 1.6692 1.2797 1.6526 -0.0999 0.0065  -0.3419 314 LEU   A CD2 
1986 N  N   . SER   A 295 ? 1.6105 1.4363 1.6833 -0.1929 -0.0174 -0.3861 315 SER   A N   
1987 C  CA  . SER   A 295 ? 1.6380 1.5029 1.7360 -0.2151 -0.0327 -0.4196 315 SER   A CA  
1988 C  C   . SER   A 295 ? 1.5762 1.4900 1.6493 -0.1928 -0.0516 -0.4387 315 SER   A C   
1989 O  O   . SER   A 295 ? 1.6256 1.5451 1.6962 -0.1988 -0.0672 -0.4761 315 SER   A O   
1990 C  CB  . SER   A 295 ? 1.6968 1.6078 1.8346 -0.2389 -0.0305 -0.4072 315 SER   A CB  
1991 O  OG  . SER   A 295 ? 1.7352 1.6033 1.8839 -0.2517 -0.0064 -0.3789 315 SER   A OG  
1992 N  N   . PHE   A 296 ? 1.4875 1.4343 1.5399 -0.1667 -0.0495 -0.4139 316 PHE   A N   
1993 C  CA  . PHE   A 296 ? 1.4882 1.4766 1.5121 -0.1436 -0.0608 -0.4256 316 PHE   A CA  
1994 C  C   . PHE   A 296 ? 1.5225 1.4718 1.5163 -0.1263 -0.0594 -0.4499 316 PHE   A C   
1995 O  O   . PHE   A 296 ? 1.4876 1.4542 1.4587 -0.1195 -0.0717 -0.4794 316 PHE   A O   
1996 C  CB  . PHE   A 296 ? 1.4654 1.4870 1.4796 -0.1216 -0.0533 -0.3911 316 PHE   A CB  
1997 C  CG  . PHE   A 296 ? 1.4874 1.5671 1.5174 -0.1287 -0.0610 -0.3781 316 PHE   A CG  
1998 C  CD1 . PHE   A 296 ? 1.4235 1.5457 1.4529 -0.1340 -0.0797 -0.4008 316 PHE   A CD1 
1999 C  CD2 . PHE   A 296 ? 1.4526 1.5433 1.4964 -0.1277 -0.0515 -0.3447 316 PHE   A CD2 
2000 C  CE1 . PHE   A 296 ? 1.4562 1.6322 1.5020 -0.1370 -0.0882 -0.3887 316 PHE   A CE1 
2001 C  CE2 . PHE   A 296 ? 1.4341 1.5761 1.4934 -0.1319 -0.0575 -0.3335 316 PHE   A CE2 
2002 C  CZ  . PHE   A 296 ? 1.4945 1.6798 1.5567 -0.1360 -0.0756 -0.3546 316 PHE   A CZ  
2003 N  N   . ILE   A 297 ? 1.5666 1.4622 1.5567 -0.1159 -0.0450 -0.4384 317 ILE   A N   
2004 C  CA  . ILE   A 297 ? 1.5627 1.4201 1.5281 -0.0960 -0.0413 -0.4607 317 ILE   A CA  
2005 C  C   . ILE   A 297 ? 1.6723 1.4956 1.6376 -0.1151 -0.0511 -0.5019 317 ILE   A C   
2006 O  O   . ILE   A 297 ? 1.7009 1.5233 1.6385 -0.1022 -0.0574 -0.5338 317 ILE   A O   
2007 C  CB  . ILE   A 297 ? 1.5742 1.3816 1.5414 -0.0792 -0.0268 -0.4389 317 ILE   A CB  
2008 C  CG1 . ILE   A 297 ? 1.5458 1.3897 1.5175 -0.0612 -0.0212 -0.4029 317 ILE   A CG1 
2009 C  CG2 . ILE   A 297 ? 1.5394 1.3094 1.4862 -0.0559 -0.0218 -0.4629 317 ILE   A CG2 
2010 C  CD1 . ILE   A 297 ? 1.4524 1.2540 1.4278 -0.0422 -0.0132 -0.3824 317 ILE   A CD1 
2011 N  N   . MET   A 298 ? 1.6296 1.4233 1.6259 -0.1465 -0.0513 -0.5031 318 MET   A N   
2012 C  CA  . MET   A 298 ? 1.8316 1.5868 1.8370 -0.1686 -0.0600 -0.5438 318 MET   A CA  
2013 C  C   . MET   A 298 ? 1.8274 1.6370 1.8319 -0.1790 -0.0845 -0.5785 318 MET   A C   
2014 O  O   . MET   A 298 ? 1.7233 1.5098 1.7164 -0.1834 -0.0973 -0.6216 318 MET   A O   
2015 C  CB  . MET   A 298 ? 1.8605 1.5711 1.9053 -0.2022 -0.0496 -0.5331 318 MET   A CB  
2016 C  CG  . MET   A 298 ? 1.8934 1.5393 1.9294 -0.1895 -0.0278 -0.5000 318 MET   A CG  
2017 S  SD  . MET   A 298 ? 2.0472 1.6430 2.0432 -0.1490 -0.0238 -0.5121 318 MET   A SD  
2018 C  CE  . MET   A 298 ? 1.7737 1.3160 1.7728 -0.1688 -0.0321 -0.5669 318 MET   A CE  
2019 N  N   . TYR   A 299 ? 1.5907 1.4702 1.6048 -0.1810 -0.0934 -0.5620 319 TYR   A N   
2020 C  CA  . TYR   A 299 ? 1.6191 1.5532 1.6240 -0.1826 -0.1201 -0.5926 319 TYR   A CA  
2021 C  C   . TYR   A 299 ? 1.6961 1.6333 1.6397 -0.1480 -0.1245 -0.6112 319 TYR   A C   
2022 O  O   . TYR   A 299 ? 1.7970 1.7411 1.7179 -0.1475 -0.1463 -0.6530 319 TYR   A O   
2023 C  CB  . TYR   A 299 ? 1.6317 1.6370 1.6559 -0.1853 -0.1269 -0.5663 319 TYR   A CB  
2024 C  CG  . TYR   A 299 ? 1.6711 1.7355 1.6715 -0.1745 -0.1551 -0.5899 319 TYR   A CG  
2025 C  CD1 . TYR   A 299 ? 1.7057 1.7943 1.7352 -0.1981 -0.1838 -0.6277 319 TYR   A CD1 
2026 C  CD2 . TYR   A 299 ? 1.6219 1.7166 1.5710 -0.1399 -0.1533 -0.5743 319 TYR   A CD2 
2027 C  CE1 . TYR   A 299 ? 1.7356 1.8773 1.7376 -0.1841 -0.2141 -0.6498 319 TYR   A CE1 
2028 C  CE2 . TYR   A 299 ? 1.6581 1.8003 1.5752 -0.1262 -0.1784 -0.5926 319 TYR   A CE2 
2029 C  CZ  . TYR   A 299 ? 1.7609 1.9265 1.7014 -0.1465 -0.2108 -0.6306 319 TYR   A CZ  
2030 O  OH  . TYR   A 299 ? 1.8739 2.0862 1.7766 -0.1286 -0.2401 -0.6490 319 TYR   A OH  
2031 N  N   . GLU   A 300 ? 1.7717 1.7046 1.6885 -0.1184 -0.1035 -0.5819 320 GLU   A N   
2032 C  CA  . GLU   A 300 ? 1.7694 1.7073 1.6305 -0.0846 -0.1001 -0.5954 320 GLU   A CA  
2033 C  C   . GLU   A 300 ? 1.9243 1.7996 1.7654 -0.0780 -0.0961 -0.6313 320 GLU   A C   
2034 O  O   . GLU   A 300 ? 1.9019 1.7773 1.6965 -0.0611 -0.1041 -0.6650 320 GLU   A O   
2035 C  CB  . GLU   A 300 ? 1.7243 1.6805 1.5760 -0.0580 -0.0767 -0.5537 320 GLU   A CB  
2036 C  CG  . GLU   A 300 ? 1.6853 1.7032 1.5445 -0.0581 -0.0806 -0.5224 320 GLU   A CG  
2037 C  CD  . GLU   A 300 ? 1.7683 1.8301 1.5869 -0.0475 -0.0985 -0.5402 320 GLU   A CD  
2038 O  OE1 . GLU   A 300 ? 1.5350 1.5822 1.3068 -0.0306 -0.1010 -0.5708 320 GLU   A OE1 
2039 O  OE2 . GLU   A 300 ? 1.7348 1.8437 1.5644 -0.0535 -0.1103 -0.5237 320 GLU   A OE2 
2040 N  N   . LEU   A 301 ? 1.8257 1.6431 1.6962 -0.0884 -0.0832 -0.6246 321 LEU   A N   
2041 C  CA  . LEU   A 301 ? 1.9204 1.6713 1.7758 -0.0830 -0.0798 -0.6595 321 LEU   A CA  
2042 C  C   . LEU   A 301 ? 2.0274 1.7656 1.8838 -0.1081 -0.1051 -0.7095 321 LEU   A C   
2043 O  O   . LEU   A 301 ? 2.0964 1.7978 1.9201 -0.0967 -0.1095 -0.7506 321 LEU   A O   
2044 C  CB  . LEU   A 301 ? 1.8878 1.5753 1.7743 -0.0890 -0.0623 -0.6383 321 LEU   A CB  
2045 C  CG  . LEU   A 301 ? 1.7859 1.4799 1.6783 -0.0655 -0.0423 -0.5917 321 LEU   A CG  
2046 C  CD1 . LEU   A 301 ? 1.7412 1.3626 1.6538 -0.0678 -0.0302 -0.5771 321 LEU   A CD1 
2047 C  CD2 . LEU   A 301 ? 1.8210 1.5375 1.6800 -0.0261 -0.0308 -0.5938 321 LEU   A CD2 
2048 N  N   . ALA   A 302 ? 2.2171 1.9866 2.1139 -0.1419 -0.1224 -0.7092 322 ALA   A N   
2049 C  CA  . ALA   A 302 ? 2.1585 1.9229 2.0696 -0.1693 -0.1500 -0.7590 322 ALA   A CA  
2050 C  C   . ALA   A 302 ? 2.0808 1.8916 1.9394 -0.1491 -0.1752 -0.7899 322 ALA   A C   
2051 O  O   . ALA   A 302 ? 2.1384 1.9193 1.9668 -0.1448 -0.1880 -0.8205 322 ALA   A O   
2052 C  CB  . ALA   A 302 ? 2.1556 1.9475 2.1347 -0.2104 -0.1587 -0.7476 322 ALA   A CB  
2053 N  N   . THR   A 303 ? 1.9753 1.8542 1.8157 -0.1331 -0.1795 -0.7653 323 THR   A N   
2054 C  CA  . THR   A 303 ? 1.9524 1.8731 1.7331 -0.1091 -0.2011 -0.7852 323 THR   A CA  
2055 C  C   . THR   A 303 ? 1.9645 1.8613 1.6715 -0.0675 -0.1818 -0.7914 323 THR   A C   
2056 O  O   . THR   A 303 ? 2.0238 1.9435 1.6690 -0.0436 -0.1933 -0.8013 323 THR   A O   
2057 C  CB  . THR   A 303 ? 1.9513 1.9479 1.7362 -0.1044 -0.2104 -0.7555 323 THR   A CB  
2058 O  OG1 . THR   A 303 ? 1.9343 1.9373 1.7115 -0.0836 -0.1770 -0.7033 323 THR   A OG1 
2059 C  CG2 . THR   A 303 ? 1.9687 1.9937 1.8318 -0.1441 -0.2264 -0.7504 323 THR   A CG2 
2060 N  N   . HIS   A 304 ? 2.0335 1.8842 1.7465 -0.0565 -0.1498 -0.7755 324 HIS   A N   
2061 C  CA  . HIS   A 304 ? 2.0727 1.8980 1.7284 -0.0177 -0.1264 -0.7822 324 HIS   A CA  
2062 C  C   . HIS   A 304 ? 2.1543 1.9029 1.8279 -0.0208 -0.1126 -0.8013 324 HIS   A C   
2063 O  O   . HIS   A 304 ? 2.1441 1.8692 1.8396 -0.0095 -0.0850 -0.7700 324 HIS   A O   
2064 C  CB  . HIS   A 304 ? 1.9851 1.8448 1.6347 0.0079  -0.0963 -0.7301 324 HIS   A CB  
2065 C  CG  . HIS   A 304 ? 1.8980 1.8254 1.5295 0.0126  -0.1065 -0.7072 324 HIS   A CG  
2066 N  ND1 . HIS   A 304 ? 1.8354 1.8002 1.5147 -0.0135 -0.1219 -0.6831 324 HIS   A ND1 
2067 C  CD2 . HIS   A 304 ? 1.9520 1.9128 1.5206 0.0423  -0.1016 -0.7035 324 HIS   A CD2 
2068 C  CE1 . HIS   A 304 ? 1.8091 1.8273 1.4579 0.0006  -0.1284 -0.6664 324 HIS   A CE1 
2069 N  NE2 . HIS   A 304 ? 1.8487 1.8637 1.4282 0.0342  -0.1161 -0.6770 324 HIS   A NE2 
2070 N  N   . PRO   A 305 ? 2.2907 1.9970 1.9568 -0.0354 -0.1306 -0.8368 325 PRO   A N   
2071 C  CA  . PRO   A 305 ? 2.3052 1.9315 1.9915 -0.0414 -0.1180 -0.8495 325 PRO   A CA  
2072 C  C   . PRO   A 305 ? 2.3334 1.9253 1.9810 -0.0003 -0.0887 -0.8526 325 PRO   A C   
2073 O  O   . PRO   A 305 ? 2.3439 1.8740 2.0150 0.0016  -0.0731 -0.8524 325 PRO   A O   
2074 C  CB  . PRO   A 305 ? 2.3137 1.9123 1.9926 -0.0643 -0.1453 -0.8847 325 PRO   A CB  
2075 C  CG  . PRO   A 305 ? 2.3215 1.9902 2.0096 -0.0828 -0.1751 -0.8829 325 PRO   A CG  
2076 C  CD  . PRO   A 305 ? 2.3584 2.0871 2.0063 -0.0505 -0.1649 -0.8604 325 PRO   A CD  
2077 N  N   . ASP   A 306 ? 2.2484 1.8764 1.8378 0.0339  -0.0790 -0.8539 326 ASP   A N   
2078 C  CA  . ASP   A 306 ? 2.1987 1.8022 1.7605 0.0739  -0.0458 -0.8539 326 ASP   A CA  
2079 C  C   . ASP   A 306 ? 2.2221 1.8357 1.8332 0.0840  -0.0212 -0.8164 326 ASP   A C   
2080 O  O   . ASP   A 306 ? 2.2267 1.7990 1.8506 0.1050  0.0011  -0.8139 326 ASP   A O   
2081 C  CB  . ASP   A 306 ? 2.2374 1.8799 1.7266 0.1063  -0.0358 -0.8579 326 ASP   A CB  
2082 C  CG  . ASP   A 306 ? 2.3150 2.0327 1.8017 0.1102  -0.0350 -0.8282 326 ASP   A CG  
2083 O  OD1 . ASP   A 306 ? 2.3259 2.0731 1.8492 0.0799  -0.0595 -0.8175 326 ASP   A OD1 
2084 O  OD2 . ASP   A 306 ? 2.4119 2.1584 1.8618 0.1436  -0.0073 -0.8144 326 ASP   A OD2 
2085 N  N   . VAL   A 307 ? 2.2326 1.9011 1.8738 0.0684  -0.0253 -0.7735 327 VAL   A N   
2086 C  CA  . VAL   A 307 ? 2.1380 1.8172 1.8277 0.0731  -0.0057 -0.7234 327 VAL   A CA  
2087 C  C   . VAL   A 307 ? 2.1063 1.7298 1.8453 0.0494  -0.0118 -0.7162 327 VAL   A C   
2088 O  O   . VAL   A 307 ? 2.1990 1.8018 1.9679 0.0626  0.0043  -0.6886 327 VAL   A O   
2089 C  CB  . VAL   A 307 ? 1.9297 1.6808 1.6310 0.0648  -0.0085 -0.6828 327 VAL   A CB  
2090 C  CG1 . VAL   A 307 ? 1.9995 1.7653 1.7444 0.0751  0.0117  -0.6355 327 VAL   A CG1 
2091 C  CG2 . VAL   A 307 ? 1.9605 1.7580 1.6039 0.0860  -0.0044 -0.6915 327 VAL   A CG2 
2092 N  N   . GLN   A 308 ? 2.1282 1.7253 1.8770 0.0151  -0.0347 -0.7408 328 GLN   A N   
2093 C  CA  . GLN   A 308 ? 2.1438 1.6813 1.9362 -0.0092 -0.0358 -0.7321 328 GLN   A CA  
2094 C  C   . GLN   A 308 ? 2.2198 1.6771 2.0040 0.0101  -0.0234 -0.7555 328 GLN   A C   
2095 O  O   . GLN   A 308 ? 2.2119 1.6248 2.0227 0.0156  -0.0111 -0.7298 328 GLN   A O   
2096 C  CB  . GLN   A 308 ? 2.1146 1.6490 1.9282 -0.0537 -0.0600 -0.7532 328 GLN   A CB  
2097 C  CG  . GLN   A 308 ? 2.0072 1.4786 1.8662 -0.0829 -0.0561 -0.7410 328 GLN   A CG  
2098 C  CD  . GLN   A 308 ? 2.0222 1.5055 1.9164 -0.1297 -0.0757 -0.7559 328 GLN   A CD  
2099 O  OE1 . GLN   A 308 ? 2.0809 1.5114 2.0127 -0.1588 -0.0707 -0.7514 328 GLN   A OE1 
2100 N  NE2 . GLN   A 308 ? 2.0124 1.5653 1.8962 -0.1363 -0.0971 -0.7728 328 GLN   A NE2 
2101 N  N   . GLN   A 309 ? 2.1668 1.6024 1.9105 0.0235  -0.0271 -0.8047 329 GLN   A N   
2102 C  CA  . GLN   A 309 ? 2.2796 1.6380 2.0130 0.0451  -0.0141 -0.8272 329 GLN   A CA  
2103 C  C   . GLN   A 309 ? 2.2857 1.6541 2.0174 0.0907  0.0127  -0.8048 329 GLN   A C   
2104 O  O   . GLN   A 309 ? 2.3215 1.6341 2.0747 0.1061  0.0246  -0.7944 329 GLN   A O   
2105 C  CB  . GLN   A 309 ? 2.1705 1.5085 1.8527 0.0469  -0.0235 -0.8657 329 GLN   A CB  
2106 C  CG  . GLN   A 309 ? 2.2573 1.5141 1.9242 0.0685  -0.0088 -0.8831 329 GLN   A CG  
2107 C  CD  . GLN   A 309 ? 2.1739 1.4159 1.7809 0.0787  -0.0133 -0.9219 329 GLN   A CD  
2108 O  OE1 . GLN   A 309 ? 2.1880 1.4318 1.7804 0.0497  -0.0384 -0.9445 329 GLN   A OE1 
2109 N  NE2 . GLN   A 309 ? 2.1889 1.4176 1.7628 0.1209  0.0113  -0.9304 329 GLN   A NE2 
2110 N  N   . LYS   A 310 ? 2.2180 1.6576 1.9268 0.1130  0.0229  -0.7942 330 LYS   A N   
2111 C  CA  . LYS   A 310 ? 2.1666 1.6259 1.8848 0.1536  0.0503  -0.7710 330 LYS   A CA  
2112 C  C   . LYS   A 310 ? 2.1627 1.6255 1.9357 0.1511  0.0530  -0.7211 330 LYS   A C   
2113 O  O   . LYS   A 310 ? 2.1379 1.5898 1.9332 0.1827  0.0695  -0.7074 330 LYS   A O   
2114 C  CB  . LYS   A 310 ? 2.1400 1.6765 1.8279 0.1716  0.0633  -0.7641 330 LYS   A CB  
2115 C  CG  . LYS   A 310 ? 2.1624 1.7205 1.8603 0.2144  0.0965  -0.7506 330 LYS   A CG  
2116 C  CD  . LYS   A 310 ? 2.1348 1.7635 1.8007 0.2291  0.1144  -0.7417 330 LYS   A CD  
2117 C  CE  . LYS   A 310 ? 2.2130 1.8650 1.8991 0.2694  0.1520  -0.7298 330 LYS   A CE  
2118 N  NZ  . LYS   A 310 ? 2.1587 1.8754 1.8153 0.2823  0.1756  -0.7164 330 LYS   A NZ  
2119 N  N   . LEU   A 311 ? 2.1632 1.6417 1.9580 0.1159  0.0362  -0.6950 331 LEU   A N   
2120 C  CA  . LEU   A 311 ? 2.1448 1.6158 1.9816 0.1131  0.0363  -0.6507 331 LEU   A CA  
2121 C  C   . LEU   A 311 ? 2.1993 1.5790 2.0476 0.1080  0.0333  -0.6557 331 LEU   A C   
2122 O  O   . LEU   A 311 ? 2.2143 1.5671 2.0844 0.1289  0.0391  -0.6298 331 LEU   A O   
2123 C  CB  . LEU   A 311 ? 2.0723 1.5916 1.9237 0.0800  0.0233  -0.6208 331 LEU   A CB  
2124 C  CG  . LEU   A 311 ? 1.9988 1.5101 1.8845 0.0749  0.0217  -0.5758 331 LEU   A CG  
2125 C  CD1 . LEU   A 311 ? 2.0097 1.5437 1.9142 0.1129  0.0336  -0.5530 331 LEU   A CD1 
2126 C  CD2 . LEU   A 311 ? 1.9554 1.5189 1.8512 0.0445  0.0114  -0.5512 331 LEU   A CD2 
2127 N  N   . GLN   A 312 ? 2.2387 1.5683 2.0733 0.0808  0.0232  -0.6889 332 GLN   A N   
2128 C  CA  . GLN   A 312 ? 2.3013 1.5346 2.1449 0.0747  0.0239  -0.6955 332 GLN   A CA  
2129 C  C   . GLN   A 312 ? 2.4206 1.6049 2.2552 0.1188  0.0377  -0.7118 332 GLN   A C   
2130 O  O   . GLN   A 312 ? 2.4326 1.5462 2.2796 0.1303  0.0419  -0.6978 332 GLN   A O   
2131 C  CB  . GLN   A 312 ? 2.3459 1.5393 2.1825 0.0354  0.0112  -0.7347 332 GLN   A CB  
2132 C  CG  . GLN   A 312 ? 2.2469 1.4679 2.1076 -0.0115 -0.0008 -0.7163 332 GLN   A CG  
2133 C  CD  . GLN   A 312 ? 2.2660 1.4608 2.1297 -0.0503 -0.0158 -0.7614 332 GLN   A CD  
2134 O  OE1 . GLN   A 312 ? 2.0311 1.2323 1.8645 -0.0430 -0.0249 -0.8020 332 GLN   A OE1 
2135 N  NE2 . GLN   A 312 ? 2.2759 1.4440 2.1741 -0.0914 -0.0180 -0.7480 332 GLN   A NE2 
2136 N  N   . GLU   A 313 ? 2.3626 1.5819 2.1737 0.1463  0.0464  -0.7404 333 GLU   A N   
2137 C  CA  . GLU   A 313 ? 2.4448 1.6236 2.2505 0.1908  0.0626  -0.7589 333 GLU   A CA  
2138 C  C   . GLU   A 313 ? 2.4757 1.6791 2.3162 0.2253  0.0727  -0.7177 333 GLU   A C   
2139 O  O   . GLU   A 313 ? 2.5637 1.7138 2.4156 0.2581  0.0804  -0.7204 333 GLU   A O   
2140 C  CB  . GLU   A 313 ? 2.3496 1.5624 2.1170 0.2110  0.0731  -0.7999 333 GLU   A CB  
2141 C  CG  . GLU   A 313 ? 2.3247 1.5086 2.0480 0.1805  0.0601  -0.8331 333 GLU   A CG  
2142 C  CD  . GLU   A 313 ? 2.3530 1.5895 2.0265 0.1942  0.0670  -0.8565 333 GLU   A CD  
2143 O  OE1 . GLU   A 313 ? 2.3088 1.6065 1.9844 0.2239  0.0855  -0.8441 333 GLU   A OE1 
2144 O  OE2 . GLU   A 313 ? 2.4775 1.6928 2.1096 0.1758  0.0544  -0.8863 333 GLU   A OE2 
2145 N  N   . GLU   A 314 ? 2.6413 1.9239 2.5016 0.2196  0.0707  -0.6812 334 GLU   A N   
2146 C  CA  . GLU   A 314 ? 2.6342 1.9443 2.5334 0.2493  0.0752  -0.6443 334 GLU   A CA  
2147 C  C   . GLU   A 314 ? 2.7031 1.9546 2.6181 0.2422  0.0614  -0.6127 334 GLU   A C   
2148 O  O   . GLU   A 314 ? 2.7916 2.0209 2.7295 0.2764  0.0617  -0.5963 334 GLU   A O   
2149 C  CB  . GLU   A 314 ? 2.5848 1.9937 2.5004 0.2435  0.0771  -0.6179 334 GLU   A CB  
2150 C  CG  . GLU   A 314 ? 2.6908 2.1378 2.6534 0.2734  0.0799  -0.5854 334 GLU   A CG  
2151 C  CD  . GLU   A 314 ? 2.5193 2.0394 2.5010 0.2542  0.0728  -0.5508 334 GLU   A CD  
2152 O  OE1 . GLU   A 314 ? 2.4043 1.9167 2.3710 0.2186  0.0582  -0.5367 334 GLU   A OE1 
2153 O  OE2 . GLU   A 314 ? 2.4165 2.0014 2.4315 0.2742  0.0832  -0.5386 334 GLU   A OE2 
2154 N  N   . ILE   A 315 ? 2.4667 1.6936 2.3695 0.1996  0.0498  -0.6033 335 ILE   A N   
2155 C  CA  . ILE   A 315 ? 2.4405 1.6109 2.3503 0.1911  0.0412  -0.5692 335 ILE   A CA  
2156 C  C   . ILE   A 315 ? 2.4449 1.5106 2.3458 0.2110  0.0450  -0.5818 335 ILE   A C   
2157 O  O   . ILE   A 315 ? 2.4534 1.4767 2.3614 0.2354  0.0412  -0.5532 335 ILE   A O   
2158 C  CB  . ILE   A 315 ? 2.3644 1.5355 2.2665 0.1394  0.0339  -0.5587 335 ILE   A CB  
2159 C  CG1 . ILE   A 315 ? 2.3562 1.6281 2.2682 0.1256  0.0293  -0.5410 335 ILE   A CG1 
2160 C  CG2 . ILE   A 315 ? 2.3651 1.4665 2.2662 0.1302  0.0312  -0.5243 335 ILE   A CG2 
2161 C  CD1 . ILE   A 315 ? 2.1967 1.4813 2.1064 0.0776  0.0227  -0.5347 335 ILE   A CD1 
2162 N  N   . ASP   A 316 ? 2.4454 1.4649 2.3280 0.2028  0.0509  -0.6256 336 ASP   A N   
2163 C  CA  . ASP   A 316 ? 2.5237 1.4393 2.3979 0.2238  0.0562  -0.6416 336 ASP   A CA  
2164 C  C   . ASP   A 316 ? 2.5881 1.5088 2.4753 0.2823  0.0634  -0.6454 336 ASP   A C   
2165 O  O   . ASP   A 316 ? 2.6009 1.4399 2.4877 0.3101  0.0649  -0.6421 336 ASP   A O   
2166 C  CB  . ASP   A 316 ? 2.5516 1.4192 2.4045 0.1993  0.0591  -0.6931 336 ASP   A CB  
2167 C  CG  . ASP   A 316 ? 2.5830 1.4403 2.4348 0.1407  0.0511  -0.6928 336 ASP   A CG  
2168 O  OD1 . ASP   A 316 ? 2.6072 1.4550 2.4699 0.1217  0.0488  -0.6504 336 ASP   A OD1 
2169 O  OD2 . ASP   A 316 ? 2.1995 1.0601 2.0383 0.1146  0.0469  -0.7339 336 ASP   A OD2 
2170 N  N   . ALA   A 317 ? 2.5101 1.5240 2.4115 0.3023  0.0694  -0.6515 337 ALA   A N   
2171 C  CA  . ALA   A 317 ? 2.4740 1.5048 2.4002 0.3572  0.0789  -0.6550 337 ALA   A CA  
2172 C  C   . ALA   A 317 ? 2.4624 1.5026 2.4208 0.3817  0.0664  -0.6094 337 ALA   A C   
2173 O  O   . ALA   A 317 ? 2.4138 1.3960 2.3825 0.4199  0.0638  -0.6046 337 ALA   A O   
2174 C  CB  . ALA   A 317 ? 2.4174 1.5456 2.3517 0.3680  0.0940  -0.6731 337 ALA   A CB  
2175 N  N   . VAL   A 318 ? 2.3949 1.5068 2.3678 0.3625  0.0565  -0.5769 338 VAL   A N   
2176 C  CA  . VAL   A 318 ? 2.4278 1.5528 2.4274 0.3847  0.0402  -0.5362 338 VAL   A CA  
2177 C  C   . VAL   A 318 ? 2.4132 1.4353 2.3854 0.3814  0.0281  -0.5133 338 VAL   A C   
2178 O  O   . VAL   A 318 ? 2.4193 1.4085 2.4019 0.4193  0.0160  -0.4919 338 VAL   A O   
2179 C  CB  . VAL   A 318 ? 2.3698 1.5869 2.3851 0.3602  0.0325  -0.5100 338 VAL   A CB  
2180 C  CG1 . VAL   A 318 ? 2.3218 1.5396 2.3535 0.3772  0.0108  -0.4695 338 VAL   A CG1 
2181 C  CG2 . VAL   A 318 ? 2.3712 1.6856 2.4189 0.3722  0.0472  -0.5261 338 VAL   A CG2 
2182 N  N   . LEU   A 319 ? 2.4584 1.4271 2.3959 0.3371  0.0317  -0.5171 339 LEU   A N   
2183 C  CA  . LEU   A 319 ? 2.4490 1.3155 2.3579 0.3266  0.0272  -0.4932 339 LEU   A CA  
2184 C  C   . LEU   A 319 ? 2.6276 1.4005 2.5156 0.3155  0.0403  -0.5274 339 LEU   A C   
2185 O  O   . LEU   A 319 ? 2.6624 1.4139 2.5357 0.2674  0.0462  -0.5407 339 LEU   A O   
2186 C  CB  . LEU   A 319 ? 2.4946 1.3788 2.3892 0.2802  0.0229  -0.4637 339 LEU   A CB  
2187 C  CG  . LEU   A 319 ? 2.4921 1.4619 2.4037 0.2886  0.0089  -0.4311 339 LEU   A CG  
2188 C  CD1 . LEU   A 319 ? 2.5042 1.4891 2.3997 0.2418  0.0085  -0.4074 339 LEU   A CD1 
2189 C  CD2 . LEU   A 319 ? 2.4657 1.4036 2.3784 0.3369  -0.0066 -0.4020 339 LEU   A CD2 
2190 N  N   . PRO   A 320 ? 2.7029 1.4187 2.5932 0.3590  0.0441  -0.5442 340 PRO   A N   
2191 C  CA  . PRO   A 320 ? 2.8563 1.4754 2.7265 0.3500  0.0563  -0.5794 340 PRO   A CA  
2192 C  C   . PRO   A 320 ? 3.1257 1.6344 2.9707 0.3276  0.0588  -0.5520 340 PRO   A C   
2193 O  O   . PRO   A 320 ? 3.0999 1.5828 2.9345 0.3405  0.0498  -0.5067 340 PRO   A O   
2194 C  CB  . PRO   A 320 ? 2.7981 1.4150 2.6829 0.4019  0.0664  -0.5890 340 PRO   A CB  
2195 C  CG  . PRO   A 320 ? 2.6528 1.3063 2.5611 0.4447  0.0498  -0.5521 340 PRO   A CG  
2196 C  CD  . PRO   A 320 ? 2.5851 1.3248 2.5017 0.4195  0.0368  -0.5348 340 PRO   A CD  
2197 N  N   . ASN   A 321 ? 3.4015 1.8488 3.2361 0.2916  0.0742  -0.5783 341 ASN   A N   
2198 C  CA  . ASN   A 321 ? 3.5515 1.9030 3.3811 0.2602  0.0802  -0.5592 341 ASN   A CA  
2199 C  C   . ASN   A 321 ? 3.5418 1.8992 3.3530 0.2229  0.0756  -0.5251 341 ASN   A C   
2200 O  O   . ASN   A 321 ? 3.6977 1.9898 3.4948 0.2153  0.0805  -0.4836 341 ASN   A O   
2201 C  CB  . ASN   A 321 ? 3.6338 1.9116 3.4636 0.3017  0.0813  -0.5270 341 ASN   A CB  
2202 C  CG  . ASN   A 321 ? 3.6654 1.9202 3.5136 0.3317  0.0929  -0.5600 341 ASN   A CG  
2203 O  OD1 . ASN   A 321 ? 3.6985 1.9590 3.5502 0.3089  0.1058  -0.6060 341 ASN   A OD1 
2204 N  ND2 . ASN   A 321 ? 3.7163 1.9423 3.5681 0.3832  0.0907  -0.5350 341 ASN   A ND2 
2205 N  N   . LYS   A 322 ? 3.1915 1.6571 3.0174 0.1954  0.0696  -0.5358 342 LYS   A N   
2206 C  CA  . LYS   A 322 ? 3.0434 1.5590 2.8709 0.1587  0.0679  -0.5003 342 LYS   A CA  
2207 C  C   . LYS   A 322 ? 3.0369 1.5439 2.8474 0.1919  0.0615  -0.4451 342 LYS   A C   
2208 O  O   . LYS   A 322 ? 3.0854 1.5402 2.8755 0.1735  0.0690  -0.4071 342 LYS   A O   
2209 C  CB  . LYS   A 322 ? 3.1312 1.5844 2.9592 0.1007  0.0820  -0.5028 342 LYS   A CB  
2210 C  CG  . LYS   A 322 ? 3.0560 1.5412 2.9056 0.0593  0.0810  -0.5570 342 LYS   A CG  
2211 C  CD  . LYS   A 322 ? 3.0178 1.4633 2.8817 -0.0011 0.0918  -0.5528 342 LYS   A CD  
2212 C  CE  . LYS   A 322 ? 2.8638 1.3521 2.7473 -0.0392 0.0794  -0.6020 342 LYS   A CE  
2213 N  NZ  . LYS   A 322 ? 2.8610 1.3359 2.7712 -0.0984 0.0855  -0.5942 342 LYS   A NZ  
2214 N  N   . ALA   A 323 ? 3.1460 1.7050 2.9652 0.2424  0.0477  -0.4420 343 ALA   A N   
2215 C  CA  . ALA   A 323 ? 3.0430 1.5957 2.8479 0.2809  0.0349  -0.3961 343 ALA   A CA  
2216 C  C   . ALA   A 323 ? 3.0569 1.6785 2.8583 0.2542  0.0290  -0.3634 343 ALA   A C   
2217 O  O   . ALA   A 323 ? 3.0269 1.7379 2.8502 0.2222  0.0293  -0.3793 343 ALA   A O   
2218 C  CB  . ALA   A 323 ? 2.9865 1.5932 2.8164 0.3383  0.0199  -0.4064 343 ALA   A CB  
2219 N  N   . PRO   A 324 ? 2.9290 1.5071 2.6983 0.2690  0.0235  -0.3176 344 PRO   A N   
2220 C  CA  . PRO   A 324 ? 2.8969 1.5356 2.6579 0.2482  0.0180  -0.2869 344 PRO   A CA  
2221 C  C   . PRO   A 324 ? 2.7971 1.5530 2.5900 0.2720  -0.0036 -0.2918 344 PRO   A C   
2222 O  O   . PRO   A 324 ? 2.8062 1.5716 2.6102 0.3222  -0.0210 -0.2910 344 PRO   A O   
2223 C  CB  . PRO   A 324 ? 2.9648 1.5122 2.6732 0.2709  0.0166  -0.2390 344 PRO   A CB  
2224 C  CG  . PRO   A 324 ? 3.0579 1.4840 2.7472 0.2863  0.0292  -0.2444 344 PRO   A CG  
2225 C  CD  . PRO   A 324 ? 3.0096 1.4712 2.7410 0.3057  0.0233  -0.2913 344 PRO   A CD  
2226 N  N   . PRO   A 325 ? 2.6400 1.4872 2.4528 0.2375  -0.0026 -0.2973 345 PRO   A N   
2227 C  CA  . PRO   A 325 ? 2.5552 1.5112 2.4015 0.2566  -0.0199 -0.3012 345 PRO   A CA  
2228 C  C   . PRO   A 325 ? 2.4799 1.4413 2.3107 0.2887  -0.0417 -0.2649 345 PRO   A C   
2229 O  O   . PRO   A 325 ? 2.5157 1.4308 2.3048 0.2782  -0.0408 -0.2326 345 PRO   A O   
2230 C  CB  . PRO   A 325 ? 2.5142 1.5461 2.3751 0.2082  -0.0113 -0.3106 345 PRO   A CB  
2231 C  CG  . PRO   A 325 ? 2.6357 1.6025 2.4667 0.1683  0.0046  -0.2957 345 PRO   A CG  
2232 C  CD  . PRO   A 325 ? 2.6957 1.5517 2.5070 0.1798  0.0146  -0.3015 345 PRO   A CD  
2233 N  N   . THR   A 326 ? 2.4313 1.4494 2.2968 0.3288  -0.0611 -0.2720 346 THR   A N   
2234 C  CA  . THR   A 326 ? 2.4456 1.4845 2.3075 0.3628  -0.0889 -0.2458 346 THR   A CA  
2235 C  C   . THR   A 326 ? 2.3856 1.5438 2.2957 0.3555  -0.0988 -0.2543 346 THR   A C   
2236 O  O   . THR   A 326 ? 2.2979 1.5171 2.2394 0.3288  -0.0828 -0.2778 346 THR   A O   
2237 C  CB  . THR   A 326 ? 2.3816 1.3795 2.2511 0.4212  -0.1073 -0.2462 346 THR   A CB  
2238 O  OG1 . THR   A 326 ? 2.3857 1.4311 2.3115 0.4360  -0.1004 -0.2820 346 THR   A OG1 
2239 C  CG2 . THR   A 326 ? 2.6165 1.4845 2.4292 0.4307  -0.0982 -0.2301 346 THR   A CG2 
2240 N  N   . TYR   A 327 ? 2.3097 1.4969 2.2224 0.3804  -0.1264 -0.2349 347 TYR   A N   
2241 C  CA  . TYR   A 327 ? 2.2334 1.5274 2.1943 0.3737  -0.1371 -0.2412 347 TYR   A CA  
2242 C  C   . TYR   A 327 ? 2.1861 1.5498 2.2168 0.3864  -0.1299 -0.2725 347 TYR   A C   
2243 O  O   . TYR   A 327 ? 2.2083 1.6474 2.2723 0.3606  -0.1164 -0.2857 347 TYR   A O   
2244 C  CB  . TYR   A 327 ? 2.3049 1.6088 2.2597 0.4051  -0.1729 -0.2203 347 TYR   A CB  
2245 C  CG  . TYR   A 327 ? 2.3203 1.7241 2.3212 0.3949  -0.1858 -0.2244 347 TYR   A CG  
2246 C  CD1 . TYR   A 327 ? 2.2760 1.7596 2.3555 0.4146  -0.1948 -0.2455 347 TYR   A CD1 
2247 C  CD2 . TYR   A 327 ? 2.2216 1.6378 2.1900 0.3661  -0.1868 -0.2072 347 TYR   A CD2 
2248 C  CE1 . TYR   A 327 ? 2.1987 1.7682 2.3241 0.4031  -0.2044 -0.2488 347 TYR   A CE1 
2249 C  CE2 . TYR   A 327 ? 2.2562 1.7568 2.2664 0.3569  -0.1984 -0.2116 347 TYR   A CE2 
2250 C  CZ  . TYR   A 327 ? 2.1631 1.7384 2.2521 0.3744  -0.2073 -0.2321 347 TYR   A CZ  
2251 O  OH  . TYR   A 327 ? 2.0409 1.6956 2.1753 0.3629  -0.2166 -0.2362 347 TYR   A OH  
2252 N  N   . ASP   A 328 ? 2.2429 1.5801 2.2947 0.4282  -0.1366 -0.2837 348 ASP   A N   
2253 C  CA  . ASP   A 328 ? 2.2176 1.6232 2.3398 0.4469  -0.1285 -0.3120 348 ASP   A CA  
2254 C  C   . ASP   A 328 ? 2.2565 1.6512 2.3750 0.4264  -0.0939 -0.3387 348 ASP   A C   
2255 O  O   . ASP   A 328 ? 2.2704 1.7354 2.4356 0.4251  -0.0774 -0.3607 348 ASP   A O   
2256 C  CB  . ASP   A 328 ? 2.2385 1.6270 2.3916 0.5041  -0.1512 -0.3144 348 ASP   A CB  
2257 C  CG  . ASP   A 328 ? 2.2586 1.6681 2.4204 0.5285  -0.1915 -0.2934 348 ASP   A CG  
2258 O  OD1 . ASP   A 328 ? 2.2351 1.7370 2.4586 0.5280  -0.2021 -0.2999 348 ASP   A OD1 
2259 O  OD2 . ASP   A 328 ? 2.2819 1.6127 2.3862 0.5478  -0.2122 -0.2705 348 ASP   A OD2 
2260 N  N   . THR   A 329 ? 2.2518 1.5581 2.3148 0.4106  -0.0821 -0.3380 349 THR   A N   
2261 C  CA  . THR   A 329 ? 2.2531 1.5473 2.3084 0.3883  -0.0536 -0.3671 349 THR   A CA  
2262 C  C   . THR   A 329 ? 2.2710 1.6219 2.3204 0.3399  -0.0398 -0.3714 349 THR   A C   
2263 O  O   . THR   A 329 ? 2.2507 1.6251 2.3052 0.3265  -0.0197 -0.3991 349 THR   A O   
2264 C  CB  . THR   A 329 ? 2.2486 1.4288 2.2534 0.3837  -0.0465 -0.3675 349 THR   A CB  
2265 O  OG1 . THR   A 329 ? 2.2641 1.3957 2.2239 0.3622  -0.0550 -0.3349 349 THR   A OG1 
2266 C  CG2 . THR   A 329 ? 2.1981 1.3219 2.2119 0.4361  -0.0545 -0.3721 349 THR   A CG2 
2267 N  N   . VAL   A 330 ? 2.2451 1.6166 2.2803 0.3163  -0.0507 -0.3454 350 VAL   A N   
2268 C  CA  . VAL   A 330 ? 2.1786 1.6088 2.2126 0.2747  -0.0399 -0.3478 350 VAL   A CA  
2269 C  C   . VAL   A 330 ? 2.2265 1.7545 2.3111 0.2835  -0.0367 -0.3567 350 VAL   A C   
2270 O  O   . VAL   A 330 ? 2.2703 1.8414 2.3601 0.2654  -0.0183 -0.3749 350 VAL   A O   
2271 C  CB  . VAL   A 330 ? 2.1646 1.5832 2.1684 0.2492  -0.0502 -0.3174 350 VAL   A CB  
2272 C  CG1 . VAL   A 330 ? 1.9822 1.4717 1.9936 0.2129  -0.0421 -0.3187 350 VAL   A CG1 
2273 C  CG2 . VAL   A 330 ? 2.1114 1.4350 2.0673 0.2328  -0.0439 -0.3093 350 VAL   A CG2 
2274 N  N   . LEU   A 331 ? 2.0307 1.5937 2.1531 0.3118  -0.0544 -0.3441 351 LEU   A N   
2275 C  CA  . LEU   A 331 ? 2.0614 1.7160 2.2419 0.3192  -0.0493 -0.3511 351 LEU   A CA  
2276 C  C   . LEU   A 331 ? 2.1514 1.8275 2.3630 0.3391  -0.0260 -0.3796 351 LEU   A C   
2277 O  O   . LEU   A 331 ? 2.0936 1.8437 2.3476 0.3388  -0.0109 -0.3867 351 LEU   A O   
2278 C  CB  . LEU   A 331 ? 2.0531 1.7363 2.2747 0.3462  -0.0771 -0.3356 351 LEU   A CB  
2279 C  CG  . LEU   A 331 ? 2.0763 1.7667 2.2771 0.3271  -0.0980 -0.3100 351 LEU   A CG  
2280 C  CD1 . LEU   A 331 ? 2.0045 1.7208 2.2466 0.3590  -0.1300 -0.3014 351 LEU   A CD1 
2281 C  CD2 . LEU   A 331 ? 2.0673 1.8196 2.2755 0.2905  -0.0820 -0.3091 351 LEU   A CD2 
2282 N  N   . GLN   A 332 ? 2.3217 1.9322 2.5123 0.3570  -0.0202 -0.3955 352 GLN   A N   
2283 C  CA  . GLN   A 332 ? 2.2680 1.8931 2.4805 0.3773  0.0046  -0.4253 352 GLN   A CA  
2284 C  C   . GLN   A 332 ? 2.2761 1.9068 2.4504 0.3466  0.0294  -0.4448 352 GLN   A C   
2285 O  O   . GLN   A 332 ? 2.2940 1.9703 2.4866 0.3553  0.0539  -0.4642 352 GLN   A O   
2286 C  CB  . GLN   A 332 ? 2.3150 1.8634 2.5191 0.4118  0.0002  -0.4369 352 GLN   A CB  
2287 C  CG  . GLN   A 332 ? 2.3848 1.9378 2.6055 0.4358  0.0274  -0.4707 352 GLN   A CG  
2288 C  CD  . GLN   A 332 ? 2.4956 1.9666 2.7075 0.4715  0.0225  -0.4823 352 GLN   A CD  
2289 O  OE1 . GLN   A 332 ? 2.5947 2.0130 2.7972 0.4854  -0.0029 -0.4617 352 GLN   A OE1 
2290 N  NE2 . GLN   A 332 ? 2.4225 1.8784 2.6325 0.4886  0.0474  -0.5151 352 GLN   A NE2 
2291 N  N   . MET   A 333 ? 2.2599 1.8464 2.3818 0.3118  0.0237  -0.4403 353 MET   A N   
2292 C  CA  . MET   A 333 ? 2.2186 1.8069 2.3029 0.2834  0.0403  -0.4617 353 MET   A CA  
2293 C  C   . MET   A 333 ? 2.1337 1.8076 2.2310 0.2669  0.0503  -0.4549 353 MET   A C   
2294 O  O   . MET   A 333 ? 2.1637 1.8643 2.2617 0.2437  0.0383  -0.4308 353 MET   A O   
2295 C  CB  . MET   A 333 ? 2.1825 1.7084 2.2218 0.2493  0.0292  -0.4572 353 MET   A CB  
2296 C  CG  . MET   A 333 ? 2.3023 1.7347 2.3266 0.2637  0.0216  -0.4580 353 MET   A CG  
2297 S  SD  . MET   A 333 ? 2.3814 1.7414 2.3629 0.2202  0.0142  -0.4473 353 MET   A SD  
2298 C  CE  . MET   A 333 ? 2.3850 1.6358 2.3545 0.2498  0.0091  -0.4413 353 MET   A CE  
2299 N  N   . GLU   A 334 ? 2.0377 1.7509 2.1421 0.2804  0.0745  -0.4755 354 GLU   A N   
2300 C  CA  . GLU   A 334 ? 1.9338 1.7231 2.0482 0.2690  0.0892  -0.4675 354 GLU   A CA  
2301 C  C   . GLU   A 334 ? 1.8020 1.5920 1.8605 0.2386  0.0928  -0.4784 354 GLU   A C   
2302 O  O   . GLU   A 334 ? 1.8070 1.6437 1.8632 0.2183  0.0922  -0.4610 354 GLU   A O   
2303 C  CB  . GLU   A 334 ? 1.9577 1.7910 2.1074 0.3003  0.1183  -0.4804 354 GLU   A CB  
2304 C  CG  . GLU   A 334 ? 2.1483 2.0003 2.3692 0.3311  0.1135  -0.4703 354 GLU   A CG  
2305 C  CD  . GLU   A 334 ? 2.2370 2.1427 2.5043 0.3589  0.1473  -0.4822 354 GLU   A CD  
2306 O  OE1 . GLU   A 334 ? 2.2249 2.1640 2.4690 0.3502  0.1756  -0.4883 354 GLU   A OE1 
2307 O  OE2 . GLU   A 334 ? 2.2071 2.1215 2.5338 0.3907  0.1464  -0.4849 354 GLU   A OE2 
2308 N  N   . TYR   A 335 ? 1.8396 1.5783 1.8545 0.2362  0.0947  -0.5084 355 TYR   A N   
2309 C  CA  . TYR   A 335 ? 1.7939 1.5348 1.7586 0.2083  0.0920  -0.5226 355 TYR   A CA  
2310 C  C   . TYR   A 335 ? 1.6525 1.3830 1.6120 0.1724  0.0680  -0.5031 355 TYR   A C   
2311 O  O   . TYR   A 335 ? 1.6541 1.4181 1.5928 0.1492  0.0636  -0.5001 355 TYR   A O   
2312 C  CB  . TYR   A 335 ? 1.9031 1.5888 1.8264 0.2141  0.0960  -0.5641 355 TYR   A CB  
2313 C  CG  . TYR   A 335 ? 1.8422 1.5423 1.7129 0.1956  0.0949  -0.5869 355 TYR   A CG  
2314 C  CD1 . TYR   A 335 ? 1.8503 1.6012 1.6978 0.2103  0.1158  -0.5923 355 TYR   A CD1 
2315 C  CD2 . TYR   A 335 ? 1.8908 1.5532 1.7355 0.1646  0.0731  -0.6034 355 TYR   A CD2 
2316 C  CE1 . TYR   A 335 ? 1.9388 1.7007 1.7301 0.1980  0.1112  -0.6131 355 TYR   A CE1 
2317 C  CE2 . TYR   A 335 ? 1.9193 1.5985 1.7187 0.1500  0.0664  -0.6273 355 TYR   A CE2 
2318 C  CZ  . TYR   A 335 ? 1.8945 1.6225 1.6632 0.1685  0.0836  -0.6319 355 TYR   A CZ  
2319 O  OH  . TYR   A 335 ? 1.8656 1.6082 1.5813 0.1582  0.0734  -0.6555 355 TYR   A OH  
2320 N  N   . LEU   A 336 ? 1.8104 1.4942 1.7869 0.1696  0.0536  -0.4888 356 LEU   A N   
2321 C  CA  . LEU   A 336 ? 1.8079 1.4848 1.7828 0.1383  0.0363  -0.4656 356 LEU   A CA  
2322 C  C   . LEU   A 336 ? 1.7499 1.4939 1.7476 0.1338  0.0345  -0.4352 356 LEU   A C   
2323 O  O   . LEU   A 336 ? 1.7084 1.4764 1.6959 0.1066  0.0272  -0.4243 356 LEU   A O   
2324 C  CB  . LEU   A 336 ? 1.8642 1.4726 1.8459 0.1424  0.0260  -0.4531 356 LEU   A CB  
2325 C  CG  . LEU   A 336 ? 1.7348 1.3225 1.7094 0.1114  0.0135  -0.4295 356 LEU   A CG  
2326 C  CD1 . LEU   A 336 ? 1.7666 1.3348 1.7187 0.0764  0.0124  -0.4504 356 LEU   A CD1 
2327 C  CD2 . LEU   A 336 ? 1.7894 1.3097 1.7649 0.1244  0.0067  -0.4110 356 LEU   A CD2 
2328 N  N   . ASP   A 337 ? 1.6934 1.4689 1.7266 0.1604  0.0408  -0.4229 357 ASP   A N   
2329 C  CA  . ASP   A 337 ? 1.7059 1.5446 1.7658 0.1565  0.0406  -0.3977 357 ASP   A CA  
2330 C  C   . ASP   A 337 ? 1.5398 1.4279 1.5805 0.1444  0.0543  -0.4032 357 ASP   A C   
2331 O  O   . ASP   A 337 ? 1.2914 1.2161 1.3342 0.1269  0.0496  -0.3837 357 ASP   A O   
2332 C  CB  . ASP   A 337 ? 1.6048 1.4700 1.7155 0.1874  0.0458  -0.3903 357 ASP   A CB  
2333 C  CG  . ASP   A 337 ? 1.3820 1.3091 1.5279 0.1822  0.0452  -0.3667 357 ASP   A CG  
2334 O  OD1 . ASP   A 337 ? 1.5151 1.4380 1.6626 0.1686  0.0258  -0.3461 357 ASP   A OD1 
2335 O  OD2 . ASP   A 337 ? 1.3195 1.2964 1.4911 0.1921  0.0661  -0.3688 357 ASP   A OD2 
2336 N  N   . MET   A 338 ? 1.5382 1.4246 1.5552 0.1561  0.0712  -0.4297 358 MET   A N   
2337 C  CA  . MET   A 338 ? 1.5898 1.5165 1.5758 0.1494  0.0839  -0.4353 358 MET   A CA  
2338 C  C   . MET   A 338 ? 1.5268 1.4460 1.4769 0.1188  0.0651  -0.4385 358 MET   A C   
2339 O  O   . MET   A 338 ? 1.5745 1.5351 1.5171 0.1062  0.0636  -0.4230 358 MET   A O   
2340 C  CB  . MET   A 338 ? 1.4701 1.3883 1.4288 0.1722  0.1058  -0.4656 358 MET   A CB  
2341 C  CG  . MET   A 338 ? 1.5712 1.5146 1.5714 0.2030  0.1316  -0.4615 358 MET   A CG  
2342 S  SD  . MET   A 338 ? 1.6142 1.5262 1.5876 0.2343  0.1558  -0.5011 358 MET   A SD  
2343 C  CE  . MET   A 338 ? 1.7078 1.6316 1.6005 0.2256  0.1649  -0.5196 358 MET   A CE  
2344 N  N   . VAL   A 339 ? 1.6248 1.4914 1.5574 0.1066  0.0512  -0.4588 359 VAL   A N   
2345 C  CA  . VAL   A 339 ? 1.5390 1.4010 1.4490 0.0758  0.0332  -0.4657 359 VAL   A CA  
2346 C  C   . VAL   A 339 ? 1.4788 1.3642 1.4131 0.0560  0.0223  -0.4324 359 VAL   A C   
2347 O  O   . VAL   A 339 ? 1.4244 1.3429 1.3484 0.0380  0.0141  -0.4275 359 VAL   A O   
2348 C  CB  . VAL   A 339 ? 1.4930 1.2891 1.3924 0.0642  0.0231  -0.4927 359 VAL   A CB  
2349 C  CG1 . VAL   A 339 ? 1.5230 1.3175 1.4182 0.0284  0.0047  -0.4964 359 VAL   A CG1 
2350 C  CG2 . VAL   A 339 ? 1.8515 1.6260 1.7181 0.0820  0.0316  -0.5317 359 VAL   A CG2 
2351 N  N   . VAL   A 340 ? 1.4331 1.3008 1.3976 0.0618  0.0209  -0.4102 360 VAL   A N   
2352 C  CA  . VAL   A 340 ? 1.4013 1.2868 1.3840 0.0466  0.0117  -0.3797 360 VAL   A CA  
2353 C  C   . VAL   A 340 ? 1.4057 1.3548 1.3962 0.0497  0.0175  -0.3626 360 VAL   A C   
2354 O  O   . VAL   A 340 ? 1.3762 1.3517 1.3634 0.0314  0.0105  -0.3503 360 VAL   A O   
2355 C  CB  . VAL   A 340 ? 1.3633 1.2152 1.3684 0.0589  0.0074  -0.3613 360 VAL   A CB  
2356 C  CG1 . VAL   A 340 ? 1.3610 1.2398 1.3819 0.0510  -0.0002 -0.3307 360 VAL   A CG1 
2357 C  CG2 . VAL   A 340 ? 1.3612 1.1428 1.3531 0.0500  0.0018  -0.3701 360 VAL   A CG2 
2358 N  N   . ASN   A 341 ? 1.4383 1.4118 1.4426 0.0733  0.0326  -0.3614 361 ASN   A N   
2359 C  CA  . ASN   A 341 ? 1.4125 1.4404 1.4288 0.0764  0.0425  -0.3428 361 ASN   A CA  
2360 C  C   . ASN   A 341 ? 1.4715 1.5254 1.4495 0.0675  0.0457  -0.3501 361 ASN   A C   
2361 O  O   . ASN   A 341 ? 1.3337 1.4209 1.3125 0.0583  0.0436  -0.3310 361 ASN   A O   
2362 C  CB  . ASN   A 341 ? 1.3796 1.4265 1.4252 0.1022  0.0627  -0.3421 361 ASN   A CB  
2363 C  CG  . ASN   A 341 ? 1.3728 1.4042 1.4628 0.1139  0.0541  -0.3333 361 ASN   A CG  
2364 O  OD1 . ASN   A 341 ? 1.2943 1.2959 1.3841 0.1041  0.0342  -0.3251 361 ASN   A OD1 
2365 N  ND2 . ASN   A 341 ? 1.2431 1.2949 1.3711 0.1364  0.0695  -0.3350 361 ASN   A ND2 
2366 N  N   . GLU   A 342 ? 1.4411 1.4782 1.3825 0.0722  0.0486  -0.3786 362 GLU   A N   
2367 C  CA  . GLU   A 342 ? 1.3804 1.4417 1.2784 0.0685  0.0477  -0.3879 362 GLU   A CA  
2368 C  C   . GLU   A 342 ? 1.4491 1.5152 1.3419 0.0423  0.0233  -0.3864 362 GLU   A C   
2369 O  O   . GLU   A 342 ? 1.5052 1.6059 1.3791 0.0389  0.0190  -0.3783 362 GLU   A O   
2370 C  CB  . GLU   A 342 ? 1.4512 1.4905 1.3069 0.0820  0.0539  -0.4232 362 GLU   A CB  
2371 C  CG  . GLU   A 342 ? 1.5528 1.6110 1.3530 0.0806  0.0459  -0.4388 362 GLU   A CG  
2372 C  CD  . GLU   A 342 ? 1.5393 1.6379 1.3157 0.0978  0.0666  -0.4182 362 GLU   A CD  
2373 O  OE1 . GLU   A 342 ? 1.3958 1.5166 1.2096 0.1006  0.0819  -0.3867 362 GLU   A OE1 
2374 O  OE2 . GLU   A 342 ? 1.5926 1.6981 1.3102 0.1090  0.0673  -0.4341 362 GLU   A OE2 
2375 N  N   . THR   A 343 ? 1.4477 1.4790 1.3584 0.0247  0.0091  -0.3928 363 THR   A N   
2376 C  CA  . THR   A 343 ? 1.3920 1.4316 1.3105 -0.0016 -0.0091 -0.3884 363 THR   A CA  
2377 C  C   . THR   A 343 ? 1.3933 1.4652 1.3351 -0.0050 -0.0080 -0.3535 363 THR   A C   
2378 O  O   . THR   A 343 ? 1.2840 1.3877 1.2232 -0.0161 -0.0174 -0.3465 363 THR   A O   
2379 C  CB  . THR   A 343 ? 1.2996 1.2894 1.2343 -0.0196 -0.0172 -0.3988 363 THR   A CB  
2380 O  OG1 . THR   A 343 ? 1.5839 1.5394 1.4976 -0.0171 -0.0190 -0.4342 363 THR   A OG1 
2381 C  CG2 . THR   A 343 ? 1.2849 1.2869 1.2346 -0.0482 -0.0311 -0.3946 363 THR   A CG2 
2382 N  N   . LEU   A 344 ? 1.3736 1.4385 1.3399 0.0060  0.0018  -0.3333 364 LEU   A N   
2383 C  CA  . LEU   A 344 ? 1.2875 1.3796 1.2754 0.0041  0.0021  -0.3036 364 LEU   A CA  
2384 C  C   . LEU   A 344 ? 1.3107 1.4467 1.2888 0.0141  0.0117  -0.2928 364 LEU   A C   
2385 O  O   . LEU   A 344 ? 1.1589 1.3190 1.1490 0.0093  0.0098  -0.2713 364 LEU   A O   
2386 C  CB  . LEU   A 344 ? 1.1938 1.2677 1.2105 0.0151  0.0059  -0.2894 364 LEU   A CB  
2387 C  CG  . LEU   A 344 ? 1.1935 1.2201 1.2148 0.0067  -0.0040 -0.2897 364 LEU   A CG  
2388 C  CD1 . LEU   A 344 ? 1.2547 1.2682 1.2997 0.0228  -0.0052 -0.2752 364 LEU   A CD1 
2389 C  CD2 . LEU   A 344 ? 1.1684 1.1961 1.1867 -0.0164 -0.0126 -0.2802 364 LEU   A CD2 
2390 N  N   . ARG   A 345 ? 1.3490 1.4919 1.3020 0.0294  0.0241  -0.3064 365 ARG   A N   
2391 C  CA  . ARG   A 345 ? 1.3228 1.5011 1.2553 0.0394  0.0355  -0.2943 365 ARG   A CA  
2392 C  C   . ARG   A 345 ? 1.2759 1.4723 1.1799 0.0289  0.0177  -0.2984 365 ARG   A C   
2393 O  O   . ARG   A 345 ? 1.2739 1.4972 1.1784 0.0285  0.0169  -0.2773 365 ARG   A O   
2394 C  CB  . ARG   A 345 ? 1.3749 1.5521 1.2804 0.0607  0.0571  -0.3074 365 ARG   A CB  
2395 C  CG  . ARG   A 345 ? 1.3017 1.5089 1.1835 0.0741  0.0766  -0.2892 365 ARG   A CG  
2396 C  CD  . ARG   A 345 ? 1.4177 1.6203 1.2599 0.0960  0.1006  -0.3042 365 ARG   A CD  
2397 N  NE  . ARG   A 345 ? 1.4849 1.6702 1.2760 0.0970  0.0839  -0.3371 365 ARG   A NE  
2398 C  CZ  . ARG   A 345 ? 1.5408 1.7375 1.2808 0.0976  0.0683  -0.3439 365 ARG   A CZ  
2399 N  NH1 . ARG   A 345 ? 1.4894 1.7127 1.2189 0.0990  0.0684  -0.3176 365 ARG   A NH1 
2400 N  NH2 . ARG   A 345 ? 1.7133 1.8933 1.4130 0.0978  0.0501  -0.3793 365 ARG   A NH2 
2401 N  N   . LEU   A 346 ? 1.3117 1.4935 1.1944 0.0208  0.0018  -0.3271 366 LEU   A N   
2402 C  CA  . LEU   A 346 ? 1.3603 1.5645 1.2232 0.0114  -0.0194 -0.3360 366 LEU   A CA  
2403 C  C   . LEU   A 346 ? 1.2931 1.5080 1.1943 -0.0097 -0.0329 -0.3217 366 LEU   A C   
2404 O  O   . LEU   A 346 ? 1.3416 1.5884 1.2389 -0.0124 -0.0452 -0.3151 366 LEU   A O   
2405 C  CB  . LEU   A 346 ? 1.2353 1.4210 1.0726 0.0066  -0.0345 -0.3754 366 LEU   A CB  
2406 C  CG  . LEU   A 346 ? 1.4015 1.5839 1.1834 0.0303  -0.0254 -0.3939 366 LEU   A CG  
2407 C  CD1 . LEU   A 346 ? 1.5619 1.7233 1.3201 0.0234  -0.0454 -0.4374 366 LEU   A CD1 
2408 C  CD2 . LEU   A 346 ? 1.3761 1.5943 1.1189 0.0473  -0.0235 -0.3770 366 LEU   A CD2 
2409 N  N   . PHE   A 347 ? 1.2734 1.4611 1.2086 -0.0220 -0.0300 -0.3162 367 PHE   A N   
2410 C  CA  . PHE   A 347 ? 1.2721 1.4631 1.2388 -0.0416 -0.0385 -0.3041 367 PHE   A CA  
2411 C  C   . PHE   A 347 ? 1.2643 1.4396 1.2547 -0.0389 -0.0273 -0.2787 367 PHE   A C   
2412 O  O   . PHE   A 347 ? 1.2774 1.4183 1.2821 -0.0481 -0.0269 -0.2788 367 PHE   A O   
2413 C  CB  . PHE   A 347 ? 1.2898 1.4562 1.2677 -0.0634 -0.0494 -0.3279 367 PHE   A CB  
2414 C  CG  . PHE   A 347 ? 1.3878 1.5641 1.3437 -0.0656 -0.0641 -0.3605 367 PHE   A CG  
2415 C  CD1 . PHE   A 347 ? 1.4426 1.6626 1.3961 -0.0692 -0.0814 -0.3660 367 PHE   A CD1 
2416 C  CD2 . PHE   A 347 ? 1.3477 1.4895 1.2843 -0.0616 -0.0629 -0.3874 367 PHE   A CD2 
2417 C  CE1 . PHE   A 347 ? 1.3922 1.6226 1.3230 -0.0693 -0.1004 -0.3991 367 PHE   A CE1 
2418 C  CE2 . PHE   A 347 ? 1.4476 1.5960 1.3595 -0.0627 -0.0792 -0.4214 367 PHE   A CE2 
2419 C  CZ  . PHE   A 347 ? 1.5728 1.7664 1.4810 -0.0667 -0.0995 -0.4279 367 PHE   A CZ  
2420 N  N   . PRO   A 348 ? 1.1878 1.3850 1.1813 -0.0257 -0.0187 -0.2566 368 PRO   A N   
2421 C  CA  . PRO   A 348 ? 1.2276 1.4148 1.2461 -0.0251 -0.0143 -0.2351 368 PRO   A CA  
2422 C  C   . PRO   A 348 ? 1.1643 1.3582 1.1948 -0.0401 -0.0221 -0.2246 368 PRO   A C   
2423 O  O   . PRO   A 348 ? 1.3973 1.6226 1.4290 -0.0393 -0.0240 -0.2137 368 PRO   A O   
2424 C  CB  . PRO   A 348 ? 1.2611 1.4720 1.2827 -0.0093 -0.0026 -0.2187 368 PRO   A CB  
2425 C  CG  . PRO   A 348 ? 1.3638 1.6027 1.3581 -0.0050 -0.0030 -0.2222 368 PRO   A CG  
2426 C  CD  . PRO   A 348 ? 1.2954 1.5232 1.2679 -0.0105 -0.0123 -0.2503 368 PRO   A CD  
2427 N  N   . ILE   A 349 ? 1.2395 1.4016 1.2776 -0.0521 -0.0243 -0.2268 369 ILE   A N   
2428 C  CA  . ILE   A 349 ? 1.3141 1.4797 1.3630 -0.0679 -0.0266 -0.2195 369 ILE   A CA  
2429 C  C   . ILE   A 349 ? 1.2293 1.4152 1.2860 -0.0615 -0.0247 -0.1976 369 ILE   A C   
2430 O  O   . ILE   A 349 ? 1.2825 1.4867 1.3486 -0.0706 -0.0255 -0.1921 369 ILE   A O   
2431 C  CB  . ILE   A 349 ? 1.2422 1.3598 1.2914 -0.0782 -0.0230 -0.2200 369 ILE   A CB  
2432 C  CG1 . ILE   A 349 ? 1.1485 1.2357 1.1916 -0.0621 -0.0212 -0.2070 369 ILE   A CG1 
2433 C  CG2 . ILE   A 349 ? 1.4116 1.5050 1.4566 -0.0880 -0.0244 -0.2434 369 ILE   A CG2 
2434 C  CD1 . ILE   A 349 ? 1.3311 1.3664 1.3642 -0.0672 -0.0181 -0.2021 369 ILE   A CD1 
2435 N  N   . ALA   A 350 ? 1.1209 1.3042 1.1786 -0.0462 -0.0219 -0.1866 370 ALA   A N   
2436 C  CA  . ALA   A 350 ? 1.1652 1.3638 1.2317 -0.0402 -0.0209 -0.1687 370 ALA   A CA  
2437 C  C   . ALA   A 350 ? 1.1556 1.3932 1.2219 -0.0355 -0.0198 -0.1636 370 ALA   A C   
2438 O  O   . ALA   A 350 ? 1.0809 1.3330 1.1538 -0.0345 -0.0199 -0.1512 370 ALA   A O   
2439 C  CB  . ALA   A 350 ? 1.1582 1.3419 1.2339 -0.0273 -0.0202 -0.1619 370 ALA   A CB  
2440 N  N   . MET   A 351 ? 1.0378 1.2890 1.0919 -0.0298 -0.0184 -0.1727 371 MET   A N   
2441 C  CA  . MET   A 351 ? 1.1866 1.4692 1.2291 -0.0209 -0.0174 -0.1667 371 MET   A CA  
2442 C  C   . MET   A 351 ? 1.0902 1.3771 1.1411 -0.0093 -0.0069 -0.1460 371 MET   A C   
2443 O  O   . MET   A 351 ? 0.9951 1.2920 1.0331 0.0022  0.0030  -0.1401 371 MET   A O   
2444 C  CB  . MET   A 351 ? 1.1048 1.4121 1.1497 -0.0279 -0.0282 -0.1678 371 MET   A CB  
2445 C  CG  . MET   A 351 ? 1.3019 1.6128 1.3450 -0.0413 -0.0392 -0.1910 371 MET   A CG  
2446 S  SD  . MET   A 351 ? 1.4766 1.8213 1.5432 -0.0527 -0.0506 -0.1935 371 MET   A SD  
2447 C  CE  . MET   A 351 ? 1.1881 1.5083 1.2762 -0.0615 -0.0383 -0.1776 371 MET   A CE  
2448 N  N   . ARG   A 352 ? 1.0214 1.2981 1.0921 -0.0121 -0.0075 -0.1353 372 ARG   A N   
2449 C  CA  . ARG   A 352 ? 1.0216 1.2997 1.1065 -0.0040 0.0006  -0.1182 372 ARG   A CA  
2450 C  C   . ARG   A 352 ? 0.9615 1.2164 1.0691 -0.0060 -0.0019 -0.1182 372 ARG   A C   
2451 O  O   . ARG   A 352 ? 0.9692 1.2071 1.0743 -0.0122 -0.0110 -0.1241 372 ARG   A O   
2452 C  CB  . ARG   A 352 ? 1.0847 1.3774 1.1683 -0.0015 -0.0019 -0.1055 372 ARG   A CB  
2453 C  CG  . ARG   A 352 ? 1.0155 1.3340 1.0772 0.0061  -0.0032 -0.1027 372 ARG   A CG  
2454 C  CD  . ARG   A 352 ? 1.1408 1.4748 1.2075 0.0084  -0.0101 -0.0945 372 ARG   A CD  
2455 N  NE  . ARG   A 352 ? 1.2207 1.5745 1.2688 0.0235  -0.0103 -0.0830 372 ARG   A NE  
2456 C  CZ  . ARG   A 352 ? 1.1820 1.5492 1.2347 0.0321  -0.0146 -0.0719 372 ARG   A CZ  
2457 N  NH1 . ARG   A 352 ? 1.1705 1.5346 1.2463 0.0265  -0.0164 -0.0716 372 ARG   A NH1 
2458 N  NH2 . ARG   A 352 ? 1.1119 1.4935 1.1416 0.0495  -0.0163 -0.0602 372 ARG   A NH2 
2459 N  N   . LEU   A 353 ? 1.0178 1.2717 1.1473 -0.0003 0.0065  -0.1116 373 LEU   A N   
2460 C  CA  . LEU   A 353 ? 0.9693 1.2070 1.1262 -0.0003 -0.0001 -0.1121 373 LEU   A CA  
2461 C  C   . LEU   A 353 ? 0.9420 1.1815 1.1124 0.0008  0.0024  -0.0992 373 LEU   A C   
2462 O  O   . LEU   A 353 ? 0.8999 1.1520 1.0712 0.0042  0.0162  -0.0870 373 LEU   A O   
2463 C  CB  . LEU   A 353 ? 0.9984 1.2369 1.1845 0.0040  0.0061  -0.1178 373 LEU   A CB  
2464 C  CG  . LEU   A 353 ? 0.9742 1.2084 1.1493 0.0064  0.0063  -0.1314 373 LEU   A CG  
2465 C  CD1 . LEU   A 353 ? 1.0448 1.2862 1.2566 0.0133  0.0163  -0.1358 373 LEU   A CD1 
2466 C  CD2 . LEU   A 353 ? 0.7045 0.9134 0.8647 0.0038  -0.0116 -0.1405 373 LEU   A CD2 
2467 N  N   . GLU   A 354 ? 0.8810 1.1035 1.0572 -0.0003 -0.0105 -0.1018 374 GLU   A N   
2468 C  CA  . GLU   A 354 ? 0.9306 1.1492 1.1159 0.0012  -0.0098 -0.0929 374 GLU   A CA  
2469 C  C   . GLU   A 354 ? 0.9715 1.1718 1.1835 0.0016  -0.0223 -0.1009 374 GLU   A C   
2470 O  O   . GLU   A 354 ? 0.9539 1.1402 1.1614 0.0030  -0.0376 -0.1127 374 GLU   A O   
2471 C  CB  . GLU   A 354 ? 0.8926 1.1100 1.0500 0.0017  -0.0134 -0.0899 374 GLU   A CB  
2472 C  CG  . GLU   A 354 ? 1.0355 1.2769 1.1758 0.0029  -0.0050 -0.0824 374 GLU   A CG  
2473 C  CD  . GLU   A 354 ? 1.0987 1.3455 1.2258 0.0043  -0.0076 -0.0797 374 GLU   A CD  
2474 O  OE1 . GLU   A 354 ? 1.2208 1.4493 1.3455 0.0040  -0.0127 -0.0836 374 GLU   A OE1 
2475 O  OE2 . GLU   A 354 ? 1.0380 1.3086 1.1569 0.0075  -0.0048 -0.0746 374 GLU   A OE2 
2476 N  N   . ARG   A 355 ? 0.9281 1.1263 1.1668 0.0014  -0.0171 -0.0948 375 ARG   A N   
2477 C  CA  . ARG   A 355 ? 0.9552 1.1368 1.2235 0.0008  -0.0318 -0.1054 375 ARG   A CA  
2478 C  C   . ARG   A 355 ? 0.9359 1.1063 1.2096 0.0012  -0.0265 -0.0976 375 ARG   A C   
2479 O  O   . ARG   A 355 ? 1.0583 1.2367 1.3420 0.0003  -0.0065 -0.0819 375 ARG   A O   
2480 C  CB  . ARG   A 355 ? 0.9443 1.1367 1.2665 -0.0031 -0.0296 -0.1114 375 ARG   A CB  
2481 C  CG  . ARG   A 355 ? 0.8359 1.0381 1.1603 -0.0004 -0.0350 -0.1208 375 ARG   A CG  
2482 C  CD  . ARG   A 355 ? 0.6987 0.8813 1.0055 0.0060  -0.0640 -0.1364 375 ARG   A CD  
2483 N  NE  . ARG   A 355 ? 1.0767 1.2653 1.3916 0.0111  -0.0697 -0.1449 375 ARG   A NE  
2484 C  CZ  . ARG   A 355 ? 0.9558 1.1425 1.2349 0.0130  -0.0631 -0.1422 375 ARG   A CZ  
2485 N  NH1 . ARG   A 355 ? 0.8654 1.0494 1.1023 0.0088  -0.0521 -0.1326 375 ARG   A NH1 
2486 N  NH2 . ARG   A 355 ? 0.9451 1.1332 1.2355 0.0194  -0.0684 -0.1511 375 ARG   A NH2 
2487 N  N   . VAL   A 356 ? 0.9857 1.1337 1.2487 0.0046  -0.0434 -0.1083 376 VAL   A N   
2488 C  CA  . VAL   A 356 ? 1.0489 1.1806 1.3204 0.0061  -0.0398 -0.1047 376 VAL   A CA  
2489 C  C   . VAL   A 356 ? 1.0389 1.1636 1.3681 -0.0016 -0.0430 -0.1126 376 VAL   A C   
2490 O  O   . VAL   A 356 ? 1.0337 1.1556 1.3858 -0.0036 -0.0637 -0.1314 376 VAL   A O   
2491 C  CB  . VAL   A 356 ? 1.1490 1.2573 1.3825 0.0144  -0.0544 -0.1151 376 VAL   A CB  
2492 C  CG1 . VAL   A 356 ? 1.0724 1.1599 1.3168 0.0175  -0.0511 -0.1145 376 VAL   A CG1 
2493 C  CG2 . VAL   A 356 ? 1.1244 1.2435 1.3126 0.0193  -0.0462 -0.1065 376 VAL   A CG2 
2494 N  N   . CYS   A 357 ? 1.0815 1.2030 1.4369 -0.0056 -0.0228 -0.0981 377 CYS   A N   
2495 C  CA  . CYS   A 357 ? 1.1951 1.3082 1.6140 -0.0164 -0.0212 -0.1047 377 CYS   A CA  
2496 C  C   . CYS   A 357 ? 1.0472 1.1282 1.4687 -0.0147 -0.0410 -0.1221 377 CYS   A C   
2497 O  O   . CYS   A 357 ? 1.1727 1.2333 1.5712 -0.0085 -0.0322 -0.1127 377 CYS   A O   
2498 C  CB  . CYS   A 357 ? 1.0573 1.1729 1.4989 -0.0212 0.0131  -0.0793 377 CYS   A CB  
2499 S  SG  . CYS   A 357 ? 1.1291 1.2258 1.6527 -0.0376 0.0249  -0.0818 377 CYS   A SG  
2500 N  N   . LYS   A 358 ? 1.0299 1.1056 1.4771 -0.0178 -0.0697 -0.1490 378 LYS   A N   
2501 C  CA  . LYS   A 358 ? 1.1932 1.2367 1.6271 -0.0125 -0.0952 -0.1715 378 LYS   A CA  
2502 C  C   . LYS   A 358 ? 1.1151 1.1374 1.6094 -0.0242 -0.0944 -0.1809 378 LYS   A C   
2503 O  O   . LYS   A 358 ? 1.1161 1.1079 1.6012 -0.0199 -0.1165 -0.2029 378 LYS   A O   
2504 C  CB  . LYS   A 358 ? 1.1477 1.1912 1.5671 -0.0057 -0.1320 -0.1977 378 LYS   A CB  
2505 C  CG  . LYS   A 358 ? 1.1512 1.2091 1.6447 -0.0160 -0.1520 -0.2186 378 LYS   A CG  
2506 C  CD  . LYS   A 358 ? 1.2391 1.2877 1.7094 -0.0036 -0.1959 -0.2474 378 LYS   A CD  
2507 C  CE  . LYS   A 358 ? 1.2404 1.3065 1.6732 0.0068  -0.2003 -0.2404 378 LYS   A CE  
2508 N  NZ  . LYS   A 358 ? 1.2209 1.2807 1.6486 0.0193  -0.2445 -0.2677 378 LYS   A NZ  
2509 N  N   . LYS   A 359 ? 1.0964 1.1305 1.6499 -0.0387 -0.0680 -0.1653 379 LYS   A N   
2510 C  CA  . LYS   A 359 ? 1.2098 1.2185 1.8229 -0.0523 -0.0601 -0.1698 379 LYS   A CA  
2511 C  C   . LYS   A 359 ? 1.2202 1.2413 1.8784 -0.0650 -0.0183 -0.1405 379 LYS   A C   
2512 O  O   . LYS   A 359 ? 1.2239 1.2786 1.8817 -0.0652 -0.0028 -0.1261 379 LYS   A O   
2513 C  CB  . LYS   A 359 ? 1.1312 1.1376 1.8056 -0.0630 -0.0951 -0.2079 379 LYS   A CB  
2514 C  CG  . LYS   A 359 ? 1.0870 1.1356 1.8212 -0.0725 -0.1020 -0.2167 379 LYS   A CG  
2515 C  CD  . LYS   A 359 ? 1.0712 1.1194 1.8628 -0.0790 -0.1452 -0.2584 379 LYS   A CD  
2516 C  CE  . LYS   A 359 ? 0.9188 1.0135 1.7828 -0.0870 -0.1532 -0.2689 379 LYS   A CE  
2517 N  NZ  . LYS   A 359 ? 0.9677 1.0664 1.8896 -0.0906 -0.2020 -0.3125 379 LYS   A NZ  
2518 N  N   . ASP   A 360 ? 1.1358 1.1248 1.8292 -0.0744 0.0015  -0.1317 380 ASP   A N   
2519 C  CA  . ASP   A 360 ? 1.2342 1.2243 1.9651 -0.0855 0.0461  -0.1003 380 ASP   A CA  
2520 C  C   . ASP   A 360 ? 1.2085 1.2375 2.0106 -0.1018 0.0540  -0.1062 380 ASP   A C   
2521 O  O   . ASP   A 360 ? 1.1780 1.2185 2.0439 -0.1141 0.0270  -0.1385 380 ASP   A O   
2522 C  CB  . ASP   A 360 ? 1.0961 1.0386 1.8684 -0.0966 0.0623  -0.0958 380 ASP   A CB  
2523 C  CG  . ASP   A 360 ? 1.3600 1.2628 2.0642 -0.0772 0.0638  -0.0832 380 ASP   A CG  
2524 O  OD1 . ASP   A 360 ? 1.4070 1.3215 2.0400 -0.0572 0.0459  -0.0857 380 ASP   A OD1 
2525 O  OD2 . ASP   A 360 ? 1.4463 1.3057 2.1722 -0.0819 0.0848  -0.0703 380 ASP   A OD2 
2526 N  N   . VAL   A 361 ? 1.3326 1.3830 2.1236 -0.1000 0.0903  -0.0762 381 VAL   A N   
2527 C  CA  . VAL   A 361 ? 1.3699 1.4591 2.2240 -0.1123 0.1060  -0.0780 381 VAL   A CA  
2528 C  C   . VAL   A 361 ? 1.4905 1.5761 2.3426 -0.1145 0.1620  -0.0380 381 VAL   A C   
2529 O  O   . VAL   A 361 ? 1.5385 1.5943 2.3306 -0.1031 0.1827  -0.0090 381 VAL   A O   
2530 C  CB  . VAL   A 361 ? 1.3167 1.4460 2.1381 -0.0999 0.0819  -0.0919 381 VAL   A CB  
2531 C  CG1 . VAL   A 361 ? 1.3086 1.4491 2.1695 -0.1031 0.0334  -0.1328 381 VAL   A CG1 
2532 C  CG2 . VAL   A 361 ? 1.3053 1.4274 2.0219 -0.0785 0.0750  -0.0783 381 VAL   A CG2 
2533 N  N   . GLU   A 362 ? 1.8425 1.9590 2.7597 -0.1270 0.1868  -0.0364 382 GLU   A N   
2534 C  CA  . GLU   A 362 ? 1.9412 2.0573 2.8560 -0.1281 0.2441  0.0007  382 GLU   A CA  
2535 C  C   . GLU   A 362 ? 1.8438 2.0103 2.7770 -0.1256 0.2516  -0.0066 382 GLU   A C   
2536 O  O   . GLU   A 362 ? 1.9238 2.1166 2.9518 -0.1425 0.2660  -0.0179 382 GLU   A O   
2537 C  CB  . GLU   A 362 ? 2.1388 2.2286 3.1374 -0.1516 0.2810  0.0126  382 GLU   A CB  
2538 C  CG  . GLU   A 362 ? 2.1718 2.2544 3.1650 -0.1523 0.3463  0.0543  382 GLU   A CG  
2539 C  CD  . GLU   A 362 ? 2.3243 2.3727 3.4001 -0.1772 0.3862  0.0688  382 GLU   A CD  
2540 O  OE1 . GLU   A 362 ? 2.3614 2.3760 3.4685 -0.1884 0.3636  0.0539  382 GLU   A OE1 
2541 O  OE2 . GLU   A 362 ? 2.4082 2.4609 3.5175 -0.1859 0.4421  0.0945  382 GLU   A OE2 
2542 N  N   . ILE   A 363 ? 1.6107 1.7913 2.4581 -0.1043 0.2413  -0.0020 383 ILE   A N   
2543 C  CA  . ILE   A 363 ? 1.5303 1.7536 2.3833 -0.0981 0.2426  -0.0124 383 ILE   A CA  
2544 C  C   . ILE   A 363 ? 1.5175 1.7433 2.3409 -0.0914 0.2979  0.0203  383 ILE   A C   
2545 O  O   . ILE   A 363 ? 1.5145 1.7132 2.2576 -0.0785 0.3160  0.0488  383 ILE   A O   
2546 C  CB  . ILE   A 363 ? 1.5310 1.7644 2.3115 -0.0804 0.1989  -0.0297 383 ILE   A CB  
2547 C  CG1 . ILE   A 363 ? 1.4284 1.6473 2.1028 -0.0619 0.2097  -0.0052 383 ILE   A CG1 
2548 C  CG2 . ILE   A 363 ? 1.4562 1.6739 2.2417 -0.0831 0.1502  -0.0546 383 ILE   A CG2 
2549 C  CD1 . ILE   A 363 ? 1.2375 1.4657 1.8483 -0.0481 0.1714  -0.0216 383 ILE   A CD1 
2550 N  N   . ASN   A 364 ? 1.4780 1.7364 2.3674 -0.0986 0.3251  0.0158  384 ASN   A N   
2551 C  CA  . ASN   A 364 ? 1.4074 1.6707 2.2705 -0.0908 0.3811  0.0436  384 ASN   A CA  
2552 C  C   . ASN   A 364 ? 1.4038 1.6233 2.2309 -0.0913 0.4255  0.0842  384 ASN   A C   
2553 O  O   . ASN   A 364 ? 1.4934 1.7009 2.2418 -0.0741 0.4592  0.1122  384 ASN   A O   
2554 C  CB  . ASN   A 364 ? 1.5265 1.8030 2.2951 -0.0666 0.3701  0.0416  384 ASN   A CB  
2555 C  CG  . ASN   A 364 ? 1.3946 1.7137 2.2073 -0.0643 0.3513  0.0106  384 ASN   A CG  
2556 O  OD1 . ASN   A 364 ? 1.3067 1.6353 2.1239 -0.0628 0.3006  -0.0169 384 ASN   A OD1 
2557 N  ND2 . ASN   A 364 ? 1.3036 1.6464 2.1461 -0.0618 0.3941  0.0159  384 ASN   A ND2 
2558 N  N   . GLY   A 365 ? 1.4078 1.5993 2.2887 -0.1093 0.4246  0.0870  385 GLY   A N   
2559 C  CA  . GLY   A 365 ? 1.5199 1.6629 2.3735 -0.1101 0.4675  0.1266  385 GLY   A CA  
2560 C  C   . GLY   A 365 ? 1.5726 1.6775 2.3183 -0.0889 0.4474  0.1444  385 GLY   A C   
2561 O  O   . GLY   A 365 ? 1.6524 1.7209 2.3396 -0.0771 0.4849  0.1831  385 GLY   A O   
2562 N  N   . MET   A 366 ? 1.6185 1.7305 2.3363 -0.0822 0.3903  0.1181  386 MET   A N   
2563 C  CA  . MET   A 366 ? 1.5855 1.6683 2.2133 -0.0624 0.3686  0.1308  386 MET   A CA  
2564 C  C   . MET   A 366 ? 1.5386 1.6116 2.1960 -0.0706 0.3214  0.1027  386 MET   A C   
2565 O  O   . MET   A 366 ? 1.3631 1.4658 2.0425 -0.0746 0.2823  0.0684  386 MET   A O   
2566 C  CB  . MET   A 366 ? 1.5360 1.6430 2.0715 -0.0383 0.3508  0.1295  386 MET   A CB  
2567 C  CG  . MET   A 366 ? 1.5056 1.5932 1.9599 -0.0182 0.3235  0.1376  386 MET   A CG  
2568 S  SD  . MET   A 366 ? 1.5717 1.6901 1.9295 0.0064  0.3044  0.1339  386 MET   A SD  
2569 C  CE  . MET   A 366 ? 1.5422 1.6595 1.8723 0.0147  0.3605  0.1630  386 MET   A CE  
2570 N  N   . PHE   A 367 ? 1.4131 1.4406 2.0660 -0.0707 0.3260  0.1175  387 PHE   A N   
2571 C  CA  . PHE   A 367 ? 1.4053 1.4172 2.0746 -0.0747 0.2837  0.0913  387 PHE   A CA  
2572 C  C   . PHE   A 367 ? 1.4092 1.4349 1.9971 -0.0525 0.2453  0.0814  387 PHE   A C   
2573 O  O   . PHE   A 367 ? 1.3797 1.4028 1.8916 -0.0313 0.2542  0.1053  387 PHE   A O   
2574 C  CB  . PHE   A 367 ? 1.4116 1.3664 2.0932 -0.0781 0.3024  0.1109  387 PHE   A CB  
2575 C  CG  . PHE   A 367 ? 1.5523 1.4847 2.2363 -0.0771 0.2617  0.0854  387 PHE   A CG  
2576 C  CD1 . PHE   A 367 ? 1.4779 1.4105 2.2413 -0.0991 0.2375  0.0491  387 PHE   A CD1 
2577 C  CD2 . PHE   A 367 ? 1.4257 1.3380 2.0330 -0.0525 0.2473  0.0962  387 PHE   A CD2 
2578 C  CE1 . PHE   A 367 ? 1.4514 1.3596 2.2084 -0.0958 0.2009  0.0240  387 PHE   A CE1 
2579 C  CE2 . PHE   A 367 ? 1.4683 1.3593 2.0758 -0.0497 0.2140  0.0723  387 PHE   A CE2 
2580 C  CZ  . PHE   A 367 ? 1.4524 1.3387 2.1301 -0.0710 0.1915  0.0362  387 PHE   A CZ  
2581 N  N   . ILE   A 368 ? 1.4346 1.4750 2.0394 -0.0570 0.2023  0.0456  388 ILE   A N   
2582 C  CA  . ILE   A 368 ? 1.3876 1.4412 1.9257 -0.0396 0.1682  0.0338  388 ILE   A CA  
2583 C  C   . ILE   A 368 ? 1.3560 1.3850 1.9030 -0.0406 0.1368  0.0111  388 ILE   A C   
2584 O  O   . ILE   A 368 ? 1.3415 1.3717 1.9429 -0.0551 0.1160  -0.0177 388 ILE   A O   
2585 C  CB  . ILE   A 368 ? 1.3754 1.4723 1.9076 -0.0398 0.1492  0.0135  388 ILE   A CB  
2586 C  CG1 . ILE   A 368 ? 1.3075 1.4260 1.8180 -0.0346 0.1804  0.0344  388 ILE   A CG1 
2587 C  CG2 . ILE   A 368 ? 1.2744 1.3797 1.7473 -0.0260 0.1154  -0.0004 388 ILE   A CG2 
2588 C  CD1 . ILE   A 368 ? 1.0133 1.1683 1.5035 -0.0304 0.1629  0.0168  388 ILE   A CD1 
2589 N  N   . PRO   A 369 ? 1.3746 1.3818 1.8698 -0.0237 0.1311  0.0210  389 PRO   A N   
2590 C  CA  . PRO   A 369 ? 1.3785 1.3567 1.8805 -0.0228 0.1066  -0.0003 389 PRO   A CA  
2591 C  C   . PRO   A 369 ? 1.3299 1.3290 1.8036 -0.0172 0.0697  -0.0293 389 PRO   A C   
2592 O  O   . PRO   A 369 ? 1.2885 1.3194 1.7210 -0.0088 0.0640  -0.0269 389 PRO   A O   
2593 C  CB  . PRO   A 369 ? 1.2974 1.2464 1.7541 -0.0030 0.1203  0.0254  389 PRO   A CB  
2594 C  CG  . PRO   A 369 ? 1.3765 1.3418 1.7976 0.0075  0.1482  0.0602  389 PRO   A CG  
2595 C  CD  . PRO   A 369 ? 1.3101 1.3185 1.7391 -0.0024 0.1462  0.0509  389 PRO   A CD  
2596 N  N   . LYS   A 370 ? 1.2648 1.2414 1.7593 -0.0218 0.0452  -0.0575 390 LYS   A N   
2597 C  CA  . LYS   A 370 ? 1.1949 1.1815 1.6573 -0.0149 0.0117  -0.0847 390 LYS   A CA  
2598 C  C   . LYS   A 370 ? 1.2237 1.2167 1.6168 0.0054  0.0120  -0.0734 390 LYS   A C   
2599 O  O   . LYS   A 370 ? 1.1244 1.0983 1.4990 0.0172  0.0257  -0.0571 390 LYS   A O   
2600 C  CB  . LYS   A 370 ? 1.2556 1.2085 1.7423 -0.0192 -0.0130 -0.1157 390 LYS   A CB  
2601 C  CG  . LYS   A 370 ? 1.2489 1.1996 1.6863 -0.0067 -0.0445 -0.1411 390 LYS   A CG  
2602 C  CD  . LYS   A 370 ? 1.2338 1.1473 1.6895 -0.0088 -0.0702 -0.1739 390 LYS   A CD  
2603 C  CE  . LYS   A 370 ? 1.2464 1.1520 1.6398 0.0074  -0.0979 -0.1967 390 LYS   A CE  
2604 N  NZ  . LYS   A 370 ? 1.5220 1.3893 1.9253 0.0079  -0.1262 -0.2323 390 LYS   A NZ  
2605 N  N   . GLY   A 371 ? 1.2401 1.2604 1.5991 0.0097  -0.0025 -0.0821 391 GLY   A N   
2606 C  CA  . GLY   A 371 ? 1.1537 1.1863 1.4574 0.0252  -0.0023 -0.0748 391 GLY   A CA  
2607 C  C   . GLY   A 371 ? 1.0815 1.1488 1.3657 0.0281  0.0128  -0.0530 391 GLY   A C   
2608 O  O   . GLY   A 371 ? 1.0775 1.1642 1.3246 0.0365  0.0089  -0.0523 391 GLY   A O   
2609 N  N   . VAL   A 372 ? 1.0967 1.1715 1.4053 0.0213  0.0308  -0.0364 392 VAL   A N   
2610 C  CA  . VAL   A 372 ? 1.1151 1.2203 1.3996 0.0255  0.0434  -0.0187 392 VAL   A CA  
2611 C  C   . VAL   A 372 ? 0.9965 1.1276 1.2715 0.0192  0.0298  -0.0343 392 VAL   A C   
2612 O  O   . VAL   A 372 ? 1.1190 1.2472 1.4215 0.0089  0.0187  -0.0516 392 VAL   A O   
2613 C  CB  . VAL   A 372 ? 1.2015 1.3022 1.5090 0.0211  0.0694  0.0026  392 VAL   A CB  
2614 C  CG1 . VAL   A 372 ? 1.0826 1.2139 1.3626 0.0250  0.0800  0.0147  392 VAL   A CG1 
2615 C  CG2 . VAL   A 372 ? 1.1960 1.2677 1.4991 0.0319  0.0851  0.0241  392 VAL   A CG2 
2616 N  N   . VAL   A 373 ? 1.0009 1.1563 1.2389 0.0261  0.0289  -0.0295 393 VAL   A N   
2617 C  CA  . VAL   A 373 ? 0.9876 1.1640 1.2139 0.0204  0.0200  -0.0412 393 VAL   A CA  
2618 C  C   . VAL   A 373 ? 0.9864 1.1798 1.2166 0.0183  0.0358  -0.0304 393 VAL   A C   
2619 O  O   . VAL   A 373 ? 1.0298 1.2358 1.2347 0.0269  0.0464  -0.0151 393 VAL   A O   
2620 C  CB  . VAL   A 373 ? 1.1164 1.3084 1.3069 0.0261  0.0117  -0.0447 393 VAL   A CB  
2621 C  CG1 . VAL   A 373 ? 0.9519 1.1622 1.1302 0.0195  0.0069  -0.0536 393 VAL   A CG1 
2622 C  CG2 . VAL   A 373 ? 0.9983 1.1717 1.1816 0.0283  -0.0002 -0.0572 393 VAL   A CG2 
2623 N  N   . VAL   A 374 ? 0.8922 1.0862 1.1533 0.0090  0.0370  -0.0394 394 VAL   A N   
2624 C  CA  . VAL   A 374 ? 0.8933 1.1036 1.1580 0.0078  0.0542  -0.0326 394 VAL   A CA  
2625 C  C   . VAL   A 374 ? 0.8390 1.0676 1.0704 0.0097  0.0446  -0.0425 394 VAL   A C   
2626 O  O   . VAL   A 374 ? 0.8801 1.1059 1.1056 0.0067  0.0255  -0.0584 394 VAL   A O   
2627 C  CB  . VAL   A 374 ? 1.0163 1.2247 1.3367 -0.0022 0.0597  -0.0406 394 VAL   A CB  
2628 C  CG1 . VAL   A 374 ? 0.9509 1.1776 1.2748 -0.0018 0.0807  -0.0355 394 VAL   A CG1 
2629 C  CG2 . VAL   A 374 ? 1.0318 1.2203 1.3912 -0.0073 0.0713  -0.0315 394 VAL   A CG2 
2630 N  N   . MET   A 375 ? 0.8692 1.1126 1.0753 0.0153  0.0586  -0.0334 395 MET   A N   
2631 C  CA  A MET   A 375 ? 1.0156 1.2745 1.1892 0.0167  0.0496  -0.0443 395 MET   A CA  
2632 C  CA  B MET   A 375 ? 0.9985 1.2573 1.1723 0.0167  0.0495  -0.0444 395 MET   A CA  
2633 C  C   . MET   A 375 ? 0.9226 1.1910 1.0911 0.0192  0.0664  -0.0442 395 MET   A C   
2634 O  O   . MET   A 375 ? 0.9525 1.2206 1.1180 0.0252  0.0887  -0.0275 395 MET   A O   
2635 C  CB  A MET   A 375 ? 1.0083 1.2786 1.1441 0.0246  0.0431  -0.0378 395 MET   A CB  
2636 C  CB  B MET   A 375 ? 0.9946 1.2650 1.1305 0.0245  0.0429  -0.0381 395 MET   A CB  
2637 C  CG  A MET   A 375 ? 0.9570 1.2425 1.0687 0.0219  0.0294  -0.0535 395 MET   A CG  
2638 C  CG  B MET   A 375 ? 1.0055 1.2913 1.1166 0.0220  0.0299  -0.0537 395 MET   A CG  
2639 S  SD  A MET   A 375 ? 0.8563 1.1584 0.9321 0.0299  0.0374  -0.0545 395 MET   A SD  
2640 S  SD  B MET   A 375 ? 1.1412 1.4509 1.2169 0.0330  0.0226  -0.0477 395 MET   A SD  
2641 C  CE  A MET   A 375 ? 1.0200 1.3318 1.0672 0.0469  0.0407  -0.0327 395 MET   A CE  
2642 C  CE  B MET   A 375 ? 1.0531 1.3648 1.0997 0.0472  0.0414  -0.0323 395 MET   A CE  
2643 N  N   . ILE   A 376 ? 0.8774 1.1504 1.0420 0.0160  0.0577  -0.0620 396 ILE   A N   
2644 C  CA  . ILE   A 376 ? 0.9744 1.2555 1.1289 0.0202  0.0716  -0.0674 396 ILE   A CA  
2645 C  C   . ILE   A 376 ? 0.9773 1.2665 1.0850 0.0232  0.0602  -0.0776 396 ILE   A C   
2646 O  O   . ILE   A 376 ? 0.9784 1.2635 1.0844 0.0164  0.0421  -0.0935 396 ILE   A O   
2647 C  CB  . ILE   A 376 ? 1.1421 1.4198 1.3347 0.0160  0.0694  -0.0828 396 ILE   A CB  
2648 C  CG1 . ILE   A 376 ? 0.9351 1.2119 1.1839 0.0126  0.0815  -0.0759 396 ILE   A CG1 
2649 C  CG2 . ILE   A 376 ? 0.9474 1.2320 1.1235 0.0223  0.0816  -0.0926 396 ILE   A CG2 
2650 C  CD1 . ILE   A 376 ? 0.9456 1.2102 1.2227 0.0057  0.0610  -0.0788 396 ILE   A CD1 
2651 N  N   . PRO   A 377 ? 0.9382 1.2370 1.0067 0.0336  0.0694  -0.0696 397 PRO   A N   
2652 C  CA  . PRO   A 377 ? 1.0248 1.3345 1.0521 0.0363  0.0542  -0.0836 397 PRO   A CA  
2653 C  C   . PRO   A 377 ? 0.9151 1.2209 0.9339 0.0354  0.0564  -0.1044 397 PRO   A C   
2654 O  O   . PRO   A 377 ? 1.0038 1.3126 0.9900 0.0463  0.0689  -0.1069 397 PRO   A O   
2655 C  CB  . PRO   A 377 ? 1.0942 1.4124 1.0804 0.0522  0.0629  -0.0669 397 PRO   A CB  
2656 C  CG  . PRO   A 377 ? 1.1355 1.4428 1.1333 0.0579  0.0933  -0.0478 397 PRO   A CG  
2657 C  CD  . PRO   A 377 ? 1.0264 1.3240 1.0844 0.0443  0.0946  -0.0472 397 PRO   A CD  
2658 N  N   . SER   A 378 ? 0.9584 1.2534 1.0032 0.0243  0.0445  -0.1191 398 SER   A N   
2659 C  CA  . SER   A 378 ? 1.0346 1.3196 1.0778 0.0242  0.0458  -0.1389 398 SER   A CA  
2660 C  C   . SER   A 378 ? 1.1020 1.3919 1.1006 0.0279  0.0399  -0.1554 398 SER   A C   
2661 O  O   . SER   A 378 ? 1.1055 1.3913 1.0862 0.0368  0.0521  -0.1663 398 SER   A O   
2662 C  CB  . SER   A 378 ? 0.9935 1.2608 1.0621 0.0134  0.0301  -0.1493 398 SER   A CB  
2663 O  OG  . SER   A 378 ? 1.1466 1.4085 1.2541 0.0134  0.0332  -0.1394 398 SER   A OG  
2664 N  N   . TYR   A 379 ? 1.0746 1.3750 1.0567 0.0222  0.0212  -0.1594 399 TYR   A N   
2665 C  CA  . TYR   A 379 ? 1.1222 1.4302 1.0657 0.0250  0.0102  -0.1789 399 TYR   A CA  
2666 C  C   . TYR   A 379 ? 1.1919 1.5093 1.0917 0.0449  0.0238  -0.1713 399 TYR   A C   
2667 O  O   . TYR   A 379 ? 1.2914 1.6031 1.1574 0.0534  0.0279  -0.1885 399 TYR   A O   
2668 C  CB  . TYR   A 379 ? 1.0894 1.4146 1.0356 0.0150  -0.0132 -0.1843 399 TYR   A CB  
2669 C  CG  . TYR   A 379 ? 1.0994 1.4360 1.0145 0.0156  -0.0308 -0.2093 399 TYR   A CG  
2670 C  CD1 . TYR   A 379 ? 1.3368 1.6935 1.2100 0.0331  -0.0365 -0.2071 399 TYR   A CD1 
2671 C  CD2 . TYR   A 379 ? 1.1145 1.4389 1.0406 -0.0006 -0.0428 -0.2360 399 TYR   A CD2 
2672 C  CE1 . TYR   A 379 ? 1.4352 1.8035 1.2785 0.0351  -0.0578 -0.2339 399 TYR   A CE1 
2673 C  CE2 . TYR   A 379 ? 1.0335 1.3679 0.9364 -0.0019 -0.0615 -0.2632 399 TYR   A CE2 
2674 C  CZ  . TYR   A 379 ? 1.1907 1.5490 1.0523 0.0162  -0.0709 -0.2637 399 TYR   A CZ  
2675 O  OH  . TYR   A 379 ? 1.1428 1.5121 0.9798 0.0161  -0.0946 -0.2948 399 TYR   A OH  
2676 N  N   . ALA   A 380 ? 1.1155 1.4430 1.0108 0.0540  0.0321  -0.1451 400 ALA   A N   
2677 C  CA  . ALA   A 380 ? 1.2528 1.5840 1.0978 0.0750  0.0469  -0.1332 400 ALA   A CA  
2678 C  C   . ALA   A 380 ? 1.2126 1.5296 1.0558 0.0830  0.0803  -0.1283 400 ALA   A C   
2679 O  O   . ALA   A 380 ? 1.2676 1.5819 1.0590 0.1009  0.0959  -0.1269 400 ALA   A O   
2680 C  CB  . ALA   A 380 ? 1.2700 1.6087 1.1119 0.0835  0.0499  -0.1034 400 ALA   A CB  
2681 N  N   . LEU   A 381 ? 1.1775 1.4862 1.0763 0.0719  0.0918  -0.1260 401 LEU   A N   
2682 C  CA  . LEU   A 381 ? 1.1960 1.4976 1.1080 0.0787  0.1234  -0.1239 401 LEU   A CA  
2683 C  C   . LEU   A 381 ? 1.1993 1.4931 1.0920 0.0827  0.1219  -0.1533 401 LEU   A C   
2684 O  O   . LEU   A 381 ? 1.3385 1.6290 1.2074 0.0972  0.1486  -0.1554 401 LEU   A O   
2685 C  CB  . LEU   A 381 ? 1.1363 1.4360 1.1203 0.0669  0.1307  -0.1146 401 LEU   A CB  
2686 C  CG  . LEU   A 381 ? 1.1926 1.4946 1.2004 0.0646  0.1419  -0.0859 401 LEU   A CG  
2687 C  CD1 . LEU   A 381 ? 1.1802 1.4806 1.2602 0.0522  0.1413  -0.0856 401 LEU   A CD1 
2688 C  CD2 . LEU   A 381 ? 1.2578 1.5587 1.2390 0.0789  0.1785  -0.0645 401 LEU   A CD2 
2689 N  N   . HIS   A 382 ? 1.1936 1.4813 1.0943 0.0706  0.0934  -0.1760 402 HIS   A N   
2690 C  CA  . HIS   A 382 ? 1.2876 1.5613 1.1720 0.0733  0.0901  -0.2057 402 HIS   A CA  
2691 C  C   . HIS   A 382 ? 1.3942 1.6688 1.2082 0.0873  0.0880  -0.2210 402 HIS   A C   
2692 O  O   . HIS   A 382 ? 1.4188 1.6792 1.2101 0.0949  0.0930  -0.2455 402 HIS   A O   
2693 C  CB  . HIS   A 382 ? 1.1537 1.4148 1.0632 0.0552  0.0619  -0.2232 402 HIS   A CB  
2694 C  CG  . HIS   A 382 ? 1.1495 1.4016 1.1163 0.0466  0.0625  -0.2145 402 HIS   A CG  
2695 N  ND1 . HIS   A 382 ? 1.1464 1.3791 1.1329 0.0336  0.0434  -0.2261 402 HIS   A ND1 
2696 C  CD2 . HIS   A 382 ? 1.1602 1.4186 1.1676 0.0500  0.0787  -0.1961 402 HIS   A CD2 
2697 C  CE1 . HIS   A 382 ? 1.1689 1.3956 1.1980 0.0325  0.0455  -0.2150 402 HIS   A CE1 
2698 N  NE2 . HIS   A 382 ? 1.1819 1.4264 1.2285 0.0414  0.0649  -0.1988 402 HIS   A NE2 
2699 N  N   . ARG   A 383 ? 1.4853 1.7744 1.2618 0.0932  0.0790  -0.2086 403 ARG   A N   
2700 C  CA  . ARG   A 383 ? 1.5577 1.8488 1.2606 0.1096  0.0708  -0.2235 403 ARG   A CA  
2701 C  C   . ARG   A 383 ? 1.6597 1.9545 1.3145 0.1324  0.0971  -0.1957 403 ARG   A C   
2702 O  O   . ARG   A 383 ? 1.7331 2.0312 1.3188 0.1497  0.0864  -0.2005 403 ARG   A O   
2703 C  CB  . ARG   A 383 ? 1.4388 1.7444 1.1337 0.0994  0.0294  -0.2386 403 ARG   A CB  
2704 C  CG  . ARG   A 383 ? 1.3507 1.6469 1.0824 0.0771  0.0068  -0.2686 403 ARG   A CG  
2705 C  CD  . ARG   A 383 ? 1.4237 1.7406 1.1686 0.0625  -0.0289 -0.2782 403 ARG   A CD  
2706 N  NE  . ARG   A 383 ? 1.3624 1.6665 1.1464 0.0385  -0.0450 -0.3033 403 ARG   A NE  
2707 C  CZ  . ARG   A 383 ? 1.3194 1.6216 1.0901 0.0306  -0.0687 -0.3384 403 ARG   A CZ  
2708 N  NH1 . ARG   A 383 ? 1.4086 1.7240 1.1252 0.0462  -0.0846 -0.3562 403 ARG   A NH1 
2709 N  NH2 . ARG   A 383 ? 1.3193 1.6032 1.1305 0.0069  -0.0772 -0.3566 403 ARG   A NH2 
2710 N  N   . ASP   A 384 ? 1.6797 1.9725 1.3697 0.1330  0.1306  -0.1668 404 ASP   A N   
2711 C  CA  . ASP   A 384 ? 1.8141 2.1040 1.4635 0.1527  0.1633  -0.1363 404 ASP   A CA  
2712 C  C   . ASP   A 384 ? 1.8907 2.1680 1.4818 0.1739  0.1919  -0.1478 404 ASP   A C   
2713 O  O   . ASP   A 384 ? 1.9242 2.1963 1.5503 0.1711  0.2144  -0.1593 404 ASP   A O   
2714 C  CB  . ASP   A 384 ? 1.8033 2.0938 1.5199 0.1428  0.1923  -0.1058 404 ASP   A CB  
2715 C  CG  . ASP   A 384 ? 1.9622 2.2447 1.6436 0.1598  0.2295  -0.0701 404 ASP   A CG  
2716 O  OD1 . ASP   A 384 ? 2.0628 2.3386 1.6601 0.1817  0.2296  -0.0657 404 ASP   A OD1 
2717 O  OD2 . ASP   A 384 ? 1.9676 2.2484 1.7053 0.1513  0.2583  -0.0467 404 ASP   A OD2 
2718 N  N   . PRO   A 385 ? 2.0298 2.3012 1.5301 0.1979  0.1916  -0.1462 405 PRO   A N   
2719 C  CA  . PRO   A 385 ? 2.1067 2.3624 1.5410 0.2213  0.2219  -0.1576 405 PRO   A CA  
2720 C  C   . PRO   A 385 ? 2.2368 2.4847 1.6864 0.2297  0.2829  -0.1270 405 PRO   A C   
2721 O  O   . PRO   A 385 ? 2.2803 2.5164 1.6874 0.2480  0.3158  -0.1365 405 PRO   A O   
2722 C  CB  . PRO   A 385 ? 2.0108 2.2619 1.3396 0.2465  0.2013  -0.1590 405 PRO   A CB  
2723 C  CG  . PRO   A 385 ? 2.1620 2.4325 1.5166 0.2313  0.1479  -0.1654 405 PRO   A CG  
2724 C  CD  . PRO   A 385 ? 2.0333 2.3129 1.4839 0.2067  0.1571  -0.1403 405 PRO   A CD  
2725 N  N   . LYS   A 386 ? 2.4113 2.6650 1.9216 0.2171  0.3007  -0.0922 406 LYS   A N   
2726 C  CA  . LYS   A 386 ? 2.5083 2.7581 2.0547 0.2191  0.3592  -0.0655 406 LYS   A CA  
2727 C  C   . LYS   A 386 ? 2.5393 2.8021 2.1829 0.2014  0.3699  -0.0829 406 LYS   A C   
2728 O  O   . LYS   A 386 ? 2.5188 2.7873 2.2226 0.1964  0.4123  -0.0630 406 LYS   A O   
2729 C  CB  . LYS   A 386 ? 2.5508 2.7980 2.1255 0.2120  0.3736  -0.0227 406 LYS   A CB  
2730 C  CG  . LYS   A 386 ? 2.6991 2.9284 2.1750 0.2359  0.3745  0.0028  406 LYS   A CG  
2731 C  CD  . LYS   A 386 ? 2.7504 2.9624 2.2346 0.2397  0.4266  0.0502  406 LYS   A CD  
2732 C  CE  . LYS   A 386 ? 2.8522 3.0393 2.2239 0.2698  0.4303  0.0778  406 LYS   A CE  
2733 N  NZ  . LYS   A 386 ? 2.8152 2.9762 2.1856 0.2754  0.4876  0.1270  406 LYS   A NZ  
2734 N  N   . TYR   A 387 ? 2.1542 2.4213 1.8164 0.1924  0.3320  -0.1192 407 TYR   A N   
2735 C  CA  . TYR   A 387 ? 2.0450 2.3200 1.7859 0.1819  0.3369  -0.1393 407 TYR   A CA  
2736 C  C   . TYR   A 387 ? 1.9311 2.1949 1.6353 0.1899  0.3161  -0.1806 407 TYR   A C   
2737 O  O   . TYR   A 387 ? 1.9420 2.2046 1.6720 0.1973  0.3387  -0.1973 407 TYR   A O   
2738 C  CB  . TYR   A 387 ? 1.8761 2.1623 1.7043 0.1558  0.3064  -0.1358 407 TYR   A CB  
2739 C  CG  . TYR   A 387 ? 1.9389 2.2368 1.8383 0.1455  0.3337  -0.1049 407 TYR   A CG  
2740 C  CD1 . TYR   A 387 ? 1.7814 2.0926 1.7593 0.1426  0.3625  -0.1065 407 TYR   A CD1 
2741 C  CD2 . TYR   A 387 ? 2.0266 2.3224 1.9201 0.1388  0.3291  -0.0764 407 TYR   A CD2 
2742 C  CE1 . TYR   A 387 ? 1.7734 2.0969 1.8249 0.1305  0.3851  -0.0821 407 TYR   A CE1 
2743 C  CE2 . TYR   A 387 ? 1.9810 2.2832 1.9425 0.1275  0.3533  -0.0508 407 TYR   A CE2 
2744 C  CZ  . TYR   A 387 ? 1.8679 2.1844 1.9098 0.1220  0.3808  -0.0547 407 TYR   A CZ  
2745 O  OH  . TYR   A 387 ? 1.9446 2.2692 2.0623 0.1083  0.4029  -0.0330 407 TYR   A OH  
2746 N  N   . TRP   A 388 ? 1.9613 2.2171 1.6099 0.1886  0.2738  -0.1987 408 TRP   A N   
2747 C  CA  . TRP   A 388 ? 1.9524 2.1940 1.5735 0.1908  0.2478  -0.2405 408 TRP   A CA  
2748 C  C   . TRP   A 388 ? 2.0933 2.3219 1.6068 0.2148  0.2488  -0.2559 408 TRP   A C   
2749 O  O   . TRP   A 388 ? 2.1565 2.3888 1.6134 0.2225  0.2384  -0.2401 408 TRP   A O   
2750 C  CB  . TRP   A 388 ? 1.7967 2.0393 1.4478 0.1671  0.1961  -0.2548 408 TRP   A CB  
2751 C  CG  . TRP   A 388 ? 1.6871 1.9399 1.4278 0.1458  0.1902  -0.2372 408 TRP   A CG  
2752 C  CD1 . TRP   A 388 ? 1.6357 1.9024 1.4039 0.1334  0.1807  -0.2096 408 TRP   A CD1 
2753 C  CD2 . TRP   A 388 ? 1.5534 1.8009 1.3633 0.1374  0.1916  -0.2473 408 TRP   A CD2 
2754 N  NE1 . TRP   A 388 ? 1.4682 1.7380 1.3149 0.1172  0.1757  -0.2037 408 TRP   A NE1 
2755 C  CE2 . TRP   A 388 ? 1.4653 1.7243 1.3381 0.1200  0.1809  -0.2257 408 TRP   A CE2 
2756 C  CE3 . TRP   A 388 ? 1.5561 1.7884 1.3783 0.1455  0.1997  -0.2731 408 TRP   A CE3 
2757 C  CZ2 . TRP   A 388 ? 1.3350 1.5913 1.2777 0.1113  0.1756  -0.2291 408 TRP   A CZ2 
2758 C  CZ3 . TRP   A 388 ? 1.4793 1.7095 1.3752 0.1374  0.1950  -0.2746 408 TRP   A CZ3 
2759 C  CH2 . TRP   A 388 ? 1.2500 1.4925 1.2033 0.1209  0.1819  -0.2527 408 TRP   A CH2 
2760 N  N   . THR   A 389 ? 2.0905 2.3021 1.5734 0.2289  0.2592  -0.2880 409 THR   A N   
2761 C  CA  . THR   A 389 ? 2.1493 2.3442 1.5253 0.2522  0.2530  -0.3121 409 THR   A CA  
2762 C  C   . THR   A 389 ? 2.1152 2.3045 1.4750 0.2384  0.1938  -0.3475 409 THR   A C   
2763 O  O   . THR   A 389 ? 2.0935 2.2762 1.5129 0.2183  0.1725  -0.3692 409 THR   A O   
2764 C  CB  . THR   A 389 ? 2.1995 2.3759 1.5485 0.2744  0.2904  -0.3350 409 THR   A CB  
2765 O  OG1 . THR   A 389 ? 2.2647 2.4279 1.6605 0.2621  0.2683  -0.3713 409 THR   A OG1 
2766 C  CG2 . THR   A 389 ? 2.2227 2.4111 1.6198 0.2818  0.3506  -0.3025 409 THR   A CG2 
2767 N  N   . GLU   A 390 ? 2.1492 2.3407 1.4304 0.2496  0.1675  -0.3529 410 GLU   A N   
2768 C  CA  . GLU   A 390 ? 2.0627 2.2561 1.3314 0.2363  0.1100  -0.3868 410 GLU   A CA  
2769 C  C   . GLU   A 390 ? 2.0065 2.2133 1.3753 0.2005  0.0840  -0.3817 410 GLU   A C   
2770 O  O   . GLU   A 390 ? 1.9544 2.1481 1.3576 0.1826  0.0612  -0.4140 410 GLU   A O   
2771 C  CB  . GLU   A 390 ? 2.1887 2.3549 1.4129 0.2449  0.0982  -0.4388 410 GLU   A CB  
2772 C  CG  . GLU   A 390 ? 2.3247 2.4766 1.4302 0.2814  0.1087  -0.4528 410 GLU   A CG  
2773 C  CD  . GLU   A 390 ? 2.3533 2.4738 1.4163 0.2905  0.0989  -0.5078 410 GLU   A CD  
2774 O  OE1 . GLU   A 390 ? 2.3079 2.4105 1.4228 0.2833  0.1202  -0.5206 410 GLU   A OE1 
2775 O  OE2 . GLU   A 390 ? 2.4493 2.5611 1.4289 0.3053  0.0678  -0.5385 410 GLU   A OE2 
2776 N  N   . PRO   A 391 ? 1.9608 2.1893 1.3731 0.1906  0.0883  -0.3419 411 PRO   A N   
2777 C  CA  . PRO   A 391 ? 1.8423 2.0785 1.3493 0.1605  0.0767  -0.3327 411 PRO   A CA  
2778 C  C   . PRO   A 391 ? 1.8269 2.0676 1.3573 0.1374  0.0294  -0.3591 411 PRO   A C   
2779 O  O   . PRO   A 391 ? 1.8086 2.0459 1.4085 0.1137  0.0221  -0.3579 411 PRO   A O   
2780 C  CB  . PRO   A 391 ? 1.8276 2.0840 1.3586 0.1601  0.0913  -0.2866 411 PRO   A CB  
2781 C  CG  . PRO   A 391 ? 1.9334 2.1961 1.3804 0.1844  0.0897  -0.2769 411 PRO   A CG  
2782 C  CD  . PRO   A 391 ? 1.9961 2.2385 1.3688 0.2076  0.1037  -0.3036 411 PRO   A CD  
2783 N  N   . GLU   A 392 ? 1.9110 2.1592 1.3873 0.1438  -0.0026 -0.3831 412 GLU   A N   
2784 C  CA  . GLU   A 392 ? 1.8822 2.1370 1.3902 0.1194  -0.0455 -0.4124 412 GLU   A CA  
2785 C  C   . GLU   A 392 ? 1.8525 2.0752 1.3661 0.1094  -0.0526 -0.4553 412 GLU   A C   
2786 O  O   . GLU   A 392 ? 1.7611 1.9823 1.3161 0.0837  -0.0813 -0.4782 412 GLU   A O   
2787 C  CB  . GLU   A 392 ? 1.8946 2.1754 1.3531 0.1294  -0.0824 -0.4248 412 GLU   A CB  
2788 C  CG  . GLU   A 392 ? 1.9462 2.2596 1.4183 0.1325  -0.0871 -0.3860 412 GLU   A CG  
2789 C  CD  . GLU   A 392 ? 2.0533 2.3625 1.4745 0.1614  -0.0511 -0.3477 412 GLU   A CD  
2790 O  OE1 . GLU   A 392 ? 2.1380 2.4282 1.4864 0.1861  -0.0337 -0.3568 412 GLU   A OE1 
2791 O  OE2 . GLU   A 392 ? 1.9229 2.2450 1.3763 0.1592  -0.0381 -0.3086 412 GLU   A OE2 
2792 N  N   . LYS   A 393 ? 1.9407 2.1362 1.4167 0.1289  -0.0248 -0.4663 413 LYS   A N   
2793 C  CA  . LYS   A 393 ? 1.8906 2.0502 1.3645 0.1239  -0.0305 -0.5090 413 LYS   A CA  
2794 C  C   . LYS   A 393 ? 1.8309 1.9678 1.3776 0.1082  -0.0115 -0.4994 413 LYS   A C   
2795 O  O   . LYS   A 393 ? 1.8106 1.9557 1.3896 0.1133  0.0176  -0.4640 413 LYS   A O   
2796 C  CB  . LYS   A 393 ? 1.8938 2.0331 1.2860 0.1567  -0.0099 -0.5294 413 LYS   A CB  
2797 C  CG  . LYS   A 393 ? 2.0017 2.1604 1.3071 0.1806  -0.0225 -0.5304 413 LYS   A CG  
2798 C  CD  . LYS   A 393 ? 2.0067 2.1373 1.2218 0.2099  -0.0140 -0.5661 413 LYS   A CD  
2799 C  CE  . LYS   A 393 ? 2.0896 2.1995 1.2957 0.1967  -0.0567 -0.6244 413 LYS   A CE  
2800 N  NZ  . LYS   A 393 ? 2.0116 2.0920 1.1242 0.2246  -0.0536 -0.6539 413 LYS   A NZ  
2801 N  N   . PHE   A 394 ? 1.7821 1.8887 1.3546 0.0896  -0.0296 -0.5319 414 PHE   A N   
2802 C  CA  . PHE   A 394 ? 1.7232 1.7995 1.3557 0.0774  -0.0160 -0.5262 414 PHE   A CA  
2803 C  C   . PHE   A 394 ? 1.8210 1.8660 1.4284 0.1027  0.0123  -0.5421 414 PHE   A C   
2804 O  O   . PHE   A 394 ? 1.8642 1.8770 1.4377 0.1077  0.0042  -0.5830 414 PHE   A O   
2805 C  CB  . PHE   A 394 ? 1.6566 1.7090 1.3256 0.0464  -0.0448 -0.5510 414 PHE   A CB  
2806 C  CG  . PHE   A 394 ? 1.6832 1.6920 1.3991 0.0376  -0.0326 -0.5490 414 PHE   A CG  
2807 C  CD1 . PHE   A 394 ? 1.6571 1.6712 1.4253 0.0283  -0.0231 -0.5117 414 PHE   A CD1 
2808 C  CD2 . PHE   A 394 ? 1.7393 1.6981 1.4430 0.0407  -0.0324 -0.5856 414 PHE   A CD2 
2809 C  CE1 . PHE   A 394 ? 1.6243 1.5954 1.4280 0.0242  -0.0147 -0.5088 414 PHE   A CE1 
2810 C  CE2 . PHE   A 394 ? 1.6416 1.5555 1.3847 0.0360  -0.0221 -0.5819 414 PHE   A CE2 
2811 C  CZ  . PHE   A 394 ? 1.6575 1.5779 1.4489 0.0286  -0.0139 -0.5426 414 PHE   A CZ  
2812 N  N   . LEU   A 395 ? 1.7618 1.8172 1.3901 0.1188  0.0460  -0.5115 415 LEU   A N   
2813 C  CA  . LEU   A 395 ? 1.7670 1.8030 1.3797 0.1461  0.0788  -0.5221 415 LEU   A CA  
2814 C  C   . LEU   A 395 ? 1.7470 1.7764 1.4319 0.1456  0.0964  -0.5003 415 LEU   A C   
2815 O  O   . LEU   A 395 ? 1.6921 1.7519 1.4077 0.1524  0.1184  -0.4665 415 LEU   A O   
2816 C  CB  . LEU   A 395 ? 1.7570 1.8195 1.3160 0.1730  0.1079  -0.5087 415 LEU   A CB  
2817 C  CG  . LEU   A 395 ? 1.8886 1.9486 1.3565 0.1862  0.0950  -0.5364 415 LEU   A CG  
2818 C  CD1 . LEU   A 395 ? 2.0292 2.1123 1.4433 0.2139  0.1295  -0.5125 415 LEU   A CD1 
2819 C  CD2 . LEU   A 395 ? 1.9323 1.9485 1.3653 0.1962  0.0903  -0.5863 415 LEU   A CD2 
2820 N  N   . PRO   A 396 ? 1.7925 1.7807 1.5065 0.1381  0.0858  -0.5191 416 PRO   A N   
2821 C  CA  . PRO   A 396 ? 1.7677 1.7470 1.5452 0.1428  0.0984  -0.5000 416 PRO   A CA  
2822 C  C   . PRO   A 396 ? 1.6756 1.6677 1.4631 0.1739  0.1355  -0.4959 416 PRO   A C   
2823 O  O   . PRO   A 396 ? 1.6341 1.6383 1.4812 0.1793  0.1459  -0.4737 416 PRO   A O   
2824 C  CB  . PRO   A 396 ? 1.7349 1.6572 1.5225 0.1333  0.0803  -0.5262 416 PRO   A CB  
2825 C  CG  . PRO   A 396 ? 1.7091 1.6226 1.4632 0.1090  0.0522  -0.5473 416 PRO   A CG  
2826 C  CD  . PRO   A 396 ? 1.7452 1.6929 1.4413 0.1215  0.0577  -0.5556 416 PRO   A CD  
2827 N  N   . GLU   A 397 ? 1.6560 1.6472 1.3884 0.1955  0.1561  -0.5176 417 GLU   A N   
2828 C  CA  . GLU   A 397 ? 1.7278 1.7350 1.4730 0.2252  0.1980  -0.5127 417 GLU   A CA  
2829 C  C   . GLU   A 397 ? 1.6965 1.7557 1.4738 0.2256  0.2209  -0.4720 417 GLU   A C   
2830 O  O   . GLU   A 397 ? 1.6855 1.7645 1.4903 0.2467  0.2585  -0.4638 417 GLU   A O   
2831 C  CB  . GLU   A 397 ? 1.7925 1.7841 1.4604 0.2493  0.2179  -0.5449 417 GLU   A CB  
2832 C  CG  . GLU   A 397 ? 1.8124 1.7494 1.4640 0.2586  0.2088  -0.5883 417 GLU   A CG  
2833 C  CD  . GLU   A 397 ? 1.9696 1.8955 1.6854 0.2779  0.2299  -0.5879 417 GLU   A CD  
2834 O  OE1 . GLU   A 397 ? 1.9846 1.9501 1.7428 0.2931  0.2625  -0.5633 417 GLU   A OE1 
2835 O  OE2 . GLU   A 397 ? 2.0217 1.8988 1.7490 0.2783  0.2136  -0.6124 417 GLU   A OE2 
2836 N  N   . ARG   A 398 ? 1.6870 1.7680 1.4655 0.2030  0.2009  -0.4473 418 ARG   A N   
2837 C  CA  . ARG   A 398 ? 1.5860 1.7094 1.4066 0.2003  0.2196  -0.4084 418 ARG   A CA  
2838 C  C   . ARG   A 398 ? 1.5826 1.7147 1.4924 0.2011  0.2243  -0.3955 418 ARG   A C   
2839 O  O   . ARG   A 398 ? 1.5347 1.7004 1.4904 0.2086  0.2526  -0.3740 418 ARG   A O   
2840 C  CB  . ARG   A 398 ? 1.6277 1.7665 1.4390 0.1760  0.1925  -0.3870 418 ARG   A CB  
2841 C  CG  . ARG   A 398 ? 1.7173 1.8573 1.4465 0.1769  0.1838  -0.3948 418 ARG   A CG  
2842 C  CD  . ARG   A 398 ? 1.5990 1.7595 1.3348 0.1554  0.1587  -0.3706 418 ARG   A CD  
2843 N  NE  . ARG   A 398 ? 1.6964 1.8528 1.3678 0.1509  0.1313  -0.3880 418 ARG   A NE  
2844 C  CZ  . ARG   A 398 ? 1.8383 2.0063 1.4416 0.1664  0.1392  -0.3848 418 ARG   A CZ  
2845 N  NH1 . ARG   A 398 ? 1.9195 2.1000 1.5058 0.1863  0.1793  -0.3622 418 ARG   A NH1 
2846 N  NH2 . ARG   A 398 ? 1.8801 2.0468 1.4316 0.1624  0.1064  -0.4046 418 ARG   A NH2 
2847 N  N   . PHE   A 399 ? 1.5451 1.6465 1.4812 0.1939  0.1964  -0.4084 419 PHE   A N   
2848 C  CA  . PHE   A 399 ? 1.5521 1.6580 1.5659 0.1954  0.1904  -0.3959 419 PHE   A CA  
2849 C  C   . PHE   A 399 ? 1.5298 1.6142 1.5683 0.2207  0.2026  -0.4184 419 PHE   A C   
2850 O  O   . PHE   A 399 ? 1.6356 1.7075 1.7252 0.2244  0.1865  -0.4158 419 PHE   A O   
2851 C  CB  . PHE   A 399 ? 1.4914 1.5758 1.5154 0.1717  0.1510  -0.3875 419 PHE   A CB  
2852 C  CG  . PHE   A 399 ? 1.4217 1.5303 1.4323 0.1491  0.1393  -0.3646 419 PHE   A CG  
2853 C  CD1 . PHE   A 399 ? 1.4208 1.5632 1.4795 0.1437  0.1422  -0.3362 419 PHE   A CD1 
2854 C  CD2 . PHE   A 399 ? 1.5488 1.6468 1.5020 0.1342  0.1242  -0.3737 419 PHE   A CD2 
2855 C  CE1 . PHE   A 399 ? 1.5236 1.6847 1.5696 0.1252  0.1325  -0.3158 419 PHE   A CE1 
2856 C  CE2 . PHE   A 399 ? 1.5056 1.6278 1.4499 0.1167  0.1133  -0.3530 419 PHE   A CE2 
2857 C  CZ  . PHE   A 399 ? 1.4279 1.5795 1.4165 0.1129  0.1186  -0.3233 419 PHE   A CZ  
2858 N  N   . SER   A 400 ? 1.7006 1.7784 1.6999 0.2409  0.2302  -0.4407 420 SER   A N   
2859 C  CA  . SER   A 400 ? 1.8904 1.9550 1.9195 0.2695  0.2490  -0.4609 420 SER   A CA  
2860 C  C   . SER   A 400 ? 1.9585 2.0741 2.0685 0.2833  0.2769  -0.4413 420 SER   A C   
2861 O  O   . SER   A 400 ? 1.8143 1.9723 1.9367 0.2751  0.2964  -0.4177 420 SER   A O   
2862 C  CB  . SER   A 400 ? 1.9719 2.0154 1.9317 0.2887  0.2735  -0.4918 420 SER   A CB  
2863 O  OG  . SER   A 400 ? 2.0355 2.1146 1.9608 0.2928  0.3062  -0.4799 420 SER   A OG  
2864 N  N   . LYS   A 401 ? 1.8867 1.9975 2.0563 0.3049  0.2783  -0.4516 421 LYS   A N   
2865 C  CA  . LYS   A 401 ? 1.9137 2.0775 2.1746 0.3185  0.3015  -0.4375 421 LYS   A CA  
2866 C  C   . LYS   A 401 ? 1.8702 2.0699 2.1274 0.3336  0.3571  -0.4384 421 LYS   A C   
2867 O  O   . LYS   A 401 ? 1.8041 2.0555 2.1397 0.3385  0.3830  -0.4231 421 LYS   A O   
2868 C  CB  . LYS   A 401 ? 1.9317 2.0825 2.2552 0.3432  0.2886  -0.4517 421 LYS   A CB  
2869 C  CG  . LYS   A 401 ? 1.9833 2.1590 2.3873 0.3365  0.2577  -0.4313 421 LYS   A CG  
2870 C  CD  . LYS   A 401 ? 2.0857 2.2109 2.4930 0.3472  0.2171  -0.4405 421 LYS   A CD  
2871 C  CE  . LYS   A 401 ? 2.0829 2.1948 2.5205 0.3857  0.2318  -0.4652 421 LYS   A CE  
2872 N  NZ  . LYS   A 401 ? 2.1488 2.2103 2.5950 0.3997  0.1919  -0.4692 421 LYS   A NZ  
2873 N  N   . LYS   A 402 ? 2.1344 2.3073 2.3025 0.3413  0.3765  -0.4565 422 LYS   A N   
2874 C  CA  . LYS   A 402 ? 2.1282 2.3287 2.2685 0.3535  0.4301  -0.4522 422 LYS   A CA  
2875 C  C   . LYS   A 402 ? 2.1381 2.3615 2.2476 0.3291  0.4342  -0.4212 422 LYS   A C   
2876 O  O   . LYS   A 402 ? 2.1706 2.4280 2.2890 0.3349  0.4808  -0.4037 422 LYS   A O   
2877 C  CB  . LYS   A 402 ? 2.2449 2.4027 2.2904 0.3743  0.4454  -0.4859 422 LYS   A CB  
2878 C  CG  . LYS   A 402 ? 2.3876 2.5616 2.3729 0.3887  0.4986  -0.4823 422 LYS   A CG  
2879 C  CD  . LYS   A 402 ? 2.5359 2.6609 2.4135 0.4081  0.5029  -0.5197 422 LYS   A CD  
2880 C  CE  . LYS   A 402 ? 2.6153 2.7461 2.3994 0.4155  0.5385  -0.5113 422 LYS   A CE  
2881 N  NZ  . LYS   A 402 ? 2.5724 2.7126 2.3243 0.3858  0.5102  -0.4828 422 LYS   A NZ  
2882 N  N   . ASN   A 403 ? 2.1021 2.3067 2.1792 0.3027  0.3889  -0.4126 423 ASN   A N   
2883 C  CA  . ASN   A 403 ? 1.9625 2.1842 2.0071 0.2816  0.3881  -0.3844 423 ASN   A CA  
2884 C  C   . ASN   A 403 ? 1.9302 2.1686 2.0341 0.2550  0.3539  -0.3596 423 ASN   A C   
2885 O  O   . ASN   A 403 ? 1.9129 2.1668 2.0001 0.2385  0.3548  -0.3344 423 ASN   A O   
2886 C  CB  . ASN   A 403 ? 1.8362 2.0231 1.7697 0.2764  0.3682  -0.3983 423 ASN   A CB  
2887 C  CG  . ASN   A 403 ? 2.0859 2.2583 1.9420 0.3030  0.4045  -0.4194 423 ASN   A CG  
2888 O  OD1 . ASN   A 403 ? 2.1960 2.3909 2.0720 0.3228  0.4548  -0.4129 423 ASN   A OD1 
2889 N  ND2 . ASN   A 403 ? 2.0057 2.1407 1.7738 0.3038  0.3798  -0.4462 423 ASN   A ND2 
2890 N  N   . LYS   A 404 ? 1.7859 2.0183 1.9534 0.2526  0.3240  -0.3655 424 LYS   A N   
2891 C  CA  . LYS   A 404 ? 1.7675 2.0101 1.9793 0.2295  0.2894  -0.3444 424 LYS   A CA  
2892 C  C   . LYS   A 404 ? 1.7929 2.0847 2.0823 0.2239  0.3108  -0.3191 424 LYS   A C   
2893 O  O   . LYS   A 404 ? 1.7923 2.0935 2.1164 0.2051  0.2840  -0.3022 424 LYS   A O   
2894 C  CB  . LYS   A 404 ? 1.7712 1.9885 2.0199 0.2323  0.2517  -0.3569 424 LYS   A CB  
2895 C  CG  . LYS   A 404 ? 1.8203 2.0605 2.1559 0.2547  0.2637  -0.3636 424 LYS   A CG  
2896 C  CD  . LYS   A 404 ? 1.8607 2.0881 2.2440 0.2529  0.2202  -0.3614 424 LYS   A CD  
2897 C  CE  . LYS   A 404 ? 1.9046 2.0699 2.2272 0.2512  0.1883  -0.3755 424 LYS   A CE  
2898 N  NZ  . LYS   A 404 ? 1.8018 1.9489 2.1597 0.2515  0.1486  -0.3690 424 LYS   A NZ  
2899 N  N   . ASP   A 405 ? 1.8064 2.1279 2.1253 0.2391  0.3596  -0.3171 425 ASP   A N   
2900 C  CA  . ASP   A 405 ? 1.7644 2.1321 2.1612 0.2307  0.3857  -0.2934 425 ASP   A CA  
2901 C  C   . ASP   A 405 ? 1.7550 2.1266 2.1000 0.2165  0.4087  -0.2673 425 ASP   A C   
2902 O  O   . ASP   A 405 ? 1.6638 2.0617 2.0643 0.2004  0.4160  -0.2440 425 ASP   A O   
2903 C  CB  . ASP   A 405 ? 1.8140 2.2150 2.2796 0.2529  0.4325  -0.3020 425 ASP   A CB  
2904 C  CG  . ASP   A 405 ? 1.8822 2.2597 2.3293 0.2800  0.4309  -0.3338 425 ASP   A CG  
2905 O  OD1 . ASP   A 405 ? 1.8463 2.2037 2.3121 0.2828  0.3868  -0.3480 425 ASP   A OD1 
2906 O  OD2 . ASP   A 405 ? 1.8587 2.2336 2.2673 0.2998  0.4749  -0.3441 425 ASP   A OD2 
2907 N  N   . ASN   A 406 ? 2.0148 2.3586 2.2546 0.2232  0.4182  -0.2715 426 ASN   A N   
2908 C  CA  . ASN   A 406 ? 1.9810 2.3231 2.1586 0.2145  0.4355  -0.2464 426 ASN   A CA  
2909 C  C   . ASN   A 406 ? 1.9509 2.2779 2.0980 0.1922  0.3874  -0.2359 426 ASN   A C   
2910 O  O   . ASN   A 406 ? 2.0518 2.3629 2.1156 0.1907  0.3836  -0.2281 426 ASN   A O   
2911 C  CB  . ASN   A 406 ? 2.0713 2.3909 2.1448 0.2356  0.4628  -0.2579 426 ASN   A CB  
2912 C  CG  . ASN   A 406 ? 2.1941 2.5161 2.2844 0.2612  0.4956  -0.2825 426 ASN   A CG  
2913 O  OD1 . ASN   A 406 ? 2.2018 2.5554 2.3856 0.2659  0.5238  -0.2788 426 ASN   A OD1 
2914 N  ND2 . ASN   A 406 ? 2.2693 2.5586 2.2730 0.2785  0.4910  -0.3100 426 ASN   A ND2 
2915 N  N   . ILE   A 407 ? 1.6654 1.9972 1.8766 0.1770  0.3498  -0.2363 427 ILE   A N   
2916 C  CA  . ILE   A 407 ? 1.6083 1.9257 1.7953 0.1571  0.3058  -0.2283 427 ILE   A CA  
2917 C  C   . ILE   A 407 ? 1.4806 1.8200 1.7508 0.1409  0.2953  -0.2100 427 ILE   A C   
2918 O  O   . ILE   A 407 ? 1.4614 1.8125 1.8058 0.1427  0.2841  -0.2193 427 ILE   A O   
2919 C  CB  . ILE   A 407 ? 1.6017 1.8885 1.7612 0.1560  0.2635  -0.2532 427 ILE   A CB  
2920 C  CG1 . ILE   A 407 ? 1.6389 1.9009 1.7083 0.1669  0.2672  -0.2727 427 ILE   A CG1 
2921 C  CG2 . ILE   A 407 ? 1.1025 1.3801 1.2609 0.1346  0.2223  -0.2433 427 ILE   A CG2 
2922 C  CD1 . ILE   A 407 ? 1.5892 1.8174 1.6322 0.1620  0.2285  -0.2972 427 ILE   A CD1 
2923 N  N   . ASP   A 408 ? 1.2841 1.6274 1.5408 0.1270  0.2966  -0.1856 428 ASP   A N   
2924 C  CA  . ASP   A 408 ? 1.1544 1.5149 1.4855 0.1110  0.2876  -0.1698 428 ASP   A CA  
2925 C  C   . ASP   A 408 ? 1.1812 1.5261 1.5147 0.0996  0.2355  -0.1775 428 ASP   A C   
2926 O  O   . ASP   A 408 ? 1.1527 1.4770 1.4210 0.0941  0.2138  -0.1768 428 ASP   A O   
2927 C  CB  . ASP   A 408 ? 1.2552 1.6190 1.5676 0.1023  0.3112  -0.1405 428 ASP   A CB  
2928 C  CG  . ASP   A 408 ? 1.1775 1.5619 1.5807 0.0879  0.3189  -0.1258 428 ASP   A CG  
2929 O  OD1 . ASP   A 408 ? 1.0879 1.4780 1.5481 0.0798  0.2847  -0.1368 428 ASP   A OD1 
2930 O  OD2 . ASP   A 408 ? 1.2026 1.5945 1.6176 0.0850  0.3589  -0.1035 428 ASP   A OD2 
2931 N  N   . PRO   A 409 ? 1.3109 1.6651 1.7169 0.0973  0.2144  -0.1855 429 PRO   A N   
2932 C  CA  . PRO   A 409 ? 1.1450 1.4778 1.5404 0.0902  0.1676  -0.1924 429 PRO   A CA  
2933 C  C   . PRO   A 409 ? 0.9601 1.2900 1.3503 0.0730  0.1514  -0.1750 429 PRO   A C   
2934 O  O   . PRO   A 409 ? 0.9177 1.2311 1.3014 0.0666  0.1165  -0.1779 429 PRO   A O   
2935 C  CB  . PRO   A 409 ? 1.0452 1.3891 1.5157 0.0990  0.1521  -0.2063 429 PRO   A CB  
2936 C  CG  . PRO   A 409 ? 1.0908 1.4726 1.6350 0.1008  0.1866  -0.2009 429 PRO   A CG  
2937 C  CD  . PRO   A 409 ? 1.1799 1.5630 1.6747 0.1053  0.2311  -0.1926 429 PRO   A CD  
2938 N  N   . TYR   A 410 ? 1.0315 1.3742 1.4221 0.0669  0.1790  -0.1558 430 TYR   A N   
2939 C  CA  . TYR   A 410 ? 1.1944 1.5303 1.5690 0.0534  0.1680  -0.1384 430 TYR   A CA  
2940 C  C   . TYR   A 410 ? 1.1319 1.4564 1.4258 0.0549  0.1775  -0.1272 430 TYR   A C   
2941 O  O   . TYR   A 410 ? 1.2461 1.5645 1.5201 0.0469  0.1692  -0.1123 430 TYR   A O   
2942 C  CB  . TYR   A 410 ? 1.2019 1.5560 1.6453 0.0447  0.1875  -0.1241 430 TYR   A CB  
2943 C  CG  . TYR   A 410 ? 1.1266 1.4950 1.6534 0.0427  0.1677  -0.1388 430 TYR   A CG  
2944 C  CD1 . TYR   A 410 ? 1.0152 1.3705 1.5472 0.0374  0.1253  -0.1465 430 TYR   A CD1 
2945 C  CD2 . TYR   A 410 ? 1.0799 1.4760 1.6793 0.0482  0.1908  -0.1461 430 TYR   A CD2 
2946 C  CE1 . TYR   A 410 ? 1.2521 1.6192 1.8531 0.0391  0.1019  -0.1616 430 TYR   A CE1 
2947 C  CE2 . TYR   A 410 ? 1.0626 1.4762 1.7424 0.0486  0.1674  -0.1621 430 TYR   A CE2 
2948 C  CZ  . TYR   A 410 ? 1.2091 1.6071 1.8864 0.0449  0.1207  -0.1701 430 TYR   A CZ  
2949 O  OH  . TYR   A 410 ? 1.2357 1.6505 1.9874 0.0487  0.0932  -0.1873 430 TYR   A OH  
2950 N  N   . ILE   A 411 ? 1.2745 1.5960 1.5215 0.0670  0.1930  -0.1359 431 ILE   A N   
2951 C  CA  . ILE   A 411 ? 1.2654 1.5750 1.4307 0.0703  0.1874  -0.1348 431 ILE   A CA  
2952 C  C   . ILE   A 411 ? 1.1036 1.3968 1.2405 0.0678  0.1535  -0.1570 431 ILE   A C   
2953 O  O   . ILE   A 411 ? 1.1531 1.4391 1.2545 0.0603  0.1309  -0.1560 431 ILE   A O   
2954 C  CB  . ILE   A 411 ? 1.3449 1.6573 1.4660 0.0861  0.2238  -0.1324 431 ILE   A CB  
2955 C  CG1 . ILE   A 411 ? 1.3781 1.7014 1.5248 0.0869  0.2626  -0.1053 431 ILE   A CG1 
2956 C  CG2 . ILE   A 411 ? 1.3252 1.6264 1.3598 0.0920  0.2104  -0.1370 431 ILE   A CG2 
2957 C  CD1 . ILE   A 411 ? 1.3932 1.7121 1.5355 0.0768  0.2532  -0.0818 431 ILE   A CD1 
2958 N  N   . TYR   A 412 ? 1.1222 1.4089 1.2788 0.0741  0.1512  -0.1770 432 TYR   A N   
2959 C  CA  . TYR   A 412 ? 1.2075 1.4716 1.3453 0.0709  0.1220  -0.1968 432 TYR   A CA  
2960 C  C   . TYR   A 412 ? 1.1794 1.4366 1.3624 0.0624  0.0974  -0.1940 432 TYR   A C   
2961 O  O   . TYR   A 412 ? 1.0540 1.3143 1.2872 0.0692  0.0973  -0.1988 432 TYR   A O   
2962 C  CB  . TYR   A 412 ? 1.0785 1.3317 1.2094 0.0851  0.1321  -0.2192 432 TYR   A CB  
2963 C  CG  . TYR   A 412 ? 1.1313 1.3535 1.2379 0.0810  0.1054  -0.2390 432 TYR   A CG  
2964 C  CD1 . TYR   A 412 ? 1.2239 1.4346 1.2763 0.0724  0.0921  -0.2471 432 TYR   A CD1 
2965 C  CD2 . TYR   A 412 ? 1.0542 1.2580 1.1947 0.0859  0.0932  -0.2493 432 TYR   A CD2 
2966 C  CE1 . TYR   A 412 ? 1.2620 1.4425 1.2988 0.0651  0.0710  -0.2650 432 TYR   A CE1 
2967 C  CE2 . TYR   A 412 ? 1.1799 1.3479 1.2961 0.0817  0.0726  -0.2644 432 TYR   A CE2 
2968 C  CZ  . TYR   A 412 ? 1.2083 1.3643 1.2750 0.0694  0.0633  -0.2722 432 TYR   A CZ  
2969 O  OH  . TYR   A 412 ? 1.1679 1.2867 1.2174 0.0617  0.0460  -0.2873 432 TYR   A OH  
2970 N  N   . THR   A 413 ? 1.0623 1.3109 1.2266 0.0496  0.0758  -0.1869 433 THR   A N   
2971 C  CA  . THR   A 413 ? 1.0482 1.2869 1.2419 0.0429  0.0531  -0.1826 433 THR   A CA  
2972 C  C   . THR   A 413 ? 1.1722 1.3866 1.3292 0.0332  0.0312  -0.1876 433 THR   A C   
2973 O  O   . THR   A 413 ? 1.1448 1.3602 1.2929 0.0233  0.0215  -0.1768 433 THR   A O   
2974 C  CB  . THR   A 413 ? 1.2723 1.5280 1.4916 0.0367  0.0563  -0.1639 433 THR   A CB  
2975 O  OG1 . THR   A 413 ? 1.0486 1.3114 1.2288 0.0315  0.0628  -0.1527 433 THR   A OG1 
2976 C  CG2 . THR   A 413 ? 1.0098 1.2874 1.2808 0.0429  0.0790  -0.1592 433 THR   A CG2 
2977 N  N   . PRO   A 414 ? 1.2381 1.4287 1.3761 0.0355  0.0253  -0.2039 434 PRO   A N   
2978 C  CA  . PRO   A 414 ? 1.1228 1.2886 1.2312 0.0232  0.0092  -0.2082 434 PRO   A CA  
2979 C  C   . PRO   A 414 ? 1.1632 1.3062 1.2823 0.0205  -0.0074 -0.2005 434 PRO   A C   
2980 O  O   . PRO   A 414 ? 1.1466 1.2717 1.2440 0.0087  -0.0159 -0.1984 434 PRO   A O   
2981 C  CB  . PRO   A 414 ? 1.2508 1.3930 1.3403 0.0272  0.0112  -0.2289 434 PRO   A CB  
2982 C  CG  . PRO   A 414 ? 1.1632 1.3074 1.2823 0.0454  0.0205  -0.2336 434 PRO   A CG  
2983 C  CD  . PRO   A 414 ? 1.1949 1.3775 1.3412 0.0494  0.0349  -0.2196 434 PRO   A CD  
2984 N  N   . PHE   A 415 ? 1.1702 1.3138 1.3223 0.0321  -0.0123 -0.1972 435 PHE   A N   
2985 C  CA  . PHE   A 415 ? 1.1677 1.2878 1.3233 0.0346  -0.0313 -0.1912 435 PHE   A CA  
2986 C  C   . PHE   A 415 ? 1.0531 1.1956 1.2392 0.0357  -0.0367 -0.1812 435 PHE   A C   
2987 O  O   . PHE   A 415 ? 1.0033 1.1304 1.1978 0.0429  -0.0551 -0.1800 435 PHE   A O   
2988 C  CB  . PHE   A 415 ? 1.1629 1.2558 1.3279 0.0510  -0.0412 -0.2007 435 PHE   A CB  
2989 C  CG  . PHE   A 415 ? 1.2225 1.2799 1.3552 0.0493  -0.0382 -0.2104 435 PHE   A CG  
2990 C  CD1 . PHE   A 415 ? 1.3302 1.3460 1.4285 0.0420  -0.0467 -0.2054 435 PHE   A CD1 
2991 C  CD2 . PHE   A 415 ? 1.1839 1.2460 1.3200 0.0551  -0.0248 -0.2251 435 PHE   A CD2 
2992 C  CE1 . PHE   A 415 ? 1.4162 1.3948 1.4900 0.0377  -0.0423 -0.2146 435 PHE   A CE1 
2993 C  CE2 . PHE   A 415 ? 1.3242 1.3489 1.4320 0.0527  -0.0233 -0.2371 435 PHE   A CE2 
2994 C  CZ  . PHE   A 415 ? 1.3933 1.3757 1.4728 0.0426  -0.0323 -0.2317 435 PHE   A CZ  
2995 N  N   . GLY   A 416 ? 1.1198 1.2945 1.3195 0.0299  -0.0218 -0.1746 436 GLY   A N   
2996 C  CA  . GLY   A 416 ? 1.0829 1.2741 1.3175 0.0300  -0.0257 -0.1670 436 GLY   A CA  
2997 C  C   . GLY   A 416 ? 1.0829 1.2900 1.3722 0.0410  -0.0247 -0.1745 436 GLY   A C   
2998 O  O   . GLY   A 416 ? 0.9727 1.1829 1.2719 0.0500  -0.0157 -0.1837 436 GLY   A O   
2999 N  N   . SER   A 417 ? 1.0768 1.2952 1.4064 0.0406  -0.0343 -0.1724 437 SER   A N   
3000 C  CA  . SER   A 417 ? 1.0941 1.3345 1.4905 0.0490  -0.0355 -0.1812 437 SER   A CA  
3001 C  C   . SER   A 417 ? 1.1414 1.3823 1.5711 0.0482  -0.0604 -0.1842 437 SER   A C   
3002 O  O   . SER   A 417 ? 0.9979 1.2262 1.4015 0.0397  -0.0674 -0.1769 437 SER   A O   
3003 C  CB  . SER   A 417 ? 1.1059 1.3787 1.5374 0.0449  -0.0008 -0.1758 437 SER   A CB  
3004 O  OG  . SER   A 417 ? 0.9507 1.2443 1.4384 0.0560  0.0062  -0.1871 437 SER   A OG  
3005 N  N   . GLY   A 418 ? 1.0078 1.2648 1.4981 0.0583  -0.0746 -0.1973 438 GLY   A N   
3006 C  CA  . GLY   A 418 ? 0.6485 0.9107 1.1805 0.0584  -0.1018 -0.2057 438 GLY   A CA  
3007 C  C   . GLY   A 418 ? 0.8829 1.1088 1.3672 0.0707  -0.1404 -0.2119 438 GLY   A C   
3008 O  O   . GLY   A 418 ? 0.6280 0.8246 1.0555 0.0798  -0.1444 -0.2090 438 GLY   A O   
3009 N  N   . PRO   A 419 ? 0.9432 1.1667 1.4469 0.0714  -0.1685 -0.2208 439 PRO   A N   
3010 C  CA  . PRO   A 419 ? 1.0194 1.2051 1.4704 0.0872  -0.2064 -0.2271 439 PRO   A CA  
3011 C  C   . PRO   A 419 ? 1.1111 1.2551 1.4686 0.0847  -0.1979 -0.2118 439 PRO   A C   
3012 O  O   . PRO   A 419 ? 1.0682 1.1748 1.3711 0.1001  -0.2195 -0.2122 439 PRO   A O   
3013 C  CB  . PRO   A 419 ? 1.0668 1.2597 1.5537 0.0842  -0.2323 -0.2402 439 PRO   A CB  
3014 C  CG  . PRO   A 419 ? 0.8524 1.0930 1.4368 0.0706  -0.2141 -0.2458 439 PRO   A CG  
3015 C  CD  . PRO   A 419 ? 0.6443 0.8963 1.2189 0.0587  -0.1671 -0.2270 439 PRO   A CD  
3016 N  N   . ARG   A 420 ? 1.1098 1.2588 1.4479 0.0670  -0.1669 -0.1979 440 ARG   A N   
3017 C  CA  . ARG   A 420 ? 1.1430 1.2608 1.4058 0.0625  -0.1571 -0.1851 440 ARG   A CA  
3018 C  C   . ARG   A 420 ? 1.1264 1.2487 1.3719 0.0551  -0.1292 -0.1764 440 ARG   A C   
3019 O  O   . ARG   A 420 ? 1.1893 1.3109 1.4043 0.0429  -0.1103 -0.1659 440 ARG   A O   
3020 C  CB  . ARG   A 420 ? 1.1422 1.2602 1.3926 0.0508  -0.1502 -0.1787 440 ARG   A CB  
3021 C  CG  . ARG   A 420 ? 1.3260 1.4092 1.5035 0.0513  -0.1494 -0.1700 440 ARG   A CG  
3022 C  CD  . ARG   A 420 ? 1.2486 1.3244 1.4147 0.0489  -0.1547 -0.1705 440 ARG   A CD  
3023 N  NE  . ARG   A 420 ? 0.7948 0.8348 0.8915 0.0539  -0.1552 -0.1643 440 ARG   A NE  
3024 C  CZ  . ARG   A 420 ? 1.3259 1.3502 1.3952 0.0560  -0.1584 -0.1650 440 ARG   A CZ  
3025 N  NH1 . ARG   A 420 ? 0.9197 0.9572 1.0244 0.0528  -0.1641 -0.1725 440 ARG   A NH1 
3026 N  NH2 . ARG   A 420 ? 0.8199 0.8117 0.8252 0.0615  -0.1532 -0.1580 440 ARG   A NH2 
3027 N  N   . ASN   A 421 ? 1.0161 1.1438 1.2825 0.0640  -0.1281 -0.1829 441 ASN   A N   
3028 C  CA  . ASN   A 421 ? 1.0546 1.1775 1.2963 0.0596  -0.1067 -0.1793 441 ASN   A CA  
3029 C  C   . ASN   A 421 ? 0.9778 1.0543 1.1575 0.0631  -0.1147 -0.1752 441 ASN   A C   
3030 O  O   . ASN   A 421 ? 0.9342 0.9825 1.0849 0.0707  -0.1339 -0.1729 441 ASN   A O   
3031 C  CB  . ASN   A 421 ? 1.0264 1.1691 1.3122 0.0692  -0.0998 -0.1891 441 ASN   A CB  
3032 C  CG  . ASN   A 421 ? 1.0358 1.1589 1.3308 0.0906  -0.1258 -0.1989 441 ASN   A CG  
3033 O  OD1 . ASN   A 421 ? 1.0573 1.1556 1.3308 0.0995  -0.1524 -0.1988 441 ASN   A OD1 
3034 N  ND2 . ASN   A 421 ? 0.9789 1.1118 1.3028 0.1018  -0.1184 -0.2076 441 ASN   A ND2 
3035 N  N   . CYS   A 422 ? 1.0230 1.0886 1.1800 0.0575  -0.0984 -0.1746 442 CYS   A N   
3036 C  CA  . CYS   A 422 ? 1.2104 1.2289 1.3152 0.0581  -0.1009 -0.1702 442 CYS   A CA  
3037 C  C   . CYS   A 422 ? 1.1947 1.1790 1.2913 0.0808  -0.1241 -0.1732 442 CYS   A C   
3038 O  O   . CYS   A 422 ? 1.0295 1.0190 1.1557 0.0946  -0.1288 -0.1827 442 CYS   A O   
3039 C  CB  . CYS   A 422 ? 1.1295 1.1433 1.2232 0.0478  -0.0817 -0.1743 442 CYS   A CB  
3040 S  SG  . CYS   A 422 ? 1.0424 0.9935 1.0828 0.0452  -0.0800 -0.1697 442 CYS   A SG  
3041 N  N   . ILE   A 423 ? 1.3758 1.3241 1.4295 0.0875  -0.1384 -0.1651 443 ILE   A N   
3042 C  CA  . ILE   A 423 ? 1.4042 1.3169 1.4409 0.1136  -0.1649 -0.1665 443 ILE   A CA  
3043 C  C   . ILE   A 423 ? 1.4772 1.3452 1.4857 0.1211  -0.1583 -0.1637 443 ILE   A C   
3044 O  O   . ILE   A 423 ? 1.4815 1.3303 1.4949 0.1457  -0.1776 -0.1684 443 ILE   A O   
3045 C  CB  . ILE   A 423 ? 1.3597 1.2407 1.3456 0.1213  -0.1808 -0.1580 443 ILE   A CB  
3046 C  CG1 . ILE   A 423 ? 1.4253 1.2789 1.3985 0.1531  -0.2165 -0.1626 443 ILE   A CG1 
3047 C  CG2 . ILE   A 423 ? 1.4197 1.2556 1.3415 0.1100  -0.1594 -0.1420 443 ILE   A CG2 
3048 C  CD1 . ILE   A 423 ? 1.5657 1.3767 1.4711 0.1659  -0.2328 -0.1542 443 ILE   A CD1 
3049 N  N   . GLY   A 424 ? 1.4388 1.2895 1.4214 0.1008  -0.1325 -0.1575 444 GLY   A N   
3050 C  CA  . GLY   A 424 ? 1.5309 1.3340 1.4889 0.1043  -0.1240 -0.1562 444 GLY   A CA  
3051 C  C   . GLY   A 424 ? 1.4977 1.3259 1.4939 0.0969  -0.1096 -0.1710 444 GLY   A C   
3052 O  O   . GLY   A 424 ? 1.5157 1.3105 1.4936 0.0885  -0.0952 -0.1729 444 GLY   A O   
3053 N  N   . MET   A 425 ? 1.4766 1.3610 1.5252 0.0999  -0.1120 -0.1822 445 MET   A N   
3054 C  CA  . MET   A 425 ? 1.3940 1.3043 1.4735 0.0956  -0.0957 -0.1965 445 MET   A CA  
3055 C  C   . MET   A 425 ? 1.4785 1.3487 1.5531 0.1140  -0.0980 -0.2047 445 MET   A C   
3056 O  O   . MET   A 425 ? 1.4566 1.3083 1.5187 0.1045  -0.0819 -0.2130 445 MET   A O   
3057 C  CB  . MET   A 425 ? 1.1283 1.0994 1.2645 0.1004  -0.0957 -0.2038 445 MET   A CB  
3058 C  CG  . MET   A 425 ? 1.2371 1.2321 1.4009 0.1024  -0.0768 -0.2181 445 MET   A CG  
3059 S  SD  . MET   A 425 ? 1.2873 1.3392 1.5260 0.1183  -0.0760 -0.2264 445 MET   A SD  
3060 C  CE  . MET   A 425 ? 1.3940 1.4367 1.6485 0.1351  -0.1122 -0.2212 445 MET   A CE  
3061 N  N   . ARG   A 426 ? 1.4167 1.2725 1.5022 0.1420  -0.1200 -0.2044 446 ARG   A N   
3062 C  CA  . ARG   A 426 ? 1.4761 1.2937 1.5607 0.1648  -0.1239 -0.2119 446 ARG   A CA  
3063 C  C   . ARG   A 426 ? 1.5242 1.2671 1.5486 0.1591  -0.1173 -0.2023 446 ARG   A C   
3064 O  O   . ARG   A 426 ? 1.5355 1.2480 1.5544 0.1596  -0.1047 -0.2119 446 ARG   A O   
3065 C  CB  . ARG   A 426 ? 1.5833 1.4045 1.6942 0.1986  -0.1538 -0.2130 446 ARG   A CB  
3066 C  CG  . ARG   A 426 ? 1.5158 1.4087 1.7038 0.2060  -0.1551 -0.2276 446 ARG   A CG  
3067 C  CD  . ARG   A 426 ? 1.5323 1.4416 1.7539 0.2322  -0.1901 -0.2292 446 ARG   A CD  
3068 N  NE  . ARG   A 426 ? 1.7526 1.6686 2.0203 0.2639  -0.2007 -0.2425 446 ARG   A NE  
3069 C  CZ  . ARG   A 426 ? 1.7808 1.6553 2.0309 0.2966  -0.2299 -0.2404 446 ARG   A CZ  
3070 N  NH1 . ARG   A 426 ? 1.9329 1.7517 2.1136 0.3025  -0.2500 -0.2241 446 ARG   A NH1 
3071 N  NH2 . ARG   A 426 ? 1.6088 1.4973 1.9104 0.3264  -0.2381 -0.2542 446 ARG   A NH2 
3072 N  N   . PHE   A 427 ? 1.5748 1.2849 1.5538 0.1534  -0.1235 -0.1837 447 PHE   A N   
3073 C  CA  . PHE   A 427 ? 1.6669 1.3034 1.5903 0.1458  -0.1119 -0.1710 447 PHE   A CA  
3074 C  C   . PHE   A 427 ? 1.6473 1.2865 1.5732 0.1123  -0.0842 -0.1798 447 PHE   A C   
3075 O  O   . PHE   A 427 ? 1.8305 1.4198 1.7416 0.1090  -0.0729 -0.1844 447 PHE   A O   
3076 C  CB  . PHE   A 427 ? 1.7895 1.3978 1.6635 0.1442  -0.1175 -0.1488 447 PHE   A CB  
3077 C  CG  . PHE   A 427 ? 1.8882 1.4333 1.7121 0.1249  -0.0942 -0.1336 447 PHE   A CG  
3078 C  CD1 . PHE   A 427 ? 1.9034 1.4704 1.7296 0.0892  -0.0710 -0.1321 447 PHE   A CD1 
3079 C  CD2 . PHE   A 427 ? 1.9623 1.4257 1.7401 0.1429  -0.0944 -0.1202 447 PHE   A CD2 
3080 C  CE1 . PHE   A 427 ? 1.9989 1.5126 1.7907 0.0688  -0.0470 -0.1194 447 PHE   A CE1 
3081 C  CE2 . PHE   A 427 ? 2.1302 1.5328 1.8666 0.1224  -0.0681 -0.1047 447 PHE   A CE2 
3082 C  CZ  . PHE   A 427 ? 2.1461 1.5764 1.8936 0.0839  -0.0435 -0.1052 447 PHE   A CZ  
3083 N  N   . ALA   A 428 ? 1.6188 1.3143 1.5638 0.0878  -0.0750 -0.1832 448 ALA   A N   
3084 C  CA  . ALA   A 428 ? 1.6273 1.3320 1.5756 0.0569  -0.0542 -0.1932 448 ALA   A CA  
3085 C  C   . ALA   A 428 ? 1.6493 1.3572 1.6189 0.0606  -0.0484 -0.2166 448 ALA   A C   
3086 O  O   . ALA   A 428 ? 1.7835 1.4587 1.7423 0.0443  -0.0362 -0.2269 448 ALA   A O   
3087 C  CB  . ALA   A 428 ? 1.4242 1.1935 1.3907 0.0376  -0.0499 -0.1926 448 ALA   A CB  
3088 N  N   . LEU   A 429 ? 1.5450 1.2918 1.5468 0.0815  -0.0557 -0.2269 449 LEU   A N   
3089 C  CA  . LEU   A 429 ? 1.5638 1.3105 1.5818 0.0904  -0.0479 -0.2495 449 LEU   A CA  
3090 C  C   . LEU   A 429 ? 1.7234 1.3949 1.7195 0.1038  -0.0488 -0.2523 449 LEU   A C   
3091 O  O   . LEU   A 429 ? 1.7745 1.4196 1.7640 0.0955  -0.0374 -0.2705 449 LEU   A O   
3092 C  CB  . LEU   A 429 ? 1.3538 1.1518 1.4140 0.1140  -0.0524 -0.2564 449 LEU   A CB  
3093 C  CG  . LEU   A 429 ? 1.5206 1.3902 1.6066 0.1024  -0.0452 -0.2566 449 LEU   A CG  
3094 C  CD1 . LEU   A 429 ? 1.4914 1.4038 1.6262 0.1259  -0.0465 -0.2616 449 LEU   A CD1 
3095 C  CD2 . LEU   A 429 ? 1.3094 1.1947 1.3826 0.0827  -0.0278 -0.2715 449 LEU   A CD2 
3096 N  N   . MET   A 430 ? 1.8001 1.4325 1.7814 0.1257  -0.0636 -0.2350 450 MET   A N   
3097 C  CA  . MET   A 430 ? 1.8212 1.3749 1.7773 0.1428  -0.0649 -0.2335 450 MET   A CA  
3098 C  C   . MET   A 430 ? 1.9293 1.4230 1.8476 0.1141  -0.0489 -0.2266 450 MET   A C   
3099 O  O   . MET   A 430 ? 1.8672 1.3082 1.7767 0.1115  -0.0388 -0.2387 450 MET   A O   
3100 C  CB  . MET   A 430 ? 1.9201 1.4480 1.8640 0.1770  -0.0880 -0.2149 450 MET   A CB  
3101 C  CG  . MET   A 430 ? 2.0197 1.4534 1.9214 0.1948  -0.0897 -0.2036 450 MET   A CG  
3102 S  SD  . MET   A 430 ? 2.0684 1.4892 1.9847 0.2512  -0.1196 -0.2027 450 MET   A SD  
3103 C  CE  . MET   A 430 ? 2.1650 1.6375 2.1455 0.2594  -0.1093 -0.2373 450 MET   A CE  
3104 N  N   . ASN   A 431 ? 1.8544 1.3548 1.7540 0.0917  -0.0448 -0.2083 451 ASN   A N   
3105 C  CA  . ASN   A 431 ? 1.9160 1.3641 1.7887 0.0624  -0.0259 -0.2003 451 ASN   A CA  
3106 C  C   . ASN   A 431 ? 1.8847 1.3501 1.7810 0.0323  -0.0119 -0.2273 451 ASN   A C   
3107 O  O   . ASN   A 431 ? 1.9156 1.3224 1.8022 0.0168  0.0011  -0.2337 451 ASN   A O   
3108 C  CB  . ASN   A 431 ? 1.9150 1.3790 1.7697 0.0459  -0.0218 -0.1774 451 ASN   A CB  
3109 C  CG  . ASN   A 431 ? 2.0368 1.4498 1.8704 0.0151  0.0022  -0.1669 451 ASN   A CG  
3110 O  OD1 . ASN   A 431 ? 2.1781 1.5173 1.9936 0.0147  0.0128  -0.1649 451 ASN   A OD1 
3111 N  ND2 . ASN   A 431 ? 1.9979 1.4497 1.8383 -0.0112 0.0127  -0.1601 451 ASN   A ND2 
3112 N  N   . MET   A 432 ? 2.0202 1.5631 1.9462 0.0245  -0.0151 -0.2439 452 MET   A N   
3113 C  CA  . MET   A 432 ? 1.9108 1.4734 1.8529 0.0005  -0.0069 -0.2721 452 MET   A CA  
3114 C  C   . MET   A 432 ? 1.8987 1.4240 1.8417 0.0166  -0.0061 -0.2966 452 MET   A C   
3115 O  O   . MET   A 432 ? 1.8992 1.3858 1.8394 -0.0024 0.0019  -0.3157 452 MET   A O   
3116 C  CB  . MET   A 432 ? 1.5000 1.1495 1.4638 -0.0051 -0.0110 -0.2808 452 MET   A CB  
3117 C  CG  . MET   A 432 ? 1.7030 1.3909 1.6689 -0.0234 -0.0105 -0.2614 452 MET   A CG  
3118 S  SD  . MET   A 432 ? 1.5486 1.3288 1.5363 -0.0292 -0.0141 -0.2717 452 MET   A SD  
3119 C  CE  . MET   A 432 ? 1.4316 1.2357 1.4315 0.0073  -0.0202 -0.2721 452 MET   A CE  
3120 N  N   . LYS   A 433 ? 1.6963 1.2334 1.6475 0.0517  -0.0142 -0.2984 453 LYS   A N   
3121 C  CA  . LYS   A 433 ? 1.7696 1.2764 1.7241 0.0714  -0.0115 -0.3230 453 LYS   A CA  
3122 C  C   . LYS   A 433 ? 1.9723 1.3832 1.9043 0.0748  -0.0077 -0.3194 453 LYS   A C   
3123 O  O   . LYS   A 433 ? 1.8625 1.2327 1.7912 0.0696  -0.0002 -0.3448 453 LYS   A O   
3124 C  CB  . LYS   A 433 ? 1.7204 1.2638 1.6973 0.1095  -0.0191 -0.3228 453 LYS   A CB  
3125 C  CG  . LYS   A 433 ? 1.5620 1.1902 1.5630 0.1078  -0.0151 -0.3343 453 LYS   A CG  
3126 C  CD  . LYS   A 433 ? 1.6231 1.2888 1.6571 0.1425  -0.0194 -0.3317 453 LYS   A CD  
3127 C  CE  . LYS   A 433 ? 1.5659 1.3067 1.6220 0.1409  -0.0080 -0.3430 453 LYS   A CE  
3128 N  NZ  . LYS   A 433 ? 1.5627 1.3465 1.6629 0.1699  -0.0093 -0.3384 453 LYS   A NZ  
3129 N  N   . LEU   A 434 ? 2.0320 1.4008 1.9440 0.0851  -0.0124 -0.2883 454 LEU   A N   
3130 C  CA  . LEU   A 434 ? 1.9394 1.2088 1.8227 0.0874  -0.0053 -0.2788 454 LEU   A CA  
3131 C  C   . LEU   A 434 ? 1.9962 1.2330 1.8763 0.0432  0.0123  -0.2890 454 LEU   A C   
3132 O  O   . LEU   A 434 ? 2.1578 1.3198 2.0291 0.0386  0.0219  -0.3001 454 LEU   A O   
3133 C  CB  . LEU   A 434 ? 1.9851 1.2178 1.8371 0.1053  -0.0126 -0.2404 454 LEU   A CB  
3134 C  CG  . LEU   A 434 ? 2.0430 1.2711 1.8935 0.1553  -0.0337 -0.2313 454 LEU   A CG  
3135 C  CD1 . LEU   A 434 ? 2.1505 1.3451 1.9608 0.1707  -0.0441 -0.1947 454 LEU   A CD1 
3136 C  CD2 . LEU   A 434 ? 2.2607 1.4214 2.1082 0.1807  -0.0320 -0.2451 454 LEU   A CD2 
3137 N  N   . ALA   A 435 ? 2.0585 1.3515 1.9509 0.0103  0.0161  -0.2870 455 ALA   A N   
3138 C  CA  . ALA   A 435 ? 2.0476 1.3240 1.9502 -0.0334 0.0304  -0.3003 455 ALA   A CA  
3139 C  C   . ALA   A 435 ? 2.0690 1.3628 1.9917 -0.0434 0.0275  -0.3442 455 ALA   A C   
3140 O  O   . ALA   A 435 ? 2.1898 1.4305 2.1173 -0.0662 0.0363  -0.3637 455 ALA   A O   
3141 C  CB  . ALA   A 435 ? 1.9839 1.3221 1.8985 -0.0612 0.0334  -0.2866 455 ALA   A CB  
3142 N  N   . LEU   A 436 ? 1.9535 1.3185 1.8864 -0.0265 0.0163  -0.3610 456 LEU   A N   
3143 C  CA  . LEU   A 436 ? 1.8965 1.2801 1.8376 -0.0318 0.0136  -0.4030 456 LEU   A CA  
3144 C  C   . LEU   A 436 ? 2.0914 1.3996 2.0217 -0.0127 0.0174  -0.4239 456 LEU   A C   
3145 O  O   . LEU   A 436 ? 2.1288 1.4153 2.0608 -0.0283 0.0183  -0.4600 456 LEU   A O   
3146 C  CB  . LEU   A 436 ? 1.8335 1.3024 1.7802 -0.0127 0.0060  -0.4104 456 LEU   A CB  
3147 C  CG  . LEU   A 436 ? 1.8152 1.3622 1.7726 -0.0345 0.0013  -0.4032 456 LEU   A CG  
3148 C  CD1 . LEU   A 436 ? 1.7318 1.3494 1.6905 -0.0123 -0.0020 -0.4091 456 LEU   A CD1 
3149 C  CD2 . LEU   A 436 ? 1.8699 1.4193 1.8349 -0.0718 -0.0008 -0.4288 456 LEU   A CD2 
3150 N  N   . ILE   A 437 ? 2.1357 1.4032 2.0554 0.0225  0.0175  -0.4038 457 ILE   A N   
3151 C  CA  . ILE   A 437 ? 2.1834 1.3769 2.0937 0.0461  0.0212  -0.4219 457 ILE   A CA  
3152 C  C   . ILE   A 437 ? 2.3095 1.4114 2.2115 0.0181  0.0318  -0.4257 457 ILE   A C   
3153 O  O   . ILE   A 437 ? 2.3768 1.4380 2.2800 0.0093  0.0353  -0.4616 457 ILE   A O   
3154 C  CB  . ILE   A 437 ? 2.2170 1.3915 2.1219 0.0927  0.0156  -0.3969 457 ILE   A CB  
3155 C  CG1 . ILE   A 437 ? 2.1587 1.4228 2.0840 0.1194  0.0081  -0.4012 457 ILE   A CG1 
3156 C  CG2 . ILE   A 437 ? 2.4358 1.5196 2.3294 0.1175  0.0201  -0.4099 457 ILE   A CG2 
3157 C  CD1 . ILE   A 437 ? 2.1276 1.3931 2.0597 0.1602  -0.0024 -0.3753 457 ILE   A CD1 
3158 N  N   . ARG   A 438 ? 2.4661 1.5314 2.3586 0.0032  0.0388  -0.3894 458 ARG   A N   
3159 C  CA  . ARG   A 438 ? 2.5537 1.5242 2.4397 -0.0230 0.0546  -0.3865 458 ARG   A CA  
3160 C  C   . ARG   A 438 ? 2.4957 1.4825 2.4095 -0.0723 0.0589  -0.4205 458 ARG   A C   
3161 O  O   . ARG   A 438 ? 2.6120 1.5239 2.5314 -0.0922 0.0688  -0.4403 458 ARG   A O   
3162 C  CB  . ARG   A 438 ? 2.6962 1.6320 2.5617 -0.0279 0.0652  -0.3373 458 ARG   A CB  
3163 C  CG  . ARG   A 438 ? 2.8385 1.6553 2.6719 -0.0097 0.0774  -0.3145 458 ARG   A CG  
3164 C  CD  . ARG   A 438 ? 2.9012 1.6904 2.7226 0.0417  0.0640  -0.3251 458 ARG   A CD  
3165 N  NE  . ARG   A 438 ? 3.0865 1.7604 2.8727 0.0655  0.0729  -0.2995 458 ARG   A NE  
3166 C  CZ  . ARG   A 438 ? 3.0717 1.6858 2.8502 0.1014  0.0686  -0.3135 458 ARG   A CZ  
3167 N  NH1 . ARG   A 438 ? 2.9850 1.6425 2.7887 0.1169  0.0584  -0.3544 458 ARG   A NH1 
3168 N  NH2 . ARG   A 438 ? 3.1261 1.6313 2.8678 0.1242  0.0765  -0.2850 458 ARG   A NH2 
3169 N  N   . VAL   A 439 ? 2.3497 1.4324 2.2832 -0.0916 0.0500  -0.4290 459 VAL   A N   
3170 C  CA  . VAL   A 439 ? 2.2749 1.3825 2.2383 -0.1367 0.0487  -0.4618 459 VAL   A CA  
3171 C  C   . VAL   A 439 ? 2.3460 1.4548 2.3098 -0.1306 0.0368  -0.5142 459 VAL   A C   
3172 O  O   . VAL   A 439 ? 2.3711 1.4310 2.3495 -0.1577 0.0387  -0.5467 459 VAL   A O   
3173 C  CB  . VAL   A 439 ? 2.1554 1.3639 2.1371 -0.1546 0.0413  -0.4517 459 VAL   A CB  
3174 C  CG1 . VAL   A 439 ? 2.1618 1.4117 2.1753 -0.1919 0.0314  -0.4929 459 VAL   A CG1 
3175 C  CG2 . VAL   A 439 ? 2.2552 1.4513 2.2384 -0.1690 0.0571  -0.4064 459 VAL   A CG2 
3176 N  N   . LEU   A 440 ? 2.2274 1.3903 2.1751 -0.0953 0.0258  -0.5242 460 LEU   A N   
3177 C  CA  . LEU   A 440 ? 2.2733 1.4403 2.2118 -0.0848 0.0170  -0.5735 460 LEU   A CA  
3178 C  C   . LEU   A 440 ? 2.3822 1.4522 2.3066 -0.0639 0.0250  -0.5903 460 LEU   A C   
3179 O  O   . LEU   A 440 ? 2.3592 1.4087 2.2766 -0.0639 0.0201  -0.6369 460 LEU   A O   
3180 C  CB  . LEU   A 440 ? 2.1468 1.3975 2.0712 -0.0520 0.0099  -0.5746 460 LEU   A CB  
3181 C  CG  . LEU   A 440 ? 2.0584 1.4040 1.9930 -0.0708 0.0005  -0.5649 460 LEU   A CG  
3182 C  CD1 . LEU   A 440 ? 1.6894 1.1050 1.6113 -0.0361 -0.0002 -0.5537 460 LEU   A CD1 
3183 C  CD2 . LEU   A 440 ? 2.1108 1.4791 2.0512 -0.1022 -0.0130 -0.6075 460 LEU   A CD2 
3184 N  N   . GLN   A 441 ? 2.4641 1.4715 2.3806 -0.0434 0.0360  -0.5543 461 GLN   A N   
3185 C  CA  . GLN   A 441 ? 2.5403 1.4443 2.4445 -0.0249 0.0443  -0.5668 461 GLN   A CA  
3186 C  C   . GLN   A 441 ? 2.6505 1.4797 2.5683 -0.0680 0.0509  -0.5917 461 GLN   A C   
3187 O  O   . GLN   A 441 ? 2.6241 1.3735 2.5339 -0.0586 0.0549  -0.6199 461 GLN   A O   
3188 C  CB  . GLN   A 441 ? 2.5791 1.4299 2.4688 0.0059  0.0520  -0.5186 461 GLN   A CB  
3189 C  CG  . GLN   A 441 ? 2.5622 1.4239 2.4408 0.0634  0.0469  -0.5161 461 GLN   A CG  
3190 C  CD  . GLN   A 441 ? 2.6273 1.4417 2.4917 0.0950  0.0480  -0.4690 461 GLN   A CD  
3191 O  OE1 . GLN   A 441 ? 2.6880 1.4651 2.5423 0.0749  0.0542  -0.4344 461 GLN   A OE1 
3192 N  NE2 . GLN   A 441 ? 2.5941 1.4105 2.4568 0.1465  0.0419  -0.4680 461 GLN   A NE2 
3193 N  N   . ASN   A 442 ? 2.6288 1.4818 2.5717 -0.1153 0.0528  -0.5834 462 ASN   A N   
3194 C  CA  . ASN   A 442 ? 2.6872 1.4708 2.6555 -0.1613 0.0622  -0.6021 462 ASN   A CA  
3195 C  C   . ASN   A 442 ? 2.6532 1.4988 2.6542 -0.2035 0.0464  -0.6459 462 ASN   A C   
3196 O  O   . ASN   A 442 ? 2.7962 1.6046 2.8091 -0.2282 0.0406  -0.6671 462 ASN   A O   
3197 C  CB  . ASN   A 442 ? 2.7508 1.4916 2.7281 -0.1840 0.0840  -0.5509 462 ASN   A CB  
3198 C  CG  . ASN   A 442 ? 2.8706 1.5122 2.8125 -0.1486 0.0998  -0.5136 462 ASN   A CG  
3199 O  OD1 . ASN   A 442 ? 3.0089 1.5448 2.9519 -0.1633 0.1178  -0.5115 462 ASN   A OD1 
3200 N  ND2 . ASN   A 442 ? 2.8532 1.5275 2.7654 -0.1011 0.0923  -0.4841 462 ASN   A ND2 
3201 N  N   . PHE   A 443 ? 2.4335 1.3880 2.4403 -0.2058 0.0319  -0.6449 463 PHE   A N   
3202 C  CA  . PHE   A 443 ? 2.4408 1.4594 2.4794 -0.2442 0.0138  -0.6811 463 PHE   A CA  
3203 C  C   . PHE   A 443 ? 2.3666 1.4732 2.3803 -0.2190 -0.0088 -0.7082 463 PHE   A C   
3204 O  O   . PHE   A 443 ? 2.3074 1.4571 2.2928 -0.1813 -0.0071 -0.6814 463 PHE   A O   
3205 C  CB  . PHE   A 443 ? 2.3849 1.4508 2.4637 -0.2815 0.0209  -0.6503 463 PHE   A CB  
3206 C  CG  . PHE   A 443 ? 2.4719 1.4546 2.5709 -0.3061 0.0499  -0.6169 463 PHE   A CG  
3207 C  CD1 . PHE   A 443 ? 2.6084 1.5412 2.7379 -0.3408 0.0530  -0.6297 463 PHE   A CD1 
3208 C  CD2 . PHE   A 443 ? 2.4279 1.3968 2.5048 -0.2871 0.0693  -0.5581 463 PHE   A CD2 
3209 C  CE1 . PHE   A 443 ? 2.6719 1.5292 2.8164 -0.3617 0.0830  -0.5932 463 PHE   A CE1 
3210 C  CE2 . PHE   A 443 ? 2.5160 1.4036 2.6006 -0.3066 0.0986  -0.5243 463 PHE   A CE2 
3211 C  CZ  . PHE   A 443 ? 2.6774 1.5019 2.7989 -0.3470 0.1100  -0.5449 463 PHE   A CZ  
3212 N  N   . SER   A 444 ? 2.3368 1.4774 2.3527 -0.2357 -0.0318 -0.7460 464 SER   A N   
3213 C  CA  . SER   A 444 ? 2.2545 1.4847 2.2478 -0.2210 -0.0542 -0.7692 464 SER   A CA  
3214 C  C   . SER   A 444 ? 2.2733 1.5812 2.3068 -0.2572 -0.0695 -0.7669 464 SER   A C   
3215 O  O   . SER   A 444 ? 2.3623 1.6533 2.4441 -0.2965 -0.0649 -0.7574 464 SER   A O   
3216 C  CB  . SER   A 444 ? 2.1283 1.3409 2.0832 -0.2071 -0.0710 -0.8116 464 SER   A CB  
3217 O  OG  . SER   A 444 ? 2.2039 1.3636 2.1184 -0.1653 -0.0564 -0.8142 464 SER   A OG  
3218 N  N   . PHE   A 445 ? 2.1839 1.5781 2.1982 -0.2418 -0.0861 -0.7739 465 PHE   A N   
3219 C  CA  . PHE   A 445 ? 2.1403 1.6158 2.1903 -0.2680 -0.1014 -0.7682 465 PHE   A CA  
3220 C  C   . PHE   A 445 ? 2.1011 1.6391 2.1226 -0.2583 -0.1334 -0.8000 465 PHE   A C   
3221 O  O   . PHE   A 445 ? 2.0549 1.6087 2.0195 -0.2210 -0.1369 -0.8101 465 PHE   A O   
3222 C  CB  . PHE   A 445 ? 1.9714 1.4965 2.0219 -0.2542 -0.0875 -0.7207 465 PHE   A CB  
3223 C  CG  . PHE   A 445 ? 2.0753 1.5504 2.1498 -0.2647 -0.0591 -0.6746 465 PHE   A CG  
3224 C  CD1 . PHE   A 445 ? 2.0962 1.4980 2.1433 -0.2392 -0.0393 -0.6561 465 PHE   A CD1 
3225 C  CD2 . PHE   A 445 ? 2.1542 1.6551 2.2762 -0.2975 -0.0519 -0.6499 465 PHE   A CD2 
3226 C  CE1 . PHE   A 445 ? 2.1151 1.4669 2.1742 -0.2449 -0.0155 -0.6130 465 PHE   A CE1 
3227 C  CE2 . PHE   A 445 ? 2.0910 1.5415 2.2243 -0.3046 -0.0236 -0.6066 465 PHE   A CE2 
3228 C  CZ  . PHE   A 445 ? 2.0441 1.4183 2.1422 -0.2777 -0.0067 -0.5877 465 PHE   A CZ  
3229 N  N   . LYS   A 446 ? 2.1124 1.6846 2.1731 -0.2905 -0.1553 -0.8146 466 LYS   A N   
3230 C  CA  . LYS   A 446 ? 2.1638 1.7932 2.2009 -0.2839 -0.1896 -0.8443 466 LYS   A CA  
3231 C  C   . LYS   A 446 ? 2.0765 1.7910 2.1608 -0.3045 -0.2066 -0.8331 466 LYS   A C   
3232 O  O   . LYS   A 446 ? 2.0330 1.7513 2.1810 -0.3351 -0.1925 -0.8111 466 LYS   A O   
3233 C  CB  . LYS   A 446 ? 2.1774 1.7606 2.2168 -0.3007 -0.2069 -0.8828 466 LYS   A CB  
3234 C  CG  . LYS   A 446 ? 2.2342 1.7225 2.2382 -0.2861 -0.1886 -0.8940 466 LYS   A CG  
3235 C  CD  . LYS   A 446 ? 2.2611 1.7505 2.1860 -0.2371 -0.1842 -0.9005 466 LYS   A CD  
3236 C  CE  . LYS   A 446 ? 2.3264 1.7236 2.2189 -0.2198 -0.1664 -0.9140 466 LYS   A CE  
3237 N  NZ  . LYS   A 446 ? 2.3399 1.6925 2.2286 -0.2377 -0.1851 -0.9538 466 LYS   A NZ  
3238 N  N   . PRO   A 447 ? 2.0891 1.8707 2.1415 -0.2861 -0.2349 -0.8462 467 PRO   A N   
3239 C  CA  . PRO   A 447 ? 2.0715 1.9347 2.1704 -0.3024 -0.2544 -0.8373 467 PRO   A CA  
3240 C  C   . PRO   A 447 ? 2.1520 2.0168 2.3206 -0.3429 -0.2708 -0.8574 467 PRO   A C   
3241 O  O   . PRO   A 447 ? 2.0868 1.9031 2.2504 -0.3529 -0.2806 -0.8883 467 PRO   A O   
3242 C  CB  . PRO   A 447 ? 2.0715 1.9893 2.1046 -0.2669 -0.2816 -0.8493 467 PRO   A CB  
3243 C  CG  . PRO   A 447 ? 2.0324 1.9065 1.9878 -0.2301 -0.2636 -0.8501 467 PRO   A CG  
3244 C  CD  . PRO   A 447 ? 2.0629 1.8497 2.0306 -0.2447 -0.2455 -0.8631 467 PRO   A CD  
3245 N  N   . CYS   A 448 ? 2.1177 2.0401 2.3542 -0.3661 -0.2728 -0.8401 468 CYS   A N   
3246 C  CA  . CYS   A 448 ? 2.1222 2.0605 2.4381 -0.4053 -0.2857 -0.8557 468 CYS   A CA  
3247 C  C   . CYS   A 448 ? 2.1606 2.1858 2.4870 -0.3982 -0.3267 -0.8719 468 CYS   A C   
3248 O  O   . CYS   A 448 ? 2.1261 2.1945 2.3943 -0.3629 -0.3434 -0.8680 468 CYS   A O   
3249 C  CB  . CYS   A 448 ? 2.0970 2.0315 2.4902 -0.4386 -0.2518 -0.8231 468 CYS   A CB  
3250 S  SG  . CYS   A 448 ? 2.2382 2.0624 2.6586 -0.4697 -0.2148 -0.8194 468 CYS   A SG  
3251 N  N   . LYS   A 449 ? 2.2637 2.3128 2.6663 -0.4316 -0.3423 -0.8897 469 LYS   A N   
3252 C  CA  . LYS   A 449 ? 2.2744 2.4074 2.6997 -0.4267 -0.3823 -0.9051 469 LYS   A CA  
3253 C  C   . LYS   A 449 ? 2.2136 2.4194 2.6646 -0.4170 -0.3757 -0.8697 469 LYS   A C   
3254 O  O   . LYS   A 449 ? 2.2244 2.4901 2.6415 -0.3877 -0.4042 -0.8703 469 LYS   A O   
3255 C  CB  . LYS   A 449 ? 2.3573 2.4982 2.8691 -0.4670 -0.3975 -0.9328 469 LYS   A CB  
3256 C  CG  . LYS   A 449 ? 2.3582 2.5918 2.9448 -0.4772 -0.4193 -0.9314 469 LYS   A CG  
3257 C  CD  . LYS   A 449 ? 2.4574 2.6926 3.1396 -0.5214 -0.4263 -0.9572 469 LYS   A CD  
3258 C  CE  . LYS   A 449 ? 2.5219 2.8468 3.2960 -0.5357 -0.4362 -0.9494 469 LYS   A CE  
3259 N  NZ  . LYS   A 449 ? 2.6018 2.9268 3.4775 -0.5817 -0.4362 -0.9724 469 LYS   A NZ  
3260 N  N   . GLU   A 450 ? 2.0931 2.2907 2.5992 -0.4396 -0.3373 -0.8376 470 GLU   A N   
3261 C  CA  . GLU   A 450 ? 2.0847 2.3455 2.6183 -0.4328 -0.3263 -0.8035 470 GLU   A CA  
3262 C  C   . GLU   A 450 ? 2.0579 2.3028 2.5207 -0.4022 -0.3055 -0.7742 470 GLU   A C   
3263 O  O   . GLU   A 450 ? 1.8503 2.1345 2.3331 -0.3987 -0.2895 -0.7430 470 GLU   A O   
3264 C  CB  . GLU   A 450 ? 2.0678 2.3309 2.6983 -0.4734 -0.2932 -0.7838 470 GLU   A CB  
3265 C  CG  . GLU   A 450 ? 2.1557 2.3281 2.7881 -0.4960 -0.2506 -0.7712 470 GLU   A CG  
3266 C  CD  . GLU   A 450 ? 2.2407 2.4100 2.9666 -0.5377 -0.2171 -0.7542 470 GLU   A CD  
3267 O  OE1 . GLU   A 450 ? 2.2161 2.4593 3.0039 -0.5455 -0.2201 -0.7449 470 GLU   A OE1 
3268 O  OE2 . GLU   A 450 ? 2.3243 2.4154 3.0602 -0.5609 -0.1860 -0.7488 470 GLU   A OE2 
3269 N  N   . THR   A 451 ? 2.0464 2.2354 2.4292 -0.3800 -0.3044 -0.7842 471 THR   A N   
3270 C  CA  . THR   A 451 ? 1.9801 2.1570 2.2970 -0.3494 -0.2858 -0.7593 471 THR   A CA  
3271 C  C   . THR   A 451 ? 1.8567 2.1016 2.1267 -0.3131 -0.3122 -0.7543 471 THR   A C   
3272 O  O   . THR   A 451 ? 1.7939 2.0534 2.0216 -0.2938 -0.3446 -0.7792 471 THR   A O   
3273 C  CB  . THR   A 451 ? 1.9950 2.0930 2.2455 -0.3348 -0.2748 -0.7728 471 THR   A CB  
3274 O  OG1 . THR   A 451 ? 2.0448 2.0728 2.3341 -0.3647 -0.2448 -0.7685 471 THR   A OG1 
3275 C  CG2 . THR   A 451 ? 1.8624 1.9583 2.0433 -0.2984 -0.2600 -0.7514 471 THR   A CG2 
3276 N  N   . GLN   A 452 ? 1.7752 2.0576 2.0490 -0.3028 -0.2976 -0.7212 472 GLN   A N   
3277 C  CA  . GLN   A 452 ? 1.7213 2.0655 1.9528 -0.2681 -0.3187 -0.7101 472 GLN   A CA  
3278 C  C   . GLN   A 452 ? 1.8485 2.1632 1.9795 -0.2301 -0.3183 -0.7130 472 GLN   A C   
3279 O  O   . GLN   A 452 ? 1.8936 2.1786 1.9942 -0.2201 -0.2898 -0.6942 472 GLN   A O   
3280 C  CB  . GLN   A 452 ? 1.5161 1.9022 1.7824 -0.2699 -0.2999 -0.6737 472 GLN   A CB  
3281 C  CG  . GLN   A 452 ? 1.4358 1.8890 1.6725 -0.2369 -0.3218 -0.6592 472 GLN   A CG  
3282 C  CD  . GLN   A 452 ? 1.6491 2.1340 1.9204 -0.2368 -0.2984 -0.6156 472 GLN   A CD  
3283 O  OE1 . GLN   A 452 ? 1.6167 2.0577 1.8834 -0.2405 -0.2592 -0.5809 472 GLN   A OE1 
3284 N  NE2 . GLN   A 452 ? 1.6195 2.1759 1.9224 -0.2289 -0.3215 -0.6132 472 GLN   A NE2 
3285 N  N   . ILE   A 453 ? 1.7214 2.0438 1.8003 -0.2082 -0.3484 -0.7366 473 ILE   A N   
3286 C  CA  . ILE   A 453 ? 1.8191 2.1162 1.7991 -0.1700 -0.3463 -0.7398 473 ILE   A CA  
3287 C  C   . ILE   A 453 ? 1.8382 2.1881 1.7686 -0.1373 -0.3764 -0.7372 473 ILE   A C   
3288 O  O   . ILE   A 453 ? 1.9790 2.3498 1.9198 -0.1406 -0.4105 -0.7610 473 ILE   A O   
3289 C  CB  . ILE   A 453 ? 1.9125 2.1454 1.8591 -0.1723 -0.3475 -0.7737 473 ILE   A CB  
3290 C  CG1 . ILE   A 453 ? 1.9030 2.0766 1.8962 -0.2022 -0.3173 -0.7737 473 ILE   A CG1 
3291 C  CG2 . ILE   A 453 ? 1.8656 2.0761 1.7089 -0.1301 -0.3406 -0.7752 473 ILE   A CG2 
3292 C  CD1 . ILE   A 453 ? 1.9796 2.0848 1.9441 -0.2044 -0.3166 -0.8058 473 ILE   A CD1 
3293 N  N   . PRO   A 454 ? 1.8968 2.2669 1.7721 -0.1048 -0.3651 -0.7086 474 PRO   A N   
3294 C  CA  . PRO   A 454 ? 1.7843 2.1369 1.6440 -0.0973 -0.3272 -0.6807 474 PRO   A CA  
3295 C  C   . PRO   A 454 ? 1.6719 2.0464 1.6116 -0.1214 -0.3094 -0.6453 474 PRO   A C   
3296 O  O   . PRO   A 454 ? 1.5746 2.0022 1.5661 -0.1334 -0.3319 -0.6478 474 PRO   A O   
3297 C  CB  . PRO   A 454 ? 1.7457 2.1173 1.5189 -0.0524 -0.3256 -0.6587 474 PRO   A CB  
3298 C  CG  . PRO   A 454 ? 1.8668 2.2905 1.6432 -0.0435 -0.3650 -0.6631 474 PRO   A CG  
3299 C  CD  . PRO   A 454 ? 1.8658 2.2780 1.6856 -0.0703 -0.3912 -0.7015 474 PRO   A CD  
3300 N  N   . LEU   A 455 ? 1.7474 2.0814 1.6986 -0.1268 -0.2689 -0.6116 475 LEU   A N   
3301 C  CA  . LEU   A 455 ? 1.6397 1.9863 1.6566 -0.1469 -0.2493 -0.5766 475 LEU   A CA  
3302 C  C   . LEU   A 455 ? 1.6038 2.0014 1.6117 -0.1249 -0.2506 -0.5409 475 LEU   A C   
3303 O  O   . LEU   A 455 ? 1.5845 1.9784 1.5323 -0.0935 -0.2393 -0.5180 475 LEU   A O   
3304 C  CB  . LEU   A 455 ? 1.6519 1.9398 1.6701 -0.1516 -0.2098 -0.5500 475 LEU   A CB  
3305 C  CG  . LEU   A 455 ? 1.5590 1.8493 1.6279 -0.1668 -0.1858 -0.5108 475 LEU   A CG  
3306 C  CD1 . LEU   A 455 ? 1.5091 1.7380 1.6047 -0.1900 -0.1631 -0.5107 475 LEU   A CD1 
3307 C  CD2 . LEU   A 455 ? 1.4816 1.7798 1.5179 -0.1389 -0.1663 -0.4675 475 LEU   A CD2 
3308 N  N   . LYS   A 456 ? 1.5460 1.9901 1.6167 -0.1414 -0.2621 -0.5363 476 LYS   A N   
3309 C  CA  . LYS   A 456 ? 1.5313 2.0171 1.6051 -0.1234 -0.2583 -0.4992 476 LYS   A CA  
3310 C  C   . LYS   A 456 ? 1.4709 1.9307 1.5710 -0.1325 -0.2197 -0.4589 476 LYS   A C   
3311 O  O   . LYS   A 456 ? 1.4350 1.8722 1.5846 -0.1619 -0.2047 -0.4613 476 LYS   A O   
3312 C  CB  . LYS   A 456 ? 1.5790 2.1308 1.7106 -0.1328 -0.2893 -0.5141 476 LYS   A CB  
3313 C  CG  . LYS   A 456 ? 1.7061 2.2975 1.8001 -0.1103 -0.3337 -0.5439 476 LYS   A CG  
3314 C  CD  . LYS   A 456 ? 1.7924 2.4562 1.9416 -0.1086 -0.3610 -0.5444 476 LYS   A CD  
3315 C  CE  . LYS   A 456 ? 1.8420 2.5349 2.0523 -0.1328 -0.3948 -0.5888 476 LYS   A CE  
3316 N  NZ  . LYS   A 456 ? 1.8706 2.5701 2.0208 -0.1041 -0.4324 -0.6079 476 LYS   A NZ  
3317 N  N   . LEU   A 457 ? 1.5453 2.0050 1.6095 -0.1068 -0.2034 -0.4223 477 LEU   A N   
3318 C  CA  . LEU   A 457 ? 1.5698 2.0118 1.6575 -0.1122 -0.1728 -0.3859 477 LEU   A CA  
3319 C  C   . LEU   A 457 ? 1.6806 2.1676 1.8253 -0.1225 -0.1770 -0.3752 477 LEU   A C   
3320 O  O   . LEU   A 457 ? 1.7373 2.2757 1.8941 -0.1145 -0.2032 -0.3861 477 LEU   A O   
3321 C  CB  . LEU   A 457 ? 1.4675 1.8952 1.5057 -0.0834 -0.1551 -0.3536 477 LEU   A CB  
3322 C  CG  . LEU   A 457 ? 1.4344 1.8130 1.4314 -0.0753 -0.1384 -0.3561 477 LEU   A CG  
3323 C  CD1 . LEU   A 457 ? 1.4733 1.8467 1.4332 -0.0487 -0.1202 -0.3250 477 LEU   A CD1 
3324 C  CD2 . LEU   A 457 ? 1.4781 1.8127 1.5056 -0.0974 -0.1206 -0.3557 477 LEU   A CD2 
3325 N  N   . SER   A 458 ? 1.8106 2.2779 1.9891 -0.1381 -0.1513 -0.3544 478 SER   A N   
3326 C  CA  . SER   A 458 ? 1.7727 2.2796 2.0027 -0.1451 -0.1482 -0.3412 478 SER   A CA  
3327 C  C   . SER   A 458 ? 1.8980 2.4367 2.1042 -0.1143 -0.1541 -0.3176 478 SER   A C   
3328 O  O   . SER   A 458 ? 1.8156 2.3279 1.9902 -0.0988 -0.1353 -0.2893 478 SER   A O   
3329 C  CB  . SER   A 458 ? 1.6716 2.1424 1.9252 -0.1623 -0.1157 -0.3202 478 SER   A CB  
3330 O  OG  . SER   A 458 ? 1.6700 2.1775 1.9667 -0.1647 -0.1082 -0.3057 478 SER   A OG  
3331 N  N   . LEU   A 459 ? 2.4189 3.0134 2.6422 -0.1047 -0.1815 -0.3297 479 LEU   A N   
3332 C  CA  . LEU   A 459 ? 2.3939 3.0170 2.5962 -0.0738 -0.1880 -0.3064 479 LEU   A CA  
3333 C  C   . LEU   A 459 ? 2.3431 2.9678 2.5775 -0.0746 -0.1638 -0.2775 479 LEU   A C   
3334 O  O   . LEU   A 459 ? 2.3696 3.0091 2.5900 -0.0499 -0.1639 -0.2550 479 LEU   A O   
3335 C  CB  . LEU   A 459 ? 2.4081 3.0921 2.6265 -0.0619 -0.2262 -0.3274 479 LEU   A CB  
3336 C  CG  . LEU   A 459 ? 2.4378 3.1243 2.5938 -0.0404 -0.2549 -0.3455 479 LEU   A CG  
3337 C  CD1 . LEU   A 459 ? 2.3893 3.0449 2.5334 -0.0612 -0.2589 -0.3780 479 LEU   A CD1 
3338 C  CD2 . LEU   A 459 ? 2.5390 3.2896 2.7136 -0.0242 -0.2958 -0.3623 479 LEU   A CD2 
3339 N  N   . GLY   A 460 ? 1.9492 2.5542 2.2224 -0.1013 -0.1418 -0.2778 480 GLY   A N   
3340 C  CA  . GLY   A 460 ? 1.7168 2.3155 2.0121 -0.1022 -0.1162 -0.2528 480 GLY   A CA  
3341 C  C   . GLY   A 460 ? 1.8748 2.4209 2.1228 -0.0904 -0.0946 -0.2264 480 GLY   A C   
3342 O  O   . GLY   A 460 ? 1.8819 2.4167 2.0847 -0.0695 -0.1004 -0.2171 480 GLY   A O   
3343 N  N   . GLY   A 461 ? 1.8106 2.3238 2.0684 -0.1034 -0.0693 -0.2148 481 GLY   A N   
3344 C  CA  . GLY   A 461 ? 1.7196 2.1901 1.9412 -0.0908 -0.0528 -0.1913 481 GLY   A CA  
3345 C  C   . GLY   A 461 ? 1.8278 2.2470 2.0135 -0.0941 -0.0474 -0.1923 481 GLY   A C   
3346 O  O   . GLY   A 461 ? 1.8413 2.2461 1.9943 -0.0772 -0.0494 -0.1831 481 GLY   A O   
3347 N  N   . LEU   A 462 ? 2.1283 2.5188 2.3226 -0.1151 -0.0387 -0.2025 482 LEU   A N   
3348 C  CA  . LEU   A 462 ? 2.0897 2.4284 2.2538 -0.1165 -0.0329 -0.2029 482 LEU   A CA  
3349 C  C   . LEU   A 462 ? 2.1929 2.5313 2.3488 -0.1215 -0.0471 -0.2267 482 LEU   A C   
3350 O  O   . LEU   A 462 ? 2.2184 2.5889 2.3976 -0.1323 -0.0603 -0.2468 482 LEU   A O   
3351 C  CB  . LEU   A 462 ? 2.1441 2.4405 2.3130 -0.1325 -0.0138 -0.1973 482 LEU   A CB  
3352 C  CG  . LEU   A 462 ? 2.1539 2.4593 2.3623 -0.1586 -0.0050 -0.2086 482 LEU   A CG  
3353 C  CD1 . LEU   A 462 ? 2.2112 2.4553 2.4065 -0.1723 0.0132  -0.2048 482 LEU   A CD1 
3354 C  CD2 . LEU   A 462 ? 2.0851 2.4268 2.3248 -0.1595 0.0056  -0.1981 482 LEU   A CD2 
3355 N  N   . LEU   A 463 ? 1.7430 2.0456 1.8673 -0.1124 -0.0451 -0.2266 483 LEU   A N   
3356 C  CA  . LEU   A 463 ? 1.6689 1.9666 1.7769 -0.1119 -0.0562 -0.2492 483 LEU   A CA  
3357 C  C   . LEU   A 463 ? 1.6674 1.9372 1.7925 -0.1359 -0.0544 -0.2691 483 LEU   A C   
3358 O  O   . LEU   A 463 ? 1.6406 1.8609 1.7557 -0.1394 -0.0428 -0.2656 483 LEU   A O   
3359 C  CB  . LEU   A 463 ? 1.4888 1.7599 1.5640 -0.0932 -0.0506 -0.2424 483 LEU   A CB  
3360 C  CG  . LEU   A 463 ? 1.4682 1.7430 1.5193 -0.0861 -0.0603 -0.2647 483 LEU   A CG  
3361 C  CD1 . LEU   A 463 ? 1.3220 1.6443 1.3627 -0.0748 -0.0741 -0.2669 483 LEU   A CD1 
3362 C  CD2 . LEU   A 463 ? 1.4305 1.6780 1.4575 -0.0692 -0.0496 -0.2597 483 LEU   A CD2 
3363 N  N   . GLN   A 464 ? 1.5985 1.8996 1.7518 -0.1518 -0.0671 -0.2904 484 GLN   A N   
3364 C  CA  . GLN   A 464 ? 1.5346 1.8136 1.7124 -0.1780 -0.0671 -0.3140 484 GLN   A CA  
3365 C  C   . GLN   A 464 ? 1.5588 1.8765 1.7467 -0.1825 -0.0936 -0.3471 484 GLN   A C   
3366 O  O   . GLN   A 464 ? 1.6162 1.9795 1.7921 -0.1644 -0.1103 -0.3468 484 GLN   A O   
3367 C  CB  . GLN   A 464 ? 1.5248 1.8023 1.7460 -0.2010 -0.0499 -0.3038 484 GLN   A CB  
3368 C  CG  . GLN   A 464 ? 1.6657 1.8868 1.8681 -0.2000 -0.0244 -0.2778 484 GLN   A CG  
3369 C  CD  . GLN   A 464 ? 1.6759 1.8962 1.9130 -0.2195 -0.0029 -0.2650 484 GLN   A CD  
3370 O  OE1 . GLN   A 464 ? 1.6412 1.9136 1.9216 -0.2298 -0.0059 -0.2710 484 GLN   A OE1 
3371 N  NE2 . GLN   A 464 ? 1.6112 1.7723 1.8283 -0.2226 0.0197  -0.2469 484 GLN   A NE2 
3372 N  N   . PRO   A 465 ? 1.5344 1.8325 1.7405 -0.2043 -0.0999 -0.3768 485 PRO   A N   
3373 C  CA  . PRO   A 465 ? 1.6593 1.9985 1.8814 -0.2107 -0.1298 -0.4129 485 PRO   A CA  
3374 C  C   . PRO   A 465 ? 1.6572 2.0524 1.9444 -0.2290 -0.1379 -0.4177 485 PRO   A C   
3375 O  O   . PRO   A 465 ? 1.4022 1.7918 1.7299 -0.2468 -0.1148 -0.4001 485 PRO   A O   
3376 C  CB  . PRO   A 465 ? 1.6214 1.9116 1.8461 -0.2306 -0.1309 -0.4438 485 PRO   A CB  
3377 C  CG  . PRO   A 465 ? 1.5564 1.7798 1.7491 -0.2234 -0.1038 -0.4210 485 PRO   A CG  
3378 C  CD  . PRO   A 465 ? 1.5061 1.7365 1.7072 -0.2183 -0.0832 -0.3811 485 PRO   A CD  
3379 N  N   . GLU   A 466 ? 1.7104 2.1612 2.0062 -0.2222 -0.1710 -0.4420 486 GLU   A N   
3380 C  CA  . GLU   A 466 ? 1.6797 2.1918 2.0478 -0.2393 -0.1847 -0.4545 486 GLU   A CA  
3381 C  C   . GLU   A 466 ? 1.6822 2.1754 2.1153 -0.2812 -0.1747 -0.4771 486 GLU   A C   
3382 O  O   . GLU   A 466 ? 1.6892 2.1836 2.1739 -0.3016 -0.1478 -0.4599 486 GLU   A O   
3383 C  CB  . GLU   A 466 ? 1.7250 2.2958 2.0865 -0.2224 -0.2289 -0.4825 486 GLU   A CB  
3384 C  CG  . GLU   A 466 ? 1.7634 2.3740 2.0918 -0.1859 -0.2376 -0.4559 486 GLU   A CG  
3385 C  CD  . GLU   A 466 ? 1.8242 2.4954 2.1522 -0.1693 -0.2835 -0.4831 486 GLU   A CD  
3386 O  OE1 . GLU   A 466 ? 1.8443 2.5332 2.2070 -0.1888 -0.3106 -0.5256 486 GLU   A OE1 
3387 O  OE2 . GLU   A 466 ? 1.9850 2.6842 2.2774 -0.1360 -0.2939 -0.4628 486 GLU   A OE2 
3388 N  N   . LYS   A 467 ? 1.6677 2.1397 2.0968 -0.2941 -0.1942 -0.5160 487 LYS   A N   
3389 C  CA  . LYS   A 467 ? 1.6102 2.0495 2.0952 -0.3348 -0.1831 -0.5391 487 LYS   A CA  
3390 C  C   . LYS   A 467 ? 1.6271 1.9765 2.0678 -0.3372 -0.1512 -0.5221 487 LYS   A C   
3391 O  O   . LYS   A 467 ? 1.4338 1.7510 1.8012 -0.3086 -0.1523 -0.5134 487 LYS   A O   
3392 C  CB  . LYS   A 467 ? 1.4915 1.9507 1.9967 -0.3476 -0.2235 -0.5941 487 LYS   A CB  
3393 C  CG  . LYS   A 467 ? 1.4726 2.0180 2.0186 -0.3404 -0.2608 -0.6110 487 LYS   A CG  
3394 C  CD  . LYS   A 467 ? 1.4965 2.0396 2.0245 -0.3351 -0.2991 -0.6477 487 LYS   A CD  
3395 C  CE  . LYS   A 467 ? 1.3240 1.8457 1.9243 -0.3751 -0.2943 -0.6694 487 LYS   A CE  
3396 N  NZ  . LYS   A 467 ? 1.5678 2.1563 2.2587 -0.3907 -0.3017 -0.6693 487 LYS   A NZ  
3397 N  N   . PRO   A 468 ? 1.6366 1.9439 2.1211 -0.3694 -0.1210 -0.5157 488 PRO   A N   
3398 C  CA  . PRO   A 468 ? 1.6029 1.8202 2.0444 -0.3696 -0.0934 -0.5004 488 PRO   A CA  
3399 C  C   . PRO   A 468 ? 1.6515 1.8291 2.0576 -0.3659 -0.1141 -0.5370 488 PRO   A C   
3400 O  O   . PRO   A 468 ? 1.6142 1.8240 2.0425 -0.3754 -0.1465 -0.5800 488 PRO   A O   
3401 C  CB  . PRO   A 468 ? 1.5595 1.7455 2.0635 -0.4087 -0.0604 -0.4925 488 PRO   A CB  
3402 C  CG  . PRO   A 468 ? 1.4924 1.7556 2.0606 -0.4192 -0.0591 -0.4852 488 PRO   A CG  
3403 C  CD  . PRO   A 468 ? 1.5607 1.9008 2.1344 -0.4035 -0.1057 -0.5156 488 PRO   A CD  
3404 N  N   . VAL   A 469 ? 1.6768 1.7841 2.0263 -0.3495 -0.0965 -0.5210 489 VAL   A N   
3405 C  CA  . VAL   A 469 ? 1.7869 1.8502 2.0946 -0.3395 -0.1108 -0.5520 489 VAL   A CA  
3406 C  C   . VAL   A 469 ? 1.7652 1.7673 2.1125 -0.3755 -0.1003 -0.5758 489 VAL   A C   
3407 O  O   . VAL   A 469 ? 1.8093 1.7481 2.1587 -0.3852 -0.0678 -0.5497 489 VAL   A O   
3408 C  CB  . VAL   A 469 ? 1.7187 1.7390 1.9555 -0.3033 -0.0966 -0.5253 489 VAL   A CB  
3409 C  CG1 . VAL   A 469 ? 1.7034 1.6802 1.9003 -0.2915 -0.1085 -0.5591 489 VAL   A CG1 
3410 C  CG2 . VAL   A 469 ? 1.4583 1.5364 1.6633 -0.2716 -0.1036 -0.5007 489 VAL   A CG2 
3411 N  N   . VAL   A 470 ? 1.7346 1.7524 2.1115 -0.3945 -0.1285 -0.6260 490 VAL   A N   
3412 C  CA  . VAL   A 470 ? 1.9073 1.8671 2.3270 -0.4311 -0.1225 -0.6563 490 VAL   A CA  
3413 C  C   . VAL   A 470 ? 2.0151 1.9372 2.3826 -0.4129 -0.1454 -0.6922 490 VAL   A C   
3414 O  O   . VAL   A 470 ? 1.8879 1.8592 2.2269 -0.3922 -0.1796 -0.7146 490 VAL   A O   
3415 C  CB  . VAL   A 470 ? 1.9522 1.9624 2.4552 -0.4644 -0.1326 -0.6679 490 VAL   A CB  
3416 C  CG1 . VAL   A 470 ? 1.8294 1.8527 2.3893 -0.4886 -0.0968 -0.6329 490 VAL   A CG1 
3417 C  CG2 . VAL   A 470 ? 1.9712 2.0716 2.4727 -0.4462 -0.1757 -0.6873 490 VAL   A CG2 
3418 N  N   . LEU   A 471 ? 2.1500 1.9814 2.4992 -0.4168 -0.1248 -0.6937 491 LEU   A N   
3419 C  CA  . LEU   A 471 ? 2.2318 2.0172 2.5285 -0.3969 -0.1404 -0.7239 491 LEU   A CA  
3420 C  C   . LEU   A 471 ? 2.2410 1.9438 2.5645 -0.4236 -0.1262 -0.7335 491 LEU   A C   
3421 O  O   . LEU   A 471 ? 2.2709 1.9312 2.6329 -0.4484 -0.0944 -0.7078 491 LEU   A O   
3422 C  CB  . LEU   A 471 ? 2.1065 1.8603 2.3322 -0.3576 -0.1288 -0.7139 491 LEU   A CB  
3423 C  CG  . LEU   A 471 ? 1.9980 1.8235 2.1805 -0.3210 -0.1376 -0.6892 491 LEU   A CG  
3424 C  CD1 . LEU   A 471 ? 1.9869 1.7737 2.1094 -0.2819 -0.1167 -0.6589 491 LEU   A CD1 
3425 C  CD2 . LEU   A 471 ? 2.0091 1.8901 2.1679 -0.3093 -0.1759 -0.7320 491 LEU   A CD2 
3426 N  N   . LYS   A 472 ? 2.3027 1.9793 2.6010 -0.4174 -0.1483 -0.7696 492 LYS   A N   
3427 C  CA  . LYS   A 472 ? 2.2091 1.8004 2.5241 -0.4388 -0.1367 -0.7816 492 LYS   A CA  
3428 C  C   . LYS   A 472 ? 2.2208 1.7234 2.4851 -0.4152 -0.1100 -0.7670 492 LYS   A C   
3429 O  O   . LYS   A 472 ? 2.1405 1.6479 2.3448 -0.3765 -0.1136 -0.7685 492 LYS   A O   
3430 C  CB  . LYS   A 472 ? 2.1016 1.6952 2.4061 -0.4406 -0.1715 -0.8282 492 LYS   A CB  
3431 C  CG  . LYS   A 472 ? 2.0754 1.6251 2.4401 -0.4821 -0.1686 -0.8429 492 LYS   A CG  
3432 C  CD  . LYS   A 472 ? 2.0128 1.5592 2.3604 -0.4821 -0.2049 -0.8924 492 LYS   A CD  
3433 C  CE  . LYS   A 472 ? 2.0994 1.5720 2.3671 -0.4498 -0.2033 -0.9094 492 LYS   A CE  
3434 N  NZ  . LYS   A 472 ? 2.2441 1.7034 2.4916 -0.4515 -0.2357 -0.9587 492 LYS   A NZ  
3435 N  N   . VAL   A 473 ? 2.3087 1.7299 2.5981 -0.4367 -0.0820 -0.7513 493 VAL   A N   
3436 C  CA  . VAL   A 473 ? 2.3254 1.6554 2.5725 -0.4143 -0.0552 -0.7321 493 VAL   A CA  
3437 C  C   . VAL   A 473 ? 2.4129 1.6562 2.6565 -0.4233 -0.0548 -0.7540 493 VAL   A C   
3438 O  O   . VAL   A 473 ? 2.5459 1.7657 2.8417 -0.4616 -0.0486 -0.7555 493 VAL   A O   
3439 C  CB  . VAL   A 473 ? 2.2948 1.5942 2.5620 -0.4255 -0.0173 -0.6836 493 VAL   A CB  
3440 C  CG1 . VAL   A 473 ? 2.3178 1.5249 2.5348 -0.3948 0.0059  -0.6630 493 VAL   A CG1 
3441 C  CG2 . VAL   A 473 ? 2.2363 1.6239 2.5123 -0.4214 -0.0190 -0.6649 493 VAL   A CG2 
3442 N  N   . GLU   A 474 ? 2.4062 1.6029 2.5908 -0.3876 -0.0598 -0.7710 494 GLU   A N   
3443 C  CA  . GLU   A 474 ? 2.5841 1.6912 2.7552 -0.3891 -0.0588 -0.7921 494 GLU   A CA  
3444 C  C   . GLU   A 474 ? 2.5992 1.6161 2.7330 -0.3594 -0.0307 -0.7652 494 GLU   A C   
3445 O  O   . GLU   A 474 ? 2.4807 1.5141 2.5858 -0.3277 -0.0206 -0.7428 494 GLU   A O   
3446 C  CB  . GLU   A 474 ? 2.5666 1.6933 2.6970 -0.3706 -0.0908 -0.8407 494 GLU   A CB  
3447 C  CG  . GLU   A 474 ? 2.5475 1.7560 2.7104 -0.3969 -0.1230 -0.8694 494 GLU   A CG  
3448 C  CD  . GLU   A 474 ? 2.6371 1.8691 2.7449 -0.3718 -0.1538 -0.9129 494 GLU   A CD  
3449 O  OE1 . GLU   A 474 ? 2.6294 1.8513 2.6738 -0.3293 -0.1486 -0.9139 494 GLU   A OE1 
3450 O  OE2 . GLU   A 474 ? 2.6267 1.8870 2.7542 -0.3938 -0.1820 -0.9460 494 GLU   A OE2 
3451 N  N   . SER   A 475 ? 2.6342 1.5551 2.7701 -0.3685 -0.0193 -0.7674 495 SER   A N   
3452 C  CA  . SER   A 475 ? 2.6898 1.5152 2.7953 -0.3417 0.0070  -0.7380 495 SER   A CA  
3453 C  C   . SER   A 475 ? 2.7383 1.5128 2.7915 -0.3037 -0.0032 -0.7683 495 SER   A C   
3454 O  O   . SER   A 475 ? 2.8646 1.6177 2.9165 -0.3163 -0.0199 -0.8066 495 SER   A O   
3455 C  CB  . SER   A 475 ? 2.7660 1.5108 2.9070 -0.3752 0.0316  -0.7115 495 SER   A CB  
3456 O  OG  . SER   A 475 ? 2.8014 1.4579 2.9092 -0.3460 0.0570  -0.6745 495 SER   A OG  
3457 N  N   . ARG   A 476 ? 2.7192 1.4744 2.7311 -0.2568 0.0074  -0.7517 496 ARG   A N   
3458 C  CA  . ARG   A 476 ? 2.7809 1.4912 2.7442 -0.2148 0.0027  -0.7767 496 ARG   A CA  
3459 C  C   . ARG   A 476 ? 2.7150 1.3043 2.6711 -0.2099 0.0173  -0.7666 496 ARG   A C   
3460 O  O   . ARG   A 476 ? 2.6902 1.2325 2.6581 -0.2368 0.0105  -0.7901 496 ARG   A O   
3461 C  CB  . ARG   A 476 ? 2.6822 1.4288 2.6134 -0.1646 0.0089  -0.7630 496 ARG   A CB  
3462 C  CG  . ARG   A 476 ? 2.6198 1.4810 2.5599 -0.1678 -0.0013 -0.7624 496 ARG   A CG  
3463 C  CD  . ARG   A 476 ? 2.5450 1.4371 2.4621 -0.1197 0.0076  -0.7458 496 ARG   A CD  
3464 N  NE  . ARG   A 476 ? 2.5179 1.4178 2.3950 -0.0803 0.0025  -0.7766 496 ARG   A NE  
3465 C  CZ  . ARG   A 476 ? 2.4752 1.3873 2.3344 -0.0325 0.0126  -0.7678 496 ARG   A CZ  
3466 N  NH1 . ARG   A 476 ? 2.3810 1.2973 2.2579 -0.0160 0.0237  -0.7304 496 ARG   A NH1 
3467 N  NH2 . ARG   A 476 ? 2.4501 1.3711 2.2742 0.0002  0.0121  -0.7966 496 ARG   A NH2 
3468 C  CHA . HEM   B .   ? 1.2217 1.2496 1.2696 0.0209  -0.0765 -0.1470 601 HEM   A CHA 
3469 C  CHB . HEM   B .   ? 1.2343 1.2877 1.2986 -0.0020 -0.0393 -0.1782 601 HEM   A CHB 
3470 C  CHC . HEM   B .   ? 1.3796 1.2469 1.3514 -0.0005 -0.0417 -0.1679 601 HEM   A CHC 
3471 C  CHD . HEM   B .   ? 1.4666 1.3105 1.3743 0.0429  -0.0816 -0.1287 601 HEM   A CHD 
3472 C  C1A . HEM   B .   ? 1.1703 1.2210 1.2361 0.0127  -0.0636 -0.1530 601 HEM   A C1A 
3473 C  C2A . HEM   B .   ? 1.2038 1.2983 1.2999 0.0082  -0.0543 -0.1546 601 HEM   A C2A 
3474 C  C3A . HEM   B .   ? 1.0925 1.1944 1.1880 0.0036  -0.0440 -0.1621 601 HEM   A C3A 
3475 C  C4A . HEM   B .   ? 1.1924 1.2550 1.2637 0.0028  -0.0465 -0.1669 601 HEM   A C4A 
3476 C  CMA . HEM   B .   ? 0.9931 1.1327 1.1041 0.0013  -0.0307 -0.1650 601 HEM   A CMA 
3477 C  CAA . HEM   B .   ? 1.0603 1.1821 1.1812 0.0095  -0.0552 -0.1486 601 HEM   A CAA 
3478 C  CBA . HEM   B .   ? 0.8075 0.9419 0.9699 0.0203  -0.0611 -0.1545 601 HEM   A CBA 
3479 C  CGA . HEM   B .   ? 1.0205 1.1814 1.2140 0.0174  -0.0563 -0.1489 601 HEM   A CGA 
3480 O  O1A . HEM   B .   ? 1.1391 1.3188 1.3771 0.0217  -0.0537 -0.1525 601 HEM   A O1A 
3481 O  O2A . HEM   B .   ? 0.8926 1.0551 1.0699 0.0109  -0.0532 -0.1405 601 HEM   A O2A 
3482 C  C1B . HEM   B .   ? 1.2971 1.3067 1.3402 -0.0043 -0.0398 -0.1821 601 HEM   A C1B 
3483 C  C2B . HEM   B .   ? 1.3187 1.3145 1.3557 -0.0113 -0.0329 -0.1970 601 HEM   A C2B 
3484 C  C3B . HEM   B .   ? 1.2600 1.2038 1.2766 -0.0128 -0.0335 -0.1950 601 HEM   A C3B 
3485 C  C4B . HEM   B .   ? 1.2543 1.1782 1.2568 -0.0043 -0.0409 -0.1777 601 HEM   A C4B 
3486 C  CMB . HEM   B .   ? 1.3380 1.3695 1.3848 -0.0145 -0.0259 -0.2120 601 HEM   A CMB 
3487 C  CAB . HEM   B .   ? 1.4244 1.3274 1.4295 -0.0207 -0.0274 -0.2084 601 HEM   A CAB 
3488 C  CBB . HEM   B .   ? 1.3677 1.2836 1.3806 -0.0245 -0.0236 -0.2287 601 HEM   A CBB 
3489 C  C1C . HEM   B .   ? 1.4924 1.3360 1.4399 0.0123  -0.0505 -0.1526 601 HEM   A C1C 
3490 C  C2C . HEM   B .   ? 1.5389 1.3166 1.4447 0.0237  -0.0526 -0.1406 601 HEM   A C2C 
3491 C  C3C . HEM   B .   ? 1.4775 1.2485 1.3605 0.0376  -0.0642 -0.1289 601 HEM   A C3C 
3492 C  C4C . HEM   B .   ? 1.4402 1.2726 1.3559 0.0331  -0.0691 -0.1341 601 HEM   A C4C 
3493 C  CMC . HEM   B .   ? 1.6062 1.3255 1.4933 0.0217  -0.0431 -0.1416 601 HEM   A CMC 
3494 C  CAC . HEM   B .   ? 1.5414 1.2438 1.3664 0.0565  -0.0702 -0.1124 601 HEM   A CAC 
3495 C  CBC . HEM   B .   ? 1.7197 1.4142 1.5161 0.0747  -0.0866 -0.1044 601 HEM   A CBC 
3496 C  C1D . HEM   B .   ? 1.3765 1.2722 1.3184 0.0394  -0.0862 -0.1339 601 HEM   A C1D 
3497 C  C2D . HEM   B .   ? 1.3660 1.2688 1.2996 0.0476  -0.0983 -0.1308 601 HEM   A C2D 
3498 C  C3D . HEM   B .   ? 1.3366 1.2898 1.3139 0.0398  -0.0968 -0.1368 601 HEM   A C3D 
3499 C  C4D . HEM   B .   ? 1.2042 1.1846 1.2128 0.0286  -0.0838 -0.1428 601 HEM   A C4D 
3500 C  CMD . HEM   B .   ? 1.3935 1.2484 1.2708 0.0641  -0.1100 -0.1221 601 HEM   A CMD 
3501 C  CAD . HEM   B .   ? 1.1631 1.1375 1.1529 0.0433  -0.1069 -0.1380 601 HEM   A CAD 
3502 C  CBD . HEM   B .   ? 1.1898 1.1691 1.2088 0.0606  -0.1332 -0.1489 601 HEM   A CBD 
3503 C  CGD . HEM   B .   ? 1.2661 1.2576 1.2980 0.0646  -0.1477 -0.1538 601 HEM   A CGD 
3504 O  O1D . HEM   B .   ? 1.1546 1.1430 1.2034 0.0800  -0.1750 -0.1647 601 HEM   A O1D 
3505 O  O2D . HEM   B .   ? 1.0710 1.0749 1.0988 0.0533  -0.1338 -0.1486 601 HEM   A O2D 
3506 N  NA  . HEM   B .   ? 1.2409 1.2720 1.2938 0.0087  -0.0571 -0.1590 601 HEM   A NA  
3507 N  NB  . HEM   B .   ? 1.2792 1.2452 1.2994 0.0003  -0.0461 -0.1724 601 HEM   A NB  
3508 N  NC  . HEM   B .   ? 1.3870 1.2612 1.3406 0.0181  -0.0594 -0.1465 601 HEM   A NC  
3509 N  ND  . HEM   B .   ? 1.3022 1.2472 1.2889 0.0284  -0.0788 -0.1429 601 HEM   A ND  
3510 FE FE  . HEM   B .   ? 1.3823 1.3400 1.3900 0.0145  -0.0617 -0.1554 601 HEM   A FE  
3511 C  C11 . A1A4S C .   ? 1.6055 1.7379 1.6280 -0.0378 0.0109  -0.1023 602 A1A4S A C11 
3512 C  C13 . A1A4S C .   ? 1.6387 1.6214 1.5323 -0.0184 0.0346  -0.0796 602 A1A4S A C13 
3513 C  C14 . A1A4S C .   ? 1.5781 1.5493 1.4760 -0.0364 0.0523  -0.0772 602 A1A4S A C14 
3514 C  C15 . A1A4S C .   ? 1.6397 1.6429 1.5929 -0.0746 0.0772  -0.0839 602 A1A4S A C15 
3515 C  C16 . A1A4S C .   ? 1.5736 1.5171 1.4889 -0.0737 0.0853  -0.0759 602 A1A4S A C16 
3516 C  C17 . A1A4S C .   ? 1.5931 1.4919 1.4572 -0.0512 0.0750  -0.0676 602 A1A4S A C17 
3517 C  C18 . A1A4S C .   ? 1.6366 1.5517 1.4939 -0.0330 0.0569  -0.0700 602 A1A4S A C18 
3518 C  C19 . A1A4S C .   ? 1.6069 1.6216 1.5496 -0.0556 0.0623  -0.0828 602 A1A4S A C19 
3519 C  C20 . A1A4S C .   ? 1.3980 1.5264 1.4320 -0.0097 -0.0153 -0.0997 602 A1A4S A C20 
3520 C  C23 . A1A4S C .   ? 1.7508 1.9258 1.7950 -0.0371 0.0150  -0.0992 602 A1A4S A C23 
3521 C  C01 . A1A4S C .   ? 1.4727 1.3865 1.3880 -0.0298 0.0027  -0.1053 602 A1A4S A C01 
3522 C  C02 . A1A4S C .   ? 1.4854 1.4010 1.3832 -0.0148 -0.0054 -0.0979 602 A1A4S A C02 
3523 C  C03 . A1A4S C .   ? 1.4009 1.3672 1.3331 -0.0124 -0.0155 -0.1045 602 A1A4S A C03 
3524 C  C05 . A1A4S C .   ? 1.5829 1.5649 1.4984 -0.0116 -0.0001 -0.0926 602 A1A4S A C05 
3525 C  C06 . A1A4S C .   ? 1.6237 1.6366 1.5513 -0.0169 0.0139  -0.0889 602 A1A4S A C06 
3526 C  C08 . A1A4S C .   ? 1.6740 1.7517 1.6563 -0.0038 -0.0078 -0.0946 602 A1A4S A C08 
3527 C  C09 . A1A4S C .   ? 1.5469 1.6403 1.5505 -0.0113 -0.0120 -0.0997 602 A1A4S A C09 
3528 C  C21 . A1A4S C .   ? 1.4116 1.5535 1.4613 -0.0130 -0.0177 -0.1052 602 A1A4S A C21 
3529 C  C24 . A1A4S C .   ? 1.2438 1.1887 1.1918 -0.0276 -0.0097 -0.1194 602 A1A4S A C24 
3530 C  C25 . A1A4S C .   ? 1.1492 1.1396 1.1275 -0.0414 -0.0045 -0.1284 602 A1A4S A C25 
3531 C  C26 . A1A4S C .   ? 1.3149 1.3288 1.3135 -0.0367 -0.0123 -0.1398 602 A1A4S A C26 
3532 C  C27 . A1A4S C .   ? 1.3934 1.3896 1.3917 -0.0201 -0.0234 -0.1425 602 A1A4S A C27 
3533 C  C29 . A1A4S C .   ? 1.3831 1.3116 1.3297 -0.0098 -0.0258 -0.1233 602 A1A4S A C29 
3534 C  C30 . A1A4S C .   ? 1.7235 1.9111 1.7733 -0.0245 0.0099  -0.0938 602 A1A4S A C30 
3535 C  C32 . A1A4S C .   ? 1.6800 1.9311 1.7644 -0.0306 0.0195  -0.0936 602 A1A4S A C32 
3536 C  C33 . A1A4S C .   ? 1.7283 1.9726 1.8146 -0.0466 0.0249  -0.1011 602 A1A4S A C33 
3537 C  C34 . A1A4S C .   ? 1.7692 1.9715 1.8325 -0.0497 0.0238  -0.1029 602 A1A4S A C34 
3538 C  C35 . A1A4S C .   ? 1.3303 1.4541 1.3747 -0.0146 -0.0212 -0.1126 602 A1A4S A C35 
3539 C  C36 . A1A4S C .   ? 1.3680 1.5150 1.4299 -0.0152 -0.0195 -0.1170 602 A1A4S A C36 
3540 C  C38 . A1A4S C .   ? 1.2738 1.4470 1.3426 -0.0125 -0.0147 -0.1034 602 A1A4S A C38 
3541 C  C39 . A1A4S C .   ? 1.3184 1.4048 1.3414 -0.0134 -0.0248 -0.1150 602 A1A4S A C39 
3542 C  C40 . A1A4S C .   ? 1.3378 1.4098 1.3612 -0.0127 -0.0280 -0.1224 602 A1A4S A C40 
3543 C  C41 . A1A4S C .   ? 1.3889 1.4867 1.4339 -0.0136 -0.0262 -0.1294 602 A1A4S A C41 
3544 C  C42 . A1A4S C .   ? 1.4419 1.5767 1.5036 -0.0148 -0.0213 -0.1262 602 A1A4S A C42 
3545 N  N04 . A1A4S C .   ? 1.5285 1.5253 1.4705 -0.0209 -0.0030 -0.1004 602 A1A4S A N04 
3546 N  N10 . A1A4S C .   ? 1.6018 1.7013 1.6064 -0.0252 -0.0007 -0.1015 602 A1A4S A N10 
3547 N  N28 . A1A4S C .   ? 1.3259 1.2825 1.3021 -0.0074 -0.0313 -0.1350 602 A1A4S A N28 
3548 N  N31 . A1A4S C .   ? 1.6862 1.9077 1.7532 -0.0216 0.0133  -0.0902 602 A1A4S A N31 
3549 N  N37 . A1A4S C .   ? 1.3861 1.5615 1.4594 -0.0139 -0.0150 -0.1105 602 A1A4S A N37 
3550 O  O12 . A1A4S C .   ? 1.5777 1.5216 1.4594 0.0026  -0.0098 -0.0901 602 A1A4S A O12 
3551 O  O22 . A1A4S C .   ? 1.5722 1.6986 1.5961 -0.0499 0.0165  -0.1071 602 A1A4S A O22 
3552 S  S07 . A1A4S C .   ? 1.8490 1.8751 1.7817 -0.0007 -0.0010 -0.0909 602 A1A4S A S07 
# 
