data_9GBL
# 
_entry.id   9GBL 
# 
_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   9GBL         pdb_00009gbl 10.2210/pdb9gbl/pdb 
WWPDB D_1292139094 ?            ?                   
# 
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 2025-01-22 ? 
2 'Structure model' 1 1 2025-03-19 ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Database references' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' citation        
2 2 'Structure model' citation_author 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 2 'Structure model' '_citation.journal_volume'          
2 2 'Structure model' '_citation.page_first'              
3 2 'Structure model' '_citation.page_last'               
4 2 'Structure model' '_citation_author.identifier_ORCID' 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9GBL 
_pdbx_database_status.recvd_initial_deposition_date   2024-07-31 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_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              bsskra@bath.ac.uk 
_pdbx_contact_author.name_first         K.Ravi 
_pdbx_contact_author.name_last          Acharya 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-3009-4058 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Gregory, K.S.' 1 ? 
'Acharya, K.R.' 2 ? 
'Cozier, G.E.'  3 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Febs J.' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           1742-464X 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            292 
_citation.language                  ? 
_citation.page_first                1141 
_citation.page_last                 1158 
_citation.title                     
'Molecular basis of human angiotensin-1 converting enzyme inhibition by a series of diprolyl-derived compounds.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1111/febs.17384 
_citation.pdbx_database_id_PubMed   39763019 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Gregory, K.S.'  1 ? 
primary 'Cozier, G.E.'   2 ? 
primary 'Fienberg, S.'   3 ? 
primary 'Chibale, K.'    4 ? 
primary 'Sturrock, E.D.' 5 ? 
primary 'Acharya, K.R.'  6 ? 
# 
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 'Angiotensin-converting enzyme' 68861.875 1   3.2.1.-,3.4.15.1 ? ? g13-tACE 
2 branched    man 
;beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose
;
732.682   1   ?                ? ? ?        
3 non-polymer syn 'ZINC ION' 65.409    1   ?                ? ? ?        
4 non-polymer syn 'CHLORIDE ION' 35.453    2   ?                ? ? ?        
5 non-polymer syn 
;(2S)-1-[(2S)-2-[[(1S)-1-[(2S)-1-(4-carboxyphenyl)carbonylpyrrolidin-2-yl]-2-oxidanyl-2-oxidanylidene-ethyl]amino]propanoyl]pyrrolidine-2-carboxylic acid
;
461.465   1   ?                ? ? ?        
6 water       nat water 18.015    158 ?                ? ? ?        
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'ACE,Dipeptidyl carboxypeptidase I,Kininase II' 
# 
_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       
;LVTDEAEASKFVEEYDRTSQVVWNEYAGANWNYNTNITTETSKILLQKNMQIAQHTLKYGTQARKFDVNQLQNTTIKRII
KKVQDLERAALPAQELEEYNKILLDMETTYSVATVCHPQGSCLQLEPDLTNVMATSRKYEDLLWAWEGWRDKAGRAILQF
YPKYVELINQAARLNGYVDAGDSWRSMYETPSLEQDLERLFQELQPLYLNLHAYVRRALHRHYGAQHINLEGPIPAHLLG
NMWAQTWSNIYDLVVPFPSAPSMDTTEAMLKQGWTPRRMFKEADDFFTSLGLLPVPPEFWQKSMLEKPTDGREVVCHASA
WDFYNGKDFRIKQCTTVNLEDLVVAHHEMGHIQYFMQYKDLPVALREGANPGFHEAIGDVLALSVSTPKHLHSLNLLSSE
GGSDEHDINFLMKMALDKIAFIPFSYLVDQWRWRVFDGSITKENYNQEWWSLRLKYQGLCPPVPRTQGDFDPGAKFHIPS
SVPYIRYFVSFIIQFQFHEALCQAAGHTGPLHKCDIYQSKEAGQRLATAMKLGFSRPWPEAMQLITGQPQMSASAMLSYF
KPLLDWLRTENELHGEKLGWPQYNWTPNSARSEGPLP
;
_entity_poly.pdbx_seq_one_letter_code_can   
;LVTDEAEASKFVEEYDRTSQVVWNEYAGANWNYNTNITTETSKILLQKNMQIAQHTLKYGTQARKFDVNQLQNTTIKRII
KKVQDLERAALPAQELEEYNKILLDMETTYSVATVCHPQGSCLQLEPDLTNVMATSRKYEDLLWAWEGWRDKAGRAILQF
YPKYVELINQAARLNGYVDAGDSWRSMYETPSLEQDLERLFQELQPLYLNLHAYVRRALHRHYGAQHINLEGPIPAHLLG
NMWAQTWSNIYDLVVPFPSAPSMDTTEAMLKQGWTPRRMFKEADDFFTSLGLLPVPPEFWQKSMLEKPTDGREVVCHASA
WDFYNGKDFRIKQCTTVNLEDLVVAHHEMGHIQYFMQYKDLPVALREGANPGFHEAIGDVLALSVSTPKHLHSLNLLSSE
GGSDEHDINFLMKMALDKIAFIPFSYLVDQWRWRVFDGSITKENYNQEWWSLRLKYQGLCPPVPRTQGDFDPGAKFHIPS
SVPYIRYFVSFIIQFQFHEALCQAAGHTGPLHKCDIYQSKEAGQRLATAMKLGFSRPWPEAMQLITGQPQMSASAMLSYF
KPLLDWLRTENELHGEKLGWPQYNWTPNSARSEGPLP
;
_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 
3 'ZINC ION' ZN    
4 'CHLORIDE ION' CL    
5 
;(2S)-1-[(2S)-2-[[(1S)-1-[(2S)-1-(4-carboxyphenyl)carbonylpyrrolidin-2-yl]-2-oxidanyl-2-oxidanylidene-ethyl]amino]propanoyl]pyrrolidine-2-carboxylic acid
;
A1IJY 
6 water HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   LEU n 
1 2   VAL n 
1 3   THR n 
1 4   ASP n 
1 5   GLU n 
1 6   ALA n 
1 7   GLU n 
1 8   ALA n 
1 9   SER n 
1 10  LYS n 
1 11  PHE n 
1 12  VAL n 
1 13  GLU n 
1 14  GLU n 
1 15  TYR n 
1 16  ASP n 
1 17  ARG n 
1 18  THR n 
1 19  SER n 
1 20  GLN n 
1 21  VAL n 
1 22  VAL n 
1 23  TRP n 
1 24  ASN n 
1 25  GLU n 
1 26  TYR n 
1 27  ALA n 
1 28  GLY n 
1 29  ALA n 
1 30  ASN n 
1 31  TRP n 
1 32  ASN n 
1 33  TYR n 
1 34  ASN n 
1 35  THR n 
1 36  ASN n 
1 37  ILE n 
1 38  THR n 
1 39  THR n 
1 40  GLU n 
1 41  THR n 
1 42  SER n 
1 43  LYS n 
1 44  ILE n 
1 45  LEU n 
1 46  LEU n 
1 47  GLN n 
1 48  LYS n 
1 49  ASN n 
1 50  MET n 
1 51  GLN n 
1 52  ILE n 
1 53  ALA n 
1 54  GLN n 
1 55  HIS n 
1 56  THR n 
1 57  LEU n 
1 58  LYS n 
1 59  TYR n 
1 60  GLY n 
1 61  THR n 
1 62  GLN n 
1 63  ALA n 
1 64  ARG n 
1 65  LYS n 
1 66  PHE n 
1 67  ASP n 
1 68  VAL n 
1 69  ASN n 
1 70  GLN n 
1 71  LEU n 
1 72  GLN n 
1 73  ASN n 
1 74  THR n 
1 75  THR n 
1 76  ILE n 
1 77  LYS n 
1 78  ARG n 
1 79  ILE n 
1 80  ILE n 
1 81  LYS n 
1 82  LYS n 
1 83  VAL n 
1 84  GLN n 
1 85  ASP n 
1 86  LEU n 
1 87  GLU n 
1 88  ARG n 
1 89  ALA n 
1 90  ALA n 
1 91  LEU n 
1 92  PRO n 
1 93  ALA n 
1 94  GLN n 
1 95  GLU n 
1 96  LEU n 
1 97  GLU n 
1 98  GLU n 
1 99  TYR n 
1 100 ASN n 
1 101 LYS n 
1 102 ILE n 
1 103 LEU n 
1 104 LEU n 
1 105 ASP n 
1 106 MET n 
1 107 GLU n 
1 108 THR n 
1 109 THR n 
1 110 TYR n 
1 111 SER n 
1 112 VAL n 
1 113 ALA n 
1 114 THR n 
1 115 VAL n 
1 116 CYS n 
1 117 HIS n 
1 118 PRO n 
1 119 GLN n 
1 120 GLY n 
1 121 SER n 
1 122 CYS n 
1 123 LEU n 
1 124 GLN n 
1 125 LEU n 
1 126 GLU n 
1 127 PRO n 
1 128 ASP n 
1 129 LEU n 
1 130 THR n 
1 131 ASN n 
1 132 VAL n 
1 133 MET n 
1 134 ALA n 
1 135 THR n 
1 136 SER n 
1 137 ARG n 
1 138 LYS n 
1 139 TYR n 
1 140 GLU n 
1 141 ASP n 
1 142 LEU n 
1 143 LEU n 
1 144 TRP n 
1 145 ALA n 
1 146 TRP n 
1 147 GLU n 
1 148 GLY n 
1 149 TRP n 
1 150 ARG n 
1 151 ASP n 
1 152 LYS n 
1 153 ALA n 
1 154 GLY n 
1 155 ARG n 
1 156 ALA n 
1 157 ILE n 
1 158 LEU n 
1 159 GLN n 
1 160 PHE n 
1 161 TYR n 
1 162 PRO n 
1 163 LYS n 
1 164 TYR n 
1 165 VAL n 
1 166 GLU n 
1 167 LEU n 
1 168 ILE n 
1 169 ASN n 
1 170 GLN n 
1 171 ALA n 
1 172 ALA n 
1 173 ARG n 
1 174 LEU n 
1 175 ASN n 
1 176 GLY n 
1 177 TYR n 
1 178 VAL n 
1 179 ASP n 
1 180 ALA n 
1 181 GLY n 
1 182 ASP n 
1 183 SER n 
1 184 TRP n 
1 185 ARG n 
1 186 SER n 
1 187 MET n 
1 188 TYR n 
1 189 GLU n 
1 190 THR n 
1 191 PRO n 
1 192 SER n 
1 193 LEU n 
1 194 GLU n 
1 195 GLN n 
1 196 ASP n 
1 197 LEU n 
1 198 GLU n 
1 199 ARG n 
1 200 LEU n 
1 201 PHE n 
1 202 GLN n 
1 203 GLU n 
1 204 LEU n 
1 205 GLN n 
1 206 PRO n 
1 207 LEU n 
1 208 TYR n 
1 209 LEU n 
1 210 ASN n 
1 211 LEU n 
1 212 HIS n 
1 213 ALA n 
1 214 TYR n 
1 215 VAL n 
1 216 ARG n 
1 217 ARG n 
1 218 ALA n 
1 219 LEU n 
1 220 HIS n 
1 221 ARG n 
1 222 HIS n 
1 223 TYR n 
1 224 GLY n 
1 225 ALA n 
1 226 GLN n 
1 227 HIS n 
1 228 ILE n 
1 229 ASN n 
1 230 LEU n 
1 231 GLU n 
1 232 GLY n 
1 233 PRO n 
1 234 ILE n 
1 235 PRO n 
1 236 ALA n 
1 237 HIS n 
1 238 LEU n 
1 239 LEU n 
1 240 GLY n 
1 241 ASN n 
1 242 MET n 
1 243 TRP n 
1 244 ALA n 
1 245 GLN n 
1 246 THR n 
1 247 TRP n 
1 248 SER n 
1 249 ASN n 
1 250 ILE n 
1 251 TYR n 
1 252 ASP n 
1 253 LEU n 
1 254 VAL n 
1 255 VAL n 
1 256 PRO n 
1 257 PHE n 
1 258 PRO n 
1 259 SER n 
1 260 ALA n 
1 261 PRO n 
1 262 SER n 
1 263 MET n 
1 264 ASP n 
1 265 THR n 
1 266 THR n 
1 267 GLU n 
1 268 ALA n 
1 269 MET n 
1 270 LEU n 
1 271 LYS n 
1 272 GLN n 
1 273 GLY n 
1 274 TRP n 
1 275 THR n 
1 276 PRO n 
1 277 ARG n 
1 278 ARG n 
1 279 MET n 
1 280 PHE n 
1 281 LYS n 
1 282 GLU n 
1 283 ALA n 
1 284 ASP n 
1 285 ASP n 
1 286 PHE n 
1 287 PHE n 
1 288 THR n 
1 289 SER n 
1 290 LEU n 
1 291 GLY n 
1 292 LEU n 
1 293 LEU n 
1 294 PRO n 
1 295 VAL n 
1 296 PRO n 
1 297 PRO n 
1 298 GLU n 
1 299 PHE n 
1 300 TRP n 
1 301 GLN n 
1 302 LYS n 
1 303 SER n 
1 304 MET n 
1 305 LEU n 
1 306 GLU n 
1 307 LYS n 
1 308 PRO n 
1 309 THR n 
1 310 ASP n 
1 311 GLY n 
1 312 ARG n 
1 313 GLU n 
1 314 VAL n 
1 315 VAL n 
1 316 CYS n 
1 317 HIS n 
1 318 ALA n 
1 319 SER n 
1 320 ALA n 
1 321 TRP n 
1 322 ASP n 
1 323 PHE n 
1 324 TYR n 
1 325 ASN n 
1 326 GLY n 
1 327 LYS n 
1 328 ASP n 
1 329 PHE n 
1 330 ARG n 
1 331 ILE n 
1 332 LYS n 
1 333 GLN n 
1 334 CYS n 
1 335 THR n 
1 336 THR n 
1 337 VAL n 
1 338 ASN n 
1 339 LEU n 
1 340 GLU n 
1 341 ASP n 
1 342 LEU n 
1 343 VAL n 
1 344 VAL n 
1 345 ALA n 
1 346 HIS n 
1 347 HIS n 
1 348 GLU n 
1 349 MET n 
1 350 GLY n 
1 351 HIS n 
1 352 ILE n 
1 353 GLN n 
1 354 TYR n 
1 355 PHE n 
1 356 MET n 
1 357 GLN n 
1 358 TYR n 
1 359 LYS n 
1 360 ASP n 
1 361 LEU n 
1 362 PRO n 
1 363 VAL n 
1 364 ALA n 
1 365 LEU n 
1 366 ARG n 
1 367 GLU n 
1 368 GLY n 
1 369 ALA n 
1 370 ASN n 
1 371 PRO n 
1 372 GLY n 
1 373 PHE n 
1 374 HIS n 
1 375 GLU n 
1 376 ALA n 
1 377 ILE n 
1 378 GLY n 
1 379 ASP n 
1 380 VAL n 
1 381 LEU n 
1 382 ALA n 
1 383 LEU n 
1 384 SER n 
1 385 VAL n 
1 386 SER n 
1 387 THR n 
1 388 PRO n 
1 389 LYS n 
1 390 HIS n 
1 391 LEU n 
1 392 HIS n 
1 393 SER n 
1 394 LEU n 
1 395 ASN n 
1 396 LEU n 
1 397 LEU n 
1 398 SER n 
1 399 SER n 
1 400 GLU n 
1 401 GLY n 
1 402 GLY n 
1 403 SER n 
1 404 ASP n 
1 405 GLU n 
1 406 HIS n 
1 407 ASP n 
1 408 ILE n 
1 409 ASN n 
1 410 PHE n 
1 411 LEU n 
1 412 MET n 
1 413 LYS n 
1 414 MET n 
1 415 ALA n 
1 416 LEU n 
1 417 ASP n 
1 418 LYS n 
1 419 ILE n 
1 420 ALA n 
1 421 PHE n 
1 422 ILE n 
1 423 PRO n 
1 424 PHE n 
1 425 SER n 
1 426 TYR n 
1 427 LEU n 
1 428 VAL n 
1 429 ASP n 
1 430 GLN n 
1 431 TRP n 
1 432 ARG n 
1 433 TRP n 
1 434 ARG n 
1 435 VAL n 
1 436 PHE n 
1 437 ASP n 
1 438 GLY n 
1 439 SER n 
1 440 ILE n 
1 441 THR n 
1 442 LYS n 
1 443 GLU n 
1 444 ASN n 
1 445 TYR n 
1 446 ASN n 
1 447 GLN n 
1 448 GLU n 
1 449 TRP n 
1 450 TRP n 
1 451 SER n 
1 452 LEU n 
1 453 ARG n 
1 454 LEU n 
1 455 LYS n 
1 456 TYR n 
1 457 GLN n 
1 458 GLY n 
1 459 LEU n 
1 460 CYS n 
1 461 PRO n 
1 462 PRO n 
1 463 VAL n 
1 464 PRO n 
1 465 ARG n 
1 466 THR n 
1 467 GLN n 
1 468 GLY n 
1 469 ASP n 
1 470 PHE n 
1 471 ASP n 
1 472 PRO n 
1 473 GLY n 
1 474 ALA n 
1 475 LYS n 
1 476 PHE n 
1 477 HIS n 
1 478 ILE n 
1 479 PRO n 
1 480 SER n 
1 481 SER n 
1 482 VAL n 
1 483 PRO n 
1 484 TYR n 
1 485 ILE n 
1 486 ARG n 
1 487 TYR n 
1 488 PHE n 
1 489 VAL n 
1 490 SER n 
1 491 PHE n 
1 492 ILE n 
1 493 ILE n 
1 494 GLN n 
1 495 PHE n 
1 496 GLN n 
1 497 PHE n 
1 498 HIS n 
1 499 GLU n 
1 500 ALA n 
1 501 LEU n 
1 502 CYS n 
1 503 GLN n 
1 504 ALA n 
1 505 ALA n 
1 506 GLY n 
1 507 HIS n 
1 508 THR n 
1 509 GLY n 
1 510 PRO n 
1 511 LEU n 
1 512 HIS n 
1 513 LYS n 
1 514 CYS n 
1 515 ASP n 
1 516 ILE n 
1 517 TYR n 
1 518 GLN n 
1 519 SER n 
1 520 LYS n 
1 521 GLU n 
1 522 ALA n 
1 523 GLY n 
1 524 GLN n 
1 525 ARG n 
1 526 LEU n 
1 527 ALA n 
1 528 THR n 
1 529 ALA n 
1 530 MET n 
1 531 LYS n 
1 532 LEU n 
1 533 GLY n 
1 534 PHE n 
1 535 SER n 
1 536 ARG n 
1 537 PRO n 
1 538 TRP n 
1 539 PRO n 
1 540 GLU n 
1 541 ALA n 
1 542 MET n 
1 543 GLN n 
1 544 LEU n 
1 545 ILE n 
1 546 THR n 
1 547 GLY n 
1 548 GLN n 
1 549 PRO n 
1 550 GLN n 
1 551 MET n 
1 552 SER n 
1 553 ALA n 
1 554 SER n 
1 555 ALA n 
1 556 MET n 
1 557 LEU n 
1 558 SER n 
1 559 TYR n 
1 560 PHE n 
1 561 LYS n 
1 562 PRO n 
1 563 LEU n 
1 564 LEU n 
1 565 ASP n 
1 566 TRP n 
1 567 LEU n 
1 568 ARG n 
1 569 THR n 
1 570 GLU n 
1 571 ASN n 
1 572 GLU n 
1 573 LEU n 
1 574 HIS n 
1 575 GLY n 
1 576 GLU n 
1 577 LYS n 
1 578 LEU n 
1 579 GLY n 
1 580 TRP n 
1 581 PRO n 
1 582 GLN n 
1 583 TYR n 
1 584 ASN n 
1 585 TRP n 
1 586 THR n 
1 587 PRO n 
1 588 ASN n 
1 589 SER n 
1 590 ALA n 
1 591 ARG n 
1 592 SER n 
1 593 GLU n 
1 594 GLY n 
1 595 PRO n 
1 596 LEU n 
1 597 PRO 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                   597 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'ACE, DCP, DCP1' 
_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      'Cricetulus griseus' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     10029 
_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              ? 
_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          ? 
_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                   ? 
# 
_pdbx_entity_branch.entity_id   2 
_pdbx_entity_branch.type        oligosaccharide 
# 
loop_
_pdbx_entity_branch_descriptor.ordinal 
_pdbx_entity_branch_descriptor.entity_id 
_pdbx_entity_branch_descriptor.descriptor 
_pdbx_entity_branch_descriptor.type 
_pdbx_entity_branch_descriptor.program 
_pdbx_entity_branch_descriptor.program_version 
1 2 'DManpb1-4DGlcpNAcb1-4[LFucpa1-6]DGlcpNAcb1-ROH'                                                    
'Glycam Condensed Sequence' GMML       1.0   
2 2 'WURCS=2.0/3,4,3/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5][a1221m-1a_1-5]/1-1-2-3/a4-b1_a6-d1_b4-c1' WURCS PDB2Glycan 1.1.0 
3 2 '[][D-1-deoxy-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{}}[(6+1)][a-L-Fucp]{}}'               LINUCS PDB-CARE   ?     
# 
loop_
_pdbx_entity_branch_link.link_id 
_pdbx_entity_branch_link.entity_id 
_pdbx_entity_branch_link.entity_branch_list_num_1 
_pdbx_entity_branch_link.comp_id_1 
_pdbx_entity_branch_link.atom_id_1 
_pdbx_entity_branch_link.leaving_atom_id_1 
_pdbx_entity_branch_link.entity_branch_list_num_2 
_pdbx_entity_branch_link.comp_id_2 
_pdbx_entity_branch_link.atom_id_2 
_pdbx_entity_branch_link.leaving_atom_id_2 
_pdbx_entity_branch_link.value_order 
_pdbx_entity_branch_link.details 
1 2 2 NAG C1 O1 1 NAG O4 HO4 sing ? 
2 2 3 BMA C1 O1 2 NAG O4 HO4 sing ? 
3 2 4 FUC C1 O1 1 NAG O6 HO6 sing ? 
# 
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 
A1IJY non-polymer                   . 
;(2S)-1-[(2S)-2-[[(1S)-1-[(2S)-1-(4-carboxyphenyl)carbonylpyrrolidin-2-yl]-2-oxidanyl-2-oxidanylidene-ethyl]amino]propanoyl]pyrrolidine-2-carboxylic acid
;
? 'C22 H27 N3 O8'  461.465 
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 
BMA   'D-saccharide, beta linking'  . beta-D-mannopyranose 'beta-D-mannose; D-mannose; mannose' 'C6 H12 O6'      180.156 
CL    non-polymer                   . 'CHLORIDE ION' ? 'Cl -1'          35.453  
CYS   'L-peptide linking'           y CYSTEINE ? 'C3 H7 N O2 S'   121.158 
FUC   'L-saccharide, alpha linking' . alpha-L-fucopyranose 'alpha-L-fucose; 6-deoxy-alpha-L-galactopyranose; L-fucose; fucose' 
'C6 H12 O5'      164.156 
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  
HIS   'L-peptide linking'           y HISTIDINE ? 'C6 H10 N3 O2 1' 156.162 
HOH   non-polymer                   . WATER ? 'H2 O'           18.015  
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 
NAG   'D-saccharide, beta linking'  . 2-acetamido-2-deoxy-beta-D-glucopyranose 
;N-acetyl-beta-D-glucosamine; 2-acetamido-2-deoxy-beta-D-glucose; 2-acetamido-2-deoxy-D-glucose; 2-acetamido-2-deoxy-glucose; N-ACETYL-D-GLUCOSAMINE
;
'C8 H15 N O6'    221.208 
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 
ZN    non-polymer                   . 'ZINC ION' ? 'Zn 2'           65.409  
# 
loop_
_pdbx_chem_comp_identifier.comp_id 
_pdbx_chem_comp_identifier.type 
_pdbx_chem_comp_identifier.program 
_pdbx_chem_comp_identifier.program_version 
_pdbx_chem_comp_identifier.identifier 
BMA 'CONDENSED IUPAC CARBOHYDRATE SYMBOL' GMML     1.0 DManpb                         
BMA 'COMMON NAME'                         GMML     1.0 b-D-mannopyranose              
BMA 'IUPAC CARBOHYDRATE SYMBOL'           PDB-CARE 1.0 b-D-Manp                       
BMA 'SNFG CARBOHYDRATE SYMBOL'            GMML     1.0 Man                            
FUC 'CONDENSED IUPAC CARBOHYDRATE SYMBOL' GMML     1.0 LFucpa                         
FUC 'COMMON NAME'                         GMML     1.0 a-L-fucopyranose               
FUC 'IUPAC CARBOHYDRATE SYMBOL'           PDB-CARE 1.0 a-L-Fucp                       
FUC 'SNFG CARBOHYDRATE SYMBOL'            GMML     1.0 Fuc                            
NAG 'CONDENSED IUPAC CARBOHYDRATE SYMBOL' GMML     1.0 DGlcpNAcb                      
NAG 'COMMON NAME'                         GMML     1.0 N-acetyl-b-D-glucopyranosamine 
NAG 'IUPAC CARBOHYDRATE SYMBOL'           PDB-CARE 1.0 b-D-GlcpNAc                    
NAG 'SNFG CARBOHYDRATE SYMBOL'            GMML     1.0 GlcNAc                         
# 
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   LEU 1   37  ?   ?   ?   A . n 
A 1 2   VAL 2   38  ?   ?   ?   A . n 
A 1 3   THR 3   39  ?   ?   ?   A . n 
A 1 4   ASP 4   40  40  ASP ASP A . n 
A 1 5   GLU 5   41  41  GLU GLU A . n 
A 1 6   ALA 6   42  42  ALA ALA A . n 
A 1 7   GLU 7   43  43  GLU GLU A . n 
A 1 8   ALA 8   44  44  ALA ALA A . n 
A 1 9   SER 9   45  45  SER SER A . n 
A 1 10  LYS 10  46  46  LYS LYS A . n 
A 1 11  PHE 11  47  47  PHE PHE A . n 
A 1 12  VAL 12  48  48  VAL VAL A . n 
A 1 13  GLU 13  49  49  GLU GLU A . n 
A 1 14  GLU 14  50  50  GLU GLU A . n 
A 1 15  TYR 15  51  51  TYR TYR A . n 
A 1 16  ASP 16  52  52  ASP ASP A . n 
A 1 17  ARG 17  53  53  ARG ARG A . n 
A 1 18  THR 18  54  54  THR THR A . n 
A 1 19  SER 19  55  55  SER SER A . n 
A 1 20  GLN 20  56  56  GLN GLN A . n 
A 1 21  VAL 21  57  57  VAL VAL A . n 
A 1 22  VAL 22  58  58  VAL VAL A . n 
A 1 23  TRP 23  59  59  TRP TRP A . n 
A 1 24  ASN 24  60  60  ASN ASN A . n 
A 1 25  GLU 25  61  61  GLU GLU A . n 
A 1 26  TYR 26  62  62  TYR TYR A . n 
A 1 27  ALA 27  63  63  ALA ALA A . n 
A 1 28  GLY 28  64  64  GLY GLY A . n 
A 1 29  ALA 29  65  65  ALA ALA A . n 
A 1 30  ASN 30  66  66  ASN ASN A . n 
A 1 31  TRP 31  67  67  TRP TRP A . n 
A 1 32  ASN 32  68  68  ASN ASN A . n 
A 1 33  TYR 33  69  69  TYR TYR A . n 
A 1 34  ASN 34  70  70  ASN ASN A . n 
A 1 35  THR 35  71  71  THR THR A . n 
A 1 36  ASN 36  72  72  ASN ASN A . n 
A 1 37  ILE 37  73  73  ILE ILE A . n 
A 1 38  THR 38  74  74  THR THR A . n 
A 1 39  THR 39  75  75  THR THR A . n 
A 1 40  GLU 40  76  76  GLU GLU A . n 
A 1 41  THR 41  77  77  THR THR A . n 
A 1 42  SER 42  78  78  SER SER A . n 
A 1 43  LYS 43  79  79  LYS LYS A . n 
A 1 44  ILE 44  80  80  ILE ILE A . n 
A 1 45  LEU 45  81  81  LEU LEU A . n 
A 1 46  LEU 46  82  82  LEU LEU A . n 
A 1 47  GLN 47  83  83  GLN GLN A . n 
A 1 48  LYS 48  84  84  LYS LYS A . n 
A 1 49  ASN 49  85  85  ASN ASN A . n 
A 1 50  MET 50  86  86  MET MET A . n 
A 1 51  GLN 51  87  87  GLN GLN A . n 
A 1 52  ILE 52  88  88  ILE ILE A . n 
A 1 53  ALA 53  89  89  ALA ALA A . n 
A 1 54  GLN 54  90  90  GLN GLN A . n 
A 1 55  HIS 55  91  91  HIS HIS A . n 
A 1 56  THR 56  92  92  THR THR A . n 
A 1 57  LEU 57  93  93  LEU LEU A . n 
A 1 58  LYS 58  94  94  LYS LYS A . n 
A 1 59  TYR 59  95  95  TYR TYR A . n 
A 1 60  GLY 60  96  96  GLY GLY A . n 
A 1 61  THR 61  97  97  THR THR A . n 
A 1 62  GLN 62  98  98  GLN GLN A . n 
A 1 63  ALA 63  99  99  ALA ALA A . n 
A 1 64  ARG 64  100 100 ARG ARG A . n 
A 1 65  LYS 65  101 101 LYS LYS A . n 
A 1 66  PHE 66  102 102 PHE PHE A . n 
A 1 67  ASP 67  103 103 ASP ASP A . n 
A 1 68  VAL 68  104 104 VAL VAL A . n 
A 1 69  ASN 69  105 105 ASN ASN A . n 
A 1 70  GLN 70  106 106 GLN GLN A . n 
A 1 71  LEU 71  107 107 LEU LEU A . n 
A 1 72  GLN 72  108 108 GLN GLN A . n 
A 1 73  ASN 73  109 109 ASN ASN A . n 
A 1 74  THR 74  110 110 THR THR A . n 
A 1 75  THR 75  111 111 THR THR A . n 
A 1 76  ILE 76  112 112 ILE ILE A . n 
A 1 77  LYS 77  113 113 LYS LYS A . n 
A 1 78  ARG 78  114 114 ARG ARG A . n 
A 1 79  ILE 79  115 115 ILE ILE A . n 
A 1 80  ILE 80  116 116 ILE ILE A . n 
A 1 81  LYS 81  117 117 LYS LYS A . n 
A 1 82  LYS 82  118 118 LYS LYS A . n 
A 1 83  VAL 83  119 119 VAL VAL A . n 
A 1 84  GLN 84  120 120 GLN GLN A . n 
A 1 85  ASP 85  121 121 ASP ASP A . n 
A 1 86  LEU 86  122 122 LEU LEU A . n 
A 1 87  GLU 87  123 123 GLU GLU A . n 
A 1 88  ARG 88  124 124 ARG ARG A . n 
A 1 89  ALA 89  125 125 ALA ALA A . n 
A 1 90  ALA 90  126 126 ALA ALA A . n 
A 1 91  LEU 91  127 127 LEU LEU A . n 
A 1 92  PRO 92  128 128 PRO PRO A . n 
A 1 93  ALA 93  129 129 ALA ALA A . n 
A 1 94  GLN 94  130 130 GLN GLN A . n 
A 1 95  GLU 95  131 131 GLU GLU A . n 
A 1 96  LEU 96  132 132 LEU LEU A . n 
A 1 97  GLU 97  133 133 GLU GLU A . n 
A 1 98  GLU 98  134 134 GLU GLU A . n 
A 1 99  TYR 99  135 135 TYR TYR A . n 
A 1 100 ASN 100 136 136 ASN ASN A . n 
A 1 101 LYS 101 137 137 LYS LYS A . n 
A 1 102 ILE 102 138 138 ILE ILE A . n 
A 1 103 LEU 103 139 139 LEU LEU A . n 
A 1 104 LEU 104 140 140 LEU LEU A . n 
A 1 105 ASP 105 141 141 ASP ASP A . n 
A 1 106 MET 106 142 142 MET MET A . n 
A 1 107 GLU 107 143 143 GLU GLU A . n 
A 1 108 THR 108 144 144 THR THR A . n 
A 1 109 THR 109 145 145 THR THR A . n 
A 1 110 TYR 110 146 146 TYR TYR A . n 
A 1 111 SER 111 147 147 SER SER A . n 
A 1 112 VAL 112 148 148 VAL VAL A . n 
A 1 113 ALA 113 149 149 ALA ALA A . n 
A 1 114 THR 114 150 150 THR THR A . n 
A 1 115 VAL 115 151 151 VAL VAL A . n 
A 1 116 CYS 116 152 152 CYS CYS A . n 
A 1 117 HIS 117 153 153 HIS HIS A . n 
A 1 118 PRO 118 154 154 PRO PRO A . n 
A 1 119 GLN 119 155 155 GLN GLN A . n 
A 1 120 GLY 120 156 156 GLY GLY A . n 
A 1 121 SER 121 157 157 SER SER A . n 
A 1 122 CYS 122 158 158 CYS CYS A . n 
A 1 123 LEU 123 159 159 LEU LEU A . n 
A 1 124 GLN 124 160 160 GLN GLN A . n 
A 1 125 LEU 125 161 161 LEU LEU A . n 
A 1 126 GLU 126 162 162 GLU GLU A . n 
A 1 127 PRO 127 163 163 PRO PRO A . n 
A 1 128 ASP 128 164 164 ASP ASP A . n 
A 1 129 LEU 129 165 165 LEU LEU A . n 
A 1 130 THR 130 166 166 THR THR A . n 
A 1 131 ASN 131 167 167 ASN ASN A . n 
A 1 132 VAL 132 168 168 VAL VAL A . n 
A 1 133 MET 133 169 169 MET MET A . n 
A 1 134 ALA 134 170 170 ALA ALA A . n 
A 1 135 THR 135 171 171 THR THR A . n 
A 1 136 SER 136 172 172 SER SER A . n 
A 1 137 ARG 137 173 173 ARG ARG A . n 
A 1 138 LYS 138 174 174 LYS LYS A . n 
A 1 139 TYR 139 175 175 TYR TYR A . n 
A 1 140 GLU 140 176 176 GLU GLU A . n 
A 1 141 ASP 141 177 177 ASP ASP A . n 
A 1 142 LEU 142 178 178 LEU LEU A . n 
A 1 143 LEU 143 179 179 LEU LEU A . n 
A 1 144 TRP 144 180 180 TRP TRP A . n 
A 1 145 ALA 145 181 181 ALA ALA A . n 
A 1 146 TRP 146 182 182 TRP TRP A . n 
A 1 147 GLU 147 183 183 GLU GLU A . n 
A 1 148 GLY 148 184 184 GLY GLY A . n 
A 1 149 TRP 149 185 185 TRP TRP A . n 
A 1 150 ARG 150 186 186 ARG ARG A . n 
A 1 151 ASP 151 187 187 ASP ASP A . n 
A 1 152 LYS 152 188 188 LYS LYS A . n 
A 1 153 ALA 153 189 189 ALA ALA A . n 
A 1 154 GLY 154 190 190 GLY GLY A . n 
A 1 155 ARG 155 191 191 ARG ARG A . n 
A 1 156 ALA 156 192 192 ALA ALA A . n 
A 1 157 ILE 157 193 193 ILE ILE A . n 
A 1 158 LEU 158 194 194 LEU LEU A . n 
A 1 159 GLN 159 195 195 GLN GLN A . n 
A 1 160 PHE 160 196 196 PHE PHE A . n 
A 1 161 TYR 161 197 197 TYR TYR A . n 
A 1 162 PRO 162 198 198 PRO PRO A . n 
A 1 163 LYS 163 199 199 LYS LYS A . n 
A 1 164 TYR 164 200 200 TYR TYR A . n 
A 1 165 VAL 165 201 201 VAL VAL A . n 
A 1 166 GLU 166 202 202 GLU GLU A . n 
A 1 167 LEU 167 203 203 LEU LEU A . n 
A 1 168 ILE 168 204 204 ILE ILE A . n 
A 1 169 ASN 169 205 205 ASN ASN A . n 
A 1 170 GLN 170 206 206 GLN GLN A . n 
A 1 171 ALA 171 207 207 ALA ALA A . n 
A 1 172 ALA 172 208 208 ALA ALA A . n 
A 1 173 ARG 173 209 209 ARG ARG A . n 
A 1 174 LEU 174 210 210 LEU LEU A . n 
A 1 175 ASN 175 211 211 ASN ASN A . n 
A 1 176 GLY 176 212 212 GLY GLY A . n 
A 1 177 TYR 177 213 213 TYR TYR A . n 
A 1 178 VAL 178 214 214 VAL VAL A . n 
A 1 179 ASP 179 215 215 ASP ASP A . n 
A 1 180 ALA 180 216 216 ALA ALA A . n 
A 1 181 GLY 181 217 217 GLY GLY A . n 
A 1 182 ASP 182 218 218 ASP ASP A . n 
A 1 183 SER 183 219 219 SER SER A . n 
A 1 184 TRP 184 220 220 TRP TRP A . n 
A 1 185 ARG 185 221 221 ARG ARG A . n 
A 1 186 SER 186 222 222 SER SER A . n 
A 1 187 MET 187 223 223 MET MET A . n 
A 1 188 TYR 188 224 224 TYR TYR A . n 
A 1 189 GLU 189 225 225 GLU GLU A . n 
A 1 190 THR 190 226 226 THR THR A . n 
A 1 191 PRO 191 227 227 PRO PRO A . n 
A 1 192 SER 192 228 228 SER SER A . n 
A 1 193 LEU 193 229 229 LEU LEU A . n 
A 1 194 GLU 194 230 230 GLU GLU A . n 
A 1 195 GLN 195 231 231 GLN GLN A . n 
A 1 196 ASP 196 232 232 ASP ASP A . n 
A 1 197 LEU 197 233 233 LEU LEU A . n 
A 1 198 GLU 198 234 234 GLU GLU A . n 
A 1 199 ARG 199 235 235 ARG ARG A . n 
A 1 200 LEU 200 236 236 LEU LEU A . n 
A 1 201 PHE 201 237 237 PHE PHE A . n 
A 1 202 GLN 202 238 238 GLN GLN A . n 
A 1 203 GLU 203 239 239 GLU GLU A . n 
A 1 204 LEU 204 240 240 LEU LEU A . n 
A 1 205 GLN 205 241 241 GLN GLN A . n 
A 1 206 PRO 206 242 242 PRO PRO A . n 
A 1 207 LEU 207 243 243 LEU LEU A . n 
A 1 208 TYR 208 244 244 TYR TYR A . n 
A 1 209 LEU 209 245 245 LEU LEU A . n 
A 1 210 ASN 210 246 246 ASN ASN A . n 
A 1 211 LEU 211 247 247 LEU LEU A . n 
A 1 212 HIS 212 248 248 HIS HIS A . n 
A 1 213 ALA 213 249 249 ALA ALA A . n 
A 1 214 TYR 214 250 250 TYR TYR A . n 
A 1 215 VAL 215 251 251 VAL VAL A . n 
A 1 216 ARG 216 252 252 ARG ARG A . n 
A 1 217 ARG 217 253 253 ARG ARG A . n 
A 1 218 ALA 218 254 254 ALA ALA A . n 
A 1 219 LEU 219 255 255 LEU LEU A . n 
A 1 220 HIS 220 256 256 HIS HIS A . n 
A 1 221 ARG 221 257 257 ARG ARG A . n 
A 1 222 HIS 222 258 258 HIS HIS A . n 
A 1 223 TYR 223 259 259 TYR TYR A . n 
A 1 224 GLY 224 260 260 GLY GLY A . n 
A 1 225 ALA 225 261 261 ALA ALA A . n 
A 1 226 GLN 226 262 262 GLN GLN A . n 
A 1 227 HIS 227 263 263 HIS HIS A . n 
A 1 228 ILE 228 264 264 ILE ILE A . n 
A 1 229 ASN 229 265 265 ASN ASN A . n 
A 1 230 LEU 230 266 266 LEU LEU A . n 
A 1 231 GLU 231 267 267 GLU GLU A . n 
A 1 232 GLY 232 268 268 GLY GLY A . n 
A 1 233 PRO 233 269 269 PRO PRO A . n 
A 1 234 ILE 234 270 270 ILE ILE A . n 
A 1 235 PRO 235 271 271 PRO PRO A . n 
A 1 236 ALA 236 272 272 ALA ALA A . n 
A 1 237 HIS 237 273 273 HIS HIS A . n 
A 1 238 LEU 238 274 274 LEU LEU A . n 
A 1 239 LEU 239 275 275 LEU LEU A . n 
A 1 240 GLY 240 276 276 GLY GLY A . n 
A 1 241 ASN 241 277 277 ASN ASN A . n 
A 1 242 MET 242 278 278 MET MET A . n 
A 1 243 TRP 243 279 279 TRP TRP A . n 
A 1 244 ALA 244 280 280 ALA ALA A . n 
A 1 245 GLN 245 281 281 GLN GLN A . n 
A 1 246 THR 246 282 282 THR THR A . n 
A 1 247 TRP 247 283 283 TRP TRP A . n 
A 1 248 SER 248 284 284 SER SER A . n 
A 1 249 ASN 249 285 285 ASN ASN A . n 
A 1 250 ILE 250 286 286 ILE ILE A . n 
A 1 251 TYR 251 287 287 TYR TYR A . n 
A 1 252 ASP 252 288 288 ASP ASP A . n 
A 1 253 LEU 253 289 289 LEU LEU A . n 
A 1 254 VAL 254 290 290 VAL VAL A . n 
A 1 255 VAL 255 291 291 VAL VAL A . n 
A 1 256 PRO 256 292 292 PRO PRO A . n 
A 1 257 PHE 257 293 293 PHE PHE A . n 
A 1 258 PRO 258 294 294 PRO PRO A . n 
A 1 259 SER 259 295 295 SER SER A . n 
A 1 260 ALA 260 296 296 ALA ALA A . n 
A 1 261 PRO 261 297 297 PRO PRO A . n 
A 1 262 SER 262 298 298 SER SER A . n 
A 1 263 MET 263 299 299 MET MET A . n 
A 1 264 ASP 264 300 300 ASP ASP A . n 
A 1 265 THR 265 301 301 THR THR A . n 
A 1 266 THR 266 302 302 THR THR A . n 
A 1 267 GLU 267 303 303 GLU GLU A . n 
A 1 268 ALA 268 304 304 ALA ALA A . n 
A 1 269 MET 269 305 305 MET MET A . n 
A 1 270 LEU 270 306 306 LEU LEU A . n 
A 1 271 LYS 271 307 307 LYS LYS A . n 
A 1 272 GLN 272 308 308 GLN GLN A . n 
A 1 273 GLY 273 309 309 GLY GLY A . n 
A 1 274 TRP 274 310 310 TRP TRP A . n 
A 1 275 THR 275 311 311 THR THR A . n 
A 1 276 PRO 276 312 312 PRO PRO A . n 
A 1 277 ARG 277 313 313 ARG ARG A . n 
A 1 278 ARG 278 314 314 ARG ARG A . n 
A 1 279 MET 279 315 315 MET MET A . n 
A 1 280 PHE 280 316 316 PHE PHE A . n 
A 1 281 LYS 281 317 317 LYS LYS A . n 
A 1 282 GLU 282 318 318 GLU GLU A . n 
A 1 283 ALA 283 319 319 ALA ALA A . n 
A 1 284 ASP 284 320 320 ASP ASP A . n 
A 1 285 ASP 285 321 321 ASP ASP A . n 
A 1 286 PHE 286 322 322 PHE PHE A . n 
A 1 287 PHE 287 323 323 PHE PHE A . n 
A 1 288 THR 288 324 324 THR THR A . n 
A 1 289 SER 289 325 325 SER SER A . n 
A 1 290 LEU 290 326 326 LEU LEU A . n 
A 1 291 GLY 291 327 327 GLY GLY A . n 
A 1 292 LEU 292 328 328 LEU LEU A . n 
A 1 293 LEU 293 329 329 LEU LEU A . n 
A 1 294 PRO 294 330 330 PRO PRO A . n 
A 1 295 VAL 295 331 331 VAL VAL A . n 
A 1 296 PRO 296 332 332 PRO PRO A . n 
A 1 297 PRO 297 333 333 PRO PRO A . n 
A 1 298 GLU 298 334 334 GLU GLU A . n 
A 1 299 PHE 299 335 335 PHE PHE A . n 
A 1 300 TRP 300 336 336 TRP TRP A . n 
A 1 301 GLN 301 337 337 GLN GLN A . n 
A 1 302 LYS 302 338 338 LYS LYS A . n 
A 1 303 SER 303 339 339 SER SER A . n 
A 1 304 MET 304 340 340 MET MET A . n 
A 1 305 LEU 305 341 341 LEU LEU A . n 
A 1 306 GLU 306 342 342 GLU GLU A . n 
A 1 307 LYS 307 343 343 LYS LYS A . n 
A 1 308 PRO 308 344 344 PRO PRO A . n 
A 1 309 THR 309 345 345 THR THR A . n 
A 1 310 ASP 310 346 346 ASP ASP A . n 
A 1 311 GLY 311 347 347 GLY GLY A . n 
A 1 312 ARG 312 348 348 ARG ARG A . n 
A 1 313 GLU 313 349 ?   ?   ?   A . n 
A 1 314 VAL 314 350 350 VAL VAL A . n 
A 1 315 VAL 315 351 351 VAL VAL A . n 
A 1 316 CYS 316 352 352 CYS CYS A . n 
A 1 317 HIS 317 353 353 HIS HIS A . n 
A 1 318 ALA 318 354 354 ALA ALA A . n 
A 1 319 SER 319 355 355 SER SER A . n 
A 1 320 ALA 320 356 356 ALA ALA A . n 
A 1 321 TRP 321 357 357 TRP TRP A . n 
A 1 322 ASP 322 358 358 ASP ASP A . n 
A 1 323 PHE 323 359 359 PHE PHE A . n 
A 1 324 TYR 324 360 360 TYR TYR A . n 
A 1 325 ASN 325 361 361 ASN ASN A . n 
A 1 326 GLY 326 362 362 GLY GLY A . n 
A 1 327 LYS 327 363 363 LYS LYS A . n 
A 1 328 ASP 328 364 364 ASP ASP A . n 
A 1 329 PHE 329 365 365 PHE PHE A . n 
A 1 330 ARG 330 366 366 ARG ARG A . n 
A 1 331 ILE 331 367 367 ILE ILE A . n 
A 1 332 LYS 332 368 368 LYS LYS A . n 
A 1 333 GLN 333 369 369 GLN GLN A . n 
A 1 334 CYS 334 370 370 CYS CYS A . n 
A 1 335 THR 335 371 371 THR THR A . n 
A 1 336 THR 336 372 372 THR THR A . n 
A 1 337 VAL 337 373 373 VAL VAL A . n 
A 1 338 ASN 338 374 374 ASN ASN A . n 
A 1 339 LEU 339 375 375 LEU LEU A . n 
A 1 340 GLU 340 376 376 GLU GLU A . n 
A 1 341 ASP 341 377 377 ASP ASP A . n 
A 1 342 LEU 342 378 378 LEU LEU A . n 
A 1 343 VAL 343 379 379 VAL VAL A . n 
A 1 344 VAL 344 380 380 VAL VAL A . n 
A 1 345 ALA 345 381 381 ALA ALA A . n 
A 1 346 HIS 346 382 382 HIS HIS A . n 
A 1 347 HIS 347 383 383 HIS HIS A . n 
A 1 348 GLU 348 384 384 GLU GLU A . n 
A 1 349 MET 349 385 385 MET MET A . n 
A 1 350 GLY 350 386 386 GLY GLY A . n 
A 1 351 HIS 351 387 387 HIS HIS A . n 
A 1 352 ILE 352 388 388 ILE ILE A . n 
A 1 353 GLN 353 389 389 GLN GLN A . n 
A 1 354 TYR 354 390 390 TYR TYR A . n 
A 1 355 PHE 355 391 391 PHE PHE A . n 
A 1 356 MET 356 392 392 MET MET A . n 
A 1 357 GLN 357 393 393 GLN GLN A . n 
A 1 358 TYR 358 394 394 TYR TYR A . n 
A 1 359 LYS 359 395 395 LYS LYS A . n 
A 1 360 ASP 360 396 396 ASP ASP A . n 
A 1 361 LEU 361 397 397 LEU LEU A . n 
A 1 362 PRO 362 398 398 PRO PRO A . n 
A 1 363 VAL 363 399 399 VAL VAL A . n 
A 1 364 ALA 364 400 400 ALA ALA A . n 
A 1 365 LEU 365 401 401 LEU LEU A . n 
A 1 366 ARG 366 402 402 ARG ARG A . n 
A 1 367 GLU 367 403 403 GLU GLU A . n 
A 1 368 GLY 368 404 404 GLY GLY A . n 
A 1 369 ALA 369 405 405 ALA ALA A . n 
A 1 370 ASN 370 406 406 ASN ASN A . n 
A 1 371 PRO 371 407 407 PRO PRO A . n 
A 1 372 GLY 372 408 408 GLY GLY A . n 
A 1 373 PHE 373 409 409 PHE PHE A . n 
A 1 374 HIS 374 410 410 HIS HIS A . n 
A 1 375 GLU 375 411 411 GLU GLU A . n 
A 1 376 ALA 376 412 412 ALA ALA A . n 
A 1 377 ILE 377 413 413 ILE ILE A . n 
A 1 378 GLY 378 414 414 GLY GLY A . n 
A 1 379 ASP 379 415 415 ASP ASP A . n 
A 1 380 VAL 380 416 416 VAL VAL A . n 
A 1 381 LEU 381 417 417 LEU LEU A . n 
A 1 382 ALA 382 418 418 ALA ALA A . n 
A 1 383 LEU 383 419 419 LEU LEU A . n 
A 1 384 SER 384 420 420 SER SER A . n 
A 1 385 VAL 385 421 421 VAL VAL A . n 
A 1 386 SER 386 422 422 SER SER A . n 
A 1 387 THR 387 423 423 THR THR A . n 
A 1 388 PRO 388 424 424 PRO PRO A . n 
A 1 389 LYS 389 425 425 LYS LYS A . n 
A 1 390 HIS 390 426 426 HIS HIS A . n 
A 1 391 LEU 391 427 427 LEU LEU A . n 
A 1 392 HIS 392 428 428 HIS HIS A . n 
A 1 393 SER 393 429 429 SER SER A . n 
A 1 394 LEU 394 430 430 LEU LEU A . n 
A 1 395 ASN 395 431 431 ASN ASN A . n 
A 1 396 LEU 396 432 432 LEU LEU A . n 
A 1 397 LEU 397 433 433 LEU LEU A . n 
A 1 398 SER 398 434 434 SER SER A . n 
A 1 399 SER 399 435 435 SER SER A . n 
A 1 400 GLU 400 436 ?   ?   ?   A . n 
A 1 401 GLY 401 437 ?   ?   ?   A . n 
A 1 402 GLY 402 438 438 GLY GLY A . n 
A 1 403 SER 403 439 439 SER SER A . n 
A 1 404 ASP 404 440 440 ASP ASP A . n 
A 1 405 GLU 405 441 441 GLU GLU A . n 
A 1 406 HIS 406 442 442 HIS HIS A . n 
A 1 407 ASP 407 443 443 ASP ASP A . n 
A 1 408 ILE 408 444 444 ILE ILE A . n 
A 1 409 ASN 409 445 445 ASN ASN A . n 
A 1 410 PHE 410 446 446 PHE PHE A . n 
A 1 411 LEU 411 447 447 LEU LEU A . n 
A 1 412 MET 412 448 448 MET MET A . n 
A 1 413 LYS 413 449 449 LYS LYS A . n 
A 1 414 MET 414 450 450 MET MET A . n 
A 1 415 ALA 415 451 451 ALA ALA A . n 
A 1 416 LEU 416 452 452 LEU LEU A . n 
A 1 417 ASP 417 453 453 ASP ASP A . n 
A 1 418 LYS 418 454 454 LYS LYS A . n 
A 1 419 ILE 419 455 455 ILE ILE A . n 
A 1 420 ALA 420 456 456 ALA ALA A . n 
A 1 421 PHE 421 457 457 PHE PHE A . n 
A 1 422 ILE 422 458 458 ILE ILE A . n 
A 1 423 PRO 423 459 459 PRO PRO A . n 
A 1 424 PHE 424 460 460 PHE PHE A . n 
A 1 425 SER 425 461 461 SER SER A . n 
A 1 426 TYR 426 462 462 TYR TYR A . n 
A 1 427 LEU 427 463 463 LEU LEU A . n 
A 1 428 VAL 428 464 464 VAL VAL A . n 
A 1 429 ASP 429 465 465 ASP ASP A . n 
A 1 430 GLN 430 466 466 GLN GLN A . n 
A 1 431 TRP 431 467 467 TRP TRP A . n 
A 1 432 ARG 432 468 468 ARG ARG A . n 
A 1 433 TRP 433 469 469 TRP TRP A . n 
A 1 434 ARG 434 470 470 ARG ARG A . n 
A 1 435 VAL 435 471 471 VAL VAL A . n 
A 1 436 PHE 436 472 472 PHE PHE A . n 
A 1 437 ASP 437 473 473 ASP ASP A . n 
A 1 438 GLY 438 474 474 GLY GLY A . n 
A 1 439 SER 439 475 475 SER SER A . n 
A 1 440 ILE 440 476 476 ILE ILE A . n 
A 1 441 THR 441 477 477 THR THR A . n 
A 1 442 LYS 442 478 478 LYS LYS A . n 
A 1 443 GLU 443 479 479 GLU GLU A . n 
A 1 444 ASN 444 480 480 ASN ASN A . n 
A 1 445 TYR 445 481 481 TYR TYR A . n 
A 1 446 ASN 446 482 482 ASN ASN A . n 
A 1 447 GLN 447 483 483 GLN GLN A . n 
A 1 448 GLU 448 484 484 GLU GLU A . n 
A 1 449 TRP 449 485 485 TRP TRP A . n 
A 1 450 TRP 450 486 486 TRP TRP A . n 
A 1 451 SER 451 487 487 SER SER A . n 
A 1 452 LEU 452 488 488 LEU LEU A . n 
A 1 453 ARG 453 489 489 ARG ARG A . n 
A 1 454 LEU 454 490 490 LEU LEU A . n 
A 1 455 LYS 455 491 491 LYS LYS A . n 
A 1 456 TYR 456 492 492 TYR TYR A . n 
A 1 457 GLN 457 493 493 GLN GLN A . n 
A 1 458 GLY 458 494 494 GLY GLY A . n 
A 1 459 LEU 459 495 495 LEU LEU A . n 
A 1 460 CYS 460 496 496 CYS CYS A . n 
A 1 461 PRO 461 497 497 PRO PRO A . n 
A 1 462 PRO 462 498 498 PRO PRO A . n 
A 1 463 VAL 463 499 499 VAL VAL A . n 
A 1 464 PRO 464 500 500 PRO PRO A . n 
A 1 465 ARG 465 501 501 ARG ARG A . n 
A 1 466 THR 466 502 502 THR THR A . n 
A 1 467 GLN 467 503 503 GLN GLN A . n 
A 1 468 GLY 468 504 504 GLY GLY A . n 
A 1 469 ASP 469 505 505 ASP ASP A . n 
A 1 470 PHE 470 506 506 PHE PHE A . n 
A 1 471 ASP 471 507 507 ASP ASP A . n 
A 1 472 PRO 472 508 508 PRO PRO A . n 
A 1 473 GLY 473 509 509 GLY GLY A . n 
A 1 474 ALA 474 510 510 ALA ALA A . n 
A 1 475 LYS 475 511 511 LYS LYS A . n 
A 1 476 PHE 476 512 512 PHE PHE A . n 
A 1 477 HIS 477 513 513 HIS HIS A . n 
A 1 478 ILE 478 514 514 ILE ILE A . n 
A 1 479 PRO 479 515 515 PRO PRO A . n 
A 1 480 SER 480 516 516 SER SER A . n 
A 1 481 SER 481 517 517 SER SER A . n 
A 1 482 VAL 482 518 518 VAL VAL A . n 
A 1 483 PRO 483 519 519 PRO PRO A . n 
A 1 484 TYR 484 520 520 TYR TYR A . n 
A 1 485 ILE 485 521 521 ILE ILE A . n 
A 1 486 ARG 486 522 522 ARG ARG A . n 
A 1 487 TYR 487 523 523 TYR TYR A . n 
A 1 488 PHE 488 524 524 PHE PHE A . n 
A 1 489 VAL 489 525 525 VAL VAL A . n 
A 1 490 SER 490 526 526 SER SER A . n 
A 1 491 PHE 491 527 527 PHE PHE A . n 
A 1 492 ILE 492 528 528 ILE ILE A . n 
A 1 493 ILE 493 529 529 ILE ILE A . n 
A 1 494 GLN 494 530 530 GLN GLN A . n 
A 1 495 PHE 495 531 531 PHE PHE A . n 
A 1 496 GLN 496 532 532 GLN GLN A . n 
A 1 497 PHE 497 533 533 PHE PHE A . n 
A 1 498 HIS 498 534 534 HIS HIS A . n 
A 1 499 GLU 499 535 535 GLU GLU A . n 
A 1 500 ALA 500 536 536 ALA ALA A . n 
A 1 501 LEU 501 537 537 LEU LEU A . n 
A 1 502 CYS 502 538 538 CYS CYS A . n 
A 1 503 GLN 503 539 539 GLN GLN A . n 
A 1 504 ALA 504 540 540 ALA ALA A . n 
A 1 505 ALA 505 541 541 ALA ALA A . n 
A 1 506 GLY 506 542 542 GLY GLY A . n 
A 1 507 HIS 507 543 543 HIS HIS A . n 
A 1 508 THR 508 544 544 THR THR A . n 
A 1 509 GLY 509 545 545 GLY GLY A . n 
A 1 510 PRO 510 546 546 PRO PRO A . n 
A 1 511 LEU 511 547 547 LEU LEU A . n 
A 1 512 HIS 512 548 548 HIS HIS A . n 
A 1 513 LYS 513 549 549 LYS LYS A . n 
A 1 514 CYS 514 550 550 CYS CYS A . n 
A 1 515 ASP 515 551 551 ASP ASP A . n 
A 1 516 ILE 516 552 552 ILE ILE A . n 
A 1 517 TYR 517 553 553 TYR TYR A . n 
A 1 518 GLN 518 554 554 GLN GLN A . n 
A 1 519 SER 519 555 555 SER SER A . n 
A 1 520 LYS 520 556 556 LYS LYS A . n 
A 1 521 GLU 521 557 557 GLU GLU A . n 
A 1 522 ALA 522 558 558 ALA ALA A . n 
A 1 523 GLY 523 559 559 GLY GLY A . n 
A 1 524 GLN 524 560 560 GLN GLN A . n 
A 1 525 ARG 525 561 561 ARG ARG A . n 
A 1 526 LEU 526 562 562 LEU LEU A . n 
A 1 527 ALA 527 563 563 ALA ALA A . n 
A 1 528 THR 528 564 564 THR THR A . n 
A 1 529 ALA 529 565 565 ALA ALA A . n 
A 1 530 MET 530 566 566 MET MET A . n 
A 1 531 LYS 531 567 567 LYS LYS A . n 
A 1 532 LEU 532 568 568 LEU LEU A . n 
A 1 533 GLY 533 569 569 GLY GLY A . n 
A 1 534 PHE 534 570 570 PHE PHE A . n 
A 1 535 SER 535 571 571 SER SER A . n 
A 1 536 ARG 536 572 572 ARG ARG A . n 
A 1 537 PRO 537 573 573 PRO PRO A . n 
A 1 538 TRP 538 574 574 TRP TRP A . n 
A 1 539 PRO 539 575 575 PRO PRO A . n 
A 1 540 GLU 540 576 576 GLU GLU A . n 
A 1 541 ALA 541 577 577 ALA ALA A . n 
A 1 542 MET 542 578 578 MET MET A . n 
A 1 543 GLN 543 579 579 GLN GLN A . n 
A 1 544 LEU 544 580 580 LEU LEU A . n 
A 1 545 ILE 545 581 581 ILE ILE A . n 
A 1 546 THR 546 582 582 THR THR A . n 
A 1 547 GLY 547 583 583 GLY GLY A . n 
A 1 548 GLN 548 584 584 GLN GLN A . n 
A 1 549 PRO 549 585 585 PRO PRO A . n 
A 1 550 GLN 550 586 586 GLN GLN A . n 
A 1 551 MET 551 587 587 MET MET A . n 
A 1 552 SER 552 588 588 SER SER A . n 
A 1 553 ALA 553 589 589 ALA ALA A . n 
A 1 554 SER 554 590 590 SER SER A . n 
A 1 555 ALA 555 591 591 ALA ALA A . n 
A 1 556 MET 556 592 592 MET MET A . n 
A 1 557 LEU 557 593 593 LEU LEU A . n 
A 1 558 SER 558 594 594 SER SER A . n 
A 1 559 TYR 559 595 595 TYR TYR A . n 
A 1 560 PHE 560 596 596 PHE PHE A . n 
A 1 561 LYS 561 597 597 LYS LYS A . n 
A 1 562 PRO 562 598 598 PRO PRO A . n 
A 1 563 LEU 563 599 599 LEU LEU A . n 
A 1 564 LEU 564 600 600 LEU LEU A . n 
A 1 565 ASP 565 601 601 ASP ASP A . n 
A 1 566 TRP 566 602 602 TRP TRP A . n 
A 1 567 LEU 567 603 603 LEU LEU A . n 
A 1 568 ARG 568 604 604 ARG ARG A . n 
A 1 569 THR 569 605 605 THR THR A . n 
A 1 570 GLU 570 606 606 GLU GLU A . n 
A 1 571 ASN 571 607 607 ASN ASN A . n 
A 1 572 GLU 572 608 608 GLU GLU A . n 
A 1 573 LEU 573 609 609 LEU LEU A . n 
A 1 574 HIS 574 610 610 HIS HIS A . n 
A 1 575 GLY 575 611 611 GLY GLY A . n 
A 1 576 GLU 576 612 612 GLU GLU A . n 
A 1 577 LYS 577 613 613 LYS LYS A . n 
A 1 578 LEU 578 614 614 LEU LEU A . n 
A 1 579 GLY 579 615 615 GLY GLY A . n 
A 1 580 TRP 580 616 616 TRP TRP A . n 
A 1 581 PRO 581 617 617 PRO PRO A . n 
A 1 582 GLN 582 618 ?   ?   ?   A . n 
A 1 583 TYR 583 619 ?   ?   ?   A . n 
A 1 584 ASN 584 620 ?   ?   ?   A . n 
A 1 585 TRP 585 621 ?   ?   ?   A . n 
A 1 586 THR 586 622 ?   ?   ?   A . n 
A 1 587 PRO 587 623 ?   ?   ?   A . n 
A 1 588 ASN 588 624 ?   ?   ?   A . n 
A 1 589 SER 589 625 ?   ?   ?   A . n 
A 1 590 ALA 590 626 ?   ?   ?   A . n 
A 1 591 ARG 591 627 ?   ?   ?   A . n 
A 1 592 SER 592 628 ?   ?   ?   A . n 
A 1 593 GLU 593 629 ?   ?   ?   A . n 
A 1 594 GLY 594 630 ?   ?   ?   A . n 
A 1 595 PRO 595 631 ?   ?   ?   A . n 
A 1 596 LEU 596 632 ?   ?   ?   A . n 
A 1 597 PRO 597 633 ?   ?   ?   A . n 
# 
loop_
_pdbx_branch_scheme.asym_id 
_pdbx_branch_scheme.entity_id 
_pdbx_branch_scheme.mon_id 
_pdbx_branch_scheme.num 
_pdbx_branch_scheme.pdb_asym_id 
_pdbx_branch_scheme.pdb_mon_id 
_pdbx_branch_scheme.pdb_seq_num 
_pdbx_branch_scheme.auth_asym_id 
_pdbx_branch_scheme.auth_mon_id 
_pdbx_branch_scheme.auth_seq_num 
_pdbx_branch_scheme.hetero 
B 2 NAG 1 B NAG 1 B NAG 1 n 
B 2 NAG 2 B NAG 2 B NAG 2 n 
B 2 BMA 3 B BMA 3 B BMA 3 n 
B 2 FUC 4 B FUC 4 B FUC 5 n 
# 
loop_
_pdbx_entity_instance_feature.ordinal 
_pdbx_entity_instance_feature.comp_id 
_pdbx_entity_instance_feature.asym_id 
_pdbx_entity_instance_feature.seq_num 
_pdbx_entity_instance_feature.auth_comp_id 
_pdbx_entity_instance_feature.auth_asym_id 
_pdbx_entity_instance_feature.auth_seq_num 
_pdbx_entity_instance_feature.feature_type 
_pdbx_entity_instance_feature.details 
1 A1IJY ? ? A1IJY ? ? 'SUBJECT OF INVESTIGATION' ? 
2 ZN    ? ? ZN    ? ? 'SUBJECT OF INVESTIGATION' ? 
# 
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 
C 3 ZN    1   701 705 ZN    ZN  A . 
D 4 CL    1   702 706 CL    CL  A . 
E 4 CL    1   703 707 CL    CL  A . 
F 5 A1IJY 1   704 959 A1IJY SG2 A . 
G 6 HOH   1   801 801 HOH   HOH A . 
G 6 HOH   2   802 802 HOH   HOH A . 
G 6 HOH   3   803 803 HOH   HOH A . 
G 6 HOH   4   804 805 HOH   HOH A . 
G 6 HOH   5   805 814 HOH   HOH A . 
G 6 HOH   6   806 804 HOH   HOH A . 
G 6 HOH   7   807 806 HOH   HOH A . 
G 6 HOH   8   808 807 HOH   HOH A . 
G 6 HOH   9   809 809 HOH   HOH A . 
G 6 HOH   10  810 816 HOH   HOH A . 
G 6 HOH   11  811 823 HOH   HOH A . 
G 6 HOH   12  812 812 HOH   HOH A . 
G 6 HOH   13  813 813 HOH   HOH A . 
G 6 HOH   14  814 818 HOH   HOH A . 
G 6 HOH   15  815 811 HOH   HOH A . 
G 6 HOH   16  816 815 HOH   HOH A . 
G 6 HOH   17  817 808 HOH   HOH A . 
G 6 HOH   18  818 810 HOH   HOH A . 
G 6 HOH   19  819 820 HOH   HOH A . 
G 6 HOH   20  820 817 HOH   HOH A . 
G 6 HOH   21  821 819 HOH   HOH A . 
G 6 HOH   22  822 830 HOH   HOH A . 
G 6 HOH   23  823 829 HOH   HOH A . 
G 6 HOH   24  824 822 HOH   HOH A . 
G 6 HOH   25  825 831 HOH   HOH A . 
G 6 HOH   26  826 827 HOH   HOH A . 
G 6 HOH   27  827 867 HOH   HOH A . 
G 6 HOH   28  828 832 HOH   HOH A . 
G 6 HOH   29  829 828 HOH   HOH A . 
G 6 HOH   30  830 825 HOH   HOH A . 
G 6 HOH   31  831 838 HOH   HOH A . 
G 6 HOH   32  832 833 HOH   HOH A . 
G 6 HOH   33  833 836 HOH   HOH A . 
G 6 HOH   34  834 842 HOH   HOH A . 
G 6 HOH   35  835 834 HOH   HOH A . 
G 6 HOH   36  836 843 HOH   HOH A . 
G 6 HOH   37  837 826 HOH   HOH A . 
G 6 HOH   38  838 821 HOH   HOH A . 
G 6 HOH   39  839 837 HOH   HOH A . 
G 6 HOH   40  840 854 HOH   HOH A . 
G 6 HOH   41  841 839 HOH   HOH A . 
G 6 HOH   42  842 840 HOH   HOH A . 
G 6 HOH   43  843 856 HOH   HOH A . 
G 6 HOH   44  844 859 HOH   HOH A . 
G 6 HOH   45  845 849 HOH   HOH A . 
G 6 HOH   46  846 845 HOH   HOH A . 
G 6 HOH   47  847 848 HOH   HOH A . 
G 6 HOH   48  848 824 HOH   HOH A . 
G 6 HOH   49  849 852 HOH   HOH A . 
G 6 HOH   50  850 847 HOH   HOH A . 
G 6 HOH   51  851 864 HOH   HOH A . 
G 6 HOH   52  852 858 HOH   HOH A . 
G 6 HOH   53  853 857 HOH   HOH A . 
G 6 HOH   54  854 835 HOH   HOH A . 
G 6 HOH   55  855 861 HOH   HOH A . 
G 6 HOH   56  856 878 HOH   HOH A . 
G 6 HOH   57  857 844 HOH   HOH A . 
G 6 HOH   58  858 851 HOH   HOH A . 
G 6 HOH   59  859 853 HOH   HOH A . 
G 6 HOH   60  860 870 HOH   HOH A . 
G 6 HOH   61  861 846 HOH   HOH A . 
G 6 HOH   62  862 841 HOH   HOH A . 
G 6 HOH   63  863 871 HOH   HOH A . 
G 6 HOH   64  864 890 HOH   HOH A . 
G 6 HOH   65  865 863 HOH   HOH A . 
G 6 HOH   66  866 875 HOH   HOH A . 
G 6 HOH   67  867 860 HOH   HOH A . 
G 6 HOH   68  868 865 HOH   HOH A . 
G 6 HOH   69  869 881 HOH   HOH A . 
G 6 HOH   70  870 850 HOH   HOH A . 
G 6 HOH   71  871 868 HOH   HOH A . 
G 6 HOH   72  872 886 HOH   HOH A . 
G 6 HOH   73  873 880 HOH   HOH A . 
G 6 HOH   74  874 862 HOH   HOH A . 
G 6 HOH   75  875 866 HOH   HOH A . 
G 6 HOH   76  876 874 HOH   HOH A . 
G 6 HOH   77  877 869 HOH   HOH A . 
G 6 HOH   78  878 877 HOH   HOH A . 
G 6 HOH   79  879 873 HOH   HOH A . 
G 6 HOH   80  880 882 HOH   HOH A . 
G 6 HOH   81  881 855 HOH   HOH A . 
G 6 HOH   82  882 879 HOH   HOH A . 
G 6 HOH   83  883 872 HOH   HOH A . 
G 6 HOH   84  884 904 HOH   HOH A . 
G 6 HOH   85  885 897 HOH   HOH A . 
G 6 HOH   86  886 901 HOH   HOH A . 
G 6 HOH   87  887 893 HOH   HOH A . 
G 6 HOH   88  888 889 HOH   HOH A . 
G 6 HOH   89  889 902 HOH   HOH A . 
G 6 HOH   90  890 884 HOH   HOH A . 
G 6 HOH   91  891 883 HOH   HOH A . 
G 6 HOH   92  892 876 HOH   HOH A . 
G 6 HOH   93  893 906 HOH   HOH A . 
G 6 HOH   94  894 887 HOH   HOH A . 
G 6 HOH   95  895 885 HOH   HOH A . 
G 6 HOH   96  896 898 HOH   HOH A . 
G 6 HOH   97  897 894 HOH   HOH A . 
G 6 HOH   98  898 900 HOH   HOH A . 
G 6 HOH   99  899 895 HOH   HOH A . 
G 6 HOH   100 900 899 HOH   HOH A . 
G 6 HOH   101 901 905 HOH   HOH A . 
G 6 HOH   102 902 888 HOH   HOH A . 
G 6 HOH   103 903 891 HOH   HOH A . 
G 6 HOH   104 904 892 HOH   HOH A . 
G 6 HOH   105 905 919 HOH   HOH A . 
G 6 HOH   106 906 914 HOH   HOH A . 
G 6 HOH   107 907 917 HOH   HOH A . 
G 6 HOH   108 908 910 HOH   HOH A . 
G 6 HOH   109 909 911 HOH   HOH A . 
G 6 HOH   110 910 907 HOH   HOH A . 
G 6 HOH   111 911 903 HOH   HOH A . 
G 6 HOH   112 912 922 HOH   HOH A . 
G 6 HOH   113 913 912 HOH   HOH A . 
G 6 HOH   114 914 923 HOH   HOH A . 
G 6 HOH   115 915 915 HOH   HOH A . 
G 6 HOH   116 916 913 HOH   HOH A . 
G 6 HOH   117 917 925 HOH   HOH A . 
G 6 HOH   118 918 908 HOH   HOH A . 
G 6 HOH   119 919 896 HOH   HOH A . 
G 6 HOH   120 920 916 HOH   HOH A . 
G 6 HOH   121 921 924 HOH   HOH A . 
G 6 HOH   122 922 927 HOH   HOH A . 
G 6 HOH   123 923 921 HOH   HOH A . 
G 6 HOH   124 924 918 HOH   HOH A . 
G 6 HOH   125 925 920 HOH   HOH A . 
G 6 HOH   126 926 926 HOH   HOH A . 
G 6 HOH   127 927 909 HOH   HOH A . 
G 6 HOH   128 928 932 HOH   HOH A . 
G 6 HOH   129 929 931 HOH   HOH A . 
G 6 HOH   130 930 929 HOH   HOH A . 
G 6 HOH   131 931 928 HOH   HOH A . 
G 6 HOH   132 932 933 HOH   HOH A . 
G 6 HOH   133 933 934 HOH   HOH A . 
G 6 HOH   134 934 937 HOH   HOH A . 
G 6 HOH   135 935 935 HOH   HOH A . 
G 6 HOH   136 936 930 HOH   HOH A . 
G 6 HOH   137 937 938 HOH   HOH A . 
G 6 HOH   138 938 936 HOH   HOH A . 
G 6 HOH   139 939 939 HOH   HOH A . 
G 6 HOH   140 940 940 HOH   HOH A . 
G 6 HOH   141 941 941 HOH   HOH A . 
G 6 HOH   142 942 942 HOH   HOH A . 
G 6 HOH   143 943 944 HOH   HOH A . 
G 6 HOH   144 944 949 HOH   HOH A . 
G 6 HOH   145 945 945 HOH   HOH A . 
G 6 HOH   146 946 947 HOH   HOH A . 
G 6 HOH   147 947 948 HOH   HOH A . 
G 6 HOH   148 948 943 HOH   HOH A . 
G 6 HOH   149 949 946 HOH   HOH A . 
G 6 HOH   150 950 950 HOH   HOH A . 
G 6 HOH   151 951 951 HOH   HOH A . 
G 6 HOH   152 952 952 HOH   HOH A . 
G 6 HOH   153 953 953 HOH   HOH A . 
G 6 HOH   154 954 955 HOH   HOH A . 
G 6 HOH   155 955 954 HOH   HOH A . 
G 6 HOH   156 956 956 HOH   HOH A . 
G 6 HOH   157 957 957 HOH   HOH A . 
G 6 HOH   158 958 958 HOH   HOH 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       ? ? ? ? ? ? ? ? ? ? ? REFMAC  ? ? ? 5.8.0425 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? DIALS   ? ? ? .        2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .        3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER  ? ? ? .        4 
# 
_cell.angle_alpha                  90 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9GBL 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     56.821 
_cell.length_a_esd                 ? 
_cell.length_b                     85.683 
_cell.length_b_esd                 ? 
_cell.length_c                     135.12 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_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                         9GBL 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_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                   9GBL 
_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             2.39 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          48.50 
_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, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.1 M MIB pH 4.0, 5% glycerol, and 15% PEG 3350' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            289.15 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER2 XE 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2019-10-21 
_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   0.97625 
_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                        'DIAMOND BEAMLINE I03' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.97625 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   I03 
_diffrn_source.pdbx_synchrotron_site       Diamond 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9GBL 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.4 
_reflns.d_resolution_low                               135.12 
_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                                     26594 
_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                           100 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                25.7 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          8.4 
_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                                0.062 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.994 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_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                                    2.40 
_reflns_shell.d_res_low                                     2.49 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             2750 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               0.296 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.841 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_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]                            -0.450 
_refine.aniso_B[1][2]                            -0.000 
_refine.aniso_B[1][3]                            -0.000 
_refine.aniso_B[2][2]                            -0.664 
_refine.aniso_B[2][3]                            0.000 
_refine.aniso_B[3][3]                            1.114 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               35.814 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.942 
_refine.correlation_coeff_Fo_to_Fc_free          0.906 
_refine.details                                  'Hydrogens have not been used' 
_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                                 9GBL 
_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                            2.400 
_refine.ls_d_res_low                             72.466 
_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                     26527 
_refine.ls_number_reflns_R_free                  1320 
_refine.ls_number_reflns_R_work                  25207 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.955 
_refine.ls_percent_reflns_R_free                 4.976 
_refine.ls_R_factor_all                          0.182 
_refine.ls_R_factor_obs                          ? 
_refine.ls_R_factor_R_free                       0.2487 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1784 
_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                      0.236 
_refine.ls_wR_factor_R_work                      0.169 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'MASK BULK SOLVENT' 
_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                          ? 
_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               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.415 
_refine.pdbx_overall_ESU_R_Free                  0.269 
_refine.pdbx_solvent_vdw_probe_radii             1.200 
_refine.pdbx_solvent_ion_probe_radii             0.800 
_refine.pdbx_solvent_shrinkage_radii             0.800 
_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                 ? 
_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                             8.531 
_refine.overall_SU_ML                            0.197 
_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                    0.9779 
_refine.pdbx_average_fsc_free                    0.9554 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.400 
_refine_hist.d_res_low                        72.466 
_refine_hist.number_atoms_solvent             158 
_refine_hist.number_atoms_total               4927 
_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        4684 
_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' ? 0.013  0.012  4928 ? r_bond_refined_d               ? ? 
'X-RAY DIFFRACTION' ? 2.653  1.837  6709 ? r_angle_refined_deg            ? ? 
'X-RAY DIFFRACTION' ? 7.224  5.000  576  ? r_dihedral_angle_1_deg         ? ? 
'X-RAY DIFFRACTION' ? 11.052 5.000  26   ? r_dihedral_angle_2_deg         ? ? 
'X-RAY DIFFRACTION' ? 17.227 10.000 805  ? r_dihedral_angle_3_deg         ? ? 
'X-RAY DIFFRACTION' ? 15.501 10.000 240  ? r_dihedral_angle_6_deg         ? ? 
'X-RAY DIFFRACTION' ? 0.174  0.200  714  ? r_chiral_restr                 ? ? 
'X-RAY DIFFRACTION' ? 0.013  0.020  3872 ? r_gen_planes_refined           ? ? 
'X-RAY DIFFRACTION' ? 0.234  0.200  2231 ? r_nbd_refined                  ? ? 
'X-RAY DIFFRACTION' ? 0.324  0.200  3342 ? r_nbtor_refined                ? ? 
'X-RAY DIFFRACTION' ? 0.165  0.200  221  ? r_xyhbond_nbd_refined          ? ? 
'X-RAY DIFFRACTION' ? 0.200  0.200  31   ? r_symmetry_nbd_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.183  0.200  4    ? r_symmetry_xyhbond_nbd_refined ? ? 
'X-RAY DIFFRACTION' ? 4.658  3.360  2307 ? r_mcbond_it                    ? ? 
'X-RAY DIFFRACTION' ? 6.374  6.011  2882 ? r_mcangle_it                   ? ? 
'X-RAY DIFFRACTION' ? 6.615  3.709  2621 ? r_scbond_it                    ? ? 
'X-RAY DIFFRACTION' ? 9.350  6.582  3827 ? r_scangle_it                   ? ? 
'X-RAY DIFFRACTION' ? 10.164 35.376 7501 ? r_lrange_it                    ? ? 
# 
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' 2.400  2.462  1944 . 110 1833 99.9486  . 0.226 . . 0.222 . . . . . 0.215 . 20 . 0.967 0.931 0.292 
'X-RAY DIFFRACTION' 2.462  2.530  1857 . 81  1775 99.9461  . 0.194 . . 0.190 . . . . . 0.183 . 20 . 0.976 0.954 0.274 
'X-RAY DIFFRACTION' 2.530  2.603  1834 . 78  1756 100.0000 . 0.189 . . 0.187 . . . . . 0.177 . 20 . 0.977 0.961 0.242 
'X-RAY DIFFRACTION' 2.603  2.683  1780 . 91  1688 99.9438  . 0.200 . . 0.197 . . . . . 0.185 . 20 . 0.977 0.958 0.256 
'X-RAY DIFFRACTION' 2.683  2.771  1720 . 81  1638 99.9419  . 0.222 . . 0.219 . . . . . 0.203 . 20 . 0.969 0.948 0.293 
'X-RAY DIFFRACTION' 2.771  2.868  1674 . 87  1586 99.9403  . 0.207 . . 0.201 . . . . . 0.185 . 20 . 0.974 0.937 0.313 
'X-RAY DIFFRACTION' 2.868  2.976  1614 . 73  1541 100.0000 . 0.197 . . 0.192 . . . . . 0.177 . 20 . 0.976 0.940 0.305 
'X-RAY DIFFRACTION' 2.976  3.097  1548 . 97  1451 100.0000 . 0.194 . . 0.190 . . . . . 0.175 . 20 . 0.977 0.962 0.254 
'X-RAY DIFFRACTION' 3.097  3.235  1494 . 66  1428 100.0000 . 0.203 . . 0.198 . . . . . 0.187 . 20 . 0.975 0.937 0.313 
'X-RAY DIFFRACTION' 3.235  3.392  1457 . 77  1379 99.9314  . 0.205 . . 0.200 . . . . . 0.188 . 20 . 0.977 0.948 0.286 
'X-RAY DIFFRACTION' 3.392  3.575  1373 . 71  1300 99.8543  . 0.196 . . 0.191 . . . . . 0.183 . 20 . 0.981 0.947 0.297 
'X-RAY DIFFRACTION' 3.575  3.792  1290 . 56  1231 99.7674  . 0.172 . . 0.171 . . . . . 0.165 . 20 . 0.985 0.974 0.197 
'X-RAY DIFFRACTION' 3.792  4.053  1226 . 59  1167 100.0000 . 0.149 . . 0.147 . . . . . 0.142 . 20 . 0.987 0.978 0.193 
'X-RAY DIFFRACTION' 4.053  4.376  1136 . 53  1083 100.0000 . 0.134 . . 0.129 . . . . . 0.125 . 20 . 0.990 0.968 0.229 
'X-RAY DIFFRACTION' 4.376  4.792  1062 . 65  997  100.0000 . 0.131 . . 0.127 . . . . . 0.123 . 20 . 0.991 0.979 0.203 
'X-RAY DIFFRACTION' 4.792  5.355  973  . 55  918  100.0000 . 0.155 . . 0.151 . . . . . 0.149 . 20 . 0.988 0.976 0.211 
'X-RAY DIFFRACTION' 5.355  6.178  863  . 39  824  100.0000 . 0.185 . . 0.182 . . . . . 0.177 . 20 . 0.984 0.970 0.235 
'X-RAY DIFFRACTION' 6.178  7.552  737  . 32  705  100.0000 . 0.163 . . 0.161 . . . . . 0.159 . 20 . 0.986 0.977 0.210 
'X-RAY DIFFRACTION' 7.552  10.623 593  . 30  563  100.0000 . 0.140 . . 0.138 . . . . . 0.141 . 20 . 0.988 0.980 0.185 
'X-RAY DIFFRACTION' 10.623 72.466 364  . 19  344  99.7253  . 0.279 . . 0.278 . . . . . 0.272 . 20 . 0.928 0.920 0.302 
# 
_struct.entry_id                     9GBL 
_struct.title                        'Human Angiotensin-1 converting enzyme C-domain in complex with a diprolyl inhibitor- SG18' 
_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        9GBL 
_struct_keywords.text            'Inhibitor, complex, protease, HYDROLASE' 
_struct_keywords.pdbx_keywords   HYDROLASE 
# 
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 ? 
D N N 4 ? 
E N N 4 ? 
F N N 5 ? 
G N N 6 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    ACE_HUMAN 
_struct_ref.pdbx_db_accession          P12821 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;LVTDEAEASKFVEEYDRTSQVVWNEYAEANWNYNTNITTETSKILLQKNMQIANHTLKYGTQARKFDVNQLQNTTIKRII
KKVQDLERAALPAQELEEYNKILLDMETTYSVATVCHPNGSCLQLEPDLTNVMATSRKYEDLLWAWEGWRDKAGRAILQF
YPKYVELINQAARLNGYVDAGDSWRSMYETPSLEQDLERLFQELQPLYLNLHAYVRRALHRHYGAQHINLEGPIPAHLLG
NMWAQTWSNIYDLVVPFPSAPSMDTTEAMLKQGWTPRRMFKEADDFFTSLGLLPVPPEFWNKSMLEKPTDGREVVCHASA
WDFYNGKDFRIKQCTTVNLEDLVVAHHEMGHIQYFMQYKDLPVALREGANPGFHEAIGDVLALSVSTPKHLHSLNLLSSE
GGSDEHDINFLMKMALDKIAFIPFSYLVDQWRWRVFDGSITKENYNQEWWSLRLKYQGLCPPVPRTQGDFDPGAKFHIPS
SVPYIRYFVSFIIQFQFHEALCQAAGHTGPLHKCDIYQSKEAGQRLATAMKLGFSRPWPEAMQLITGQPNMSASAMLSYF
KPLLDWLRTENELHGEKLGWPQYNWTPNSARSEGPLP
;
_struct_ref.pdbx_align_begin           642 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9GBL 
_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                 597 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             P12821 
_struct_ref_seq.db_align_beg                  642 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  1238 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       37 
_struct_ref_seq.pdbx_auth_seq_align_end       633 
# 
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 9GBL GLY A 28  ? UNP P12821 GLU 669  'engineered mutation' 64  1 
1 9GBL GLN A 54  ? UNP P12821 ASN 695  'engineered mutation' 90  2 
1 9GBL GLN A 119 ? UNP P12821 ASN 760  'engineered mutation' 155 3 
1 9GBL GLN A 301 ? UNP P12821 ASN 942  'engineered mutation' 337 4 
1 9GBL GLN A 550 ? UNP P12821 ASN 1191 'engineered mutation' 586 5 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 1210  ? 
1 MORE         -10   ? 
1 'SSA (A^2)'  24150 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 GLU A 5   ? THR A 35  ? GLU A 41  THR A 71  1 ? 31 
HELX_P HELX_P2  AA2 THR A 38  ? LYS A 65  ? THR A 74  LYS A 101 1 ? 28 
HELX_P HELX_P3  AA3 PHE A 66  ? LEU A 71  ? PHE A 102 LEU A 107 5 ? 6  
HELX_P HELX_P4  AA4 ASN A 73  ? GLN A 84  ? ASN A 109 GLN A 120 1 ? 12 
HELX_P HELX_P5  AA5 LEU A 86  ? LEU A 91  ? LEU A 122 LEU A 127 5 ? 6  
HELX_P HELX_P6  AA6 PRO A 92  ? ALA A 113 ? PRO A 128 ALA A 149 1 ? 22 
HELX_P HELX_P7  AA7 PRO A 127 ? SER A 136 ? PRO A 163 SER A 172 1 ? 10 
HELX_P HELX_P8  AA8 LYS A 138 ? ALA A 153 ? LYS A 174 ALA A 189 1 ? 16 
HELX_P HELX_P9  AA9 ALA A 153 ? LEU A 158 ? ALA A 189 LEU A 194 1 ? 6  
HELX_P HELX_P10 AB1 PHE A 160 ? ASN A 175 ? PHE A 196 ASN A 211 1 ? 16 
HELX_P HELX_P11 AB2 ASP A 179 ? SER A 186 ? ASP A 215 SER A 222 1 ? 8  
HELX_P HELX_P12 AB3 MET A 187 ? GLU A 189 ? MET A 223 GLU A 225 5 ? 3  
HELX_P HELX_P13 AB4 SER A 192 ? LEU A 204 ? SER A 228 LEU A 240 1 ? 13 
HELX_P HELX_P14 AB5 LEU A 204 ? GLY A 224 ? LEU A 240 GLY A 260 1 ? 21 
HELX_P HELX_P15 AB6 TRP A 247 ? VAL A 254 ? TRP A 283 VAL A 290 5 ? 8  
HELX_P HELX_P16 AB7 ASP A 264 ? GLN A 272 ? ASP A 300 GLN A 308 1 ? 9  
HELX_P HELX_P17 AB8 THR A 275 ? LEU A 290 ? THR A 311 LEU A 326 1 ? 16 
HELX_P HELX_P18 AB9 PRO A 296 ? SER A 303 ? PRO A 332 SER A 339 1 ? 8  
HELX_P HELX_P19 AC1 ASN A 338 ? TYR A 358 ? ASN A 374 TYR A 394 1 ? 21 
HELX_P HELX_P20 AC2 PRO A 362 ? ARG A 366 ? PRO A 398 ARG A 402 5 ? 5  
HELX_P HELX_P21 AC3 ASN A 370 ? SER A 386 ? ASN A 406 SER A 422 1 ? 17 
HELX_P HELX_P22 AC4 THR A 387 ? LEU A 394 ? THR A 423 LEU A 430 1 ? 8  
HELX_P HELX_P23 AC5 SER A 403 ? ASP A 437 ? SER A 439 ASP A 473 1 ? 35 
HELX_P HELX_P24 AC6 ASN A 444 ? GLY A 458 ? ASN A 480 GLY A 494 1 ? 15 
HELX_P HELX_P25 AC7 PHE A 470 ? LYS A 475 ? PHE A 506 LYS A 511 5 ? 6  
HELX_P HELX_P26 AC8 TYR A 484 ? ALA A 505 ? TYR A 520 ALA A 541 1 ? 22 
HELX_P HELX_P27 AC9 PRO A 510 ? CYS A 514 ? PRO A 546 CYS A 550 5 ? 5  
HELX_P HELX_P28 AD1 SER A 519 ? LEU A 532 ? SER A 555 LEU A 568 1 ? 14 
HELX_P HELX_P29 AD2 PRO A 537 ? GLY A 547 ? PRO A 573 GLY A 583 1 ? 11 
HELX_P HELX_P30 AD3 ALA A 553 ? PHE A 560 ? ALA A 589 PHE A 596 1 ? 8  
HELX_P HELX_P31 AD4 PHE A 560 ? GLY A 575 ? PHE A 596 GLY A 611 1 ? 16 
# 
_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 
disulf1 disulf ?    ? A CYS 116 SG  ? ? ? 1_555 A CYS   122 SG  ? ? A CYS 152 A CYS   158 1_555 ? ? ? ? ? ? ? 2.112 ? ? 
disulf2 disulf ?    ? A CYS 316 SG  ? ? ? 1_555 A CYS   334 SG  ? ? A CYS 352 A CYS   370 1_555 ? ? ? ? ? ? ? 2.132 ? ? 
disulf3 disulf ?    ? A CYS 502 SG  ? ? ? 1_555 A CYS   514 SG  ? ? A CYS 538 A CYS   550 1_555 ? ? ? ? ? ? ? 2.061 ? ? 
covale1 covale one  ? A ASN 73  ND2 ? ? ? 1_555 B NAG   .   C1  ? ? A ASN 109 B NAG   1   1_555 ? ? ? ? ? ? ? 1.463 ? 
N-Glycosylation 
covale2 covale both ? B NAG .   O4  ? ? ? 1_555 B NAG   .   C1  ? ? B NAG 1   B NAG   2   1_555 ? ? ? ? ? ? ? 1.386 ? ? 
covale3 covale both ? B NAG .   O6  ? ? ? 1_555 B FUC   .   C1  ? ? B NAG 1   B FUC   4   1_555 ? ? ? ? ? ? ? 1.395 ? ? 
covale4 covale both ? B NAG .   O4  ? ? ? 1_555 B BMA   .   C1  ? ? B NAG 2   B BMA   3   1_555 ? ? ? ? ? ? ? 1.395 ? ? 
metalc1 metalc ?    ? A HIS 347 NE2 ? ? ? 1_555 C ZN    .   ZN  ? ? A HIS 383 A ZN    701 1_555 ? ? ? ? ? ? ? 1.954 ? ? 
metalc2 metalc ?    ? A HIS 351 NE2 ? ? ? 1_555 C ZN    .   ZN  ? ? A HIS 387 A ZN    701 1_555 ? ? ? ? ? ? ? 1.915 ? ? 
metalc3 metalc ?    ? A GLU 375 OE1 ? ? ? 1_555 C ZN    .   ZN  ? ? A GLU 411 A ZN    701 1_555 ? ? ? ? ? ? ? 1.945 ? ? 
metalc4 metalc ?    ? C ZN  .   ZN  ? ? ? 1_555 F A1IJY .   O24 ? ? A ZN  701 A A1IJY 704 1_555 ? ? ? ? ? ? ? 2.375 ? ? 
metalc5 metalc ?    ? C ZN  .   ZN  ? ? ? 1_555 F A1IJY .   O23 ? ? A ZN  701 A A1IJY 704 1_555 ? ? ? ? ? ? ? 2.026 ? ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
covale ? ? 
metalc ? ? 
# 
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  NE2 ? A HIS   347 ? A HIS   383 ? 1_555 ZN ? C ZN . ? A ZN 701 ? 1_555 NE2 ? A HIS   351 ? A HIS   387 ? 1_555 109.5 ? 
2  NE2 ? A HIS   347 ? A HIS   383 ? 1_555 ZN ? C ZN . ? A ZN 701 ? 1_555 OE1 ? A GLU   375 ? A GLU   411 ? 1_555 99.7  ? 
3  NE2 ? A HIS   351 ? A HIS   387 ? 1_555 ZN ? C ZN . ? A ZN 701 ? 1_555 OE1 ? A GLU   375 ? A GLU   411 ? 1_555 100.6 ? 
4  NE2 ? A HIS   347 ? A HIS   383 ? 1_555 ZN ? C ZN . ? A ZN 701 ? 1_555 O24 ? F A1IJY .   ? A A1IJY 704 ? 1_555 92.2  ? 
5  NE2 ? A HIS   351 ? A HIS   387 ? 1_555 ZN ? C ZN . ? A ZN 701 ? 1_555 O24 ? F A1IJY .   ? A A1IJY 704 ? 1_555 94.9  ? 
6  OE1 ? A GLU   375 ? A GLU   411 ? 1_555 ZN ? C ZN . ? A ZN 701 ? 1_555 O24 ? F A1IJY .   ? A A1IJY 704 ? 1_555 155.9 ? 
7  NE2 ? A HIS   347 ? A HIS   383 ? 1_555 ZN ? C ZN . ? A ZN 701 ? 1_555 O23 ? F A1IJY .   ? A A1IJY 704 ? 1_555 118.0 ? 
8  NE2 ? A HIS   351 ? A HIS   387 ? 1_555 ZN ? C ZN . ? A ZN 701 ? 1_555 O23 ? F A1IJY .   ? A A1IJY 704 ? 1_555 125.1 ? 
9  OE1 ? A GLU   375 ? A GLU   411 ? 1_555 ZN ? C ZN . ? A ZN 701 ? 1_555 O23 ? F A1IJY .   ? A A1IJY 704 ? 1_555 97.2  ? 
10 O24 ? F A1IJY .   ? A A1IJY 704 ? 1_555 ZN ? C ZN . ? A ZN 701 ? 1_555 O23 ? F A1IJY .   ? A A1IJY 704 ? 1_555 58.8  ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1 NAG B .   ? ASN A 73  ? NAG B 1   ? 1_555 ASN A 109 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
2 CYS A 116 ? CYS A 122 ? CYS A 152 ? 1_555 CYS A 158 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
3 CYS A 316 ? CYS A 334 ? CYS A 352 ? 1_555 CYS A 370 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
4 CYS A 502 ? CYS A 514 ? CYS A 538 ? 1_555 CYS A 550 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
# 
_struct_mon_prot_cis.pdbx_id                1 
_struct_mon_prot_cis.label_comp_id          GLU 
_struct_mon_prot_cis.label_seq_id           126 
_struct_mon_prot_cis.label_asym_id          A 
_struct_mon_prot_cis.label_alt_id           . 
_struct_mon_prot_cis.pdbx_PDB_ins_code      ? 
_struct_mon_prot_cis.auth_comp_id           GLU 
_struct_mon_prot_cis.auth_seq_id            162 
_struct_mon_prot_cis.auth_asym_id           A 
_struct_mon_prot_cis.pdbx_label_comp_id_2   PRO 
_struct_mon_prot_cis.pdbx_label_seq_id_2    127 
_struct_mon_prot_cis.pdbx_label_asym_id_2   A 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2    ? 
_struct_mon_prot_cis.pdbx_auth_comp_id_2    PRO 
_struct_mon_prot_cis.pdbx_auth_seq_id_2     163 
_struct_mon_prot_cis.pdbx_auth_asym_id_2    A 
_struct_mon_prot_cis.pdbx_PDB_model_num     1 
_struct_mon_prot_cis.pdbx_omega_angle       11.54 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2 ? 
AA2 ? 2 ? 
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 
AA2 1 2 ? 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 THR A 114 ? CYS A 116 ? THR A 150 CYS A 152 
AA1 2 CYS A 122 ? GLN A 124 ? CYS A 158 GLN A 160 
AA2 1 ILE A 234 ? PRO A 235 ? ILE A 270 PRO A 271 
AA2 2 LEU A 459 ? CYS A 460 ? LEU A 495 CYS A 496 
AA3 1 SER A 319 ? ASP A 322 ? SER A 355 ASP A 358 
AA3 2 PHE A 329 ? LYS A 332 ? PHE A 365 LYS A 368 
# 
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 VAL A 115 ? N VAL A 151 O LEU A 123 ? O LEU A 159 
AA2 1 2 N ILE A 234 ? N ILE A 270 O CYS A 460 ? O CYS A 496 
AA3 1 2 N TRP A 321 ? N TRP A 357 O ARG A 330 ? O ARG A 366 
# 
_pdbx_entry_details.entry_id                   9GBL 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   Y 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   O 
_pdbx_validate_close_contact.auth_asym_id_1   A 
_pdbx_validate_close_contact.auth_comp_id_1   HOH 
_pdbx_validate_close_contact.auth_seq_id_1    933 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   O 
_pdbx_validate_close_contact.auth_asym_id_2   A 
_pdbx_validate_close_contact.auth_comp_id_2   HOH 
_pdbx_validate_close_contact.auth_seq_id_2    954 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             2.19 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1  1 CB  A ARG 53  ? ? CA A ARG 53  ? ? C   A ARG 53  ? ? 90.74  110.40 -19.66 2.00 N 
2  1 CB  A LEU 139 ? ? CG A LEU 139 ? ? CD1 A LEU 139 ? ? 99.66  111.00 -11.34 1.70 N 
3  1 CG  A MET 142 ? ? SD A MET 142 ? ? CE  A MET 142 ? ? 87.39  100.20 -12.81 1.60 N 
4  1 OG1 A THR 150 ? ? CB A THR 150 ? ? CG2 A THR 150 ? ? 94.25  110.00 -15.75 2.30 N 
5  1 CG  A MET 169 ? ? SD A MET 169 ? ? CE  A MET 169 ? ? 113.92 100.20 13.72  1.60 N 
6  1 CA  A ARG 191 ? ? CB A ARG 191 ? ? CG  A ARG 191 ? ? 141.94 113.40 28.54  2.20 N 
7  1 CG  A ARG 191 ? ? CD A ARG 191 ? ? NE  A ARG 191 ? ? 96.09  111.80 -15.71 2.10 N 
8  1 NE  A ARG 253 ? ? CZ A ARG 253 ? ? NH2 A ARG 253 ? ? 115.53 120.30 -4.77  0.50 N 
9  1 CD  A ARG 257 ? ? NE A ARG 257 ? ? CZ  A ARG 257 ? ? 132.78 123.60 9.18   1.40 N 
10 1 CB  A GLN 337 ? ? CA A GLN 337 ? ? C   A GLN 337 ? ? 93.18  110.40 -17.22 2.00 N 
11 1 N   A GLN 337 ? ? CA A GLN 337 ? ? CB  A GLN 337 ? ? 122.44 110.60 11.84  1.80 N 
12 1 CD  A LYS 395 ? ? CE A LYS 395 ? ? NZ  A LYS 395 ? ? 97.17  111.70 -14.53 2.30 N 
13 1 CG  A MET 448 ? ? SD A MET 448 ? ? CE  A MET 448 ? ? 110.22 100.20 10.02  1.60 N 
14 1 CB  A ASN 480 ? ? CA A ASN 480 ? ? C   A ASN 480 ? ? 94.64  110.40 -15.76 2.00 N 
15 1 N   A GLN 493 ? ? CA A GLN 493 ? ? CB  A GLN 493 ? ? 121.55 110.60 10.95  1.80 N 
16 1 NE  A ARG 561 ? ? CZ A ARG 561 ? ? NH1 A ARG 561 ? ? 123.86 120.30 3.56   0.50 N 
17 1 NE  A ARG 561 ? ? CZ A ARG 561 ? ? NH2 A ARG 561 ? ? 117.20 120.30 -3.10  0.50 N 
18 1 CB  A LEU 614 ? ? CG A LEU 614 ? ? CD2 A LEU 614 ? ? 122.58 111.00 11.58  1.70 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 ASN A 72  ? ? 173.66 56.77   
2 1 GLU A 76  ? ? -67.27 -74.91  
3 1 LYS A 79  ? ? -60.74 -71.83  
4 1 GLU A 123 ? ? 61.99  -137.59 
5 1 ALA A 125 ? ? -58.75 -6.66   
6 1 GLN A 155 ? ? 53.17  14.46   
7 1 ASP A 346 ? ? -91.78 59.15   
# 
loop_
_pdbx_validate_planes.id 
_pdbx_validate_planes.PDB_model_num 
_pdbx_validate_planes.auth_comp_id 
_pdbx_validate_planes.auth_asym_id 
_pdbx_validate_planes.auth_seq_id 
_pdbx_validate_planes.PDB_ins_code 
_pdbx_validate_planes.label_alt_id 
_pdbx_validate_planes.rmsd 
_pdbx_validate_planes.type 
1 1 ARG A 191 ? ? 0.157 'SIDE CHAIN' 
2 1 ARG A 402 ? ? 0.105 'SIDE CHAIN' 
3 1 ARG A 468 ? ? 0.085 'SIDE CHAIN' 
4 1 ARG A 489 ? ? 0.122 'SIDE CHAIN' 
# 
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 LEU 37  ? A LEU 1   
2  1 Y 1 A VAL 38  ? A VAL 2   
3  1 Y 1 A THR 39  ? A THR 3   
4  1 Y 1 A GLU 349 ? A GLU 313 
5  1 Y 1 A GLU 436 ? A GLU 400 
6  1 Y 1 A GLY 437 ? A GLY 401 
7  1 Y 1 A GLN 618 ? A GLN 582 
8  1 Y 1 A TYR 619 ? A TYR 583 
9  1 Y 1 A ASN 620 ? A ASN 584 
10 1 Y 1 A TRP 621 ? A TRP 585 
11 1 Y 1 A THR 622 ? A THR 586 
12 1 Y 1 A PRO 623 ? A PRO 587 
13 1 Y 1 A ASN 624 ? A ASN 588 
14 1 Y 1 A SER 625 ? A SER 589 
15 1 Y 1 A ALA 626 ? A ALA 590 
16 1 Y 1 A ARG 627 ? A ARG 591 
17 1 Y 1 A SER 628 ? A SER 592 
18 1 Y 1 A GLU 629 ? A GLU 593 
19 1 Y 1 A GLY 630 ? A GLY 594 
20 1 Y 1 A PRO 631 ? A PRO 595 
21 1 Y 1 A LEU 632 ? A LEU 596 
22 1 Y 1 A PRO 633 ? A PRO 597 
# 
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 
A1IJY C11  C  N N 1   
A1IJY O01  O  N N 2   
A1IJY C02  C  N N 3   
A1IJY C03  C  N S 4   
A1IJY N04  N  N N 5   
A1IJY C05  C  N S 6   
A1IJY C06  C  N S 7   
A1IJY C07  C  N N 8   
A1IJY C08  C  N N 9   
A1IJY C09  C  N N 10  
A1IJY N10  N  N N 11  
A1IJY C12  C  Y N 12  
A1IJY C13  C  Y N 13  
A1IJY C14  C  Y N 14  
A1IJY C15  C  Y N 15  
A1IJY C16  C  N N 16  
A1IJY O17  O  N N 17  
A1IJY O18  O  N N 18  
A1IJY C19  C  Y N 19  
A1IJY C20  C  Y N 20  
A1IJY O21  O  N N 21  
A1IJY C22  C  N N 22  
A1IJY O23  O  N N 23  
A1IJY O24  O  N N 24  
A1IJY C25  C  N N 25  
A1IJY N26  N  N N 26  
A1IJY C27  C  N N 27  
A1IJY C28  C  N N 28  
A1IJY C29  C  N N 29  
A1IJY C30  C  N S 30  
A1IJY C31  C  N N 31  
A1IJY O32  O  N N 32  
A1IJY O33  O  N N 33  
A1IJY H1   H  N N 34  
A1IJY H2   H  N N 35  
A1IJY H4   H  N N 36  
A1IJY H5   H  N N 37  
A1IJY H6   H  N N 38  
A1IJY H7   H  N N 39  
A1IJY H8   H  N N 40  
A1IJY H9   H  N N 41  
A1IJY H10  H  N N 42  
A1IJY H11  H  N N 43  
A1IJY H12  H  N N 44  
A1IJY H13  H  N N 45  
A1IJY H14  H  N N 46  
A1IJY H15  H  N N 47  
A1IJY H16  H  N N 48  
A1IJY H17  H  N N 49  
A1IJY H18  H  N N 50  
A1IJY H19  H  N N 51  
A1IJY H20  H  N N 52  
A1IJY H21  H  N N 53  
A1IJY H22  H  N N 54  
A1IJY H23  H  N N 55  
A1IJY H24  H  N N 56  
A1IJY H25  H  N N 57  
A1IJY H26  H  N N 58  
A1IJY H27  H  N N 59  
A1IJY H28  H  N N 60  
ALA   N    N  N N 61  
ALA   CA   C  N S 62  
ALA   C    C  N N 63  
ALA   O    O  N N 64  
ALA   CB   C  N N 65  
ALA   OXT  O  N N 66  
ALA   H    H  N N 67  
ALA   H2   H  N N 68  
ALA   HA   H  N N 69  
ALA   HB1  H  N N 70  
ALA   HB2  H  N N 71  
ALA   HB3  H  N N 72  
ALA   HXT  H  N N 73  
ARG   N    N  N N 74  
ARG   CA   C  N S 75  
ARG   C    C  N N 76  
ARG   O    O  N N 77  
ARG   CB   C  N N 78  
ARG   CG   C  N N 79  
ARG   CD   C  N N 80  
ARG   NE   N  N N 81  
ARG   CZ   C  N N 82  
ARG   NH1  N  N N 83  
ARG   NH2  N  N N 84  
ARG   OXT  O  N N 85  
ARG   H    H  N N 86  
ARG   H2   H  N N 87  
ARG   HA   H  N N 88  
ARG   HB2  H  N N 89  
ARG   HB3  H  N N 90  
ARG   HG2  H  N N 91  
ARG   HG3  H  N N 92  
ARG   HD2  H  N N 93  
ARG   HD3  H  N N 94  
ARG   HE   H  N N 95  
ARG   HH11 H  N N 96  
ARG   HH12 H  N N 97  
ARG   HH21 H  N N 98  
ARG   HH22 H  N N 99  
ARG   HXT  H  N N 100 
ASN   N    N  N N 101 
ASN   CA   C  N S 102 
ASN   C    C  N N 103 
ASN   O    O  N N 104 
ASN   CB   C  N N 105 
ASN   CG   C  N N 106 
ASN   OD1  O  N N 107 
ASN   ND2  N  N N 108 
ASN   OXT  O  N N 109 
ASN   H    H  N N 110 
ASN   H2   H  N N 111 
ASN   HA   H  N N 112 
ASN   HB2  H  N N 113 
ASN   HB3  H  N N 114 
ASN   HD21 H  N N 115 
ASN   HD22 H  N N 116 
ASN   HXT  H  N N 117 
ASP   N    N  N N 118 
ASP   CA   C  N S 119 
ASP   C    C  N N 120 
ASP   O    O  N N 121 
ASP   CB   C  N N 122 
ASP   CG   C  N N 123 
ASP   OD1  O  N N 124 
ASP   OD2  O  N N 125 
ASP   OXT  O  N N 126 
ASP   H    H  N N 127 
ASP   H2   H  N N 128 
ASP   HA   H  N N 129 
ASP   HB2  H  N N 130 
ASP   HB3  H  N N 131 
ASP   HD2  H  N N 132 
ASP   HXT  H  N N 133 
BMA   C1   C  N R 134 
BMA   C2   C  N S 135 
BMA   C3   C  N S 136 
BMA   C4   C  N S 137 
BMA   C5   C  N R 138 
BMA   C6   C  N N 139 
BMA   O1   O  N N 140 
BMA   O2   O  N N 141 
BMA   O3   O  N N 142 
BMA   O4   O  N N 143 
BMA   O5   O  N N 144 
BMA   O6   O  N N 145 
BMA   H1   H  N N 146 
BMA   H2   H  N N 147 
BMA   H3   H  N N 148 
BMA   H4   H  N N 149 
BMA   H5   H  N N 150 
BMA   H61  H  N N 151 
BMA   H62  H  N N 152 
BMA   HO1  H  N N 153 
BMA   HO2  H  N N 154 
BMA   HO3  H  N N 155 
BMA   HO4  H  N N 156 
BMA   HO6  H  N N 157 
CL    CL   CL N N 158 
CYS   N    N  N N 159 
CYS   CA   C  N R 160 
CYS   C    C  N N 161 
CYS   O    O  N N 162 
CYS   CB   C  N N 163 
CYS   SG   S  N N 164 
CYS   OXT  O  N N 165 
CYS   H    H  N N 166 
CYS   H2   H  N N 167 
CYS   HA   H  N N 168 
CYS   HB2  H  N N 169 
CYS   HB3  H  N N 170 
CYS   HG   H  N N 171 
CYS   HXT  H  N N 172 
FUC   C1   C  N R 173 
FUC   C2   C  N S 174 
FUC   C3   C  N R 175 
FUC   C4   C  N S 176 
FUC   C5   C  N S 177 
FUC   C6   C  N N 178 
FUC   O1   O  N N 179 
FUC   O2   O  N N 180 
FUC   O3   O  N N 181 
FUC   O4   O  N N 182 
FUC   O5   O  N N 183 
FUC   H1   H  N N 184 
FUC   H2   H  N N 185 
FUC   H3   H  N N 186 
FUC   H4   H  N N 187 
FUC   H5   H  N N 188 
FUC   H61  H  N N 189 
FUC   H62  H  N N 190 
FUC   H63  H  N N 191 
FUC   HO1  H  N N 192 
FUC   HO2  H  N N 193 
FUC   HO3  H  N N 194 
FUC   HO4  H  N N 195 
GLN   N    N  N N 196 
GLN   CA   C  N S 197 
GLN   C    C  N N 198 
GLN   O    O  N N 199 
GLN   CB   C  N N 200 
GLN   CG   C  N N 201 
GLN   CD   C  N N 202 
GLN   OE1  O  N N 203 
GLN   NE2  N  N N 204 
GLN   OXT  O  N N 205 
GLN   H    H  N N 206 
GLN   H2   H  N N 207 
GLN   HA   H  N N 208 
GLN   HB2  H  N N 209 
GLN   HB3  H  N N 210 
GLN   HG2  H  N N 211 
GLN   HG3  H  N N 212 
GLN   HE21 H  N N 213 
GLN   HE22 H  N N 214 
GLN   HXT  H  N N 215 
GLU   N    N  N N 216 
GLU   CA   C  N S 217 
GLU   C    C  N N 218 
GLU   O    O  N N 219 
GLU   CB   C  N N 220 
GLU   CG   C  N N 221 
GLU   CD   C  N N 222 
GLU   OE1  O  N N 223 
GLU   OE2  O  N N 224 
GLU   OXT  O  N N 225 
GLU   H    H  N N 226 
GLU   H2   H  N N 227 
GLU   HA   H  N N 228 
GLU   HB2  H  N N 229 
GLU   HB3  H  N N 230 
GLU   HG2  H  N N 231 
GLU   HG3  H  N N 232 
GLU   HE2  H  N N 233 
GLU   HXT  H  N N 234 
GLY   N    N  N N 235 
GLY   CA   C  N N 236 
GLY   C    C  N N 237 
GLY   O    O  N N 238 
GLY   OXT  O  N N 239 
GLY   H    H  N N 240 
GLY   H2   H  N N 241 
GLY   HA2  H  N N 242 
GLY   HA3  H  N N 243 
GLY   HXT  H  N N 244 
HIS   N    N  N N 245 
HIS   CA   C  N S 246 
HIS   C    C  N N 247 
HIS   O    O  N N 248 
HIS   CB   C  N N 249 
HIS   CG   C  Y N 250 
HIS   ND1  N  Y N 251 
HIS   CD2  C  Y N 252 
HIS   CE1  C  Y N 253 
HIS   NE2  N  Y N 254 
HIS   OXT  O  N N 255 
HIS   H    H  N N 256 
HIS   H2   H  N N 257 
HIS   HA   H  N N 258 
HIS   HB2  H  N N 259 
HIS   HB3  H  N N 260 
HIS   HD1  H  N N 261 
HIS   HD2  H  N N 262 
HIS   HE1  H  N N 263 
HIS   HE2  H  N N 264 
HIS   HXT  H  N N 265 
HOH   O    O  N N 266 
HOH   H1   H  N N 267 
HOH   H2   H  N N 268 
ILE   N    N  N N 269 
ILE   CA   C  N S 270 
ILE   C    C  N N 271 
ILE   O    O  N N 272 
ILE   CB   C  N S 273 
ILE   CG1  C  N N 274 
ILE   CG2  C  N N 275 
ILE   CD1  C  N N 276 
ILE   OXT  O  N N 277 
ILE   H    H  N N 278 
ILE   H2   H  N N 279 
ILE   HA   H  N N 280 
ILE   HB   H  N N 281 
ILE   HG12 H  N N 282 
ILE   HG13 H  N N 283 
ILE   HG21 H  N N 284 
ILE   HG22 H  N N 285 
ILE   HG23 H  N N 286 
ILE   HD11 H  N N 287 
ILE   HD12 H  N N 288 
ILE   HD13 H  N N 289 
ILE   HXT  H  N N 290 
LEU   N    N  N N 291 
LEU   CA   C  N S 292 
LEU   C    C  N N 293 
LEU   O    O  N N 294 
LEU   CB   C  N N 295 
LEU   CG   C  N N 296 
LEU   CD1  C  N N 297 
LEU   CD2  C  N N 298 
LEU   OXT  O  N N 299 
LEU   H    H  N N 300 
LEU   H2   H  N N 301 
LEU   HA   H  N N 302 
LEU   HB2  H  N N 303 
LEU   HB3  H  N N 304 
LEU   HG   H  N N 305 
LEU   HD11 H  N N 306 
LEU   HD12 H  N N 307 
LEU   HD13 H  N N 308 
LEU   HD21 H  N N 309 
LEU   HD22 H  N N 310 
LEU   HD23 H  N N 311 
LEU   HXT  H  N N 312 
LYS   N    N  N N 313 
LYS   CA   C  N S 314 
LYS   C    C  N N 315 
LYS   O    O  N N 316 
LYS   CB   C  N N 317 
LYS   CG   C  N N 318 
LYS   CD   C  N N 319 
LYS   CE   C  N N 320 
LYS   NZ   N  N N 321 
LYS   OXT  O  N N 322 
LYS   H    H  N N 323 
LYS   H2   H  N N 324 
LYS   HA   H  N N 325 
LYS   HB2  H  N N 326 
LYS   HB3  H  N N 327 
LYS   HG2  H  N N 328 
LYS   HG3  H  N N 329 
LYS   HD2  H  N N 330 
LYS   HD3  H  N N 331 
LYS   HE2  H  N N 332 
LYS   HE3  H  N N 333 
LYS   HZ1  H  N N 334 
LYS   HZ2  H  N N 335 
LYS   HZ3  H  N N 336 
LYS   HXT  H  N N 337 
MET   N    N  N N 338 
MET   CA   C  N S 339 
MET   C    C  N N 340 
MET   O    O  N N 341 
MET   CB   C  N N 342 
MET   CG   C  N N 343 
MET   SD   S  N N 344 
MET   CE   C  N N 345 
MET   OXT  O  N N 346 
MET   H    H  N N 347 
MET   H2   H  N N 348 
MET   HA   H  N N 349 
MET   HB2  H  N N 350 
MET   HB3  H  N N 351 
MET   HG2  H  N N 352 
MET   HG3  H  N N 353 
MET   HE1  H  N N 354 
MET   HE2  H  N N 355 
MET   HE3  H  N N 356 
MET   HXT  H  N N 357 
NAG   C1   C  N R 358 
NAG   C2   C  N R 359 
NAG   C3   C  N R 360 
NAG   C4   C  N S 361 
NAG   C5   C  N R 362 
NAG   C6   C  N N 363 
NAG   C7   C  N N 364 
NAG   C8   C  N N 365 
NAG   N2   N  N N 366 
NAG   O1   O  N N 367 
NAG   O3   O  N N 368 
NAG   O4   O  N N 369 
NAG   O5   O  N N 370 
NAG   O6   O  N N 371 
NAG   O7   O  N N 372 
NAG   H1   H  N N 373 
NAG   H2   H  N N 374 
NAG   H3   H  N N 375 
NAG   H4   H  N N 376 
NAG   H5   H  N N 377 
NAG   H61  H  N N 378 
NAG   H62  H  N N 379 
NAG   H81  H  N N 380 
NAG   H82  H  N N 381 
NAG   H83  H  N N 382 
NAG   HN2  H  N N 383 
NAG   HO1  H  N N 384 
NAG   HO3  H  N N 385 
NAG   HO4  H  N N 386 
NAG   HO6  H  N N 387 
PHE   N    N  N N 388 
PHE   CA   C  N S 389 
PHE   C    C  N N 390 
PHE   O    O  N N 391 
PHE   CB   C  N N 392 
PHE   CG   C  Y N 393 
PHE   CD1  C  Y N 394 
PHE   CD2  C  Y N 395 
PHE   CE1  C  Y N 396 
PHE   CE2  C  Y N 397 
PHE   CZ   C  Y N 398 
PHE   OXT  O  N N 399 
PHE   H    H  N N 400 
PHE   H2   H  N N 401 
PHE   HA   H  N N 402 
PHE   HB2  H  N N 403 
PHE   HB3  H  N N 404 
PHE   HD1  H  N N 405 
PHE   HD2  H  N N 406 
PHE   HE1  H  N N 407 
PHE   HE2  H  N N 408 
PHE   HZ   H  N N 409 
PHE   HXT  H  N N 410 
PRO   N    N  N N 411 
PRO   CA   C  N S 412 
PRO   C    C  N N 413 
PRO   O    O  N N 414 
PRO   CB   C  N N 415 
PRO   CG   C  N N 416 
PRO   CD   C  N N 417 
PRO   OXT  O  N N 418 
PRO   H    H  N N 419 
PRO   HA   H  N N 420 
PRO   HB2  H  N N 421 
PRO   HB3  H  N N 422 
PRO   HG2  H  N N 423 
PRO   HG3  H  N N 424 
PRO   HD2  H  N N 425 
PRO   HD3  H  N N 426 
PRO   HXT  H  N N 427 
SER   N    N  N N 428 
SER   CA   C  N S 429 
SER   C    C  N N 430 
SER   O    O  N N 431 
SER   CB   C  N N 432 
SER   OG   O  N N 433 
SER   OXT  O  N N 434 
SER   H    H  N N 435 
SER   H2   H  N N 436 
SER   HA   H  N N 437 
SER   HB2  H  N N 438 
SER   HB3  H  N N 439 
SER   HG   H  N N 440 
SER   HXT  H  N N 441 
THR   N    N  N N 442 
THR   CA   C  N S 443 
THR   C    C  N N 444 
THR   O    O  N N 445 
THR   CB   C  N R 446 
THR   OG1  O  N N 447 
THR   CG2  C  N N 448 
THR   OXT  O  N N 449 
THR   H    H  N N 450 
THR   H2   H  N N 451 
THR   HA   H  N N 452 
THR   HB   H  N N 453 
THR   HG1  H  N N 454 
THR   HG21 H  N N 455 
THR   HG22 H  N N 456 
THR   HG23 H  N N 457 
THR   HXT  H  N N 458 
TRP   N    N  N N 459 
TRP   CA   C  N S 460 
TRP   C    C  N N 461 
TRP   O    O  N N 462 
TRP   CB   C  N N 463 
TRP   CG   C  Y N 464 
TRP   CD1  C  Y N 465 
TRP   CD2  C  Y N 466 
TRP   NE1  N  Y N 467 
TRP   CE2  C  Y N 468 
TRP   CE3  C  Y N 469 
TRP   CZ2  C  Y N 470 
TRP   CZ3  C  Y N 471 
TRP   CH2  C  Y N 472 
TRP   OXT  O  N N 473 
TRP   H    H  N N 474 
TRP   H2   H  N N 475 
TRP   HA   H  N N 476 
TRP   HB2  H  N N 477 
TRP   HB3  H  N N 478 
TRP   HD1  H  N N 479 
TRP   HE1  H  N N 480 
TRP   HE3  H  N N 481 
TRP   HZ2  H  N N 482 
TRP   HZ3  H  N N 483 
TRP   HH2  H  N N 484 
TRP   HXT  H  N N 485 
TYR   N    N  N N 486 
TYR   CA   C  N S 487 
TYR   C    C  N N 488 
TYR   O    O  N N 489 
TYR   CB   C  N N 490 
TYR   CG   C  Y N 491 
TYR   CD1  C  Y N 492 
TYR   CD2  C  Y N 493 
TYR   CE1  C  Y N 494 
TYR   CE2  C  Y N 495 
TYR   CZ   C  Y N 496 
TYR   OH   O  N N 497 
TYR   OXT  O  N N 498 
TYR   H    H  N N 499 
TYR   H2   H  N N 500 
TYR   HA   H  N N 501 
TYR   HB2  H  N N 502 
TYR   HB3  H  N N 503 
TYR   HD1  H  N N 504 
TYR   HD2  H  N N 505 
TYR   HE1  H  N N 506 
TYR   HE2  H  N N 507 
TYR   HH   H  N N 508 
TYR   HXT  H  N N 509 
VAL   N    N  N N 510 
VAL   CA   C  N S 511 
VAL   C    C  N N 512 
VAL   O    O  N N 513 
VAL   CB   C  N N 514 
VAL   CG1  C  N N 515 
VAL   CG2  C  N N 516 
VAL   OXT  O  N N 517 
VAL   H    H  N N 518 
VAL   H2   H  N N 519 
VAL   HA   H  N N 520 
VAL   HB   H  N N 521 
VAL   HG11 H  N N 522 
VAL   HG12 H  N N 523 
VAL   HG13 H  N N 524 
VAL   HG21 H  N N 525 
VAL   HG22 H  N N 526 
VAL   HG23 H  N N 527 
VAL   HXT  H  N N 528 
ZN    ZN   ZN N N 529 
# 
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 
A1IJY O17 C16  doub N N 1   
A1IJY C19 C20  doub Y N 2   
A1IJY C19 C15  sing Y N 3   
A1IJY C16 O18  sing N N 4   
A1IJY C16 C15  sing N N 5   
A1IJY C20 C12  sing Y N 6   
A1IJY C15 C14  doub Y N 7   
A1IJY C12 C11  sing N N 8   
A1IJY C12 C13  doub Y N 9   
A1IJY O21 C11  doub N N 10  
A1IJY C11 N10  sing N N 11  
A1IJY C14 C13  sing Y N 12  
A1IJY N10 C09  sing N N 13  
A1IJY N10 C06  sing N N 14  
A1IJY C07 C08  sing N N 15  
A1IJY C07 C06  sing N N 16  
A1IJY C09 C08  sing N N 17  
A1IJY C06 C05  sing N N 18  
A1IJY C05 C22  sing N N 19  
A1IJY C05 N04  sing N N 20  
A1IJY O24 C22  doub N N 21  
A1IJY C22 O23  sing N N 22  
A1IJY N04 C03  sing N N 23  
A1IJY C03 C25  sing N N 24  
A1IJY C03 C02  sing N N 25  
A1IJY O01 C02  doub N N 26  
A1IJY C02 N26  sing N N 27  
A1IJY N26 C27  sing N N 28  
A1IJY N26 C30  sing N N 29  
A1IJY C27 C28  sing N N 30  
A1IJY C30 C31  sing N N 31  
A1IJY C30 C29  sing N N 32  
A1IJY O33 C31  doub N N 33  
A1IJY C31 O32  sing N N 34  
A1IJY C28 C29  sing N N 35  
A1IJY C03 H1   sing N N 36  
A1IJY N04 H2   sing N N 37  
A1IJY C05 H4   sing N N 38  
A1IJY C06 H5   sing N N 39  
A1IJY C07 H6   sing N N 40  
A1IJY C07 H7   sing N N 41  
A1IJY C08 H8   sing N N 42  
A1IJY C08 H9   sing N N 43  
A1IJY C09 H10  sing N N 44  
A1IJY C09 H11  sing N N 45  
A1IJY C13 H12  sing N N 46  
A1IJY C14 H13  sing N N 47  
A1IJY O18 H14  sing N N 48  
A1IJY C19 H15  sing N N 49  
A1IJY C20 H16  sing N N 50  
A1IJY O23 H17  sing N N 51  
A1IJY C25 H18  sing N N 52  
A1IJY C25 H19  sing N N 53  
A1IJY C25 H20  sing N N 54  
A1IJY C27 H21  sing N N 55  
A1IJY C27 H22  sing N N 56  
A1IJY C28 H23  sing N N 57  
A1IJY C28 H24  sing N N 58  
A1IJY C29 H25  sing N N 59  
A1IJY C29 H26  sing N N 60  
A1IJY C30 H27  sing N N 61  
A1IJY O32 H28  sing N N 62  
ALA   N   CA   sing N N 63  
ALA   N   H    sing N N 64  
ALA   N   H2   sing N N 65  
ALA   CA  C    sing N N 66  
ALA   CA  CB   sing N N 67  
ALA   CA  HA   sing N N 68  
ALA   C   O    doub N N 69  
ALA   C   OXT  sing N N 70  
ALA   CB  HB1  sing N N 71  
ALA   CB  HB2  sing N N 72  
ALA   CB  HB3  sing N N 73  
ALA   OXT HXT  sing N N 74  
ARG   N   CA   sing N N 75  
ARG   N   H    sing N N 76  
ARG   N   H2   sing N N 77  
ARG   CA  C    sing N N 78  
ARG   CA  CB   sing N N 79  
ARG   CA  HA   sing N N 80  
ARG   C   O    doub N N 81  
ARG   C   OXT  sing N N 82  
ARG   CB  CG   sing N N 83  
ARG   CB  HB2  sing N N 84  
ARG   CB  HB3  sing N N 85  
ARG   CG  CD   sing N N 86  
ARG   CG  HG2  sing N N 87  
ARG   CG  HG3  sing N N 88  
ARG   CD  NE   sing N N 89  
ARG   CD  HD2  sing N N 90  
ARG   CD  HD3  sing N N 91  
ARG   NE  CZ   sing N N 92  
ARG   NE  HE   sing N N 93  
ARG   CZ  NH1  sing N N 94  
ARG   CZ  NH2  doub N N 95  
ARG   NH1 HH11 sing N N 96  
ARG   NH1 HH12 sing N N 97  
ARG   NH2 HH21 sing N N 98  
ARG   NH2 HH22 sing N N 99  
ARG   OXT HXT  sing N N 100 
ASN   N   CA   sing N N 101 
ASN   N   H    sing N N 102 
ASN   N   H2   sing N N 103 
ASN   CA  C    sing N N 104 
ASN   CA  CB   sing N N 105 
ASN   CA  HA   sing N N 106 
ASN   C   O    doub N N 107 
ASN   C   OXT  sing N N 108 
ASN   CB  CG   sing N N 109 
ASN   CB  HB2  sing N N 110 
ASN   CB  HB3  sing N N 111 
ASN   CG  OD1  doub N N 112 
ASN   CG  ND2  sing N N 113 
ASN   ND2 HD21 sing N N 114 
ASN   ND2 HD22 sing N N 115 
ASN   OXT HXT  sing N N 116 
ASP   N   CA   sing N N 117 
ASP   N   H    sing N N 118 
ASP   N   H2   sing N N 119 
ASP   CA  C    sing N N 120 
ASP   CA  CB   sing N N 121 
ASP   CA  HA   sing N N 122 
ASP   C   O    doub N N 123 
ASP   C   OXT  sing N N 124 
ASP   CB  CG   sing N N 125 
ASP   CB  HB2  sing N N 126 
ASP   CB  HB3  sing N N 127 
ASP   CG  OD1  doub N N 128 
ASP   CG  OD2  sing N N 129 
ASP   OD2 HD2  sing N N 130 
ASP   OXT HXT  sing N N 131 
BMA   C1  C2   sing N N 132 
BMA   C1  O1   sing N N 133 
BMA   C1  O5   sing N N 134 
BMA   C1  H1   sing N N 135 
BMA   C2  C3   sing N N 136 
BMA   C2  O2   sing N N 137 
BMA   C2  H2   sing N N 138 
BMA   C3  C4   sing N N 139 
BMA   C3  O3   sing N N 140 
BMA   C3  H3   sing N N 141 
BMA   C4  C5   sing N N 142 
BMA   C4  O4   sing N N 143 
BMA   C4  H4   sing N N 144 
BMA   C5  C6   sing N N 145 
BMA   C5  O5   sing N N 146 
BMA   C5  H5   sing N N 147 
BMA   C6  O6   sing N N 148 
BMA   C6  H61  sing N N 149 
BMA   C6  H62  sing N N 150 
BMA   O1  HO1  sing N N 151 
BMA   O2  HO2  sing N N 152 
BMA   O3  HO3  sing N N 153 
BMA   O4  HO4  sing N N 154 
BMA   O6  HO6  sing N N 155 
CYS   N   CA   sing N N 156 
CYS   N   H    sing N N 157 
CYS   N   H2   sing N N 158 
CYS   CA  C    sing N N 159 
CYS   CA  CB   sing N N 160 
CYS   CA  HA   sing N N 161 
CYS   C   O    doub N N 162 
CYS   C   OXT  sing N N 163 
CYS   CB  SG   sing N N 164 
CYS   CB  HB2  sing N N 165 
CYS   CB  HB3  sing N N 166 
CYS   SG  HG   sing N N 167 
CYS   OXT HXT  sing N N 168 
FUC   C1  C2   sing N N 169 
FUC   C1  O1   sing N N 170 
FUC   C1  O5   sing N N 171 
FUC   C1  H1   sing N N 172 
FUC   C2  C3   sing N N 173 
FUC   C2  O2   sing N N 174 
FUC   C2  H2   sing N N 175 
FUC   C3  C4   sing N N 176 
FUC   C3  O3   sing N N 177 
FUC   C3  H3   sing N N 178 
FUC   C4  C5   sing N N 179 
FUC   C4  O4   sing N N 180 
FUC   C4  H4   sing N N 181 
FUC   C5  C6   sing N N 182 
FUC   C5  O5   sing N N 183 
FUC   C5  H5   sing N N 184 
FUC   C6  H61  sing N N 185 
FUC   C6  H62  sing N N 186 
FUC   C6  H63  sing N N 187 
FUC   O1  HO1  sing N N 188 
FUC   O2  HO2  sing N N 189 
FUC   O3  HO3  sing N N 190 
FUC   O4  HO4  sing N N 191 
GLN   N   CA   sing N N 192 
GLN   N   H    sing N N 193 
GLN   N   H2   sing N N 194 
GLN   CA  C    sing N N 195 
GLN   CA  CB   sing N N 196 
GLN   CA  HA   sing N N 197 
GLN   C   O    doub N N 198 
GLN   C   OXT  sing N N 199 
GLN   CB  CG   sing N N 200 
GLN   CB  HB2  sing N N 201 
GLN   CB  HB3  sing N N 202 
GLN   CG  CD   sing N N 203 
GLN   CG  HG2  sing N N 204 
GLN   CG  HG3  sing N N 205 
GLN   CD  OE1  doub N N 206 
GLN   CD  NE2  sing N N 207 
GLN   NE2 HE21 sing N N 208 
GLN   NE2 HE22 sing N N 209 
GLN   OXT HXT  sing N N 210 
GLU   N   CA   sing N N 211 
GLU   N   H    sing N N 212 
GLU   N   H2   sing N N 213 
GLU   CA  C    sing N N 214 
GLU   CA  CB   sing N N 215 
GLU   CA  HA   sing N N 216 
GLU   C   O    doub N N 217 
GLU   C   OXT  sing N N 218 
GLU   CB  CG   sing N N 219 
GLU   CB  HB2  sing N N 220 
GLU   CB  HB3  sing N N 221 
GLU   CG  CD   sing N N 222 
GLU   CG  HG2  sing N N 223 
GLU   CG  HG3  sing N N 224 
GLU   CD  OE1  doub N N 225 
GLU   CD  OE2  sing N N 226 
GLU   OE2 HE2  sing N N 227 
GLU   OXT HXT  sing N N 228 
GLY   N   CA   sing N N 229 
GLY   N   H    sing N N 230 
GLY   N   H2   sing N N 231 
GLY   CA  C    sing N N 232 
GLY   CA  HA2  sing N N 233 
GLY   CA  HA3  sing N N 234 
GLY   C   O    doub N N 235 
GLY   C   OXT  sing N N 236 
GLY   OXT HXT  sing N N 237 
HIS   N   CA   sing N N 238 
HIS   N   H    sing N N 239 
HIS   N   H2   sing N N 240 
HIS   CA  C    sing N N 241 
HIS   CA  CB   sing N N 242 
HIS   CA  HA   sing N N 243 
HIS   C   O    doub N N 244 
HIS   C   OXT  sing N N 245 
HIS   CB  CG   sing N N 246 
HIS   CB  HB2  sing N N 247 
HIS   CB  HB3  sing N N 248 
HIS   CG  ND1  sing Y N 249 
HIS   CG  CD2  doub Y N 250 
HIS   ND1 CE1  doub Y N 251 
HIS   ND1 HD1  sing N N 252 
HIS   CD2 NE2  sing Y N 253 
HIS   CD2 HD2  sing N N 254 
HIS   CE1 NE2  sing Y N 255 
HIS   CE1 HE1  sing N N 256 
HIS   NE2 HE2  sing N N 257 
HIS   OXT HXT  sing N N 258 
HOH   O   H1   sing N N 259 
HOH   O   H2   sing N N 260 
ILE   N   CA   sing N N 261 
ILE   N   H    sing N N 262 
ILE   N   H2   sing N N 263 
ILE   CA  C    sing N N 264 
ILE   CA  CB   sing N N 265 
ILE   CA  HA   sing N N 266 
ILE   C   O    doub N N 267 
ILE   C   OXT  sing N N 268 
ILE   CB  CG1  sing N N 269 
ILE   CB  CG2  sing N N 270 
ILE   CB  HB   sing N N 271 
ILE   CG1 CD1  sing N N 272 
ILE   CG1 HG12 sing N N 273 
ILE   CG1 HG13 sing N N 274 
ILE   CG2 HG21 sing N N 275 
ILE   CG2 HG22 sing N N 276 
ILE   CG2 HG23 sing N N 277 
ILE   CD1 HD11 sing N N 278 
ILE   CD1 HD12 sing N N 279 
ILE   CD1 HD13 sing N N 280 
ILE   OXT HXT  sing N N 281 
LEU   N   CA   sing N N 282 
LEU   N   H    sing N N 283 
LEU   N   H2   sing N N 284 
LEU   CA  C    sing N N 285 
LEU   CA  CB   sing N N 286 
LEU   CA  HA   sing N N 287 
LEU   C   O    doub N N 288 
LEU   C   OXT  sing N N 289 
LEU   CB  CG   sing N N 290 
LEU   CB  HB2  sing N N 291 
LEU   CB  HB3  sing N N 292 
LEU   CG  CD1  sing N N 293 
LEU   CG  CD2  sing N N 294 
LEU   CG  HG   sing N N 295 
LEU   CD1 HD11 sing N N 296 
LEU   CD1 HD12 sing N N 297 
LEU   CD1 HD13 sing N N 298 
LEU   CD2 HD21 sing N N 299 
LEU   CD2 HD22 sing N N 300 
LEU   CD2 HD23 sing N N 301 
LEU   OXT HXT  sing N N 302 
LYS   N   CA   sing N N 303 
LYS   N   H    sing N N 304 
LYS   N   H2   sing N N 305 
LYS   CA  C    sing N N 306 
LYS   CA  CB   sing N N 307 
LYS   CA  HA   sing N N 308 
LYS   C   O    doub N N 309 
LYS   C   OXT  sing N N 310 
LYS   CB  CG   sing N N 311 
LYS   CB  HB2  sing N N 312 
LYS   CB  HB3  sing N N 313 
LYS   CG  CD   sing N N 314 
LYS   CG  HG2  sing N N 315 
LYS   CG  HG3  sing N N 316 
LYS   CD  CE   sing N N 317 
LYS   CD  HD2  sing N N 318 
LYS   CD  HD3  sing N N 319 
LYS   CE  NZ   sing N N 320 
LYS   CE  HE2  sing N N 321 
LYS   CE  HE3  sing N N 322 
LYS   NZ  HZ1  sing N N 323 
LYS   NZ  HZ2  sing N N 324 
LYS   NZ  HZ3  sing N N 325 
LYS   OXT HXT  sing N N 326 
MET   N   CA   sing N N 327 
MET   N   H    sing N N 328 
MET   N   H2   sing N N 329 
MET   CA  C    sing N N 330 
MET   CA  CB   sing N N 331 
MET   CA  HA   sing N N 332 
MET   C   O    doub N N 333 
MET   C   OXT  sing N N 334 
MET   CB  CG   sing N N 335 
MET   CB  HB2  sing N N 336 
MET   CB  HB3  sing N N 337 
MET   CG  SD   sing N N 338 
MET   CG  HG2  sing N N 339 
MET   CG  HG3  sing N N 340 
MET   SD  CE   sing N N 341 
MET   CE  HE1  sing N N 342 
MET   CE  HE2  sing N N 343 
MET   CE  HE3  sing N N 344 
MET   OXT HXT  sing N N 345 
NAG   C1  C2   sing N N 346 
NAG   C1  O1   sing N N 347 
NAG   C1  O5   sing N N 348 
NAG   C1  H1   sing N N 349 
NAG   C2  C3   sing N N 350 
NAG   C2  N2   sing N N 351 
NAG   C2  H2   sing N N 352 
NAG   C3  C4   sing N N 353 
NAG   C3  O3   sing N N 354 
NAG   C3  H3   sing N N 355 
NAG   C4  C5   sing N N 356 
NAG   C4  O4   sing N N 357 
NAG   C4  H4   sing N N 358 
NAG   C5  C6   sing N N 359 
NAG   C5  O5   sing N N 360 
NAG   C5  H5   sing N N 361 
NAG   C6  O6   sing N N 362 
NAG   C6  H61  sing N N 363 
NAG   C6  H62  sing N N 364 
NAG   C7  C8   sing N N 365 
NAG   C7  N2   sing N N 366 
NAG   C7  O7   doub N N 367 
NAG   C8  H81  sing N N 368 
NAG   C8  H82  sing N N 369 
NAG   C8  H83  sing N N 370 
NAG   N2  HN2  sing N N 371 
NAG   O1  HO1  sing N N 372 
NAG   O3  HO3  sing N N 373 
NAG   O4  HO4  sing N N 374 
NAG   O6  HO6  sing N N 375 
PHE   N   CA   sing N N 376 
PHE   N   H    sing N N 377 
PHE   N   H2   sing N N 378 
PHE   CA  C    sing N N 379 
PHE   CA  CB   sing N N 380 
PHE   CA  HA   sing N N 381 
PHE   C   O    doub N N 382 
PHE   C   OXT  sing N N 383 
PHE   CB  CG   sing N N 384 
PHE   CB  HB2  sing N N 385 
PHE   CB  HB3  sing N N 386 
PHE   CG  CD1  doub Y N 387 
PHE   CG  CD2  sing Y N 388 
PHE   CD1 CE1  sing Y N 389 
PHE   CD1 HD1  sing N N 390 
PHE   CD2 CE2  doub Y N 391 
PHE   CD2 HD2  sing N N 392 
PHE   CE1 CZ   doub Y N 393 
PHE   CE1 HE1  sing N N 394 
PHE   CE2 CZ   sing Y N 395 
PHE   CE2 HE2  sing N N 396 
PHE   CZ  HZ   sing N N 397 
PHE   OXT HXT  sing N N 398 
PRO   N   CA   sing N N 399 
PRO   N   CD   sing N N 400 
PRO   N   H    sing N N 401 
PRO   CA  C    sing N N 402 
PRO   CA  CB   sing N N 403 
PRO   CA  HA   sing N N 404 
PRO   C   O    doub N N 405 
PRO   C   OXT  sing N N 406 
PRO   CB  CG   sing N N 407 
PRO   CB  HB2  sing N N 408 
PRO   CB  HB3  sing N N 409 
PRO   CG  CD   sing N N 410 
PRO   CG  HG2  sing N N 411 
PRO   CG  HG3  sing N N 412 
PRO   CD  HD2  sing N N 413 
PRO   CD  HD3  sing N N 414 
PRO   OXT HXT  sing N N 415 
SER   N   CA   sing N N 416 
SER   N   H    sing N N 417 
SER   N   H2   sing N N 418 
SER   CA  C    sing N N 419 
SER   CA  CB   sing N N 420 
SER   CA  HA   sing N N 421 
SER   C   O    doub N N 422 
SER   C   OXT  sing N N 423 
SER   CB  OG   sing N N 424 
SER   CB  HB2  sing N N 425 
SER   CB  HB3  sing N N 426 
SER   OG  HG   sing N N 427 
SER   OXT HXT  sing N N 428 
THR   N   CA   sing N N 429 
THR   N   H    sing N N 430 
THR   N   H2   sing N N 431 
THR   CA  C    sing N N 432 
THR   CA  CB   sing N N 433 
THR   CA  HA   sing N N 434 
THR   C   O    doub N N 435 
THR   C   OXT  sing N N 436 
THR   CB  OG1  sing N N 437 
THR   CB  CG2  sing N N 438 
THR   CB  HB   sing N N 439 
THR   OG1 HG1  sing N N 440 
THR   CG2 HG21 sing N N 441 
THR   CG2 HG22 sing N N 442 
THR   CG2 HG23 sing N N 443 
THR   OXT HXT  sing N N 444 
TRP   N   CA   sing N N 445 
TRP   N   H    sing N N 446 
TRP   N   H2   sing N N 447 
TRP   CA  C    sing N N 448 
TRP   CA  CB   sing N N 449 
TRP   CA  HA   sing N N 450 
TRP   C   O    doub N N 451 
TRP   C   OXT  sing N N 452 
TRP   CB  CG   sing N N 453 
TRP   CB  HB2  sing N N 454 
TRP   CB  HB3  sing N N 455 
TRP   CG  CD1  doub Y N 456 
TRP   CG  CD2  sing Y N 457 
TRP   CD1 NE1  sing Y N 458 
TRP   CD1 HD1  sing N N 459 
TRP   CD2 CE2  doub Y N 460 
TRP   CD2 CE3  sing Y N 461 
TRP   NE1 CE2  sing Y N 462 
TRP   NE1 HE1  sing N N 463 
TRP   CE2 CZ2  sing Y N 464 
TRP   CE3 CZ3  doub Y N 465 
TRP   CE3 HE3  sing N N 466 
TRP   CZ2 CH2  doub Y N 467 
TRP   CZ2 HZ2  sing N N 468 
TRP   CZ3 CH2  sing Y N 469 
TRP   CZ3 HZ3  sing N N 470 
TRP   CH2 HH2  sing N N 471 
TRP   OXT HXT  sing N N 472 
TYR   N   CA   sing N N 473 
TYR   N   H    sing N N 474 
TYR   N   H2   sing N N 475 
TYR   CA  C    sing N N 476 
TYR   CA  CB   sing N N 477 
TYR   CA  HA   sing N N 478 
TYR   C   O    doub N N 479 
TYR   C   OXT  sing N N 480 
TYR   CB  CG   sing N N 481 
TYR   CB  HB2  sing N N 482 
TYR   CB  HB3  sing N N 483 
TYR   CG  CD1  doub Y N 484 
TYR   CG  CD2  sing Y N 485 
TYR   CD1 CE1  sing Y N 486 
TYR   CD1 HD1  sing N N 487 
TYR   CD2 CE2  doub Y N 488 
TYR   CD2 HD2  sing N N 489 
TYR   CE1 CZ   doub Y N 490 
TYR   CE1 HE1  sing N N 491 
TYR   CE2 CZ   sing Y N 492 
TYR   CE2 HE2  sing N N 493 
TYR   CZ  OH   sing N N 494 
TYR   OH  HH   sing N N 495 
TYR   OXT HXT  sing N N 496 
VAL   N   CA   sing N N 497 
VAL   N   H    sing N N 498 
VAL   N   H2   sing N N 499 
VAL   CA  C    sing N N 500 
VAL   CA  CB   sing N N 501 
VAL   CA  HA   sing N N 502 
VAL   C   O    doub N N 503 
VAL   C   OXT  sing N N 504 
VAL   CB  CG1  sing N N 505 
VAL   CB  CG2  sing N N 506 
VAL   CB  HB   sing N N 507 
VAL   CG1 HG11 sing N N 508 
VAL   CG1 HG12 sing N N 509 
VAL   CG1 HG13 sing N N 510 
VAL   CG2 HG21 sing N N 511 
VAL   CG2 HG22 sing N N 512 
VAL   CG2 HG23 sing N N 513 
VAL   OXT HXT  sing N N 514 
# 
_pdbx_audit_support.funding_organization   'Biotechnology and Biological Sciences Research Council (BBSRC)' 
_pdbx_audit_support.country                'United Kingdom' 
_pdbx_audit_support.grant_number           BB/X001032/1 
_pdbx_audit_support.ordinal                1 
# 
loop_
_pdbx_entity_branch_list.entity_id 
_pdbx_entity_branch_list.comp_id 
_pdbx_entity_branch_list.num 
_pdbx_entity_branch_list.hetero 
2 NAG 1 n 
2 NAG 2 n 
2 BMA 3 n 
2 FUC 4 n 
# 
_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   6F9T 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9GBL 
_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]   0.017599 
_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]   0.011671 
_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]   0.007401 
_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 
_atom_type.pdbx_scat_Z 
_atom_type.pdbx_N_electrons 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
C  6  6  2.3103  20.8439 1.0201 10.2075 1.5888 0.5687  0.8651 51.6512 0.2156   
CL 17 17 11.4601 0.0104  7.1962 1.1662  6.2554 18.5194 1.6455 47.7784 -9.3453  
N  7  7  12.2220 0.0057  3.1346 9.8933  2.0141 28.9975 1.1672 0.5826  -11.5379 
O  8  8  3.0487  13.2771 2.2870 5.7011  1.5464 0.3239  0.8671 32.9089 0.2508   
S  16 16 6.9054  1.4679  5.2035 22.2151 1.4379 0.2536  1.5863 56.1720 1.0486   
ZN 30 30 14.0812 3.2655  7.0352 0.2333  5.1677 10.3163 2.4112 58.7097 1.0042   
# 
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   . ASP   A 1 4   ? -8.006  29.303  -1.604 1    71.147  ? 40  ASP   A N   1 
ATOM   2    C  CA  . ASP   A 1 4   ? -8.063  29.984  -0.279 1    96.027  ? 40  ASP   A CA  1 
ATOM   3    C  C   . ASP   A 1 4   ? -8.389  28.938  0.798  1    88.105  ? 40  ASP   A C   1 
ATOM   4    O  O   . ASP   A 1 4   ? -7.596  28.026  1.058  1    72.896  ? 40  ASP   A O   1 
ATOM   5    C  CB  . ASP   A 1 4   ? -9.012  31.179  -0.387 1    103.687 ? 40  ASP   A CB  1 
ATOM   6    C  CG  . ASP   A 1 4   ? -8.762  32.338  0.577  1    106.892 ? 40  ASP   A CG  1 
ATOM   7    O  OD1 . ASP   A 1 4   ? -7.583  32.762  0.706  1    102.57  ? 40  ASP   A OD1 1 
ATOM   8    O  OD2 . ASP   A 1 4   ? -9.748  32.824  1.181  1    84.656  ? 40  ASP   A OD2 1 
ATOM   9    N  N   . GLU   A 1 5   ? -9.579  29.105  1.403  1    75.256  ? 41  GLU   A N   1 
ATOM   10   C  CA  . GLU   A 1 5   ? -10.354 28.112  2.13   1    62.471  ? 41  GLU   A CA  1 
ATOM   11   C  C   . GLU   A 1 5   ? -11.052 27.156  1.15   1    70.247  ? 41  GLU   A C   1 
ATOM   12   O  O   . GLU   A 1 5   ? -11.57  26.094  1.533  1    56.535  ? 41  GLU   A O   1 
ATOM   13   C  CB  . GLU   A 1 5   ? -11.419 28.958  2.828  1    62.401  ? 41  GLU   A CB  1 
ATOM   14   C  CG  . GLU   A 1 5   ? -12.289 28.202  3.831  1    79.324  ? 41  GLU   A CG  1 
ATOM   15   C  CD  . GLU   A 1 5   ? -11.892 28.232  5.308  1    97.63   ? 41  GLU   A CD  1 
ATOM   16   O  OE1 . GLU   A 1 5   ? -12.877 28.378  6.075  1    92.486  ? 41  GLU   A OE1 1 
ATOM   17   O  OE2 . GLU   A 1 5   ? -10.689 28.121  5.708  1    74.853  ? 41  GLU   A OE2 1 
ATOM   18   N  N   . ALA   A 1 6   ? -11.088 27.526  -0.14  1    58.298  ? 42  ALA   A N   1 
ATOM   19   C  CA  . ALA   A 1 6   ? -11.855 26.695  -1.052 1    58.245  ? 42  ALA   A CA  1 
ATOM   20   C  C   . ALA   A 1 6   ? -11.024 25.549  -1.654 1    53.992  ? 42  ALA   A C   1 
ATOM   21   O  O   . ALA   A 1 6   ? -11.612 24.558  -2.074 1    53.942  ? 42  ALA   A O   1 
ATOM   22   C  CB  . ALA   A 1 6   ? -12.619 27.526  -2.064 1    62.498  ? 42  ALA   A CB  1 
ATOM   23   N  N   . GLU   A 1 7   ? -9.682  25.662  -1.689 1    41.322  ? 43  GLU   A N   1 
ATOM   24   C  CA  . GLU   A 1 7   ? -8.806  24.534  -2.011 1    54.48   ? 43  GLU   A CA  1 
ATOM   25   C  C   . GLU   A 1 7   ? -8.868  23.41   -0.958 1    53.302  ? 43  GLU   A C   1 
ATOM   26   O  O   . GLU   A 1 7   ? -8.706  22.231  -1.323 1    41.666  ? 43  GLU   A O   1 
ATOM   27   C  CB  . GLU   A 1 7   ? -7.325  24.86   -2.268 1    59.733  ? 43  GLU   A CB  1 
ATOM   28   C  CG  . GLU   A 1 7   ? -6.961  25.009  -3.748 1    77.882  ? 43  GLU   A CG  1 
ATOM   29   C  CD  . GLU   A 1 7   ? -5.53   24.71   -4.196 1    99.222  ? 43  GLU   A CD  1 
ATOM   30   O  OE1 . GLU   A 1 7   ? -4.744  24.139  -3.399 1    82.308  ? 43  GLU   A OE1 1 
ATOM   31   O  OE2 . GLU   A 1 7   ? -5.201  25.047  -5.365 1    120.253 ? 43  GLU   A OE2 1 
ATOM   32   N  N   . ALA   A 1 8   ? -9.063  23.795  0.325  1    44.256  ? 44  ALA   A N   1 
ATOM   33   C  CA  . ALA   A 1 8   ? -9.229  22.894  1.462  1    37.403  ? 44  ALA   A CA  1 
ATOM   34   C  C   . ALA   A 1 8   ? -10.529 22.102  1.343  1    33.909  ? 44  ALA   A C   1 
ATOM   35   O  O   . ALA   A 1 8   ? -10.543 20.887  1.516  1    35.984  ? 44  ALA   A O   1 
ATOM   36   C  CB  . ALA   A 1 8   ? -9.219  23.686  2.765  1    34.14   ? 44  ALA   A CB  1 
ATOM   37   N  N   . SER   A 1 9   ? -11.617 22.811  1.052  1    29.316  ? 45  SER   A N   1 
ATOM   38   C  CA  . SER   A 1 9   ? -12.914 22.237  0.752  1    37.001  ? 45  SER   A CA  1 
ATOM   39   C  C   . SER   A 1 9   ? -12.825 21.156  -0.333 1    44.104  ? 45  SER   A C   1 
ATOM   40   O  O   . SER   A 1 9   ? -13.258 20.032  -0.087 1    53.955  ? 45  SER   A O   1 
ATOM   41   C  CB  . SER   A 1 9   ? -13.901 23.327  0.364  1    38.4    ? 45  SER   A CB  1 
ATOM   42   O  OG  . SER   A 1 9   ? -15.005 23.305  1.257  1    41.795  ? 45  SER   A OG  1 
ATOM   43   N  N   . LYS   A 1 10  ? -12.243 21.495  -1.5   1    40.621  ? 46  LYS   A N   1 
ATOM   44   C  CA  . LYS   A 1 10  ? -12.011 20.618  -2.647 1    37.186  ? 46  LYS   A CA  1 
ATOM   45   C  C   . LYS   A 1 10  ? -11.131 19.413  -2.264 1    38.691  ? 46  LYS   A C   1 
ATOM   46   O  O   . LYS   A 1 10  ? -11.384 18.271  -2.715 1    30.156  ? 46  LYS   A O   1 
ATOM   47   C  CB  . LYS   A 1 10  ? -11.348 21.383  -3.809 1    36.988  ? 46  LYS   A CB  1 
ATOM   48   C  CG  . LYS   A 1 10  ? -11.693 20.931  -5.243 1    47.846  ? 46  LYS   A CG  1 
ATOM   49   C  CD  . LYS   A 1 10  ? -10.873 21.495  -6.403 1    49.284  ? 46  LYS   A CD  1 
ATOM   50   C  CE  . LYS   A 1 10  ? -9.724  20.557  -6.661 1    57.426  ? 46  LYS   A CE  1 
ATOM   51   N  NZ  . LYS   A 1 10  ? -8.487  21.114  -7.227 1    69.355  ? 46  LYS   A NZ  1 
ATOM   52   N  N   . PHE   A 1 11  ? -10.079 19.648  -1.443 1    30.835  ? 47  PHE   A N   1 
ATOM   53   C  CA  . PHE   A 1 11  ? -9.261  18.512  -1.051 1    29.123  ? 47  PHE   A CA  1 
ATOM   54   C  C   . PHE   A 1 11  ? -10.115 17.565  -0.191 1    33.376  ? 47  PHE   A C   1 
ATOM   55   O  O   . PHE   A 1 11  ? -10.221 16.35   -0.452 1    35.592  ? 47  PHE   A O   1 
ATOM   56   C  CB  . PHE   A 1 11  ? -7.925  18.99   -0.505 1    31.524  ? 47  PHE   A CB  1 
ATOM   57   C  CG  . PHE   A 1 11  ? -7.164  17.932  0.269  1    36.59   ? 47  PHE   A CG  1 
ATOM   58   C  CD1 . PHE   A 1 11  ? -7.354  17.789  1.65   1    34.559  ? 47  PHE   A CD1 1 
ATOM   59   C  CD2 . PHE   A 1 11  ? -6.225  17.119  -0.381 1    34.14   ? 47  PHE   A CD2 1 
ATOM   60   C  CE1 . PHE   A 1 11  ? -6.64   16.82   2.354  1    30.166  ? 47  PHE   A CE1 1 
ATOM   61   C  CE2 . PHE   A 1 11  ? -5.49   16.181  0.344  1    35.781  ? 47  PHE   A CE2 1 
ATOM   62   C  CZ  . PHE   A 1 11  ? -5.701  16.032  1.712  1    30.914  ? 47  PHE   A CZ  1 
ATOM   63   N  N   . VAL   A 1 12  ? -10.876 18.119  0.753  1    31.747  ? 48  VAL   A N   1 
ATOM   64   C  CA  . VAL   A 1 12  ? -11.494 17.143  1.639  1    32.839  ? 48  VAL   A CA  1 
ATOM   65   C  C   . VAL   A 1 12  ? -12.543 16.363  0.856  1    32.771  ? 48  VAL   A C   1 
ATOM   66   O  O   . VAL   A 1 12  ? -12.64  15.138  0.977  1    29.297  ? 48  VAL   A O   1 
ATOM   67   C  CB  . VAL   A 1 12  ? -11.939 17.479  3.074  1    30.107  ? 48  VAL   A CB  1 
ATOM   68   C  CG1 . VAL   A 1 12  ? -10.94  18.351  3.806  1    24.251  ? 48  VAL   A CG1 1 
ATOM   69   C  CG2 . VAL   A 1 12  ? -13.322 18.065  3.145  1    27.914  ? 48  VAL   A CG2 1 
ATOM   70   N  N   . GLU   A 1 13  ? -13.266 17.074  -0.012 1    33.371  ? 49  GLU   A N   1 
ATOM   71   C  CA  . GLU   A 1 13  ? -14.195 16.392  -0.902 1    32.312  ? 49  GLU   A CA  1 
ATOM   72   C  C   . GLU   A 1 13  ? -13.493 15.29   -1.692 1    29.893  ? 49  GLU   A C   1 
ATOM   73   O  O   . GLU   A 1 13  ? -14.088 14.214  -1.866 1    26.955  ? 49  GLU   A O   1 
ATOM   74   C  CB  . GLU   A 1 13  ? -14.93  17.309  -1.881 1    40.678  ? 49  GLU   A CB  1 
ATOM   75   C  CG  . GLU   A 1 13  ? -15.903 18.276  -1.198 1    51.408  ? 49  GLU   A CG  1 
ATOM   76   C  CD  . GLU   A 1 13  ? -16.313 19.517  -1.996 1    64.428  ? 49  GLU   A CD  1 
ATOM   77   O  OE1 . GLU   A 1 13  ? -16.21  19.513  -3.255 1    57.522  ? 49  GLU   A OE1 1 
ATOM   78   O  OE2 . GLU   A 1 13  ? -16.684 20.525  -1.342 1    65.39   ? 49  GLU   A OE2 1 
ATOM   79   N  N   . GLU   A 1 14  ? -12.239 15.529  -2.148 1    28.268  ? 50  GLU   A N   1 
ATOM   80   C  CA  . GLU   A 1 14  ? -11.675 14.539  -3.054 1    28.731  ? 50  GLU   A CA  1 
ATOM   81   C  C   . GLU   A 1 14  ? -11.187 13.318  -2.264 1    34.277  ? 50  GLU   A C   1 
ATOM   82   O  O   . GLU   A 1 14  ? -11.376 12.179  -2.703 1    38.478  ? 50  GLU   A O   1 
ATOM   83   C  CB  . GLU   A 1 14  ? -10.561 15.031  -3.977 1    33.477  ? 50  GLU   A CB  1 
ATOM   84   C  CG  . GLU   A 1 14  ? -10.9   16.283  -4.781 1    39.693  ? 50  GLU   A CG  1 
ATOM   85   C  CD  . GLU   A 1 14  ? -9.851  16.554  -5.847 1    46.201  ? 50  GLU   A CD  1 
ATOM   86   O  OE1 . GLU   A 1 14  ? -8.7    16.033  -5.75  1    45.121  ? 50  GLU   A OE1 1 
ATOM   87   O  OE2 . GLU   A 1 14  ? -10.241 17.257  -6.813 1    46.066  ? 50  GLU   A OE2 1 
ATOM   88   N  N   . TYR   A 1 15  ? -10.551 13.561  -1.097 1    39.16   ? 51  TYR   A N   1 
ATOM   89   C  CA  . TYR   A 1 15  ? -10.073 12.508  -0.209 1    31.096  ? 51  TYR   A CA  1 
ATOM   90   C  C   . TYR   A 1 15  ? -11.247 11.622  0.212  1    31.772  ? 51  TYR   A C   1 
ATOM   91   O  O   . TYR   A 1 15  ? -11.153 10.393  0.155  1    32.856  ? 51  TYR   A O   1 
ATOM   92   C  CB  . TYR   A 1 15  ? -9.552  13.301  0.987  1    35.688  ? 51  TYR   A CB  1 
ATOM   93   C  CG  . TYR   A 1 15  ? -9.18   12.344  2.103  1    35.968  ? 51  TYR   A CG  1 
ATOM   94   C  CD1 . TYR   A 1 15  ? -7.999  11.612  2.003  1    29.793  ? 51  TYR   A CD1 1 
ATOM   95   C  CD2 . TYR   A 1 15  ? -10.043 12.097  3.189  1    32.639  ? 51  TYR   A CD2 1 
ATOM   96   C  CE1 . TYR   A 1 15  ? -7.649  10.701  2.983  1    27.726  ? 51  TYR   A CE1 1 
ATOM   97   C  CE2 . TYR   A 1 15  ? -9.666  11.22   4.214  1    30.726  ? 51  TYR   A CE2 1 
ATOM   98   C  CZ  . TYR   A 1 15  ? -8.453  10.545  4.113  1    30.506  ? 51  TYR   A CZ  1 
ATOM   99   O  OH  . TYR   A 1 15  ? -8.026  9.638   5.03   1    27.08   ? 51  TYR   A OH  1 
ATOM   100  N  N   . ASP   A 1 16  ? -12.38  12.253  0.572  1    31.463  ? 52  ASP   A N   1 
ATOM   101  C  CA  . ASP   A 1 16  ? -13.613 11.54   0.887  1    38.432  ? 52  ASP   A CA  1 
ATOM   102  C  C   . ASP   A 1 16  ? -14.093 10.543  -0.192 1    37.574  ? 52  ASP   A C   1 
ATOM   103  O  O   . ASP   A 1 16  ? -14.274 9.369   0.125  1    38.472  ? 52  ASP   A O   1 
ATOM   104  C  CB  . ASP   A 1 16  ? -14.664 12.424  1.543  1    45.973  ? 52  ASP   A CB  1 
ATOM   105  C  CG  . ASP   A 1 16  ? -15.501 11.592  2.5    1    69.683  ? 52  ASP   A CG  1 
ATOM   106  O  OD1 . ASP   A 1 16  ? -14.883 11.041  3.457  1    66.914  ? 52  ASP   A OD1 1 
ATOM   107  O  OD2 . ASP   A 1 16  ? -16.72  11.415  2.224  1    71.535  ? 52  ASP   A OD2 1 
ATOM   108  N  N   . ARG   A 1 17  ? -14.297 10.968  -1.452 1    36.094  ? 53  ARG   A N   1 
ATOM   109  C  CA  . ARG   A 1 17  ? -14.737 10.071  -2.525 1    30.853  ? 53  ARG   A CA  1 
ATOM   110  C  C   . ARG   A 1 17  ? -13.732 8.961   -2.807 1    30.275  ? 53  ARG   A C   1 
ATOM   111  O  O   . ARG   A 1 17  ? -14.134 7.858   -3.114 1    32.94   ? 53  ARG   A O   1 
ATOM   112  C  CB  . ARG   A 1 17  ? -14.537 10.636  -3.929 1    28.973  ? 53  ARG   A CB  1 
ATOM   113  C  CG  . ARG   A 1 17  ? -15.712 11.474  -4.347 1    27.834  ? 53  ARG   A CG  1 
ATOM   114  C  CD  . ARG   A 1 17  ? -15.208 12.299  -5.433 1    24.768  ? 53  ARG   A CD  1 
ATOM   115  N  NE  . ARG   A 1 17  ? -16.122 13.449  -5.374 1    26.68   ? 53  ARG   A NE  1 
ATOM   116  C  CZ  . ARG   A 1 17  ? -15.728 14.689  -5.453 1    24.503  ? 53  ARG   A CZ  1 
ATOM   117  N  NH1 . ARG   A 1 17  ? -14.488 14.998  -5.807 1    27.022  ? 53  ARG   A NH1 1 
ATOM   118  N  NH2 . ARG   A 1 17  ? -16.594 15.616  -5.133 1    26.239  ? 53  ARG   A NH2 1 
ATOM   119  N  N   . THR   A 1 18  ? -12.43  9.253   -2.787 1    35.473  ? 54  THR   A N   1 
ATOM   120  C  CA  . THR   A 1 18  ? -11.478 8.229   -3.193 1    39.514  ? 54  THR   A CA  1 
ATOM   121  C  C   . THR   A 1 18  ? -11.205 7.297   -1.998 1    40.654  ? 54  THR   A C   1 
ATOM   122  O  O   . THR   A 1 18  ? -10.894 6.125   -2.177 1    45.385  ? 54  THR   A O   1 
ATOM   123  C  CB  . THR   A 1 18  ? -10.198 8.853   -3.77  1    46.232  ? 54  THR   A CB  1 
ATOM   124  O  OG1 . THR   A 1 18  ? -9.543  9.523   -2.694 1    38.238  ? 54  THR   A OG1 1 
ATOM   125  C  CG2 . THR   A 1 18  ? -10.419 9.817   -4.929 1    44.229  ? 54  THR   A CG2 1 
ATOM   126  N  N   . SER   A 1 19  ? -11.32  7.806   -0.766 1    32.784  ? 55  SER   A N   1 
ATOM   127  C  CA  . SER   A 1 19  ? -11.188 6.948   0.401  1    34.986  ? 55  SER   A CA  1 
ATOM   128  C  C   . SER   A 1 19  ? -12.124 5.759   0.326  1    32.669  ? 55  SER   A C   1 
ATOM   129  O  O   . SER   A 1 19  ? -11.704 4.61    0.486  1    32.139  ? 55  SER   A O   1 
ATOM   130  C  CB  . SER   A 1 19  ? -11.417 7.699   1.656  1    31.731  ? 55  SER   A CB  1 
ATOM   131  O  OG  . SER   A 1 19  ? -10.263 8.513   1.778  1    38.327  ? 55  SER   A OG  1 
ATOM   132  N  N   . GLN   A 1 20  ? -13.382 6.083   0.055  1    36.625  ? 56  GLN   A N   1 
ATOM   133  C  CA  . GLN   A 1 20  ? -14.476 5.137   0.124  1    40.719  ? 56  GLN   A CA  1 
ATOM   134  C  C   . GLN   A 1 20  ? -14.207 3.931   -0.753 1    37.728  ? 56  GLN   A C   1 
ATOM   135  O  O   . GLN   A 1 20  ? -14.421 2.795   -0.339 1    36.381  ? 56  GLN   A O   1 
ATOM   136  C  CB  . GLN   A 1 20  ? -15.713 5.927   -0.282 1    57.057  ? 56  GLN   A CB  1 
ATOM   137  C  CG  . GLN   A 1 20  ? -16.17  6.893   0.809  1    59.239  ? 56  GLN   A CG  1 
ATOM   138  C  CD  . GLN   A 1 20  ? -17.641 7.193   0.664  1    69.326  ? 56  GLN   A CD  1 
ATOM   139  O  OE1 . GLN   A 1 20  ? -18.325 6.586   -0.169 1    76.145  ? 56  GLN   A OE1 1 
ATOM   140  N  NE2 . GLN   A 1 20  ? -18.149 8.111   1.473  1    70.261  ? 56  GLN   A NE2 1 
ATOM   141  N  N   . VAL   A 1 21  ? -13.694 4.188   -1.953 1    40.678  ? 57  VAL   A N   1 
ATOM   142  C  CA  . VAL   A 1 21  ? -13.424 3.119   -2.899 1    41.393  ? 57  VAL   A CA  1 
ATOM   143  C  C   . VAL   A 1 21  ? -12.272 2.249   -2.393 1    41.762  ? 57  VAL   A C   1 
ATOM   144  O  O   . VAL   A 1 21  ? -12.375 1.015   -2.33  1    42.83   ? 57  VAL   A O   1 
ATOM   145  C  CB  . VAL   A 1 21  ? -13.09  3.733   -4.274 1    43.487  ? 57  VAL   A CB  1 
ATOM   146  C  CG1 . VAL   A 1 21  ? -12.48  2.691   -5.227 1    36.08   ? 57  VAL   A CG1 1 
ATOM   147  C  CG2 . VAL   A 1 21  ? -14.304 4.45    -4.863 1    42.998  ? 57  VAL   A CG2 1 
ATOM   148  N  N   . VAL   A 1 22  ? -11.141 2.893   -2.086 1    36.632  ? 58  VAL   A N   1 
ATOM   149  C  CA  . VAL   A 1 22  ? -9.971  2.094   -1.766 1    41.218  ? 58  VAL   A CA  1 
ATOM   150  C  C   . VAL   A 1 22  ? -10.194 1.328   -0.443 1    38.915  ? 58  VAL   A C   1 
ATOM   151  O  O   . VAL   A 1 22  ? -9.826  0.155   -0.332 1    38.908  ? 58  VAL   A O   1 
ATOM   152  C  CB  . VAL   A 1 22  ? -8.665  2.924   -1.855 1    34.744  ? 58  VAL   A CB  1 
ATOM   153  C  CG1 . VAL   A 1 22  ? -8.67   4.136   -0.96  1    40.655  ? 58  VAL   A CG1 1 
ATOM   154  C  CG2 . VAL   A 1 22  ? -7.424  2.101   -1.528 1    46.825  ? 58  VAL   A CG2 1 
ATOM   155  N  N   . TRP   A 1 23  ? -10.833 1.981   0.541  1    35.666  ? 59  TRP   A N   1 
ATOM   156  C  CA  . TRP   A 1 23  ? -11.206 1.35    1.803  1    42.562  ? 59  TRP   A CA  1 
ATOM   157  C  C   . TRP   A 1 23  ? -12.212 0.221   1.583  1    33.201  ? 59  TRP   A C   1 
ATOM   158  O  O   . TRP   A 1 23  ? -12.134 -0.808  2.225  1    32.71   ? 59  TRP   A O   1 
ATOM   159  C  CB  . TRP   A 1 23  ? -11.744 2.369   2.819  1    46.797  ? 59  TRP   A CB  1 
ATOM   160  C  CG  . TRP   A 1 23  ? -10.645 3.119   3.522  1    60.358  ? 59  TRP   A CG  1 
ATOM   161  C  CD1 . TRP   A 1 23  ? -10.145 4.343   3.193  1    54.561  ? 59  TRP   A CD1 1 
ATOM   162  C  CD2 . TRP   A 1 23  ? -9.867  2.657   4.652  1    73.049  ? 59  TRP   A CD2 1 
ATOM   163  N  NE1 . TRP   A 1 23  ? -9.136  4.692   4.039  1    51.216  ? 59  TRP   A NE1 1 
ATOM   164  C  CE2 . TRP   A 1 23  ? -8.931  3.679   4.944  1    71.489  ? 59  TRP   A CE2 1 
ATOM   165  C  CE3 . TRP   A 1 23  ? -9.862  1.495   5.444  1    77.262  ? 59  TRP   A CE3 1 
ATOM   166  C  CZ2 . TRP   A 1 23  ? -8.008  3.564   5.994  1    75.617  ? 59  TRP   A CZ2 1 
ATOM   167  C  CZ3 . TRP   A 1 23  ? -8.949  1.386   6.479  1    77.885  ? 59  TRP   A CZ3 1 
ATOM   168  C  CH2 . TRP   A 1 23  ? -8.033  2.41    6.75   1    73.732  ? 59  TRP   A CH2 1 
ATOM   169  N  N   . ASN   A 1 24  ? -13.094 0.378   0.607  1    32.356  ? 60  ASN   A N   1 
ATOM   170  C  CA  . ASN   A 1 24  ? -14.097 -0.633  0.37   1    32.61   ? 60  ASN   A CA  1 
ATOM   171  C  C   . ASN   A 1 24  ? -13.439 -1.89   -0.178 1    39.799  ? 60  ASN   A C   1 
ATOM   172  O  O   . ASN   A 1 24  ? -13.867 -3.012  0.117  1    42.334  ? 60  ASN   A O   1 
ATOM   173  C  CB  . ASN   A 1 24  ? -15.236 -0.112  -0.487 1    30.487  ? 60  ASN   A CB  1 
ATOM   174  C  CG  . ASN   A 1 24  ? -16.167 -1.242  -0.842 1    37.388  ? 60  ASN   A CG  1 
ATOM   175  O  OD1 . ASN   A 1 24  ? -16.003 -1.859  -1.908 1    41.059  ? 60  ASN   A OD1 1 
ATOM   176  N  ND2 . ASN   A 1 24  ? -17.118 -1.533  0.04   1    30.511  ? 60  ASN   A ND2 1 
ATOM   177  N  N   . GLU   A 1 25  ? -12.379 -1.699  -0.962 1    41.714  ? 61  GLU   A N   1 
ATOM   178  C  CA  . GLU   A 1 25  ? -11.737 -2.84   -1.598 1    42.35   ? 61  GLU   A CA  1 
ATOM   179  C  C   . GLU   A 1 25  ? -10.865 -3.542  -0.576 1    34.24   ? 61  GLU   A C   1 
ATOM   180  O  O   . GLU   A 1 25  ? -10.744 -4.757  -0.56  1    38.941  ? 61  GLU   A O   1 
ATOM   181  C  CB  . GLU   A 1 25  ? -10.824 -2.423  -2.752 1    47.396  ? 61  GLU   A CB  1 
ATOM   182  C  CG  . GLU   A 1 25  ? -11.552 -2.221  -4.078 1    57.602  ? 61  GLU   A CG  1 
ATOM   183  C  CD  . GLU   A 1 25  ? -10.635 -1.695  -5.178 1    67.1    ? 61  GLU   A CD  1 
ATOM   184  O  OE1 . GLU   A 1 25  ? -9.487  -2.229  -5.339 1    60.742  ? 61  GLU   A OE1 1 
ATOM   185  O  OE2 . GLU   A 1 25  ? -11.084 -0.734  -5.865 1    56.059  ? 61  GLU   A OE2 1 
ATOM   186  N  N   . TYR   A 1 26  ? -10.227 -2.764  0.272  1    35.826  ? 62  TYR   A N   1 
ATOM   187  C  CA  . TYR   A 1 26  ? -9.396  -3.394  1.281  1    37.997  ? 62  TYR   A CA  1 
ATOM   188  C  C   . TYR   A 1 26  ? -10.232 -4.075  2.37   1    35.763  ? 62  TYR   A C   1 
ATOM   189  O  O   . TYR   A 1 26  ? -9.817  -5.124  2.821  1    38.577  ? 62  TYR   A O   1 
ATOM   190  C  CB  . TYR   A 1 26  ? -8.399  -2.405  1.867  1    34.027  ? 62  TYR   A CB  1 
ATOM   191  C  CG  . TYR   A 1 26  ? -7.725  -2.861  3.154  1    38.442  ? 62  TYR   A CG  1 
ATOM   192  C  CD1 . TYR   A 1 26  ? -8.338  -2.686  4.402  1    42.465  ? 62  TYR   A CD1 1 
ATOM   193  C  CD2 . TYR   A 1 26  ? -6.455  -3.43   3.123  1    42.535  ? 62  TYR   A CD2 1 
ATOM   194  C  CE1 . TYR   A 1 26  ? -7.692  -3.042  5.577  1    49.26   ? 62  TYR   A CE1 1 
ATOM   195  C  CE2 . TYR   A 1 26  ? -5.789  -3.789  4.287  1    48.187  ? 62  TYR   A CE2 1 
ATOM   196  C  CZ  . TYR   A 1 26  ? -6.416  -3.602  5.513  1    60.585  ? 62  TYR   A CZ  1 
ATOM   197  O  OH  . TYR   A 1 26  ? -5.745  -3.993  6.639  1    63.183  ? 62  TYR   A OH  1 
ATOM   198  N  N   . ALA   A 1 27  ? -11.373 -3.51   2.798  1    35.28   ? 63  ALA   A N   1 
ATOM   199  C  CA  . ALA   A 1 27  ? -12.241 -4.188  3.763  1    36.535  ? 63  ALA   A CA  1 
ATOM   200  C  C   . ALA   A 1 27  ? -12.623 -5.584  3.25   1    40.648  ? 63  ALA   A C   1 
ATOM   201  O  O   . ALA   A 1 27  ? -12.543 -6.553  4.023  1    35.198  ? 63  ALA   A O   1 
ATOM   202  C  CB  . ALA   A 1 27  ? -13.458 -3.345  4.142  1    27.143  ? 63  ALA   A CB  1 
ATOM   203  N  N   . GLY   A 1 28  ? -12.959 -5.668  1.936  1    43.152  ? 64  GLY   A N   1 
ATOM   204  C  CA  . GLY   A 1 28  ? -13.331 -6.885  1.213  1    42.987  ? 64  GLY   A CA  1 
ATOM   205  C  C   . GLY   A 1 28  ? -12.259 -7.974  1.333  1    50.263  ? 64  GLY   A C   1 
ATOM   206  O  O   . GLY   A 1 28  ? -12.512 -9.071  1.846  1    43.889  ? 64  GLY   A O   1 
ATOM   207  N  N   . ALA   A 1 29  ? -11.038 -7.644  0.894  1    41.049  ? 65  ALA   A N   1 
ATOM   208  C  CA  . ALA   A 1 29  ? -9.921  -8.559  1.004  1    38.475  ? 65  ALA   A CA  1 
ATOM   209  C  C   . ALA   A 1 29  ? -9.609  -8.842  2.471  1    42.551  ? 65  ALA   A C   1 
ATOM   210  O  O   . ALA   A 1 29  ? -8.945  -9.816  2.806  1    46.981  ? 65  ALA   A O   1 
ATOM   211  C  CB  . ALA   A 1 29  ? -8.672  -7.959  0.339  1    35.172  ? 65  ALA   A CB  1 
ATOM   212  N  N   . ASN   A 1 30  ? -9.915  -7.917  3.37   1    46.821  ? 66  ASN   A N   1 
ATOM   213  C  CA  . ASN   A 1 30  ? -9.436  -8.217  4.711  1    42.799  ? 66  ASN   A CA  1 
ATOM   214  C  C   . ASN   A 1 30  ? -10.404 -9.238  5.295  1    40.596  ? 66  ASN   A C   1 
ATOM   215  O  O   . ASN   A 1 30  ? -10.005 -10.085 6.094  1    41.589  ? 66  ASN   A O   1 
ATOM   216  C  CB  . ASN   A 1 30  ? -9.002  -6.976  5.491  1    37.972  ? 66  ASN   A CB  1 
ATOM   217  C  CG  . ASN   A 1 30  ? -8.573  -7.27   6.913  1    41.637  ? 66  ASN   A CG  1 
ATOM   218  O  OD1 . ASN   A 1 30  ? -7.995  -8.322  7.208  1    45.128  ? 66  ASN   A OD1 1 
ATOM   219  N  ND2 . ASN   A 1 30  ? -8.899  -6.377  7.829  1    33.343  ? 66  ASN   A ND2 1 
ATOM   220  N  N   . TRP   A 1 31  ? -11.642 -9.181  4.799  1    31.188  ? 67  TRP   A N   1 
ATOM   221  C  CA  . TRP   A 1 31  ? -12.686 -10.071 5.244  1    41.672  ? 67  TRP   A CA  1 
ATOM   222  C  C   . TRP   A 1 31  ? -12.438 -11.485 4.714  1    50.654  ? 67  TRP   A C   1 
ATOM   223  O  O   . TRP   A 1 31  ? -12.465 -12.476 5.47   1    42.332  ? 67  TRP   A O   1 
ATOM   224  C  CB  . TRP   A 1 31  ? -14.012 -9.485  4.767  1    37.407  ? 67  TRP   A CB  1 
ATOM   225  C  CG  . TRP   A 1 31  ? -15.203 -10.384 4.92   1    43.911  ? 67  TRP   A CG  1 
ATOM   226  C  CD1 . TRP   A 1 31  ? -15.757 -11.146 3.939  1    47.336  ? 67  TRP   A CD1 1 
ATOM   227  C  CD2 . TRP   A 1 31  ? -16.013 -10.575 6.105  1    46.689  ? 67  TRP   A CD2 1 
ATOM   228  N  NE1 . TRP   A 1 31  ? -16.871 -11.783 4.419  1    48.783  ? 67  TRP   A NE1 1 
ATOM   229  C  CE2 . TRP   A 1 31  ? -17.061 -11.465 5.736  1    44.316  ? 67  TRP   A CE2 1 
ATOM   230  C  CE3 . TRP   A 1 31  ? -15.962 -10.085 7.431  1    39.352  ? 67  TRP   A CE3 1 
ATOM   231  C  CZ2 . TRP   A 1 31  ? -18.049 -11.882 6.638  1    35.678  ? 67  TRP   A CZ2 1 
ATOM   232  C  CZ3 . TRP   A 1 31  ? -16.92  -10.522 8.332  1    32.558  ? 67  TRP   A CZ3 1 
ATOM   233  C  CH2 . TRP   A 1 31  ? -17.947 -11.401 7.938  1    33.934  ? 67  TRP   A CH2 1 
ATOM   234  N  N   . ASN   A 1 32  ? -12.147 -11.525 3.405  1    52.397  ? 68  ASN   A N   1 
ATOM   235  C  CA  . ASN   A 1 32  ? -11.972 -12.735 2.621  1    53.041  ? 68  ASN   A CA  1 
ATOM   236  C  C   . ASN   A 1 32  ? -10.854 -13.581 3.193  1    47.104  ? 68  ASN   A C   1 
ATOM   237  O  O   . ASN   A 1 32  ? -10.859 -14.792 3.035  1    51.865  ? 68  ASN   A O   1 
ATOM   238  C  CB  . ASN   A 1 32  ? -11.563 -12.437 1.189  1    52.486  ? 68  ASN   A CB  1 
ATOM   239  C  CG  . ASN   A 1 32  ? -12.768 -12.016 0.401  1    46.269  ? 68  ASN   A CG  1 
ATOM   240  O  OD1 . ASN   A 1 32  ? -13.885 -12.054 0.916  1    39.285  ? 68  ASN   A OD1 1 
ATOM   241  N  ND2 . ASN   A 1 32  ? -12.558 -11.602 -0.831 1    48.245  ? 68  ASN   A ND2 1 
ATOM   242  N  N   . TYR   A 1 33  ? -9.917  -12.922 3.857  1    40.355  ? 69  TYR   A N   1 
ATOM   243  C  CA  . TYR   A 1 33  ? -8.82   -13.66  4.444  1    41.256  ? 69  TYR   A CA  1 
ATOM   244  C  C   . TYR   A 1 33  ? -9.145  -14.092 5.875  1    48.444  ? 69  TYR   A C   1 
ATOM   245  O  O   . TYR   A 1 33  ? -8.754  -15.175 6.281  1    48.889  ? 69  TYR   A O   1 
ATOM   246  C  CB  . TYR   A 1 33  ? -7.604  -12.738 4.399  1    39.452  ? 69  TYR   A CB  1 
ATOM   247  C  CG  . TYR   A 1 33  ? -6.475  -13.331 5.235  1    52.489  ? 69  TYR   A CG  1 
ATOM   248  C  CD1 . TYR   A 1 33  ? -5.766  -14.444 4.772  1    61.918  ? 69  TYR   A CD1 1 
ATOM   249  C  CD2 . TYR   A 1 33  ? -6.108  -12.79  6.468  1    39.963  ? 69  TYR   A CD2 1 
ATOM   250  C  CE1 . TYR   A 1 33  ? -4.728  -15.003 5.505  1    60.495  ? 69  TYR   A CE1 1 
ATOM   251  C  CE2 . TYR   A 1 33  ? -5.075  -13.342 7.21   1    50.216  ? 69  TYR   A CE2 1 
ATOM   252  C  CZ  . TYR   A 1 33  ? -4.394  -14.457 6.733  1    56.066  ? 69  TYR   A CZ  1 
ATOM   253  O  OH  . TYR   A 1 33  ? -3.364  -15.033 7.413  1    49.017  ? 69  TYR   A OH  1 
ATOM   254  N  N   . ASN   A 1 34  ? -9.776  -13.206 6.664  1    51.116  ? 70  ASN   A N   1 
ATOM   255  C  CA  . ASN   A 1 34  ? -10.185 -13.488 8.029  1    51.569  ? 70  ASN   A CA  1 
ATOM   256  C  C   . ASN   A 1 34  ? -11.216 -14.627 7.977  1    54.318  ? 70  ASN   A C   1 
ATOM   257  O  O   . ASN   A 1 34  ? -11.44  -15.337 8.953  1    46.276  ? 70  ASN   A O   1 
ATOM   258  C  CB  . ASN   A 1 34  ? -10.79  -12.249 8.705  1    47.542  ? 70  ASN   A CB  1 
ATOM   259  C  CG  . ASN   A 1 34  ? -9.809  -11.322 9.391  1    42.31   ? 70  ASN   A CG  1 
ATOM   260  O  OD1 . ASN   A 1 34  ? -9.868  -11.122 10.614 1    40.493  ? 70  ASN   A OD1 1 
ATOM   261  N  ND2 . ASN   A 1 34  ? -8.952  -10.67  8.627  1    46.121  ? 70  ASN   A ND2 1 
ATOM   262  N  N   . THR   A 1 35  ? -11.863 -14.826 6.827  1    49.668  ? 71  THR   A N   1 
ATOM   263  C  CA  . THR   A 1 35  ? -12.809 -15.931 6.805  1    46.586  ? 71  THR   A CA  1 
ATOM   264  C  C   . THR   A 1 35  ? -12.315 -17.079 5.923  1    55.354  ? 71  THR   A C   1 
ATOM   265  O  O   . THR   A 1 35  ? -13.14  -17.84  5.409  1    64.12   ? 71  THR   A O   1 
ATOM   266  C  CB  . THR   A 1 35  ? -14.22  -15.461 6.437  1    39.942  ? 71  THR   A CB  1 
ATOM   267  O  OG1 . THR   A 1 35  ? -14.222 -15.013 5.086  1    38.559  ? 71  THR   A OG1 1 
ATOM   268  C  CG2 . THR   A 1 35  ? -14.775 -14.438 7.425  1    37.455  ? 71  THR   A CG2 1 
ATOM   269  N  N   . ASN   A 1 36  ? -10.981 -17.238 5.787  1    50.416  ? 72  ASN   A N   1 
ATOM   270  C  CA  . ASN   A 1 36  ? -10.441 -18.121 4.76   1    49.213  ? 72  ASN   A CA  1 
ATOM   271  C  C   . ASN   A 1 36  ? -8.922  -17.989 4.73   1    45.539  ? 72  ASN   A C   1 
ATOM   272  O  O   . ASN   A 1 36  ? -8.39   -17.646 3.687  1    47.089  ? 72  ASN   A O   1 
ATOM   273  C  CB  . ASN   A 1 36  ? -11.005 -17.747 3.373  1    43.748  ? 72  ASN   A CB  1 
ATOM   274  C  CG  . ASN   A 1 36  ? -11.189 -18.934 2.457  1    62.627  ? 72  ASN   A CG  1 
ATOM   275  O  OD1 . ASN   A 1 36  ? -10.495 -19.941 2.63   1    68.424  ? 72  ASN   A OD1 1 
ATOM   276  N  ND2 . ASN   A 1 36  ? -12.099 -18.86  1.484  1    61.766  ? 72  ASN   A ND2 1 
ATOM   277  N  N   . ILE   A 1 37  ? -8.22   -18.221 5.849  1    51.696  ? 73  ILE   A N   1 
ATOM   278  C  CA  . ILE   A 1 37  ? -6.759  -18.144 5.832  1    59.243  ? 73  ILE   A CA  1 
ATOM   279  C  C   . ILE   A 1 37  ? -6.204  -19.13  4.796  1    69.963  ? 73  ILE   A C   1 
ATOM   280  O  O   . ILE   A 1 37  ? -6.374  -20.33  4.995  1    72.932  ? 73  ILE   A O   1 
ATOM   281  C  CB  . ILE   A 1 37  ? -6.126  -18.396 7.219  1    61.137  ? 73  ILE   A CB  1 
ATOM   282  C  CG1 . ILE   A 1 37  ? -6.858  -17.66  8.375  1    64.364  ? 73  ILE   A CG1 1 
ATOM   283  C  CG2 . ILE   A 1 37  ? -4.601  -18.156 7.204  1    49.566  ? 73  ILE   A CG2 1 
ATOM   284  C  CD1 . ILE   A 1 37  ? -6.115  -17.667 9.707  1    56.936  ? 73  ILE   A CD1 1 
ATOM   285  N  N   . THR   A 1 38  ? -5.598  -18.6   3.699  1    73.565  ? 74  THR   A N   1 
ATOM   286  C  CA  . THR   A 1 38  ? -4.88   -19.284 2.615  1    67.194  ? 74  THR   A CA  1 
ATOM   287  C  C   . THR   A 1 38  ? -3.58   -18.506 2.36   1    67.294  ? 74  THR   A C   1 
ATOM   288  O  O   . THR   A 1 38  ? -3.359  -17.463 2.96   1    61.406  ? 74  THR   A O   1 
ATOM   289  C  CB  . THR   A 1 38  ? -5.675  -19.397 1.296  1    61.264  ? 74  THR   A CB  1 
ATOM   290  O  OG1 . THR   A 1 38  ? -5.728  -18.12  0.688  1    57.175  ? 74  THR   A OG1 1 
ATOM   291  C  CG2 . THR   A 1 38  ? -7.121  -19.847 1.372  1    49.744  ? 74  THR   A CG2 1 
ATOM   292  N  N   . THR   A 1 39  ? -2.726  -18.968 1.436  1    75.901  ? 75  THR   A N   1 
ATOM   293  C  CA  . THR   A 1 39  ? -1.66   -18.101 0.931  1    80.219  ? 75  THR   A CA  1 
ATOM   294  C  C   . THR   A 1 39  ? -2.189  -17.13  -0.147 1    69.206  ? 75  THR   A C   1 
ATOM   295  O  O   . THR   A 1 39  ? -1.617  -16.047 -0.337 1    52.268  ? 75  THR   A O   1 
ATOM   296  C  CB  . THR   A 1 39  ? -0.384  -18.847 0.501  1    75.235  ? 75  THR   A CB  1 
ATOM   297  O  OG1 . THR   A 1 39  ? -0.754  -19.736 -0.55  1    73.979  ? 75  THR   A OG1 1 
ATOM   298  C  CG2 . THR   A 1 39  ? 0.336   -19.54  1.646  1    65.725  ? 75  THR   A CG2 1 
ATOM   299  N  N   . GLU   A 1 40  ? -3.275  -17.511 -0.848 1    50.783  ? 76  GLU   A N   1 
ATOM   300  C  CA  . GLU   A 1 40  ? -3.874  -16.679 -1.879 1    47.106  ? 76  GLU   A CA  1 
ATOM   301  C  C   . GLU   A 1 40  ? -4.472  -15.446 -1.201 1    56.821  ? 76  GLU   A C   1 
ATOM   302  O  O   . GLU   A 1 40  ? -3.87   -14.382 -1.268 1    41.018  ? 76  GLU   A O   1 
ATOM   303  C  CB  . GLU   A 1 40  ? -4.911  -17.417 -2.732 1    53.667  ? 76  GLU   A CB  1 
ATOM   304  C  CG  . GLU   A 1 40  ? -4.337  -18.666 -3.402 1    87.68   ? 76  GLU   A CG  1 
ATOM   305  C  CD  . GLU   A 1 40  ? -3.482  -19.673 -2.62  1    105.031 ? 76  GLU   A CD  1 
ATOM   306  O  OE1 . GLU   A 1 40  ? -3.584  -19.817 -1.37  1    83.492  ? 76  GLU   A OE1 1 
ATOM   307  O  OE2 . GLU   A 1 40  ? -2.646  -20.313 -3.305 1    125.017 ? 76  GLU   A OE2 1 
ATOM   308  N  N   . THR   A 1 41  ? -5.624  -15.603 -0.514 1    56.864  ? 77  THR   A N   1 
ATOM   309  C  CA  . THR   A 1 41  ? -6.226  -14.52  0.243  1    49.02   ? 77  THR   A CA  1 
ATOM   310  C  C   . THR   A 1 41  ? -5.145  -13.736 1.001  1    47.484  ? 77  THR   A C   1 
ATOM   311  O  O   . THR   A 1 41  ? -5.211  -12.505 1.04   1    43.372  ? 77  THR   A O   1 
ATOM   312  C  CB  . THR   A 1 41  ? -7.39   -14.977 1.135  1    50.856  ? 77  THR   A CB  1 
ATOM   313  O  OG1 . THR   A 1 41  ? -6.915  -15.665 2.296  1    48.459  ? 77  THR   A OG1 1 
ATOM   314  C  CG2 . THR   A 1 41  ? -8.547  -15.624 0.386  1    42.517  ? 77  THR   A CG2 1 
ATOM   315  N  N   . SER   A 1 42  ? -4.148  -14.434 1.578  1    47.296  ? 78  SER   A N   1 
ATOM   316  C  CA  . SER   A 1 42  ? -2.968  -13.785 2.169  1    60.341  ? 78  SER   A CA  1 
ATOM   317  C  C   . SER   A 1 42  ? -2.33   -12.72  1.268  1    67.79   ? 78  SER   A C   1 
ATOM   318  O  O   . SER   A 1 42  ? -2.018  -11.632 1.761  1    63.54   ? 78  SER   A O   1 
ATOM   319  C  CB  . SER   A 1 42  ? -1.9    -14.76  2.647  1    55.196  ? 78  SER   A CB  1 
ATOM   320  O  OG  . SER   A 1 42  ? -1.754  -14.734 4.059  1    52.548  ? 78  SER   A OG  1 
ATOM   321  N  N   . LYS   A 1 43  ? -2.069  -13.091 -0.004 1    71.042  ? 79  LYS   A N   1 
ATOM   322  C  CA  . LYS   A 1 43  ? -1.518  -12.27  -1.076 1    68.899  ? 79  LYS   A CA  1 
ATOM   323  C  C   . LYS   A 1 43  ? -2.432  -11.085 -1.373 1    57.351  ? 79  LYS   A C   1 
ATOM   324  O  O   . LYS   A 1 43  ? -2.048  -9.967  -1.068 1    67.258  ? 79  LYS   A O   1 
ATOM   325  C  CB  . LYS   A 1 43  ? -1.296  -13.084 -2.362 1    80.389  ? 79  LYS   A CB  1 
ATOM   326  C  CG  . LYS   A 1 43  ? -1.136  -12.296 -3.659 1    97.608  ? 79  LYS   A CG  1 
ATOM   327  C  CD  . LYS   A 1 43  ? -0.11   -12.936 -4.58  1    102.93  ? 79  LYS   A CD  1 
ATOM   328  C  CE  . LYS   A 1 43  ? 0.881   -11.856 -4.904 1    101.882 ? 79  LYS   A CE  1 
ATOM   329  N  NZ  . LYS   A 1 43  ? 2.232   -12.416 -4.826 1    101.332 ? 79  LYS   A NZ  1 
ATOM   330  N  N   . ILE   A 1 44  ? -3.598  -11.338 -1.993 1    59.599  ? 80  ILE   A N   1 
ATOM   331  C  CA  . ILE   A 1 44  ? -4.524  -10.312 -2.452 1    53.189  ? 80  ILE   A CA  1 
ATOM   332  C  C   . ILE   A 1 44  ? -4.651  -9.233  -1.378 1    59.783  ? 80  ILE   A C   1 
ATOM   333  O  O   . ILE   A 1 44  ? -4.914  -8.085  -1.707 1    78.509  ? 80  ILE   A O   1 
ATOM   334  C  CB  . ILE   A 1 44  ? -5.916  -10.885 -2.8   1    59.666  ? 80  ILE   A CB  1 
ATOM   335  C  CG1 . ILE   A 1 44  ? -5.974  -11.636 -4.145 1    62.944  ? 80  ILE   A CG1 1 
ATOM   336  C  CG2 . ILE   A 1 44  ? -6.996  -9.795  -2.757 1    53.533  ? 80  ILE   A CG2 1 
ATOM   337  C  CD1 . ILE   A 1 44  ? -7.386  -11.746 -4.731 1    52.021  ? 80  ILE   A CD1 1 
ATOM   338  N  N   . LEU   A 1 45  ? -4.447  -9.595  -0.105 1    50.719  ? 81  LEU   A N   1 
ATOM   339  C  CA  . LEU   A 1 45  ? -4.629  -8.666  0.987  1    43.839  ? 81  LEU   A CA  1 
ATOM   340  C  C   . LEU   A 1 45  ? -3.36   -7.833  1.187  1    59.953  ? 81  LEU   A C   1 
ATOM   341  O  O   . LEU   A 1 45  ? -3.467  -6.606  1.268  1    75.499  ? 81  LEU   A O   1 
ATOM   342  C  CB  . LEU   A 1 45  ? -5.127  -9.386  2.245  1    39.041  ? 81  LEU   A CB  1 
ATOM   343  C  CG  . LEU   A 1 45  ? -4.919  -8.665  3.591  1    42.698  ? 81  LEU   A CG  1 
ATOM   344  C  CD1 . LEU   A 1 45  ? -5.906  -7.515  3.664  1    43.188  ? 81  LEU   A CD1 1 
ATOM   345  C  CD2 . LEU   A 1 45  ? -5.004  -9.46   4.925  1    41.526  ? 81  LEU   A CD2 1 
ATOM   346  N  N   . LEU   A 1 46  ? -2.178  -8.482  1.296  1    71.054  ? 82  LEU   A N   1 
ATOM   347  C  CA  . LEU   A 1 46  ? -0.857  -7.837  1.279  1    69.662  ? 82  LEU   A CA  1 
ATOM   348  C  C   . LEU   A 1 46  ? -0.782  -6.901  0.068  1    64.679  ? 82  LEU   A C   1 
ATOM   349  O  O   . LEU   A 1 46  ? -0.045  -5.921  0.097  1    66.775  ? 82  LEU   A O   1 
ATOM   350  C  CB  . LEU   A 1 46  ? 0.386   -8.748  1.309  1    73.747  ? 82  LEU   A CB  1 
ATOM   351  C  CG  . LEU   A 1 46  ? 0.729   -9.561  2.579  1    77.68   ? 82  LEU   A CG  1 
ATOM   352  C  CD1 . LEU   A 1 46  ? 1.439   -10.876 2.201  1    75.47   ? 82  LEU   A CD1 1 
ATOM   353  C  CD2 . LEU   A 1 46  ? 1.538   -8.877  3.712  1    65.739  ? 82  LEU   A CD2 1 
ATOM   354  N  N   . GLN   A 1 47  ? -1.58   -7.199  -0.967 1    59.033  ? 83  GLN   A N   1 
ATOM   355  C  CA  . GLN   A 1 47  ? -1.709  -6.405  -2.173 1    54.868  ? 83  GLN   A CA  1 
ATOM   356  C  C   . GLN   A 1 47  ? -2.517  -5.152  -1.84  1    59.355  ? 83  GLN   A C   1 
ATOM   357  O  O   . GLN   A 1 47  ? -1.973  -4.056  -1.891 1    55.824  ? 83  GLN   A O   1 
ATOM   358  C  CB  . GLN   A 1 47  ? -2.361  -7.246  -3.273 1    53.778  ? 83  GLN   A CB  1 
ATOM   359  C  CG  . GLN   A 1 47  ? -2.138  -6.746  -4.697 1    67.532  ? 83  GLN   A CG  1 
ATOM   360  C  CD  . GLN   A 1 47  ? -3.054  -5.612  -5.129 1    80.293  ? 83  GLN   A CD  1 
ATOM   361  O  OE1 . GLN   A 1 47  ? -4.183  -5.819  -5.603 1    82.122  ? 83  GLN   A OE1 1 
ATOM   362  N  NE2 . GLN   A 1 47  ? -2.547  -4.388  -5.037 1    65.249  ? 83  GLN   A NE2 1 
ATOM   363  N  N   . LYS   A 1 48  ? -3.819  -5.314  -1.527 1    60.242  ? 84  LYS   A N   1 
ATOM   364  C  CA  . LYS   A 1 48  ? -4.719  -4.203  -1.243 1    45.536  ? 84  LYS   A CA  1 
ATOM   365  C  C   . LYS   A 1 48  ? -4.172  -3.365  -0.087 1    44.234  ? 84  LYS   A C   1 
ATOM   366  O  O   . LYS   A 1 48  ? -4.56   -2.216  0.06   1    53.246  ? 84  LYS   A O   1 
ATOM   367  C  CB  . LYS   A 1 48  ? -6.187  -4.544  -0.955 1    46.585  ? 84  LYS   A CB  1 
ATOM   368  C  CG  . LYS   A 1 48  ? -6.903  -5.406  -1.984 1    44.912  ? 84  LYS   A CG  1 
ATOM   369  C  CD  . LYS   A 1 48  ? -7.499  -4.653  -3.168 1    51.588  ? 84  LYS   A CD  1 
ATOM   370  C  CE  . LYS   A 1 48  ? -7.562  -5.575  -4.354 1    53.288  ? 84  LYS   A CE  1 
ATOM   371  N  NZ  . LYS   A 1 48  ? -8.655  -5.196  -5.246 1    53.725  ? 84  LYS   A NZ  1 
ATOM   372  N  N   . ASN   A 1 49  ? -3.237  -3.908  0.692  1    45.038  ? 85  ASN   A N   1 
ATOM   373  C  CA  . ASN   A 1 49  ? -2.524  -3.149  1.707  1    41.909  ? 85  ASN   A CA  1 
ATOM   374  C  C   . ASN   A 1 49  ? -1.657  -2.032  1.084  1    42.472  ? 85  ASN   A C   1 
ATOM   375  O  O   . ASN   A 1 49  ? -1.697  -0.871  1.531  1    39.29   ? 85  ASN   A O   1 
ATOM   376  C  CB  . ASN   A 1 49  ? -1.787  -4.093  2.655  1    45.261  ? 85  ASN   A CB  1 
ATOM   377  C  CG  . ASN   A 1 49  ? -1.836  -3.609  4.083  1    51.882  ? 85  ASN   A CG  1 
ATOM   378  O  OD1 . ASN   A 1 49  ? -1.735  -2.401  4.351  1    68.105  ? 85  ASN   A OD1 1 
ATOM   379  N  ND2 . ASN   A 1 49  ? -2.053  -4.526  5.008  1    42.203  ? 85  ASN   A ND2 1 
ATOM   380  N  N   . MET   A 1 50  ? -0.847  -2.381  0.074  1    37.077  ? 86  MET   A N   1 
ATOM   381  C  CA  . MET   A 1 50  ? -0.115  -1.451  -0.777 1    38.333  ? 86  MET   A CA  1 
ATOM   382  C  C   . MET   A 1 50  ? -1.031  -0.382  -1.351 1    36.575  ? 86  MET   A C   1 
ATOM   383  O  O   . MET   A 1 50  ? -0.708  0.805   -1.291 1    42.133  ? 86  MET   A O   1 
ATOM   384  C  CB  . MET   A 1 50  ? 0.662   -2.152  -1.908 1    43.007  ? 86  MET   A CB  1 
ATOM   385  C  CG  . MET   A 1 50  ? 2.154   -2.281  -1.589 1    60.921  ? 86  MET   A CG  1 
ATOM   386  S  SD  . MET   A 1 50  ? 2.463   -1.952  0.168  1    95.786  ? 86  MET   A SD  1 
ATOM   387  C  CE  . MET   A 1 50  ? 4.241   -1.917  0.473  1    81.952  ? 86  MET   A CE  1 
ATOM   388  N  N   . GLN   A 1 51  ? -2.168  -0.784  -1.911 1    34.973  ? 87  GLN   A N   1 
ATOM   389  C  CA  . GLN   A 1 51  ? -2.983  0.23    -2.567 1    40.055  ? 87  GLN   A CA  1 
ATOM   390  C  C   . GLN   A 1 51  ? -3.421  1.268   -1.526 1    42.472  ? 87  GLN   A C   1 
ATOM   391  O  O   . GLN   A 1 51  ? -3.169  2.457   -1.71  1    43.941  ? 87  GLN   A O   1 
ATOM   392  C  CB  . GLN   A 1 51  ? -4.016  -0.464  -3.453 1    37.161  ? 87  GLN   A CB  1 
ATOM   393  C  CG  . GLN   A 1 51  ? -5.129  0.42    -3.986 1    48.352  ? 87  GLN   A CG  1 
ATOM   394  C  CD  . GLN   A 1 51  ? -6.153  -0.376  -4.787 1    68.226  ? 87  GLN   A CD  1 
ATOM   395  O  OE1 . GLN   A 1 51  ? -5.924  -0.697  -5.96  1    85.704  ? 87  GLN   A OE1 1 
ATOM   396  N  NE2 . GLN   A 1 51  ? -7.298  -0.704  -4.19  1    49.238  ? 87  GLN   A NE2 1 
ATOM   397  N  N   . ILE   A 1 52  ? -4.01   0.812   -0.402 1    35.475  ? 88  ILE   A N   1 
ATOM   398  C  CA  . ILE   A 1 52  ? -4.329  1.665   0.736  1    34.681  ? 88  ILE   A CA  1 
ATOM   399  C  C   . ILE   A 1 52  ? -3.141  2.548   1.137  1    30.074  ? 88  ILE   A C   1 
ATOM   400  O  O   . ILE   A 1 52  ? -3.296  3.763   1.294  1    38.286  ? 88  ILE   A O   1 
ATOM   401  C  CB  . ILE   A 1 52  ? -4.869  0.795   1.894  1    45.965  ? 88  ILE   A CB  1 
ATOM   402  C  CG1 . ILE   A 1 52  ? -6.338  0.557   1.679  1    46.595  ? 88  ILE   A CG1 1 
ATOM   403  C  CG2 . ILE   A 1 52  ? -4.647  1.418   3.282  1    51.091  ? 88  ILE   A CG2 1 
ATOM   404  C  CD1 . ILE   A 1 52  ? -7.184  1.648   2.302  1    49.595  ? 88  ILE   A CD1 1 
ATOM   405  N  N   . ALA   A 1 53  ? -1.954  1.962   1.306  1    23.603  ? 89  ALA   A N   1 
ATOM   406  C  CA  . ALA   A 1 53  ? -0.793  2.727   1.76   1    29.956  ? 89  ALA   A CA  1 
ATOM   407  C  C   . ALA   A 1 53  ? -0.462  3.856   0.791  1    32.115  ? 89  ALA   A C   1 
ATOM   408  O  O   . ALA   A 1 53  ? -0.122  4.964   1.201  1    28.089  ? 89  ALA   A O   1 
ATOM   409  C  CB  . ALA   A 1 53  ? 0.425   1.842   1.975  1    29.42   ? 89  ALA   A CB  1 
ATOM   410  N  N   . GLN   A 1 54  ? -0.59   3.566   -0.503 1    29.381  ? 90  GLN   A N   1 
ATOM   411  C  CA  . GLN   A 1 54  ? -0.245  4.575   -1.491 1    33.877  ? 90  GLN   A CA  1 
ATOM   412  C  C   . GLN   A 1 54  ? -1.327  5.657   -1.523 1    30.243  ? 90  GLN   A C   1 
ATOM   413  O  O   . GLN   A 1 54  ? -1.017  6.805   -1.776 1    42.476  ? 90  GLN   A O   1 
ATOM   414  C  CB  . GLN   A 1 54  ? 0.027   3.783   -2.774 1    36.031  ? 90  GLN   A CB  1 
ATOM   415  C  CG  . GLN   A 1 54  ? -0.267  4.548   -4.056 1    57.795  ? 90  GLN   A CG  1 
ATOM   416  C  CD  . GLN   A 1 54  ? -0.389  3.618   -5.246 1    77.684  ? 90  GLN   A CD  1 
ATOM   417  O  OE1 . GLN   A 1 54  ? -0.15   2.4     -5.167 1    75.411  ? 90  GLN   A OE1 1 
ATOM   418  N  NE2 . GLN   A 1 54  ? -0.76   4.205   -6.372 1    71.539  ? 90  GLN   A NE2 1 
ATOM   419  N  N   . HIS   A 1 55  ? -2.605  5.299   -1.307 1    30.655  ? 91  HIS   A N   1 
ATOM   420  C  CA  . HIS   A 1 55  ? -3.659  6.303   -1.18  1    27.828  ? 91  HIS   A CA  1 
ATOM   421  C  C   . HIS   A 1 55  ? -3.407  7.148   0.073  1    29.713  ? 91  HIS   A C   1 
ATOM   422  O  O   . HIS   A 1 55  ? -3.596  8.353   0.031  1    28.007  ? 91  HIS   A O   1 
ATOM   423  C  CB  . HIS   A 1 55  ? -5.047  5.664   -1.067 1    28.436  ? 91  HIS   A CB  1 
ATOM   424  C  CG  . HIS   A 1 55  ? -6.105  6.683   -0.817 1    29.647  ? 91  HIS   A CG  1 
ATOM   425  N  ND1 . HIS   A 1 55  ? -6.575  6.963   0.454  1    30.982  ? 91  HIS   A ND1 1 
ATOM   426  C  CD2 . HIS   A 1 55  ? -6.78   7.474   -1.648 1    27.03   ? 91  HIS   A CD2 1 
ATOM   427  C  CE1 . HIS   A 1 55  ? -7.508  7.915   0.382  1    29.659  ? 91  HIS   A CE1 1 
ATOM   428  N  NE2 . HIS   A 1 55  ? -7.654  8.229   -0.894 1    33.366  ? 91  HIS   A NE2 1 
ATOM   429  N  N   . THR   A 1 56  ? -2.987  6.534   1.196  1    26.326  ? 92  THR   A N   1 
ATOM   430  C  CA  . THR   A 1 56  ? -2.699  7.344   2.373  1    29.684  ? 92  THR   A CA  1 
ATOM   431  C  C   . THR   A 1 56  ? -1.507  8.276   2.097  1    29.435  ? 92  THR   A C   1 
ATOM   432  O  O   . THR   A 1 56  ? -1.496  9.435   2.49   1    27.115  ? 92  THR   A O   1 
ATOM   433  C  CB  . THR   A 1 56  ? -2.489  6.423   3.587  1    32.101  ? 92  THR   A CB  1 
ATOM   434  O  OG1 . THR   A 1 56  ? -3.687  5.662   3.628  1    37.994  ? 92  THR   A OG1 1 
ATOM   435  C  CG2 . THR   A 1 56  ? -2.51   7.134   4.921  1    26.932  ? 92  THR   A CG2 1 
ATOM   436  N  N   . LEU   A 1 57  ? -0.48   7.795   1.405  1    32.754  ? 93  LEU   A N   1 
ATOM   437  C  CA  . LEU   A 1 57  ? 0.751   8.565   1.272  1    36.43   ? 93  LEU   A CA  1 
ATOM   438  C  C   . LEU   A 1 57  ? 0.457   9.811   0.453  1    39.845  ? 93  LEU   A C   1 
ATOM   439  O  O   . LEU   A 1 57  ? 0.864   10.906  0.829  1    43.708  ? 93  LEU   A O   1 
ATOM   440  C  CB  . LEU   A 1 57  ? 1.845   7.703   0.641  1    39.337  ? 93  LEU   A CB  1 
ATOM   441  C  CG  . LEU   A 1 57  ? 3.15    8.395   0.222  1    43.907  ? 93  LEU   A CG  1 
ATOM   442  C  CD1 . LEU   A 1 57  ? 3.793   9.316   1.286  1    32.146  ? 93  LEU   A CD1 1 
ATOM   443  C  CD2 . LEU   A 1 57  ? 4.127   7.293   -0.273 1    39.704  ? 93  LEU   A CD2 1 
ATOM   444  N  N   . LYS   A 1 58  ? -0.329  9.648   -0.621 1    43.613  ? 94  LYS   A N   1 
ATOM   445  C  CA  . LYS   A 1 58  ? -0.62   10.737  -1.539 1    35.04   ? 94  LYS   A CA  1 
ATOM   446  C  C   . LYS   A 1 58  ? -1.573  11.763  -0.903 1    28.703  ? 94  LYS   A C   1 
ATOM   447  O  O   . LYS   A 1 58  ? -1.331  12.957  -0.989 1    28.625  ? 94  LYS   A O   1 
ATOM   448  C  CB  . LYS   A 1 58  ? -1.172  10.134  -2.835 1    34.147  ? 94  LYS   A CB  1 
ATOM   449  C  CG  . LYS   A 1 58  ? -1.583  11.246  -3.847 1    44.119  ? 94  LYS   A CG  1 
ATOM   450  C  CD  . LYS   A 1 58  ? -2.746  10.921  -4.795 1    48.26   ? 94  LYS   A CD  1 
ATOM   451  C  CE  . LYS   A 1 58  ? -2.986  11.898  -5.921 1    56.166  ? 94  LYS   A CE  1 
ATOM   452  N  NZ  . LYS   A 1 58  ? -4.202  11.52   -6.644 1    53.271  ? 94  LYS   A NZ  1 
ATOM   453  N  N   . TYR   A 1 59  ? -2.697  11.34   -0.301 1    27.057  ? 95  TYR   A N   1 
ATOM   454  C  CA  . TYR   A 1 59  ? -3.555  12.329  0.345  1    24.518  ? 95  TYR   A CA  1 
ATOM   455  C  C   . TYR   A 1 59  ? -2.868  12.913  1.584  1    26.086  ? 95  TYR   A C   1 
ATOM   456  O  O   . TYR   A 1 59  ? -2.978  14.108  1.852  1    32.528  ? 95  TYR   A O   1 
ATOM   457  C  CB  . TYR   A 1 59  ? -5.016  11.94   0.531  1    27.643  ? 95  TYR   A CB  1 
ATOM   458  C  CG  . TYR   A 1 59  ? -5.731  11.935  -0.811 1    31.351  ? 95  TYR   A CG  1 
ATOM   459  C  CD1 . TYR   A 1 59  ? -5.626  10.831  -1.646 1    33.023  ? 95  TYR   A CD1 1 
ATOM   460  C  CD2 . TYR   A 1 59  ? -6.479  13.024  -1.264 1    32.66   ? 95  TYR   A CD2 1 
ATOM   461  C  CE1 . TYR   A 1 59  ? -6.234  10.776  -2.883 1    30.371  ? 95  TYR   A CE1 1 
ATOM   462  C  CE2 . TYR   A 1 59  ? -7.077  13.002  -2.512 1    33.77   ? 95  TYR   A CE2 1 
ATOM   463  C  CZ  . TYR   A 1 59  ? -6.941  11.879  -3.32  1    38.368  ? 95  TYR   A CZ  1 
ATOM   464  O  OH  . TYR   A 1 59  ? -7.495  11.747  -4.555 1    41.18   ? 95  TYR   A OH  1 
ATOM   465  N  N   . GLY   A 1 60  ? -2.08   12.11   2.287  1    24.004  ? 96  GLY   A N   1 
ATOM   466  C  CA  . GLY   A 1 60  ? -1.403  12.562  3.488  1    25.661  ? 96  GLY   A CA  1 
ATOM   467  C  C   . GLY   A 1 60  ? -0.286  13.547  3.182  1    29.838  ? 96  GLY   A C   1 
ATOM   468  O  O   . GLY   A 1 60  ? -0.105  14.505  3.934  1    34.951  ? 96  GLY   A O   1 
ATOM   469  N  N   . THR   A 1 61  ? 0.448   13.339  2.08   1    34.881  ? 97  THR   A N   1 
ATOM   470  C  CA  . THR   A 1 61  ? 1.398   14.351  1.594  1    37.9    ? 97  THR   A CA  1 
ATOM   471  C  C   . THR   A 1 61  ? 0.689   15.669  1.258  1    37.889  ? 97  THR   A C   1 
ATOM   472  O  O   . THR   A 1 61  ? 1.054   16.732  1.769  1    44.011  ? 97  THR   A O   1 
ATOM   473  C  CB  . THR   A 1 61  ? 2.172   13.884  0.365  1    39.019  ? 97  THR   A CB  1 
ATOM   474  O  OG1 . THR   A 1 61  ? 2.783   12.634  0.701  1    34.913  ? 97  THR   A OG1 1 
ATOM   475  C  CG2 . THR   A 1 61  ? 3.158   14.958  -0.066 1    40.776  ? 97  THR   A CG2 1 
ATOM   476  N  N   . GLN   A 1 62  ? -0.32   15.62   0.387  1    28.514  ? 98  GLN   A N   1 
ATOM   477  C  CA  . GLN   A 1 62  ? -1.093  16.834  0.143  1    29.298  ? 98  GLN   A CA  1 
ATOM   478  C  C   . GLN   A 1 62  ? -1.579  17.483  1.438  1    32.323  ? 98  GLN   A C   1 
ATOM   479  O  O   . GLN   A 1 62  ? -1.432  18.709  1.553  1    41.544  ? 98  GLN   A O   1 
ATOM   480  C  CB  . GLN   A 1 62  ? -2.323  16.764  -0.762 1    38.09   ? 98  GLN   A CB  1 
ATOM   481  C  CG  . GLN   A 1 62  ? -2.083  17.119  -2.225 1    66.455  ? 98  GLN   A CG  1 
ATOM   482  C  CD  . GLN   A 1 62  ? -2.844  16.217  -3.189 1    81.296  ? 98  GLN   A CD  1 
ATOM   483  O  OE1 . GLN   A 1 62  ? -2.227  15.485  -3.98  1    99.221  ? 98  GLN   A OE1 1 
ATOM   484  N  NE2 . GLN   A 1 62  ? -4.179  16.23   -3.144 1    51.433  ? 98  GLN   A NE2 1 
ATOM   485  N  N   . ALA   A 1 63  ? -2.211  16.736  2.374  1    29.127  ? 99  ALA   A N   1 
ATOM   486  C  CA  . ALA   A 1 63  ? -2.714  17.383  3.599  1    29.168  ? 99  ALA   A CA  1 
ATOM   487  C  C   . ALA   A 1 63  ? -1.604  18.125  4.365  1    28.1    ? 99  ALA   A C   1 
ATOM   488  O  O   . ALA   A 1 63  ? -1.869  19.117  5.037  1    24.937  ? 99  ALA   A O   1 
ATOM   489  C  CB  . ALA   A 1 63  ? -3.428  16.412  4.552  1    26.007  ? 99  ALA   A CB  1 
ATOM   490  N  N   . ARG   A 1 64  ? -0.375  17.593  4.34   1    32.785  ? 100 ARG   A N   1 
ATOM   491  C  CA  . ARG   A 1 64  ? 0.766   18.151  5.065  1    38.217  ? 100 ARG   A CA  1 
ATOM   492  C  C   . ARG   A 1 64  ? 1.134   19.548  4.531  1    46.071  ? 100 ARG   A C   1 
ATOM   493  O  O   . ARG   A 1 64  ? 1.755   20.349  5.24   1    37.921  ? 100 ARG   A O   1 
ATOM   494  C  CB  . ARG   A 1 64  ? 1.913   17.131  4.99   1    32.062  ? 100 ARG   A CB  1 
ATOM   495  C  CG  . ARG   A 1 64  ? 2.139   16.492  6.346  1    36.774  ? 100 ARG   A CG  1 
ATOM   496  C  CD  . ARG   A 1 64  ? 2.305   15.037  6.169  1    35.495  ? 100 ARG   A CD  1 
ATOM   497  N  NE  . ARG   A 1 64  ? 2.524   14.237  7.377  1    37.838  ? 100 ARG   A NE  1 
ATOM   498  C  CZ  . ARG   A 1 64  ? 3.619   13.485  7.558  1    45.438  ? 100 ARG   A CZ  1 
ATOM   499  N  NH1 . ARG   A 1 64  ? 4.695   13.637  6.792  1    34.652  ? 100 ARG   A NH1 1 
ATOM   500  N  NH2 . ARG   A 1 64  ? 3.645   12.59   8.532  1    51.85   ? 100 ARG   A NH2 1 
ATOM   501  N  N   . LYS   A 1 65  ? 0.698   19.845  3.291  1    49.779  ? 101 LYS   A N   1 
ATOM   502  C  CA  . LYS   A 1 65  ? 1.061   21.07   2.58   1    52.071  ? 101 LYS   A CA  1 
ATOM   503  C  C   . LYS   A 1 65  ? 0.181   22.239  2.98   1    44.815  ? 101 LYS   A C   1 
ATOM   504  O  O   . LYS   A 1 65  ? 0.501   23.356  2.621  1    51.976  ? 101 LYS   A O   1 
ATOM   505  C  CB  . LYS   A 1 65  ? 0.939   21.004  1.053  1    53.025  ? 101 LYS   A CB  1 
ATOM   506  C  CG  . LYS   A 1 65  ? 2.111   20.342  0.313  1    57.082  ? 101 LYS   A CG  1 
ATOM   507  C  CD  . LYS   A 1 65  ? 1.648   20.05   -1.118 1    69.817  ? 101 LYS   A CD  1 
ATOM   508  C  CE  . LYS   A 1 65  ? 2.755   19.769  -2.096 1    69.204  ? 101 LYS   A CE  1 
ATOM   509  N  NZ  . LYS   A 1 65  ? 3.907   19.192  -1.395 1    69.644  ? 101 LYS   A NZ  1 
ATOM   510  N  N   . PHE   A 1 66  ? -0.944  21.983  3.658  1    40.254  ? 102 PHE   A N   1 
ATOM   511  C  CA  . PHE   A 1 66  ? -1.798  23.051  4.158  1    43.936  ? 102 PHE   A CA  1 
ATOM   512  C  C   . PHE   A 1 66  ? -1.349  23.445  5.559  1    52.409  ? 102 PHE   A C   1 
ATOM   513  O  O   . PHE   A 1 66  ? -1.094  22.584  6.417  1    56.981  ? 102 PHE   A O   1 
ATOM   514  C  CB  . PHE   A 1 66  ? -3.254  22.626  4.372  1    44.808  ? 102 PHE   A CB  1 
ATOM   515  C  CG  . PHE   A 1 66  ? -4.008  22.345  3.089  1    42.641  ? 102 PHE   A CG  1 
ATOM   516  C  CD1 . PHE   A 1 66  ? -3.976  21.073  2.517  1    41.577  ? 102 PHE   A CD1 1 
ATOM   517  C  CD2 . PHE   A 1 66  ? -4.734  23.354  2.464  1    40.364  ? 102 PHE   A CD2 1 
ATOM   518  C  CE1 . PHE   A 1 66  ? -4.67   20.82   1.35   1    38.177  ? 102 PHE   A CE1 1 
ATOM   519  C  CE2 . PHE   A 1 66  ? -5.454  23.101  1.312  1    42.424  ? 102 PHE   A CE2 1 
ATOM   520  C  CZ  . PHE   A 1 66  ? -5.394  21.844  0.748  1    47.358  ? 102 PHE   A CZ  1 
ATOM   521  N  N   . ASP   A 1 67  ? -1.279  24.759  5.785  1    54.391  ? 103 ASP   A N   1 
ATOM   522  C  CA  . ASP   A 1 67  ? -1.036  25.253  7.131  1    57.597  ? 103 ASP   A CA  1 
ATOM   523  C  C   . ASP   A 1 67  ? -2.374  25.272  7.872  1    48.419  ? 103 ASP   A C   1 
ATOM   524  O  O   . ASP   A 1 67  ? -3.236  26.115  7.63   1    38.361  ? 103 ASP   A O   1 
ATOM   525  C  CB  . ASP   A 1 67  ? -0.185  26.515  7.111  1    67.735  ? 103 ASP   A CB  1 
ATOM   526  C  CG  . ASP   A 1 67  ? -0.236  27.346  8.382  1    75.274  ? 103 ASP   A CG  1 
ATOM   527  O  OD1 . ASP   A 1 67  ? 0.119   26.816  9.473  1    63.646  ? 103 ASP   A OD1 1 
ATOM   528  O  OD2 . ASP   A 1 67  ? -0.643  28.515  8.259  1    85.666  ? 103 ASP   A OD2 1 
ATOM   529  N  N   . VAL   A 1 68  ? -2.558  24.269  8.732  1    46.333  ? 104 VAL   A N   1 
ATOM   530  C  CA  . VAL   A 1 68  ? -3.808  24.065  9.448  1    52.486  ? 104 VAL   A CA  1 
ATOM   531  C  C   . VAL   A 1 68  ? -4.122  25.269  10.341 1    55.384  ? 104 VAL   A C   1 
ATOM   532  O  O   . VAL   A 1 68  ? -5.284  25.465  10.73  1    50.276  ? 104 VAL   A O   1 
ATOM   533  C  CB  . VAL   A 1 68  ? -3.695  22.753  10.252 1    55.735  ? 104 VAL   A CB  1 
ATOM   534  C  CG1 . VAL   A 1 68  ? -4.615  22.73   11.47  1    64.099  ? 104 VAL   A CG1 1 
ATOM   535  C  CG2 . VAL   A 1 68  ? -3.89   21.518  9.376  1    53.252  ? 104 VAL   A CG2 1 
ATOM   536  N  N   . ASN   A 1 69  ? -3.074  26.042  10.686 1    56.264  ? 105 ASN   A N   1 
ATOM   537  C  CA  . ASN   A 1 69  ? -3.252  27.224  11.513 1    61.547  ? 105 ASN   A CA  1 
ATOM   538  C  C   . ASN   A 1 69  ? -4.276  28.147  10.839 1    65.156  ? 105 ASN   A C   1 
ATOM   539  O  O   . ASN   A 1 69  ? -5.304  28.471  11.447 1    70.578  ? 105 ASN   A O   1 
ATOM   540  C  CB  . ASN   A 1 69  ? -1.902  27.797  11.941 1    56.202  ? 105 ASN   A CB  1 
ATOM   541  C  CG  . ASN   A 1 69  ? -1.21   26.949  12.991 1    53.97   ? 105 ASN   A CG  1 
ATOM   542  O  OD1 . ASN   A 1 69  ? -1.833  26.572  14     1    55.703  ? 105 ASN   A OD1 1 
ATOM   543  N  ND2 . ASN   A 1 69  ? 0.085   26.69   12.809 1    34.539  ? 105 ASN   A ND2 1 
ATOM   544  N  N   . GLN   A 1 70  ? -4.056  28.404  9.536  1    65.354  ? 106 GLN   A N   1 
ATOM   545  C  CA  . GLN   A 1 70  ? -4.749  29.397  8.712  1    74.008  ? 106 GLN   A CA  1 
ATOM   546  C  C   . GLN   A 1 70  ? -6.163  28.987  8.274  1    62.408  ? 106 GLN   A C   1 
ATOM   547  O  O   . GLN   A 1 70  ? -6.829  29.765  7.596  1    65.671  ? 106 GLN   A O   1 
ATOM   548  C  CB  . GLN   A 1 70  ? -3.935  29.835  7.488  1    71.818  ? 106 GLN   A CB  1 
ATOM   549  C  CG  . GLN   A 1 70  ? -2.577  30.442  7.823  1    74.075  ? 106 GLN   A CG  1 
ATOM   550  C  CD  . GLN   A 1 70  ? -2.645  31.457  8.947  1    91.185  ? 106 GLN   A CD  1 
ATOM   551  O  OE1 . GLN   A 1 70  ? -3.239  32.533  8.807  1    102.536 ? 106 GLN   A OE1 1 
ATOM   552  N  NE2 . GLN   A 1 70  ? -2.056  31.116  10.085 1    83.043  ? 106 GLN   A NE2 1 
ATOM   553  N  N   . LEU   A 1 71  ? -6.649  27.809  8.686  1    66.511  ? 107 LEU   A N   1 
ATOM   554  C  CA  . LEU   A 1 71  ? -7.964  27.328  8.269  1    53.54   ? 107 LEU   A CA  1 
ATOM   555  C  C   . LEU   A 1 71  ? -9.028  27.879  9.195  1    57.769  ? 107 LEU   A C   1 
ATOM   556  O  O   . LEU   A 1 71  ? -8.889  27.831  10.421 1    61.729  ? 107 LEU   A O   1 
ATOM   557  C  CB  . LEU   A 1 71  ? -8.098  25.81   8.182  1    45.293  ? 107 LEU   A CB  1 
ATOM   558  C  CG  . LEU   A 1 71  ? -7.253  25.165  7.079  1    60.919  ? 107 LEU   A CG  1 
ATOM   559  C  CD1 . LEU   A 1 71  ? -7.215  23.651  7.157  1    56.5    ? 107 LEU   A CD1 1 
ATOM   560  C  CD2 . LEU   A 1 71  ? -7.756  25.638  5.714  1    63.844  ? 107 LEU   A CD2 1 
ATOM   561  N  N   . GLN   A 1 72  ? -10.116 28.313  8.563  1    51.034  ? 108 GLN   A N   1 
ATOM   562  C  CA  . GLN   A 1 72  ? -11.185 28.945  9.304  1    53.349  ? 108 GLN   A CA  1 
ATOM   563  C  C   . GLN   A 1 72  ? -12.242 27.907  9.649  1    50.766  ? 108 GLN   A C   1 
ATOM   564  O  O   . GLN   A 1 72  ? -12.712 27.902  10.783 1    56.768  ? 108 GLN   A O   1 
ATOM   565  C  CB  . GLN   A 1 72  ? -11.636 30.239  8.631  1    55.583  ? 108 GLN   A CB  1 
ATOM   566  C  CG  . GLN   A 1 72  ? -10.445 31.094  8.208  1    69.578  ? 108 GLN   A CG  1 
ATOM   567  C  CD  . GLN   A 1 72  ? -10.732 32.576  8.284  1    86.518  ? 108 GLN   A CD  1 
ATOM   568  O  OE1 . GLN   A 1 72  ? -10.769 33.283  7.266  1    75.675  ? 108 GLN   A OE1 1 
ATOM   569  N  NE2 . GLN   A 1 72  ? -10.949 33.053  9.504  1    88.371  ? 108 GLN   A NE2 1 
ATOM   570  N  N   . ASN   A 1 73  ? -12.561 27.018  8.697  1    47.504  ? 109 ASN   A N   1 
ATOM   571  C  CA  . ASN   A 1 73  ? -13.679 26.107  8.884  1    43.691  ? 109 ASN   A CA  1 
ATOM   572  C  C   . ASN   A 1 73  ? -13.242 25.036  9.874  1    41.039  ? 109 ASN   A C   1 
ATOM   573  O  O   . ASN   A 1 73  ? -12.214 24.417  9.605  1    39.284  ? 109 ASN   A O   1 
ATOM   574  C  CB  . ASN   A 1 73  ? -14.242 25.521  7.588  1    34.799  ? 109 ASN   A CB  1 
ATOM   575  C  CG  . ASN   A 1 73  ? -15.446 24.673  7.93   1    43.7    ? 109 ASN   A CG  1 
ATOM   576  O  OD1 . ASN   A 1 73  ? -15.296 23.683  8.654  1    55.017  ? 109 ASN   A OD1 1 
ATOM   577  N  ND2 . ASN   A 1 73  ? -16.646 25.036  7.488  1    46.083  ? 109 ASN   A ND2 1 
ATOM   578  N  N   . THR   A 1 74  ? -13.998 24.858  10.987 1    38.711  ? 110 THR   A N   1 
ATOM   579  C  CA  . THR   A 1 74  ? -13.546 23.978  12.056 1    48.879  ? 110 THR   A CA  1 
ATOM   580  C  C   . THR   A 1 74  ? -13.573 22.513  11.596 1    48.389  ? 110 THR   A C   1 
ATOM   581  O  O   . THR   A 1 74  ? -12.574 21.813  11.789 1    41.304  ? 110 THR   A O   1 
ATOM   582  C  CB  . THR   A 1 74  ? -14.116 24.228  13.465 1    50.907  ? 110 THR   A CB  1 
ATOM   583  O  OG1 . THR   A 1 74  ? -15.494 24.555  13.389 1    56.447  ? 110 THR   A OG1 1 
ATOM   584  C  CG2 . THR   A 1 74  ? -13.418 25.357  14.211 1    45.717  ? 110 THR   A CG2 1 
ATOM   585  N  N   . THR   A 1 75  ? -14.657 22.076  10.922 1    46.882  ? 111 THR   A N   1 
ATOM   586  C  CA  . THR   A 1 75  ? -14.752 20.711  10.4   1    41.393  ? 111 THR   A CA  1 
ATOM   587  C  C   . THR   A 1 75  ? -13.57  20.378  9.477  1    47.683  ? 111 THR   A C   1 
ATOM   588  O  O   . THR   A 1 75  ? -13.011 19.277  9.559  1    52.595  ? 111 THR   A O   1 
ATOM   589  C  CB  . THR   A 1 75  ? -16.093 20.509  9.705  1    38.966  ? 111 THR   A CB  1 
ATOM   590  O  OG1 . THR   A 1 75  ? -16.97  20.719  10.807 1    46.368  ? 111 THR   A OG1 1 
ATOM   591  C  CG2 . THR   A 1 75  ? -16.302 19.101  9.177  1    38.931  ? 111 THR   A CG2 1 
ATOM   592  N  N   . ILE   A 1 76  ? -13.16  21.321  8.615  1    35.886  ? 112 ILE   A N   1 
ATOM   593  C  CA  . ILE   A 1 76  ? -12.217 20.979  7.554  1    34.46   ? 112 ILE   A CA  1 
ATOM   594  C  C   . ILE   A 1 76  ? -10.797 21.056  8.099  1    38.38   ? 112 ILE   A C   1 
ATOM   595  O  O   . ILE   A 1 76  ? -9.899  20.362  7.627  1    32.955  ? 112 ILE   A O   1 
ATOM   596  C  CB  . ILE   A 1 76  ? -12.402 21.949  6.372  1    33.34   ? 112 ILE   A CB  1 
ATOM   597  C  CG1 . ILE   A 1 76  ? -13.708 21.658  5.628  1    37.428  ? 112 ILE   A CG1 1 
ATOM   598  C  CG2 . ILE   A 1 76  ? -11.18  21.989  5.45   1    28.189  ? 112 ILE   A CG2 1 
ATOM   599  C  CD1 . ILE   A 1 76  ? -13.957 22.589  4.452  1    50.087  ? 112 ILE   A CD1 1 
ATOM   600  N  N   . LYS   A 1 77  ? -10.589 22.004  9.015  1    43.927  ? 113 LYS   A N   1 
ATOM   601  C  CA  . LYS   A 1 77  ? -9.405  22.022  9.846  1    44.094  ? 113 LYS   A CA  1 
ATOM   602  C  C   . LYS   A 1 77  ? -9.173  20.596  10.37  1    43.843  ? 113 LYS   A C   1 
ATOM   603  O  O   . LYS   A 1 77  ? -8.093  20.023  10.157 1    39.323  ? 113 LYS   A O   1 
ATOM   604  C  CB  . LYS   A 1 77  ? -9.614  23.081  10.94  1    50.928  ? 113 LYS   A CB  1 
ATOM   605  C  CG  . LYS   A 1 77  ? -8.414  23.827  11.563 1    55.257  ? 113 LYS   A CG  1 
ATOM   606  C  CD  . LYS   A 1 77  ? -8.733  24.4    12.949 1    68.047  ? 113 LYS   A CD  1 
ATOM   607  C  CE  . LYS   A 1 77  ? -7.872  25.543  13.413 1    77.257  ? 113 LYS   A CE  1 
ATOM   608  N  NZ  . LYS   A 1 77  ? -6.463  25.147  13.454 1    73.124  ? 113 LYS   A NZ  1 
ATOM   609  N  N   . ARG   A 1 78  ? -10.196 20.022  11.034 1    35.304  ? 114 ARG   A N   1 
ATOM   610  C  CA  . ARG   A 1 78  ? -10.072 18.755  11.77  1    35.943  ? 114 ARG   A CA  1 
ATOM   611  C  C   . ARG   A 1 78  ? -9.816  17.572  10.835 1    34.471  ? 114 ARG   A C   1 
ATOM   612  O  O   . ARG   A 1 78  ? -8.975  16.726  11.115 1    29.953  ? 114 ARG   A O   1 
ATOM   613  C  CB  . ARG   A 1 78  ? -11.368 18.439  12.528 1    30.27   ? 114 ARG   A CB  1 
ATOM   614  C  CG  . ARG   A 1 78  ? -11.415 17.243  13.466 1    33.581  ? 114 ARG   A CG  1 
ATOM   615  C  CD  . ARG   A 1 78  ? -12.56  17.489  14.471 1    34.432  ? 114 ARG   A CD  1 
ATOM   616  N  NE  . ARG   A 1 78  ? -12.729 16.375  15.409 1    42.166  ? 114 ARG   A NE  1 
ATOM   617  C  CZ  . ARG   A 1 78  ? -11.906 16.048  16.418 1    39.282  ? 114 ARG   A CZ  1 
ATOM   618  N  NH1 . ARG   A 1 78  ? -10.904 16.833  16.716 1    29.306  ? 114 ARG   A NH1 1 
ATOM   619  N  NH2 . ARG   A 1 78  ? -12.102 14.946  17.133 1    42.191  ? 114 ARG   A NH2 1 
ATOM   620  N  N   . ILE   A 1 79  ? -10.548 17.515  9.712  1    36.512  ? 115 ILE   A N   1 
ATOM   621  C  CA  . ILE   A 1 79  ? -10.271 16.491  8.725  1    31.882  ? 115 ILE   A CA  1 
ATOM   622  C  C   . ILE   A 1 79  ? -8.822  16.559  8.246  1    31.845  ? 115 ILE   A C   1 
ATOM   623  O  O   . ILE   A 1 79  ? -8.111  15.553  8.271  1    35.621  ? 115 ILE   A O   1 
ATOM   624  C  CB  . ILE   A 1 79  ? -11.269 16.612  7.592  1    33.659  ? 115 ILE   A CB  1 
ATOM   625  C  CG1 . ILE   A 1 79  ? -12.704 16.353  8.146  1    31.009  ? 115 ILE   A CG1 1 
ATOM   626  C  CG2 . ILE   A 1 79  ? -10.829 15.668  6.478  1    33.707  ? 115 ILE   A CG2 1 
ATOM   627  C  CD1 . ILE   A 1 79  ? -13.848 16.653  7.173  1    28.874  ? 115 ILE   A CD1 1 
ATOM   628  N  N   . ILE   A 1 80  ? -8.365  17.752  7.878  1    28.105  ? 116 ILE   A N   1 
ATOM   629  C  CA  . ILE   A 1 80  ? -7.053  17.902  7.277  1    33.649  ? 116 ILE   A CA  1 
ATOM   630  C  C   . ILE   A 1 80  ? -5.989  17.503  8.306  1    32.923  ? 116 ILE   A C   1 
ATOM   631  O  O   . ILE   A 1 80  ? -5.085  16.722  7.989  1    30.578  ? 116 ILE   A O   1 
ATOM   632  C  CB  . ILE   A 1 80  ? -6.853  19.318  6.688  1    33.549  ? 116 ILE   A CB  1 
ATOM   633  C  CG1 . ILE   A 1 80  ? -7.732  19.525  5.469  1    38.96   ? 116 ILE   A CG1 1 
ATOM   634  C  CG2 . ILE   A 1 80  ? -5.379  19.6    6.361  1    32.128  ? 116 ILE   A CG2 1 
ATOM   635  C  CD1 . ILE   A 1 80  ? -7.307  20.709  4.602  1    33.653  ? 116 ILE   A CD1 1 
ATOM   636  N  N   . LYS   A 1 81  ? -6.151  17.979  9.546  1    31.683  ? 117 LYS   A N   1 
ATOM   637  C  CA  . LYS   A 1 81  ? -5.215  17.645  10.614 1    41.361  ? 117 LYS   A CA  1 
ATOM   638  C  C   . LYS   A 1 81  ? -4.996  16.126  10.741 1    35.469  ? 117 LYS   A C   1 
ATOM   639  O  O   . LYS   A 1 81  ? -3.867  15.642  10.77  1    37.254  ? 117 LYS   A O   1 
ATOM   640  C  CB  . LYS   A 1 81  ? -5.565  18.297  11.96  1    42.065  ? 117 LYS   A CB  1 
ATOM   641  C  CG  . LYS   A 1 81  ? -4.304  18.243  12.813 1    55.24   ? 117 LYS   A CG  1 
ATOM   642  C  CD  . LYS   A 1 81  ? -4.496  18.037  14.31  1    75.826  ? 117 LYS   A CD  1 
ATOM   643  C  CE  . LYS   A 1 81  ? -3.275  17.375  14.885 1    79.09   ? 117 LYS   A CE  1 
ATOM   644  N  NZ  . LYS   A 1 81  ? -3.685  16.54   16.02  1    68.69   ? 117 LYS   A NZ  1 
ATOM   645  N  N   . LYS   A 1 82  ? -6.093  15.368  10.817 1    32.271  ? 118 LYS   A N   1 
ATOM   646  C  CA  . LYS   A 1 82  ? -6.098  13.913  10.892 1    30.301  ? 118 LYS   A CA  1 
ATOM   647  C  C   . LYS   A 1 82  ? -5.46   13.236  9.659  1    33.105  ? 118 LYS   A C   1 
ATOM   648  O  O   . LYS   A 1 82  ? -4.61   12.37   9.82   1    31.42   ? 118 LYS   A O   1 
ATOM   649  C  CB  . LYS   A 1 82  ? -7.566  13.604  11.167 1    31.411  ? 118 LYS   A CB  1 
ATOM   650  C  CG  . LYS   A 1 82  ? -7.94   12.144  11.014 1    44.946  ? 118 LYS   A CG  1 
ATOM   651  C  CD  . LYS   A 1 82  ? -9.011  11.704  12.02  1    52.505  ? 118 LYS   A CD  1 
ATOM   652  C  CE  . LYS   A 1 82  ? -8.69   10.395  12.638 1    50.406  ? 118 LYS   A CE  1 
ATOM   653  N  NZ  . LYS   A 1 82  ? -7.953  9.61    11.652 1    55.538  ? 118 LYS   A NZ  1 
ATOM   654  N  N   . VAL   A 1 83  ? -5.812  13.637  8.422  1    34.29   ? 119 VAL   A N   1 
ATOM   655  C  CA  . VAL   A 1 83  ? -5.206  13.089  7.202  1    29.534  ? 119 VAL   A CA  1 
ATOM   656  C  C   . VAL   A 1 83  ? -3.691  13.29   7.132  1    27.811  ? 119 VAL   A C   1 
ATOM   657  O  O   . VAL   A 1 83  ? -3.012  12.524  6.474  1    31.45   ? 119 VAL   A O   1 
ATOM   658  C  CB  . VAL   A 1 83  ? -5.876  13.633  5.933  1    26.773  ? 119 VAL   A CB  1 
ATOM   659  C  CG1 . VAL   A 1 83  ? -5.268  13.04   4.673  1    24.783  ? 119 VAL   A CG1 1 
ATOM   660  C  CG2 . VAL   A 1 83  ? -7.356  13.373  6.003  1    26.979  ? 119 VAL   A CG2 1 
ATOM   661  N  N   . GLN   A 1 84  ? -3.138  14.327  7.765  1    31.725  ? 120 GLN   A N   1 
ATOM   662  C  CA  . GLN   A 1 84  ? -1.686  14.518  7.834  1    33.71   ? 120 GLN   A CA  1 
ATOM   663  C  C   . GLN   A 1 84  ? -0.968  13.408  8.614  1    35.553  ? 120 GLN   A C   1 
ATOM   664  O  O   . GLN   A 1 84  ? 0.269   13.32   8.596  1    28.888  ? 120 GLN   A O   1 
ATOM   665  C  CB  . GLN   A 1 84  ? -1.349  15.833  8.556  1    33.459  ? 120 GLN   A CB  1 
ATOM   666  C  CG  . GLN   A 1 84  ? -1.781  17.097  7.821  1    29.725  ? 120 GLN   A CG  1 
ATOM   667  C  CD  . GLN   A 1 84  ? -1.3    18.37   8.485  1    33.023  ? 120 GLN   A CD  1 
ATOM   668  O  OE1 . GLN   A 1 84  ? -1.048  18.418  9.691  1    35.77   ? 120 GLN   A OE1 1 
ATOM   669  N  NE2 . GLN   A 1 84  ? -1.246  19.451  7.724  1    30.901  ? 120 GLN   A NE2 1 
ATOM   670  N  N   . ASP   A 1 85  ? -1.742  12.59   9.34   1    34.353  ? 121 ASP   A N   1 
ATOM   671  C  CA  . ASP   A 1 85  ? -1.165  11.449  10.034 1    37.83   ? 121 ASP   A CA  1 
ATOM   672  C  C   . ASP   A 1 85  ? -1.267  10.278  9.072  1    29.748  ? 121 ASP   A C   1 
ATOM   673  O  O   . ASP   A 1 85  ? -2.338  9.797   8.838  1    28.643  ? 121 ASP   A O   1 
ATOM   674  C  CB  . ASP   A 1 85  ? -1.747  11.273  11.443 1    35.881  ? 121 ASP   A CB  1 
ATOM   675  C  CG  . ASP   A 1 85  ? -1.337  10.031  12.226 1    33.445  ? 121 ASP   A CG  1 
ATOM   676  O  OD1 . ASP   A 1 85  ? -0.536  9.228   11.724 1    32.968  ? 121 ASP   A OD1 1 
ATOM   677  O  OD2 . ASP   A 1 85  ? -1.753  9.904   13.393 1    44.905  ? 121 ASP   A OD2 1 
ATOM   678  N  N   . LEU   A 1 86  ? -0.137  9.837   8.532  1    34.144  ? 122 LEU   A N   1 
ATOM   679  C  CA  . LEU   A 1 86  ? -0.095  8.848   7.478  1    29.097  ? 122 LEU   A CA  1 
ATOM   680  C  C   . LEU   A 1 86  ? -0.11   7.475   8.125  1    32.559  ? 122 LEU   A C   1 
ATOM   681  O  O   . LEU   A 1 86  ? -0.281  6.486   7.409  1    32.816  ? 122 LEU   A O   1 
ATOM   682  C  CB  . LEU   A 1 86  ? 1.253   9.001   6.769  1    33.954  ? 122 LEU   A CB  1 
ATOM   683  C  CG  . LEU   A 1 86  ? 1.446   10.139  5.768  1    44.762  ? 122 LEU   A CG  1 
ATOM   684  C  CD1 . LEU   A 1 86  ? 2.923   10.361  5.474  1    36.934  ? 122 LEU   A CD1 1 
ATOM   685  C  CD2 . LEU   A 1 86  ? 0.775   9.669   4.515  1    53.07   ? 122 LEU   A CD2 1 
ATOM   686  N  N   . GLU   A 1 87  ? 0.231   7.406   9.432  1    36.486  ? 123 GLU   A N   1 
ATOM   687  C  CA  . GLU   A 1 87  ? 0.407   6.144   10.157 1    38.125  ? 123 GLU   A CA  1 
ATOM   688  C  C   . GLU   A 1 87  ? 1.552   5.366   9.507  1    32.53   ? 123 GLU   A C   1 
ATOM   689  O  O   . GLU   A 1 87  ? 2.529   5.976   9.097  1    37.379  ? 123 GLU   A O   1 
ATOM   690  C  CB  . GLU   A 1 87  ? -0.804  5.209   10.137 1    41.112  ? 123 GLU   A CB  1 
ATOM   691  C  CG  . GLU   A 1 87  ? -2.158  5.906   10.225 1    61.471  ? 123 GLU   A CG  1 
ATOM   692  C  CD  . GLU   A 1 87  ? -2.592  5.956   11.677 1    84.861  ? 123 GLU   A CD  1 
ATOM   693  O  OE1 . GLU   A 1 87  ? -1.703  6.273   12.509 1    105.104 ? 123 GLU   A OE1 1 
ATOM   694  O  OE2 . GLU   A 1 87  ? -3.785  5.694   11.978 1    66.971  ? 123 GLU   A OE2 1 
ATOM   695  N  N   . ARG   A 1 88  ? 1.384   4.05    9.334  1    30.739  ? 124 ARG   A N   1 
ATOM   696  C  CA  . ARG   A 1 88  ? 2.392   3.173   8.739  1    31.302  ? 124 ARG   A CA  1 
ATOM   697  C  C   . ARG   A 1 88  ? 2.79    3.671   7.34   1    31.855  ? 124 ARG   A C   1 
ATOM   698  O  O   . ARG   A 1 88  ? 3.945   3.483   6.913  1    25.79   ? 124 ARG   A O   1 
ATOM   699  C  CB  . ARG   A 1 88  ? 1.853   1.731   8.616  1    32.958  ? 124 ARG   A CB  1 
ATOM   700  C  CG  . ARG   A 1 88  ? 0.77    1.511   7.557  1    33.481  ? 124 ARG   A CG  1 
ATOM   701  C  CD  . ARG   A 1 88  ? 0.251   0.111   7.262  1    37.364  ? 124 ARG   A CD  1 
ATOM   702  N  NE  . ARG   A 1 88  ? -0.584  -0.232  8.409  1    55.687  ? 124 ARG   A NE  1 
ATOM   703  C  CZ  . ARG   A 1 88  ? -1.032  -1.434  8.748  1    63.471  ? 124 ARG   A CZ  1 
ATOM   704  N  NH1 . ARG   A 1 88  ? -0.702  -2.502  8.015  1    58.1    ? 124 ARG   A NH1 1 
ATOM   705  N  NH2 . ARG   A 1 88  ? -1.809  -1.531  9.828  1    46.722  ? 124 ARG   A NH2 1 
ATOM   706  N  N   . ALA   A 1 89  ? 1.825   4.287   6.613  1    30.043  ? 125 ALA   A N   1 
ATOM   707  C  CA  . ALA   A 1 89  ? 2.16    4.733   5.259  1    33.438  ? 125 ALA   A CA  1 
ATOM   708  C  C   . ALA   A 1 89  ? 3.339   5.728   5.28   1    34.494  ? 125 ALA   A C   1 
ATOM   709  O  O   . ALA   A 1 89  ? 3.874   6.082   4.234  1    32.071  ? 125 ALA   A O   1 
ATOM   710  C  CB  . ALA   A 1 89  ? 0.94    5.287   4.549  1    25.592  ? 125 ALA   A CB  1 
ATOM   711  N  N   . ALA   A 1 90  ? 3.785   6.143   6.478  1    25.67   ? 126 ALA   A N   1 
ATOM   712  C  CA  . ALA   A 1 90  ? 4.865   7.115   6.573  1    26.8    ? 126 ALA   A CA  1 
ATOM   713  C  C   . ALA   A 1 90  ? 6.196   6.375   6.45   1    26.968  ? 126 ALA   A C   1 
ATOM   714  O  O   . ALA   A 1 90  ? 7.226   6.966   6.246  1    33.334  ? 126 ALA   A O   1 
ATOM   715  C  CB  . ALA   A 1 90  ? 4.771   7.836   7.914  1    22.34   ? 126 ALA   A CB  1 
ATOM   716  N  N   . LEU   A 1 91  ? 6.178   5.07    6.643  1    28.161  ? 127 LEU   A N   1 
ATOM   717  C  CA  . LEU   A 1 91  ? 7.388   4.281   6.585  1    30.551  ? 127 LEU   A CA  1 
ATOM   718  C  C   . LEU   A 1 91  ? 7.923   4.245   5.141  1    33.85   ? 127 LEU   A C   1 
ATOM   719  O  O   . LEU   A 1 91  ? 7.158   4.289   4.174  1    38.079  ? 127 LEU   A O   1 
ATOM   720  C  CB  . LEU   A 1 91  ? 7.012   2.89    7.1    1    25.3    ? 127 LEU   A CB  1 
ATOM   721  C  CG  . LEU   A 1 91  ? 6.936   2.727   8.629  1    28.668  ? 127 LEU   A CG  1 
ATOM   722  C  CD1 . LEU   A 1 91  ? 6.403   1.336   8.991  1    26.917  ? 127 LEU   A CD1 1 
ATOM   723  C  CD2 . LEU   A 1 91  ? 8.262   2.939   9.326  1    21.491  ? 127 LEU   A CD2 1 
ATOM   724  N  N   . PRO   A 1 92  ? 9.262   4.137   4.967  1    32.078  ? 128 PRO   A N   1 
ATOM   725  C  CA  . PRO   A 1 92  ? 9.853   3.885   3.646  1    34.856  ? 128 PRO   A CA  1 
ATOM   726  C  C   . PRO   A 1 92  ? 9.438   2.484   3.208  1    39.473  ? 128 PRO   A C   1 
ATOM   727  O  O   . PRO   A 1 92  ? 9.194   1.611   4.057  1    34.665  ? 128 PRO   A O   1 
ATOM   728  C  CB  . PRO   A 1 92  ? 11.394  3.988   3.858  1    30.643  ? 128 PRO   A CB  1 
ATOM   729  C  CG  . PRO   A 1 92  ? 11.534  4.584   5.252  1    33.574  ? 128 PRO   A CG  1 
ATOM   730  C  CD  . PRO   A 1 92  ? 10.258  4.219   6.061  1    26.79   ? 128 PRO   A CD  1 
ATOM   731  N  N   . ALA   A 1 93  ? 9.454   2.279   1.883  1    38.444  ? 129 ALA   A N   1 
ATOM   732  C  CA  . ALA   A 1 93  ? 8.875   1.138   1.189  1    43.108  ? 129 ALA   A CA  1 
ATOM   733  C  C   . ALA   A 1 93  ? 9.325   -0.191  1.824  1    42.629  ? 129 ALA   A C   1 
ATOM   734  O  O   . ALA   A 1 93  ? 8.524   -1.129  2.037  1    34.679  ? 129 ALA   A O   1 
ATOM   735  C  CB  . ALA   A 1 93  ? 9.204   1.224   -0.315 1    36.052  ? 129 ALA   A CB  1 
ATOM   736  N  N   . GLN   A 1 94  ? 10.621  -0.272  2.119  1    39.121  ? 130 GLN   A N   1 
ATOM   737  C  CA  . GLN   A 1 94  ? 11.14   -1.515  2.659  1    43.921  ? 130 GLN   A CA  1 
ATOM   738  C  C   . GLN   A 1 94  ? 10.467  -1.836  3.995  1    39.019  ? 130 GLN   A C   1 
ATOM   739  O  O   . GLN   A 1 94  ? 9.769   -2.829  4.109  1    42.156  ? 130 GLN   A O   1 
ATOM   740  C  CB  . GLN   A 1 94  ? 12.664  -1.569  2.756  1    46.957  ? 130 GLN   A CB  1 
ATOM   741  C  CG  . GLN   A 1 94  ? 13.192  -2.991  2.942  1    58.85   ? 130 GLN   A CG  1 
ATOM   742  C  CD  . GLN   A 1 94  ? 14.66   -3.055  3.285  1    77.448  ? 130 GLN   A CD  1 
ATOM   743  O  OE1 . GLN   A 1 94  ? 15.025  -3.311  4.44   1    95.079  ? 130 GLN   A OE1 1 
ATOM   744  N  NE2 . GLN   A 1 94  ? 15.508  -2.811  2.288  1    77.441  ? 130 GLN   A NE2 1 
ATOM   745  N  N   . GLU   A 1 95  ? 10.691  -0.996  5.003  1    42.667  ? 131 GLU   A N   1 
ATOM   746  C  CA  . GLU   A 1 95  ? 10.109  -1.147  6.336  1    38.397  ? 131 GLU   A CA  1 
ATOM   747  C  C   . GLU   A 1 95  ? 8.587   -1.257  6.249  1    32.102  ? 131 GLU   A C   1 
ATOM   748  O  O   . GLU   A 1 95  ? 7.982   -1.865  7.108  1    29.385  ? 131 GLU   A O   1 
ATOM   749  C  CB  . GLU   A 1 95  ? 10.379  0.083   7.213  1    35.656  ? 131 GLU   A CB  1 
ATOM   750  C  CG  . GLU   A 1 95  ? 11.831  0.264   7.669  1    44.719  ? 131 GLU   A CG  1 
ATOM   751  C  CD  . GLU   A 1 95  ? 12.924  0.237   6.61   1    59.869  ? 131 GLU   A CD  1 
ATOM   752  O  OE1 . GLU   A 1 95  ? 12.846  1.016   5.632  1    68.713  ? 131 GLU   A OE1 1 
ATOM   753  O  OE2 . GLU   A 1 95  ? 13.846  -0.605  6.739  1    74.784  ? 131 GLU   A OE2 1 
ATOM   754  N  N   . LEU   A 1 96  ? 7.948   -0.697  5.215  1    27.931  ? 132 LEU   A N   1 
ATOM   755  C  CA  . LEU   A 1 96  ? 6.496   -0.727  5.224  1    29.181  ? 132 LEU   A CA  1 
ATOM   756  C  C   . LEU   A 1 96  ? 6.097   -2.173  4.99   1    33.926  ? 132 LEU   A C   1 
ATOM   757  O  O   . LEU   A 1 96  ? 5.226   -2.723  5.672  1    36.5    ? 132 LEU   A O   1 
ATOM   758  C  CB  . LEU   A 1 96  ? 5.873   0.207   4.189  1    33.792  ? 132 LEU   A CB  1 
ATOM   759  C  CG  . LEU   A 1 96  ? 4.363   0.044   3.961  1    40.655  ? 132 LEU   A CG  1 
ATOM   760  C  CD1 . LEU   A 1 96  ? 3.621   0.111   5.307  1    37.657  ? 132 LEU   A CD1 1 
ATOM   761  C  CD2 . LEU   A 1 96  ? 3.749   1.003   2.882  1    35.448  ? 132 LEU   A CD2 1 
ATOM   762  N  N   . GLU   A 1 97  ? 6.833   -2.767  4.045  1    40.005  ? 133 GLU   A N   1 
ATOM   763  C  CA  . GLU   A 1 97  ? 6.675   -4.141  3.616  1    43.559  ? 133 GLU   A CA  1 
ATOM   764  C  C   . GLU   A 1 97  ? 6.965   -5.057  4.807  1    35.14   ? 133 GLU   A C   1 
ATOM   765  O  O   . GLU   A 1 97  ? 6.286   -6.052  5.013  1    35.758  ? 133 GLU   A O   1 
ATOM   766  C  CB  . GLU   A 1 97  ? 7.592   -4.419  2.414  1    48.96   ? 133 GLU   A CB  1 
ATOM   767  C  CG  . GLU   A 1 97  ? 7.243   -5.67   1.603  1    62.38   ? 133 GLU   A CG  1 
ATOM   768  C  CD  . GLU   A 1 97  ? 8.482   -6.387  1.052  1    84.748  ? 133 GLU   A CD  1 
ATOM   769  O  OE1 . GLU   A 1 97  ? 8.684   -7.554  1.467  1    85.707  ? 133 GLU   A OE1 1 
ATOM   770  O  OE2 . GLU   A 1 97  ? 9.267   -5.813  0.244  1    76.005  ? 133 GLU   A OE2 1 
ATOM   771  N  N   . GLU   A 1 98  ? 8       -4.735  5.567  1    36.386  ? 134 GLU   A N   1 
ATOM   772  C  CA  . GLU   A 1 98  ? 8.433   -5.576  6.66   1    36.788  ? 134 GLU   A CA  1 
ATOM   773  C  C   . GLU   A 1 98  ? 7.354   -5.514  7.749  1    41.783  ? 134 GLU   A C   1 
ATOM   774  O  O   . GLU   A 1 98  ? 6.771   -6.54   8.157  1    41.97   ? 134 GLU   A O   1 
ATOM   775  C  CB  . GLU   A 1 98  ? 9.859   -5.17   6.999  1    30.206  ? 134 GLU   A CB  1 
ATOM   776  C  CG  . GLU   A 1 98  ? 10.276  -5.764  8.335  1    41.252  ? 134 GLU   A CG  1 
ATOM   777  C  CD  . GLU   A 1 98  ? 11.703  -5.396  8.701  1    54.95   ? 134 GLU   A CD  1 
ATOM   778  O  OE1 . GLU   A 1 98  ? 12.276  -4.495  8.012  1    54.315  ? 134 GLU   A OE1 1 
ATOM   779  O  OE2 . GLU   A 1 98  ? 12.239  -6.028  9.661  1    58.337  ? 134 GLU   A OE2 1 
ATOM   780  N  N   . TYR   A 1 99  ? 6.97    -4.281  8.071  1    37.057  ? 135 TYR   A N   1 
ATOM   781  C  CA  . TYR   A 1 99  ? 5.909   -4.073  9.035  1    34.638  ? 135 TYR   A CA  1 
ATOM   782  C  C   . TYR   A 1 99  ? 4.635   -4.782  8.588  1    34.751  ? 135 TYR   A C   1 
ATOM   783  O  O   . TYR   A 1 99  ? 3.976   -5.405  9.412  1    32.688  ? 135 TYR   A O   1 
ATOM   784  C  CB  . TYR   A 1 99  ? 5.64    -2.586  9.234  1    30.153  ? 135 TYR   A CB  1 
ATOM   785  C  CG  . TYR   A 1 99  ? 4.592   -2.271  10.295 1    32.344  ? 135 TYR   A CG  1 
ATOM   786  C  CD1 . TYR   A 1 99  ? 4.853   -2.395  11.667 1    30.188  ? 135 TYR   A CD1 1 
ATOM   787  C  CD2 . TYR   A 1 99  ? 3.323   -1.867  9.91   1    33.053  ? 135 TYR   A CD2 1 
ATOM   788  C  CE1 . TYR   A 1 99  ? 3.892   -2.082  12.618 1    28.643  ? 135 TYR   A CE1 1 
ATOM   789  C  CE2 . TYR   A 1 99  ? 2.368   -1.517  10.85  1    38.983  ? 135 TYR   A CE2 1 
ATOM   790  C  CZ  . TYR   A 1 99  ? 2.665   -1.589  12.205 1    38.012  ? 135 TYR   A CZ  1 
ATOM   791  O  OH  . TYR   A 1 99  ? 1.645   -1.266  13.063 1    44.271  ? 135 TYR   A OH  1 
ATOM   792  N  N   . ASN   A 1 100 ? 4.239   -4.649  7.319  1    30.047  ? 136 ASN   A N   1 
ATOM   793  C  CA  . ASN   A 1 100 ? 3.018   -5.358  6.974  1    33.074  ? 136 ASN   A CA  1 
ATOM   794  C  C   . ASN   A 1 100 ? 3.167   -6.867  7.186  1    34.813  ? 136 ASN   A C   1 
ATOM   795  O  O   . ASN   A 1 100 ? 2.186   -7.518  7.586  1    31.501  ? 136 ASN   A O   1 
ATOM   796  C  CB  . ASN   A 1 100 ? 2.545   -5.089  5.561  1    31.315  ? 136 ASN   A CB  1 
ATOM   797  C  CG  . ASN   A 1 100 ? 2.029   -3.686  5.456  1    37.294  ? 136 ASN   A CG  1 
ATOM   798  O  OD1 . ASN   A 1 100 ? 1.18    -3.252  6.246  1    48.654  ? 136 ASN   A OD1 1 
ATOM   799  N  ND2 . ASN   A 1 100 ? 2.602   -2.946  4.536  1    38.798  ? 136 ASN   A ND2 1 
ATOM   800  N  N   . LYS   A 1 101 ? 4.384   -7.397  6.941  1    30.29   ? 137 LYS   A N   1 
ATOM   801  C  CA  . LYS   A 1 101 ? 4.597   -8.834  7.015  1    37.452  ? 137 LYS   A CA  1 
ATOM   802  C  C   . LYS   A 1 101 ? 4.482   -9.241  8.485  1    39.473  ? 137 LYS   A C   1 
ATOM   803  O  O   . LYS   A 1 101 ? 3.739   -10.178 8.802  1    38.378  ? 137 LYS   A O   1 
ATOM   804  C  CB  . LYS   A 1 101 ? 5.898   -9.355  6.376  1    36.952  ? 137 LYS   A CB  1 
ATOM   805  C  CG  . LYS   A 1 101 ? 5.792   -10.783 5.808  1    41.367  ? 137 LYS   A CG  1 
ATOM   806  C  CD  . LYS   A 1 101 ? 7.079   -11.587 5.553  1    49.372  ? 137 LYS   A CD  1 
ATOM   807  C  CE  . LYS   A 1 101 ? 6.805   -13.043 5.903  1    48.169  ? 137 LYS   A CE  1 
ATOM   808  N  NZ  . LYS   A 1 101 ? 5.401   -13.439 5.633  1    45.638  ? 137 LYS   A NZ  1 
ATOM   809  N  N   . ILE   A 1 102 ? 5.112   -8.446  9.372  1    27.739  ? 138 ILE   A N   1 
ATOM   810  C  CA  . ILE   A 1 102 ? 5.168   -8.789  10.773 1    28.634  ? 138 ILE   A CA  1 
ATOM   811  C  C   . ILE   A 1 102 ? 3.76    -8.891  11.38  1    27.535  ? 138 ILE   A C   1 
ATOM   812  O  O   . ILE   A 1 102 ? 3.461   -9.748  12.198 1    26.689  ? 138 ILE   A O   1 
ATOM   813  C  CB  . ILE   A 1 102 ? 6.059   -7.779  11.506 1    38.421  ? 138 ILE   A CB  1 
ATOM   814  C  CG1 . ILE   A 1 102 ? 7.525   -7.902  11.076 1    42.482  ? 138 ILE   A CG1 1 
ATOM   815  C  CG2 . ILE   A 1 102 ? 5.951   -8.005  13.013 1    41.48   ? 138 ILE   A CG2 1 
ATOM   816  C  CD1 . ILE   A 1 102 ? 8.396   -8.574  12.126 1    46.229  ? 138 ILE   A CD1 1 
ATOM   817  N  N   . LEU   A 1 103 ? 2.881   -7.974  11.022 1    24.788  ? 139 LEU   A N   1 
ATOM   818  C  CA  . LEU   A 1 103 ? 1.599   -7.937  11.683 1    27.985  ? 139 LEU   A CA  1 
ATOM   819  C  C   . LEU   A 1 103 ? 0.841   -9.177  11.207 1    36.996  ? 139 LEU   A C   1 
ATOM   820  O  O   . LEU   A 1 103 ? 0.132   -9.821  11.984 1    34.897  ? 139 LEU   A O   1 
ATOM   821  C  CB  . LEU   A 1 103 ? 0.891   -6.652  11.242 1    25.868  ? 139 LEU   A CB  1 
ATOM   822  C  CG  . LEU   A 1 103 ? 1.337   -5.317  11.834 1    27.535  ? 139 LEU   A CG  1 
ATOM   823  C  CD1 . LEU   A 1 103 ? 0.377   -4.369  11.087 1    27.101  ? 139 LEU   A CD1 1 
ATOM   824  C  CD2 . LEU   A 1 103 ? 1.023   -5.303  13.33  1    23.214  ? 139 LEU   A CD2 1 
ATOM   825  N  N   . LEU   A 1 104 ? 1.023   -9.503  9.912  1    34.967  ? 140 LEU   A N   1 
ATOM   826  C  CA  . LEU   A 1 104 ? 0.309   -10.61  9.313  1    37.069  ? 140 LEU   A CA  1 
ATOM   827  C  C   . LEU   A 1 104 ? 0.748   -11.885 10.013 1    33.666  ? 140 LEU   A C   1 
ATOM   828  O  O   . LEU   A 1 104 ? -0.099  -12.667 10.422 1    34.238  ? 140 LEU   A O   1 
ATOM   829  C  CB  . LEU   A 1 104 ? 0.516   -10.71  7.804  1    46.142  ? 140 LEU   A CB  1 
ATOM   830  C  CG  . LEU   A 1 104 ? -0.111  -11.959 7.176  1    49.469  ? 140 LEU   A CG  1 
ATOM   831  C  CD1 . LEU   A 1 104 ? -1.31   -11.623 6.335  1    48.873  ? 140 LEU   A CD1 1 
ATOM   832  C  CD2 . LEU   A 1 104 ? 0.962   -12.731 6.409  1    49.538  ? 140 LEU   A CD2 1 
ATOM   833  N  N   . ASP   A 1 105 ? 2.07    -12.041 10.157 1    29.562  ? 141 ASP   A N   1 
ATOM   834  C  CA  . ASP   A 1 105 ? 2.668   -13.185 10.821 1    32.61   ? 141 ASP   A CA  1 
ATOM   835  C  C   . ASP   A 1 105 ? 2.267   -13.264 12.308 1    34.086  ? 141 ASP   A C   1 
ATOM   836  O  O   . ASP   A 1 105 ? 2.22    -14.347 12.857 1    40.851  ? 141 ASP   A O   1 
ATOM   837  C  CB  . ASP   A 1 105 ? 4.185   -13.226 10.631 1    32.733  ? 141 ASP   A CB  1 
ATOM   838  C  CG  . ASP   A 1 105 ? 4.759   -13.409 9.212  1    43.777  ? 141 ASP   A CG  1 
ATOM   839  O  OD1 . ASP   A 1 105 ? 3.983   -13.588 8.202  1    35.516  ? 141 ASP   A OD1 1 
ATOM   840  O  OD2 . ASP   A 1 105 ? 6.015   -13.349 9.095  1    48.861  ? 141 ASP   A OD2 1 
ATOM   841  N  N   . MET   A 1 106 ? 2.096   -12.145 13.017 1    34.329  ? 142 MET   A N   1 
ATOM   842  C  CA  . MET   A 1 106 ? 1.667   -12.196 14.416 1    36.58   ? 142 MET   A CA  1 
ATOM   843  C  C   . MET   A 1 106 ? 0.218   -12.693 14.499 1    33.904  ? 142 MET   A C   1 
ATOM   844  O  O   . MET   A 1 106 ? -0.035  -13.611 15.259 1    30.953  ? 142 MET   A O   1 
ATOM   845  C  CB  . MET   A 1 106 ? 1.844   -10.872 15.179 1    28.601  ? 142 MET   A CB  1 
ATOM   846  C  CG  . MET   A 1 106 ? 3.286   -10.553 15.43  1    31.231  ? 142 MET   A CG  1 
ATOM   847  S  SD  . MET   A 1 106 ? 3.725   -9.316  16.662 1    32.841  ? 142 MET   A SD  1 
ATOM   848  C  CE  . MET   A 1 106 ? 2.674   -8.174  15.771 1    33.628  ? 142 MET   A CE  1 
ATOM   849  N  N   . GLU   A 1 107 ? -0.697  -12.134 13.696 1    30.978  ? 143 GLU   A N   1 
ATOM   850  C  CA  . GLU   A 1 107 ? -2.109  -12.505 13.705 1    39.14   ? 143 GLU   A CA  1 
ATOM   851  C  C   . GLU   A 1 107 ? -2.288  -14.006 13.442 1    44.388  ? 143 GLU   A C   1 
ATOM   852  O  O   . GLU   A 1 107 ? -3.05   -14.698 14.148 1    35.346  ? 143 GLU   A O   1 
ATOM   853  C  CB  . GLU   A 1 107 ? -2.898  -11.83  12.579 1    39.742  ? 143 GLU   A CB  1 
ATOM   854  C  CG  . GLU   A 1 107 ? -2.93   -10.313 12.703 1    69.875  ? 143 GLU   A CG  1 
ATOM   855  C  CD  . GLU   A 1 107 ? -4.273  -9.703  12.356 1    81.448  ? 143 GLU   A CD  1 
ATOM   856  O  OE1 . GLU   A 1 107 ? -4.471  -9.428  11.152 1    68.671  ? 143 GLU   A OE1 1 
ATOM   857  O  OE2 . GLU   A 1 107 ? -5.116  -9.553  13.29  1    88.306  ? 143 GLU   A OE2 1 
ATOM   858  N  N   . THR   A 1 108 ? -1.621  -14.453 12.366 1    30.455  ? 144 THR   A N   1 
ATOM   859  C  CA  . THR   A 1 108 ? -1.691  -15.805 11.853 1    35.436  ? 144 THR   A CA  1 
ATOM   860  C  C   . THR   A 1 108 ? -1.146  -16.732 12.931 1    35.604  ? 144 THR   A C   1 
ATOM   861  O  O   . THR   A 1 108 ? -1.873  -17.586 13.434 1    42.386  ? 144 THR   A O   1 
ATOM   862  C  CB  . THR   A 1 108 ? -0.92   -15.922 10.524 1    37.916  ? 144 THR   A CB  1 
ATOM   863  O  OG1 . THR   A 1 108 ? -1.494  -15.009 9.584  1    31.142  ? 144 THR   A OG1 1 
ATOM   864  C  CG2 . THR   A 1 108 ? -0.864  -17.345 9.992  1    31.014  ? 144 THR   A CG2 1 
ATOM   865  N  N   . THR   A 1 109 ? 0.117   -16.524 13.325 1    32.106  ? 145 THR   A N   1 
ATOM   866  C  CA  . THR   A 1 109 ? 0.63    -17.293 14.451 1    34.518  ? 145 THR   A CA  1 
ATOM   867  C  C   . THR   A 1 109 ? -0.429  -17.38  15.545 1    33.432  ? 145 THR   A C   1 
ATOM   868  O  O   . THR   A 1 109 ? -0.732  -18.464 16.004 1    33.941  ? 145 THR   A O   1 
ATOM   869  C  CB  . THR   A 1 109 ? 1.94    -16.751 15.016 1    34.528  ? 145 THR   A CB  1 
ATOM   870  O  OG1 . THR   A 1 109 ? 2.82    -16.785 13.9   1    28.905  ? 145 THR   A OG1 1 
ATOM   871  C  CG2 . THR   A 1 109 ? 2.384   -17.545 16.233 1    32.288  ? 145 THR   A CG2 1 
ATOM   872  N  N   . TYR   A 1 110 ? -1.026  -16.258 15.971 1    31.454  ? 146 TYR   A N   1 
ATOM   873  C  CA  . TYR   A 1 110 ? -1.882  -16.414 17.143 1    34.7    ? 146 TYR   A CA  1 
ATOM   874  C  C   . TYR   A 1 110 ? -3.108  -17.275 16.801 1    35.307  ? 146 TYR   A C   1 
ATOM   875  O  O   . TYR   A 1 110 ? -3.58   -18.062 17.619 1    43.886  ? 146 TYR   A O   1 
ATOM   876  C  CB  . TYR   A 1 110 ? -2.225  -15.062 17.753 1    26.691  ? 146 TYR   A CB  1 
ATOM   877  C  CG  . TYR   A 1 110 ? -3.261  -15.062 18.874 1    27.542  ? 146 TYR   A CG  1 
ATOM   878  C  CD1 . TYR   A 1 110 ? -4.627  -15.174 18.592 1    21.04   ? 146 TYR   A CD1 1 
ATOM   879  C  CD2 . TYR   A 1 110 ? -2.847  -14.911 20.222 1    23.642  ? 146 TYR   A CD2 1 
ATOM   880  C  CE1 . TYR   A 1 110 ? -5.559  -15.129 19.631 1    19.889  ? 146 TYR   A CE1 1 
ATOM   881  C  CE2 . TYR   A 1 110 ? -3.768  -14.88  21.261 1    19.325  ? 146 TYR   A CE2 1 
ATOM   882  C  CZ  . TYR   A 1 110 ? -5.115  -14.967 20.952 1    21.049  ? 146 TYR   A CZ  1 
ATOM   883  O  OH  . TYR   A 1 110 ? -5.925  -14.835 22.029 1    23.246  ? 146 TYR   A OH  1 
ATOM   884  N  N   . SER   A 1 111 ? -3.583  -17.169 15.56  1    36.785  ? 147 SER   A N   1 
ATOM   885  C  CA  . SER   A 1 111 ? -4.909  -17.672 15.238 1    36.07   ? 147 SER   A CA  1 
ATOM   886  C  C   . SER   A 1 111 ? -4.872  -19.149 14.926 1    32.325  ? 147 SER   A C   1 
ATOM   887  O  O   . SER   A 1 111 ? -5.93   -19.749 14.945 1    36.696  ? 147 SER   A O   1 
ATOM   888  C  CB  . SER   A 1 111 ? -5.58   -16.929 14.099 1    41.991  ? 147 SER   A CB  1 
ATOM   889  O  OG  . SER   A 1 111 ? -6.201  -15.729 14.545 1    48.079  ? 147 SER   A OG  1 
ATOM   890  N  N   . VAL   A 1 112 ? -3.681  -19.697 14.642 1    32.426  ? 148 VAL   A N   1 
ATOM   891  C  CA  . VAL   A 1 112 ? -3.551  -21.077 14.2   1    33.394  ? 148 VAL   A CA  1 
ATOM   892  C  C   . VAL   A 1 112 ? -2.857  -21.935 15.247 1    35.895  ? 148 VAL   A C   1 
ATOM   893  O  O   . VAL   A 1 112 ? -2.801  -23.147 15.068 1    32.838  ? 148 VAL   A O   1 
ATOM   894  C  CB  . VAL   A 1 112 ? -3.028  -21.376 12.779 1    31.939  ? 148 VAL   A CB  1 
ATOM   895  C  CG1 . VAL   A 1 112 ? -3.831  -20.586 11.741 1    36.558  ? 148 VAL   A CG1 1 
ATOM   896  C  CG2 . VAL   A 1 112 ? -1.523  -21.172 12.642 1    28.132  ? 148 VAL   A CG2 1 
ATOM   897  N  N   . ALA   A 1 113 ? -2.421  -21.32  16.357 1    38.176  ? 149 ALA   A N   1 
ATOM   898  C  CA  . ALA   A 1 113 ? -1.87   -22.041 17.498 1    37.071  ? 149 ALA   A CA  1 
ATOM   899  C  C   . ALA   A 1 113 ? -2.811  -23.146 18.004 1    34.103  ? 149 ALA   A C   1 
ATOM   900  O  O   . ALA   A 1 113 ? -4.029  -22.948 18.076 1    34.758  ? 149 ALA   A O   1 
ATOM   901  C  CB  . ALA   A 1 113 ? -1.57   -21.059 18.595 1    37.97   ? 149 ALA   A CB  1 
ATOM   902  N  N   . THR   A 1 114 ? -2.222  -24.301 18.386 1    34.709  ? 150 THR   A N   1 
ATOM   903  C  CA  . THR   A 1 114 ? -2.922  -25.432 19.001 1    33.541  ? 150 THR   A CA  1 
ATOM   904  C  C   . THR   A 1 114 ? -2.093  -25.928 20.188 1    29.666  ? 150 THR   A C   1 
ATOM   905  O  O   . THR   A 1 114 ? -0.877  -25.905 20.16  1    33.976  ? 150 THR   A O   1 
ATOM   906  C  CB  . THR   A 1 114 ? -3.222  -26.589 18.02  1    32.977  ? 150 THR   A CB  1 
ATOM   907  O  OG1 . THR   A 1 114 ? -1.983  -26.772 17.365 1    38.864  ? 150 THR   A OG1 1 
ATOM   908  C  CG2 . THR   A 1 114 ? -3.978  -26.258 16.741 1    29.833  ? 150 THR   A CG2 1 
ATOM   909  N  N   . VAL   A 1 115 ? -2.773  -26.411 21.219 1    30.975  ? 151 VAL   A N   1 
ATOM   910  C  CA  . VAL   A 1 115 ? -2.174  -27.131 22.333 1    38.455  ? 151 VAL   A CA  1 
ATOM   911  C  C   . VAL   A 1 115 ? -2.544  -28.62  22.183 1    35.538  ? 151 VAL   A C   1 
ATOM   912  O  O   . VAL   A 1 115 ? -3.729  -28.962 22.172 1    31.304  ? 151 VAL   A O   1 
ATOM   913  C  CB  . VAL   A 1 115 ? -2.609  -26.567 23.718 1    29.758  ? 151 VAL   A CB  1 
ATOM   914  C  CG1 . VAL   A 1 115 ? -1.809  -27.189 24.871 1    26.867  ? 151 VAL   A CG1 1 
ATOM   915  C  CG2 . VAL   A 1 115 ? -2.433  -25.068 23.753 1    33.384  ? 151 VAL   A CG2 1 
ATOM   916  N  N   . CYS   A 1 116 ? -1.515  -29.485 22.114 1    38.209  ? 152 CYS   A N   1 
ATOM   917  C  CA  . CYS   A 1 116 ? -1.631  -30.913 21.824 1    46.207  ? 152 CYS   A CA  1 
ATOM   918  C  C   . CYS   A 1 116 ? -1.224  -31.696 23.06  1    53.41   ? 152 CYS   A C   1 
ATOM   919  O  O   . CYS   A 1 116 ? -0.158  -31.418 23.623 1    51.591  ? 152 CYS   A O   1 
ATOM   920  C  CB  . CYS   A 1 116 ? -0.678  -31.342 20.704 1    42.953  ? 152 CYS   A CB  1 
ATOM   921  S  SG  . CYS   A 1 116 ? -1.025  -30.475 19.147 1    59.324  ? 152 CYS   A SG  1 
ATOM   922  N  N   . HIS   A 1 117 ? -2.123  -32.614 23.465 1    61.776  ? 153 HIS   A N   1 
ATOM   923  C  CA  . HIS   A 1 117 ? -1.835  -33.834 24.221 1    59.638  ? 153 HIS   A CA  1 
ATOM   924  C  C   . HIS   A 1 117 ? -0.922  -34.787 23.436 1    74.678  ? 153 HIS   A C   1 
ATOM   925  O  O   . HIS   A 1 117 ? -1.035  -34.977 22.211 1    62.512  ? 153 HIS   A O   1 
ATOM   926  C  CB  . HIS   A 1 117 ? -3.112  -34.616 24.556 1    48.984  ? 153 HIS   A CB  1 
ATOM   927  C  CG  . HIS   A 1 117 ? -4.137  -33.912 25.387 1    52.828  ? 153 HIS   A CG  1 
ATOM   928  N  ND1 . HIS   A 1 117 ? -3.922  -33.572 26.71  1    53.773  ? 153 HIS   A ND1 1 
ATOM   929  C  CD2 . HIS   A 1 117 ? -5.395  -33.492 25.094 1    60.397  ? 153 HIS   A CD2 1 
ATOM   930  C  CE1 . HIS   A 1 117 ? -5.019  -32.985 27.206 1    57.365  ? 153 HIS   A CE1 1 
ATOM   931  N  NE2 . HIS   A 1 117 ? -5.928  -32.924 26.242 1    65.31   ? 153 HIS   A NE2 1 
ATOM   932  N  N   . PRO   A 1 118 ? -0.004  -35.483 24.142 1    94.664  ? 154 PRO   A N   1 
ATOM   933  C  CA  . PRO   A 1 118 ? 0.961   -36.355 23.468 1    90.912  ? 154 PRO   A CA  1 
ATOM   934  C  C   . PRO   A 1 118 ? 0.102   -37.516 22.996 1    98.798  ? 154 PRO   A C   1 
ATOM   935  O  O   . PRO   A 1 118 ? -0.755  -37.991 23.748 1    92.757  ? 154 PRO   A O   1 
ATOM   936  C  CB  . PRO   A 1 118 ? 1.82    -36.742 24.662 1    106.082 ? 154 PRO   A CB  1 
ATOM   937  C  CG  . PRO   A 1 118 ? 0.818   -36.826 25.813 1    100.244 ? 154 PRO   A CG  1 
ATOM   938  C  CD  . PRO   A 1 118 ? 0.067   -35.531 25.615 1    106.408 ? 154 PRO   A CD  1 
ATOM   939  N  N   . GLN   A 1 119 ? 0.288   -37.93  21.74  1    101.485 ? 155 GLN   A N   1 
ATOM   940  C  CA  . GLN   A 1 119 ? -0.399  -39.126 21.279 1    118.515 ? 155 GLN   A CA  1 
ATOM   941  C  C   . GLN   A 1 119 ? -1.912  -39.04  21.529 1    107.017 ? 155 GLN   A C   1 
ATOM   942  O  O   . GLN   A 1 119 ? -2.587  -40.071 21.503 1    96.444  ? 155 GLN   A O   1 
ATOM   943  C  CB  . GLN   A 1 119 ? 0.131   -40.35  22.037 1    128.195 ? 155 GLN   A CB  1 
ATOM   944  C  CG  . GLN   A 1 119 ? 1.291   -41.084 21.374 1    105.241 ? 155 GLN   A CG  1 
ATOM   945  C  CD  . GLN   A 1 119 ? 1.042   -42.579 21.302 1    107.78  ? 155 GLN   A CD  1 
ATOM   946  O  OE1 . GLN   A 1 119 ? 0.253   -43.174 22.056 1    94.964  ? 155 GLN   A OE1 1 
ATOM   947  N  NE2 . GLN   A 1 119 ? 1.712   -43.204 20.348 1    90.851  ? 155 GLN   A NE2 1 
ATOM   948  N  N   . GLY   A 1 120 ? -2.418  -37.829 21.83  1    103.32  ? 156 GLY   A N   1 
ATOM   949  C  CA  . GLY   A 1 120 ? -3.835  -37.467 21.873 1    78.822  ? 156 GLY   A CA  1 
ATOM   950  C  C   . GLY   A 1 120 ? -4.118  -36.45  20.766 1    74.746  ? 156 GLY   A C   1 
ATOM   951  O  O   . GLY   A 1 120 ? -3.307  -36.329 19.851 1    69.294  ? 156 GLY   A O   1 
ATOM   952  N  N   . SER   A 1 121 ? -5.224  -35.697 20.85  1    71.397  ? 157 SER   A N   1 
ATOM   953  C  CA  . SER   A 1 121 ? -5.527  -34.72  19.802 1    72.19   ? 157 SER   A CA  1 
ATOM   954  C  C   . SER   A 1 121 ? -5.325  -33.275 20.293 1    62.409  ? 157 SER   A C   1 
ATOM   955  O  O   . SER   A 1 121 ? -5.002  -33.071 21.478 1    49.851  ? 157 SER   A O   1 
ATOM   956  C  CB  . SER   A 1 121 ? -6.9    -34.907 19.27  1    68.72   ? 157 SER   A CB  1 
ATOM   957  O  OG  . SER   A 1 121 ? -7.736  -34.282 20.229 1    66.423  ? 157 SER   A OG  1 
ATOM   958  N  N   . CYS   A 1 122 ? -5.545  -32.305 19.362 1    55.681  ? 158 CYS   A N   1 
ATOM   959  C  CA  . CYS   A 1 122 ? -5.024  -30.928 19.389 1    54.812  ? 158 CYS   A CA  1 
ATOM   960  C  C   . CYS   A 1 122 ? -6.094  -29.84  19.569 1    46.066  ? 158 CYS   A C   1 
ATOM   961  O  O   . CYS   A 1 122 ? -6.881  -29.539 18.678 1    43.418  ? 158 CYS   A O   1 
ATOM   962  C  CB  . CYS   A 1 122 ? -4.161  -30.554 18.178 1    53.884  ? 158 CYS   A CB  1 
ATOM   963  S  SG  . CYS   A 1 122 ? -2.571  -31.438 18.078 1    65.399  ? 158 CYS   A SG  1 
ATOM   964  N  N   . LEU   A 1 123 ? -5.993  -29.121 20.687 1    44.706  ? 159 LEU   A N   1 
ATOM   965  C  CA  . LEU   A 1 123 ? -6.962  -28.091 21.03  1    40.251  ? 159 LEU   A CA  1 
ATOM   966  C  C   . LEU   A 1 123 ? -6.603  -26.7   20.494 1    36.813  ? 159 LEU   A C   1 
ATOM   967  O  O   . LEU   A 1 123 ? -5.483  -26.196 20.587 1    35.877  ? 159 LEU   A O   1 
ATOM   968  C  CB  . LEU   A 1 123 ? -7.265  -28.118 22.525 1    33.946  ? 159 LEU   A CB  1 
ATOM   969  C  CG  . LEU   A 1 123 ? -8.07   -29.333 22.993 1    36.694  ? 159 LEU   A CG  1 
ATOM   970  C  CD1 . LEU   A 1 123 ? -7.322  -30.603 22.848 1    32.205  ? 159 LEU   A CD1 1 
ATOM   971  C  CD2 . LEU   A 1 123 ? -8.482  -29.143 24.455 1    41.303  ? 159 LEU   A CD2 1 
ATOM   972  N  N   . GLN   A 1 124 ? -7.618  -26.088 19.908 1    34.906  ? 160 GLN   A N   1 
ATOM   973  C  CA  . GLN   A 1 124 ? -7.582  -24.694 19.526 1    39.142  ? 160 GLN   A CA  1 
ATOM   974  C  C   . GLN   A 1 124 ? -8.137  -23.824 20.644 1    39.309  ? 160 GLN   A C   1 
ATOM   975  O  O   . GLN   A 1 124 ? -8.926  -24.262 21.484 1    35.518  ? 160 GLN   A O   1 
ATOM   976  C  CB  . GLN   A 1 124 ? -8.467  -24.442 18.304 1    35.872  ? 160 GLN   A CB  1 
ATOM   977  C  CG  . GLN   A 1 124 ? -7.639  -24.344 17.032 1    51.028  ? 160 GLN   A CG  1 
ATOM   978  C  CD  . GLN   A 1 124 ? -8.427  -24.616 15.774 1    61.893  ? 160 GLN   A CD  1 
ATOM   979  O  OE1 . GLN   A 1 124 ? -9.67   -24.588 15.729 1    56.355  ? 160 GLN   A OE1 1 
ATOM   980  N  NE2 . GLN   A 1 124 ? -7.654  -24.888 14.736 1    77.15   ? 160 GLN   A NE2 1 
ATOM   981  N  N   . LEU   A 1 125 ? -7.772  -22.548 20.544 1    34.385  ? 161 LEU   A N   1 
ATOM   982  C  CA  . LEU   A 1 125 ? -8.293  -21.524 21.41  1    27.444  ? 161 LEU   A CA  1 
ATOM   983  C  C   . LEU   A 1 125 ? -9.826  -21.51  21.433 1    26.86   ? 161 LEU   A C   1 
ATOM   984  O  O   . LEU   A 1 125 ? -10.419 -21.637 22.508 1    30.252  ? 161 LEU   A O   1 
ATOM   985  C  CB  . LEU   A 1 125 ? -7.617  -20.171 21.207 1    20.879  ? 161 LEU   A CB  1 
ATOM   986  C  CG  . LEU   A 1 125 ? -8.121  -19.133 22.222 1    31.86   ? 161 LEU   A CG  1 
ATOM   987  C  CD1 . LEU   A 1 125 ? -7.848  -19.538 23.709 1    23.987  ? 161 LEU   A CD1 1 
ATOM   988  C  CD2 . LEU   A 1 125 ? -7.713  -17.663 21.873 1    27.944  ? 161 LEU   A CD2 1 
ATOM   989  N  N   . GLU   A 1 126 ? -10.481 -21.291 20.295 1    37.107  ? 162 GLU   A N   1 
ATOM   990  C  CA  . GLU   A 1 126 ? -11.943 -21.241 20.295 1    47.124  ? 162 GLU   A CA  1 
ATOM   991  C  C   . GLU   A 1 126 ? -12.434 -22.415 19.452 1    55.94   ? 162 GLU   A C   1 
ATOM   992  O  O   . GLU   A 1 126 ? -12.135 -22.447 18.26  1    65.723  ? 162 GLU   A O   1 
ATOM   993  C  CB  . GLU   A 1 126 ? -12.414 -19.861 19.81  1    52.764  ? 162 GLU   A CB  1 
ATOM   994  C  CG  . GLU   A 1 126 ? -11.377 -18.779 20.121 1    62.778  ? 162 GLU   A CG  1 
ATOM   995  C  CD  . GLU   A 1 126 ? -11.458 -17.295 19.766 1    73.325  ? 162 GLU   A CD  1 
ATOM   996  O  OE1 . GLU   A 1 126 ? -12.46  -16.644 20.182 1    73.365  ? 162 GLU   A OE1 1 
ATOM   997  O  OE2 . GLU   A 1 126 ? -10.488 -16.786 19.119 1    52.697  ? 162 GLU   A OE2 1 
ATOM   998  N  N   . PRO   A 1 127 ? -13.202 -23.396 20.01  1    55.575  ? 163 PRO   A N   1 
ATOM   999  C  CA  . PRO   A 1 127 ? -13.803 -23.276 21.342 1    43.291  ? 163 PRO   A CA  1 
ATOM   1000 C  C   . PRO   A 1 127 ? -13.176 -24.136 22.442 1    35.649  ? 163 PRO   A C   1 
ATOM   1001 O  O   . PRO   A 1 127 ? -13.605 -24.07  23.59  1    39.696  ? 163 PRO   A O   1 
ATOM   1002 C  CB  . PRO   A 1 127 ? -15.241 -23.788 20.947 1    39.364  ? 163 PRO   A CB  1 
ATOM   1003 C  CG  . PRO   A 1 127 ? -14.957 -24.945 19.978 1    40.231  ? 163 PRO   A CG  1 
ATOM   1004 C  CD  . PRO   A 1 127 ? -13.582 -24.668 19.36  1    45.373  ? 163 PRO   A CD  1 
ATOM   1005 N  N   . ASP   A 1 128 ? -12.143 -24.927 22.107 1    32.87   ? 164 ASP   A N   1 
ATOM   1006 C  CA  . ASP   A 1 128 ? -11.728 -26.03  22.965 1    33.938  ? 164 ASP   A CA  1 
ATOM   1007 C  C   . ASP   A 1 128 ? -11.102 -25.513 24.254 1    33.739  ? 164 ASP   A C   1 
ATOM   1008 O  O   . ASP   A 1 128 ? -11.596 -25.884 25.318 1    37.346  ? 164 ASP   A O   1 
ATOM   1009 C  CB  . ASP   A 1 128 ? -10.897 -27.076 22.234 1    36.402  ? 164 ASP   A CB  1 
ATOM   1010 C  CG  . ASP   A 1 128 ? -11.417 -27.438 20.85  1    48.404  ? 164 ASP   A CG  1 
ATOM   1011 O  OD1 . ASP   A 1 128 ? -12.655 -27.707 20.718 1    50.764  ? 164 ASP   A OD1 1 
ATOM   1012 O  OD2 . ASP   A 1 128 ? -10.575 -27.437 19.917 1    45.052  ? 164 ASP   A OD2 1 
ATOM   1013 N  N   . LEU   A 1 129 ? -10.068 -24.65  24.152 1    27.817  ? 165 LEU   A N   1 
ATOM   1014 C  CA  . LEU   A 1 129 ? -9.311  -24.29  25.345 1    31.368  ? 165 LEU   A CA  1 
ATOM   1015 C  C   . LEU   A 1 129 ? -10.171 -23.351 26.193 1    36.046  ? 165 LEU   A C   1 
ATOM   1016 O  O   . LEU   A 1 129 ? -10.132 -23.432 27.427 1    29.894  ? 165 LEU   A O   1 
ATOM   1017 C  CB  . LEU   A 1 129 ? -7.904  -23.732 25.142 1    32.148  ? 165 LEU   A CB  1 
ATOM   1018 C  CG  . LEU   A 1 129 ? -6.842  -24.617 24.491 1    40.603  ? 165 LEU   A CG  1 
ATOM   1019 C  CD1 . LEU   A 1 129 ? -5.736  -23.637 24.135 1    36.181  ? 165 LEU   A CD1 1 
ATOM   1020 C  CD2 . LEU   A 1 129 ? -6.264  -25.734 25.357 1    29.41   ? 165 LEU   A CD2 1 
ATOM   1021 N  N   . THR   A 1 130 ? -10.949 -22.491 25.501 1    31.62   ? 166 THR   A N   1 
ATOM   1022 C  CA  . THR   A 1 130 ? -11.98  -21.687 26.146 1    36.01   ? 166 THR   A CA  1 
ATOM   1023 C  C   . THR   A 1 130 ? -12.873 -22.568 27.031 1    31.511  ? 166 THR   A C   1 
ATOM   1024 O  O   . THR   A 1 130 ? -13.014 -22.281 28.212 1    29.934  ? 166 THR   A O   1 
ATOM   1025 C  CB  . THR   A 1 130 ? -12.766 -20.756 25.198 1    35.377  ? 166 THR   A CB  1 
ATOM   1026 O  OG1 . THR   A 1 130 ? -11.868 -19.872 24.526 1    28.317  ? 166 THR   A OG1 1 
ATOM   1027 C  CG2 . THR   A 1 130 ? -13.766 -19.83  25.901 1    28.498  ? 166 THR   A CG2 1 
ATOM   1028 N  N   . ASN   A 1 131 ? -13.453 -23.638 26.475 1    32.475  ? 167 ASN   A N   1 
ATOM   1029 C  CA  . ASN   A 1 131 ? -14.336 -24.52  27.24  1    32.485  ? 167 ASN   A CA  1 
ATOM   1030 C  C   . ASN   A 1 131 ? -13.585 -25.18  28.417 1    26.982  ? 167 ASN   A C   1 
ATOM   1031 O  O   . ASN   A 1 131 ? -14.169 -25.36  29.474 1    27.888  ? 167 ASN   A O   1 
ATOM   1032 C  CB  . ASN   A 1 131 ? -15.063 -25.54  26.351 1    34.559  ? 167 ASN   A CB  1 
ATOM   1033 C  CG  . ASN   A 1 131 ? -15.895 -24.951 25.214 1    50.799  ? 167 ASN   A CG  1 
ATOM   1034 O  OD1 . ASN   A 1 131 ? -16.383 -23.814 25.287 1    57.21   ? 167 ASN   A OD1 1 
ATOM   1035 N  ND2 . ASN   A 1 131 ? -16.123 -25.705 24.141 1    40.922  ? 167 ASN   A ND2 1 
ATOM   1036 N  N   . VAL   A 1 132 ? -12.327 -25.619 28.23  1    21.762  ? 168 VAL   A N   1 
ATOM   1037 C  CA  . VAL   A 1 132 ? -11.58  -26.194 29.321 1    25.03   ? 168 VAL   A CA  1 
ATOM   1038 C  C   . VAL   A 1 132 ? -11.471 -25.161 30.451 1    29.857  ? 168 VAL   A C   1 
ATOM   1039 O  O   . VAL   A 1 132 ? -11.853 -25.445 31.603 1    26.174  ? 168 VAL   A O   1 
ATOM   1040 C  CB  . VAL   A 1 132 ? -10.193 -26.76  28.94  1    35.649  ? 168 VAL   A CB  1 
ATOM   1041 C  CG1 . VAL   A 1 132 ? -9.342  -27.167 30.166 1    23.995  ? 168 VAL   A CG1 1 
ATOM   1042 C  CG2 . VAL   A 1 132 ? -10.318 -27.912 27.934 1    31.39   ? 168 VAL   A CG2 1 
ATOM   1043 N  N   . MET   A 1 133 ? -10.974 -23.952 30.107 1    31.546  ? 169 MET   A N   1 
ATOM   1044 C  CA  . MET   A 1 133 ? -10.846 -22.873 31.074 1    26.446  ? 169 MET   A CA  1 
ATOM   1045 C  C   . MET   A 1 133 ? -12.184 -22.565 31.746 1    26.798  ? 169 MET   A C   1 
ATOM   1046 O  O   . MET   A 1 133 ? -12.212 -22.34  32.96  1    25.843  ? 169 MET   A O   1 
ATOM   1047 C  CB  . MET   A 1 133 ? -10.183 -21.648 30.458 1    29.565  ? 169 MET   A CB  1 
ATOM   1048 C  CG  . MET   A 1 133 ? -8.76   -21.874 30.007 1    27.011  ? 169 MET   A CG  1 
ATOM   1049 S  SD  . MET   A 1 133 ? -7.603  -22.486 31.245 1    27.518  ? 169 MET   A SD  1 
ATOM   1050 C  CE  . MET   A 1 133 ? -7.504  -21.46  32.723 1    25.203  ? 169 MET   A CE  1 
ATOM   1051 N  N   . ALA   A 1 134 ? -13.302 -22.634 30.999 1    25.036  ? 170 ALA   A N   1 
ATOM   1052 C  CA  . ALA   A 1 134 ? -14.606 -22.237 31.546 1    25.821  ? 170 ALA   A CA  1 
ATOM   1053 C  C   . ALA   A 1 134 ? -15.17  -23.234 32.547 1    31.613  ? 170 ALA   A C   1 
ATOM   1054 O  O   . ALA   A 1 134 ? -15.842 -22.824 33.49  1    29.404  ? 170 ALA   A O   1 
ATOM   1055 C  CB  . ALA   A 1 134 ? -15.645 -22.03  30.468 1    25.278  ? 170 ALA   A CB  1 
ATOM   1056 N  N   . THR   A 1 135 ? -14.929 -24.544 32.333 1    38.586  ? 171 THR   A N   1 
ATOM   1057 C  CA  . THR   A 1 135 ? -15.753 -25.542 33.004 1    36.814  ? 171 THR   A CA  1 
ATOM   1058 C  C   . THR   A 1 135 ? -14.91  -26.524 33.8   1    32.351  ? 171 THR   A C   1 
ATOM   1059 O  O   . THR   A 1 135 ? -15.424 -27.077 34.742 1    39.75   ? 171 THR   A O   1 
ATOM   1060 C  CB  . THR   A 1 135 ? -16.681 -26.271 32.02  1    40.098  ? 171 THR   A CB  1 
ATOM   1061 O  OG1 . THR   A 1 135 ? -15.73  -26.944 31.22  1    36.787  ? 171 THR   A OG1 1 
ATOM   1062 C  CG2 . THR   A 1 135 ? -17.509 -25.351 31.131 1    40.783  ? 171 THR   A CG2 1 
ATOM   1063 N  N   . SER   A 1 136 ? -13.646 -26.769 33.44  1    32.36   ? 172 SER   A N   1 
ATOM   1064 C  CA  . SER   A 1 136 ? -12.887 -27.721 34.22  1    28.484  ? 172 SER   A CA  1 
ATOM   1065 C  C   . SER   A 1 136 ? -12.661 -27.199 35.653 1    32.65   ? 172 SER   A C   1 
ATOM   1066 O  O   . SER   A 1 136 ? -12.574 -25.989 35.899 1    37.199  ? 172 SER   A O   1 
ATOM   1067 C  CB  . SER   A 1 136 ? -11.63  -28.064 33.536 1    26.506  ? 172 SER   A CB  1 
ATOM   1068 O  OG  . SER   A 1 136 ? -10.783 -28.752 34.463 1    29.139  ? 172 SER   A OG  1 
ATOM   1069 N  N   . ARG   A 1 137 ? -12.523 -28.118 36.611 1    26.888  ? 173 ARG   A N   1 
ATOM   1070 C  CA  . ARG   A 1 137 ? -12.42  -27.778 38.031 1    30.114  ? 173 ARG   A CA  1 
ATOM   1071 C  C   . ARG   A 1 137 ? -11.312 -28.631 38.652 1    27.895  ? 173 ARG   A C   1 
ATOM   1072 O  O   . ARG   A 1 137 ? -11.317 -28.846 39.869 1    25.414  ? 173 ARG   A O   1 
ATOM   1073 C  CB  . ARG   A 1 137 ? -13.668 -27.901 38.925 1    29.466  ? 173 ARG   A CB  1 
ATOM   1074 C  CG  . ARG   A 1 137 ? -14.94  -27.192 38.455 1    30.08   ? 173 ARG   A CG  1 
ATOM   1075 C  CD  . ARG   A 1 137 ? -14.671 -25.696 38.464 1    32.743  ? 173 ARG   A CD  1 
ATOM   1076 N  NE  . ARG   A 1 137 ? -15.837 -24.808 38.353 1    36.115  ? 173 ARG   A NE  1 
ATOM   1077 C  CZ  . ARG   A 1 137 ? -16.126 -23.964 37.347 1    38.115  ? 173 ARG   A CZ  1 
ATOM   1078 N  NH1 . ARG   A 1 137 ? -17.288 -23.329 37.318 1    40.977  ? 173 ARG   A NH1 1 
ATOM   1079 N  NH2 . ARG   A 1 137 ? -15.282 -23.762 36.345 1    44.208  ? 173 ARG   A NH2 1 
ATOM   1080 N  N   . LYS   A 1 138 ? -10.351 -29.023 37.798 1    27.393  ? 174 LYS   A N   1 
ATOM   1081 C  CA  . LYS   A 1 138 ? -9.175  -29.812 38.154 1    30.993  ? 174 LYS   A CA  1 
ATOM   1082 C  C   . LYS   A 1 138 ? -7.903  -29.002 37.948 1    27.234  ? 174 LYS   A C   1 
ATOM   1083 O  O   . LYS   A 1 138 ? -7.525  -28.743 36.815 1    30.451  ? 174 LYS   A O   1 
ATOM   1084 C  CB  . LYS   A 1 138 ? -9.174  -31.132 37.375 1    36.448  ? 174 LYS   A CB  1 
ATOM   1085 C  CG  . LYS   A 1 138 ? -10.35  -31.988 37.889 1    41.189  ? 174 LYS   A CG  1 
ATOM   1086 C  CD  . LYS   A 1 138 ? -10.514 -33.376 37.269 1    57.725  ? 174 LYS   A CD  1 
ATOM   1087 C  CE  . LYS   A 1 138 ? -9.278  -34.236 37.229 1    54.036  ? 174 LYS   A CE  1 
ATOM   1088 N  NZ  . LYS   A 1 138 ? -9.705  -35.549 36.754 1    74.153  ? 174 LYS   A NZ  1 
ATOM   1089 N  N   . TYR   A 1 139 ? -7.313  -28.544 39.064 1    26.015  ? 175 TYR   A N   1 
ATOM   1090 C  CA  . TYR   A 1 139 ? -6.09   -27.743 39.106 1    26.659  ? 175 TYR   A CA  1 
ATOM   1091 C  C   . TYR   A 1 139 ? -5.123  -28.076 37.961 1    25.213  ? 175 TYR   A C   1 
ATOM   1092 O  O   . TYR   A 1 139 ? -4.67   -27.166 37.229 1    23.914  ? 175 TYR   A O   1 
ATOM   1093 C  CB  . TYR   A 1 139 ? -5.402  -27.952 40.455 1    25.936  ? 175 TYR   A CB  1 
ATOM   1094 C  CG  . TYR   A 1 139 ? -4.398  -26.832 40.718 1    27.707  ? 175 TYR   A CG  1 
ATOM   1095 C  CD1 . TYR   A 1 139 ? -3.035  -26.96  40.367 1    28.417  ? 175 TYR   A CD1 1 
ATOM   1096 C  CD2 . TYR   A 1 139 ? -4.771  -25.679 41.395 1    27.696  ? 175 TYR   A CD2 1 
ATOM   1097 C  CE1 . TYR   A 1 139 ? -2.102  -25.968 40.631 1    22.851  ? 175 TYR   A CE1 1 
ATOM   1098 C  CE2 . TYR   A 1 139 ? -3.832  -24.695 41.7   1    29.702  ? 175 TYR   A CE2 1 
ATOM   1099 C  CZ  . TYR   A 1 139 ? -2.509  -24.808 41.272 1    31.879  ? 175 TYR   A CZ  1 
ATOM   1100 O  OH  . TYR   A 1 139 ? -1.622  -23.755 41.476 1    36.566  ? 175 TYR   A OH  1 
ATOM   1101 N  N   . GLU   A 1 140 ? -4.866  -29.386 37.8   1    19.156  ? 176 GLU   A N   1 
ATOM   1102 C  CA  . GLU   A 1 140 ? -3.879  -29.91  36.858 1    22.856  ? 176 GLU   A CA  1 
ATOM   1103 C  C   . GLU   A 1 140 ? -4.34   -29.766 35.413 1    24.697  ? 176 GLU   A C   1 
ATOM   1104 O  O   . GLU   A 1 140 ? -3.494  -29.599 34.539 1    23.331  ? 176 GLU   A O   1 
ATOM   1105 C  CB  . GLU   A 1 140 ? -3.636  -31.402 37.041 1    25.605  ? 176 GLU   A CB  1 
ATOM   1106 C  CG  . GLU   A 1 140 ? -2.792  -31.629 38.295 1    38.89   ? 176 GLU   A CG  1 
ATOM   1107 C  CD  . GLU   A 1 140 ? -1.333  -31.115 38.287 1    51.764  ? 176 GLU   A CD  1 
ATOM   1108 O  OE1 . GLU   A 1 140 ? -0.614  -31.146 37.195 1    46.414  ? 176 GLU   A OE1 1 
ATOM   1109 O  OE2 . GLU   A 1 140 ? -0.883  -30.734 39.434 1    49.009  ? 176 GLU   A OE2 1 
ATOM   1110 N  N   . ASP   A 1 141 ? -5.659  -29.858 35.16  1    28.337  ? 177 ASP   A N   1 
ATOM   1111 C  CA  . ASP   A 1 141 ? -6.194  -29.742 33.799 1    33.549  ? 177 ASP   A CA  1 
ATOM   1112 C  C   . ASP   A 1 141 ? -6.183  -28.268 33.399 1    34.582  ? 177 ASP   A C   1 
ATOM   1113 O  O   . ASP   A 1 141 ? -5.847  -27.925 32.256 1    38.743  ? 177 ASP   A O   1 
ATOM   1114 C  CB  . ASP   A 1 141 ? -7.573  -30.381 33.614 1    37.242  ? 177 ASP   A CB  1 
ATOM   1115 C  CG  . ASP   A 1 141 ? -7.672  -31.908 33.763 1    52.449  ? 177 ASP   A CG  1 
ATOM   1116 O  OD1 . ASP   A 1 141 ? -6.644  -32.61  33.646 1    50.487  ? 177 ASP   A OD1 1 
ATOM   1117 O  OD2 . ASP   A 1 141 ? -8.787  -32.426 34.015 1    65.548  ? 177 ASP   A OD2 1 
ATOM   1118 N  N   . LEU   A 1 142 ? -6.562  -27.4   34.346 1    28.166  ? 178 LEU   A N   1 
ATOM   1119 C  CA  . LEU   A 1 142 ? -6.491  -25.963 34.08  1    28.795  ? 178 LEU   A CA  1 
ATOM   1120 C  C   . LEU   A 1 142 ? -5.031  -25.559 33.775 1    26.038  ? 178 LEU   A C   1 
ATOM   1121 O  O   . LEU   A 1 142 ? -4.75   -24.801 32.833 1    18.056  ? 178 LEU   A O   1 
ATOM   1122 C  CB  . LEU   A 1 142 ? -7.15   -25.226 35.252 1    22.677  ? 178 LEU   A CB  1 
ATOM   1123 C  CG  . LEU   A 1 142 ? -8.661  -25.489 35.373 1    21.514  ? 178 LEU   A CG  1 
ATOM   1124 C  CD1 . LEU   A 1 142 ? -9.362  -25.092 36.701 1    20.343  ? 178 LEU   A CD1 1 
ATOM   1125 C  CD2 . LEU   A 1 142 ? -9.452  -24.983 34.164 1    21.232  ? 178 LEU   A CD2 1 
ATOM   1126 N  N   . LEU   A 1 143 ? -4.088  -26.173 34.515 1    28.838  ? 179 LEU   A N   1 
ATOM   1127 C  CA  . LEU   A 1 143 ? -2.697  -25.757 34.388 1    28.325  ? 179 LEU   A CA  1 
ATOM   1128 C  C   . LEU   A 1 143 ? -2.164  -26.17  33.014 1    25.124  ? 179 LEU   A C   1 
ATOM   1129 O  O   . LEU   A 1 143 ? -1.506  -25.443 32.304 1    29.02   ? 179 LEU   A O   1 
ATOM   1130 C  CB  . LEU   A 1 143 ? -1.959  -26.283 35.607 1    23.675  ? 179 LEU   A CB  1 
ATOM   1131 C  CG  . LEU   A 1 143 ? -0.468  -25.959 35.685 1    27.189  ? 179 LEU   A CG  1 
ATOM   1132 C  CD1 . LEU   A 1 143 ? -0.086  -26.233 37.094 1    22.833  ? 179 LEU   A CD1 1 
ATOM   1133 C  CD2 . LEU   A 1 143 ? 0.269   -26.995 34.883 1    25.85   ? 179 LEU   A CD2 1 
ATOM   1134 N  N   . TRP   A 1 144 ? -2.617  -27.309 32.567 1    27.288  ? 180 TRP   A N   1 
ATOM   1135 C  CA  . TRP   A 1 144 ? -2.224  -27.878 31.307 1    26.538  ? 180 TRP   A CA  1 
ATOM   1136 C  C   . TRP   A 1 144 ? -2.652  -26.875 30.211 1    27.777  ? 180 TRP   A C   1 
ATOM   1137 O  O   . TRP   A 1 144 ? -1.886  -26.505 29.307 1    23.672  ? 180 TRP   A O   1 
ATOM   1138 C  CB  . TRP   A 1 144 ? -2.798  -29.328 31.2   1    28.483  ? 180 TRP   A CB  1 
ATOM   1139 C  CG  . TRP   A 1 144 ? -2.437  -29.912 29.863 1    39.667  ? 180 TRP   A CG  1 
ATOM   1140 C  CD1 . TRP   A 1 144 ? -1.257  -30.511 29.474 1    36.377  ? 180 TRP   A CD1 1 
ATOM   1141 C  CD2 . TRP   A 1 144 ? -3.229  -29.715 28.667 1    33.009  ? 180 TRP   A CD2 1 
ATOM   1142 N  NE1 . TRP   A 1 144 ? -1.272  -30.697 28.107 1    38.765  ? 180 TRP   A NE1 1 
ATOM   1143 C  CE2 . TRP   A 1 144 ? -2.457  -30.217 27.589 1    32.942  ? 180 TRP   A CE2 1 
ATOM   1144 C  CE3 . TRP   A 1 144 ? -4.515  -29.202 28.428 1    37.479  ? 180 TRP   A CE3 1 
ATOM   1145 C  CZ2 . TRP   A 1 144 ? -2.928  -30.184 26.276 1    34.001  ? 180 TRP   A CZ2 1 
ATOM   1146 C  CZ3 . TRP   A 1 144 ? -4.996  -29.208 27.126 1    31.624  ? 180 TRP   A CZ3 1 
ATOM   1147 C  CH2 . TRP   A 1 144 ? -4.188  -29.65  26.067 1    30.62   ? 180 TRP   A CH2 1 
ATOM   1148 N  N   . ALA   A 1 145 ? -3.881  -26.348 30.315 1    28.141  ? 181 ALA   A N   1 
ATOM   1149 C  CA  . ALA   A 1 145 ? -4.354  -25.493 29.242 1    25.241  ? 181 ALA   A CA  1 
ATOM   1150 C  C   . ALA   A 1 145 ? -3.694  -24.105 29.317 1    28.816  ? 181 ALA   A C   1 
ATOM   1151 O  O   . ALA   A 1 145 ? -3.354  -23.502 28.291 1    26.496  ? 181 ALA   A O   1 
ATOM   1152 C  CB  . ALA   A 1 145 ? -5.853  -25.444 29.279 1    21.523  ? 181 ALA   A CB  1 
ATOM   1153 N  N   . TRP   A 1 146 ? -3.496  -23.613 30.553 1    28.979  ? 182 TRP   A N   1 
ATOM   1154 C  CA  . TRP   A 1 146 ? -2.988  -22.28  30.792 1    24.491  ? 182 TRP   A CA  1 
ATOM   1155 C  C   . TRP   A 1 146 ? -1.533  -22.225 30.337 1    23.655  ? 182 TRP   A C   1 
ATOM   1156 O  O   . TRP   A 1 146 ? -1.191  -21.351 29.559 1    23.385  ? 182 TRP   A O   1 
ATOM   1157 C  CB  . TRP   A 1 146 ? -3.189  -21.867 32.268 1    25.536  ? 182 TRP   A CB  1 
ATOM   1158 C  CG  . TRP   A 1 146 ? -2.758  -20.454 32.617 1    22.603  ? 182 TRP   A CG  1 
ATOM   1159 C  CD1 . TRP   A 1 146 ? -3.538  -19.336 32.705 1    25.61   ? 182 TRP   A CD1 1 
ATOM   1160 C  CD2 . TRP   A 1 146 ? -1.417  -20.009 32.907 1    19.04   ? 182 TRP   A CD2 1 
ATOM   1161 N  NE1 . TRP   A 1 146 ? -2.795  -18.245 33.094 1    20.1    ? 182 TRP   A NE1 1 
ATOM   1162 C  CE2 . TRP   A 1 146 ? -1.482  -18.617 33.165 1    20.375  ? 182 TRP   A CE2 1 
ATOM   1163 C  CE3 . TRP   A 1 146 ? -0.168  -20.658 32.98  1    16.892  ? 182 TRP   A CE3 1 
ATOM   1164 C  CZ2 . TRP   A 1 146 ? -0.346  -17.857 33.484 1    19.581  ? 182 TRP   A CZ2 1 
ATOM   1165 C  CZ3 . TRP   A 1 146 ? 0.953   -19.894 33.229 1    17.655  ? 182 TRP   A CZ3 1 
ATOM   1166 C  CH2 . TRP   A 1 146 ? 0.858   -18.531 33.547 1    21.315  ? 182 TRP   A CH2 1 
ATOM   1167 N  N   . GLU   A 1 147 ? -0.695  -23.149 30.827 1    25.538  ? 183 GLU   A N   1 
ATOM   1168 C  CA  . GLU   A 1 147 ? 0.691   -23.228 30.403 1    23.883  ? 183 GLU   A CA  1 
ATOM   1169 C  C   . GLU   A 1 147 ? 0.821   -23.571 28.904 1    29.306  ? 183 GLU   A C   1 
ATOM   1170 O  O   . GLU   A 1 147 ? 1.603   -22.954 28.182 1    27.404  ? 183 GLU   A O   1 
ATOM   1171 C  CB  . GLU   A 1 147 ? 1.41    -24.253 31.265 1    26.436  ? 183 GLU   A CB  1 
ATOM   1172 C  CG  . GLU   A 1 147 ? 2.929   -24.315 30.991 1    31.932  ? 183 GLU   A CG  1 
ATOM   1173 C  CD  . GLU   A 1 147 ? 3.693   -23.012 31.267 1    43.691  ? 183 GLU   A CD  1 
ATOM   1174 O  OE1 . GLU   A 1 147 ? 3.324   -22.36  32.279 1    46.699  ? 183 GLU   A OE1 1 
ATOM   1175 O  OE2 . GLU   A 1 147 ? 4.657   -22.619 30.553 1    44.982  ? 183 GLU   A OE2 1 
ATOM   1176 N  N   . GLY   A 1 148 ? 0.076   -24.567 28.419 1    31.451  ? 184 GLY   A N   1 
ATOM   1177 C  CA  . GLY   A 1 148 ? 0.156   -24.943 27.015 1    33.22   ? 184 GLY   A CA  1 
ATOM   1178 C  C   . GLY   A 1 148 ? -0.115  -23.78  26.062 1    32.722  ? 184 GLY   A C   1 
ATOM   1179 O  O   . GLY   A 1 148 ? 0.628   -23.608 25.096 1    32.282  ? 184 GLY   A O   1 
ATOM   1180 N  N   . TRP   A 1 149 ? -1.126  -22.956 26.365 1    30.692  ? 185 TRP   A N   1 
ATOM   1181 C  CA  . TRP   A 1 149 ? -1.428  -21.8   25.516 1    29.77   ? 185 TRP   A CA  1 
ATOM   1182 C  C   . TRP   A 1 149 ? -0.291  -20.768 25.48  1    28.952  ? 185 TRP   A C   1 
ATOM   1183 O  O   . TRP   A 1 149 ? 0.068   -20.227 24.435 1    26.12   ? 185 TRP   A O   1 
ATOM   1184 C  CB  . TRP   A 1 149 ? -2.795  -21.174 25.85  1    25.528  ? 185 TRP   A CB  1 
ATOM   1185 C  CG  . TRP   A 1 149 ? -3.168  -20.044 24.937 1    25.565  ? 185 TRP   A CG  1 
ATOM   1186 C  CD1 . TRP   A 1 149 ? -3.244  -18.707 25.245 1    25.201  ? 185 TRP   A CD1 1 
ATOM   1187 C  CD2 . TRP   A 1 149 ? -3.467  -20.133 23.53  1    24.79   ? 185 TRP   A CD2 1 
ATOM   1188 N  NE1 . TRP   A 1 149 ? -3.569  -17.962 24.133 1    18.755  ? 185 TRP   A NE1 1 
ATOM   1189 C  CE2 . TRP   A 1 149 ? -3.713  -18.81  23.069 1    24.659  ? 185 TRP   A CE2 1 
ATOM   1190 C  CE3 . TRP   A 1 149 ? -3.504  -21.181 22.603 1    28.162  ? 185 TRP   A CE3 1 
ATOM   1191 C  CZ2 . TRP   A 1 149 ? -4.038  -18.544 21.727 1    29.6    ? 185 TRP   A CZ2 1 
ATOM   1192 C  CZ3 . TRP   A 1 149 ? -3.817  -20.918 21.282 1    22.464  ? 185 TRP   A CZ3 1 
ATOM   1193 C  CH2 . TRP   A 1 149 ? -4.08   -19.616 20.849 1    25.989  ? 185 TRP   A CH2 1 
ATOM   1194 N  N   . ARG   A 1 150 ? 0.259   -20.439 26.648 1    29.559  ? 186 ARG   A N   1 
ATOM   1195 C  CA  . ARG   A 1 150 ? 1.411   -19.538 26.712 1    29.89   ? 186 ARG   A CA  1 
ATOM   1196 C  C   . ARG   A 1 150 ? 2.661   -20.099 25.978 1    32.565  ? 186 ARG   A C   1 
ATOM   1197 O  O   . ARG   A 1 150 ? 3.448   -19.346 25.38  1    35.798  ? 186 ARG   A O   1 
ATOM   1198 C  CB  . ARG   A 1 150 ? 1.541   -19.08  28.175 1    23.066  ? 186 ARG   A CB  1 
ATOM   1199 C  CG  . ARG   A 1 150 ? 0.355   -18.151 28.44  1    22.065  ? 186 ARG   A CG  1 
ATOM   1200 C  CD  . ARG   A 1 150 ? 0.247   -17.882 29.926 1    24.597  ? 186 ARG   A CD  1 
ATOM   1201 N  NE  . ARG   A 1 150 ? -0.846  -17     30.343 1    28.469  ? 186 ARG   A NE  1 
ATOM   1202 C  CZ  . ARG   A 1 150 ? -2.123  -17.304 30.126 1    24.432  ? 186 ARG   A CZ  1 
ATOM   1203 N  NH1 . ARG   A 1 150 ? -3.01   -16.359 30.208 1    23.176  ? 186 ARG   A NH1 1 
ATOM   1204 N  NH2 . ARG   A 1 150 ? -2.471  -18.501 29.693 1    23.14   ? 186 ARG   A NH2 1 
ATOM   1205 N  N   . ASP   A 1 151 ? 2.85    -21.42  26.043 1    25.445  ? 187 ASP   A N   1 
ATOM   1206 C  CA  . ASP   A 1 151 ? 3.942   -22.154 25.429 1    33.451  ? 187 ASP   A CA  1 
ATOM   1207 C  C   . ASP   A 1 151 ? 3.873   -22.104 23.891 1    31.131  ? 187 ASP   A C   1 
ATOM   1208 O  O   . ASP   A 1 151 ? 4.893   -21.961 23.259 1    27.656  ? 187 ASP   A O   1 
ATOM   1209 C  CB  . ASP   A 1 151 ? 3.941   -23.572 25.979 1    34.051  ? 187 ASP   A CB  1 
ATOM   1210 C  CG  . ASP   A 1 151 ? 4.548   -23.721 27.362 1    50.145  ? 187 ASP   A CG  1 
ATOM   1211 O  OD1 . ASP   A 1 151 ? 4.961   -22.652 27.91  1    54.839  ? 187 ASP   A OD1 1 
ATOM   1212 O  OD2 . ASP   A 1 151 ? 4.627   -24.902 27.865 1    47.885  ? 187 ASP   A OD2 1 
ATOM   1213 N  N   . LYS   A 1 152 ? 2.684   -22.242 23.299 1    27.026  ? 188 LYS   A N   1 
ATOM   1214 C  CA  . LYS   A 1 152 ? 2.523   -22.345 21.865 1    28.323  ? 188 LYS   A CA  1 
ATOM   1215 C  C   . LYS   A 1 152 ? 2.12    -20.99  21.265 1    34.162  ? 188 LYS   A C   1 
ATOM   1216 O  O   . LYS   A 1 152 ? 2.722   -20.642 20.251 1    48.761  ? 188 LYS   A O   1 
ATOM   1217 C  CB  . LYS   A 1 152 ? 1.493   -23.4   21.436 1    31.524  ? 188 LYS   A CB  1 
ATOM   1218 C  CG  . LYS   A 1 152 ? 1.682   -24.81  22.001 1    39.534  ? 188 LYS   A CG  1 
ATOM   1219 C  CD  . LYS   A 1 152 ? 2.969   -25.602 21.726 1    47.081  ? 188 LYS   A CD  1 
ATOM   1220 C  CE  . LYS   A 1 152 ? 3.443   -25.776 20.301 1    50.943  ? 188 LYS   A CE  1 
ATOM   1221 N  NZ  . LYS   A 1 152 ? 2.316   -26.031 19.397 1    60.23   ? 188 LYS   A NZ  1 
ATOM   1222 N  N   . ALA   A 1 153 ? 1.147   -20.221 21.825 1    25.978  ? 189 ALA   A N   1 
ATOM   1223 C  CA  . ALA   A 1 153 ? 0.891   -18.879 21.269 1    27.254  ? 189 ALA   A CA  1 
ATOM   1224 C  C   . ALA   A 1 153 ? 1.896   -17.85  21.755 1    26.57   ? 189 ALA   A C   1 
ATOM   1225 O  O   . ALA   A 1 153 ? 2.445   -17.062 20.982 1    28.438  ? 189 ALA   A O   1 
ATOM   1226 C  CB  . ALA   A 1 153 ? -0.514  -18.363 21.495 1    24.159  ? 189 ALA   A CB  1 
ATOM   1227 N  N   . GLY   A 1 154 ? 2.084   -17.854 23.071 1    31.43   ? 190 GLY   A N   1 
ATOM   1228 C  CA  . GLY   A 1 154 ? 2.904   -16.857 23.725 1    33.661  ? 190 GLY   A CA  1 
ATOM   1229 C  C   . GLY   A 1 154 ? 4.3     -16.8   23.115 1    30.617  ? 190 GLY   A C   1 
ATOM   1230 O  O   . GLY   A 1 154 ? 4.599   -15.807 22.461 1    36.189  ? 190 GLY   A O   1 
ATOM   1231 N  N   . ARG   A 1 155 ? 5.107   -17.837 23.408 1    30.527  ? 191 ARG   A N   1 
ATOM   1232 C  CA  . ARG   A 1 155 ? 6.503   -18.01  23.018 1    31.719  ? 191 ARG   A CA  1 
ATOM   1233 C  C   . ARG   A 1 155 ? 6.629   -17.777 21.501 1    29.214  ? 191 ARG   A C   1 
ATOM   1234 O  O   . ARG   A 1 155 ? 7.632   -17.248 21.017 1    27.249  ? 191 ARG   A O   1 
ATOM   1235 C  CB  . ARG   A 1 155 ? 6.973   -19.455 23.202 1    29.389  ? 191 ARG   A CB  1 
ATOM   1236 C  CG  . ARG   A 1 155 ? 7.742   -20.354 24.164 1    35.093  ? 191 ARG   A CG  1 
ATOM   1237 C  CD  . ARG   A 1 155 ? 7.55    -20.359 25.666 1    34.736  ? 191 ARG   A CD  1 
ATOM   1238 N  NE  . ARG   A 1 155 ? 8.285   -21.597 25.912 1    30.923  ? 191 ARG   A NE  1 
ATOM   1239 C  CZ  . ARG   A 1 155 ? 8.284   -22.365 27.017 1    32.74   ? 191 ARG   A CZ  1 
ATOM   1240 N  NH1 . ARG   A 1 155 ? 8.362   -23.679 26.892 1    29.247  ? 191 ARG   A NH1 1 
ATOM   1241 N  NH2 . ARG   A 1 155 ? 8.084   -21.881 28.24  1    30.507  ? 191 ARG   A NH2 1 
ATOM   1242 N  N   . ALA   A 1 156 ? 5.611   -18.169 20.731 1    27.921  ? 192 ALA   A N   1 
ATOM   1243 C  CA  . ALA   A 1 156 ? 5.811   -18.128 19.282 1    28.984  ? 192 ALA   A CA  1 
ATOM   1244 C  C   . ALA   A 1 156 ? 5.747   -16.693 18.769 1    32.896  ? 192 ALA   A C   1 
ATOM   1245 O  O   . ALA   A 1 156 ? 6.265   -16.408 17.689 1    37.702  ? 192 ALA   A O   1 
ATOM   1246 C  CB  . ALA   A 1 156 ? 4.789   -18.964 18.558 1    23.528  ? 192 ALA   A CB  1 
ATOM   1247 N  N   . ILE   A 1 157 ? 5.068   -15.812 19.518 1    26.537  ? 193 ILE   A N   1 
ATOM   1248 C  CA  . ILE   A 1 157 ? 5.028   -14.407 19.15  1    28.685  ? 193 ILE   A CA  1 
ATOM   1249 C  C   . ILE   A 1 157 ? 6.36    -13.734 19.486 1    27.352  ? 193 ILE   A C   1 
ATOM   1250 O  O   . ILE   A 1 157 ? 6.639   -12.721 18.839 1    28.564  ? 193 ILE   A O   1 
ATOM   1251 C  CB  . ILE   A 1 157 ? 3.818   -13.671 19.776 1    33.989  ? 193 ILE   A CB  1 
ATOM   1252 C  CG1 . ILE   A 1 157 ? 2.479   -14.32  19.393 1    39.663  ? 193 ILE   A CG1 1 
ATOM   1253 C  CG2 . ILE   A 1 157 ? 3.778   -12.188 19.393 1    26.207  ? 193 ILE   A CG2 1 
ATOM   1254 C  CD1 . ILE   A 1 157 ? 2.159   -14.137 17.926 1    31.389  ? 193 ILE   A CD1 1 
ATOM   1255 N  N   . LEU   A 1 158 ? 7.122   -14.212 20.518 1    24.139  ? 194 LEU   A N   1 
ATOM   1256 C  CA  . LEU   A 1 158 ? 8.319   -13.506 20.998 1    24.915  ? 194 LEU   A CA  1 
ATOM   1257 C  C   . LEU   A 1 158 ? 9.286   -13.094 19.86  1    31.8    ? 194 LEU   A C   1 
ATOM   1258 O  O   . LEU   A 1 158 ? 10.014  -12.09  19.968 1    34.417  ? 194 LEU   A O   1 
ATOM   1259 C  CB  . LEU   A 1 158 ? 9.022   -14.312 22.1   1    22.826  ? 194 LEU   A CB  1 
ATOM   1260 C  CG  . LEU   A 1 158 ? 10.313  -13.724 22.699 1    24.544  ? 194 LEU   A CG  1 
ATOM   1261 C  CD1 . LEU   A 1 158 ? 10.253  -12.253 23.093 1    23.761  ? 194 LEU   A CD1 1 
ATOM   1262 C  CD2 . LEU   A 1 158 ? 10.997  -14.482 23.885 1    23.513  ? 194 LEU   A CD2 1 
ATOM   1263 N  N   . GLN   A 1 159 ? 9.336   -13.869 18.758 1    35.224  ? 195 GLN   A N   1 
ATOM   1264 C  CA  . GLN   A 1 159 ? 10.384  -13.664 17.745 1    38.715  ? 195 GLN   A CA  1 
ATOM   1265 C  C   . GLN   A 1 159 ? 10.151  -12.39  16.907 1    38.806  ? 195 GLN   A C   1 
ATOM   1266 O  O   . GLN   A 1 159 ? 11.109  -11.834 16.366 1    33.216  ? 195 GLN   A O   1 
ATOM   1267 C  CB  . GLN   A 1 159 ? 10.576  -14.892 16.855 1    33.618  ? 195 GLN   A CB  1 
ATOM   1268 C  CG  . GLN   A 1 159 ? 9.509   -14.997 15.77  1    40.562  ? 195 GLN   A CG  1 
ATOM   1269 C  CD  . GLN   A 1 159 ? 9.44    -16.328 15.043 1    51.345  ? 195 GLN   A CD  1 
ATOM   1270 O  OE1 . GLN   A 1 159 ? 10.251  -16.613 14.145 1    44.518  ? 195 GLN   A OE1 1 
ATOM   1271 N  NE2 . GLN   A 1 159 ? 8.411   -17.12  15.362 1    53.509  ? 195 GLN   A NE2 1 
ATOM   1272 N  N   . PHE   A 1 160 ? 8.893   -11.898 16.851 1    26.967  ? 196 PHE   A N   1 
ATOM   1273 C  CA  . PHE   A 1 160 ? 8.519   -10.753 16.044 1    24.223  ? 196 PHE   A CA  1 
ATOM   1274 C  C   . PHE   A 1 160 ? 8.297   -9.441  16.789 1    22.793  ? 196 PHE   A C   1 
ATOM   1275 O  O   . PHE   A 1 160 ? 8.209   -8.4    16.14  1    26.764  ? 196 PHE   A O   1 
ATOM   1276 C  CB  . PHE   A 1 160 ? 7.091   -11.049 15.585 1    28.984  ? 196 PHE   A CB  1 
ATOM   1277 C  CG  . PHE   A 1 160 ? 6.954   -12.273 14.703 1    33.208  ? 196 PHE   A CG  1 
ATOM   1278 C  CD1 . PHE   A 1 160 ? 7.561   -12.3   13.439 1    36.58   ? 196 PHE   A CD1 1 
ATOM   1279 C  CD2 . PHE   A 1 160 ? 6.19    -13.364 15.121 1    35.49   ? 196 PHE   A CD2 1 
ATOM   1280 C  CE1 . PHE   A 1 160 ? 7.435   -13.429 12.627 1    43.894  ? 196 PHE   A CE1 1 
ATOM   1281 C  CE2 . PHE   A 1 160 ? 6.062   -14.491 14.311 1    46.29   ? 196 PHE   A CE2 1 
ATOM   1282 C  CZ  . PHE   A 1 160 ? 6.661   -14.503 13.05  1    53.799  ? 196 PHE   A CZ  1 
ATOM   1283 N  N   . TYR   A 1 161 ? 8.12    -9.481  18.121 1    23.011  ? 197 TYR   A N   1 
ATOM   1284 C  CA  . TYR   A 1 161 ? 7.722   -8.332  18.913 1    19.318  ? 197 TYR   A CA  1 
ATOM   1285 C  C   . TYR   A 1 161 ? 8.759   -7.212  18.878 1    18.258  ? 197 TYR   A C   1 
ATOM   1286 O  O   . TYR   A 1 161 ? 8.387   -6.089  18.574 1    21.983  ? 197 TYR   A O   1 
ATOM   1287 C  CB  . TYR   A 1 161 ? 7.217   -8.692  20.322 1    21.561  ? 197 TYR   A CB  1 
ATOM   1288 C  CG  . TYR   A 1 161 ? 6.079   -7.759  20.734 1    26.027  ? 197 TYR   A CG  1 
ATOM   1289 C  CD1 . TYR   A 1 161 ? 4.814   -7.887  20.174 1    21.9    ? 197 TYR   A CD1 1 
ATOM   1290 C  CD2 . TYR   A 1 161 ? 6.272   -6.73   21.666 1    26.581  ? 197 TYR   A CD2 1 
ATOM   1291 C  CE1 . TYR   A 1 161 ? 3.791   -7.031  20.56  1    25.333  ? 197 TYR   A CE1 1 
ATOM   1292 C  CE2 . TYR   A 1 161 ? 5.227   -5.938  22.128 1    20.595  ? 197 TYR   A CE2 1 
ATOM   1293 C  CZ  . TYR   A 1 161 ? 3.997   -6.06   21.528 1    21.552  ? 197 TYR   A CZ  1 
ATOM   1294 O  OH  . TYR   A 1 161 ? 2.991   -5.227  21.854 1    17.542  ? 197 TYR   A OH  1 
ATOM   1295 N  N   . PRO   A 1 162 ? 10.054  -7.389  19.218 1    18.932  ? 198 PRO   A N   1 
ATOM   1296 C  CA  . PRO   A 1 162 ? 10.988  -6.259  19.208 1    20.474  ? 198 PRO   A CA  1 
ATOM   1297 C  C   . PRO   A 1 162 ? 10.979  -5.631  17.806 1    23.16   ? 198 PRO   A C   1 
ATOM   1298 O  O   . PRO   A 1 162 ? 11.009  -4.411  17.643 1    27.623  ? 198 PRO   A O   1 
ATOM   1299 C  CB  . PRO   A 1 162 ? 12.403  -6.849  19.539 1    20.944  ? 198 PRO   A CB  1 
ATOM   1300 C  CG  . PRO   A 1 162 ? 12.16   -8.306  19.953 1    19.487  ? 198 PRO   A CG  1 
ATOM   1301 C  CD  . PRO   A 1 162 ? 10.703  -8.656  19.596 1    20.649  ? 198 PRO   A CD  1 
ATOM   1302 N  N   . LYS   A 1 163 ? 10.925  -6.44   16.756 1    24.37   ? 199 LYS   A N   1 
ATOM   1303 C  CA  . LYS   A 1 163 ? 10.921  -5.804  15.424 1    30.681  ? 199 LYS   A CA  1 
ATOM   1304 C  C   . LYS   A 1 163 ? 9.65    -4.975  15.177 1    27.823  ? 199 LYS   A C   1 
ATOM   1305 O  O   . LYS   A 1 163 ? 9.728   -3.841  14.704 1    24.997  ? 199 LYS   A O   1 
ATOM   1306 C  CB  . LYS   A 1 163 ? 11.19   -6.724  14.223 1    27.641  ? 199 LYS   A CB  1 
ATOM   1307 C  CG  . LYS   A 1 163 ? 11.596  -6.031  12.944 1    39.067  ? 199 LYS   A CG  1 
ATOM   1308 C  CD  . LYS   A 1 163 ? 13.029  -5.529  13.149 1    53.818  ? 199 LYS   A CD  1 
ATOM   1309 C  CE  . LYS   A 1 163 ? 13.546  -4.579  12.108 1    63.057  ? 199 LYS   A CE  1 
ATOM   1310 N  NZ  . LYS   A 1 163 ? 15.002  -4.433  12.219 1    58.214  ? 199 LYS   A NZ  1 
ATOM   1311 N  N   . TYR   A 1 164 ? 8.47    -5.531  15.5   1    27.071  ? 200 TYR   A N   1 
ATOM   1312 C  CA  . TYR   A 1 164 ? 7.229   -4.756  15.458 1    23.031  ? 200 TYR   A CA  1 
ATOM   1313 C  C   . TYR   A 1 164 ? 7.331   -3.438  16.236 1    23.824  ? 200 TYR   A C   1 
ATOM   1314 O  O   . TYR   A 1 164 ? 6.978   -2.397  15.697 1    22.617  ? 200 TYR   A O   1 
ATOM   1315 C  CB  . TYR   A 1 164 ? 6.222   -5.639  16.184 1    24.058  ? 200 TYR   A CB  1 
ATOM   1316 C  CG  . TYR   A 1 164 ? 4.996   -4.925  16.749 1    24.726  ? 200 TYR   A CG  1 
ATOM   1317 C  CD1 . TYR   A 1 164 ? 4.011   -4.44   15.904 1    23.511  ? 200 TYR   A CD1 1 
ATOM   1318 C  CD2 . TYR   A 1 164 ? 4.802   -4.805  18.129 1    23.837  ? 200 TYR   A CD2 1 
ATOM   1319 C  CE1 . TYR   A 1 164 ? 2.871   -3.833  16.43  1    28.581  ? 200 TYR   A CE1 1 
ATOM   1320 C  CE2 . TYR   A 1 164 ? 3.674   -4.196  18.668 1    22.571  ? 200 TYR   A CE2 1 
ATOM   1321 C  CZ  . TYR   A 1 164 ? 2.699   -3.725  17.803 1    23.634  ? 200 TYR   A CZ  1 
ATOM   1322 O  OH  . TYR   A 1 164 ? 1.567   -3.145  18.262 1    22.803  ? 200 TYR   A OH  1 
ATOM   1323 N  N   . VAL   A 1 165 ? 7.793   -3.494  17.512 1    23.915  ? 201 VAL   A N   1 
ATOM   1324 C  CA  . VAL   A 1 165 ? 8.004   -2.324  18.347 1    23.544  ? 201 VAL   A CA  1 
ATOM   1325 C  C   . VAL   A 1 165 ? 8.819   -1.262  17.584 1    28.86   ? 201 VAL   A C   1 
ATOM   1326 O  O   . VAL   A 1 165 ? 8.415   -0.123  17.455 1    31.96   ? 201 VAL   A O   1 
ATOM   1327 C  CB  . VAL   A 1 165 ? 8.603   -2.584  19.752 1    19.526  ? 201 VAL   A CB  1 
ATOM   1328 C  CG1 . VAL   A 1 165 ? 8.981   -1.251  20.415 1    18.534  ? 201 VAL   A CG1 1 
ATOM   1329 C  CG2 . VAL   A 1 165 ? 7.634   -3.394  20.606 1    15.97   ? 201 VAL   A CG2 1 
ATOM   1330 N  N   . GLU   A 1 166 ? 9.986   -1.611  17.056 1    31.058  ? 202 GLU   A N   1 
ATOM   1331 C  CA  . GLU   A 1 166 ? 10.791  -0.621  16.347 1    29.722  ? 202 GLU   A CA  1 
ATOM   1332 C  C   . GLU   A 1 166 ? 10.009  -0.042  15.172 1    24.603  ? 202 GLU   A C   1 
ATOM   1333 O  O   . GLU   A 1 166 ? 9.982   1.171   14.988 1    24.346  ? 202 GLU   A O   1 
ATOM   1334 C  CB  . GLU   A 1 166 ? 12.163  -1.255  16.095 1    36.085  ? 202 GLU   A CB  1 
ATOM   1335 C  CG  . GLU   A 1 166 ? 12.82   -0.808  14.801 1    51.892  ? 202 GLU   A CG  1 
ATOM   1336 C  CD  . GLU   A 1 166 ? 14.149  -1.515  14.598 1    61.195  ? 202 GLU   A CD  1 
ATOM   1337 O  OE1 . GLU   A 1 166 ? 15.108  -0.865  14.102 1    63.691  ? 202 GLU   A OE1 1 
ATOM   1338 O  OE2 . GLU   A 1 166 ? 14.216  -2.708  14.974 1    63.12   ? 202 GLU   A OE2 1 
ATOM   1339 N  N   . LEU   A 1 167 ? 9.277   -0.867  14.428 1    23.732  ? 203 LEU   A N   1 
ATOM   1340 C  CA  . LEU   A 1 167 ? 8.599   -0.291  13.27  1    26.957  ? 203 LEU   A CA  1 
ATOM   1341 C  C   . LEU   A 1 167 ? 7.406   0.594   13.639 1    29.027  ? 203 LEU   A C   1 
ATOM   1342 O  O   . LEU   A 1 167 ? 7.206   1.624   12.99  1    30.259  ? 203 LEU   A O   1 
ATOM   1343 C  CB  . LEU   A 1 167 ? 8.259   -1.318  12.197 1    31.142  ? 203 LEU   A CB  1 
ATOM   1344 C  CG  . LEU   A 1 167 ? 9.478   -2.015  11.557 1    32.254  ? 203 LEU   A CG  1 
ATOM   1345 C  CD1 . LEU   A 1 167 ? 8.982   -3.259  10.908 1    28.894  ? 203 LEU   A CD1 1 
ATOM   1346 C  CD2 . LEU   A 1 167 ? 10.132  -1.211  10.477 1    27.053  ? 203 LEU   A CD2 1 
ATOM   1347 N  N   . ILE   A 1 168 ? 6.614   0.213   14.662 1    25.007  ? 204 ILE   A N   1 
ATOM   1348 C  CA  . ILE   A 1 168 ? 5.43    0.992   14.949 1    20.906  ? 204 ILE   A CA  1 
ATOM   1349 C  C   . ILE   A 1 168 ? 5.896   2.289   15.599 1    24.019  ? 204 ILE   A C   1 
ATOM   1350 O  O   . ILE   A 1 168 ? 5.294   3.34    15.38  1    25.826  ? 204 ILE   A O   1 
ATOM   1351 C  CB  . ILE   A 1 168 ? 4.373   0.225   15.775 1    21.988  ? 204 ILE   A CB  1 
ATOM   1352 C  CG1 . ILE   A 1 168 ? 2.99    0.883   15.652 1    21.334  ? 204 ILE   A CG1 1 
ATOM   1353 C  CG2 . ILE   A 1 168 ? 4.775   -0.013  17.239 1    16.165  ? 204 ILE   A CG2 1 
ATOM   1354 C  CD1 . ILE   A 1 168 ? 1.883   0.216   16.476 1    18.076  ? 204 ILE   A CD1 1 
ATOM   1355 N  N   . ASN   A 1 169 ? 7.011   2.231   16.34  1    22.609  ? 205 ASN   A N   1 
ATOM   1356 C  CA  . ASN   A 1 169 ? 7.64    3.435   16.863 1    22.061  ? 205 ASN   A CA  1 
ATOM   1357 C  C   . ASN   A 1 169 ? 8.153   4.311   15.717 1    23.327  ? 205 ASN   A C   1 
ATOM   1358 O  O   . ASN   A 1 169 ? 7.876   5.527   15.662 1    19.522  ? 205 ASN   A O   1 
ATOM   1359 C  CB  . ASN   A 1 169 ? 8.704   3.132   17.91  1    18.55   ? 205 ASN   A CB  1 
ATOM   1360 C  CG  . ASN   A 1 169 ? 8.073   2.847   19.271 1    20.332  ? 205 ASN   A CG  1 
ATOM   1361 O  OD1 . ASN   A 1 169 ? 6.863   3.011   19.524 1    16.335  ? 205 ASN   A OD1 1 
ATOM   1362 N  ND2 . ASN   A 1 169 ? 8.935   2.598   20.232 1    16.419  ? 205 ASN   A ND2 1 
ATOM   1363 N  N   . GLN   A 1 170 ? 8.821   3.686   14.736 1    24.419  ? 206 GLN   A N   1 
ATOM   1364 C  CA  . GLN   A 1 170 ? 9.363   4.525   13.672 1    24.461  ? 206 GLN   A CA  1 
ATOM   1365 C  C   . GLN   A 1 170 ? 8.23    5.274   12.999 1    22.263  ? 206 GLN   A C   1 
ATOM   1366 O  O   . GLN   A 1 170 ? 8.34    6.464   12.737 1    24.39   ? 206 GLN   A O   1 
ATOM   1367 C  CB  . GLN   A 1 170 ? 10.026  3.79    12.531 1    25.968  ? 206 GLN   A CB  1 
ATOM   1368 C  CG  . GLN   A 1 170 ? 11.048  4.599   11.755 1    31.507  ? 206 GLN   A CG  1 
ATOM   1369 C  CD  . GLN   A 1 170 ? 11.679  3.645   10.763 1    45.344  ? 206 GLN   A CD  1 
ATOM   1370 O  OE1 . GLN   A 1 170 ? 11.841  2.458   11.075 1    56.734  ? 206 GLN   A OE1 1 
ATOM   1371 N  NE2 . GLN   A 1 170 ? 11.908  4.085   9.532  1    43.433  ? 206 GLN   A NE2 1 
ATOM   1372 N  N   . ALA   A 1 171 ? 7.137   4.58    12.734 1    20.215  ? 207 ALA   A N   1 
ATOM   1373 C  CA  . ALA   A 1 171 ? 6.076   5.256   12.017 1    22.453  ? 207 ALA   A CA  1 
ATOM   1374 C  C   . ALA   A 1 171 ? 5.484   6.409   12.853 1    26.724  ? 207 ALA   A C   1 
ATOM   1375 O  O   . ALA   A 1 171 ? 5.091   7.43    12.263 1    22.664  ? 207 ALA   A O   1 
ATOM   1376 C  CB  . ALA   A 1 171 ? 5.007   4.26    11.582 1    22.522  ? 207 ALA   A CB  1 
ATOM   1377 N  N   . ALA   A 1 172 ? 5.36    6.236   14.2   1    22.431  ? 208 ALA   A N   1 
ATOM   1378 C  CA  . ALA   A 1 172 ? 4.78    7.262   15.052 1    20.721  ? 208 ALA   A CA  1 
ATOM   1379 C  C   . ALA   A 1 172 ? 5.694   8.499   15.039 1    27.318  ? 208 ALA   A C   1 
ATOM   1380 O  O   . ALA   A 1 172 ? 5.206   9.654   14.991 1    33.998  ? 208 ALA   A O   1 
ATOM   1381 C  CB  . ALA   A 1 172 ? 4.571   6.746   16.494 1    18.35   ? 208 ALA   A CB  1 
ATOM   1382 N  N   . ARG   A 1 173 ? 7.02    8.254   15.095 1    25.011  ? 209 ARG   A N   1 
ATOM   1383 C  CA  . ARG   A 1 173 ? 8.009   9.337   15.074 1    26.664  ? 209 ARG   A CA  1 
ATOM   1384 C  C   . ARG   A 1 173 ? 7.831   10.149  13.789 1    26.216  ? 209 ARG   A C   1 
ATOM   1385 O  O   . ARG   A 1 173 ? 7.703   11.368  13.844 1    28.02   ? 209 ARG   A O   1 
ATOM   1386 C  CB  . ARG   A 1 173 ? 9.462   8.909   15.398 1    22.165  ? 209 ARG   A CB  1 
ATOM   1387 C  CG  . ARG   A 1 173 ? 9.599   8.514   16.87  1    25.397  ? 209 ARG   A CG  1 
ATOM   1388 C  CD  . ARG   A 1 173 ? 11.024  8.174   17.381 1    24.978  ? 209 ARG   A CD  1 
ATOM   1389 N  NE  . ARG   A 1 173 ? 11.8    7.596   16.284 1    28.282  ? 209 ARG   A NE  1 
ATOM   1390 C  CZ  . ARG   A 1 173 ? 11.957  6.278   16.121 1    31.617  ? 209 ARG   A CZ  1 
ATOM   1391 N  NH1 . ARG   A 1 173 ? 11.527  5.476   17.088 1    25.466  ? 209 ARG   A NH1 1 
ATOM   1392 N  NH2 . ARG   A 1 173 ? 12.559  5.781   15.03  1    27.858  ? 209 ARG   A NH2 1 
ATOM   1393 N  N   . LEU   A 1 174 ? 7.701   9.463   12.655 1    23.213  ? 210 LEU   A N   1 
ATOM   1394 C  CA  . LEU   A 1 174 ? 7.602   10.149  11.367 1    27.352  ? 210 LEU   A CA  1 
ATOM   1395 C  C   . LEU   A 1 174 ? 6.23    10.78   11.205 1    25.509  ? 210 LEU   A C   1 
ATOM   1396 O  O   . LEU   A 1 174 ? 6.032   11.506  10.252 1    23.305  ? 210 LEU   A O   1 
ATOM   1397 C  CB  . LEU   A 1 174 ? 7.82    9.179   10.202 1    29.584  ? 210 LEU   A CB  1 
ATOM   1398 C  CG  . LEU   A 1 174 ? 9.233   8.584   10.08  1    31.633  ? 210 LEU   A CG  1 
ATOM   1399 C  CD1 . LEU   A 1 174 ? 9.165   7.286   9.284  1    29.551  ? 210 LEU   A CD1 1 
ATOM   1400 C  CD2 . LEU   A 1 174 ? 10.075  9.625   9.315  1    35.219  ? 210 LEU   A CD2 1 
ATOM   1401 N  N   . ASN   A 1 175 ? 5.277   10.462  12.087 1    22.483  ? 211 ASN   A N   1 
ATOM   1402 C  CA  . ASN   A 1 175 ? 4.041   11.246  12.076 1    28.963  ? 211 ASN   A CA  1 
ATOM   1403 C  C   . ASN   A 1 175 ? 4.047   12.348  13.131 1    24.515  ? 211 ASN   A C   1 
ATOM   1404 O  O   . ASN   A 1 175 ? 3.036   12.957  13.351 1    29.934  ? 211 ASN   A O   1 
ATOM   1405 C  CB  . ASN   A 1 175 ? 2.779   10.385  12.129 1    30.534  ? 211 ASN   A CB  1 
ATOM   1406 C  CG  . ASN   A 1 175 ? 2.606   9.578   10.864 1    36.037  ? 211 ASN   A CG  1 
ATOM   1407 O  OD1 . ASN   A 1 175 ? 2.074   10.065  9.848  1    37.537  ? 211 ASN   A OD1 1 
ATOM   1408 N  ND2 . ASN   A 1 175 ? 3.017   8.325   10.924 1    36.581  ? 211 ASN   A ND2 1 
ATOM   1409 N  N   . GLY   A 1 176 ? 5.143   12.539  13.852 1    23.74   ? 212 GLY   A N   1 
ATOM   1410 C  CA  . GLY   A 1 176 ? 5.233   13.631  14.792 1    21.062  ? 212 GLY   A CA  1 
ATOM   1411 C  C   . GLY   A 1 176 ? 4.937   13.275  16.259 1    23.358  ? 212 GLY   A C   1 
ATOM   1412 O  O   . GLY   A 1 176 ? 4.88    14.179  17.124 1    25.315  ? 212 GLY   A O   1 
ATOM   1413 N  N   . TYR   A 1 177 ? 4.729   11.998  16.569 1    20.359  ? 213 TYR   A N   1 
ATOM   1414 C  CA  . TYR   A 1 177 ? 4.591   11.639  17.986 1    24.555  ? 213 TYR   A CA  1 
ATOM   1415 C  C   . TYR   A 1 177 ? 5.97    11.191  18.505 1    26.844  ? 213 TYR   A C   1 
ATOM   1416 O  O   . TYR   A 1 177 ? 6.889   11.005  17.69  1    29.849  ? 213 TYR   A O   1 
ATOM   1417 C  CB  . TYR   A 1 177 ? 3.566   10.492  18.151 1    18.954  ? 213 TYR   A CB  1 
ATOM   1418 C  CG  . TYR   A 1 177 ? 2.159   10.881  17.735 1    19.679  ? 213 TYR   A CG  1 
ATOM   1419 C  CD1 . TYR   A 1 177 ? 1.284   11.502  18.624 1    22.836  ? 213 TYR   A CD1 1 
ATOM   1420 C  CD2 . TYR   A 1 177 ? 1.711   10.688  16.434 1    19.111  ? 213 TYR   A CD2 1 
ATOM   1421 C  CE1 . TYR   A 1 177 ? 0.029   11.969  18.233 1    21.842  ? 213 TYR   A CE1 1 
ATOM   1422 C  CE2 . TYR   A 1 177 ? 0.419   11.043  16.057 1    23.179  ? 213 TYR   A CE2 1 
ATOM   1423 C  CZ  . TYR   A 1 177 ? -0.421  11.709  16.952 1    23.929  ? 213 TYR   A CZ  1 
ATOM   1424 O  OH  . TYR   A 1 177 ? -1.687  12.068  16.576 1    25.601  ? 213 TYR   A OH  1 
ATOM   1425 N  N   . VAL   A 1 178 ? 6.08    10.88   19.815 1    24.986  ? 214 VAL   A N   1 
ATOM   1426 C  CA  . VAL   A 1 178 ? 7.366   10.469  20.379 1    26.414  ? 214 VAL   A CA  1 
ATOM   1427 C  C   . VAL   A 1 178 ? 7.583   8.96    20.281 1    25.62   ? 214 VAL   A C   1 
ATOM   1428 O  O   . VAL   A 1 178 ? 8.732   8.472   20.122 1    27.613  ? 214 VAL   A O   1 
ATOM   1429 C  CB  . VAL   A 1 178 ? 7.721   11.067  21.762 1    29.562  ? 214 VAL   A CB  1 
ATOM   1430 C  CG1 . VAL   A 1 178 ? 7.953   12.568  21.647 1    29.939  ? 214 VAL   A CG1 1 
ATOM   1431 C  CG2 . VAL   A 1 178 ? 6.633   10.874  22.777 1    27.247  ? 214 VAL   A CG2 1 
ATOM   1432 N  N   . ASP   A 1 179 ? 6.47    8.222   20.399 1    21.718  ? 215 ASP   A N   1 
ATOM   1433 C  CA  . ASP   A 1 179 ? 6.466   6.782   20.214 1    17.627  ? 215 ASP   A CA  1 
ATOM   1434 C  C   . ASP   A 1 179 ? 5.015   6.338   19.975 1    18.657  ? 215 ASP   A C   1 
ATOM   1435 O  O   . ASP   A 1 179 ? 4.101   7.149   19.966 1    17.329  ? 215 ASP   A O   1 
ATOM   1436 C  CB  . ASP   A 1 179 ? 7.038   6.146   21.451 1    16.642  ? 215 ASP   A CB  1 
ATOM   1437 C  CG  . ASP   A 1 179 ? 6.193   6.409   22.691 1    21.604  ? 215 ASP   A CG  1 
ATOM   1438 O  OD1 . ASP   A 1 179 ? 4.982   5.971   22.733 1    20.801  ? 215 ASP   A OD1 1 
ATOM   1439 O  OD2 . ASP   A 1 179 ? 6.745   7.022   23.62  1    23.126  ? 215 ASP   A OD2 1 
ATOM   1440 N  N   . ALA   A 1 180 ? 4.781   5.028   19.879 1    17.505  ? 216 ALA   A N   1 
ATOM   1441 C  CA  . ALA   A 1 180 ? 3.532   4.55    19.343 1    18.263  ? 216 ALA   A CA  1 
ATOM   1442 C  C   . ALA   A 1 180 ? 2.45    4.671   20.408 1    22.073  ? 216 ALA   A C   1 
ATOM   1443 O  O   . ALA   A 1 180 ? 1.292   4.85    20.047 1    26.557  ? 216 ALA   A O   1 
ATOM   1444 C  CB  . ALA   A 1 180 ? 3.722   3.151   18.89  1    17.469  ? 216 ALA   A CB  1 
ATOM   1445 N  N   . GLY   A 1 181 ? 2.849   4.641   21.7   1    23.698  ? 217 GLY   A N   1 
ATOM   1446 C  CA  . GLY   A 1 181 ? 1.931   4.752   22.83  1    20.571  ? 217 GLY   A CA  1 
ATOM   1447 C  C   . GLY   A 1 181 ? 1.411   6.178   22.953 1    21.149  ? 217 GLY   A C   1 
ATOM   1448 O  O   . GLY   A 1 181 ? 0.226   6.423   23.249 1    26.078  ? 217 GLY   A O   1 
ATOM   1449 N  N   . ASP   A 1 182 ? 2.322   7.125   22.725 1    20.516  ? 218 ASP   A N   1 
ATOM   1450 C  CA  . ASP   A 1 182 ? 1.941   8.534   22.592 1    22.02   ? 218 ASP   A CA  1 
ATOM   1451 C  C   . ASP   A 1 182 ? 0.891   8.695   21.469 1    22.557  ? 218 ASP   A C   1 
ATOM   1452 O  O   . ASP   A 1 182 ? -0.148  9.316   21.679 1    26.175  ? 218 ASP   A O   1 
ATOM   1453 C  CB  . ASP   A 1 182 ? 3.177   9.415   22.507 1    22.563  ? 218 ASP   A CB  1 
ATOM   1454 C  CG  . ASP   A 1 182 ? 2.932   10.87   22.155 1    27.342  ? 218 ASP   A CG  1 
ATOM   1455 O  OD1 . ASP   A 1 182 ? 1.935   11.391  22.655 1    25.256  ? 218 ASP   A OD1 1 
ATOM   1456 O  OD2 . ASP   A 1 182 ? 3.75    11.466  21.408 1    30.427  ? 218 ASP   A OD2 1 
ATOM   1457 N  N   A SER   A 1 183 ? 1.165   8.094   20.301 0.52 21.468  ? 219 SER   A N   1 
ATOM   1458 N  N   B SER   A 1 183 ? 1.117   8.084   20.295 0.48 21.659  ? 219 SER   A N   1 
ATOM   1459 C  CA  A SER   A 1 183 ? 0.233   8.108   19.183 0.52 21.952  ? 219 SER   A CA  1 
ATOM   1460 C  CA  B SER   A 1 183 ? 0.158   8.186   19.199 0.48 21.868  ? 219 SER   A CA  1 
ATOM   1461 C  C   A SER   A 1 183 ? -1.144  7.588   19.601 0.52 22.868  ? 219 SER   A C   1 
ATOM   1462 C  C   B SER   A 1 183 ? -1.193  7.568   19.57  0.48 22.747  ? 219 SER   A C   1 
ATOM   1463 O  O   A SER   A 1 183 ? -2.161  8.208   19.28  0.52 22.023  ? 219 SER   A O   1 
ATOM   1464 O  O   B SER   A 1 183 ? -2.245  8.079   19.174 0.48 21.215  ? 219 SER   A O   1 
ATOM   1465 C  CB  A SER   A 1 183 ? 0.782   7.334   17.995 0.52 18.501  ? 219 SER   A CB  1 
ATOM   1466 C  CB  B SER   A 1 183 ? 0.698   7.559   17.928 0.48 19.15   ? 219 SER   A CB  1 
ATOM   1467 O  OG  A SER   A 1 183 ? -0.202  7.277   16.976 0.52 19.57   ? 219 SER   A OG  1 
ATOM   1468 O  OG  B SER   A 1 183 ? 0.55    6.153   17.991 0.48 19.955  ? 219 SER   A OG  1 
ATOM   1469 N  N   . TRP   A 1 184 ? -1.173  6.431   20.287 1    23.489  ? 220 TRP   A N   1 
ATOM   1470 C  CA  . TRP   A 1 184 ? -2.44   5.799   20.715 1    29.428  ? 220 TRP   A CA  1 
ATOM   1471 C  C   . TRP   A 1 184 ? -3.199  6.683   21.704 1    27.395  ? 220 TRP   A C   1 
ATOM   1472 O  O   . TRP   A 1 184 ? -4.42   6.844   21.584 1    30.24   ? 220 TRP   A O   1 
ATOM   1473 C  CB  . TRP   A 1 184 ? -2.232  4.389   21.316 1    29.025  ? 220 TRP   A CB  1 
ATOM   1474 C  CG  . TRP   A 1 184 ? -1.822  3.344   20.315 1    25.293  ? 220 TRP   A CG  1 
ATOM   1475 C  CD1 . TRP   A 1 184 ? -1.581  3.502   18.979 1    24.222  ? 220 TRP   A CD1 1 
ATOM   1476 C  CD2 . TRP   A 1 184 ? -1.561  1.968   20.599 1    24.007  ? 220 TRP   A CD2 1 
ATOM   1477 N  NE1 . TRP   A 1 184 ? -1.225  2.309   18.409 1    22.728  ? 220 TRP   A NE1 1 
ATOM   1478 C  CE2 . TRP   A 1 184 ? -1.203  1.356   19.378 1    21.472  ? 220 TRP   A CE2 1 
ATOM   1479 C  CE3 . TRP   A 1 184 ? -1.614  1.194   21.762 1    25.998  ? 220 TRP   A CE3 1 
ATOM   1480 C  CZ2 . TRP   A 1 184 ? -0.91   0.003   19.281 1    21.311  ? 220 TRP   A CZ2 1 
ATOM   1481 C  CZ3 . TRP   A 1 184 ? -1.392  -0.165  21.648 1    24.241  ? 220 TRP   A CZ3 1 
ATOM   1482 C  CH2 . TRP   A 1 184 ? -1.006  -0.74   20.431 1    21.579  ? 220 TRP   A CH2 1 
ATOM   1483 N  N   . ARG   A 1 185 ? -2.462  7.231   22.693 1    27.339  ? 221 ARG   A N   1 
ATOM   1484 C  CA  . ARG   A 1 185 ? -3.096  8.013   23.758 1    29.104  ? 221 ARG   A CA  1 
ATOM   1485 C  C   . ARG   A 1 185 ? -3.788  9.234   23.147 1    32.98   ? 221 ARG   A C   1 
ATOM   1486 O  O   . ARG   A 1 185 ? -4.796  9.69    23.687 1    26.97   ? 221 ARG   A O   1 
ATOM   1487 C  CB  . ARG   A 1 185 ? -2.218  8.439   24.933 1    22.466  ? 221 ARG   A CB  1 
ATOM   1488 C  CG  . ARG   A 1 185 ? -1.768  7.211   25.707 1    25.159  ? 221 ARG   A CG  1 
ATOM   1489 C  CD  . ARG   A 1 185 ? -0.876  7.564   26.908 1    23.57   ? 221 ARG   A CD  1 
ATOM   1490 N  NE  . ARG   A 1 185 ? 0.313   8.289   26.454 1    19.972  ? 221 ARG   A NE  1 
ATOM   1491 C  CZ  . ARG   A 1 185 ? 1.527   7.793   26.221 1    21.506  ? 221 ARG   A CZ  1 
ATOM   1492 N  NH1 . ARG   A 1 185 ? 2.547   8.623   25.973 1    17.461  ? 221 ARG   A NH1 1 
ATOM   1493 N  NH2 . ARG   A 1 185 ? 1.738   6.471   26.239 1    22.893  ? 221 ARG   A NH2 1 
ATOM   1494 N  N   . SER   A 1 186 ? -3.288  9.679   21.977 1    28.975  ? 222 SER   A N   1 
ATOM   1495 C  CA  . SER   A 1 186 ? -3.75   10.94   21.419 1    30.114  ? 222 SER   A CA  1 
ATOM   1496 C  C   . SER   A 1 186 ? -5.125  10.761  20.763 1    24.544  ? 222 SER   A C   1 
ATOM   1497 O  O   . SER   A 1 186 ? -5.812  11.715  20.487 1    26.041  ? 222 SER   A O   1 
ATOM   1498 C  CB  . SER   A 1 186 ? -2.73   11.608  20.508 1    32.815  ? 222 SER   A CB  1 
ATOM   1499 O  OG  . SER   A 1 186 ? -2.841  11.019  19.222 1    35.713  ? 222 SER   A OG  1 
ATOM   1500 N  N   . MET   A 1 187 ? -5.584  9.536   20.588 1    24.275  ? 223 MET   A N   1 
ATOM   1501 C  CA  . MET   A 1 187 ? -6.9    9.369   20.006 1    23.264  ? 223 MET   A CA  1 
ATOM   1502 C  C   . MET   A 1 187 ? -7.963  9.895   20.988 1    25.342  ? 223 MET   A C   1 
ATOM   1503 O  O   . MET   A 1 187 ? -9.086  10.103  20.577 1    28.035  ? 223 MET   A O   1 
ATOM   1504 C  CB  . MET   A 1 187 ? -7.195  7.886   19.715 1    30.129  ? 223 MET   A CB  1 
ATOM   1505 C  CG  . MET   A 1 187 ? -6.345  7.208   18.631 1    34.334  ? 223 MET   A CG  1 
ATOM   1506 S  SD  . MET   A 1 187 ? -6.619  5.415   18.51  1    40.653  ? 223 MET   A SD  1 
ATOM   1507 C  CE  . MET   A 1 187 ? -6.104  4.732   20.083 1    40.382  ? 223 MET   A CE  1 
ATOM   1508 N  N   . TYR   A 1 188 ? -7.648  10.167  22.262 1    22.485  ? 224 TYR   A N   1 
ATOM   1509 C  CA  . TYR   A 1 188 ? -8.675  10.709  23.145 1    20.673  ? 224 TYR   A CA  1 
ATOM   1510 C  C   . TYR   A 1 188 ? -8.582  12.234  23.259 1    23.699  ? 224 TYR   A C   1 
ATOM   1511 O  O   . TYR   A 1 188 ? -9.388  12.826  23.975 1    18.876  ? 224 TYR   A O   1 
ATOM   1512 C  CB  . TYR   A 1 188 ? -8.336  10.275  24.572 1    21.467  ? 224 TYR   A CB  1 
ATOM   1513 C  CG  . TYR   A 1 188 ? -8.648  8.806   24.705 1    23.668  ? 224 TYR   A CG  1 
ATOM   1514 C  CD1 . TYR   A 1 188 ? -7.695  7.856   24.352 1    19.787  ? 224 TYR   A CD1 1 
ATOM   1515 C  CD2 . TYR   A 1 188 ? -9.937  8.378   25.114 1    22.68   ? 224 TYR   A CD2 1 
ATOM   1516 C  CE1 . TYR   A 1 188 ? -8.027  6.508   24.367 1    21.719  ? 224 TYR   A CE1 1 
ATOM   1517 C  CE2 . TYR   A 1 188 ? -10.252 7.023   25.17  1    20.504  ? 224 TYR   A CE2 1 
ATOM   1518 C  CZ  . TYR   A 1 188 ? -9.305  6.092   24.76  1    22.436  ? 224 TYR   A CZ  1 
ATOM   1519 O  OH  . TYR   A 1 188 ? -9.598  4.747   24.747 1    25.158  ? 224 TYR   A OH  1 
ATOM   1520 N  N   . GLU   A 1 189 ? -7.553  12.88   22.655 1    27.025  ? 225 GLU   A N   1 
ATOM   1521 C  CA  . GLU   A 1 189 ? -7.372  14.341  22.734 1    26.813  ? 225 GLU   A CA  1 
ATOM   1522 C  C   . GLU   A 1 189 ? -7.547  14.883  24.16  1    24.921  ? 225 GLU   A C   1 
ATOM   1523 O  O   . GLU   A 1 189 ? -8.264  15.838  24.43  1    26.54   ? 225 GLU   A O   1 
ATOM   1524 C  CB  . GLU   A 1 189 ? -8.314  15.106  21.807 1    25.13   ? 225 GLU   A CB  1 
ATOM   1525 C  CG  . GLU   A 1 189 ? -8.234  14.569  20.392 1    33.951  ? 225 GLU   A CG  1 
ATOM   1526 C  CD  . GLU   A 1 189 ? -9.206  15.195  19.388 1    42.002  ? 225 GLU   A CD  1 
ATOM   1527 O  OE1 . GLU   A 1 189 ? -10.457 15.286  19.597 1    38.422  ? 225 GLU   A OE1 1 
ATOM   1528 O  OE2 . GLU   A 1 189 ? -8.654  15.561  18.322 1    44.967  ? 225 GLU   A OE2 1 
ATOM   1529 N  N   . THR   A 1 190 ? -6.88   14.253  25.107 1    23.563  ? 226 THR   A N   1 
ATOM   1530 C  CA  . THR   A 1 190 ? -7.155  14.532  26.5   1    23.754  ? 226 THR   A CA  1 
ATOM   1531 C  C   . THR   A 1 190 ? -5.828  14.463  27.247 1    21.717  ? 226 THR   A C   1 
ATOM   1532 O  O   . THR   A 1 190 ? -5.449  13.402  27.736 1    26.239  ? 226 THR   A O   1 
ATOM   1533 C  CB  . THR   A 1 190 ? -8.143  13.51   27.05  1    24.936  ? 226 THR   A CB  1 
ATOM   1534 O  OG1 . THR   A 1 190 ? -9.408  13.637  26.403 1    30.127  ? 226 THR   A OG1 1 
ATOM   1535 C  CG2 . THR   A 1 190 ? -8.247  13.683  28.548 1    23.978  ? 226 THR   A CG2 1 
ATOM   1536 N  N   . PRO   A 1 191 ? -5.072  15.58   27.305 1    24.66   ? 227 PRO   A N   1 
ATOM   1537 C  CA  . PRO   A 1 191 ? -3.721  15.603  27.892 1    26.338  ? 227 PRO   A CA  1 
ATOM   1538 C  C   . PRO   A 1 191 ? -3.644  15.05   29.31  1    25.358  ? 227 PRO   A C   1 
ATOM   1539 O  O   . PRO   A 1 191 ? -2.624  14.463  29.654 1    26.911  ? 227 PRO   A O   1 
ATOM   1540 C  CB  . PRO   A 1 191 ? -3.418  17.099  27.911 1    25.731  ? 227 PRO   A CB  1 
ATOM   1541 C  CG  . PRO   A 1 191 ? -4.136  17.582  26.659 1    28.071  ? 227 PRO   A CG  1 
ATOM   1542 C  CD  . PRO   A 1 191 ? -5.501  16.902  26.794 1    26.381  ? 227 PRO   A CD  1 
ATOM   1543 N  N   . SER   A 1 192 ? -4.739  15.168  30.08  1    22.562  ? 228 SER   A N   1 
ATOM   1544 C  CA  . SER   A 1 192 ? -4.741  14.697  31.465 1    25.627  ? 228 SER   A CA  1 
ATOM   1545 C  C   . SER   A 1 192 ? -5.183  13.228  31.559 1    26.357  ? 228 SER   A C   1 
ATOM   1546 O  O   . SER   A 1 192 ? -5.554  12.751  32.64  1    32.206  ? 228 SER   A O   1 
ATOM   1547 C  CB  . SER   A 1 192 ? -5.58   15.631  32.344 1    23.458  ? 228 SER   A CB  1 
ATOM   1548 O  OG  . SER   A 1 192 ? -6.93   15.609  31.875 1    27.432  ? 228 SER   A OG  1 
ATOM   1549 N  N   . LEU   A 1 193 ? -5.156  12.49   30.44  1    25.565  ? 229 LEU   A N   1 
ATOM   1550 C  CA  . LEU   A 1 193 ? -5.69   11.12   30.386 1    28.113  ? 229 LEU   A CA  1 
ATOM   1551 C  C   . LEU   A 1 193 ? -5.057  10.145  31.404 1    25.739  ? 229 LEU   A C   1 
ATOM   1552 O  O   . LEU   A 1 193 ? -5.746  9.437   32.126 1    25.337  ? 229 LEU   A O   1 
ATOM   1553 C  CB  . LEU   A 1 193 ? -5.487  10.628  28.954 1    26.059  ? 229 LEU   A CB  1 
ATOM   1554 C  CG  . LEU   A 1 193 ? -5.919  9.187   28.675 1    25.806  ? 229 LEU   A CG  1 
ATOM   1555 C  CD1 . LEU   A 1 193 ? -7.423  9.125   28.85  1    26.194  ? 229 LEU   A CD1 1 
ATOM   1556 C  CD2 . LEU   A 1 193 ? -5.488  8.679   27.273 1    21.723  ? 229 LEU   A CD2 1 
ATOM   1557 N  N   . GLU   A 1 194 ? -3.732  10.038  31.445 1    25.379  ? 230 GLU   A N   1 
ATOM   1558 C  CA  . GLU   A 1 194 ? -3.108  9.093   32.354 1    27.96   ? 230 GLU   A CA  1 
ATOM   1559 C  C   . GLU   A 1 194 ? -3.576  9.32    33.8   1    25.47   ? 230 GLU   A C   1 
ATOM   1560 O  O   . GLU   A 1 194 ? -3.872  8.373   34.493 1    31.472  ? 230 GLU   A O   1 
ATOM   1561 C  CB  . GLU   A 1 194 ? -1.578  9.048   32.238 1    26.024  ? 230 GLU   A CB  1 
ATOM   1562 C  CG  . GLU   A 1 194 ? -1.128  8.409   30.922 1    27.748  ? 230 GLU   A CG  1 
ATOM   1563 C  CD  . GLU   A 1 194 ? 0.357   8.207   30.71  1    29.25   ? 230 GLU   A CD  1 
ATOM   1564 O  OE1 . GLU   A 1 194 ? 1.104   8.278   31.721 1    31.217  ? 230 GLU   A OE1 1 
ATOM   1565 O  OE2 . GLU   A 1 194 ? 0.787   8.086   29.528 1    32.505  ? 230 GLU   A OE2 1 
ATOM   1566 N  N   . GLN   A 1 195 ? -3.663  10.553  34.255 1    24.752  ? 231 GLN   A N   1 
ATOM   1567 C  CA  . GLN   A 1 195 ? -4.072  10.807  35.624 1    30.356  ? 231 GLN   A CA  1 
ATOM   1568 C  C   . GLN   A 1 195 ? -5.564  10.565  35.728 1    30.716  ? 231 GLN   A C   1 
ATOM   1569 O  O   . GLN   A 1 195 ? -6.015  10.125  36.772 1    31.131  ? 231 GLN   A O   1 
ATOM   1570 C  CB  . GLN   A 1 195 ? -3.819  12.239  36.086 1    34.642  ? 231 GLN   A CB  1 
ATOM   1571 C  CG  . GLN   A 1 195 ? -2.386  12.704  35.815 1    58.211  ? 231 GLN   A CG  1 
ATOM   1572 C  CD  . GLN   A 1 195 ? -2.283  14.199  35.553 1    87.065  ? 231 GLN   A CD  1 
ATOM   1573 O  OE1 . GLN   A 1 195 ? -2.998  14.779  34.721 1    101.119 ? 231 GLN   A OE1 1 
ATOM   1574 N  NE2 . GLN   A 1 195 ? -1.386  14.858  36.272 1    89.167  ? 231 GLN   A NE2 1 
ATOM   1575 N  N   . ASP   A 1 196 ? -6.319  10.866  34.662 1    26.199  ? 232 ASP   A N   1 
ATOM   1576 C  CA  . ASP   A 1 196 ? -7.751  10.658  34.757 1    28.081  ? 232 ASP   A CA  1 
ATOM   1577 C  C   . ASP   A 1 196 ? -8.007  9.171   35.009 1    26.126  ? 232 ASP   A C   1 
ATOM   1578 O  O   . ASP   A 1 196 ? -8.774  8.825   35.887 1    30.771  ? 232 ASP   A O   1 
ATOM   1579 C  CB  . ASP   A 1 196 ? -8.509  11.264  33.581 1    29.663  ? 232 ASP   A CB  1 
ATOM   1580 C  CG  . ASP   A 1 196 ? -8.554  12.793  33.515 1    40.27   ? 232 ASP   A CG  1 
ATOM   1581 O  OD1 . ASP   A 1 196 ? -8.309  13.41   34.577 1    34.825  ? 232 ASP   A OD1 1 
ATOM   1582 O  OD2 . ASP   A 1 196 ? -8.752  13.362  32.373 1    41.069  ? 232 ASP   A OD2 1 
ATOM   1583 N  N   . LEU   A 1 197 ? -7.36   8.304   34.224 1    26.126  ? 233 LEU   A N   1 
ATOM   1584 C  CA  . LEU   A 1 197 ? -7.584  6.881   34.302 1    22.564  ? 233 LEU   A CA  1 
ATOM   1585 C  C   . LEU   A 1 197 ? -7.119  6.414   35.674 1    26.602  ? 233 LEU   A C   1 
ATOM   1586 O  O   . LEU   A 1 197 ? -7.903  5.761   36.333 1    27.613  ? 233 LEU   A O   1 
ATOM   1587 C  CB  . LEU   A 1 197 ? -6.868  6.174   33.162 1    18.931  ? 233 LEU   A CB  1 
ATOM   1588 C  CG  . LEU   A 1 197 ? -7.35   6.631   31.791 1    21.675  ? 233 LEU   A CG  1 
ATOM   1589 C  CD1 . LEU   A 1 197 ? -6.849  5.953   30.59  1    23.243  ? 233 LEU   A CD1 1 
ATOM   1590 C  CD2 . LEU   A 1 197 ? -8.827  6.913   31.669 1    25.514  ? 233 LEU   A CD2 1 
ATOM   1591 N  N   . GLU   A 1 198 ? -5.908  6.822   36.129 1    26.829  ? 234 GLU   A N   1 
ATOM   1592 C  CA  . GLU   A 1 198 ? -5.363  6.508   37.454 1    28.112  ? 234 GLU   A CA  1 
ATOM   1593 C  C   . GLU   A 1 198 ? -6.384  6.836   38.557 1    32.083  ? 234 GLU   A C   1 
ATOM   1594 O  O   . GLU   A 1 198 ? -6.678  6.006   39.428 1    26.99   ? 234 GLU   A O   1 
ATOM   1595 C  CB  . GLU   A 1 198 ? -3.949  7.085   37.579 1    31.287  ? 234 GLU   A CB  1 
ATOM   1596 C  CG  . GLU   A 1 198 ? -3.124  6.765   38.827 1    47.725  ? 234 GLU   A CG  1 
ATOM   1597 C  CD  . GLU   A 1 198 ? -3.267  5.395   39.493 1    77.645  ? 234 GLU   A CD  1 
ATOM   1598 O  OE1 . GLU   A 1 198 ? -2.945  4.294   38.95  1    64.881  ? 234 GLU   A OE1 1 
ATOM   1599 O  OE2 . GLU   A 1 198 ? -3.76   5.46    40.647 1    100.989 ? 234 GLU   A OE2 1 
ATOM   1600 N  N   . ARG   A 1 199 ? -7.02   8.011   38.454 1    32.754  ? 235 ARG   A N   1 
ATOM   1601 C  CA  . ARG   A 1 199 ? -7.978  8.436   39.463 1    35.694  ? 235 ARG   A CA  1 
ATOM   1602 C  C   . ARG   A 1 199 ? -9.152  7.469   39.442 1    38.044  ? 235 ARG   A C   1 
ATOM   1603 O  O   . ARG   A 1 199 ? -9.638  7.1     40.515 1    36.627  ? 235 ARG   A O   1 
ATOM   1604 C  CB  . ARG   A 1 199 ? -8.493  9.844   39.185 1    40.387  ? 235 ARG   A CB  1 
ATOM   1605 C  CG  . ARG   A 1 199 ? -8.323  10.651  40.46  1    54.029  ? 235 ARG   A CG  1 
ATOM   1606 C  CD  . ARG   A 1 199 ? -8.696  12.124  40.217 1    61.116  ? 235 ARG   A CD  1 
ATOM   1607 N  NE  . ARG   A 1 199 ? -7.552  12.838  39.64  1    68.89   ? 235 ARG   A NE  1 
ATOM   1608 C  CZ  . ARG   A 1 199 ? -7.539  13.282  38.382 1    75.806  ? 235 ARG   A CZ  1 
ATOM   1609 N  NH1 . ARG   A 1 199 ? -8.687  13.32   37.71  1    60.424  ? 235 ARG   A NH1 1 
ATOM   1610 N  NH2 . ARG   A 1 199 ? -6.391  13.671  37.819 1    69.273  ? 235 ARG   A NH2 1 
ATOM   1611 N  N   . LEU   A 1 200 ? -9.571  7.082   38.212 1    29.456  ? 236 LEU   A N   1 
ATOM   1612 C  CA  . LEU   A 1 200 ? -10.735 6.234   37.991 1    29.594  ? 236 LEU   A CA  1 
ATOM   1613 C  C   . LEU   A 1 200 ? -10.501 4.846   38.592 1    26.978  ? 236 LEU   A C   1 
ATOM   1614 O  O   . LEU   A 1 200 ? -11.387 4.305   39.286 1    24.388  ? 236 LEU   A O   1 
ATOM   1615 C  CB  . LEU   A 1 200 ? -11.08  6.132   36.505 1    23.517  ? 236 LEU   A CB  1 
ATOM   1616 C  CG  . LEU   A 1 200 ? -11.655 7.425   35.933 1    24.457  ? 236 LEU   A CG  1 
ATOM   1617 C  CD1 . LEU   A 1 200 ? -11.843 7.271   34.431 1    22.204  ? 236 LEU   A CD1 1 
ATOM   1618 C  CD2 . LEU   A 1 200 ? -12.967 7.838   36.633 1    18.405  ? 236 LEU   A CD2 1 
ATOM   1619 N  N   . PHE   A 1 201 ? -9.274  4.344   38.356 1    22.083  ? 237 PHE   A N   1 
ATOM   1620 C  CA  . PHE   A 1 201 ? -8.821  3.049   38.811 1    24.688  ? 237 PHE   A CA  1 
ATOM   1621 C  C   . PHE   A 1 201 ? -8.811  2.983   40.342 1    21.582  ? 237 PHE   A C   1 
ATOM   1622 O  O   . PHE   A 1 201 ? -9.191  1.96    40.882 1    27.314  ? 237 PHE   A O   1 
ATOM   1623 C  CB  . PHE   A 1 201 ? -7.471  2.641   38.217 1    31.933  ? 237 PHE   A CB  1 
ATOM   1624 C  CG  . PHE   A 1 201 ? -6.943  1.326   38.788 1    39.282  ? 237 PHE   A CG  1 
ATOM   1625 C  CD1 . PHE   A 1 201 ? -7.502  0.1     38.396 1    33.354  ? 237 PHE   A CD1 1 
ATOM   1626 C  CD2 . PHE   A 1 201 ? -5.94   1.319   39.768 1    41.366  ? 237 PHE   A CD2 1 
ATOM   1627 C  CE1 . PHE   A 1 201 ? -7.021  -1.091  38.909 1    33.366  ? 237 PHE   A CE1 1 
ATOM   1628 C  CE2 . PHE   A 1 201 ? -5.494  0.121   40.318 1    38.516  ? 237 PHE   A CE2 1 
ATOM   1629 C  CZ  . PHE   A 1 201 ? -6.023  -1.083  39.876 1    37.574  ? 237 PHE   A CZ  1 
ATOM   1630 N  N   . GLN   A 1 202 ? -8.435  4.056   41.019 1    22.583  ? 238 GLN   A N   1 
ATOM   1631 C  CA  . GLN   A 1 202 ? -8.257  4.085   42.467 1    27.017  ? 238 GLN   A CA  1 
ATOM   1632 C  C   . GLN   A 1 202 ? -9.649  4.082   43.079 1    24.994  ? 238 GLN   A C   1 
ATOM   1633 O  O   . GLN   A 1 202 ? -9.858  3.516   44.113 1    22.702  ? 238 GLN   A O   1 
ATOM   1634 C  CB  . GLN   A 1 202 ? -7.461  5.295   42.978 1    35.706  ? 238 GLN   A CB  1 
ATOM   1635 C  CG  . GLN   A 1 202 ? -5.952  5.233   42.712 1    42.372  ? 238 GLN   A CG  1 
ATOM   1636 C  CD  . GLN   A 1 202 ? -5.257  4.037   43.366 1    51.709  ? 238 GLN   A CD  1 
ATOM   1637 O  OE1 . GLN   A 1 202 ? -5.289  3.891   44.594 1    59.817  ? 238 GLN   A OE1 1 
ATOM   1638 N  NE2 . GLN   A 1 202 ? -4.572  3.181   42.604 1    37.487  ? 238 GLN   A NE2 1 
ATOM   1639 N  N   . GLU   A 1 203 ? -10.65  4.522   42.337 1    24.581  ? 239 GLU   A N   1 
ATOM   1640 C  CA  . GLU   A 1 203 ? -11.94  4.627   42.981 1    26.137  ? 239 GLU   A CA  1 
ATOM   1641 C  C   . GLU   A 1 203 ? -12.619 3.264   43.082 1    33.598  ? 239 GLU   A C   1 
ATOM   1642 O  O   . GLU   A 1 203 ? -13.509 3.116   43.94  1    30.196  ? 239 GLU   A O   1 
ATOM   1643 C  CB  . GLU   A 1 203 ? -12.776 5.674   42.258 1    31.19   ? 239 GLU   A CB  1 
ATOM   1644 C  CG  . GLU   A 1 203 ? -12.35  7.099   42.627 1    42.65   ? 239 GLU   A CG  1 
ATOM   1645 C  CD  . GLU   A 1 203 ? -13.555 7.932   42.27  1    60.71   ? 239 GLU   A CD  1 
ATOM   1646 O  OE1 . GLU   A 1 203 ? -14.327 8.189   43.218 1    72.058  ? 239 GLU   A OE1 1 
ATOM   1647 O  OE2 . GLU   A 1 203 ? -13.77  8.252   41.061 1    86.733  ? 239 GLU   A OE2 1 
ATOM   1648 N  N   . LEU   A 1 204 ? -12.213 2.321   42.189 1    28.168  ? 240 LEU   A N   1 
ATOM   1649 C  CA  . LEU   A 1 204 ? -12.711 0.961   42.05  1    25.446  ? 240 LEU   A CA  1 
ATOM   1650 C  C   . LEU   A 1 204 ? -11.968 -0.023  42.962 1    23.758  ? 240 LEU   A C   1 
ATOM   1651 O  O   . LEU   A 1 204 ? -12.342 -1.16   43.036 1    25.273  ? 240 LEU   A O   1 
ATOM   1652 C  CB  . LEU   A 1 204 ? -12.653 0.504   40.591 1    31.658  ? 240 LEU   A CB  1 
ATOM   1653 C  CG  . LEU   A 1 204 ? -13.944 0.69    39.757 1    41.51   ? 240 LEU   A CG  1 
ATOM   1654 C  CD1 . LEU   A 1 204 ? -15.171 -0.095  40.214 1    44.23   ? 240 LEU   A CD1 1 
ATOM   1655 C  CD2 . LEU   A 1 204 ? -14.411 2.078   39.494 1    29.808  ? 240 LEU   A CD2 1 
ATOM   1656 N  N   . GLN   A 1 205 ? -10.916 0.385   43.665 1    25.679  ? 241 GLN   A N   1 
ATOM   1657 C  CA  . GLN   A 1 205 ? -10.11  -0.536  44.439 1    28.537  ? 241 GLN   A CA  1 
ATOM   1658 C  C   . GLN   A 1 205 ? -10.909 -1.216  45.548 1    29.349  ? 241 GLN   A C   1 
ATOM   1659 O  O   . GLN   A 1 205 ? -10.756 -2.424  45.763 1    36.781  ? 241 GLN   A O   1 
ATOM   1660 C  CB  . GLN   A 1 205 ? -8.977  0.262   45.093 1    34.028  ? 241 GLN   A CB  1 
ATOM   1661 C  CG  . GLN   A 1 205 ? -7.824  0.499   44.134 1    32.689  ? 241 GLN   A CG  1 
ATOM   1662 C  CD  . GLN   A 1 205 ? -7.19   -0.822  43.754 1    37.604  ? 241 GLN   A CD  1 
ATOM   1663 O  OE1 . GLN   A 1 205 ? -7.502  -1.367  42.688 1    38.012  ? 241 GLN   A OE1 1 
ATOM   1664 N  NE2 . GLN   A 1 205 ? -6.324  -1.34   44.633 1    35.821  ? 241 GLN   A NE2 1 
ATOM   1665 N  N   . PRO   A 1 206 ? -11.673 -0.49   46.389 1    27.544  ? 242 PRO   A N   1 
ATOM   1666 C  CA  . PRO   A 1 206 ? -12.438 -1.157  47.44  1    28.806  ? 242 PRO   A CA  1 
ATOM   1667 C  C   . PRO   A 1 206 ? -13.352 -2.293  46.974 1    31.109  ? 242 PRO   A C   1 
ATOM   1668 O  O   . PRO   A 1 206 ? -13.306 -3.403  47.539 1    29.916  ? 242 PRO   A O   1 
ATOM   1669 C  CB  . PRO   A 1 206 ? -13.194 0.06    48.006 1    35.504  ? 242 PRO   A CB  1 
ATOM   1670 C  CG  . PRO   A 1 206 ? -12.094 1.118   48.02  1    32.575  ? 242 PRO   A CG  1 
ATOM   1671 C  CD  . PRO   A 1 206 ? -11.631 0.978   46.56  1    29.385  ? 242 PRO   A CD  1 
ATOM   1672 N  N   . LEU   A 1 207 ? -14.111 -2.049  45.893 1    24.152  ? 243 LEU   A N   1 
ATOM   1673 C  CA  . LEU   A 1 207 ? -14.919 -3.109  45.32  1    23.778  ? 243 LEU   A CA  1 
ATOM   1674 C  C   . LEU   A 1 207 ? -14.033 -4.262  44.831 1    28.597  ? 243 LEU   A C   1 
ATOM   1675 O  O   . LEU   A 1 207 ? -14.299 -5.419  45.167 1    27.868  ? 243 LEU   A O   1 
ATOM   1676 C  CB  . LEU   A 1 207 ? -15.703 -2.517  44.16  1    29.293  ? 243 LEU   A CB  1 
ATOM   1677 C  CG  . LEU   A 1 207 ? -17.167 -2.164  44.414 1    33.099  ? 243 LEU   A CG  1 
ATOM   1678 C  CD1 . LEU   A 1 207 ? -17.691 -1.361  43.215 1    38.334  ? 243 LEU   A CD1 1 
ATOM   1679 C  CD2 . LEU   A 1 207 ? -17.916 -3.465  44.515 1    33.255  ? 243 LEU   A CD2 1 
ATOM   1680 N  N   . TYR   A 1 208 ? -12.972 -3.959  44.047 1    21.736  ? 244 TYR   A N   1 
ATOM   1681 C  CA  . TYR   A 1 208 ? -12.103 -4.994  43.5   1    20.168  ? 244 TYR   A CA  1 
ATOM   1682 C  C   . TYR   A 1 208 ? -11.391 -5.809  44.589 1    21.955  ? 244 TYR   A C   1 
ATOM   1683 O  O   . TYR   A 1 208 ? -11.419 -7.038  44.543 1    19.767  ? 244 TYR   A O   1 
ATOM   1684 C  CB  . TYR   A 1 208 ? -11.041 -4.461  42.525 1    24.132  ? 244 TYR   A CB  1 
ATOM   1685 C  CG  . TYR   A 1 208 ? -10.223 -5.615  41.984 1    25.765  ? 244 TYR   A CG  1 
ATOM   1686 C  CD1 . TYR   A 1 208 ? -10.855 -6.578  41.206 1    24.04   ? 244 TYR   A CD1 1 
ATOM   1687 C  CD2 . TYR   A 1 208 ? -8.872  -5.771  42.285 1    24.017  ? 244 TYR   A CD2 1 
ATOM   1688 C  CE1 . TYR   A 1 208 ? -10.225 -7.75   40.838 1    22.391  ? 244 TYR   A CE1 1 
ATOM   1689 C  CE2 . TYR   A 1 208 ? -8.214  -6.901  41.814 1    27.86   ? 244 TYR   A CE2 1 
ATOM   1690 C  CZ  . TYR   A 1 208 ? -8.875  -7.899  41.083 1    25.391  ? 244 TYR   A CZ  1 
ATOM   1691 O  OH  . TYR   A 1 208 ? -8.223  -9.016  40.518 1    19.148  ? 244 TYR   A OH  1 
ATOM   1692 N  N   . LEU   A 1 209 ? -10.778 -5.145  45.588 1    25.983  ? 245 LEU   A N   1 
ATOM   1693 C  CA  . LEU   A 1 209 ? -10.138 -5.855  46.7   1    24.589  ? 245 LEU   A CA  1 
ATOM   1694 C  C   . LEU   A 1 209 ? -11.143 -6.73   47.422 1    21.879  ? 245 LEU   A C   1 
ATOM   1695 O  O   . LEU   A 1 209 ? -10.784 -7.811  47.855 1    24.96   ? 245 LEU   A O   1 
ATOM   1696 C  CB  . LEU   A 1 209 ? -9.371  -5.008  47.728 1    24.817  ? 245 LEU   A CB  1 
ATOM   1697 C  CG  . LEU   A 1 209 ? -8.246  -4.111  47.192 1    24.312  ? 245 LEU   A CG  1 
ATOM   1698 C  CD1 . LEU   A 1 209 ? -7.748  -3.12   48.229 1    22.741  ? 245 LEU   A CD1 1 
ATOM   1699 C  CD2 . LEU   A 1 209 ? -7.044  -4.744  46.442 1    22.268  ? 245 LEU   A CD2 1 
ATOM   1700 N  N   . ASN   A 1 210 ? -12.373 -6.246  47.6   1    22.058  ? 246 ASN   A N   1 
ATOM   1701 C  CA  . ASN   A 1 210 ? -13.367 -7.001  48.344 1    19.485  ? 246 ASN   A CA  1 
ATOM   1702 C  C   . ASN   A 1 210 ? -13.804 -8.25   47.58  1    20.401  ? 246 ASN   A C   1 
ATOM   1703 O  O   . ASN   A 1 210 ? -13.95  -9.336  48.15  1    19.39   ? 246 ASN   A O   1 
ATOM   1704 C  CB  . ASN   A 1 210 ? -14.48  -6.079  48.801 1    21.611  ? 246 ASN   A CB  1 
ATOM   1705 C  CG  . ASN   A 1 210 ? -14.051 -5.406  50.097 1    30.662  ? 246 ASN   A CG  1 
ATOM   1706 O  OD1 . ASN   A 1 210 ? -13.974 -6.061  51.142 1    26.217  ? 246 ASN   A OD1 1 
ATOM   1707 N  ND2 . ASN   A 1 210 ? -13.783 -4.098  50.08  1    33.144  ? 246 ASN   A ND2 1 
ATOM   1708 N  N   . LEU   A 1 211 ? -13.981 -8.103  46.254 1    21.868  ? 247 LEU   A N   1 
ATOM   1709 C  CA  . LEU   A 1 211 ? -14.355 -9.237  45.435 1    19.003  ? 247 LEU   A CA  1 
ATOM   1710 C  C   . LEU   A 1 211 ? -13.21  -10.264 45.407 1    20.834  ? 247 LEU   A C   1 
ATOM   1711 O  O   . LEU   A 1 211 ? -13.426 -11.468 45.543 1    22.99   ? 247 LEU   A O   1 
ATOM   1712 C  CB  . LEU   A 1 211 ? -14.635 -8.631  44.066 1    17.386  ? 247 LEU   A CB  1 
ATOM   1713 C  CG  . LEU   A 1 211 ? -15.028 -9.663  43.01  1    21.174  ? 247 LEU   A CG  1 
ATOM   1714 C  CD1 . LEU   A 1 211 ? -16.321 -10.302 43.515 1    23.06   ? 247 LEU   A CD1 1 
ATOM   1715 C  CD2 . LEU   A 1 211 ? -15.163 -9.208  41.532 1    23.076  ? 247 LEU   A CD2 1 
ATOM   1716 N  N   . HIS   A 1 212 ? -11.968 -9.796  45.245 1    19.651  ? 248 HIS   A N   1 
ATOM   1717 C  CA  . HIS   A 1 212 ? -10.777 -10.652 45.166 1    20.743  ? 248 HIS   A CA  1 
ATOM   1718 C  C   . HIS   A 1 212 ? -10.647 -11.479 46.436 1    20.375  ? 248 HIS   A C   1 
ATOM   1719 O  O   . HIS   A 1 212 ? -10.494 -12.702 46.358 1    24.218  ? 248 HIS   A O   1 
ATOM   1720 C  CB  . HIS   A 1 212 ? -9.529  -9.781  45.015 1    20.315  ? 248 HIS   A CB  1 
ATOM   1721 C  CG  . HIS   A 1 212 ? -8.237  -10.472 44.93  1    26.643  ? 248 HIS   A CG  1 
ATOM   1722 N  ND1 . HIS   A 1 212 ? -7.553  -10.942 46.036 1    25.18   ? 248 HIS   A ND1 1 
ATOM   1723 C  CD2 . HIS   A 1 212 ? -7.451  -10.687 43.817 1    23.676  ? 248 HIS   A CD2 1 
ATOM   1724 C  CE1 . HIS   A 1 212 ? -6.409  -11.467 45.596 1    29.481  ? 248 HIS   A CE1 1 
ATOM   1725 N  NE2 . HIS   A 1 212 ? -6.345  -11.356 44.241 1    23.514  ? 248 HIS   A NE2 1 
ATOM   1726 N  N   . ALA   A 1 213 ? -10.738 -10.834 47.606 1    19.366  ? 249 ALA   A N   1 
ATOM   1727 C  CA  . ALA   A 1 213 ? -10.669 -11.573 48.858 1    21.125  ? 249 ALA   A CA  1 
ATOM   1728 C  C   . ALA   A 1 213 ? -11.795 -12.611 48.984 1    23.746  ? 249 ALA   A C   1 
ATOM   1729 O  O   . ALA   A 1 213 ? -11.626 -13.721 49.533 1    27.689  ? 249 ALA   A O   1 
ATOM   1730 C  CB  . ALA   A 1 213 ? -10.742 -10.616 50.009 1    19.718  ? 249 ALA   A CB  1 
ATOM   1731 N  N   . TYR   A 1 214 ? -12.976 -12.25  48.509 1    21.949  ? 250 TYR   A N   1 
ATOM   1732 C  CA  . TYR   A 1 214 ? -14.106 -13.139 48.73  1    23.679  ? 250 TYR   A CA  1 
ATOM   1733 C  C   . TYR   A 1 214 ? -13.924 -14.37  47.84  1    22.77   ? 250 TYR   A C   1 
ATOM   1734 O  O   . TYR   A 1 214 ? -14.216 -15.488 48.262 1    22.612  ? 250 TYR   A O   1 
ATOM   1735 C  CB  . TYR   A 1 214 ? -15.399 -12.336 48.489 1    23.344  ? 250 TYR   A CB  1 
ATOM   1736 C  CG  . TYR   A 1 214 ? -16.584 -13.296 48.409 1    28.217  ? 250 TYR   A CG  1 
ATOM   1737 C  CD1 . TYR   A 1 214 ? -17.239 -13.738 49.562 1    26.359  ? 250 TYR   A CD1 1 
ATOM   1738 C  CD2 . TYR   A 1 214 ? -17.11  -13.677 47.181 1    24.771  ? 250 TYR   A CD2 1 
ATOM   1739 C  CE1 . TYR   A 1 214 ? -18.303 -14.615 49.486 1    27.215  ? 250 TYR   A CE1 1 
ATOM   1740 C  CE2 . TYR   A 1 214 ? -18.241 -14.457 47.099 1    25.521  ? 250 TYR   A CE2 1 
ATOM   1741 C  CZ  . TYR   A 1 214 ? -18.792 -14.999 48.249 1    33.91   ? 250 TYR   A CZ  1 
ATOM   1742 O  OH  . TYR   A 1 214 ? -19.869 -15.86  48.162 1    35.702  ? 250 TYR   A OH  1 
ATOM   1743 N  N   . VAL   A 1 215 ? -13.454 -14.153 46.589 1    23.389  ? 251 VAL   A N   1 
ATOM   1744 C  CA  . VAL   A 1 215 ? -13.264 -15.215 45.603 1    19.167  ? 251 VAL   A CA  1 
ATOM   1745 C  C   . VAL   A 1 215 ? -12.088 -16.1   46.029 1    20.005  ? 251 VAL   A C   1 
ATOM   1746 O  O   . VAL   A 1 215 ? -12.154 -17.333 45.928 1    23.467  ? 251 VAL   A O   1 
ATOM   1747 C  CB  . VAL   A 1 215 ? -13.067 -14.635 44.185 1    19.707  ? 251 VAL   A CB  1 
ATOM   1748 C  CG1 . VAL   A 1 215 ? -12.516 -15.68  43.163 1    15.126  ? 251 VAL   A CG1 1 
ATOM   1749 C  CG2 . VAL   A 1 215 ? -14.361 -13.939 43.742 1    16.404  ? 251 VAL   A CG2 1 
ATOM   1750 N  N   . ARG   A 1 216 ? -11.004 -15.471 46.489 1    20.602  ? 252 ARG   A N   1 
ATOM   1751 C  CA  . ARG   A 1 216 ? -9.854  -16.178 47.048 1    20.252  ? 252 ARG   A CA  1 
ATOM   1752 C  C   . ARG   A 1 216 ? -10.323 -17.186 48.089 1    22.038  ? 252 ARG   A C   1 
ATOM   1753 O  O   . ARG   A 1 216 ? -9.938  -18.392 48.024 1    26.318  ? 252 ARG   A O   1 
ATOM   1754 C  CB  . ARG   A 1 216 ? -8.728  -15.219 47.467 1    17.932  ? 252 ARG   A CB  1 
ATOM   1755 C  CG  . ARG   A 1 216 ? -7.552  -15.898 48.147 1    19.808  ? 252 ARG   A CG  1 
ATOM   1756 C  CD  . ARG   A 1 216 ? -6.493  -14.827 48.589 1    19.861  ? 252 ARG   A CD  1 
ATOM   1757 N  NE  . ARG   A 1 216 ? -7.123  -13.838 49.499 1    20.672  ? 252 ARG   A NE  1 
ATOM   1758 C  CZ  . ARG   A 1 216 ? -6.593  -12.642 49.757 1    20.963  ? 252 ARG   A CZ  1 
ATOM   1759 N  NH1 . ARG   A 1 216 ? -5.411  -12.324 49.168 1    18.055  ? 252 ARG   A NH1 1 
ATOM   1760 N  NH2 . ARG   A 1 216 ? -7.244  -11.8   50.577 1    19.022  ? 252 ARG   A NH2 1 
ATOM   1761 N  N   . ARG   A 1 217 ? -11.23  -16.735 48.981 1    20.907  ? 253 ARG   A N   1 
ATOM   1762 C  CA  . ARG   A 1 217 ? -11.681 -17.618 50.065 1    18.975  ? 253 ARG   A CA  1 
ATOM   1763 C  C   . ARG   A 1 217 ? -12.44  -18.785 49.448 1    21.179  ? 253 ARG   A C   1 
ATOM   1764 O  O   . ARG   A 1 217 ? -12.246 -19.943 49.843 1    21.727  ? 253 ARG   A O   1 
ATOM   1765 C  CB  . ARG   A 1 217 ? -12.683 -16.961 51.035 1    21.639  ? 253 ARG   A CB  1 
ATOM   1766 C  CG  . ARG   A 1 217 ? -13.339 -17.911 52.037 1    25.372  ? 253 ARG   A CG  1 
ATOM   1767 C  CD  . ARG   A 1 217 ? -12.385 -18.372 53.162 1    24.703  ? 253 ARG   A CD  1 
ATOM   1768 N  NE  . ARG   A 1 217 ? -11.826 -17.194 53.838 1    25.946  ? 253 ARG   A NE  1 
ATOM   1769 C  CZ  . ARG   A 1 217 ? -11.046 -17.384 54.895 1    29.973  ? 253 ARG   A CZ  1 
ATOM   1770 N  NH1 . ARG   A 1 217 ? -10.369 -16.384 55.489 1    24.854  ? 253 ARG   A NH1 1 
ATOM   1771 N  NH2 . ARG   A 1 217 ? -10.968 -18.628 55.328 1    25.15   ? 253 ARG   A NH2 1 
ATOM   1772 N  N   . ALA   A 1 218 ? -13.282 -18.491 48.433 1    21.501  ? 254 ALA   A N   1 
ATOM   1773 C  CA  . ALA   A 1 218 ? -14.026 -19.573 47.771 1    20.882  ? 254 ALA   A CA  1 
ATOM   1774 C  C   . ALA   A 1 218 ? -13.082 -20.553 47.075 1    22.28   ? 254 ALA   A C   1 
ATOM   1775 O  O   . ALA   A 1 218 ? -13.277 -21.759 47.145 1    27.64   ? 254 ALA   A O   1 
ATOM   1776 C  CB  . ALA   A 1 218 ? -15.027 -18.99  46.791 1    22.434  ? 254 ALA   A CB  1 
ATOM   1777 N  N   . LEU   A 1 219 ? -12.043 -20.068 46.388 1    21.252  ? 255 LEU   A N   1 
ATOM   1778 C  CA  . LEU   A 1 219 ? -11.126 -21.034 45.79  1    23.885  ? 255 LEU   A CA  1 
ATOM   1779 C  C   . LEU   A 1 219 ? -10.399 -21.887 46.853 1    27.771  ? 255 LEU   A C   1 
ATOM   1780 O  O   . LEU   A 1 219 ? -10.156 -23.08  46.646 1    22.878  ? 255 LEU   A O   1 
ATOM   1781 C  CB  . LEU   A 1 219 ? -10.165 -20.26  44.904 1    22.051  ? 255 LEU   A CB  1 
ATOM   1782 C  CG  . LEU   A 1 219 ? -10.881 -19.648 43.693 1    28.719  ? 255 LEU   A CG  1 
ATOM   1783 C  CD1 . LEU   A 1 219 ? -9.99   -18.557 43.147 1    23.617  ? 255 LEU   A CD1 1 
ATOM   1784 C  CD2 . LEU   A 1 219 ? -11.115 -20.695 42.591 1    26.417  ? 255 LEU   A CD2 1 
ATOM   1785 N  N   . HIS   A 1 220 ? -9.997  -21.255 47.971 1    25.851  ? 256 HIS   A N   1 
ATOM   1786 C  CA  . HIS   A 1 220 ? -9.349  -21.975 49.025 1    25.788  ? 256 HIS   A CA  1 
ATOM   1787 C  C   . HIS   A 1 220 ? -10.235 -23.167 49.384 1    31.518  ? 256 HIS   A C   1 
ATOM   1788 O  O   . HIS   A 1 220 ? -9.73   -24.283 49.518 1    29.167  ? 256 HIS   A O   1 
ATOM   1789 C  CB  . HIS   A 1 220 ? -9.271  -21.074 50.243 1    26.453  ? 256 HIS   A CB  1 
ATOM   1790 C  CG  . HIS   A 1 220 ? -8.665  -21.681 51.458 1    31.609  ? 256 HIS   A CG  1 
ATOM   1791 N  ND1 . HIS   A 1 220 ? -9.441  -22.266 52.452 1    35.339  ? 256 HIS   A ND1 1 
ATOM   1792 C  CD2 . HIS   A 1 220 ? -7.377  -21.685 51.907 1    29.697  ? 256 HIS   A CD2 1 
ATOM   1793 C  CE1 . HIS   A 1 220 ? -8.659  -22.625 53.47  1    30.363  ? 256 HIS   A CE1 1 
ATOM   1794 N  NE2 . HIS   A 1 220 ? -7.403  -22.283 53.154 1    32.736  ? 256 HIS   A NE2 1 
ATOM   1795 N  N   . ARG   A 1 221 ? -11.562 -22.951 49.455 1    28.072  ? 257 ARG   A N   1 
ATOM   1796 C  CA  . ARG   A 1 221 ? -12.492 -23.991 49.868 1    30.906  ? 257 ARG   A CA  1 
ATOM   1797 C  C   . ARG   A 1 221 ? -12.535 -25.097 48.818 1    31.943  ? 257 ARG   A C   1 
ATOM   1798 O  O   . ARG   A 1 221 ? -12.516 -26.255 49.169 1    34.105  ? 257 ARG   A O   1 
ATOM   1799 C  CB  . ARG   A 1 221 ? -13.899 -23.437 50.099 1    41.338  ? 257 ARG   A CB  1 
ATOM   1800 C  CG  . ARG   A 1 221 ? -15.059 -24.331 50.534 1    50.066  ? 257 ARG   A CG  1 
ATOM   1801 C  CD  . ARG   A 1 221 ? -16.189 -23.348 51.014 1    63.321  ? 257 ARG   A CD  1 
ATOM   1802 N  NE  . ARG   A 1 221 ? -16.988 -22.686 49.966 1    67.226  ? 257 ARG   A NE  1 
ATOM   1803 C  CZ  . ARG   A 1 221 ? -17.153 -21.384 49.616 1    65.99   ? 257 ARG   A CZ  1 
ATOM   1804 N  NH1 . ARG   A 1 221 ? -16.535 -20.433 50.308 1    43.464  ? 257 ARG   A NH1 1 
ATOM   1805 N  NH2 . ARG   A 1 221 ? -17.945 -21.051 48.572 1    53.798  ? 257 ARG   A NH2 1 
ATOM   1806 N  N   . HIS   A 1 222 ? -12.547 -24.754 47.528 1    33.639  ? 258 HIS   A N   1 
ATOM   1807 C  CA  . HIS   A 1 222 ? -12.655 -25.777 46.497 1    30.738  ? 258 HIS   A CA  1 
ATOM   1808 C  C   . HIS   A 1 222 ? -11.314 -26.449 46.204 1    34.015  ? 258 HIS   A C   1 
ATOM   1809 O  O   . HIS   A 1 222 ? -11.283 -27.691 46.05  1    30.984  ? 258 HIS   A O   1 
ATOM   1810 C  CB  . HIS   A 1 222 ? -13.393 -25.3   45.238 1    30.14   ? 258 HIS   A CB  1 
ATOM   1811 C  CG  . HIS   A 1 222 ? -13.426 -26.348 44.19  1    32.803  ? 258 HIS   A CG  1 
ATOM   1812 N  ND1 . HIS   A 1 222 ? -14.422 -27.299 44.147 1    33.347  ? 258 HIS   A ND1 1 
ATOM   1813 C  CD2 . HIS   A 1 222 ? -12.58  -26.625 43.159 1    35.682  ? 258 HIS   A CD2 1 
ATOM   1814 C  CE1 . HIS   A 1 222 ? -14.174 -28.122 43.116 1    35.799  ? 258 HIS   A CE1 1 
ATOM   1815 N  NE2 . HIS   A 1 222 ? -13.091 -27.721 42.485 1    41.771  ? 258 HIS   A NE2 1 
ATOM   1816 N  N   . TYR   A 1 223 ? -10.227 -25.654 46.137 1    29.532  ? 259 TYR   A N   1 
ATOM   1817 C  CA  . TYR   A 1 223 ? -8.996  -26.236 45.609 1    26.637  ? 259 TYR   A CA  1 
ATOM   1818 C  C   . TYR   A 1 223 ? -8.06   -26.556 46.756 1    30.252  ? 259 TYR   A C   1 
ATOM   1819 O  O   . TYR   A 1 223 ? -7.035  -27.188 46.529 1    28.822  ? 259 TYR   A O   1 
ATOM   1820 C  CB  . TYR   A 1 223 ? -8.233  -25.383 44.609 1    24.957  ? 259 TYR   A CB  1 
ATOM   1821 C  CG  . TYR   A 1 223 ? -8.98   -25.268 43.278 1    23.731  ? 259 TYR   A CG  1 
ATOM   1822 C  CD1 . TYR   A 1 223 ? -8.789  -26.216 42.267 1    19.759  ? 259 TYR   A CD1 1 
ATOM   1823 C  CD2 . TYR   A 1 223 ? -9.828  -24.182 43.001 1    20.6    ? 259 TYR   A CD2 1 
ATOM   1824 C  CE1 . TYR   A 1 223 ? -9.416  -26.068 41.037 1    20.249  ? 259 TYR   A CE1 1 
ATOM   1825 C  CE2 . TYR   A 1 223 ? -10.453 -24.033 41.767 1    19.386  ? 259 TYR   A CE2 1 
ATOM   1826 C  CZ  . TYR   A 1 223 ? -10.3   -25.024 40.807 1    22.234  ? 259 TYR   A CZ  1 
ATOM   1827 O  OH  . TYR   A 1 223 ? -10.9   -24.974 39.567 1    22.999  ? 259 TYR   A OH  1 
ATOM   1828 N  N   . GLY   A 1 224 ? -8.455  -26.15  47.979 1    27.348  ? 260 GLY   A N   1 
ATOM   1829 C  CA  . GLY   A 1 224 ? -7.703  -26.577 49.145 1    24.021  ? 260 GLY   A CA  1 
ATOM   1830 C  C   . GLY   A 1 224 ? -6.596  -25.608 49.57  1    23.59   ? 260 GLY   A C   1 
ATOM   1831 O  O   . GLY   A 1 224 ? -5.86   -25.066 48.756 1    25.167  ? 260 GLY   A O   1 
ATOM   1832 N  N   . ALA   A 1 225 ? -6.429  -25.523 50.887 1    22.861  ? 261 ALA   A N   1 
ATOM   1833 C  CA  . ALA   A 1 225 ? -5.485  -24.701 51.636 1    27.679  ? 261 ALA   A CA  1 
ATOM   1834 C  C   . ALA   A 1 225 ? -4.042  -24.827 51.133 1    25.882  ? 261 ALA   A C   1 
ATOM   1835 O  O   . ALA   A 1 225 ? -3.227  -23.926 51.231 1    26.106  ? 261 ALA   A O   1 
ATOM   1836 C  CB  . ALA   A 1 225 ? -5.619  -25.09  53.124 1    25.877  ? 261 ALA   A CB  1 
ATOM   1837 N  N   . GLN   A 1 226 ? -3.635  -25.987 50.663 1    26.628  ? 262 GLN   A N   1 
ATOM   1838 C  CA  . GLN   A 1 226 ? -2.247  -26.026 50.233 1    23.422  ? 262 GLN   A CA  1 
ATOM   1839 C  C   . GLN   A 1 226 ? -2.139  -25.385 48.86  1    27.65   ? 262 GLN   A C   1 
ATOM   1840 O  O   . GLN   A 1 226 ? -1.01   -25.181 48.381 1    27.525  ? 262 GLN   A O   1 
ATOM   1841 C  CB  . GLN   A 1 226 ? -1.807  -27.484 50.065 1    24.541  ? 262 GLN   A CB  1 
ATOM   1842 C  CG  . GLN   A 1 226 ? -1.814  -28.309 51.354 1    26.539  ? 262 GLN   A CG  1 
ATOM   1843 C  CD  . GLN   A 1 226 ? -0.524  -28.134 52.13  1    25.28   ? 262 GLN   A CD  1 
ATOM   1844 O  OE1 . GLN   A 1 226 ? 0.388   -27.502 51.636 1    22.66   ? 262 GLN   A OE1 1 
ATOM   1845 N  NE2 . GLN   A 1 226 ? -0.416  -28.656 53.342 1    23.988  ? 262 GLN   A NE2 1 
ATOM   1846 N  N   . HIS   A 1 227 ? -3.286  -25.093 48.197 1    28.015  ? 263 HIS   A N   1 
ATOM   1847 C  CA  . HIS   A 1 227 ? -3.128  -24.469 46.872 1    32.385  ? 263 HIS   A CA  1 
ATOM   1848 C  C   . HIS   A 1 227 ? -3.405  -22.971 46.869 1    34.754  ? 263 HIS   A C   1 
ATOM   1849 O  O   . HIS   A 1 227 ? -3.165  -22.345 45.844 1    37.909  ? 263 HIS   A O   1 
ATOM   1850 C  CB  . HIS   A 1 227 ? -3.814  -25.218 45.723 1    30.668  ? 263 HIS   A CB  1 
ATOM   1851 C  CG  . HIS   A 1 227 ? -3.292  -26.61  45.666 1    38.837  ? 263 HIS   A CG  1 
ATOM   1852 N  ND1 . HIS   A 1 227 ? -2.002  -26.884 45.274 1    42.029  ? 263 HIS   A ND1 1 
ATOM   1853 C  CD2 . HIS   A 1 227 ? -3.81   -27.779 46.107 1    44.809  ? 263 HIS   A CD2 1 
ATOM   1854 C  CE1 . HIS   A 1 227 ? -1.784  -28.188 45.428 1    46.021  ? 263 HIS   A CE1 1 
ATOM   1855 N  NE2 . HIS   A 1 227 ? -2.869  -28.745 45.949 1    43.522  ? 263 HIS   A NE2 1 
ATOM   1856 N  N   . ILE   A 1 228 ? -3.912  -22.398 47.983 1    32.488  ? 264 ILE   A N   1 
ATOM   1857 C  CA  . ILE   A 1 228 ? -4.401  -21.016 47.978 1    26.172  ? 264 ILE   A CA  1 
ATOM   1858 C  C   . ILE   A 1 228 ? -3.882  -20.341 49.244 1    31.987  ? 264 ILE   A C   1 
ATOM   1859 O  O   . ILE   A 1 228 ? -4.33   -20.69  50.331 1    35.725  ? 264 ILE   A O   1 
ATOM   1860 C  CB  . ILE   A 1 228 ? -5.948  -20.979 47.97  1    20.234  ? 264 ILE   A CB  1 
ATOM   1861 C  CG1 . ILE   A 1 228 ? -6.563  -21.653 46.754 1    22.218  ? 264 ILE   A CG1 1 
ATOM   1862 C  CG2 . ILE   A 1 228 ? -6.444  -19.553 48.08  1    19.501  ? 264 ILE   A CG2 1 
ATOM   1863 C  CD1 . ILE   A 1 228 ? -6.222  -20.932 45.441 1    27.503  ? 264 ILE   A CD1 1 
ATOM   1864 N  N   . ASN   A 1 229 ? -3.02   -19.336 49.093 1    27.677  ? 265 ASN   A N   1 
ATOM   1865 C  CA  . ASN   A 1 229 ? -2.582  -18.514 50.2   1    25.015  ? 265 ASN   A CA  1 
ATOM   1866 C  C   . ASN   A 1 229 ? -3.658  -17.467 50.513 1    25.259  ? 265 ASN   A C   1 
ATOM   1867 O  O   . ASN   A 1 229 ? -3.941  -16.606 49.702 1    25.806  ? 265 ASN   A O   1 
ATOM   1868 C  CB  . ASN   A 1 229 ? -1.202  -17.927 49.884 1    22.41   ? 265 ASN   A CB  1 
ATOM   1869 C  CG  . ASN   A 1 229 ? -0.73   -17.016 51.003 1    26.471  ? 265 ASN   A CG  1 
ATOM   1870 O  OD1 . ASN   A 1 229 ? -1.41   -16.862 52.017 1    22.129  ? 265 ASN   A OD1 1 
ATOM   1871 N  ND2 . ASN   A 1 229 ? 0.357   -16.288 50.81  1    30.596  ? 265 ASN   A ND2 1 
ATOM   1872 N  N   . LEU   A 1 230 ? -4.215  -17.431 51.727 1    30.902  ? 266 LEU   A N   1 
ATOM   1873 C  CA  . LEU   A 1 230 ? -5.392  -16.584 51.946 1    26.125  ? 266 LEU   A CA  1 
ATOM   1874 C  C   . LEU   A 1 230 ? -5.029  -15.119 52.067 1    27.267  ? 266 LEU   A C   1 
ATOM   1875 O  O   . LEU   A 1 230 ? -5.936  -14.297 52.205 1    24.398  ? 266 LEU   A O   1 
ATOM   1876 C  CB  . LEU   A 1 230 ? -6.111  -16.991 53.203 1    26.552  ? 266 LEU   A CB  1 
ATOM   1877 C  CG  . LEU   A 1 230 ? -6.888  -18.3   53.093 1    27.301  ? 266 LEU   A CG  1 
ATOM   1878 C  CD1 . LEU   A 1 230 ? -7.243  -18.69  54.562 1    22.2    ? 266 LEU   A CD1 1 
ATOM   1879 C  CD2 . LEU   A 1 230 ? -8.105  -18.065 52.205 1    17.117  ? 266 LEU   A CD2 1 
ATOM   1880 N  N   . GLU   A 1 231 ? -3.717  -14.822 52.018 1    26.651  ? 267 GLU   A N   1 
ATOM   1881 C  CA  . GLU   A 1 231 ? -3.224  -13.455 52.114 1    23.103  ? 267 GLU   A CA  1 
ATOM   1882 C  C   . GLU   A 1 231 ? -2.266  -13.182 50.954 1    20.966  ? 267 GLU   A C   1 
ATOM   1883 O  O   . GLU   A 1 231 ? -1.347  -12.375 51.019 1    22.981  ? 267 GLU   A O   1 
ATOM   1884 C  CB  . GLU   A 1 231 ? -2.323  -13.387 53.35  1    24.689  ? 267 GLU   A CB  1 
ATOM   1885 C  CG  . GLU   A 1 231 ? -3.087  -13.355 54.677 1    36.722  ? 267 GLU   A CG  1 
ATOM   1886 C  CD  . GLU   A 1 231 ? -2.113  -13.362 55.85  1    51.64   ? 267 GLU   A CD  1 
ATOM   1887 O  OE1 . GLU   A 1 231 ? -1.107  -12.605 55.759 1    66.954  ? 267 GLU   A OE1 1 
ATOM   1888 O  OE2 . GLU   A 1 231 ? -2.308  -14.118 56.828 1    49.581  ? 267 GLU   A OE2 1 
ATOM   1889 N  N   . GLY   A 1 232 ? -2.405  -13.916 49.887 1    19.481  ? 268 GLY   A N   1 
ATOM   1890 C  CA  . GLY   A 1 232 ? -1.424  -13.774 48.826 1    22.192  ? 268 GLY   A CA  1 
ATOM   1891 C  C   . GLY   A 1 232 ? -2.196  -13.635 47.515 1    18.512  ? 268 GLY   A C   1 
ATOM   1892 O  O   . GLY   A 1 232 ? -3.401  -13.557 47.565 1    17.069  ? 268 GLY   A O   1 
ATOM   1893 N  N   . PRO   A 1 233 ? -1.542  -13.569 46.343 1    18.83   ? 269 PRO   A N   1 
ATOM   1894 C  CA  . PRO   A 1 233 ? -2.272  -13.436 45.056 1    19.957  ? 269 PRO   A CA  1 
ATOM   1895 C  C   . PRO   A 1 233 ? -2.992  -14.746 44.687 1    26.664  ? 269 PRO   A C   1 
ATOM   1896 O  O   . PRO   A 1 233 ? -2.631  -15.808 45.187 1    30.426  ? 269 PRO   A O   1 
ATOM   1897 C  CB  . PRO   A 1 233 ? -1.14   -13.181 44.074 1    17.514  ? 269 PRO   A CB  1 
ATOM   1898 C  CG  . PRO   A 1 233 ? 0.097   -13.793 44.746 1    21.043  ? 269 PRO   A CG  1 
ATOM   1899 C  CD  . PRO   A 1 233 ? -0.078  -13.702 46.247 1    17.816  ? 269 PRO   A CD  1 
ATOM   1900 N  N   . ILE   A 1 234 ? -3.976  -14.696 43.781 1    22.737  ? 270 ILE   A N   1 
ATOM   1901 C  CA  . ILE   A 1 234 ? -4.754  -15.846 43.319 1    17.558  ? 270 ILE   A CA  1 
ATOM   1902 C  C   . ILE   A 1 234 ? -4.008  -16.443 42.109 1    20.923  ? 270 ILE   A C   1 
ATOM   1903 O  O   . ILE   A 1 234 ? -3.453  -15.711 41.307 1    20.498  ? 270 ILE   A O   1 
ATOM   1904 C  CB  . ILE   A 1 234 ? -6.159  -15.372 42.891 1    17.113  ? 270 ILE   A CB  1 
ATOM   1905 C  CG1 . ILE   A 1 234 ? -6.939  -14.851 44.132 1    18.522  ? 270 ILE   A CG1 1 
ATOM   1906 C  CG2 . ILE   A 1 234 ? -6.91   -16.491 42.162 1    18.253  ? 270 ILE   A CG2 1 
ATOM   1907 C  CD1 . ILE   A 1 234 ? -8.379  -14.433 43.874 1    19.938  ? 270 ILE   A CD1 1 
ATOM   1908 N  N   . PRO   A 1 235 ? -3.858  -17.776 41.985 1    18.127  ? 271 PRO   A N   1 
ATOM   1909 C  CA  . PRO   A 1 235 ? -3.207  -18.385 40.841 1    19.661  ? 271 PRO   A CA  1 
ATOM   1910 C  C   . PRO   A 1 235 ? -4.039  -18.157 39.589 1    21.184  ? 271 PRO   A C   1 
ATOM   1911 O  O   . PRO   A 1 235 ? -5.251  -18.358 39.626 1    21.659  ? 271 PRO   A O   1 
ATOM   1912 C  CB  . PRO   A 1 235 ? -3.192  -19.844 41.258 1    23.884  ? 271 PRO   A CB  1 
ATOM   1913 C  CG  . PRO   A 1 235 ? -3.168  -19.84  42.759 1    19.587  ? 271 PRO   A CG  1 
ATOM   1914 C  CD  . PRO   A 1 235 ? -4.158  -18.73  43.048 1    20.35   ? 271 PRO   A CD  1 
ATOM   1915 N  N   . ALA   A 1 236 ? -3.365  -17.712 38.517 1    20.482  ? 272 ALA   A N   1 
ATOM   1916 C  CA  . ALA   A 1 236 ? -4.019  -17.011 37.433 1    24.532  ? 272 ALA   A CA  1 
ATOM   1917 C  C   . ALA   A 1 236 ? -4.854  -17.956 36.569 1    26.285  ? 272 ALA   A C   1 
ATOM   1918 O  O   . ALA   A 1 236 ? -5.469  -17.498 35.598 1    25.546  ? 272 ALA   A O   1 
ATOM   1919 C  CB  . ALA   A 1 236 ? -2.991  -16.278 36.598 1    22.033  ? 272 ALA   A CB  1 
ATOM   1920 N  N   . HIS   A 1 237 ? -4.838  -19.269 36.885 1    25.204  ? 273 HIS   A N   1 
ATOM   1921 C  CA  . HIS   A 1 237 ? -5.49   -20.244 36.014 1    26.453  ? 273 HIS   A CA  1 
ATOM   1922 C  C   . HIS   A 1 237 ? -6.861  -20.761 36.513 1    29.517  ? 273 HIS   A C   1 
ATOM   1923 O  O   . HIS   A 1 237 ? -7.482  -21.576 35.813 1    27.813  ? 273 HIS   A O   1 
ATOM   1924 C  CB  . HIS   A 1 237 ? -4.54   -21.396 35.675 1    22.05   ? 273 HIS   A CB  1 
ATOM   1925 C  CG  . HIS   A 1 237 ? -4.216  -22.242 36.834 1    22.827  ? 273 HIS   A CG  1 
ATOM   1926 N  ND1 . HIS   A 1 237 ? -3.879  -21.708 38.069 1    23.627  ? 273 HIS   A ND1 1 
ATOM   1927 C  CD2 . HIS   A 1 237 ? -4.252  -23.575 36.981 1    21.642  ? 273 HIS   A CD2 1 
ATOM   1928 C  CE1 . HIS   A 1 237 ? -3.621  -22.697 38.926 1    24.645  ? 273 HIS   A CE1 1 
ATOM   1929 N  NE2 . HIS   A 1 237 ? -3.86   -23.849 38.301 1    23.185  ? 273 HIS   A NE2 1 
ATOM   1930 N  N   . LEU   A 1 238 ? -7.352  -20.236 37.653 1    25.209  ? 274 LEU   A N   1 
ATOM   1931 C  CA  . LEU   A 1 238 ? -8.504  -20.724 38.426 1    26.081  ? 274 LEU   A CA  1 
ATOM   1932 C  C   . LEU   A 1 238 ? -9.766  -19.869 38.3   1    24.702  ? 274 LEU   A C   1 
ATOM   1933 O  O   . LEU   A 1 238 ? -10.76  -20.12  38.973 1    32.667  ? 274 LEU   A O   1 
ATOM   1934 C  CB  . LEU   A 1 238 ? -8.043  -20.721 39.886 1    19.717  ? 274 LEU   A CB  1 
ATOM   1935 C  CG  . LEU   A 1 238 ? -6.881  -21.66  40.175 1    19.91   ? 274 LEU   A CG  1 
ATOM   1936 C  CD1 . LEU   A 1 238 ? -6.735  -21.722 41.689 1    21.556  ? 274 LEU   A CD1 1 
ATOM   1937 C  CD2 . LEU   A 1 238 ? -7.215  -23.031 39.568 1    19.854  ? 274 LEU   A CD2 1 
ATOM   1938 N  N   . LEU   A 1 239 ? -9.738  -18.855 37.437 1    26.36   ? 275 LEU   A N   1 
ATOM   1939 C  CA  . LEU   A 1 239 ? -10.781 -17.847 37.34  1    24.394  ? 275 LEU   A CA  1 
ATOM   1940 C  C   . LEU   A 1 239 ? -11.71  -18.095 36.14  1    22.135  ? 275 LEU   A C   1 
ATOM   1941 O  O   . LEU   A 1 239 ? -12.577 -17.258 35.883 1    20.769  ? 275 LEU   A O   1 
ATOM   1942 C  CB  . LEU   A 1 239 ? -10.189 -16.426 37.282 1    24.568  ? 275 LEU   A CB  1 
ATOM   1943 C  CG  . LEU   A 1 239 ? -9.639  -15.789 38.555 1    25.492  ? 275 LEU   A CG  1 
ATOM   1944 C  CD1 . LEU   A 1 239 ? -10.518 -16.235 39.713 1    29.407  ? 275 LEU   A CD1 1 
ATOM   1945 C  CD2 . LEU   A 1 239 ? -8.198  -16.097 38.799 1    21.259  ? 275 LEU   A CD2 1 
ATOM   1946 N  N   . GLY   A 1 240 ? -11.571 -19.211 35.419 1    18.885  ? 276 GLY   A N   1 
ATOM   1947 C  CA  . GLY   A 1 240 ? -12.62  -19.617 34.491 1    18.221  ? 276 GLY   A CA  1 
ATOM   1948 C  C   . GLY   A 1 240 ? -12.361 -19.049 33.082 1    25.19   ? 276 GLY   A C   1 
ATOM   1949 O  O   . GLY   A 1 240 ? -13.148 -19.266 32.114 1    24.506  ? 276 GLY   A O   1 
ATOM   1950 N  N   . ASN   A 1 241 ? -11.243 -18.299 32.976 1    19.239  ? 277 ASN   A N   1 
ATOM   1951 C  CA  . ASN   A 1 241 ? -10.979 -17.603 31.734 1    19.405  ? 277 ASN   A CA  1 
ATOM   1952 C  C   . ASN   A 1 241 ? -9.483  -17.675 31.449 1    19.689  ? 277 ASN   A C   1 
ATOM   1953 O  O   . ASN   A 1 241 ? -8.657  -17.553 32.357 1    17.246  ? 277 ASN   A O   1 
ATOM   1954 C  CB  . ASN   A 1 241 ? -11.666 -16.23  31.754 1    19.956  ? 277 ASN   A CB  1 
ATOM   1955 C  CG  . ASN   A 1 241 ? -11.141 -15.263 30.718 1    24.245  ? 277 ASN   A CG  1 
ATOM   1956 O  OD1 . ASN   A 1 241 ? -10     -14.779 30.847 1    24.844  ? 277 ASN   A OD1 1 
ATOM   1957 N  ND2 . ASN   A 1 241 ? -11.925 -15.007 29.669 1    24.161  ? 277 ASN   A ND2 1 
ATOM   1958 N  N   . MET   A 1 242 ? -9.132  -17.803 30.164 1    17.805  ? 278 MET   A N   1 
ATOM   1959 C  CA  . MET   A 1 242 ? -7.741  -17.882 29.76  1    17.195  ? 278 MET   A CA  1 
ATOM   1960 C  C   . MET   A 1 242 ? -6.847  -16.781 30.365 1    19.32   ? 278 MET   A C   1 
ATOM   1961 O  O   . MET   A 1 242 ? -5.711  -17.07  30.77  1    18.431  ? 278 MET   A O   1 
ATOM   1962 C  CB  . MET   A 1 242 ? -7.655  -18.075 28.235 1    22.438  ? 278 MET   A CB  1 
ATOM   1963 C  CG  . MET   A 1 242 ? -6.226  -18.329 27.675 1    23.718  ? 278 MET   A CG  1 
ATOM   1964 S  SD  . MET   A 1 242 ? -5.37   -19.718 28.445 1    27.045  ? 278 MET   A SD  1 
ATOM   1965 C  CE  . MET   A 1 242 ? -6.195  -21.083 27.606 1    28.067  ? 278 MET   A CE  1 
ATOM   1966 N  N   . TRP   A 1 243 ? -7.338  -15.527 30.467 1    18.47   ? 279 TRP   A N   1 
ATOM   1967 C  CA  . TRP   A 1 243 ? -6.513  -14.429 30.955 1    15.097  ? 279 TRP   A CA  1 
ATOM   1968 C  C   . TRP   A 1 243 ? -6.913  -13.921 32.34  1    16.029  ? 279 TRP   A C   1 
ATOM   1969 O  O   . TRP   A 1 243 ? -6.357  -12.951 32.848 1    16.861  ? 279 TRP   A O   1 
ATOM   1970 C  CB  . TRP   A 1 243 ? -6.569  -13.296 29.934 1    14.97   ? 279 TRP   A CB  1 
ATOM   1971 C  CG  . TRP   A 1 243 ? -6.18   -13.825 28.581 1    17.934  ? 279 TRP   A CG  1 
ATOM   1972 C  CD1 . TRP   A 1 243 ? -4.917  -13.985 28.084 1    18.427  ? 279 TRP   A CD1 1 
ATOM   1973 C  CD2 . TRP   A 1 243 ? -7.08   -14.308 27.584 1    19.058  ? 279 TRP   A CD2 1 
ATOM   1974 N  NE1 . TRP   A 1 243 ? -4.976  -14.559 26.85  1    21.836  ? 279 TRP   A NE1 1 
ATOM   1975 C  CE2 . TRP   A 1 243 ? -6.285  -14.739 26.506 1    20.512  ? 279 TRP   A CE2 1 
ATOM   1976 C  CE3 . TRP   A 1 243 ? -8.474  -14.437 27.521 1    25.197  ? 279 TRP   A CE3 1 
ATOM   1977 C  CZ2 . TRP   A 1 243 ? -6.839  -15.292 25.359 1    22.565  ? 279 TRP   A CZ2 1 
ATOM   1978 C  CZ3 . TRP   A 1 243 ? -9.042  -15.002 26.39  1    26.165  ? 279 TRP   A CZ3 1 
ATOM   1979 C  CH2 . TRP   A 1 243 ? -8.221  -15.414 25.325 1    27.767  ? 279 TRP   A CH2 1 
ATOM   1980 N  N   . ALA   A 1 244 ? -7.841  -14.601 32.98  1    17.686  ? 280 ALA   A N   1 
ATOM   1981 C  CA  . ALA   A 1 244 ? -8.4    -14.158 34.255 1    21.237  ? 280 ALA   A CA  1 
ATOM   1982 C  C   . ALA   A 1 244 ? -8.985  -12.759 34.097 1    24.22   ? 280 ALA   A C   1 
ATOM   1983 O  O   . ALA   A 1 244 ? -8.851  -11.915 34.976 1    26.982  ? 280 ALA   A O   1 
ATOM   1984 C  CB  . ALA   A 1 244 ? -7.329  -14.13  35.325 1    19.698  ? 280 ALA   A CB  1 
ATOM   1985 N  N   . GLN   A 1 245 ? -9.584  -12.486 32.944 1    24.131  ? 281 GLN   A N   1 
ATOM   1986 C  CA  . GLN   A 1 245 ? -9.939  -11.115 32.678 1    20.759  ? 281 GLN   A CA  1 
ATOM   1987 C  C   . GLN   A 1 245 ? -11.397 -10.935 33.023 1    19.839  ? 281 GLN   A C   1 
ATOM   1988 O  O   . GLN   A 1 245 ? -11.724 -9.832  33.37  1    22.266  ? 281 GLN   A O   1 
ATOM   1989 C  CB  . GLN   A 1 245 ? -9.676  -10.719 31.228 1    19.516  ? 281 GLN   A CB  1 
ATOM   1990 C  CG  . GLN   A 1 245 ? -10.839 -11.071 30.338 1    19.017  ? 281 GLN   A CG  1 
ATOM   1991 C  CD  . GLN   A 1 245 ? -10.507 -10.853 28.893 1    22.3    ? 281 GLN   A CD  1 
ATOM   1992 O  OE1 . GLN   A 1 245 ? -9.41   -11.158 28.405 1    23.113  ? 281 GLN   A OE1 1 
ATOM   1993 N  NE2 . GLN   A 1 245 ? -11.469 -10.274 28.206 1    24.853  ? 281 GLN   A NE2 1 
ATOM   1994 N  N   . THR   A 1 246 ? -12.243 -11.971 32.903 1    21.471  ? 282 THR   A N   1 
ATOM   1995 C  CA  . THR   A 1 246 ? -13.574 -11.991 33.512 1    26.031  ? 282 THR   A CA  1 
ATOM   1996 C  C   . THR   A 1 246 ? -13.641 -13.278 34.341 1    23.392  ? 282 THR   A C   1 
ATOM   1997 O  O   . THR   A 1 246 ? -13.018 -14.26  33.981 1    18.03   ? 282 THR   A O   1 
ATOM   1998 C  CB  . THR   A 1 246 ? -14.73  -11.973 32.498 1    27.032  ? 282 THR   A CB  1 
ATOM   1999 O  OG1 . THR   A 1 246 ? -14.368 -12.91  31.502 1    25.944  ? 282 THR   A OG1 1 
ATOM   2000 C  CG2 . THR   A 1 246 ? -14.798 -10.729 31.639 1    34.742  ? 282 THR   A CG2 1 
ATOM   2001 N  N   . TRP   A 1 247 ? -14.384 -13.262 35.444 1    22.636  ? 283 TRP   A N   1 
ATOM   2002 C  CA  . TRP   A 1 247 ? -14.433 -14.421 36.324 1    25.677  ? 283 TRP   A CA  1 
ATOM   2003 C  C   . TRP   A 1 247 ? -15.782 -15.15  36.343 1    29.012  ? 283 TRP   A C   1 
ATOM   2004 O  O   . TRP   A 1 247 ? -15.949 -15.944 37.267 1    25.932  ? 283 TRP   A O   1 
ATOM   2005 C  CB  . TRP   A 1 247 ? -14.103 -14.001 37.764 1    20.76   ? 283 TRP   A CB  1 
ATOM   2006 C  CG  . TRP   A 1 247 ? -12.769 -13.333 37.89  1    20.933  ? 283 TRP   A CG  1 
ATOM   2007 C  CD1 . TRP   A 1 247 ? -11.832 -13.2   36.905 1    20.119  ? 283 TRP   A CD1 1 
ATOM   2008 C  CD2 . TRP   A 1 247 ? -12.201 -12.8   39.103 1    18.991  ? 283 TRP   A CD2 1 
ATOM   2009 N  NE1 . TRP   A 1 247 ? -10.739 -12.554 37.413 1    25.356  ? 283 TRP   A NE1 1 
ATOM   2010 C  CE2 . TRP   A 1 247 ? -10.925 -12.326 38.76  1    22.228  ? 283 TRP   A CE2 1 
ATOM   2011 C  CE3 . TRP   A 1 247 ? -12.632 -12.713 40.43  1    17.418  ? 283 TRP   A CE3 1 
ATOM   2012 C  CZ2 . TRP   A 1 247 ? -10.076 -11.767 39.711 1    25.212  ? 283 TRP   A CZ2 1 
ATOM   2013 C  CZ3 . TRP   A 1 247 ? -11.801 -12.147 41.362 1    20.729  ? 283 TRP   A CZ3 1 
ATOM   2014 C  CH2 . TRP   A 1 247 ? -10.519 -11.727 41.024 1    24.209  ? 283 TRP   A CH2 1 
ATOM   2015 N  N   . SER   A 1 248 ? -16.755 -14.859 35.435 1    32.723  ? 284 SER   A N   1 
ATOM   2016 C  CA  . SER   A 1 248 ? -18.131 -15.328 35.692 1    29.504  ? 284 SER   A CA  1 
ATOM   2017 C  C   . SER   A 1 248 ? -18.288 -16.829 35.486 1    26.251  ? 284 SER   A C   1 
ATOM   2018 O  O   . SER   A 1 248 ? -19.219 -17.443 35.988 1    29.533  ? 284 SER   A O   1 
ATOM   2019 C  CB  . SER   A 1 248 ? -19.259 -14.554 35.026 1    34.187  ? 284 SER   A CB  1 
ATOM   2020 O  OG  . SER   A 1 248 ? -19.113 -14.532 33.624 1    39.258  ? 284 SER   A OG  1 
ATOM   2021 N  N   . ASN   A 1 249 ? -17.327 -17.446 34.814 1    26.511  ? 285 ASN   A N   1 
ATOM   2022 C  CA  . ASN   A 1 249 ? -17.406 -18.88  34.694 1    26.461  ? 285 ASN   A CA  1 
ATOM   2023 C  C   . ASN   A 1 249 ? -17.207 -19.58  36.023 1    25.643  ? 285 ASN   A C   1 
ATOM   2024 O  O   . ASN   A 1 249 ? -17.455 -20.771 36.036 1    31.093  ? 285 ASN   A O   1 
ATOM   2025 C  CB  . ASN   A 1 249 ? -16.523 -19.416 33.578 1    27.948  ? 285 ASN   A CB  1 
ATOM   2026 C  CG  . ASN   A 1 249 ? -17.07  -18.938 32.249 1    34.997  ? 285 ASN   A CG  1 
ATOM   2027 O  OD1 . ASN   A 1 249 ? -18.287 -18.96  32.025 1    35.313  ? 285 ASN   A OD1 1 
ATOM   2028 N  ND2 . ASN   A 1 249 ? -16.2   -18.501 31.357 1    33.927  ? 285 ASN   A ND2 1 
ATOM   2029 N  N   . ILE   A 1 250 ? -16.682 -18.928 37.082 1    22.243  ? 286 ILE   A N   1 
ATOM   2030 C  CA  . ILE   A 1 250 ? -16.561 -19.627 38.362 1    22.915  ? 286 ILE   A CA  1 
ATOM   2031 C  C   . ILE   A 1 250 ? -17.665 -19.203 39.325 1    24.306  ? 286 ILE   A C   1 
ATOM   2032 O  O   . ILE   A 1 250 ? -17.543 -19.415 40.551 1    20.117  ? 286 ILE   A O   1 
ATOM   2033 C  CB  . ILE   A 1 250 ? -15.152 -19.515 39.003 1    24.23   ? 286 ILE   A CB  1 
ATOM   2034 C  CG1 . ILE   A 1 250 ? -14.864 -18.095 39.445 1    22.355  ? 286 ILE   A CG1 1 
ATOM   2035 C  CG2 . ILE   A 1 250 ? -14.064 -20.115 38.085 1    27.58   ? 286 ILE   A CG2 1 
ATOM   2036 C  CD1 . ILE   A 1 250 ? -13.506 -17.899 40.066 1    28.933  ? 286 ILE   A CD1 1 
ATOM   2037 N  N   . TYR   A 1 251 ? -18.729 -18.594 38.754 1    24.908  ? 287 TYR   A N   1 
ATOM   2038 C  CA  . TYR   A 1 251 ? -19.872 -18.138 39.515 1    28.574  ? 287 TYR   A CA  1 
ATOM   2039 C  C   . TYR   A 1 251 ? -20.301 -19.156 40.575 1    32.479  ? 287 TYR   A C   1 
ATOM   2040 O  O   . TYR   A 1 251 ? -20.592 -18.775 41.721 1    31.145  ? 287 TYR   A O   1 
ATOM   2041 C  CB  . TYR   A 1 251 ? -21.141 -17.921 38.688 1    34.157  ? 287 TYR   A CB  1 
ATOM   2042 C  CG  . TYR   A 1 251 ? -22.338 -17.547 39.565 1    31.007  ? 287 TYR   A CG  1 
ATOM   2043 C  CD1 . TYR   A 1 251 ? -22.343 -16.352 40.283 1    27.202  ? 287 TYR   A CD1 1 
ATOM   2044 C  CD2 . TYR   A 1 251 ? -23.489 -18.358 39.643 1    37.964  ? 287 TYR   A CD2 1 
ATOM   2045 C  CE1 . TYR   A 1 251 ? -23.429 -15.96  41.058 1    29.932  ? 287 TYR   A CE1 1 
ATOM   2046 C  CE2 . TYR   A 1 251 ? -24.59  -17.953 40.405 1    36.577  ? 287 TYR   A CE2 1 
ATOM   2047 C  CZ  . TYR   A 1 251 ? -24.564 -16.749 41.109 1    32.804  ? 287 TYR   A CZ  1 
ATOM   2048 O  OH  . TYR   A 1 251 ? -25.579 -16.317 41.927 1    40.706  ? 287 TYR   A OH  1 
ATOM   2049 N  N   . ASP   A 1 252 ? -20.39  -20.422 40.144 1    28.724  ? 288 ASP   A N   1 
ATOM   2050 C  CA  . ASP   A 1 252 ? -20.936 -21.498 40.956 1    40.013  ? 288 ASP   A CA  1 
ATOM   2051 C  C   . ASP   A 1 252 ? -19.996 -21.932 42.093 1    37.782  ? 288 ASP   A C   1 
ATOM   2052 O  O   . ASP   A 1 252 ? -20.452 -22.573 43.021 1    35.61   ? 288 ASP   A O   1 
ATOM   2053 C  CB  . ASP   A 1 252 ? -21.452 -22.644 40.101 1    44.406  ? 288 ASP   A CB  1 
ATOM   2054 C  CG  . ASP   A 1 252 ? -20.444 -23.254 39.139 1    65.386  ? 288 ASP   A CG  1 
ATOM   2055 O  OD1 . ASP   A 1 252 ? -19.248 -22.892 39.231 1    62.923  ? 288 ASP   A OD1 1 
ATOM   2056 O  OD2 . ASP   A 1 252 ? -20.87  -24.067 38.283 1    75.451  ? 288 ASP   A OD2 1 
ATOM   2057 N  N   . LEU   A 1 253 ? -18.709 -21.575 42.049 1    36.994  ? 289 LEU   A N   1 
ATOM   2058 C  CA  . LEU   A 1 253 ? -17.82  -21.801 43.192 1    35.127  ? 289 LEU   A CA  1 
ATOM   2059 C  C   . LEU   A 1 253 ? -18.062 -20.763 44.286 1    32.261  ? 289 LEU   A C   1 
ATOM   2060 O  O   . LEU   A 1 253 ? -17.648 -20.999 45.436 1    31.426  ? 289 LEU   A O   1 
ATOM   2061 C  CB  . LEU   A 1 253 ? -16.335 -21.764 42.81  1    29.143  ? 289 LEU   A CB  1 
ATOM   2062 C  CG  . LEU   A 1 253 ? -15.833 -22.894 41.921 1    31.987  ? 289 LEU   A CG  1 
ATOM   2063 C  CD1 . LEU   A 1 253 ? -14.329 -22.752 41.712 1    27.864  ? 289 LEU   A CD1 1 
ATOM   2064 C  CD2 . LEU   A 1 253 ? -16.187 -24.272 42.53  1    35.624  ? 289 LEU   A CD2 1 
ATOM   2065 N  N   . VAL   A 1 254 ? -18.665 -19.613 43.899 1    29.652  ? 290 VAL   A N   1 
ATOM   2066 C  CA  . VAL   A 1 254 ? -18.712 -18.426 44.743 1    28.269  ? 290 VAL   A CA  1 
ATOM   2067 C  C   . VAL   A 1 254 ? -20.138 -17.893 44.997 1    31.122  ? 290 VAL   A C   1 
ATOM   2068 O  O   . VAL   A 1 254 ? -20.297 -16.756 45.473 1    29.839  ? 290 VAL   A O   1 
ATOM   2069 C  CB  . VAL   A 1 254 ? -17.782 -17.313 44.192 1    31.426  ? 290 VAL   A CB  1 
ATOM   2070 C  CG1 . VAL   A 1 254 ? -16.56  -17.855 43.465 1    35.858  ? 290 VAL   A CG1 1 
ATOM   2071 C  CG2 . VAL   A 1 254 ? -18.473 -16.324 43.259 1    25.11   ? 290 VAL   A CG2 1 
ATOM   2072 N  N   . VAL   A 1 255 ? -21.194 -18.668 44.705 1    31.307  ? 291 VAL   A N   1 
ATOM   2073 C  CA  . VAL   A 1 255 ? -22.567 -18.178 44.882 1    30.156  ? 291 VAL   A CA  1 
ATOM   2074 C  C   . VAL   A 1 255 ? -22.791 -17.689 46.307 1    33.594  ? 291 VAL   A C   1 
ATOM   2075 O  O   . VAL   A 1 255 ? -22.557 -18.432 47.247 1    28.254  ? 291 VAL   A O   1 
ATOM   2076 C  CB  . VAL   A 1 255 ? -23.593 -19.284 44.642 1    33.811  ? 291 VAL   A CB  1 
ATOM   2077 C  CG1 . VAL   A 1 255 ? -25.004 -18.737 44.79  1    31.278  ? 291 VAL   A CG1 1 
ATOM   2078 C  CG2 . VAL   A 1 255 ? -23.389 -19.864 43.248 1    45.242  ? 291 VAL   A CG2 1 
ATOM   2079 N  N   . PRO   A 1 256 ? -23.26  -16.432 46.514 1    34.583  ? 292 PRO   A N   1 
ATOM   2080 C  CA  . PRO   A 1 256 ? -23.542 -15.912 47.86  1    33.04   ? 292 PRO   A CA  1 
ATOM   2081 C  C   . PRO   A 1 256 ? -24.622 -16.649 48.626 1    31.949  ? 292 PRO   A C   1 
ATOM   2082 O  O   . PRO   A 1 256 ? -24.454 -16.955 49.789 1    40.082  ? 292 PRO   A O   1 
ATOM   2083 C  CB  . PRO   A 1 256 ? -23.857 -14.427 47.688 1    28.107  ? 292 PRO   A CB  1 
ATOM   2084 C  CG  . PRO   A 1 256 ? -23.243 -14.108 46.321 1    30.246  ? 292 PRO   A CG  1 
ATOM   2085 C  CD  . PRO   A 1 256 ? -23.373 -15.4   45.482 1    29.566  ? 292 PRO   A CD  1 
ATOM   2086 N  N   . PHE   A 1 257 ? -25.674 -17.001 47.91  1    35.295  ? 293 PHE   A N   1 
ATOM   2087 C  CA  . PHE   A 1 257 ? -26.907 -17.546 48.459 1    36.627  ? 293 PHE   A CA  1 
ATOM   2088 C  C   . PHE   A 1 257 ? -27.281 -18.786 47.656 1    38.784  ? 293 PHE   A C   1 
ATOM   2089 O  O   . PHE   A 1 257 ? -28.152 -18.746 46.791 1    35.253  ? 293 PHE   A O   1 
ATOM   2090 C  CB  . PHE   A 1 257 ? -27.981 -16.458 48.347 1    30.957  ? 293 PHE   A CB  1 
ATOM   2091 C  CG  . PHE   A 1 257 ? -27.845 -15.489 49.513 1    41.544  ? 293 PHE   A CG  1 
ATOM   2092 C  CD1 . PHE   A 1 257 ? -27.863 -15.961 50.843 1    40.327  ? 293 PHE   A CD1 1 
ATOM   2093 C  CD2 . PHE   A 1 257 ? -27.631 -14.128 49.289 1    39.308  ? 293 PHE   A CD2 1 
ATOM   2094 C  CE1 . PHE   A 1 257 ? -27.723 -15.08  51.913 1    37.649  ? 293 PHE   A CE1 1 
ATOM   2095 C  CE2 . PHE   A 1 257 ? -27.46  -13.256 50.363 1    43.895  ? 293 PHE   A CE2 1 
ATOM   2096 C  CZ  . PHE   A 1 257 ? -27.519 -13.731 51.668 1    43.882  ? 293 PHE   A CZ  1 
ATOM   2097 N  N   . PRO   A 1 258 ? -26.598 -19.921 47.878 1    44.226  ? 294 PRO   A N   1 
ATOM   2098 C  CA  . PRO   A 1 258 ? -26.848 -21.103 47.047 1    45.103  ? 294 PRO   A CA  1 
ATOM   2099 C  C   . PRO   A 1 258 ? -28.245 -21.665 47.298 1    45.073  ? 294 PRO   A C   1 
ATOM   2100 O  O   . PRO   A 1 258 ? -28.747 -22.41  46.487 1    45.315  ? 294 PRO   A O   1 
ATOM   2101 C  CB  . PRO   A 1 258 ? -25.741 -22.105 47.429 1    49.438  ? 294 PRO   A CB  1 
ATOM   2102 C  CG  . PRO   A 1 258 ? -25.135 -21.543 48.735 1    51.626  ? 294 PRO   A CG  1 
ATOM   2103 C  CD  . PRO   A 1 258 ? -25.636 -20.126 48.983 1    46.698  ? 294 PRO   A CD  1 
ATOM   2104 N  N   . SER   A 1 259 ? -28.887 -21.299 48.414 1    46.748  ? 295 SER   A N   1 
ATOM   2105 C  CA  . SER   A 1 259 ? -30.237 -21.79  48.668 1    53.884  ? 295 SER   A CA  1 
ATOM   2106 C  C   . SER   A 1 259 ? -31.272 -21.035 47.82  1    50.49   ? 295 SER   A C   1 
ATOM   2107 O  O   . SER   A 1 259 ? -32.458 -21.341 47.804 1    45.555  ? 295 SER   A O   1 
ATOM   2108 C  CB  . SER   A 1 259 ? -30.577 -21.736 50.148 1    50.987  ? 295 SER   A CB  1 
ATOM   2109 O  OG  . SER   A 1 259 ? -31.221 -20.493 50.414 1    72.444  ? 295 SER   A OG  1 
ATOM   2110 N  N   . ALA   A 1 260 ? -30.853 -19.987 47.127 1    54.036  ? 296 ALA   A N   1 
ATOM   2111 C  CA  . ALA   A 1 260 ? -31.786 -19.383 46.203 1    52.427  ? 296 ALA   A CA  1 
ATOM   2112 C  C   . ALA   A 1 260 ? -31.863 -20.24  44.938 1    60.673  ? 296 ALA   A C   1 
ATOM   2113 O  O   . ALA   A 1 260 ? -30.868 -20.796 44.489 1    51.676  ? 296 ALA   A O   1 
ATOM   2114 C  CB  . ALA   A 1 260 ? -31.43  -17.934 45.946 1    45.206  ? 296 ALA   A CB  1 
ATOM   2115 N  N   . PRO   A 1 261 ? -33.068 -20.447 44.362 1    77.68   ? 297 PRO   A N   1 
ATOM   2116 C  CA  . PRO   A 1 261 ? -33.175 -21.085 43.042 1    91.98   ? 297 PRO   A CA  1 
ATOM   2117 C  C   . PRO   A 1 261 ? -32.399 -20.319 41.963 1    83.622  ? 297 PRO   A C   1 
ATOM   2118 O  O   . PRO   A 1 261 ? -32.381 -19.091 41.971 1    83.095  ? 297 PRO   A O   1 
ATOM   2119 C  CB  . PRO   A 1 261 ? -34.699 -21.165 42.726 1    103.483 ? 297 PRO   A CB  1 
ATOM   2120 C  CG  . PRO   A 1 261 ? -35.409 -20.57  43.947 1    103.418 ? 297 PRO   A CG  1 
ATOM   2121 C  CD  . PRO   A 1 261 ? -34.371 -20.087 44.961 1    81.341  ? 297 PRO   A CD  1 
ATOM   2122 N  N   . SER   A 1 262 ? -31.766 -21.053 41.037 1    79.472  ? 298 SER   A N   1 
ATOM   2123 C  CA  . SER   A 1 262 ? -31.025 -20.457 39.931 1    86.37   ? 298 SER   A CA  1 
ATOM   2124 C  C   . SER   A 1 262 ? -30.981 -21.382 38.708 1    78.009  ? 298 SER   A C   1 
ATOM   2125 O  O   . SER   A 1 262 ? -30.922 -22.607 38.844 1    95.94   ? 298 SER   A O   1 
ATOM   2126 C  CB  . SER   A 1 262 ? -29.628 -20.11  40.379 1    90.017  ? 298 SER   A CB  1 
ATOM   2127 O  OG  . SER   A 1 262 ? -28.9   -21.302 40.644 1    86.785  ? 298 SER   A OG  1 
ATOM   2128 N  N   . MET   A 1 263 ? -30.956 -20.789 37.508 1    61.847  ? 299 MET   A N   1 
ATOM   2129 C  CA  . MET   A 1 263 ? -30.781 -21.552 36.276 1    65.147  ? 299 MET   A CA  1 
ATOM   2130 C  C   . MET   A 1 263 ? -29.521 -21.12  35.521 1    66.732  ? 299 MET   A C   1 
ATOM   2131 O  O   . MET   A 1 263 ? -29.278 -19.927 35.334 1    52.123  ? 299 MET   A O   1 
ATOM   2132 C  CB  . MET   A 1 263 ? -31.986 -21.403 35.342 1    57.27   ? 299 MET   A CB  1 
ATOM   2133 C  CG  . MET   A 1 263 ? -33.178 -22.253 35.734 1    53.16   ? 299 MET   A CG  1 
ATOM   2134 S  SD  . MET   A 1 263 ? -34.679 -21.874 34.806 1    57.934  ? 299 MET   A SD  1 
ATOM   2135 C  CE  . MET   A 1 263 ? -34.343 -22.265 33.068 1    36.601  ? 299 MET   A CE  1 
ATOM   2136 N  N   . ASP   A 1 264 ? -28.705 -22.094 35.087 1    68.005  ? 300 ASP   A N   1 
ATOM   2137 C  CA  . ASP   A 1 264 ? -27.636 -21.746 34.165 1    73.097  ? 300 ASP   A CA  1 
ATOM   2138 C  C   . ASP   A 1 264 ? -28.319 -21.307 32.864 1    75.411  ? 300 ASP   A C   1 
ATOM   2139 O  O   . ASP   A 1 264 ? -29.07  -22.075 32.244 1    62.892  ? 300 ASP   A O   1 
ATOM   2140 C  CB  . ASP   A 1 264 ? -26.533 -22.801 34.129 1    75.138  ? 300 ASP   A CB  1 
ATOM   2141 C  CG  . ASP   A 1 264 ? -25.233 -22.429 33.412 1    78.072  ? 300 ASP   A CG  1 
ATOM   2142 O  OD1 . ASP   A 1 264 ? -24.449 -21.608 33.942 1    60.675  ? 300 ASP   A OD1 1 
ATOM   2143 O  OD2 . ASP   A 1 264 ? -24.985 -22.988 32.324 1    91.293  ? 300 ASP   A OD2 1 
ATOM   2144 N  N   . THR   A 1 265 ? -28.125 -20.024 32.518 1    59.117  ? 301 THR   A N   1 
ATOM   2145 C  CA  . THR   A 1 265 ? -28.705 -19.469 31.307 1    54.29   ? 301 THR   A CA  1 
ATOM   2146 C  C   . THR   A 1 265 ? -28.299 -20.322 30.114 1    52.118  ? 301 THR   A C   1 
ATOM   2147 O  O   . THR   A 1 265 ? -29.136 -20.716 29.301 1    45.187  ? 301 THR   A O   1 
ATOM   2148 C  CB  . THR   A 1 265 ? -28.23  -18.036 31.118 1    60.634  ? 301 THR   A CB  1 
ATOM   2149 O  OG1 . THR   A 1 265 ? -28.59  -17.306 32.295 1    60.482  ? 301 THR   A OG1 1 
ATOM   2150 C  CG2 . THR   A 1 265 ? -28.727 -17.476 29.796 1    49.081  ? 301 THR   A CG2 1 
ATOM   2151 N  N   . THR   A 1 266 ? -26.987 -20.594 30.059 1    63.122  ? 302 THR   A N   1 
ATOM   2152 C  CA  . THR   A 1 266 ? -26.328 -21.42  29.052 1    60.918  ? 302 THR   A CA  1 
ATOM   2153 C  C   . THR   A 1 266 ? -27.034 -22.767 28.952 1    55.037  ? 302 THR   A C   1 
ATOM   2154 O  O   . THR   A 1 266 ? -27.386 -23.221 27.859 1    74.463  ? 302 THR   A O   1 
ATOM   2155 C  CB  . THR   A 1 266 ? -24.821 -21.525 29.334 1    48.212  ? 302 THR   A CB  1 
ATOM   2156 O  OG1 . THR   A 1 266 ? -24.302 -20.192 29.143 1    39.988  ? 302 THR   A OG1 1 
ATOM   2157 C  CG2 . THR   A 1 266 ? -24.173 -22.612 28.502 1    29.137  ? 302 THR   A CG2 1 
ATOM   2158 N  N   . GLU   A 1 267 ? -27.28  -23.372 30.116 1    65.021  ? 303 GLU   A N   1 
ATOM   2159 C  CA  . GLU   A 1 267 ? -28.021 -24.619 30.186 1    60.192  ? 303 GLU   A CA  1 
ATOM   2160 C  C   . GLU   A 1 267 ? -29.356 -24.455 29.446 1    51.412  ? 303 GLU   A C   1 
ATOM   2161 O  O   . GLU   A 1 267 ? -29.683 -25.286 28.603 1    51.806  ? 303 GLU   A O   1 
ATOM   2162 C  CB  . GLU   A 1 267 ? -28.03  -25.088 31.646 1    67.417  ? 303 GLU   A CB  1 
ATOM   2163 C  CG  . GLU   A 1 267 ? -28     -26.611 31.79  1    81.57   ? 303 GLU   A CG  1 
ATOM   2164 C  CD  . GLU   A 1 267 ? -28.752 -27.093 33.024 1    93.519  ? 303 GLU   A CD  1 
ATOM   2165 O  OE1 . GLU   A 1 267 ? -29.815 -27.736 32.846 1    89.715  ? 303 GLU   A OE1 1 
ATOM   2166 O  OE2 . GLU   A 1 267 ? -28.3   -26.815 34.161 1    86.837  ? 303 GLU   A OE2 1 
ATOM   2167 N  N   . ALA   A 1 268 ? -30.068 -23.335 29.692 1    43.535  ? 304 ALA   A N   1 
ATOM   2168 C  CA  . ALA   A 1 268 ? -31.445 -23.115 29.251 1    46.173  ? 304 ALA   A CA  1 
ATOM   2169 C  C   . ALA   A 1 268 ? -31.559 -22.713 27.774 1    43.304  ? 304 ALA   A C   1 
ATOM   2170 O  O   . ALA   A 1 268 ? -32.529 -23.075 27.111 1    39.545  ? 304 ALA   A O   1 
ATOM   2171 C  CB  . ALA   A 1 268 ? -32.155 -22.134 30.183 1    42.686  ? 304 ALA   A CB  1 
ATOM   2172 N  N   . MET   A 1 269 ? -30.559 -21.989 27.244 1    47.149  ? 305 MET   A N   1 
ATOM   2173 C  CA  . MET   A 1 269 ? -30.544 -21.575 25.842 1    42.402  ? 305 MET   A CA  1 
ATOM   2174 C  C   . MET   A 1 269 ? -30.487 -22.829 24.97  1    44.715  ? 305 MET   A C   1 
ATOM   2175 O  O   . MET   A 1 269 ? -31.122 -22.889 23.888 1    41.318  ? 305 MET   A O   1 
ATOM   2176 C  CB  . MET   A 1 269 ? -29.32  -20.69  25.542 1    40.114  ? 305 MET   A CB  1 
ATOM   2177 C  CG  . MET   A 1 269 ? -29.257 -19.308 26.205 1    42.757  ? 305 MET   A CG  1 
ATOM   2178 S  SD  . MET   A 1 269 ? -27.712 -18.389 25.962 1    38.802  ? 305 MET   A SD  1 
ATOM   2179 C  CE  . MET   A 1 269 ? -27.797 -18.172 24.167 1    33.424  ? 305 MET   A CE  1 
ATOM   2180 N  N   . LEU   A 1 270 ? -29.701 -23.808 25.479 1    43.229  ? 306 LEU   A N   1 
ATOM   2181 C  CA  . LEU   A 1 270 ? -29.357 -25.059 24.796 1    53.311  ? 306 LEU   A CA  1 
ATOM   2182 C  C   . LEU   A 1 270 ? -30.609 -25.937 24.647 1    51.399  ? 306 LEU   A C   1 
ATOM   2183 O  O   . LEU   A 1 270 ? -30.957 -26.292 23.524 1    48.943  ? 306 LEU   A O   1 
ATOM   2184 C  CB  . LEU   A 1 270 ? -28.171 -25.799 25.433 1    44.612  ? 306 LEU   A CB  1 
ATOM   2185 C  CG  . LEU   A 1 270 ? -26.756 -25.407 24.979 1    53.143  ? 306 LEU   A CG  1 
ATOM   2186 C  CD1 . LEU   A 1 270 ? -25.685 -26.202 25.777 1    42.794  ? 306 LEU   A CD1 1 
ATOM   2187 C  CD2 . LEU   A 1 270 ? -26.576 -25.595 23.451 1    42.258  ? 306 LEU   A CD2 1 
ATOM   2188 N  N   . LYS   A 1 271 ? -31.295 -26.201 25.781 1    51.305  ? 307 LYS   A N   1 
ATOM   2189 C  CA  . LYS   A 1 271 ? -32.638 -26.77  25.922 1    50.366  ? 307 LYS   A CA  1 
ATOM   2190 C  C   . LYS   A 1 271 ? -33.654 -26.183 24.936 1    43.413  ? 307 LYS   A C   1 
ATOM   2191 O  O   . LYS   A 1 271 ? -34.404 -26.919 24.297 1    57.761  ? 307 LYS   A O   1 
ATOM   2192 C  CB  . LYS   A 1 271 ? -33.096 -26.569 27.383 1    61.362  ? 307 LYS   A CB  1 
ATOM   2193 C  CG  . LYS   A 1 271 ? -34.252 -27.444 27.948 1    66.769  ? 307 LYS   A CG  1 
ATOM   2194 C  CD  . LYS   A 1 271 ? -33.879 -28.914 28.171 1    70.431  ? 307 LYS   A CD  1 
ATOM   2195 C  CE  . LYS   A 1 271 ? -34.997 -29.849 28.52  1    72.922  ? 307 LYS   A CE  1 
ATOM   2196 N  NZ  . LYS   A 1 271 ? -34.749 -31.202 28.005 1    67.684  ? 307 LYS   A NZ  1 
ATOM   2197 N  N   . GLN   A 1 272 ? -33.741 -24.847 24.843 1    55.116  ? 308 GLN   A N   1 
ATOM   2198 C  CA  . GLN   A 1 272 ? -34.785 -24.194 24.053 1    45.309  ? 308 GLN   A CA  1 
ATOM   2199 C  C   . GLN   A 1 272 ? -34.353 -24.043 22.603 1    47.024  ? 308 GLN   A C   1 
ATOM   2200 O  O   . GLN   A 1 272 ? -35.048 -23.388 21.826 1    46.524  ? 308 GLN   A O   1 
ATOM   2201 C  CB  . GLN   A 1 272 ? -34.959 -22.734 24.43  1    43.095  ? 308 GLN   A CB  1 
ATOM   2202 C  CG  . GLN   A 1 272 ? -35.16  -22.511 25.921 1    58.026  ? 308 GLN   A CG  1 
ATOM   2203 C  CD  . GLN   A 1 272 ? -36.596 -22.662 26.363 1    63.079  ? 308 GLN   A CD  1 
ATOM   2204 O  OE1 . GLN   A 1 272 ? -37.546 -22.185 25.724 1    55.22   ? 308 GLN   A OE1 1 
ATOM   2205 N  NE2 . GLN   A 1 272 ? -36.736 -23.348 27.482 1    69.425  ? 308 GLN   A NE2 1 
ATOM   2206 N  N   . GLY   A 1 273 ? -33.19  -24.621 22.264 1    51.953  ? 309 GLY   A N   1 
ATOM   2207 C  CA  . GLY   A 1 273 ? -32.729 -24.694 20.886 1    57.326  ? 309 GLY   A CA  1 
ATOM   2208 C  C   . GLY   A 1 273 ? -32.411 -23.327 20.277 1    51.737  ? 309 GLY   A C   1 
ATOM   2209 O  O   . GLY   A 1 273 ? -32.76  -23.098 19.13  1    47.184  ? 309 GLY   A O   1 
ATOM   2210 N  N   . TRP   A 1 274 ? -31.767 -22.434 21.053 1    44.324  ? 310 TRP   A N   1 
ATOM   2211 C  CA  . TRP   A 1 274 ? -31.267 -21.156 20.558 1    38.977  ? 310 TRP   A CA  1 
ATOM   2212 C  C   . TRP   A 1 274 ? -30.135 -21.422 19.584 1    40.901  ? 310 TRP   A C   1 
ATOM   2213 O  O   . TRP   A 1 274 ? -29.36  -22.335 19.825 1    40.755  ? 310 TRP   A O   1 
ATOM   2214 C  CB  . TRP   A 1 274 ? -30.694 -20.329 21.717 1    31.867  ? 310 TRP   A CB  1 
ATOM   2215 C  CG  . TRP   A 1 274 ? -31.77  -19.59  22.461 1    30.987  ? 310 TRP   A CG  1 
ATOM   2216 C  CD1 . TRP   A 1 274 ? -32.954 -20.093 22.923 1    31.942  ? 310 TRP   A CD1 1 
ATOM   2217 C  CD2 . TRP   A 1 274 ? -31.811 -18.181 22.734 1    30.219  ? 310 TRP   A CD2 1 
ATOM   2218 N  NE1 . TRP   A 1 274 ? -33.694 -19.125 23.538 1    28.182  ? 310 TRP   A NE1 1 
ATOM   2219 C  CE2 . TRP   A 1 274 ? -33.032 -17.935 23.423 1    28.237  ? 310 TRP   A CE2 1 
ATOM   2220 C  CE3 . TRP   A 1 274 ? -30.929 -17.12  22.465 1    29.919  ? 310 TRP   A CE3 1 
ATOM   2221 C  CZ2 . TRP   A 1 274 ? -33.404 -16.663 23.851 1    26.957  ? 310 TRP   A CZ2 1 
ATOM   2222 C  CZ3 . TRP   A 1 274 ? -31.298 -15.863 22.877 1    27.732  ? 310 TRP   A CZ3 1 
ATOM   2223 C  CH2 . TRP   A 1 274 ? -32.507 -15.646 23.567 1    34.146  ? 310 TRP   A CH2 1 
ATOM   2224 N  N   . THR   A 1 275 ? -30.019 -20.592 18.544 1    38.278  ? 311 THR   A N   1 
ATOM   2225 C  CA  . THR   A 1 275 ? -28.909 -20.652 17.593 1    40.283  ? 311 THR   A CA  1 
ATOM   2226 C  C   . THR   A 1 275 ? -28.152 -19.317 17.618 1    42.804  ? 311 THR   A C   1 
ATOM   2227 O  O   . THR   A 1 275 ? -28.621 -18.322 18.187 1    41.855  ? 311 THR   A O   1 
ATOM   2228 C  CB  . THR   A 1 275 ? -29.478 -20.91  16.193 1    33.624  ? 311 THR   A CB  1 
ATOM   2229 O  OG1 . THR   A 1 275 ? -30.452 -19.891 16.056 1    28.178  ? 311 THR   A OG1 1 
ATOM   2230 C  CG2 . THR   A 1 275 ? -30.303 -22.181 16.087 1    33.591  ? 311 THR   A CG2 1 
ATOM   2231 N  N   . PRO   A 1 276 ? -26.941 -19.218 17.02  1    41.64   ? 312 PRO   A N   1 
ATOM   2232 C  CA  . PRO   A 1 276 ? -26.349 -17.895 16.82  1    32.748  ? 312 PRO   A CA  1 
ATOM   2233 C  C   . PRO   A 1 276 ? -27.313 -16.91  16.143 1    36.67   ? 312 PRO   A C   1 
ATOM   2234 O  O   . PRO   A 1 276 ? -27.433 -15.733 16.549 1    34.9    ? 312 PRO   A O   1 
ATOM   2235 C  CB  . PRO   A 1 276 ? -25.065 -18.188 16.027 1    33.989  ? 312 PRO   A CB  1 
ATOM   2236 C  CG  . PRO   A 1 276 ? -24.722 -19.636 16.372 1    33.316  ? 312 PRO   A CG  1 
ATOM   2237 C  CD  . PRO   A 1 276 ? -26.026 -20.342 16.705 1    31.897  ? 312 PRO   A CD  1 
ATOM   2238 N  N   . ARG   A 1 277 ? -28.049 -17.392 15.134 1    33.906  ? 313 ARG   A N   1 
ATOM   2239 C  CA  . ARG   A 1 277 ? -28.964 -16.499 14.436 1    36.002  ? 313 ARG   A CA  1 
ATOM   2240 C  C   . ARG   A 1 277 ? -29.926 -15.843 15.426 1    34.347  ? 313 ARG   A C   1 
ATOM   2241 O  O   . ARG   A 1 277 ? -30.234 -14.644 15.314 1    30.066  ? 313 ARG   A O   1 
ATOM   2242 C  CB  . ARG   A 1 277 ? -29.713 -17.076 13.23  1    39.995  ? 313 ARG   A CB  1 
ATOM   2243 C  CG  . ARG   A 1 277 ? -28.674 -17.237 12.129 1    61.93   ? 313 ARG   A CG  1 
ATOM   2244 C  CD  . ARG   A 1 277 ? -29.181 -17.401 10.688 1    70.342  ? 313 ARG   A CD  1 
ATOM   2245 N  NE  . ARG   A 1 277 ? -30.356 -16.575 10.371 1    84.445  ? 313 ARG   A NE  1 
ATOM   2246 C  CZ  . ARG   A 1 277 ? -30.424 -15.665 9.394  1    85.264  ? 313 ARG   A CZ  1 
ATOM   2247 N  NH1 . ARG   A 1 277 ? -31.571 -15.042 9.119  1    65.243  ? 313 ARG   A NH1 1 
ATOM   2248 N  NH2 . ARG   A 1 277 ? -29.339 -15.409 8.678  1    79.332  ? 313 ARG   A NH2 1 
ATOM   2249 N  N   . ARG   A 1 278 ? -30.407 -16.651 16.384 1    36.137  ? 314 ARG   A N   1 
ATOM   2250 C  CA  . ARG   A 1 278 ? -31.396 -16.153 17.336 1    35.771  ? 314 ARG   A CA  1 
ATOM   2251 C  C   . ARG   A 1 278 ? -30.76  -15.088 18.223 1    34.354  ? 314 ARG   A C   1 
ATOM   2252 O  O   . ARG   A 1 278 ? -31.38  -14.031 18.405 1    36.411  ? 314 ARG   A O   1 
ATOM   2253 C  CB  . ARG   A 1 278 ? -32.208 -17.198 18.112 1    32.921  ? 314 ARG   A CB  1 
ATOM   2254 C  CG  . ARG   A 1 278 ? -33.159 -16.475 19.053 1    38.958  ? 314 ARG   A CG  1 
ATOM   2255 C  CD  . ARG   A 1 278 ? -34.455 -17.205 19.246 1    50.31   ? 314 ARG   A CD  1 
ATOM   2256 N  NE  . ARG   A 1 278 ? -35.278 -16.573 20.286 1    55.62   ? 314 ARG   A NE  1 
ATOM   2257 C  CZ  . ARG   A 1 278 ? -35.817 -17.274 21.286 1    57.745  ? 314 ARG   A CZ  1 
ATOM   2258 N  NH1 . ARG   A 1 278 ? -35.64  -18.601 21.334 1    49.381  ? 314 ARG   A NH1 1 
ATOM   2259 N  NH2 . ARG   A 1 278 ? -36.497 -16.64  22.239 1    49.803  ? 314 ARG   A NH2 1 
ATOM   2260 N  N   . MET   A 1 279 ? -29.506 -15.34  18.679 1    34.409  ? 315 MET   A N   1 
ATOM   2261 C  CA  . MET   A 1 279 ? -28.737 -14.409 19.505 1    31.415  ? 315 MET   A CA  1 
ATOM   2262 C  C   . MET   A 1 279 ? -28.612 -13.035 18.856 1    33.381  ? 315 MET   A C   1 
ATOM   2263 O  O   . MET   A 1 279 ? -28.926 -12.023 19.501 1    34.27   ? 315 MET   A O   1 
ATOM   2264 C  CB  . MET   A 1 279 ? -27.384 -15.007 19.883 1    38.826  ? 315 MET   A CB  1 
ATOM   2265 C  CG  . MET   A 1 279 ? -27.578 -16.338 20.571 1    36.509  ? 315 MET   A CG  1 
ATOM   2266 S  SD  . MET   A 1 279 ? -26.15  -17.425 20.675 1    37.94   ? 315 MET   A SD  1 
ATOM   2267 C  CE  . MET   A 1 279 ? -24.932 -16.627 21.742 1    31.421  ? 315 MET   A CE  1 
ATOM   2268 N  N   . PHE   A 1 280 ? -28.333 -13.004 17.541 1    29.994  ? 316 PHE   A N   1 
ATOM   2269 C  CA  . PHE   A 1 280 ? -28.191 -11.73  16.851 1    28.65   ? 316 PHE   A CA  1 
ATOM   2270 C  C   . PHE   A 1 280 ? -29.564 -11.119 16.59  1    28.388  ? 316 PHE   A C   1 
ATOM   2271 O  O   . PHE   A 1 280 ? -29.729 -9.888  16.678 1    25.372  ? 316 PHE   A O   1 
ATOM   2272 C  CB  . PHE   A 1 280 ? -27.292 -11.793 15.602 1    33.683  ? 316 PHE   A CB  1 
ATOM   2273 C  CG  . PHE   A 1 280 ? -25.825 -12.077 15.941 1    33.17   ? 316 PHE   A CG  1 
ATOM   2274 C  CD1 . PHE   A 1 280 ? -25.339 -13.376 16.004 1    29.532  ? 316 PHE   A CD1 1 
ATOM   2275 C  CD2 . PHE   A 1 280 ? -24.935 -11.038 16.218 1    31.757  ? 316 PHE   A CD2 1 
ATOM   2276 C  CE1 . PHE   A 1 280 ? -24.006 -13.608 16.324 1    36.624  ? 316 PHE   A CE1 1 
ATOM   2277 C  CE2 . PHE   A 1 280 ? -23.611 -11.288 16.564 1    28.552  ? 316 PHE   A CE2 1 
ATOM   2278 C  CZ  . PHE   A 1 280 ? -23.146 -12.566 16.618 1    28.546  ? 316 PHE   A CZ  1 
ATOM   2279 N  N   . LYS   A 1 281 ? -30.553 -11.971 16.282 1    30.496  ? 317 LYS   A N   1 
ATOM   2280 C  CA  . LYS   A 1 281 ? -31.92  -11.468 16.121 1    30.494  ? 317 LYS   A CA  1 
ATOM   2281 C  C   . LYS   A 1 281 ? -32.385 -10.816 17.414 1    29.326  ? 317 LYS   A C   1 
ATOM   2282 O  O   . LYS   A 1 281 ? -32.846 -9.677  17.342 1    30.797  ? 317 LYS   A O   1 
ATOM   2283 C  CB  . LYS   A 1 281 ? -32.988 -12.439 15.612 1    36.346  ? 317 LYS   A CB  1 
ATOM   2284 C  CG  . LYS   A 1 281 ? -32.83  -12.857 14.151 1    42.766  ? 317 LYS   A CG  1 
ATOM   2285 C  CD  . LYS   A 1 281 ? -33.227 -11.809 13.099 1    56.618  ? 317 LYS   A CD  1 
ATOM   2286 C  CE  . LYS   A 1 281 ? -33.101 -12.333 11.668 1    49.702  ? 317 LYS   A CE  1 
ATOM   2287 N  NZ  . LYS   A 1 281 ? -33.828 -11.509 10.702 1    40.035  ? 317 LYS   A NZ  1 
ATOM   2288 N  N   . GLU   A 1 282 ? -32.14  -11.458 18.579 1    25.503  ? 318 GLU   A N   1 
ATOM   2289 C  CA  . GLU   A 1 282 ? -32.455 -10.807 19.854 1    28.857  ? 318 GLU   A CA  1 
ATOM   2290 C  C   . GLU   A 1 282 ? -31.766 -9.455  20.034 1    34.524  ? 318 GLU   A C   1 
ATOM   2291 O  O   . GLU   A 1 282 ? -32.4   -8.48   20.499 1    34.157  ? 318 GLU   A O   1 
ATOM   2292 C  CB  . GLU   A 1 282 ? -32.198 -11.51  21.185 1    31.453  ? 318 GLU   A CB  1 
ATOM   2293 C  CG  . GLU   A 1 282 ? -33.237 -12.584 21.512 1    51.568  ? 318 GLU   A CG  1 
ATOM   2294 C  CD  . GLU   A 1 282 ? -34.742 -12.337 21.343 1    56.312  ? 318 GLU   A CD  1 
ATOM   2295 O  OE1 . GLU   A 1 282 ? -35.182 -11.212 21.67  1    53.624  ? 318 GLU   A OE1 1 
ATOM   2296 O  OE2 . GLU   A 1 282 ? -35.468 -13.282 20.915 1    56.867  ? 318 GLU   A OE2 1 
ATOM   2297 N  N   . ALA   A 1 283 ? -30.466 -9.395  19.695 1    34.338  ? 319 ALA   A N   1 
ATOM   2298 C  CA  . ALA   A 1 283 ? -29.729 -8.146  19.822 1    29.67   ? 319 ALA   A CA  1 
ATOM   2299 C  C   . ALA   A 1 283 ? -30.312 -7.052  18.899 1    28.036  ? 319 ALA   A C   1 
ATOM   2300 O  O   . ALA   A 1 283 ? -30.605 -5.966  19.373 1    29.904  ? 319 ALA   A O   1 
ATOM   2301 C  CB  . ALA   A 1 283 ? -28.239 -8.411  19.672 1    31.829  ? 319 ALA   A CB  1 
ATOM   2302 N  N   . ASP   A 1 284 ? -30.529 -7.34   17.603 1    26.844  ? 320 ASP   A N   1 
ATOM   2303 C  CA  . ASP   A 1 284 ? -31.233 -6.442  16.689 1    27.176  ? 320 ASP   A CA  1 
ATOM   2304 C  C   . ASP   A 1 284 ? -32.55  -6.005  17.29  1    28.022  ? 320 ASP   A C   1 
ATOM   2305 O  O   . ASP   A 1 284 ? -32.899 -4.831  17.168 1    36.19   ? 320 ASP   A O   1 
ATOM   2306 C  CB  . ASP   A 1 284 ? -31.631 -7.076  15.358 1    29.423  ? 320 ASP   A CB  1 
ATOM   2307 C  CG  . ASP   A 1 284 ? -31.75  -6.141  14.143 1    38.481  ? 320 ASP   A CG  1 
ATOM   2308 O  OD1 . ASP   A 1 284 ? -30.958 -5.193  14.038 1    43.595  ? 320 ASP   A OD1 1 
ATOM   2309 O  OD2 . ASP   A 1 284 ? -32.588 -6.381  13.239 1    42.516  ? 320 ASP   A OD2 1 
ATOM   2310 N  N   . ASP   A 1 285 ? -33.31  -6.939  17.885 1    26.96   ? 321 ASP   A N   1 
ATOM   2311 C  CA  . ASP   A 1 285 ? -34.594 -6.516  18.434 1    27.057  ? 321 ASP   A CA  1 
ATOM   2312 C  C   . ASP   A 1 285 ? -34.357 -5.501  19.555 1    30.17   ? 321 ASP   A C   1 
ATOM   2313 O  O   . ASP   A 1 285 ? -35.112 -4.551  19.722 1    26.902  ? 321 ASP   A O   1 
ATOM   2314 C  CB  . ASP   A 1 285 ? -35.471 -7.667  18.918 1    29.825  ? 321 ASP   A CB  1 
ATOM   2315 C  CG  . ASP   A 1 285 ? -36.865 -7.164  19.271 1    41.613  ? 321 ASP   A CG  1 
ATOM   2316 O  OD1 . ASP   A 1 285 ? -37.599 -6.765  18.324 1    53.304  ? 321 ASP   A OD1 1 
ATOM   2317 O  OD2 . ASP   A 1 285 ? -37.167 -7.043  20.463 1    34.068  ? 321 ASP   A OD2 1 
ATOM   2318 N  N   . PHE   A 1 286 ? -33.255 -5.676  20.312 1    27.711  ? 322 PHE   A N   1 
ATOM   2319 C  CA  . PHE   A 1 286 ? -33.082 -4.766  21.415 1    27.316  ? 322 PHE   A CA  1 
ATOM   2320 C  C   . PHE   A 1 286 ? -32.783 -3.383  20.848 1    30.468  ? 322 PHE   A C   1 
ATOM   2321 O  O   . PHE   A 1 286 ? -33.418 -2.4    21.25  1    31.228  ? 322 PHE   A O   1 
ATOM   2322 C  CB  . PHE   A 1 286 ? -32.061 -5.302  22.424 1    29.024  ? 322 PHE   A CB  1 
ATOM   2323 C  CG  . PHE   A 1 286 ? -32.228 -4.626  23.776 1    29.194  ? 322 PHE   A CG  1 
ATOM   2324 C  CD1 . PHE   A 1 286 ? -32.212 -3.244  23.894 1    27.054  ? 322 PHE   A CD1 1 
ATOM   2325 C  CD2 . PHE   A 1 286 ? -32.392 -5.373  24.938 1    28.267  ? 322 PHE   A CD2 1 
ATOM   2326 C  CE1 . PHE   A 1 286 ? -32.336 -2.639  25.139 1    29.101  ? 322 PHE   A CE1 1 
ATOM   2327 C  CE2 . PHE   A 1 286 ? -32.557 -4.743  26.158 1    31.161  ? 322 PHE   A CE2 1 
ATOM   2328 C  CZ  . PHE   A 1 286 ? -32.512 -3.386  26.266 1    29.29   ? 322 PHE   A CZ  1 
ATOM   2329 N  N   . PHE   A 1 287 ? -31.819 -3.321  19.909 1    25.622  ? 323 PHE   A N   1 
ATOM   2330 C  CA  . PHE   A 1 287 ? -31.544 -2.069  19.242 1    27.858  ? 323 PHE   A CA  1 
ATOM   2331 C  C   . PHE   A 1 287 ? -32.87  -1.467  18.726 1    28.708  ? 323 PHE   A C   1 
ATOM   2332 O  O   . PHE   A 1 287 ? -33.196 -0.335  19.086 1    30.196  ? 323 PHE   A O   1 
ATOM   2333 C  CB  . PHE   A 1 287 ? -30.369 -2.074  18.251 1    22.965  ? 323 PHE   A CB  1 
ATOM   2334 C  CG  . PHE   A 1 287 ? -28.982 -2.199  18.871 1    26.074  ? 323 PHE   A CG  1 
ATOM   2335 C  CD1 . PHE   A 1 287 ? -28.408 -3.454  19.114 1    25.449  ? 323 PHE   A CD1 1 
ATOM   2336 C  CD2 . PHE   A 1 287 ? -28.262 -1.059  19.26  1    25.788  ? 323 PHE   A CD2 1 
ATOM   2337 C  CE1 . PHE   A 1 287 ? -27.149 -3.566  19.672 1    21.381  ? 323 PHE   A CE1 1 
ATOM   2338 C  CE2 . PHE   A 1 287 ? -26.996 -1.169  19.805 1    22.011  ? 323 PHE   A CE2 1 
ATOM   2339 C  CZ  . PHE   A 1 287 ? -26.448 -2.43   20.006 1    23.851  ? 323 PHE   A CZ  1 
ATOM   2340 N  N   . THR   A 1 288 ? -33.646 -2.169  17.877 1    33.233  ? 324 THR   A N   1 
ATOM   2341 C  CA  . THR   A 1 288 ? -34.823 -1.471  17.331 1    40.006  ? 324 THR   A CA  1 
ATOM   2342 C  C   . THR   A 1 288 ? -35.853 -1.085  18.406 1    36.504  ? 324 THR   A C   1 
ATOM   2343 O  O   . THR   A 1 288 ? -36.501 -0.063  18.232 1    32.309  ? 324 THR   A O   1 
ATOM   2344 C  CB  . THR   A 1 288 ? -35.479 -2.108  16.11  1    38.303  ? 324 THR   A CB  1 
ATOM   2345 O  OG1 . THR   A 1 288 ? -35.812 -3.377  16.658 1    44.657  ? 324 THR   A OG1 1 
ATOM   2346 C  CG2 . THR   A 1 288 ? -34.576 -2.088  14.886 1    39.369  ? 324 THR   A CG2 1 
ATOM   2347 N  N   . SER   A 1 289 ? -35.914 -1.8    19.546 1    30.802  ? 325 SER   A N   1 
ATOM   2348 C  CA  . SER   A 1 289 ? -36.866 -1.465  20.597 1    30.495  ? 325 SER   A CA  1 
ATOM   2349 C  C   . SER   A 1 289 ? -36.653 -0.05   21.107 1    34.135  ? 325 SER   A C   1 
ATOM   2350 O  O   . SER   A 1 289 ? -37.604 0.562   21.602 1    34.977  ? 325 SER   A O   1 
ATOM   2351 C  CB  . SER   A 1 289 ? -36.801 -2.427  21.731 1    29.626  ? 325 SER   A CB  1 
ATOM   2352 O  OG  . SER   A 1 289 ? -36.08  -1.906  22.855 1    30.017  ? 325 SER   A OG  1 
ATOM   2353 N  N   . LEU   A 1 290 ? -35.397 0.435   21.009 1    29.275  ? 326 LEU   A N   1 
ATOM   2354 C  CA  . LEU   A 1 290 ? -35.006 1.77    21.468 1    28.872  ? 326 LEU   A CA  1 
ATOM   2355 C  C   . LEU   A 1 290 ? -35.243 2.789   20.354 1    32.462  ? 326 LEU   A C   1 
ATOM   2356 O  O   . LEU   A 1 290 ? -34.959 3.968   20.547 1    28.975  ? 326 LEU   A O   1 
ATOM   2357 C  CB  . LEU   A 1 290 ? -33.551 1.89    21.931 1    26.957  ? 326 LEU   A CB  1 
ATOM   2358 C  CG  . LEU   A 1 290 ? -33.098 0.904   23.009 1    28.505  ? 326 LEU   A CG  1 
ATOM   2359 C  CD1 . LEU   A 1 290 ? -31.662 1.172   23.214 1    24.731  ? 326 LEU   A CD1 1 
ATOM   2360 C  CD2 . LEU   A 1 290 ? -33.892 0.921   24.373 1    27.35   ? 326 LEU   A CD2 1 
ATOM   2361 N  N   . GLY   A 1 291 ? -35.732 2.361   19.178 1    25.999  ? 327 GLY   A N   1 
ATOM   2362 C  CA  . GLY   A 1 291 ? -35.853 3.375   18.144 1    32.358  ? 327 GLY   A CA  1 
ATOM   2363 C  C   . GLY   A 1 291 ? -34.572 3.55    17.314 1    35.961  ? 327 GLY   A C   1 
ATOM   2364 O  O   . GLY   A 1 291 ? -34.595 4.385   16.413 1    39.769  ? 327 GLY   A O   1 
ATOM   2365 N  N   . LEU   A 1 292 ? -33.524 2.709   17.555 1    32.533  ? 328 LEU   A N   1 
ATOM   2366 C  CA  . LEU   A 1 292 ? -32.257 2.675   16.825 1    33.987  ? 328 LEU   A CA  1 
ATOM   2367 C  C   . LEU   A 1 292 ? -32.429 1.961   15.479 1    36.079  ? 328 LEU   A C   1 
ATOM   2368 O  O   . LEU   A 1 292 ? -33.495 1.384   15.244 1    33.358  ? 328 LEU   A O   1 
ATOM   2369 C  CB  . LEU   A 1 292 ? -31.085 2.108   17.637 1    27.913  ? 328 LEU   A CB  1 
ATOM   2370 C  CG  . LEU   A 1 292 ? -30.828 2.872   18.943 1    28.254  ? 328 LEU   A CG  1 
ATOM   2371 C  CD1 . LEU   A 1 292 ? -29.964 2.135   19.893 1    28.58   ? 328 LEU   A CD1 1 
ATOM   2372 C  CD2 . LEU   A 1 292 ? -30.256 4.271   18.735 1    28.791  ? 328 LEU   A CD2 1 
ATOM   2373 N  N   . LEU   A 1 293 ? -31.35  1.958   14.656 1    29.646  ? 329 LEU   A N   1 
ATOM   2374 C  CA  . LEU   A 1 293 ? -31.398 1.383   13.318 1    26.683  ? 329 LEU   A CA  1 
ATOM   2375 C  C   . LEU   A 1 293 ? -31.349 -0.135  13.378 1    34.152  ? 329 LEU   A C   1 
ATOM   2376 O  O   . LEU   A 1 293 ? -30.644 -0.716  14.199 1    35.392  ? 329 LEU   A O   1 
ATOM   2377 C  CB  . LEU   A 1 293 ? -30.289 1.931   12.427 1    26.88   ? 329 LEU   A CB  1 
ATOM   2378 C  CG  . LEU   A 1 293 ? -30.311 3.448   12.307 1    30.752  ? 329 LEU   A CG  1 
ATOM   2379 C  CD1 . LEU   A 1 293 ? -28.982 4.002   11.844 1    28.545  ? 329 LEU   A CD1 1 
ATOM   2380 C  CD2 . LEU   A 1 293 ? -31.546 3.858   11.42  1    30.122  ? 329 LEU   A CD2 1 
ATOM   2381 N  N   . PRO   A 1 294 ? -32.132 -0.823  12.508 1    37.721  ? 330 PRO   A N   1 
ATOM   2382 C  CA  . PRO   A 1 294 ? -31.927 -2.253  12.251 1    34.391  ? 330 PRO   A CA  1 
ATOM   2383 C  C   . PRO   A 1 294 ? -30.701 -2.482  11.377 1    38.214  ? 330 PRO   A C   1 
ATOM   2384 O  O   . PRO   A 1 294 ? -30.361 -1.622  10.547 1    37.505  ? 330 PRO   A O   1 
ATOM   2385 C  CB  . PRO   A 1 294 ? -33.209 -2.696  11.501 1    33.232  ? 330 PRO   A CB  1 
ATOM   2386 C  CG  . PRO   A 1 294 ? -33.752 -1.407  10.92  1    35.127  ? 330 PRO   A CG  1 
ATOM   2387 C  CD  . PRO   A 1 294 ? -33.285 -0.251  11.785 1    32.458  ? 330 PRO   A CD  1 
ATOM   2388 N  N   . VAL   A 1 295 ? -30.1   -3.675  11.491 1    28.641  ? 331 VAL   A N   1 
ATOM   2389 C  CA  . VAL   A 1 295 ? -29.126 -3.959  10.464 1    35.893  ? 331 VAL   A CA  1 
ATOM   2390 C  C   . VAL   A 1 295 ? -29.859 -4.212  9.133  1    38.644  ? 331 VAL   A C   1 
ATOM   2391 O  O   . VAL   A 1 295 ? -30.939 -4.801  9.136  1    38.281  ? 331 VAL   A O   1 
ATOM   2392 C  CB  . VAL   A 1 295 ? -28.268 -5.157  10.889 1    31.957  ? 331 VAL   A CB  1 
ATOM   2393 C  CG1 . VAL   A 1 295 ? -27.362 -4.85   12.087 1    27.412  ? 331 VAL   A CG1 1 
ATOM   2394 C  CG2 . VAL   A 1 295 ? -29.143 -6.379  11.081 1    25.876  ? 331 VAL   A CG2 1 
ATOM   2395 N  N   . PRO   A 1 296 ? -29.264 -3.829  7.968  1    37.49   ? 332 PRO   A N   1 
ATOM   2396 C  CA  . PRO   A 1 296 ? -29.847 -4.081  6.641  1    36.453  ? 332 PRO   A CA  1 
ATOM   2397 C  C   . PRO   A 1 296 ? -29.943 -5.583  6.427  1    39.471  ? 332 PRO   A C   1 
ATOM   2398 O  O   . PRO   A 1 296 ? -29.179 -6.312  7.06   1    39.614  ? 332 PRO   A O   1 
ATOM   2399 C  CB  . PRO   A 1 296 ? -28.885 -3.473  5.58   1    31.122  ? 332 PRO   A CB  1 
ATOM   2400 C  CG  . PRO   A 1 296 ? -27.637 -3.158  6.352  1    36.974  ? 332 PRO   A CG  1 
ATOM   2401 C  CD  . PRO   A 1 296 ? -27.937 -3.198  7.862  1    34.213  ? 332 PRO   A CD  1 
ATOM   2402 N  N   . PRO   A 1 297 ? -30.871 -6.045  5.54   1    41.28   ? 333 PRO   A N   1 
ATOM   2403 C  CA  . PRO   A 1 297 ? -30.891 -7.431  5.013  1    38.118  ? 333 PRO   A CA  1 
ATOM   2404 C  C   . PRO   A 1 297 ? -29.56  -8.062  4.572  1    41.008  ? 333 PRO   A C   1 
ATOM   2405 O  O   . PRO   A 1 297 ? -29.275 -9.254  4.816  1    41.906  ? 333 PRO   A O   1 
ATOM   2406 C  CB  . PRO   A 1 297 ? -31.887 -7.256  3.783  1    44.311  ? 333 PRO   A CB  1 
ATOM   2407 C  CG  . PRO   A 1 297 ? -32.86  -6.129  4.165  1    39.048  ? 333 PRO   A CG  1 
ATOM   2408 C  CD  . PRO   A 1 297 ? -31.99  -5.216  5.037  1    38.291  ? 333 PRO   A CD  1 
ATOM   2409 N  N   . GLU   A 1 298 ? -28.726 -7.247  3.899  1    43.201  ? 334 GLU   A N   1 
ATOM   2410 C  CA  . GLU   A 1 298 ? -27.395 -7.664  3.486  1    40.358  ? 334 GLU   A CA  1 
ATOM   2411 C  C   . GLU   A 1 298 ? -26.613 -8.26   4.672  1    42.975  ? 334 GLU   A C   1 
ATOM   2412 O  O   . GLU   A 1 298 ? -25.952 -9.294  4.528  1    36.096  ? 334 GLU   A O   1 
ATOM   2413 C  CB  . GLU   A 1 298 ? -26.764 -6.414  2.882  1    46.075  ? 334 GLU   A CB  1 
ATOM   2414 C  CG  . GLU   A 1 298 ? -25.724 -6.764  1.824  1    56.961  ? 334 GLU   A CG  1 
ATOM   2415 C  CD  . GLU   A 1 298 ? -24.827 -5.671  1.266  1    61.368  ? 334 GLU   A CD  1 
ATOM   2416 O  OE1 . GLU   A 1 298 ? -25.333 -4.57   0.931  1    56.241  ? 334 GLU   A OE1 1 
ATOM   2417 O  OE2 . GLU   A 1 298 ? -23.607 -5.953  1.123  1    60.004  ? 334 GLU   A OE2 1 
ATOM   2418 N  N   . PHE   A 1 299 ? -26.73  -7.646  5.872  1    41.245  ? 335 PHE   A N   1 
ATOM   2419 C  CA  . PHE   A 1 299 ? -26.011 -8.101  7.066  1    35.447  ? 335 PHE   A CA  1 
ATOM   2420 C  C   . PHE   A 1 299 ? -26.282 -9.572  7.369  1    33.272  ? 335 PHE   A C   1 
ATOM   2421 O  O   . PHE   A 1 299 ? -25.377 -10.313 7.714  1    30.18   ? 335 PHE   A O   1 
ATOM   2422 C  CB  . PHE   A 1 299 ? -26.383 -7.27   8.288  1    33.647  ? 335 PHE   A CB  1 
ATOM   2423 C  CG  . PHE   A 1 299 ? -25.886 -7.839  9.611  1    32.841  ? 335 PHE   A CG  1 
ATOM   2424 C  CD1 . PHE   A 1 299 ? -26.512 -8.925  10.212 1    33.103  ? 335 PHE   A CD1 1 
ATOM   2425 C  CD2 . PHE   A 1 299 ? -24.853 -7.223  10.305 1    31.131  ? 335 PHE   A CD2 1 
ATOM   2426 C  CE1 . PHE   A 1 299 ? -26.065 -9.399  11.444 1    34.793  ? 335 PHE   A CE1 1 
ATOM   2427 C  CE2 . PHE   A 1 299 ? -24.407 -7.704  11.53  1    27.067  ? 335 PHE   A CE2 1 
ATOM   2428 C  CZ  . PHE   A 1 299 ? -25.004 -8.796  12.104 1    27.516  ? 335 PHE   A CZ  1 
ATOM   2429 N  N   . TRP   A 1 300 ? -27.543 -10.017 7.233  1    44.048  ? 336 TRP   A N   1 
ATOM   2430 C  CA  . TRP   A 1 300 ? -27.862 -11.422 7.464  1    36.749  ? 336 TRP   A CA  1 
ATOM   2431 C  C   . TRP   A 1 300 ? -27.328 -12.305 6.333  1    40.721  ? 336 TRP   A C   1 
ATOM   2432 O  O   . TRP   A 1 300 ? -26.791 -13.375 6.627  1    40.296  ? 336 TRP   A O   1 
ATOM   2433 C  CB  . TRP   A 1 300 ? -29.372 -11.559 7.646  1    33.634  ? 336 TRP   A CB  1 
ATOM   2434 C  CG  . TRP   A 1 300 ? -29.903 -10.705 8.763  1    32.869  ? 336 TRP   A CG  1 
ATOM   2435 C  CD1 . TRP   A 1 300 ? -30.639 -9.561  8.628  1    43.067  ? 336 TRP   A CD1 1 
ATOM   2436 C  CD2 . TRP   A 1 300 ? -29.771 -10.92  10.188 1    35.502  ? 336 TRP   A CD2 1 
ATOM   2437 N  NE1 . TRP   A 1 300 ? -30.999 -9.053  9.859  1    46.757  ? 336 TRP   A NE1 1 
ATOM   2438 C  CE2 . TRP   A 1 300 ? -30.469 -9.858  10.841 1    43.371  ? 336 TRP   A CE2 1 
ATOM   2439 C  CE3 . TRP   A 1 300 ? -29.131 -11.877 10.986 1    35.333  ? 336 TRP   A CE3 1 
ATOM   2440 C  CZ2 . TRP   A 1 300 ? -30.524 -9.726  12.236 1    31.393  ? 336 TRP   A CZ2 1 
ATOM   2441 C  CZ3 . TRP   A 1 300 ? -29.248 -11.773 12.362 1    32.254  ? 336 TRP   A CZ3 1 
ATOM   2442 C  CH2 . TRP   A 1 300 ? -29.925 -10.716 12.974 1    27.013  ? 336 TRP   A CH2 1 
ATOM   2443 N  N   . GLN   A 1 301 ? -27.394 -11.834 5.059  1    38.734  ? 337 GLN   A N   1 
ATOM   2444 C  CA  . GLN   A 1 301 ? -26.82  -12.605 3.962  1    40.48   ? 337 GLN   A CA  1 
ATOM   2445 C  C   . GLN   A 1 301 ? -25.331 -12.739 4.201  1    36.81   ? 337 GLN   A C   1 
ATOM   2446 O  O   . GLN   A 1 301 ? -24.774 -13.796 3.953  1    38.361  ? 337 GLN   A O   1 
ATOM   2447 C  CB  . GLN   A 1 301 ? -26.628 -12.019 2.555  1    50.51   ? 337 GLN   A CB  1 
ATOM   2448 C  CG  . GLN   A 1 301 ? -27.801 -11.225 1.993  1    68.581  ? 337 GLN   A CG  1 
ATOM   2449 C  CD  . GLN   A 1 301 ? -28.937 -12.135 1.601  1    76.013  ? 337 GLN   A CD  1 
ATOM   2450 O  OE1 . GLN   A 1 301 ? -29.213 -13.128 2.292  1    71.545  ? 337 GLN   A OE1 1 
ATOM   2451 N  NE2 . GLN   A 1 301 ? -29.572 -11.816 0.48   1    71.276  ? 337 GLN   A NE2 1 
ATOM   2452 N  N   . LYS   A 1 302 ? -24.667 -11.652 4.614  1    33.279  ? 338 LYS   A N   1 
ATOM   2453 C  CA  . LYS   A 1 302 ? -23.232 -11.683 4.407  1    41.237  ? 338 LYS   A CA  1 
ATOM   2454 C  C   . LYS   A 1 302 ? -22.45  -12.038 5.672  1    38.039  ? 338 LYS   A C   1 
ATOM   2455 O  O   . LYS   A 1 302 ? -21.303 -12.426 5.529  1    38.557  ? 338 LYS   A O   1 
ATOM   2456 C  CB  . LYS   A 1 302 ? -22.739 -10.458 3.626  1    55.445  ? 338 LYS   A CB  1 
ATOM   2457 C  CG  . LYS   A 1 302 ? -23.11  -10.439 2.156  1    50.504  ? 338 LYS   A CG  1 
ATOM   2458 C  CD  . LYS   A 1 302 ? -22.496 -9.213  1.498  1    60.747  ? 338 LYS   A CD  1 
ATOM   2459 C  CE  . LYS   A 1 302 ? -22.917 -9.078  0.066  1    63.195  ? 338 LYS   A CE  1 
ATOM   2460 N  NZ  . LYS   A 1 302 ? -22.386 -7.833  -0.509 1    74.619  ? 338 LYS   A NZ  1 
ATOM   2461 N  N   . SER   A 1 303 ? -23.02  -11.895 6.887  1    37.075  ? 339 SER   A N   1 
ATOM   2462 C  CA  . SER   A 1 303 ? -22.226 -12.132 8.104  1    35.222  ? 339 SER   A CA  1 
ATOM   2463 C  C   . SER   A 1 303 ? -21.875 -13.606 8.24   1    34.832  ? 339 SER   A C   1 
ATOM   2464 O  O   . SER   A 1 303 ? -22.573 -14.443 7.7    1    38.408  ? 339 SER   A O   1 
ATOM   2465 C  CB  . SER   A 1 303 ? -22.901 -11.67  9.371  1    29.397  ? 339 SER   A CB  1 
ATOM   2466 O  OG  . SER   A 1 303 ? -23.02  -10.256 9.372  1    33.563  ? 339 SER   A OG  1 
ATOM   2467 N  N   . MET   A 1 304 ? -20.797 -13.888 8.976  1    33.541  ? 340 MET   A N   1 
ATOM   2468 C  CA  . MET   A 1 304 ? -20.406 -15.212 9.397  1    31.582  ? 340 MET   A CA  1 
ATOM   2469 C  C   . MET   A 1 304 ? -20.605 -15.304 10.922 1    39.744  ? 340 MET   A C   1 
ATOM   2470 O  O   . MET   A 1 304 ? -19.709 -14.957 11.7   1    39.038  ? 340 MET   A O   1 
ATOM   2471 C  CB  . MET   A 1 304 ? -18.935 -15.449 9.051  1    27.04   ? 340 MET   A CB  1 
ATOM   2472 C  CG  . MET   A 1 304 ? -18.411 -16.859 9.337  1    28.094  ? 340 MET   A CG  1 
ATOM   2473 S  SD  . MET   A 1 304 ? -16.614 -17.011 9.497  1    41.107  ? 340 MET   A SD  1 
ATOM   2474 C  CE  . MET   A 1 304 ? -16.382 -16.753 11.262 1    38.408  ? 340 MET   A CE  1 
ATOM   2475 N  N   . LEU   A 1 305 ? -21.761 -15.861 11.341 1    42.493  ? 341 LEU   A N   1 
ATOM   2476 C  CA  . LEU   A 1 305 ? -22.18  -15.849 12.735 1    33.235  ? 341 LEU   A CA  1 
ATOM   2477 C  C   . LEU   A 1 305 ? -21.919 -17.196 13.416 1    39.14   ? 341 LEU   A C   1 
ATOM   2478 O  O   . LEU   A 1 305 ? -22.197 -17.326 14.612 1    45.868  ? 341 LEU   A O   1 
ATOM   2479 C  CB  . LEU   A 1 305 ? -23.659 -15.513 12.728 1    28.156  ? 341 LEU   A CB  1 
ATOM   2480 C  CG  . LEU   A 1 305 ? -24.056 -14.204 12.042 1    30.161  ? 341 LEU   A CG  1 
ATOM   2481 C  CD1 . LEU   A 1 305 ? -25.535 -13.896 12.119 1    26.433  ? 341 LEU   A CD1 1 
ATOM   2482 C  CD2 . LEU   A 1 305 ? -23.272 -13.043 12.616 1    32.4    ? 341 LEU   A CD2 1 
ATOM   2483 N  N   . GLU   A 1 306 ? -21.382 -18.187 12.675 1    35.883  ? 342 GLU   A N   1 
ATOM   2484 C  CA  . GLU   A 1 306 ? -20.854 -19.404 13.29  1    40.707  ? 342 GLU   A CA  1 
ATOM   2485 C  C   . GLU   A 1 306 ? -19.555 -19.832 12.618 1    40.278  ? 342 GLU   A C   1 
ATOM   2486 O  O   . GLU   A 1 306 ? -19.394 -19.582 11.438 1    50.342  ? 342 GLU   A O   1 
ATOM   2487 C  CB  . GLU   A 1 306 ? -21.793 -20.616 13.273 1    44.373  ? 342 GLU   A CB  1 
ATOM   2488 C  CG  . GLU   A 1 306 ? -22.747 -20.654 12.082 1    56.97   ? 342 GLU   A CG  1 
ATOM   2489 C  CD  . GLU   A 1 306 ? -23.96  -21.525 12.409 1    71.941  ? 342 GLU   A CD  1 
ATOM   2490 O  OE1 . GLU   A 1 306 ? -25.047 -20.914 12.59  1    70.05   ? 342 GLU   A OE1 1 
ATOM   2491 O  OE2 . GLU   A 1 306 ? -23.845 -22.782 12.514 1    60.311  ? 342 GLU   A OE2 1 
ATOM   2492 N  N   . LYS   A 1 307 ? -18.672 -20.523 13.36  1    44.476  ? 343 LYS   A N   1 
ATOM   2493 C  CA  . LYS   A 1 307 ? -17.491 -21.164 12.811 1    42.791  ? 343 LYS   A CA  1 
ATOM   2494 C  C   . LYS   A 1 307 ? -17.938 -22.028 11.644 1    52.702  ? 343 LYS   A C   1 
ATOM   2495 O  O   . LYS   A 1 307 ? -18.778 -22.89  11.839 1    53.523  ? 343 LYS   A O   1 
ATOM   2496 C  CB  . LYS   A 1 307 ? -16.887 -22.106 13.85  1    38.498  ? 343 LYS   A CB  1 
ATOM   2497 C  CG  . LYS   A 1 307 ? -15.671 -22.745 13.207 1    47.458  ? 343 LYS   A CG  1 
ATOM   2498 C  CD  . LYS   A 1 307 ? -14.84  -23.656 14.098 1    55.488  ? 343 LYS   A CD  1 
ATOM   2499 C  CE  . LYS   A 1 307 ? -14.072 -23.027 15.225 1    57.422  ? 343 LYS   A CE  1 
ATOM   2500 N  NZ  . LYS   A 1 307 ? -12.613 -23.11  15.093 1    46.868  ? 343 LYS   A NZ  1 
ATOM   2501 N  N   . PRO   A 1 308 ? -17.491 -21.826 10.38  1    76.56   ? 344 PRO   A N   1 
ATOM   2502 C  CA  . PRO   A 1 308 ? -18.129 -22.545 9.276  1    84.171  ? 344 PRO   A CA  1 
ATOM   2503 C  C   . PRO   A 1 308 ? -17.527 -23.95  9.432  1    89.937  ? 344 PRO   A C   1 
ATOM   2504 O  O   . PRO   A 1 308 ? -16.565 -24.154 10.19  1    76.146  ? 344 PRO   A O   1 
ATOM   2505 C  CB  . PRO   A 1 308 ? -17.661 -21.753 8.041  1    75.739  ? 344 PRO   A CB  1 
ATOM   2506 C  CG  . PRO   A 1 308 ? -16.259 -21.324 8.436  1    69.521  ? 344 PRO   A CG  1 
ATOM   2507 C  CD  . PRO   A 1 308 ? -16.298 -21.079 9.95   1    65.516  ? 344 PRO   A CD  1 
ATOM   2508 N  N   . THR   A 1 309 ? -18.134 -24.927 8.749  1    83.043  ? 345 THR   A N   1 
ATOM   2509 C  CA  . THR   A 1 309 ? -17.885 -26.337 9.012  1    74.033  ? 345 THR   A CA  1 
ATOM   2510 C  C   . THR   A 1 309 ? -16.763 -26.899 8.111  1    79.509  ? 345 THR   A C   1 
ATOM   2511 O  O   . THR   A 1 309 ? -16.121 -27.86  8.53   1    57.554  ? 345 THR   A O   1 
ATOM   2512 C  CB  . THR   A 1 309 ? -19.218 -27.084 8.875  1    66.855  ? 345 THR   A CB  1 
ATOM   2513 O  OG1 . THR   A 1 309 ? -19.536 -27.009 7.486  1    71.425  ? 345 THR   A OG1 1 
ATOM   2514 C  CG2 . THR   A 1 309 ? -20.376 -26.442 9.629  1    59.638  ? 345 THR   A CG2 1 
ATOM   2515 N  N   . ASP   A 1 310 ? -16.485 -26.284 6.924  1    86.697  ? 346 ASP   A N   1 
ATOM   2516 C  CA  . ASP   A 1 310 ? -15.754 -26.863 5.784  1    81.173  ? 346 ASP   A CA  1 
ATOM   2517 C  C   . ASP   A 1 310 ? -14.248 -26.588 5.818  1    87.48   ? 346 ASP   A C   1 
ATOM   2518 O  O   . ASP   A 1 310 ? -13.739 -25.965 4.884  1    83.852  ? 346 ASP   A O   1 
ATOM   2519 C  CB  . ASP   A 1 310 ? -16.19  -26.288 4.439  1    87.134  ? 346 ASP   A CB  1 
ATOM   2520 C  CG  . ASP   A 1 310 ? -17.569 -25.636 4.386  1    99.386  ? 346 ASP   A CG  1 
ATOM   2521 O  OD1 . ASP   A 1 310 ? -18.589 -26.359 4.597  1    72.118  ? 346 ASP   A OD1 1 
ATOM   2522 O  OD2 . ASP   A 1 310 ? -17.609 -24.4   4.147  1    92.208  ? 346 ASP   A OD2 1 
ATOM   2523 N  N   . GLY   A 1 311 ? -13.584 -27.044 6.905  1    92.727  ? 347 GLY   A N   1 
ATOM   2524 C  CA  . GLY   A 1 311 ? -12.15  -27.051 7.204  1    101.682 ? 347 GLY   A CA  1 
ATOM   2525 C  C   . GLY   A 1 311 ? -11.318 -25.867 6.68   1    120.086 ? 347 GLY   A C   1 
ATOM   2526 O  O   . GLY   A 1 311 ? -10.502 -26.082 5.785  1    113.185 ? 347 GLY   A O   1 
ATOM   2527 N  N   . ARG   A 1 312 ? -11.42  -24.676 7.323  1    110.555 ? 348 ARG   A N   1 
ATOM   2528 C  CA  . ARG   A 1 312 ? -10.964 -23.384 6.798  1    77.329  ? 348 ARG   A CA  1 
ATOM   2529 C  C   . ARG   A 1 312 ? -9.624  -22.894 7.4    1    60.357  ? 348 ARG   A C   1 
ATOM   2530 O  O   . ARG   A 1 312 ? -9.444  -22.996 8.616  1    59.632  ? 348 ARG   A O   1 
ATOM   2531 C  CB  . ARG   A 1 312 ? -12.042 -22.289 6.765  1    58.086  ? 348 ARG   A CB  1 
ATOM   2532 C  CG  . ARG   A 1 312 ? -12.507 -21.978 5.348  1    56.556  ? 348 ARG   A CG  1 
ATOM   2533 C  CD  . ARG   A 1 312 ? -13.847 -22.506 4.881  1    67.64   ? 348 ARG   A CD  1 
ATOM   2534 N  NE  . ARG   A 1 312 ? -14.802 -21.493 5.354  1    78.993  ? 348 ARG   A NE  1 
ATOM   2535 C  CZ  . ARG   A 1 312 ? -15.574 -20.691 4.62   1    71.014  ? 348 ARG   A CZ  1 
ATOM   2536 N  NH1 . ARG   A 1 312 ? -16.275 -19.725 5.197  1    67.499  ? 348 ARG   A NH1 1 
ATOM   2537 N  NH2 . ARG   A 1 312 ? -15.617 -20.842 3.308  1    64.523  ? 348 ARG   A NH2 1 
ATOM   2538 N  N   . VAL   A 1 314 ? -9.871  -19.876 9.291  1    51.892  ? 350 VAL   A N   1 
ATOM   2539 C  CA  . VAL   A 1 314 ? -10.686 -18.713 9.786  1    53.766  ? 350 VAL   A CA  1 
ATOM   2540 C  C   . VAL   A 1 314 ? -10.097 -18.128 11.076 1    58.118  ? 350 VAL   A C   1 
ATOM   2541 O  O   . VAL   A 1 314 ? -9.439  -18.84  11.858 1    45.367  ? 350 VAL   A O   1 
ATOM   2542 C  CB  . VAL   A 1 314 ? -12.23  -18.691 9.848  1    45.573  ? 350 VAL   A CB  1 
ATOM   2543 C  CG1 . VAL   A 1 314 ? -12.884 -19.482 8.72   1    44.912  ? 350 VAL   A CG1 1 
ATOM   2544 C  CG2 . VAL   A 1 314 ? -12.789 -19.03  11.236 1    44.544  ? 350 VAL   A CG2 1 
ATOM   2545 N  N   . VAL   A 1 315 ? -10.326 -16.794 11.22  1    53.325  ? 351 VAL   A N   1 
ATOM   2546 C  CA  . VAL   A 1 315 ? -10.007 -15.994 12.4   1    54.718  ? 351 VAL   A CA  1 
ATOM   2547 C  C   . VAL   A 1 315 ? -11.282 -15.915 13.242 1    55.247  ? 351 VAL   A C   1 
ATOM   2548 O  O   . VAL   A 1 315 ? -12.32  -15.444 12.758 1    51.891  ? 351 VAL   A O   1 
ATOM   2549 C  CB  . VAL   A 1 315 ? -9.367  -14.612 12.149 1    45.956  ? 351 VAL   A CB  1 
ATOM   2550 C  CG1 . VAL   A 1 315 ? -9.069  -13.877 13.439 1    41.698  ? 351 VAL   A CG1 1 
ATOM   2551 C  CG2 . VAL   A 1 315 ? -8.039  -14.745 11.425 1    49.237  ? 351 VAL   A CG2 1 
ATOM   2552 N  N   . CYS   A 1 316 ? -11.183 -16.448 14.473 1    50.676  ? 352 CYS   A N   1 
ATOM   2553 C  CA  . CYS   A 1 316 ? -12.367 -16.738 15.261 1    54.665  ? 352 CYS   A CA  1 
ATOM   2554 C  C   . CYS   A 1 316 ? -12.699 -15.603 16.222 1    56.022  ? 352 CYS   A C   1 
ATOM   2555 O  O   . CYS   A 1 316 ? -13.854 -15.475 16.657 1    55.345  ? 352 CYS   A O   1 
ATOM   2556 C  CB  . CYS   A 1 316 ? -12.292 -18.085 15.976 1    47.84   ? 352 CYS   A CB  1 
ATOM   2557 S  SG  . CYS   A 1 316 ? -13.213 -19.381 15.107 1    47.002  ? 352 CYS   A SG  1 
ATOM   2558 N  N   . HIS   A 1 317 ? -11.687 -14.792 16.554 1    49.378  ? 353 HIS   A N   1 
ATOM   2559 C  CA  . HIS   A 1 317 ? -11.937 -13.634 17.398 1    41.638  ? 353 HIS   A CA  1 
ATOM   2560 C  C   . HIS   A 1 317 ? -13.109 -12.813 16.843 1    43.605  ? 353 HIS   A C   1 
ATOM   2561 O  O   . HIS   A 1 317 ? -13.1   -12.428 15.686 1    47.773  ? 353 HIS   A O   1 
ATOM   2562 C  CB  . HIS   A 1 317 ? -10.678 -12.785 17.49  1    39.457  ? 353 HIS   A CB  1 
ATOM   2563 C  CG  . HIS   A 1 317 ? -10.823 -11.941 18.677 1    35.604  ? 353 HIS   A CG  1 
ATOM   2564 N  ND1 . HIS   A 1 317 ? -10.312 -12.34  19.895 1    41.572  ? 353 HIS   A ND1 1 
ATOM   2565 C  CD2 . HIS   A 1 317 ? -11.484 -10.805 18.872 1    33.852  ? 353 HIS   A CD2 1 
ATOM   2566 C  CE1 . HIS   A 1 317 ? -10.628 -11.446 20.822 1    39.527  ? 353 HIS   A CE1 1 
ATOM   2567 N  NE2 . HIS   A 1 317 ? -11.32  -10.489 20.212 1    44.084  ? 353 HIS   A NE2 1 
ATOM   2568 N  N   . ALA   A 1 318 ? -14.154 -12.609 17.648 1    32.293  ? 354 ALA   A N   1 
ATOM   2569 C  CA  . ALA   A 1 318 ? -15.317 -11.861 17.21  1    33.869  ? 354 ALA   A CA  1 
ATOM   2570 C  C   . ALA   A 1 318 ? -14.939 -10.423 16.821 1    34.546  ? 354 ALA   A C   1 
ATOM   2571 O  O   . ALA   A 1 318 ? -14.295 -9.703  17.585 1    32.591  ? 354 ALA   A O   1 
ATOM   2572 C  CB  . ALA   A 1 318 ? -16.331 -11.856 18.337 1    28.138  ? 354 ALA   A CB  1 
ATOM   2573 N  N   . SER   A 1 319 ? -15.427 -9.981  15.66  1    28.01   ? 355 SER   A N   1 
ATOM   2574 C  CA  . SER   A 1 319 ? -15.209 -8.614  15.259 1    32.461  ? 355 SER   A CA  1 
ATOM   2575 C  C   . SER   A 1 319 ? -16.381 -8.081  14.415 1    32.378  ? 355 SER   A C   1 
ATOM   2576 O  O   . SER   A 1 319 ? -17.097 -8.846  13.789 1    32.13   ? 355 SER   A O   1 
ATOM   2577 C  CB  . SER   A 1 319 ? -13.947 -8.558  14.527 1    31.717  ? 355 SER   A CB  1 
ATOM   2578 O  OG  . SER   A 1 319 ? -14.085 -9.466  13.441 1    33.506  ? 355 SER   A OG  1 
ATOM   2579 N  N   . ALA   A 1 320 ? -16.584 -6.76   14.437 1    31.111  ? 356 ALA   A N   1 
ATOM   2580 C  CA  . ALA   A 1 320 ? -17.539 -6.073  13.588 1    31.396  ? 356 ALA   A CA  1 
ATOM   2581 C  C   . ALA   A 1 320 ? -16.841 -5.383  12.395 1    33.508  ? 356 ALA   A C   1 
ATOM   2582 O  O   . ALA   A 1 320 ? -15.715 -4.901  12.511 1    29.813  ? 356 ALA   A O   1 
ATOM   2583 C  CB  . ALA   A 1 320 ? -18.293 -5.11   14.474 1    22.945  ? 356 ALA   A CB  1 
ATOM   2584 N  N   . TRP   A 1 321 ? -17.56  -5.276  11.265 1    33.518  ? 357 TRP   A N   1 
ATOM   2585 C  CA  . TRP   A 1 321 ? -17.009 -4.858  9.987  1    29.34   ? 357 TRP   A CA  1 
ATOM   2586 C  C   . TRP   A 1 321 ? -17.826 -3.752  9.275  1    33.114  ? 357 TRP   A C   1 
ATOM   2587 O  O   . TRP   A 1 321 ? -19.013 -3.892  8.873  1    29.663  ? 357 TRP   A O   1 
ATOM   2588 C  CB  . TRP   A 1 321 ? -16.773 -6.089  9.098  1    30.814  ? 357 TRP   A CB  1 
ATOM   2589 C  CG  . TRP   A 1 321 ? -15.711 -7.028  9.633  1    32.516  ? 357 TRP   A CG  1 
ATOM   2590 C  CD1 . TRP   A 1 321 ? -15.787 -7.788  10.765 1    29.148  ? 357 TRP   A CD1 1 
ATOM   2591 C  CD2 . TRP   A 1 321 ? -14.395 -7.29   9.076  1    33.744  ? 357 TRP   A CD2 1 
ATOM   2592 N  NE1 . TRP   A 1 321 ? -14.652 -8.538  10.935 1    30.945  ? 357 TRP   A NE1 1 
ATOM   2593 C  CE2 . TRP   A 1 321 ? -13.775 -8.247  9.921  1    34.789  ? 357 TRP   A CE2 1 
ATOM   2594 C  CE3 . TRP   A 1 321 ? -13.685 -6.819  7.951  1    32.777  ? 357 TRP   A CE3 1 
ATOM   2595 C  CZ2 . TRP   A 1 321 ? -12.478 -8.695  9.692  1    34.847  ? 357 TRP   A CZ2 1 
ATOM   2596 C  CZ3 . TRP   A 1 321 ? -12.403 -7.267  7.714  1    33.311  ? 357 TRP   A CZ3 1 
ATOM   2597 C  CH2 . TRP   A 1 321 ? -11.809 -8.181  8.593  1    38.743  ? 357 TRP   A CH2 1 
ATOM   2598 N  N   . ASP   A 1 322 ? -17.136 -2.611  9.093  1    25.409  ? 358 ASP   A N   1 
ATOM   2599 C  CA  . ASP   A 1 322 ? -17.602 -1.566  8.224  1    25.598  ? 358 ASP   A CA  1 
ATOM   2600 C  C   . ASP   A 1 322 ? -16.794 -1.604  6.923  1    30.878  ? 358 ASP   A C   1 
ATOM   2601 O  O   . ASP   A 1 322 ? -15.552 -1.703  6.93   1    33.433  ? 358 ASP   A O   1 
ATOM   2602 C  CB  . ASP   A 1 322 ? -17.6   -0.288  9.026  1    27.224  ? 358 ASP   A CB  1 
ATOM   2603 C  CG  . ASP   A 1 322 ? -18.061 0.961   8.305  1    30.859  ? 358 ASP   A CG  1 
ATOM   2604 O  OD1 . ASP   A 1 322 ? -18.529 0.853   7.123  1    27.393  ? 358 ASP   A OD1 1 
ATOM   2605 O  OD2 . ASP   A 1 322 ? -17.943 2.01    8.967  1    26.337  ? 358 ASP   A OD2 1 
ATOM   2606 N  N   . PHE   A 1 323 ? -17.545 -1.56   5.821  1    28.552  ? 359 PHE   A N   1 
ATOM   2607 C  CA  . PHE   A 1 323 ? -17.109 -1.822  4.466  1    31.107  ? 359 PHE   A CA  1 
ATOM   2608 C  C   . PHE   A 1 323 ? -17.076 -0.514  3.704  1    36.285  ? 359 PHE   A C   1 
ATOM   2609 O  O   . PHE   A 1 323 ? -16.665 -0.544  2.549  1    37.348  ? 359 PHE   A O   1 
ATOM   2610 C  CB  . PHE   A 1 323 ? -18.064 -2.757  3.709  1    37.364  ? 359 PHE   A CB  1 
ATOM   2611 C  CG  . PHE   A 1 323 ? -17.676 -4.16   4.119  1    35.397  ? 359 PHE   A CG  1 
ATOM   2612 C  CD1 . PHE   A 1 323 ? -18.241 -4.732  5.25   1    28.063  ? 359 PHE   A CD1 1 
ATOM   2613 C  CD2 . PHE   A 1 323 ? -16.602 -4.798  3.492  1    37.191  ? 359 PHE   A CD2 1 
ATOM   2614 C  CE1 . PHE   A 1 323 ? -17.781 -5.957  5.711  1    25.933  ? 359 PHE   A CE1 1 
ATOM   2615 C  CE2 . PHE   A 1 323 ? -16.152 -6.032  3.96   1    36.896  ? 359 PHE   A CE2 1 
ATOM   2616 C  CZ  . PHE   A 1 323 ? -16.766 -6.608  5.064  1    27.283  ? 359 PHE   A CZ  1 
ATOM   2617 N  N   . TYR   A 1 324 ? -17.537 0.571   4.369  1    33.51   ? 360 TYR   A N   1 
ATOM   2618 C  CA  . TYR   A 1 324 ? -17.301 1.967   3.999  1    40.297  ? 360 TYR   A CA  1 
ATOM   2619 C  C   . TYR   A 1 324 ? -18.169 2.453   2.827  1    42.299  ? 360 TYR   A C   1 
ATOM   2620 O  O   . TYR   A 1 324 ? -17.77  3.37    2.115  1    40.627  ? 360 TYR   A O   1 
ATOM   2621 C  CB  . TYR   A 1 324 ? -15.822 2.234   3.663  1    40.736  ? 360 TYR   A CB  1 
ATOM   2622 C  CG  . TYR   A 1 324 ? -14.936 2.132   4.89   1    44.113  ? 360 TYR   A CG  1 
ATOM   2623 C  CD1 . TYR   A 1 324 ? -14.96  3.131   5.863  1    58.203  ? 360 TYR   A CD1 1 
ATOM   2624 C  CD2 . TYR   A 1 324 ? -14.177 0.997   5.124  1    45.681  ? 360 TYR   A CD2 1 
ATOM   2625 C  CE1 . TYR   A 1 324 ? -14.207 3.027   7.019  1    64.793  ? 360 TYR   A CE1 1 
ATOM   2626 C  CE2 . TYR   A 1 324 ? -13.394 0.895   6.259  1    59.325  ? 360 TYR   A CE2 1 
ATOM   2627 C  CZ  . TYR   A 1 324 ? -13.404 1.917   7.194  1    67.261  ? 360 TYR   A CZ  1 
ATOM   2628 O  OH  . TYR   A 1 324 ? -12.635 1.816   8.307  1    93.313  ? 360 TYR   A OH  1 
ATOM   2629 N  N   . ASN   A 1 325 ? -19.328 1.84    2.595  1    40.181  ? 361 ASN   A N   1 
ATOM   2630 C  CA  . ASN   A 1 325 ? -20.227 2.375   1.581  1    43.624  ? 361 ASN   A CA  1 
ATOM   2631 C  C   . ASN   A 1 325 ? -21.591 2.622   2.189  1    34.252  ? 361 ASN   A C   1 
ATOM   2632 O  O   . ASN   A 1 325 ? -22.543 2.81    1.459  1    35.685  ? 361 ASN   A O   1 
ATOM   2633 C  CB  . ASN   A 1 325 ? -20.465 1.447   0.395  1    42.7    ? 361 ASN   A CB  1 
ATOM   2634 C  CG  . ASN   A 1 325 ? -20.841 0.045   0.817  1    44.44   ? 361 ASN   A CG  1 
ATOM   2635 O  OD1 . ASN   A 1 325 ? -21.28  -0.184  1.959  1    44.794  ? 361 ASN   A OD1 1 
ATOM   2636 N  ND2 . ASN   A 1 325 ? -20.675 -0.902  -0.102 1    39.367  ? 361 ASN   A ND2 1 
ATOM   2637 N  N   . GLY   A 1 326 ? -21.653 2.628   3.515  1    37.622  ? 362 GLY   A N   1 
ATOM   2638 C  CA  . GLY   A 1 326 ? -22.909 2.908   4.191  1    33.538  ? 362 GLY   A CA  1 
ATOM   2639 C  C   . GLY   A 1 326 ? -24.013 1.899   3.877  1    30.731  ? 362 GLY   A C   1 
ATOM   2640 O  O   . GLY   A 1 326 ? -25.144 2.228   4.161  1    33.254  ? 362 GLY   A O   1 
ATOM   2641 N  N   . LYS   A 1 327 ? -23.713 0.682   3.354  1    28.656  ? 363 LYS   A N   1 
ATOM   2642 C  CA  . LYS   A 1 327 ? -24.771 -0.313  3.141  1    33.289  ? 363 LYS   A CA  1 
ATOM   2643 C  C   . LYS   A 1 327 ? -24.289 -1.688  3.586  1    31.662  ? 363 LYS   A C   1 
ATOM   2644 O  O   . LYS   A 1 327 ? -25.04  -2.573  3.977  1    33.607  ? 363 LYS   A O   1 
ATOM   2645 C  CB  . LYS   A 1 327 ? -25.182 -0.425  1.666  1    40.821  ? 363 LYS   A CB  1 
ATOM   2646 C  CG  . LYS   A 1 327 ? -25.796 0.847   1.17   1    49.121  ? 363 LYS   A CG  1 
ATOM   2647 C  CD  . LYS   A 1 327 ? -25.734 1.083   -0.325 1    68.192  ? 363 LYS   A CD  1 
ATOM   2648 C  CE  . LYS   A 1 327 ? -26.893 2.017   -0.509 1    80.196  ? 363 LYS   A CE  1 
ATOM   2649 N  NZ  . LYS   A 1 327 ? -26.675 3.015   -1.56  1    84.098  ? 363 LYS   A NZ  1 
ATOM   2650 N  N   . ASP   A 1 328 ? -22.991 -1.885  3.538  1    33.909  ? 364 ASP   A N   1 
ATOM   2651 C  CA  . ASP   A 1 328 ? -22.524 -3.213  3.889  1    32.799  ? 364 ASP   A CA  1 
ATOM   2652 C  C   . ASP   A 1 328 ? -21.822 -3.191  5.263  1    35      ? 364 ASP   A C   1 
ATOM   2653 O  O   . ASP   A 1 328 ? -20.742 -2.592  5.461  1    30.061  ? 364 ASP   A O   1 
ATOM   2654 C  CB  . ASP   A 1 328 ? -21.726 -3.74   2.713  1    27.887  ? 364 ASP   A CB  1 
ATOM   2655 C  CG  . ASP   A 1 328 ? -21.269 -5.174  2.869  1    40.096  ? 364 ASP   A CG  1 
ATOM   2656 O  OD1 . ASP   A 1 328 ? -21.771 -5.882  3.81   1    47.446  ? 364 ASP   A OD1 1 
ATOM   2657 O  OD2 . ASP   A 1 328 ? -20.387 -5.553  2.078  1    46.163  ? 364 ASP   A OD2 1 
ATOM   2658 N  N   . PHE   A 1 329 ? -22.454 -3.849  6.235  1    36.305  ? 365 PHE   A N   1 
ATOM   2659 C  CA  . PHE   A 1 329 ? -21.893 -4.035  7.562  1    31.861  ? 365 PHE   A CA  1 
ATOM   2660 C  C   . PHE   A 1 329 ? -22.047 -5.513  7.935  1    34.82   ? 365 PHE   A C   1 
ATOM   2661 O  O   . PHE   A 1 329 ? -22.978 -6.202  7.52   1    36.98   ? 365 PHE   A O   1 
ATOM   2662 C  CB  . PHE   A 1 329 ? -22.767 -3.144  8.434  1    28.886  ? 365 PHE   A CB  1 
ATOM   2663 C  CG  . PHE   A 1 329 ? -23.002 -1.708  7.977  1    29.738  ? 365 PHE   A CG  1 
ATOM   2664 C  CD1 . PHE   A 1 329 ? -22.056 -0.71   8.22   1    28.244  ? 365 PHE   A CD1 1 
ATOM   2665 C  CD2 . PHE   A 1 329 ? -24.216 -1.33   7.4    1    28.018  ? 365 PHE   A CD2 1 
ATOM   2666 C  CE1 . PHE   A 1 329 ? -22.268 0.608   7.827  1    27.37   ? 365 PHE   A CE1 1 
ATOM   2667 C  CE2 . PHE   A 1 329 ? -24.452 -0.001  7.055  1    31.982  ? 365 PHE   A CE2 1 
ATOM   2668 C  CZ  . PHE   A 1 329 ? -23.474 0.965   7.272  1    32.421  ? 365 PHE   A CZ  1 
ATOM   2669 N  N   . ARG   A 1 330 ? -21.132 -6.024  8.745  1    32.082  ? 366 ARG   A N   1 
ATOM   2670 C  CA  . ARG   A 1 330 ? -21.102 -7.451  8.97   1    30.762  ? 366 ARG   A CA  1 
ATOM   2671 C  C   . ARG   A 1 330 ? -20.418 -7.715  10.302 1    32.489  ? 366 ARG   A C   1 
ATOM   2672 O  O   . ARG   A 1 330 ? -19.615 -6.892  10.776 1    33.438  ? 366 ARG   A O   1 
ATOM   2673 C  CB  . ARG   A 1 330 ? -20.223 -8.103  7.887  1    29.465  ? 366 ARG   A CB  1 
ATOM   2674 C  CG  . ARG   A 1 330 ? -20.789 -7.981  6.482  1    30.096  ? 366 ARG   A CG  1 
ATOM   2675 C  CD  . ARG   A 1 330 ? -19.947 -8.737  5.495  1    34.151  ? 366 ARG   A CD  1 
ATOM   2676 N  NE  . ARG   A 1 330 ? -20.061 -8.34   4.085  1    42.138  ? 366 ARG   A NE  1 
ATOM   2677 C  CZ  . ARG   A 1 330 ? -19.083 -8.676  3.226  1    41.354  ? 366 ARG   A CZ  1 
ATOM   2678 N  NH1 . ARG   A 1 330 ? -18.063 -9.416  3.609  1    46.89   ? 366 ARG   A NH1 1 
ATOM   2679 N  NH2 . ARG   A 1 330 ? -19.114 -8.276  1.986  1    36.057  ? 366 ARG   A NH2 1 
ATOM   2680 N  N   . ILE   A 1 331 ? -20.699 -8.917  10.818 1    30.65   ? 367 ILE   A N   1 
ATOM   2681 C  CA  . ILE   A 1 331 ? -20.01  -9.502  11.947 1    26.479  ? 367 ILE   A CA  1 
ATOM   2682 C  C   . ILE   A 1 331 ? -19.44  -10.854 11.561 1    26.451  ? 367 ILE   A C   1 
ATOM   2683 O  O   . ILE   A 1 331 ? -20.01  -11.558 10.753 1    32.721  ? 367 ILE   A O   1 
ATOM   2684 C  CB  . ILE   A 1 331 ? -20.933 -9.578  13.166 1    26.83   ? 367 ILE   A CB  1 
ATOM   2685 C  CG1 . ILE   A 1 331 ? -21.124 -8.156  13.743 1    22.634  ? 367 ILE   A CG1 1 
ATOM   2686 C  CG2 . ILE   A 1 331 ? -20.356 -10.531 14.222 1    27.447  ? 367 ILE   A CG2 1 
ATOM   2687 C  CD1 . ILE   A 1 331 ? -22.342 -8.04   14.658 1    22.864  ? 367 ILE   A CD1 1 
ATOM   2688 N  N   . LYS   A 1 332 ? -18.271 -11.154 12.128 1    28.153  ? 368 LYS   A N   1 
ATOM   2689 C  CA  . LYS   A 1 332 ? -17.557 -12.4   11.967 1    30.178  ? 368 LYS   A CA  1 
ATOM   2690 C  C   . LYS   A 1 332 ? -17.258 -12.909 13.363 1    37.674  ? 368 LYS   A C   1 
ATOM   2691 O  O   . LYS   A 1 332 ? -16.319 -12.43  14.033 1    35.133  ? 368 LYS   A O   1 
ATOM   2692 C  CB  . LYS   A 1 332 ? -16.175 -12.131 11.376 1    25.284  ? 368 LYS   A CB  1 
ATOM   2693 C  CG  . LYS   A 1 332 ? -15.364 -13.351 11.109 1    26.312  ? 368 LYS   A CG  1 
ATOM   2694 C  CD  . LYS   A 1 332 ? -13.949 -12.849 10.84  1    33.362  ? 368 LYS   A CD  1 
ATOM   2695 C  CE  . LYS   A 1 332 ? -13.147 -12.264 12.015 1    32.571  ? 368 LYS   A CE  1 
ATOM   2696 N  NZ  . LYS   A 1 332 ? -13.57  -12.982 13.218 1    40.33   ? 368 LYS   A NZ  1 
ATOM   2697 N  N   . GLN   A 1 333 ? -18.114 -13.855 13.793 1    38.471  ? 369 GLN   A N   1 
ATOM   2698 C  CA  . GLN   A 1 333 ? -18.001 -14.468 15.112 1    30.083  ? 369 GLN   A CA  1 
ATOM   2699 C  C   . GLN   A 1 333 ? -18.255 -15.978 15.035 1    34.189  ? 369 GLN   A C   1 
ATOM   2700 O  O   . GLN   A 1 333 ? -19.194 -16.437 14.383 1    42.275  ? 369 GLN   A O   1 
ATOM   2701 C  CB  . GLN   A 1 333 ? -18.923 -13.685 16.033 1    28.309  ? 369 GLN   A CB  1 
ATOM   2702 C  CG  . GLN   A 1 333 ? -18.902 -14.239 17.452 1    31.908  ? 369 GLN   A CG  1 
ATOM   2703 C  CD  . GLN   A 1 333 ? -19.754 -13.404 18.374 1    34.735  ? 369 GLN   A CD  1 
ATOM   2704 O  OE1 . GLN   A 1 333 ? -20.313 -12.375 17.985 1    31.8    ? 369 GLN   A OE1 1 
ATOM   2705 N  NE2 . GLN   A 1 333 ? -19.848 -13.839 19.619 1    39.168  ? 369 GLN   A NE2 1 
ATOM   2706 N  N   . CYS   A 1 334 ? -17.387 -16.752 15.68  1    29.496  ? 370 CYS   A N   1 
ATOM   2707 C  CA  . CYS   A 1 334 ? -17.562 -18.183 15.852 1    34.987  ? 370 CYS   A CA  1 
ATOM   2708 C  C   . CYS   A 1 334 ? -18.414 -18.403 17.123 1    36.073  ? 370 CYS   A C   1 
ATOM   2709 O  O   . CYS   A 1 334 ? -17.898 -18.815 18.147 1    35.167  ? 370 CYS   A O   1 
ATOM   2710 C  CB  . CYS   A 1 334 ? -16.17  -18.811 15.946 1    33.119  ? 370 CYS   A CB  1 
ATOM   2711 S  SG  . CYS   A 1 334 ? -15.139 -18.762 14.433 1    40.235  ? 370 CYS   A SG  1 
ATOM   2712 N  N   . THR   A 1 335 ? -19.72  -18.089 17.081 1    34.704  ? 371 THR   A N   1 
ATOM   2713 C  CA  . THR   A 1 335 ? -20.593 -18.034 18.253 1    34.931  ? 371 THR   A CA  1 
ATOM   2714 C  C   . THR   A 1 335 ? -20.784 -19.426 18.874 1    34.622  ? 371 THR   A C   1 
ATOM   2715 O  O   . THR   A 1 335 ? -21.106 -20.375 18.185 1    40.595  ? 371 THR   A O   1 
ATOM   2716 C  CB  . THR   A 1 335 ? -21.942 -17.428 17.834 1    34.883  ? 371 THR   A CB  1 
ATOM   2717 O  OG1 . THR   A 1 335 ? -21.738 -16.486 16.779 1    28.3    ? 371 THR   A OG1 1 
ATOM   2718 C  CG2 . THR   A 1 335 ? -22.675 -16.77  18.998 1    27.266  ? 371 THR   A CG2 1 
ATOM   2719 N  N   . THR   A 1 336 ? -20.541 -19.549 20.18  1    40.567  ? 372 THR   A N   1 
ATOM   2720 C  CA  . THR   A 1 336 ? -20.998 -20.637 21.027 1    31.817  ? 372 THR   A CA  1 
ATOM   2721 C  C   . THR   A 1 336 ? -22.363 -20.215 21.565 1    30.644  ? 372 THR   A C   1 
ATOM   2722 O  O   . THR   A 1 336 ? -22.604 -19.032 21.812 1    26.067  ? 372 THR   A O   1 
ATOM   2723 C  CB  . THR   A 1 336 ? -20.017 -20.8   22.195 1    35.457  ? 372 THR   A CB  1 
ATOM   2724 O  OG1 . THR   A 1 336 ? -18.775 -21.232 21.662 1    36.695  ? 372 THR   A OG1 1 
ATOM   2725 C  CG2 . THR   A 1 336 ? -20.33  -22.018 23.06  1    36.574  ? 372 THR   A CG2 1 
ATOM   2726 N  N   . VAL   A 1 337 ? -23.254 -21.181 21.82  1    33.586  ? 373 VAL   A N   1 
ATOM   2727 C  CA  . VAL   A 1 337 ? -24.564 -20.825 22.341 1    33.965  ? 373 VAL   A CA  1 
ATOM   2728 C  C   . VAL   A 1 337 ? -24.457 -20.826 23.874 1    34.735  ? 373 VAL   A C   1 
ATOM   2729 O  O   . VAL   A 1 337 ? -24.712 -21.847 24.517 1    32.183  ? 373 VAL   A O   1 
ATOM   2730 C  CB  . VAL   A 1 337 ? -25.633 -21.784 21.758 1    34.173  ? 373 VAL   A CB  1 
ATOM   2731 C  CG1 . VAL   A 1 337 ? -26.999 -21.566 22.379 1    39.98   ? 373 VAL   A CG1 1 
ATOM   2732 C  CG2 . VAL   A 1 337 ? -25.739 -21.696 20.243 1    35.222  ? 373 VAL   A CG2 1 
ATOM   2733 N  N   . ASN   A 1 338 ? -24.025 -19.684 24.44  1    31.251  ? 374 ASN   A N   1 
ATOM   2734 C  CA  . ASN   A 1 338 ? -23.996 -19.434 25.876 1    31.897  ? 374 ASN   A CA  1 
ATOM   2735 C  C   . ASN   A 1 338 ? -24.358 -17.965 26.189 1    42.926  ? 374 ASN   A C   1 
ATOM   2736 O  O   . ASN   A 1 338 ? -24.647 -17.171 25.292 1    44.104  ? 374 ASN   A O   1 
ATOM   2737 C  CB  . ASN   A 1 338 ? -22.709 -19.946 26.502 1    32.078  ? 374 ASN   A CB  1 
ATOM   2738 C  CG  . ASN   A 1 338 ? -21.423 -19.449 25.866 1    37.797  ? 374 ASN   A CG  1 
ATOM   2739 O  OD1 . ASN   A 1 338 ? -21.231 -18.248 25.633 1    39.901  ? 374 ASN   A OD1 1 
ATOM   2740 N  ND2 . ASN   A 1 338 ? -20.474 -20.343 25.644 1    34.004  ? 374 ASN   A ND2 1 
ATOM   2741 N  N   . LEU   A 1 339 ? -24.411 -17.608 27.48  1    37.245  ? 375 LEU   A N   1 
ATOM   2742 C  CA  . LEU   A 1 339 ? -24.706 -16.256 27.898 1    35.747  ? 375 LEU   A CA  1 
ATOM   2743 C  C   . LEU   A 1 339 ? -23.571 -15.323 27.468 1    34.61   ? 375 LEU   A C   1 
ATOM   2744 O  O   . LEU   A 1 339 ? -23.819 -14.28  26.898 1    35.568  ? 375 LEU   A O   1 
ATOM   2745 C  CB  . LEU   A 1 339 ? -24.785 -16.255 29.427 1    42.644  ? 375 LEU   A CB  1 
ATOM   2746 C  CG  . LEU   A 1 339 ? -25.185 -14.899 30.034 1    42.005  ? 375 LEU   A CG  1 
ATOM   2747 C  CD1 . LEU   A 1 339 ? -26.443 -14.396 29.288 1    31.991  ? 375 LEU   A CD1 1 
ATOM   2748 C  CD2 . LEU   A 1 339 ? -25.451 -15.033 31.516 1    33.66   ? 375 LEU   A CD2 1 
ATOM   2749 N  N   . GLU   A 1 340 ? -22.345 -15.673 27.859 1    28.953  ? 376 GLU   A N   1 
ATOM   2750 C  CA  . GLU   A 1 340 ? -21.096 -15.055 27.451 1    33.346  ? 376 GLU   A CA  1 
ATOM   2751 C  C   . GLU   A 1 340 ? -21.107 -14.667 25.965 1    33.021  ? 376 GLU   A C   1 
ATOM   2752 O  O   . GLU   A 1 340 ? -20.905 -13.491 25.673 1    38.858  ? 376 GLU   A O   1 
ATOM   2753 C  CB  . GLU   A 1 340 ? -19.99  -15.963 27.985 1    38.387  ? 376 GLU   A CB  1 
ATOM   2754 C  CG  . GLU   A 1 340 ? -18.572 -15.526 27.655 1    56.966  ? 376 GLU   A CG  1 
ATOM   2755 C  CD  . GLU   A 1 340 ? -17.629 -16.082 28.719 1    69.172  ? 376 GLU   A CD  1 
ATOM   2756 O  OE1 . GLU   A 1 340 ? -17.378 -17.316 28.796 1    79.835  ? 376 GLU   A OE1 1 
ATOM   2757 O  OE2 . GLU   A 1 340 ? -17.166 -15.24  29.519 1    60.329  ? 376 GLU   A OE2 1 
ATOM   2758 N  N   . ASP   A 1 341 ? -21.379 -15.58  25.025 1    27.587  ? 377 ASP   A N   1 
ATOM   2759 C  CA  . ASP   A 1 341 ? -21.418 -15.159 23.631 1    27.615  ? 377 ASP   A CA  1 
ATOM   2760 C  C   . ASP   A 1 341 ? -22.632 -14.282 23.295 1    32.712  ? 377 ASP   A C   1 
ATOM   2761 O  O   . ASP   A 1 341 ? -22.598 -13.552 22.293 1    29.067  ? 377 ASP   A O   1 
ATOM   2762 C  CB  . ASP   A 1 341 ? -21.103 -16.275 22.656 1    30.017  ? 377 ASP   A CB  1 
ATOM   2763 C  CG  . ASP   A 1 341 ? -19.615 -16.587 22.577 1    45.777  ? 377 ASP   A CG  1 
ATOM   2764 O  OD1 . ASP   A 1 341 ? -18.866 -16.039 23.455 1    45.966  ? 377 ASP   A OD1 1 
ATOM   2765 O  OD2 . ASP   A 1 341 ? -19.209 -17.345 21.642 1    50.36   ? 377 ASP   A OD2 1 
ATOM   2766 N  N   . LEU   A 1 342 ? -23.696 -14.347 24.118 1    25.025  ? 378 LEU   A N   1 
ATOM   2767 C  CA  . LEU   A 1 342 ? -24.877 -13.525 23.883 1    26.915  ? 378 LEU   A CA  1 
ATOM   2768 C  C   . LEU   A 1 342 ? -24.539 -12.064 24.175 1    31.28   ? 378 LEU   A C   1 
ATOM   2769 O  O   . LEU   A 1 342 ? -25.002 -11.167 23.467 1    28.38   ? 378 LEU   A O   1 
ATOM   2770 C  CB  . LEU   A 1 342 ? -26.135 -13.973 24.643 1    27.858  ? 378 LEU   A CB  1 
ATOM   2771 C  CG  . LEU   A 1 342 ? -27.348 -13.016 24.593 1    33.63   ? 378 LEU   A CG  1 
ATOM   2772 C  CD1 . LEU   A 1 342 ? -27.891 -12.882 23.174 1    31.388  ? 378 LEU   A CD1 1 
ATOM   2773 C  CD2 . LEU   A 1 342 ? -28.506 -13.397 25.567 1    30.027  ? 378 LEU   A CD2 1 
ATOM   2774 N  N   . VAL   A 1 343 ? -23.733 -11.851 25.233 1    26.497  ? 379 VAL   A N   1 
ATOM   2775 C  CA  . VAL   A 1 343 ? -23.226 -10.546 25.596 1    28.13   ? 379 VAL   A CA  1 
ATOM   2776 C  C   . VAL   A 1 343 ? -22.294 -10.067 24.466 1    29.579  ? 379 VAL   A C   1 
ATOM   2777 O  O   . VAL   A 1 343 ? -22.428 -8.948  23.959 1    32.305  ? 379 VAL   A O   1 
ATOM   2778 C  CB  . VAL   A 1 343 ? -22.597 -10.647 27.022 1    28.11   ? 379 VAL   A CB  1 
ATOM   2779 C  CG1 . VAL   A 1 343 ? -21.705 -9.453  27.406 1    24.534  ? 379 VAL   A CG1 1 
ATOM   2780 C  CG2 . VAL   A 1 343 ? -23.649 -10.872 28.119 1    22.142  ? 379 VAL   A CG2 1 
ATOM   2781 N  N   . VAL   A 1 344 ? -21.368 -10.933 24.032 1    27.034  ? 380 VAL   A N   1 
ATOM   2782 C  CA  . VAL   A 1 344 ? -20.432 -10.627 22.943 1    29.085  ? 380 VAL   A CA  1 
ATOM   2783 C  C   . VAL   A 1 344 ? -21.208 -10.193 21.686 1    32.528  ? 380 VAL   A C   1 
ATOM   2784 O  O   . VAL   A 1 344 ? -20.937 -9.124  21.13  1    37.136  ? 380 VAL   A O   1 
ATOM   2785 C  CB  . VAL   A 1 344 ? -19.391 -11.72  22.615 1    26.873  ? 380 VAL   A CB  1 
ATOM   2786 C  CG1 . VAL   A 1 344 ? -18.599 -11.395 21.345 1    25.815  ? 380 VAL   A CG1 1 
ATOM   2787 C  CG2 . VAL   A 1 344 ? -18.454 -11.981 23.804 1    24.657  ? 380 VAL   A CG2 1 
ATOM   2788 N  N   . ALA   A 1 345 ? -22.25  -10.949 21.313 1    26.526  ? 381 ALA   A N   1 
ATOM   2789 C  CA  . ALA   A 1 345 ? -23.07  -10.554 20.191 1    29.28   ? 381 ALA   A CA  1 
ATOM   2790 C  C   . ALA   A 1 345 ? -23.557 -9.121  20.395 1    32.143  ? 381 ALA   A C   1 
ATOM   2791 O  O   . ALA   A 1 345 ? -23.589 -8.372  19.422 1    34.363  ? 381 ALA   A O   1 
ATOM   2792 C  CB  . ALA   A 1 345 ? -24.214 -11.536 19.994 1    29.305  ? 381 ALA   A CB  1 
ATOM   2793 N  N   . HIS   A 1 346 ? -23.94  -8.745  21.639 1    30.061  ? 382 HIS   A N   1 
ATOM   2794 C  CA  . HIS   A 1 346 ? -24.503 -7.408  21.836 1    30.853  ? 382 HIS   A CA  1 
ATOM   2795 C  C   . HIS   A 1 346 ? -23.395 -6.38   21.606 1    26.389  ? 382 HIS   A C   1 
ATOM   2796 O  O   . HIS   A 1 346 ? -23.596 -5.384  20.938 1    23.127  ? 382 HIS   A O   1 
ATOM   2797 C  CB  . HIS   A 1 346 ? -25.241 -7.285  23.188 1    35.613  ? 382 HIS   A CB  1 
ATOM   2798 C  CG  . HIS   A 1 346 ? -26.639 -7.853  23.183 1    36.062  ? 382 HIS   A CG  1 
ATOM   2799 N  ND1 . HIS   A 1 346 ? -26.886 -9.207  23.173 1    31.726  ? 382 HIS   A ND1 1 
ATOM   2800 C  CD2 . HIS   A 1 346 ? -27.854 -7.274  23.102 1    37.794  ? 382 HIS   A CD2 1 
ATOM   2801 C  CE1 . HIS   A 1 346 ? -28.195 -9.425  23.104 1    36.037  ? 382 HIS   A CE1 1 
ATOM   2802 N  NE2 . HIS   A 1 346 ? -28.813 -8.275  23.09  1    37.239  ? 382 HIS   A NE2 1 
ATOM   2803 N  N   . HIS   A 1 347 ? -22.215 -6.685  22.17  1    22.703  ? 383 HIS   A N   1 
ATOM   2804 C  CA  . HIS   A 1 347 ? -21.01  -5.902  22.041 1    21.439  ? 383 HIS   A CA  1 
ATOM   2805 C  C   . HIS   A 1 347 ? -20.725 -5.604  20.569 1    18.933  ? 383 HIS   A C   1 
ATOM   2806 O  O   . HIS   A 1 347 ? -20.605 -4.457  20.179 1    20.305  ? 383 HIS   A O   1 
ATOM   2807 C  CB  . HIS   A 1 347 ? -19.853 -6.531  22.852 1    23.789  ? 383 HIS   A CB  1 
ATOM   2808 C  CG  . HIS   A 1 347 ? -18.591 -5.787  22.645 1    23.457  ? 383 HIS   A CG  1 
ATOM   2809 N  ND1 . HIS   A 1 347 ? -18.102 -4.933  23.604 1    21.059  ? 383 HIS   A ND1 1 
ATOM   2810 C  CD2 . HIS   A 1 347 ? -17.783 -5.653  21.541 1    22.464  ? 383 HIS   A CD2 1 
ATOM   2811 C  CE1 . HIS   A 1 347 ? -17.018 -4.323  23.128 1    22.042  ? 383 HIS   A CE1 1 
ATOM   2812 N  NE2 . HIS   A 1 347 ? -16.831 -4.716  21.874 1    22.215  ? 383 HIS   A NE2 1 
ATOM   2813 N  N   . GLU   A 1 348 ? -20.623 -6.632  19.746 1    20.93   ? 384 GLU   A N   1 
ATOM   2814 C  CA  . GLU   A 1 348 ? -20.344 -6.461  18.328 1    19.4    ? 384 GLU   A CA  1 
ATOM   2815 C  C   . GLU   A 1 348 ? -21.502 -5.703  17.692 1    22.491  ? 384 GLU   A C   1 
ATOM   2816 O  O   . GLU   A 1 348 ? -21.278 -4.918  16.771 1    31.07   ? 384 GLU   A O   1 
ATOM   2817 C  CB  . GLU   A 1 348 ? -20.121 -7.813  17.643 1    17.927  ? 384 GLU   A CB  1 
ATOM   2818 C  CG  . GLU   A 1 348 ? -18.98  -8.64   18.219 1    18.497  ? 384 GLU   A CG  1 
ATOM   2819 C  CD  . GLU   A 1 348 ? -17.617 -7.936  18.259 1    26.301  ? 384 GLU   A CD  1 
ATOM   2820 O  OE1 . GLU   A 1 348 ? -17.395 -7.039  17.445 1    32.464  ? 384 GLU   A OE1 1 
ATOM   2821 O  OE2 . GLU   A 1 348 ? -16.77  -8.186  19.152 1    29.767  ? 384 GLU   A OE2 1 
ATOM   2822 N  N   . MET   A 1 349 ? -22.733 -5.943  18.153 1    21.511  ? 385 MET   A N   1 
ATOM   2823 C  CA  . MET   A 1 349 ? -23.886 -5.322  17.505 1    23.509  ? 385 MET   A CA  1 
ATOM   2824 C  C   . MET   A 1 349 ? -23.882 -3.793  17.736 1    26.711  ? 385 MET   A C   1 
ATOM   2825 O  O   . MET   A 1 349 ? -24.221 -3.015  16.837 1    24.38   ? 385 MET   A O   1 
ATOM   2826 C  CB  . MET   A 1 349 ? -25.199 -6.012  17.898 1    23.19   ? 385 MET   A CB  1 
ATOM   2827 C  CG  . MET   A 1 349 ? -25.431 -7.316  17.141 1    29.352  ? 385 MET   A CG  1 
ATOM   2828 S  SD  . MET   A 1 349 ? -25.909 -7.115  15.401 1    32.214  ? 385 MET   A SD  1 
ATOM   2829 C  CE  . MET   A 1 349 ? -27.584 -6.525  15.701 1    28.139  ? 385 MET   A CE  1 
ATOM   2830 N  N   . GLY   A 1 350 ? -23.394 -3.355  18.918 1    24.384  ? 386 GLY   A N   1 
ATOM   2831 C  CA  . GLY   A 1 350 ? -23.176 -1.95   19.204 1    21.879  ? 386 GLY   A CA  1 
ATOM   2832 C  C   . GLY   A 1 350 ? -22.118 -1.325  18.306 1    20.382  ? 386 GLY   A C   1 
ATOM   2833 O  O   . GLY   A 1 350 ? -22.308 -0.198  17.9   1    22.729  ? 386 GLY   A O   1 
ATOM   2834 N  N   . HIS   A 1 351 ? -21.036 -2.023  17.958 1    21.093  ? 387 HIS   A N   1 
ATOM   2835 C  CA  . HIS   A 1 351 ? -20.109 -1.44   16.96  1    24.614  ? 387 HIS   A CA  1 
ATOM   2836 C  C   . HIS   A 1 351 ? -20.807 -1.218  15.6   1    23.637  ? 387 HIS   A C   1 
ATOM   2837 O  O   . HIS   A 1 351 ? -20.666 -0.173  14.971 1    23.731  ? 387 HIS   A O   1 
ATOM   2838 C  CB  . HIS   A 1 351 ? -18.859 -2.304  16.733 1    20.31   ? 387 HIS   A CB  1 
ATOM   2839 C  CG  . HIS   A 1 351 ? -17.839 -2.381  17.833 1    23.472  ? 387 HIS   A CG  1 
ATOM   2840 N  ND1 . HIS   A 1 351 ? -17.273 -1.257  18.406 1    23.947  ? 387 HIS   A ND1 1 
ATOM   2841 C  CD2 . HIS   A 1 351 ? -17.204 -3.457  18.409 1    21.95   ? 387 HIS   A CD2 1 
ATOM   2842 C  CE1 . HIS   A 1 351 ? -16.318 -1.636  19.268 1    22.376  ? 387 HIS   A CE1 1 
ATOM   2843 N  NE2 . HIS   A 1 351 ? -16.285 -2.974  19.296 1    22.451  ? 387 HIS   A NE2 1 
ATOM   2844 N  N   . ILE   A 1 352 ? -21.613 -2.193  15.169 1    24.721  ? 388 ILE   A N   1 
ATOM   2845 C  CA  . ILE   A 1 352 ? -22.382 -2.149  13.924 1    28.489  ? 388 ILE   A CA  1 
ATOM   2846 C  C   . ILE   A 1 352 ? -23.338 -0.955  13.985 1    29.667  ? 388 ILE   A C   1 
ATOM   2847 O  O   . ILE   A 1 352 ? -23.518 -0.217  13.003 1    29.814  ? 388 ILE   A O   1 
ATOM   2848 C  CB  . ILE   A 1 352 ? -23.088 -3.51   13.687 1    29.24   ? 388 ILE   A CB  1 
ATOM   2849 C  CG1 . ILE   A 1 352 ? -22.064 -4.684  13.434 1    27.936  ? 388 ILE   A CG1 1 
ATOM   2850 C  CG2 . ILE   A 1 352 ? -24.113 -3.433  12.565 1    31.186  ? 388 ILE   A CG2 1 
ATOM   2851 C  CD1 . ILE   A 1 352 ? -21.347 -4.673  12.086 1    25.839  ? 388 ILE   A CD1 1 
ATOM   2852 N  N   . GLN   A 1 353 ? -23.885 -0.726  15.187 1    24.039  ? 389 GLN   A N   1 
ATOM   2853 C  CA  . GLN   A 1 353 ? -24.889 0.296   15.33  1    22.902  ? 389 GLN   A CA  1 
ATOM   2854 C  C   . GLN   A 1 353 ? -24.216 1.642   15.126 1    27      ? 389 GLN   A C   1 
ATOM   2855 O  O   . GLN   A 1 353 ? -24.85  2.568   14.622 1    31.538  ? 389 GLN   A O   1 
ATOM   2856 C  CB  . GLN   A 1 353 ? -25.548 0.335   16.707 1    22.269  ? 389 GLN   A CB  1 
ATOM   2857 C  CG  . GLN   A 1 353 ? -26.496 1.522   16.855 1    23.227  ? 389 GLN   A CG  1 
ATOM   2858 C  CD  . GLN   A 1 353 ? -27.765 1.367   16.033 1    25.421  ? 389 GLN   A CD  1 
ATOM   2859 O  OE1 . GLN   A 1 353 ? -28.414 2.348   15.618 1    23.701  ? 389 GLN   A OE1 1 
ATOM   2860 N  NE2 . GLN   A 1 353 ? -28.119 0.104   15.779 1    21.233  ? 389 GLN   A NE2 1 
ATOM   2861 N  N   . TYR   A 1 354 ? -22.961 1.774   15.6   1    27.595  ? 390 TYR   A N   1 
ATOM   2862 C  CA  . TYR   A 1 354 ? -22.243 3.05    15.514 1    25.471  ? 390 TYR   A CA  1 
ATOM   2863 C  C   . TYR   A 1 354 ? -21.899 3.335   14.035 1    25.13   ? 390 TYR   A C   1 
ATOM   2864 O  O   . TYR   A 1 354 ? -22.022 4.466   13.534 1    28.197  ? 390 TYR   A O   1 
ATOM   2865 C  CB  . TYR   A 1 354 ? -21.044 2.908   16.458 1    23.287  ? 390 TYR   A CB  1 
ATOM   2866 C  CG  . TYR   A 1 354 ? -20.653 4.115   17.287 1    22.258  ? 390 TYR   A CG  1 
ATOM   2867 C  CD1 . TYR   A 1 354 ? -20.716 5.402   16.758 1    22.511  ? 390 TYR   A CD1 1 
ATOM   2868 C  CD2 . TYR   A 1 354 ? -20.209 3.967   18.615 1    21.555  ? 390 TYR   A CD2 1 
ATOM   2869 C  CE1 . TYR   A 1 354 ? -20.405 6.526   17.525 1    20.099  ? 390 TYR   A CE1 1 
ATOM   2870 C  CE2 . TYR   A 1 354 ? -19.887 5.075   19.382 1    19.106  ? 390 TYR   A CE2 1 
ATOM   2871 C  CZ  . TYR   A 1 354 ? -19.997 6.36    18.848 1    22.451  ? 390 TYR   A CZ  1 
ATOM   2872 O  OH  . TYR   A 1 354 ? -19.675 7.495   19.594 1    22.545  ? 390 TYR   A OH  1 
ATOM   2873 N  N   . PHE   A 1 355 ? -21.476 2.294   13.327 1    22.307  ? 391 PHE   A N   1 
ATOM   2874 C  CA  . PHE   A 1 355 ? -21.159 2.371   11.907 1    23.81   ? 391 PHE   A CA  1 
ATOM   2875 C  C   . PHE   A 1 355 ? -22.326 2.949   11.137 1    22.003  ? 391 PHE   A C   1 
ATOM   2876 O  O   . PHE   A 1 355 ? -22.12  3.859   10.336 1    22.629  ? 391 PHE   A O   1 
ATOM   2877 C  CB  . PHE   A 1 355 ? -20.931 0.998   11.28  1    22.97   ? 391 PHE   A CB  1 
ATOM   2878 C  CG  . PHE   A 1 355 ? -19.709 0.269   11.821 1    23.302  ? 391 PHE   A CG  1 
ATOM   2879 C  CD1 . PHE   A 1 355 ? -18.655 0.988   12.373 1    21.503  ? 391 PHE   A CD1 1 
ATOM   2880 C  CD2 . PHE   A 1 355 ? -19.607 -1.129  11.736 1    27.073  ? 391 PHE   A CD2 1 
ATOM   2881 C  CE1 . PHE   A 1 355 ? -17.513 0.318   12.813 1    26.18   ? 391 PHE   A CE1 1 
ATOM   2882 C  CE2 . PHE   A 1 355 ? -18.457 -1.804  12.162 1    25.962  ? 391 PHE   A CE2 1 
ATOM   2883 C  CZ  . PHE   A 1 355 ? -17.409 -1.07   12.687 1    25.138  ? 391 PHE   A CZ  1 
ATOM   2884 N  N   . MET   A 1 356 ? -23.536 2.507   11.475 1    23.623  ? 392 MET   A N   1 
ATOM   2885 C  CA  . MET   A 1 356 ? -24.715 2.925   10.719 1    28.62   ? 392 MET   A CA  1 
ATOM   2886 C  C   . MET   A 1 356 ? -25.137 4.373   11.041 1    35.458  ? 392 MET   A C   1 
ATOM   2887 O  O   . MET   A 1 356 ? -25.622 5.129   10.167 1    36.981  ? 392 MET   A O   1 
ATOM   2888 C  CB  . MET   A 1 356 ? -25.912 1.972   10.914 1    26.542  ? 392 MET   A CB  1 
ATOM   2889 C  CG  . MET   A 1 356 ? -25.682 0.555   10.431 1    32.392  ? 392 MET   A CG  1 
ATOM   2890 S  SD  . MET   A 1 356 ? -27.171 -0.45   10.673 1    39.927  ? 392 MET   A SD  1 
ATOM   2891 C  CE  . MET   A 1 356 ? -27.363 -0.597  12.47  1    38.426  ? 392 MET   A CE  1 
ATOM   2892 N  N   . GLN   A 1 357 ? -25.035 4.731   12.329 1    28.848  ? 393 GLN   A N   1 
ATOM   2893 C  CA  . GLN   A 1 357 ? -25.371 6.057   12.805 1    25.129  ? 393 GLN   A CA  1 
ATOM   2894 C  C   . GLN   A 1 357 ? -24.433 7.09    12.2   1    30.223  ? 393 GLN   A C   1 
ATOM   2895 O  O   . GLN   A 1 357 ? -24.835 8.247   12.022 1    25.35   ? 393 GLN   A O   1 
ATOM   2896 C  CB  . GLN   A 1 357 ? -25.189 6.022   14.323 1    26.345  ? 393 GLN   A CB  1 
ATOM   2897 C  CG  . GLN   A 1 357 ? -26.273 5.188   15.032 1    31.454  ? 393 GLN   A CG  1 
ATOM   2898 C  CD  . GLN   A 1 357 ? -27.651 5.835   15.003 1    31.641  ? 393 GLN   A CD  1 
ATOM   2899 O  OE1 . GLN   A 1 357 ? -27.772 7.047   14.759 1    34.223  ? 393 GLN   A OE1 1 
ATOM   2900 N  NE2 . GLN   A 1 357 ? -28.711 5.057   15.238 1    28.192  ? 393 GLN   A NE2 1 
ATOM   2901 N  N   . TYR   A 1 358 ? -23.142 6.728   11.99  1    30.156  ? 394 TYR   A N   1 
ATOM   2902 C  CA  . TYR   A 1 358 ? -22.241 7.776   11.515 1    29.955  ? 394 TYR   A CA  1 
ATOM   2903 C  C   . TYR   A 1 358 ? -21.923 7.61    10.02  1    26.471  ? 394 TYR   A C   1 
ATOM   2904 O  O   . TYR   A 1 358 ? -20.953 8.161   9.551  1    26.346  ? 394 TYR   A O   1 
ATOM   2905 C  CB  . TYR   A 1 358 ? -21.031 7.975   12.44  1    24.727  ? 394 TYR   A CB  1 
ATOM   2906 C  CG  . TYR   A 1 358 ? -20.009 6.854   12.581 1    28.569  ? 394 TYR   A CG  1 
ATOM   2907 C  CD1 . TYR   A 1 358 ? -19.679 6.023   11.513 1    23.059  ? 394 TYR   A CD1 1 
ATOM   2908 C  CD2 . TYR   A 1 358 ? -19.383 6.585   13.826 1    25.543  ? 394 TYR   A CD2 1 
ATOM   2909 C  CE1 . TYR   A 1 358 ? -18.778 4.972   11.683 1    24.968  ? 394 TYR   A CE1 1 
ATOM   2910 C  CE2 . TYR   A 1 358 ? -18.473 5.544   13.981 1    22.234  ? 394 TYR   A CE2 1 
ATOM   2911 C  CZ  . TYR   A 1 358 ? -18.12  4.741   12.898 1    26.494  ? 394 TYR   A CZ  1 
ATOM   2912 O  OH  . TYR   A 1 358 ? -17.145 3.71    13.017 1    21.029  ? 394 TYR   A OH  1 
ATOM   2913 N  N   . LYS   A 1 359 ? -22.709 6.831   9.271  1    28.332  ? 395 LYS   A N   1 
ATOM   2914 C  CA  . LYS   A 1 359 ? -22.372 6.447   7.891  1    34.361  ? 395 LYS   A CA  1 
ATOM   2915 C  C   . LYS   A 1 359 ? -22.281 7.636   6.908  1    33.871  ? 395 LYS   A C   1 
ATOM   2916 O  O   . LYS   A 1 359 ? -21.651 7.504   5.865  1    29.164  ? 395 LYS   A O   1 
ATOM   2917 C  CB  . LYS   A 1 359 ? -23.317 5.33    7.397  1    28.314  ? 395 LYS   A CB  1 
ATOM   2918 C  CG  . LYS   A 1 359 ? -24.695 5.837   7.011  1    27.46   ? 395 LYS   A CG  1 
ATOM   2919 C  CD  . LYS   A 1 359 ? -25.817 4.796   6.872  1    38.504  ? 395 LYS   A CD  1 
ATOM   2920 C  CE  . LYS   A 1 359 ? -27.09  5.436   6.42   1    33.36   ? 395 LYS   A CE  1 
ATOM   2921 N  NZ  . LYS   A 1 359 ? -26.638 5.803   5.054  1    40.181  ? 395 LYS   A NZ  1 
ATOM   2922 N  N   . ASP   A 1 360 ? -22.868 8.799   7.255  1    39.606  ? 396 ASP   A N   1 
ATOM   2923 C  CA  . ASP   A 1 360 ? -22.97  9.985   6.405  1    53.588  ? 396 ASP   A CA  1 
ATOM   2924 C  C   . ASP   A 1 360 ? -21.945 11.073  6.737  1    52.821  ? 396 ASP   A C   1 
ATOM   2925 O  O   . ASP   A 1 360 ? -21.865 12.059  6.02   1    46.518  ? 396 ASP   A O   1 
ATOM   2926 C  CB  . ASP   A 1 360 ? -24.363 10.613  6.432  1    52.22   ? 396 ASP   A CB  1 
ATOM   2927 C  CG  . ASP   A 1 360 ? -25.444 9.695   5.877  1    60.126  ? 396 ASP   A CG  1 
ATOM   2928 O  OD1 . ASP   A 1 360 ? -25.107 8.923   4.946  1    54.118  ? 396 ASP   A OD1 1 
ATOM   2929 O  OD2 . ASP   A 1 360 ? -26.592 9.746   6.378  1    57.832  ? 396 ASP   A OD2 1 
ATOM   2930 N  N   . LEU   A 1 361 ? -21.162 10.92   7.803  1    40.246  ? 397 LEU   A N   1 
ATOM   2931 C  CA  . LEU   A 1 361 ? -20.079 11.863  8.038  1    36.652  ? 397 LEU   A CA  1 
ATOM   2932 C  C   . LEU   A 1 361 ? -18.993 11.622  6.986  1    31.032  ? 397 LEU   A C   1 
ATOM   2933 O  O   . LEU   A 1 361 ? -18.848 10.505  6.516  1    28.534  ? 397 LEU   A O   1 
ATOM   2934 C  CB  . LEU   A 1 361 ? -19.535 11.613  9.452  1    31.416  ? 397 LEU   A CB  1 
ATOM   2935 C  CG  . LEU   A 1 361 ? -20.462 11.968  10.626 1    33.46   ? 397 LEU   A CG  1 
ATOM   2936 C  CD1 . LEU   A 1 361 ? -19.86  11.782  11.995 1    25.412  ? 397 LEU   A CD1 1 
ATOM   2937 C  CD2 . LEU   A 1 361 ? -20.903 13.391  10.529 1    27.77   ? 397 LEU   A CD2 1 
ATOM   2938 N  N   . PRO   A 1 362 ? -18.09  12.589  6.689  1    39.398  ? 398 PRO   A N   1 
ATOM   2939 C  CA  . PRO   A 1 362 ? -16.795 12.238  6.061  1    38.367  ? 398 PRO   A CA  1 
ATOM   2940 C  C   . PRO   A 1 362 ? -16.038 11.131  6.807  1    42.135  ? 398 PRO   A C   1 
ATOM   2941 O  O   . PRO   A 1 362 ? -16.043 11.108  8.051  1    38.448  ? 398 PRO   A O   1 
ATOM   2942 C  CB  . PRO   A 1 362 ? -15.951 13.555  5.998  1    28.146  ? 398 PRO   A CB  1 
ATOM   2943 C  CG  . PRO   A 1 362 ? -16.8   14.575  6.708  1    32.062  ? 398 PRO   A CG  1 
ATOM   2944 C  CD  . PRO   A 1 362 ? -18.236 14.043  6.952  1    32.202  ? 398 PRO   A CD  1 
ATOM   2945 N  N   . VAL   A 1 363 ? -15.354 10.274  6.025  1    33.106  ? 399 VAL   A N   1 
ATOM   2946 C  CA  . VAL   A 1 363 ? -14.755 9.043   6.5    1    33.95   ? 399 VAL   A CA  1 
ATOM   2947 C  C   . VAL   A 1 363 ? -13.788 9.363   7.632  1    34.007  ? 399 VAL   A C   1 
ATOM   2948 O  O   . VAL   A 1 363 ? -13.693 8.58    8.584  1    31.644  ? 399 VAL   A O   1 
ATOM   2949 C  CB  . VAL   A 1 363 ? -14.138 8.032   5.505  1    43.596  ? 399 VAL   A CB  1 
ATOM   2950 C  CG1 . VAL   A 1 363 ? -15.047 7.734   4.316  1    56.687  ? 399 VAL   A CG1 1 
ATOM   2951 C  CG2 . VAL   A 1 363 ? -12.754 8.432   5.029  1    45.827  ? 399 VAL   A CG2 1 
ATOM   2952 N  N   . ALA   A 1 364 ? -13.117 10.519  7.548  1    27.379  ? 400 ALA   A N   1 
ATOM   2953 C  CA  . ALA   A 1 364 ? -12.059 10.792  8.499  1    29.982  ? 400 ALA   A CA  1 
ATOM   2954 C  C   . ALA   A 1 364 ? -12.683 10.936  9.882  1    28.176  ? 400 ALA   A C   1 
ATOM   2955 O  O   . ALA   A 1 364 ? -12.009 10.996  10.915 1    30.423  ? 400 ALA   A O   1 
ATOM   2956 C  CB  . ALA   A 1 364 ? -11.262 12.017  8.1    1    26.523  ? 400 ALA   A CB  1 
ATOM   2957 N  N   . LEU   A 1 365 ? -13.999 11.073  9.867  1    28.365  ? 401 LEU   A N   1 
ATOM   2958 C  CA  . LEU   A 1 365 ? -14.684 11.498  11.066 1    25.709  ? 401 LEU   A CA  1 
ATOM   2959 C  C   . LEU   A 1 365 ? -15.589 10.338  11.437 1    27.222  ? 401 LEU   A C   1 
ATOM   2960 O  O   . LEU   A 1 365 ? -16.422 10.506  12.33  1    28.06   ? 401 LEU   A O   1 
ATOM   2961 C  CB  . LEU   A 1 365 ? -15.494 12.793  10.899 1    30.114  ? 401 LEU   A CB  1 
ATOM   2962 C  CG  . LEU   A 1 365 ? -14.786 14.142  10.623 1    30.182  ? 401 LEU   A CG  1 
ATOM   2963 C  CD1 . LEU   A 1 365 ? -15.863 15.31   10.385 1    27.17   ? 401 LEU   A CD1 1 
ATOM   2964 C  CD2 . LEU   A 1 365 ? -13.806 14.543  11.729 1    19.382  ? 401 LEU   A CD2 1 
ATOM   2965 N  N   . ARG   A 1 366 ? -15.382 9.159   10.795 1    26.364  ? 402 ARG   A N   1 
ATOM   2966 C  CA  . ARG   A 1 366 ? -16.14  7.945   11.145 1    29.254  ? 402 ARG   A CA  1 
ATOM   2967 C  C   . ARG   A 1 366 ? -15.427 7.079   12.192 1    28.833  ? 402 ARG   A C   1 
ATOM   2968 O  O   . ARG   A 1 366 ? -14.746 6.079   11.916 1    32.668  ? 402 ARG   A O   1 
ATOM   2969 C  CB  . ARG   A 1 366 ? -16.427 7.125   9.894  1    28.277  ? 402 ARG   A CB  1 
ATOM   2970 C  CG  . ARG   A 1 366 ? -17.632 7.691   9.175  1    33.198  ? 402 ARG   A CG  1 
ATOM   2971 C  CD  . ARG   A 1 366 ? -17.666 6.832   7.978  1    36.897  ? 402 ARG   A CD  1 
ATOM   2972 N  NE  . ARG   A 1 366 ? -18.475 7.464   6.937  1    52.047  ? 402 ARG   A NE  1 
ATOM   2973 C  CZ  . ARG   A 1 366 ? -18.425 6.985   5.71   1    53.864  ? 402 ARG   A CZ  1 
ATOM   2974 N  NH1 . ARG   A 1 366 ? -17.375 6.277   5.32   1    45.04   ? 402 ARG   A NH1 1 
ATOM   2975 N  NH2 . ARG   A 1 366 ? -19.394 7.276   4.877  1    51.656  ? 402 ARG   A NH2 1 
ATOM   2976 N  N   . GLU   A 1 367 ? -15.595 7.487   13.432 1    26.181  ? 403 GLU   A N   1 
ATOM   2977 C  CA  . GLU   A 1 367 ? -15.003 6.831   14.586 1    27.931  ? 403 GLU   A CA  1 
ATOM   2978 C  C   . GLU   A 1 367 ? -15.837 7.224   15.777 1    22.605  ? 403 GLU   A C   1 
ATOM   2979 O  O   . GLU   A 1 367 ? -16.668 8.13    15.674 1    22.507  ? 403 GLU   A O   1 
ATOM   2980 C  CB  . GLU   A 1 367 ? -13.58  7.341   14.842 1    37.238  ? 403 GLU   A CB  1 
ATOM   2981 C  CG  . GLU   A 1 367 ? -12.578 6.68    13.897 1    58.629  ? 403 GLU   A CG  1 
ATOM   2982 C  CD  . GLU   A 1 367 ? -11.112 6.98    14.163 1    88.542  ? 403 GLU   A CD  1 
ATOM   2983 O  OE1 . GLU   A 1 367 ? -10.321 6.3     13.47  1    103.809 ? 403 GLU   A OE1 1 
ATOM   2984 O  OE2 . GLU   A 1 367 ? -10.74  7.842   15.014 1    74.608  ? 403 GLU   A OE2 1 
ATOM   2985 N  N   . GLY   A 1 368 ? -15.545 6.622   16.924 1    28.298  ? 404 GLY   A N   1 
ATOM   2986 C  CA  . GLY   A 1 368 ? -16.311 6.913   18.124 1    22.948  ? 404 GLY   A CA  1 
ATOM   2987 C  C   . GLY   A 1 368 ? -15.914 8.283   18.614 1    24.999  ? 404 GLY   A C   1 
ATOM   2988 O  O   . GLY   A 1 368 ? -14.863 8.8     18.234 1    29.048  ? 404 GLY   A O   1 
ATOM   2989 N  N   . ALA   A 1 369 ? -16.744 8.876   19.454 1    24.935  ? 405 ALA   A N   1 
ATOM   2990 C  CA  . ALA   A 1 369 ? -16.351 10.165  20     1    23.132  ? 405 ALA   A CA  1 
ATOM   2991 C  C   . ALA   A 1 369 ? -14.938 10.027  20.584 1    20.575  ? 405 ALA   A C   1 
ATOM   2992 O  O   . ALA   A 1 369 ? -14.115 10.963  20.556 1    22.5    ? 405 ALA   A O   1 
ATOM   2993 C  CB  . ALA   A 1 369 ? -17.403 10.593  21.041 1    22.28   ? 405 ALA   A CB  1 
ATOM   2994 N  N   . ASN   A 1 370 ? -14.716 8.87    21.218 1    19.054  ? 406 ASN   A N   1 
ATOM   2995 C  CA  . ASN   A 1 370 ? -13.4   8.357   21.582 1    21.062  ? 406 ASN   A CA  1 
ATOM   2996 C  C   . ASN   A 1 370 ? -13.521 6.852   21.441 1    20.77   ? 406 ASN   A C   1 
ATOM   2997 O  O   . ASN   A 1 370 ? -14.65  6.379   21.345 1    25.319  ? 406 ASN   A O   1 
ATOM   2998 C  CB  . ASN   A 1 370 ? -12.822 8.926   22.88  1    17.222  ? 406 ASN   A CB  1 
ATOM   2999 C  CG  . ASN   A 1 370 ? -13.395 8.304   24.143 1    19.879  ? 406 ASN   A CG  1 
ATOM   3000 O  OD1 . ASN   A 1 370 ? -13.626 7.086   24.191 1    20.92   ? 406 ASN   A OD1 1 
ATOM   3001 N  ND2 . ASN   A 1 370 ? -13.606 9.101   25.189 1    14.816  ? 406 ASN   A ND2 1 
ATOM   3002 N  N   . PRO   A 1 371 ? -12.412 6.069   21.396 1    25.486  ? 407 PRO   A N   1 
ATOM   3003 C  CA  . PRO   A 1 371 ? -12.486 4.605   21.19  1    21.675  ? 407 PRO   A CA  1 
ATOM   3004 C  C   . PRO   A 1 371 ? -13.295 3.945   22.303 1    21.866  ? 407 PRO   A C   1 
ATOM   3005 O  O   . PRO   A 1 371 ? -14.017 2.985   22.049 1    26.026  ? 407 PRO   A O   1 
ATOM   3006 C  CB  . PRO   A 1 371 ? -10.981 4.127   21.171 1    17.315  ? 407 PRO   A CB  1 
ATOM   3007 C  CG  . PRO   A 1 371 ? -10.247 5.376   20.805 1    20.063  ? 407 PRO   A CG  1 
ATOM   3008 C  CD  . PRO   A 1 371 ? -11.013 6.536   21.505 1    24.661  ? 407 PRO   A CD  1 
ATOM   3009 N  N   . GLY   A 1 372 ? -13.136 4.41    23.549 1    21.429  ? 408 GLY   A N   1 
ATOM   3010 C  CA  . GLY   A 1 372 ? -14.006 3.948   24.622 1    21.756  ? 408 GLY   A CA  1 
ATOM   3011 C  C   . GLY   A 1 372 ? -15.488 4.029   24.257 1    21.925  ? 408 GLY   A C   1 
ATOM   3012 O  O   . GLY   A 1 372 ? -16.262 3.136   24.628 1    24.52   ? 408 GLY   A O   1 
ATOM   3013 N  N   . PHE   A 1 373 ? -15.903 5.078   23.513 1    23.644  ? 409 PHE   A N   1 
ATOM   3014 C  CA  . PHE   A 1 373 ? -17.345 5.164   23.215 1    25.039  ? 409 PHE   A CA  1 
ATOM   3015 C  C   . PHE   A 1 373 ? -17.807 4.048   22.277 1    25.129  ? 409 PHE   A C   1 
ATOM   3016 O  O   . PHE   A 1 373 ? -18.967 3.611   22.344 1    22.154  ? 409 PHE   A O   1 
ATOM   3017 C  CB  . PHE   A 1 373 ? -17.895 6.408   22.534 1    23.427  ? 409 PHE   A CB  1 
ATOM   3018 C  CG  . PHE   A 1 373 ? -18.064 7.586   23.486 1    27.957  ? 409 PHE   A CG  1 
ATOM   3019 C  CD1 . PHE   A 1 373 ? -17.043 7.926   24.376 1    27.027  ? 409 PHE   A CD1 1 
ATOM   3020 C  CD2 . PHE   A 1 373 ? -19.245 8.344   23.491 1    24.958  ? 409 PHE   A CD2 1 
ATOM   3021 C  CE1 . PHE   A 1 373 ? -17.166 9.028   25.23  1    27.07   ? 409 PHE   A CE1 1 
ATOM   3022 C  CE2 . PHE   A 1 373 ? -19.362 9.416   24.377 1    25.426  ? 409 PHE   A CE2 1 
ATOM   3023 C  CZ  . PHE   A 1 373 ? -18.336 9.751   25.243 1    22.337  ? 409 PHE   A CZ  1 
ATOM   3024 N  N   . HIS   A 1 374 ? -16.91  3.657   21.349 1    25.212  ? 410 HIS   A N   1 
ATOM   3025 C  CA  . HIS   A 1 374 ? -17.237 2.66    20.343 1    29.256  ? 410 HIS   A CA  1 
ATOM   3026 C  C   . HIS   A 1 374 ? -17.475 1.323   21.061 1    27.563  ? 410 HIS   A C   1 
ATOM   3027 O  O   . HIS   A 1 374 ? -18.357 0.57    20.674 1    21.816  ? 410 HIS   A O   1 
ATOM   3028 C  CB  . HIS   A 1 374 ? -16.148 2.62    19.257 1    27.431  ? 410 HIS   A CB  1 
ATOM   3029 C  CG  . HIS   A 1 374 ? -16.71  2.354   17.882 1    31.134  ? 410 HIS   A CG  1 
ATOM   3030 N  ND1 . HIS   A 1 374 ? -17.494 1.262   17.558 1    29.03   ? 410 HIS   A ND1 1 
ATOM   3031 C  CD2 . HIS   A 1 374 ? -16.556 3.043   16.726 1    28.083  ? 410 HIS   A CD2 1 
ATOM   3032 C  CE1 . HIS   A 1 374 ? -17.796 1.311   16.251 1    32.209  ? 410 HIS   A CE1 1 
ATOM   3033 N  NE2 . HIS   A 1 374 ? -17.253 2.397   15.734 1    27.588  ? 410 HIS   A NE2 1 
ATOM   3034 N  N   . GLU   A 1 375 ? -16.723 1.105   22.166 1    28.356  ? 411 GLU   A N   1 
ATOM   3035 C  CA  . GLU   A 1 375 ? -16.685 -0.146  22.897 1    26.051  ? 411 GLU   A CA  1 
ATOM   3036 C  C   . GLU   A 1 375 ? -17.888 -0.204  23.828 1    27.647  ? 411 GLU   A C   1 
ATOM   3037 O  O   . GLU   A 1 375 ? -18.358 -1.289  24.163 1    34.442  ? 411 GLU   A O   1 
ATOM   3038 C  CB  . GLU   A 1 375 ? -15.421 -0.279  23.755 1    24.448  ? 411 GLU   A CB  1 
ATOM   3039 C  CG  . GLU   A 1 375 ? -14.157 -0.437  22.914 1    23.766  ? 411 GLU   A CG  1 
ATOM   3040 C  CD  . GLU   A 1 375 ? -14.196 -1.394  21.716 1    30.647  ? 411 GLU   A CD  1 
ATOM   3041 O  OE1 . GLU   A 1 375 ? -14.889 -2.455  21.866 1    26.872  ? 411 GLU   A OE1 1 
ATOM   3042 O  OE2 . GLU   A 1 375 ? -13.524 -1.115  20.668 1    26.681  ? 411 GLU   A OE2 1 
ATOM   3043 N  N   . ALA   A 1 376 ? -18.429 0.949   24.214 1    25.27   ? 412 ALA   A N   1 
ATOM   3044 C  CA  . ALA   A 1 376 ? -19.453 0.886   25.259 1    25.661  ? 412 ALA   A CA  1 
ATOM   3045 C  C   . ALA   A 1 376 ? -20.877 0.647   24.76  1    25.923  ? 412 ALA   A C   1 
ATOM   3046 O  O   . ALA   A 1 376 ? -21.641 0.065   25.516 1    22.216  ? 412 ALA   A O   1 
ATOM   3047 C  CB  . ALA   A 1 376 ? -19.4   2.042   26.222 1    24.027  ? 412 ALA   A CB  1 
ATOM   3048 N  N   . ILE   A 1 377 ? -21.26  1.071   23.536 1    27.816  ? 413 ILE   A N   1 
ATOM   3049 C  CA  . ILE   A 1 377 ? -22.657 0.951   23.077 1    26.845  ? 413 ILE   A CA  1 
ATOM   3050 C  C   . ILE   A 1 377 ? -23.239 -0.464  23.299 1    32.147  ? 413 ILE   A C   1 
ATOM   3051 O  O   . ILE   A 1 377 ? -24.268 -0.659  23.96  1    30.426  ? 413 ILE   A O   1 
ATOM   3052 C  CB  . ILE   A 1 377 ? -22.833 1.37    21.597 1    25.99   ? 413 ILE   A CB  1 
ATOM   3053 C  CG1 . ILE   A 1 377 ? -22.266 2.782   21.297 1    28.665  ? 413 ILE   A CG1 1 
ATOM   3054 C  CG2 . ILE   A 1 377 ? -24.294 1.224   21.167 1    22.044  ? 413 ILE   A CG2 1 
ATOM   3055 C  CD1 . ILE   A 1 377 ? -22.804 3.873   22.217 1    28.681  ? 413 ILE   A CD1 1 
ATOM   3056 N  N   . GLY   A 1 378 ? -22.644 -1.48   22.662 1    27.219  ? 414 GLY   A N   1 
ATOM   3057 C  CA  . GLY   A 1 378 ? -23.244 -2.782  22.843 1    24.556  ? 414 GLY   A CA  1 
ATOM   3058 C  C   . GLY   A 1 378 ? -23.342 -3.133  24.32  1    26.821  ? 414 GLY   A C   1 
ATOM   3059 O  O   . GLY   A 1 378 ? -24.304 -3.789  24.725 1    28.594  ? 414 GLY   A O   1 
ATOM   3060 N  N   . ASP   A 1 379 ? -22.31  -2.767  25.092 1    27.723  ? 415 ASP   A N   1 
ATOM   3061 C  CA  . ASP   A 1 379 ? -22.301 -3.188  26.49  1    27.159  ? 415 ASP   A CA  1 
ATOM   3062 C  C   . ASP   A 1 379 ? -23.448 -2.63   27.296 1    25.245  ? 415 ASP   A C   1 
ATOM   3063 O  O   . ASP   A 1 379 ? -23.991 -3.349  28.113 1    26.484  ? 415 ASP   A O   1 
ATOM   3064 C  CB  . ASP   A 1 379 ? -20.977 -3.041  27.199 1    33.429  ? 415 ASP   A CB  1 
ATOM   3065 C  CG  . ASP   A 1 379 ? -19.966 -4.093  26.756 1    44.664  ? 415 ASP   A CG  1 
ATOM   3066 O  OD1 . ASP   A 1 379 ? -20.151 -4.671  25.646 1    44.171  ? 415 ASP   A OD1 1 
ATOM   3067 O  OD2 . ASP   A 1 379 ? -19.025 -4.343  27.537 1    45.807  ? 415 ASP   A OD2 1 
ATOM   3068 N  N   . VAL   A 1 380 ? -23.762 -1.351  27.095 1    24.728  ? 416 VAL   A N   1 
ATOM   3069 C  CA  . VAL   A 1 380 ? -24.875 -0.715  27.747 1    24.419  ? 416 VAL   A CA  1 
ATOM   3070 C  C   . VAL   A 1 380 ? -26.16  -1.535  27.587 1    34.667  ? 416 VAL   A C   1 
ATOM   3071 O  O   . VAL   A 1 380 ? -26.789 -1.881  28.59  1    38.987  ? 416 VAL   A O   1 
ATOM   3072 C  CB  . VAL   A 1 380 ? -25.076 0.713   27.253 1    24.321  ? 416 VAL   A CB  1 
ATOM   3073 C  CG1 . VAL   A 1 380 ? -26.324 1.246   27.929 1    21.17   ? 416 VAL   A CG1 1 
ATOM   3074 C  CG2 . VAL   A 1 380 ? -23.869 1.558   27.629 1    23.06   ? 416 VAL   A CG2 1 
ATOM   3075 N  N   . LEU   A 1 381 ? -26.543 -1.867  26.349 1    29.429  ? 417 LEU   A N   1 
ATOM   3076 C  CA  . LEU   A 1 381 ? -27.765 -2.626  26.17  1    28.995  ? 417 LEU   A CA  1 
ATOM   3077 C  C   . LEU   A 1 381 ? -27.656 -3.957  26.916 1    25.817  ? 417 LEU   A C   1 
ATOM   3078 O  O   . LEU   A 1 381 ? -28.619 -4.427  27.598 1    22.759  ? 417 LEU   A O   1 
ATOM   3079 C  CB  . LEU   A 1 381 ? -28.056 -2.815  24.668 1    32.323  ? 417 LEU   A CB  1 
ATOM   3080 C  CG  . LEU   A 1 381 ? -28.865 -1.733  23.948 1    27.882  ? 417 LEU   A CG  1 
ATOM   3081 C  CD1 . LEU   A 1 381 ? -28.146 -0.41   23.813 1    30.31   ? 417 LEU   A CD1 1 
ATOM   3082 C  CD2 . LEU   A 1 381 ? -29.307 -2.199  22.581 1    28.085  ? 417 LEU   A CD2 1 
ATOM   3083 N  N   . ALA   A 1 382 ? -26.488 -4.592  26.76  1    20.66   ? 418 ALA   A N   1 
ATOM   3084 C  CA  . ALA   A 1 382 ? -26.367 -5.914  27.377 1    21.277  ? 418 ALA   A CA  1 
ATOM   3085 C  C   . ALA   A 1 382 ? -26.485 -5.866  28.912 1    22.485  ? 418 ALA   A C   1 
ATOM   3086 O  O   . ALA   A 1 382 ? -26.589 -6.926  29.539 1    21.864  ? 418 ALA   A O   1 
ATOM   3087 C  CB  . ALA   A 1 382 ? -25.119 -6.654  26.984 1    18.203  ? 418 ALA   A CB  1 
ATOM   3088 N  N   . LEU   A 1 383 ? -26.409 -4.686  29.546 1    19.058  ? 419 LEU   A N   1 
ATOM   3089 C  CA  . LEU   A 1 383 ? -26.524 -4.723  31.003 1    26.698  ? 419 LEU   A CA  1 
ATOM   3090 C  C   . LEU   A 1 383 ? -28.006 -4.923  31.344 1    30.857  ? 419 LEU   A C   1 
ATOM   3091 O  O   . LEU   A 1 383 ? -28.34  -5.421  32.423 1    27.303  ? 419 LEU   A O   1 
ATOM   3092 C  CB  . LEU   A 1 383 ? -26.063 -3.391  31.572 1    29.134  ? 419 LEU   A CB  1 
ATOM   3093 C  CG  . LEU   A 1 383 ? -24.56  -3.204  31.727 1    33.474  ? 419 LEU   A CG  1 
ATOM   3094 C  CD1 . LEU   A 1 383 ? -24.411 -1.717  31.695 1    26.561  ? 419 LEU   A CD1 1 
ATOM   3095 C  CD2 . LEU   A 1 383 ? -24.298 -3.702  33.133 1    39.331  ? 419 LEU   A CD2 1 
ATOM   3096 N  N   . SER   A 1 384 ? -28.871 -4.43   30.438 1    23.781  ? 420 SER   A N   1 
ATOM   3097 C  CA  . SER   A 1 384 ? -30.309 -4.559  30.552 1    30.422  ? 420 SER   A CA  1 
ATOM   3098 C  C   . SER   A 1 384 ? -30.699 -6.013  30.266 1    34.214  ? 420 SER   A C   1 
ATOM   3099 O  O   . SER   A 1 384 ? -31.558 -6.575  30.977 1    29.272  ? 420 SER   A O   1 
ATOM   3100 C  CB  . SER   A 1 384 ? -31.05  -3.54   29.683 1    29.723  ? 420 SER   A CB  1 
ATOM   3101 O  OG  . SER   A 1 384 ? -31.197 -2.288  30.359 1    27.915  ? 420 SER   A OG  1 
ATOM   3102 N  N   . VAL   A 1 385 ? -29.992 -6.62   29.286 1    29.02   ? 421 VAL   A N   1 
ATOM   3103 C  CA  . VAL   A 1 385 ? -30.365 -7.928  28.791 1    26.778  ? 421 VAL   A CA  1 
ATOM   3104 C  C   . VAL   A 1 385 ? -30.114 -8.896  29.955 1    27.883  ? 421 VAL   A C   1 
ATOM   3105 O  O   . VAL   A 1 385 ? -30.728 -9.944  30.095 1    31.031  ? 421 VAL   A O   1 
ATOM   3106 C  CB  . VAL   A 1 385 ? -29.668 -8.435  27.504 1    28.871  ? 421 VAL   A CB  1 
ATOM   3107 C  CG1 . VAL   A 1 385 ? -30.233 -9.788  27.107 1    26.445  ? 421 VAL   A CG1 1 
ATOM   3108 C  CG2 . VAL   A 1 385 ? -29.711 -7.509  26.272 1    25.956  ? 421 VAL   A CG2 1 
ATOM   3109 N  N   . SER   A 1 386 ? -29.205 -8.528  30.836 1    28.629  ? 422 SER   A N   1 
ATOM   3110 C  CA  . SER   A 1 386 ? -28.634 -9.494  31.735 1    25.39   ? 422 SER   A CA  1 
ATOM   3111 C  C   . SER   A 1 386 ? -29.465 -9.489  32.994 1    29.335  ? 422 SER   A C   1 
ATOM   3112 O  O   . SER   A 1 386 ? -29.162 -10.193 33.948 1    38.442  ? 422 SER   A O   1 
ATOM   3113 C  CB  . SER   A 1 386 ? -27.222 -9.116  32.038 1    26.333  ? 422 SER   A CB  1 
ATOM   3114 O  OG  . SER   A 1 386 ? -26.455 -9.417  30.89  1    30.915  ? 422 SER   A OG  1 
ATOM   3115 N  N   . THR   A 1 387 ? -30.452 -8.608  33.034 1    31.548  ? 423 THR   A N   1 
ATOM   3116 C  CA  . THR   A 1 387 ? -31.208 -8.533  34.273 1    36.307  ? 423 THR   A CA  1 
ATOM   3117 C  C   . THR   A 1 387 ? -32.058 -9.789  34.364 1    36.703  ? 423 THR   A C   1 
ATOM   3118 O  O   . THR   A 1 387 ? -32.534 -10.341 33.358 1    34.669  ? 423 THR   A O   1 
ATOM   3119 C  CB  . THR   A 1 387 ? -32.038 -7.253  34.454 1    31.628  ? 423 THR   A CB  1 
ATOM   3120 O  OG1 . THR   A 1 387 ? -32.835 -7.066  33.277 1    27.021  ? 423 THR   A OG1 1 
ATOM   3121 C  CG2 . THR   A 1 387 ? -31.144 -6.07   34.758 1    31.797  ? 423 THR   A CG2 1 
ATOM   3122 N  N   . PRO   A 1 388 ? -32.269 -10.253 35.602 1    39.43   ? 424 PRO   A N   1 
ATOM   3123 C  CA  . PRO   A 1 388 ? -33.119 -11.416 35.819 1    46.212  ? 424 PRO   A CA  1 
ATOM   3124 C  C   . PRO   A 1 388 ? -34.451 -11.251 35.086 1    45.493  ? 424 PRO   A C   1 
ATOM   3125 O  O   . PRO   A 1 388 ? -34.861 -12.138 34.344 1    46.341  ? 424 PRO   A O   1 
ATOM   3126 C  CB  . PRO   A 1 388 ? -33.227 -11.424 37.379 1    47.851  ? 424 PRO   A CB  1 
ATOM   3127 C  CG  . PRO   A 1 388 ? -31.914 -10.797 37.856 1    44.517  ? 424 PRO   A CG  1 
ATOM   3128 C  CD  . PRO   A 1 388 ? -31.689 -9.687  36.837 1    44.976  ? 424 PRO   A CD  1 
ATOM   3129 N  N   . LYS   A 1 389 ? -35.094 -10.094 35.275 1    46.582  ? 425 LYS   A N   1 
ATOM   3130 C  CA  . LYS   A 1 389 ? -36.364 -9.791  34.637 1    49.286  ? 425 LYS   A CA  1 
ATOM   3131 C  C   . LYS   A 1 389 ? -36.304 -10.02  33.114 1    43.915  ? 425 LYS   A C   1 
ATOM   3132 O  O   . LYS   A 1 389 ? -37.133 -10.749 32.558 1    39.58   ? 425 LYS   A O   1 
ATOM   3133 C  CB  . LYS   A 1 389 ? -36.608 -8.344  35.068 1    58.178  ? 425 LYS   A CB  1 
ATOM   3134 C  CG  . LYS   A 1 389 ? -37.991 -7.808  34.806 1    71.193  ? 425 LYS   A CG  1 
ATOM   3135 C  CD  . LYS   A 1 389 ? -37.811 -6.327  34.508 1    85.754  ? 425 LYS   A CD  1 
ATOM   3136 C  CE  . LYS   A 1 389 ? -38.771 -5.914  33.442 1    91.995  ? 425 LYS   A CE  1 
ATOM   3137 N  NZ  . LYS   A 1 389 ? -38.698 -4.46   33.359 1    75.933  ? 425 LYS   A NZ  1 
ATOM   3138 N  N   . HIS   A 1 390 ? -35.317 -9.407  32.432 1    37.511  ? 426 HIS   A N   1 
ATOM   3139 C  CA  . HIS   A 1 390 ? -35.199 -9.52   30.982 1    31.264  ? 426 HIS   A CA  1 
ATOM   3140 C  C   . HIS   A 1 390 ? -34.984 -10.988 30.579 1    30.454  ? 426 HIS   A C   1 
ATOM   3141 O  O   . HIS   A 1 390 ? -35.575 -11.5   29.618 1    30.523  ? 426 HIS   A O   1 
ATOM   3142 C  CB  . HIS   A 1 390 ? -34.151 -8.551  30.416 1    28.02   ? 426 HIS   A CB  1 
ATOM   3143 C  CG  . HIS   A 1 390 ? -34.224 -8.523  28.924 1    26.239  ? 426 HIS   A CG  1 
ATOM   3144 N  ND1 . HIS   A 1 390 ? -33.519 -9.389  28.14  1    30.542  ? 426 HIS   A ND1 1 
ATOM   3145 C  CD2 . HIS   A 1 390 ? -35.033 -7.893  28.071 1    29.323  ? 426 HIS   A CD2 1 
ATOM   3146 C  CE1 . HIS   A 1 390 ? -33.85  -9.226  26.851 1    28.841  ? 426 HIS   A CE1 1 
ATOM   3147 N  NE2 . HIS   A 1 390 ? -34.802 -8.346  26.791 1    26.447  ? 426 HIS   A NE2 1 
ATOM   3148 N  N   . LEU   A 1 391 ? -34.134 -11.69  31.327 1    29.662  ? 427 LEU   A N   1 
ATOM   3149 C  CA  . LEU   A 1 391 ? -33.835 -13.097 31.039 1    29.781  ? 427 LEU   A CA  1 
ATOM   3150 C  C   . LEU   A 1 391 ? -35.068 -13.994 31.282 1    30.247  ? 427 LEU   A C   1 
ATOM   3151 O  O   . LEU   A 1 391 ? -35.339 -14.866 30.465 1    25.426  ? 427 LEU   A O   1 
ATOM   3152 C  CB  . LEU   A 1 391 ? -32.614 -13.558 31.845 1    26.202  ? 427 LEU   A CB  1 
ATOM   3153 C  CG  . LEU   A 1 391 ? -31.235 -13.039 31.426 1    26.629  ? 427 LEU   A CG  1 
ATOM   3154 C  CD1 . LEU   A 1 391 ? -30.129 -13.634 32.342 1    25.146  ? 427 LEU   A CD1 1 
ATOM   3155 C  CD2 . LEU   A 1 391 ? -30.93  -13.314 29.949 1    24.26   ? 427 LEU   A CD2 1 
ATOM   3156 N  N   . HIS   A 1 392 ? -35.811 -13.787 32.399 1    31.277  ? 428 HIS   A N   1 
ATOM   3157 C  CA  . HIS   A 1 392 ? -37.143 -14.366 32.565 1    33.494  ? 428 HIS   A CA  1 
ATOM   3158 C  C   . HIS   A 1 392 ? -37.972 -14.202 31.295 1    31.632  ? 428 HIS   A C   1 
ATOM   3159 O  O   . HIS   A 1 392 ? -38.611 -15.129 30.833 1    31.58   ? 428 HIS   A O   1 
ATOM   3160 C  CB  . HIS   A 1 392 ? -38.011 -13.688 33.632 1    33.56   ? 428 HIS   A CB  1 
ATOM   3161 C  CG  . HIS   A 1 392 ? -39.304 -14.427 33.828 1    53.116  ? 428 HIS   A CG  1 
ATOM   3162 N  ND1 . HIS   A 1 392 ? -39.41  -15.811 33.7   1    59.471  ? 428 HIS   A ND1 1 
ATOM   3163 C  CD2 . HIS   A 1 392 ? -40.548 -13.979 34.07  1    52.992  ? 428 HIS   A CD2 1 
ATOM   3164 C  CE1 . HIS   A 1 392 ? -40.675 -16.174 33.862 1    56.619  ? 428 HIS   A CE1 1 
ATOM   3165 N  NE2 . HIS   A 1 392 ? -41.376 -15.079 34.095 1    57.317  ? 428 HIS   A NE2 1 
ATOM   3166 N  N   . SER   A 1 393 ? -37.98  -13.012 30.739 1    34.127  ? 429 SER   A N   1 
ATOM   3167 C  CA  . SER   A 1 393 ? -38.891 -12.77  29.643 1    39.92   ? 429 SER   A CA  1 
ATOM   3168 C  C   . SER   A 1 393 ? -38.335 -13.412 28.358 1    39.4    ? 429 SER   A C   1 
ATOM   3169 O  O   . SER   A 1 393 ? -39.026 -13.518 27.332 1    30.462  ? 429 SER   A O   1 
ATOM   3170 C  CB  . SER   A 1 393 ? -39.126 -11.272 29.502 1    36.428  ? 429 SER   A CB  1 
ATOM   3171 O  OG  . SER   A 1 393 ? -38.019 -10.724 28.797 1    32.349  ? 429 SER   A OG  1 
ATOM   3172 N  N   . LEU   A 1 394 ? -37.075 -13.858 28.421 1    29.202  ? 430 LEU   A N   1 
ATOM   3173 C  CA  . LEU   A 1 394 ? -36.542 -14.549 27.274 1    30.047  ? 430 LEU   A CA  1 
ATOM   3174 C  C   . LEU   A 1 394 ? -36.824 -16.04  27.449 1    34.812  ? 430 LEU   A C   1 
ATOM   3175 O  O   . LEU   A 1 394 ? -36.375 -16.883 26.658 1    30.681  ? 430 LEU   A O   1 
ATOM   3176 C  CB  . LEU   A 1 394 ? -35.053 -14.23  27.117 1    36.312  ? 430 LEU   A CB  1 
ATOM   3177 C  CG  . LEU   A 1 394 ? -34.749 -12.87  26.473 1    39.177  ? 430 LEU   A CG  1 
ATOM   3178 C  CD1 . LEU   A 1 394 ? -33.261 -12.693 26.455 1    30.95   ? 430 LEU   A CD1 1 
ATOM   3179 C  CD2 . LEU   A 1 394 ? -35.313 -12.68  25.042 1    32.883  ? 430 LEU   A CD2 1 
ATOM   3180 N  N   . ASN   A 1 395 ? -37.607 -16.369 28.486 1    33.367  ? 431 ASN   A N   1 
ATOM   3181 C  CA  . ASN   A 1 395 ? -37.795 -17.772 28.849 1    40.905  ? 431 ASN   A CA  1 
ATOM   3182 C  C   . ASN   A 1 395 ? -36.446 -18.479 29.161 1    38.543  ? 431 ASN   A C   1 
ATOM   3183 O  O   . ASN   A 1 395 ? -36.296 -19.649 28.85  1    40.94   ? 431 ASN   A O   1 
ATOM   3184 C  CB  . ASN   A 1 395 ? -38.819 -18.407 27.896 1    45.217  ? 431 ASN   A CB  1 
ATOM   3185 C  CG  . ASN   A 1 395 ? -39.247 -19.792 28.331 1    50.531  ? 431 ASN   A CG  1 
ATOM   3186 O  OD1 . ASN   A 1 395 ? -39.663 -19.99  29.472 1    44.627  ? 431 ASN   A OD1 1 
ATOM   3187 N  ND2 . ASN   A 1 395 ? -39.093 -20.78  27.462 1    52.946  ? 431 ASN   A ND2 1 
ATOM   3188 N  N   . LEU   A 1 396 ? -35.483 -17.805 29.826 1    30.324  ? 432 LEU   A N   1 
ATOM   3189 C  CA  . LEU   A 1 396 ? -34.148 -18.352 30.065 1    33.613  ? 432 LEU   A CA  1 
ATOM   3190 C  C   . LEU   A 1 396 ? -33.915 -18.387 31.565 1    32.535  ? 432 LEU   A C   1 
ATOM   3191 O  O   . LEU   A 1 396 ? -32.861 -18.744 32.029 1    32.77   ? 432 LEU   A O   1 
ATOM   3192 C  CB  . LEU   A 1 396 ? -32.949 -17.647 29.419 1    31.595  ? 432 LEU   A CB  1 
ATOM   3193 C  CG  . LEU   A 1 396 ? -32.936 -17.441 27.902 1    34.166  ? 432 LEU   A CG  1 
ATOM   3194 C  CD1 . LEU   A 1 396 ? -31.675 -16.664 27.455 1    31.652  ? 432 LEU   A CD1 1 
ATOM   3195 C  CD2 . LEU   A 1 396 ? -33.067 -18.745 27.124 1    33.526  ? 432 LEU   A CD2 1 
ATOM   3196 N  N   . LEU   A 1 397 ? -34.906 -17.986 32.333 1    39.73   ? 433 LEU   A N   1 
ATOM   3197 C  CA  . LEU   A 1 397 ? -34.773 -18.08  33.773 1    39.729  ? 433 LEU   A CA  1 
ATOM   3198 C  C   . LEU   A 1 397 ? -36.196 -18.194 34.317 1    42.67   ? 433 LEU   A C   1 
ATOM   3199 O  O   . LEU   A 1 397 ? -37.125 -17.926 33.575 1    49.48   ? 433 LEU   A O   1 
ATOM   3200 C  CB  . LEU   A 1 397 ? -33.984 -16.854 34.237 1    37.143  ? 433 LEU   A CB  1 
ATOM   3201 C  CG  . LEU   A 1 397 ? -33.954 -16.52  35.735 1    48.925  ? 433 LEU   A CG  1 
ATOM   3202 C  CD1 . LEU   A 1 397 ? -33.409 -17.62  36.715 1    47.049  ? 433 LEU   A CD1 1 
ATOM   3203 C  CD2 . LEU   A 1 397 ? -33.249 -15.166 35.905 1    41.341  ? 433 LEU   A CD2 1 
ATOM   3204 N  N   . SER   A 1 398 ? -36.349 -18.649 35.568 1    53.833  ? 434 SER   A N   1 
ATOM   3205 C  CA  . SER   A 1 398 ? -37.627 -18.906 36.229 1    54.42   ? 434 SER   A CA  1 
ATOM   3206 C  C   . SER   A 1 398 ? -38.236 -17.656 36.883 1    63.481  ? 434 SER   A C   1 
ATOM   3207 O  O   . SER   A 1 398 ? -39.465 -17.554 36.956 1    54.726  ? 434 SER   A O   1 
ATOM   3208 C  CB  . SER   A 1 398 ? -37.455 -20.01  37.238 1    47.94   ? 434 SER   A CB  1 
ATOM   3209 O  OG  . SER   A 1 398 ? -37.672 -21.224 36.543 1    53.129  ? 434 SER   A OG  1 
ATOM   3210 N  N   . SER   A 1 399 ? -37.358 -16.741 37.356 1    69.829  ? 435 SER   A N   1 
ATOM   3211 C  CA  . SER   A 1 399 ? -37.609 -15.515 38.116 1    80.48   ? 435 SER   A CA  1 
ATOM   3212 C  C   . SER   A 1 399 ? -38.938 -15.563 38.885 1    67.414  ? 435 SER   A C   1 
ATOM   3213 O  O   . SER   A 1 399 ? -38.964 -16.332 39.85  1    54.209  ? 435 SER   A O   1 
ATOM   3214 C  CB  . SER   A 1 399 ? -37.465 -14.252 37.279 1    88.777  ? 435 SER   A CB  1 
ATOM   3215 O  OG  . SER   A 1 399 ? -37.524 -13.071 38.077 1    93.169  ? 435 SER   A OG  1 
ATOM   3216 N  N   . GLY   A 1 402 ? -37.014 -11.526 42.64  1    49.72   ? 438 GLY   A N   1 
ATOM   3217 C  CA  . GLY   A 1 402 ? -37.615 -11.039 43.903 1    63.773  ? 438 GLY   A CA  1 
ATOM   3218 C  C   . GLY   A 1 402 ? -36.61  -10.478 44.923 1    71.959  ? 438 GLY   A C   1 
ATOM   3219 O  O   . GLY   A 1 402 ? -36.304 -9.287  44.917 1    69.117  ? 438 GLY   A O   1 
ATOM   3220 N  N   . SER   A 1 403 ? -36.092 -11.351 45.803 1    80.9    ? 439 SER   A N   1 
ATOM   3221 C  CA  . SER   A 1 403 ? -35.609 -11.005 47.143 1    72.269  ? 439 SER   A CA  1 
ATOM   3222 C  C   . SER   A 1 403 ? -34.27  -10.267 47.173 1    62.703  ? 439 SER   A C   1 
ATOM   3223 O  O   . SER   A 1 403 ? -33.687 -9.943  46.14  1    64.479  ? 439 SER   A O   1 
ATOM   3224 C  CB  . SER   A 1 403 ? -35.522 -12.223 48.016 1    55.157  ? 439 SER   A CB  1 
ATOM   3225 O  OG  . SER   A 1 403 ? -34.763 -13.226 47.353 1    58.903  ? 439 SER   A OG  1 
ATOM   3226 N  N   . ASP   A 1 404 ? -33.818 -9.994  48.406 1    55.408  ? 440 ASP   A N   1 
ATOM   3227 C  CA  . ASP   A 1 404 ? -32.524 -9.394  48.692 1    62.504  ? 440 ASP   A CA  1 
ATOM   3228 C  C   . ASP   A 1 404 ? -31.462 -10.419 48.316 1    57.513  ? 440 ASP   A C   1 
ATOM   3229 O  O   . ASP   A 1 404 ? -30.455 -10.077 47.707 1    51.016  ? 440 ASP   A O   1 
ATOM   3230 C  CB  . ASP   A 1 404 ? -32.373 -8.959  50.149 1    64.822  ? 440 ASP   A CB  1 
ATOM   3231 C  CG  . ASP   A 1 404 ? -32.858 -7.557  50.531 1    78.809  ? 440 ASP   A CG  1 
ATOM   3232 O  OD1 . ASP   A 1 404 ? -33.992 -7.175  50.146 1    83.945  ? 440 ASP   A OD1 1 
ATOM   3233 O  OD2 . ASP   A 1 404 ? -32.124 -6.851  51.266 1    75.239  ? 440 ASP   A OD2 1 
ATOM   3234 N  N   . GLU   A 1 405 ? -31.745 -11.679 48.654 1    60.111  ? 441 GLU   A N   1 
ATOM   3235 C  CA  . GLU   A 1 405 ? -30.906 -12.8   48.286 1    56.123  ? 441 GLU   A CA  1 
ATOM   3236 C  C   . GLU   A 1 405 ? -30.694 -12.832 46.771 1    61.079  ? 441 GLU   A C   1 
ATOM   3237 O  O   . GLU   A 1 405 ? -29.537 -12.798 46.35  1    54.672  ? 441 GLU   A O   1 
ATOM   3238 C  CB  . GLU   A 1 405 ? -31.404 -14.124 48.866 1    61.171  ? 441 GLU   A CB  1 
ATOM   3239 C  CG  . GLU   A 1 405 ? -31.547 -14.112 50.388 1    68.039  ? 441 GLU   A CG  1 
ATOM   3240 C  CD  . GLU   A 1 405 ? -31.46  -15.536 50.92  1    67.215  ? 441 GLU   A CD  1 
ATOM   3241 O  OE1 . GLU   A 1 405 ? -31.653 -16.48  50.121 1    74.365  ? 441 GLU   A OE1 1 
ATOM   3242 O  OE2 . GLU   A 1 405 ? -31.155 -15.721 52.115 1    57.612  ? 441 GLU   A OE2 1 
ATOM   3243 N  N   . HIS   A 1 406 ? -31.783 -12.897 45.967 1    50.382  ? 442 HIS   A N   1 
ATOM   3244 C  CA  . HIS   A 1 406 ? -31.652 -13.038 44.517 1    49.012  ? 442 HIS   A CA  1 
ATOM   3245 C  C   . HIS   A 1 406 ? -30.797 -11.908 43.935 1    45.293  ? 442 HIS   A C   1 
ATOM   3246 O  O   . HIS   A 1 406 ? -30.007 -12.133 43.02  1    33.538  ? 442 HIS   A O   1 
ATOM   3247 C  CB  . HIS   A 1 406 ? -33.006 -13.133 43.803 1    68.675  ? 442 HIS   A CB  1 
ATOM   3248 C  CG  . HIS   A 1 406 ? -33.598 -14.511 43.706 1    102.676 ? 442 HIS   A CG  1 
ATOM   3249 N  ND1 . HIS   A 1 406 ? -34.577 -14.986 44.562 1    105.912 ? 442 HIS   A ND1 1 
ATOM   3250 C  CD2 . HIS   A 1 406 ? -33.366 -15.507 42.82  1    98.37   ? 442 HIS   A CD2 1 
ATOM   3251 C  CE1 . HIS   A 1 406 ? -34.911 -16.226 44.213 1    92.821  ? 442 HIS   A CE1 1 
ATOM   3252 N  NE2 . HIS   A 1 406 ? -34.182 -16.566 43.164 1    90.094  ? 442 HIS   A NE2 1 
ATOM   3253 N  N   . ASP   A 1 407 ? -30.974 -10.706 44.499 1    43.613  ? 443 ASP   A N   1 
ATOM   3254 C  CA  . ASP   A 1 407 ? -30.303 -9.48   44.109 1    40.353  ? 443 ASP   A CA  1 
ATOM   3255 C  C   . ASP   A 1 407 ? -28.783 -9.588  44.209 1    44.256  ? 443 ASP   A C   1 
ATOM   3256 O  O   . ASP   A 1 407 ? -28.103 -9.331  43.207 1    37.102  ? 443 ASP   A O   1 
ATOM   3257 C  CB  . ASP   A 1 407 ? -30.75  -8.303  44.957 1    39.18   ? 443 ASP   A CB  1 
ATOM   3258 C  CG  . ASP   A 1 407 ? -31.731 -7.371  44.268 1    59.238  ? 443 ASP   A CG  1 
ATOM   3259 O  OD1 . ASP   A 1 407 ? -32.233 -7.764  43.189 1    66.983  ? 443 ASP   A OD1 1 
ATOM   3260 O  OD2 . ASP   A 1 407 ? -31.972 -6.263  44.81  1    70.014  ? 443 ASP   A OD2 1 
ATOM   3261 N  N   . ILE   A 1 408 ? -28.285 -9.866  45.441 1    35.998  ? 444 ILE   A N   1 
ATOM   3262 C  CA  . ILE   A 1 408 ? -26.88  -10.049 45.749 1    29.863  ? 444 ILE   A CA  1 
ATOM   3263 C  C   . ILE   A 1 408 ? -26.28  -11.089 44.792 1    29.057  ? 444 ILE   A C   1 
ATOM   3264 O  O   . ILE   A 1 408 ? -25.17  -10.894 44.308 1    26.724  ? 444 ILE   A O   1 
ATOM   3265 C  CB  . ILE   A 1 408 ? -26.695 -10.493 47.216 1    26.028  ? 444 ILE   A CB  1 
ATOM   3266 C  CG1 . ILE   A 1 408 ? -27.075 -9.423  48.19  1    25.967  ? 444 ILE   A CG1 1 
ATOM   3267 C  CG2 . ILE   A 1 408 ? -25.273 -10.974 47.46  1    24.481  ? 444 ILE   A CG2 1 
ATOM   3268 C  CD1 . ILE   A 1 408 ? -26.516 -8.058  47.829 1    24.208  ? 444 ILE   A CD1 1 
ATOM   3269 N  N   . ASN   A 1 409 ? -26.999 -12.194 44.558 1    23.417  ? 445 ASN   A N   1 
ATOM   3270 C  CA  . ASN   A 1 409 ? -26.514 -13.241 43.671 1    30.439  ? 445 ASN   A CA  1 
ATOM   3271 C  C   . ASN   A 1 409 ? -26.247 -12.646 42.275 1    29.966  ? 445 ASN   A C   1 
ATOM   3272 O  O   . ASN   A 1 409 ? -25.171 -12.863 41.686 1    27.27   ? 445 ASN   A O   1 
ATOM   3273 C  CB  . ASN   A 1 409 ? -27.445 -14.461 43.547 1    28.857  ? 445 ASN   A CB  1 
ATOM   3274 C  CG  . ASN   A 1 409 ? -27.385 -15.511 44.659 1    41.68   ? 445 ASN   A CG  1 
ATOM   3275 O  OD1 . ASN   A 1 409 ? -26.515 -15.51  45.545 1    35.972  ? 445 ASN   A OD1 1 
ATOM   3276 N  ND2 . ASN   A 1 409 ? -28.311 -16.465 44.627 1    43.559  ? 445 ASN   A ND2 1 
ATOM   3277 N  N   . PHE   A 1 410 ? -27.265 -11.949 41.757 1    21.65   ? 446 PHE   A N   1 
ATOM   3278 C  CA  . PHE   A 1 410 ? -27.257 -11.249 40.489 1    30.478  ? 446 PHE   A CA  1 
ATOM   3279 C  C   . PHE   A 1 410 ? -26.106 -10.231 40.46  1    30.489  ? 446 PHE   A C   1 
ATOM   3280 O  O   . PHE   A 1 410 ? -25.301 -10.251 39.55  1    31.648  ? 446 PHE   A O   1 
ATOM   3281 C  CB  . PHE   A 1 410 ? -28.579 -10.505 40.262 1    25.447  ? 446 PHE   A CB  1 
ATOM   3282 C  CG  . PHE   A 1 410 ? -28.438 -9.653  39.031 1    20.279  ? 446 PHE   A CG  1 
ATOM   3283 C  CD1 . PHE   A 1 410 ? -28.078 -10.224 37.813 1    22.969  ? 446 PHE   A CD1 1 
ATOM   3284 C  CD2 . PHE   A 1 410 ? -28.577 -8.289  39.101 1    21.535  ? 446 PHE   A CD2 1 
ATOM   3285 C  CE1 . PHE   A 1 410 ? -27.935 -9.467  36.642 1    23.024  ? 446 PHE   A CE1 1 
ATOM   3286 C  CE2 . PHE   A 1 410 ? -28.367 -7.502  37.95  1    22.643  ? 446 PHE   A CE2 1 
ATOM   3287 C  CZ  . PHE   A 1 410 ? -28.097 -8.098  36.717 1    26.709  ? 446 PHE   A CZ  1 
ATOM   3288 N  N   . LEU   A 1 411 ? -26.005 -9.375  41.473 1    24.597  ? 447 LEU   A N   1 
ATOM   3289 C  CA  . LEU   A 1 411 ? -24.929 -8.41   41.47  1    27.093  ? 447 LEU   A CA  1 
ATOM   3290 C  C   . LEU   A 1 411 ? -23.577 -9.123  41.471 1    26.372  ? 447 LEU   A C   1 
ATOM   3291 O  O   . LEU   A 1 411 ? -22.587 -8.552  41.034 1    27.474  ? 447 LEU   A O   1 
ATOM   3292 C  CB  . LEU   A 1 411 ? -24.961 -7.357  42.589 1    25.19   ? 447 LEU   A CB  1 
ATOM   3293 C  CG  . LEU   A 1 411 ? -26.056 -6.279  42.561 1    28.877  ? 447 LEU   A CG  1 
ATOM   3294 C  CD1 . LEU   A 1 411 ? -26.234 -5.617  43.931 1    28.043  ? 447 LEU   A CD1 1 
ATOM   3295 C  CD2 . LEU   A 1 411 ? -25.803 -5.221  41.524 1    29.833  ? 447 LEU   A CD2 1 
ATOM   3296 N  N   . MET   A 1 412 ? -23.505 -10.334 42.034 1    28.975  ? 448 MET   A N   1 
ATOM   3297 C  CA  . MET   A 1 412 ? -22.236 -11.044 42.119 1    25.282  ? 448 MET   A CA  1 
ATOM   3298 C  C   . MET   A 1 412 ? -21.846 -11.618 40.743 1    25.879  ? 448 MET   A C   1 
ATOM   3299 O  O   . MET   A 1 412 ? -20.677 -11.569 40.35  1    28.358  ? 448 MET   A O   1 
ATOM   3300 C  CB  . MET   A 1 412 ? -22.282 -12.074 43.24  1    22.111  ? 448 MET   A CB  1 
ATOM   3301 C  CG  . MET   A 1 412 ? -21.184 -13.102 43.112 1    26.992  ? 448 MET   A CG  1 
ATOM   3302 S  SD  . MET   A 1 412 ? -19.614 -12.374 43.632 1    30.605  ? 448 MET   A SD  1 
ATOM   3303 C  CE  . MET   A 1 412 ? -19.715 -11.839 45.333 1    22.738  ? 448 MET   A CE  1 
ATOM   3304 N  N   . LYS   A 1 413 ? -22.826 -12.152 40.01  1    24.412  ? 449 LYS   A N   1 
ATOM   3305 C  CA  . LYS   A 1 413 ? -22.669 -12.554 38.616 1    29.683  ? 449 LYS   A CA  1 
ATOM   3306 C  C   . LYS   A 1 413 ? -22.133 -11.38  37.788 1    30.283  ? 449 LYS   A C   1 
ATOM   3307 O  O   . LYS   A 1 413 ? -21.091 -11.494 37.119 1    30.662  ? 449 LYS   A O   1 
ATOM   3308 C  CB  . LYS   A 1 413 ? -23.969 -13.152 38.082 1    29.035  ? 449 LYS   A CB  1 
ATOM   3309 C  CG  . LYS   A 1 413 ? -23.837 -14.171 36.95  1    43.377  ? 449 LYS   A CG  1 
ATOM   3310 C  CD  . LYS   A 1 413 ? -25.203 -14.872 36.838 1    65.086  ? 449 LYS   A CD  1 
ATOM   3311 C  CE  . LYS   A 1 413 ? -25.492 -15.815 35.662 1    78.61   ? 449 LYS   A CE  1 
ATOM   3312 N  NZ  . LYS   A 1 413 ? -26.856 -15.829 35.086 1    52.128  ? 449 LYS   A NZ  1 
ATOM   3313 N  N   . MET   A 1 414 ? -22.756 -10.204 37.944 1    23.062  ? 450 MET   A N   1 
ATOM   3314 C  CA  . MET   A 1 414 ? -22.316 -9.037  37.192 1    21.362  ? 450 MET   A CA  1 
ATOM   3315 C  C   . MET   A 1 414 ? -20.888 -8.643  37.573 1    25.041  ? 450 MET   A C   1 
ATOM   3316 O  O   . MET   A 1 414 ? -20.09  -8.333  36.681 1    23.78   ? 450 MET   A O   1 
ATOM   3317 C  CB  . MET   A 1 414 ? -23.287 -7.882  37.4   1    18.873  ? 450 MET   A CB  1 
ATOM   3318 C  CG  . MET   A 1 414 ? -24.668 -8.139  36.798 1    23.635  ? 450 MET   A CG  1 
ATOM   3319 S  SD  . MET   A 1 414 ? -24.506 -8.503  35.026 1    36.127  ? 450 MET   A SD  1 
ATOM   3320 C  CE  . MET   A 1 414 ? -23.701 -7.026  34.388 1    23.436  ? 450 MET   A CE  1 
ATOM   3321 N  N   . ALA   A 1 415 ? -20.591 -8.676  38.891 1    22.83   ? 451 ALA   A N   1 
ATOM   3322 C  CA  . ALA   A 1 415 ? -19.324 -8.202  39.414 1    27.445  ? 451 ALA   A CA  1 
ATOM   3323 C  C   . ALA   A 1 415 ? -18.178 -9.107  38.924 1    26.809  ? 451 ALA   A C   1 
ATOM   3324 O  O   . ALA   A 1 415 ? -17.086 -8.621  38.633 1    27.736  ? 451 ALA   A O   1 
ATOM   3325 C  CB  . ALA   A 1 415 ? -19.354 -8.011  40.924 1    20.368  ? 451 ALA   A CB  1 
ATOM   3326 N  N   . LEU   A 1 416 ? -18.453 -10.395 38.758 1    24.48   ? 452 LEU   A N   1 
ATOM   3327 C  CA  . LEU   A 1 416 ? -17.442 -11.294 38.244 1    27.74   ? 452 LEU   A CA  1 
ATOM   3328 C  C   . LEU   A 1 416 ? -17.085 -10.916 36.787 1    29.984  ? 452 LEU   A C   1 
ATOM   3329 O  O   . LEU   A 1 416 ? -15.946 -11.122 36.354 1    29.309  ? 452 LEU   A O   1 
ATOM   3330 C  CB  . LEU   A 1 416 ? -17.893 -12.743 38.446 1    23.101  ? 452 LEU   A CB  1 
ATOM   3331 C  CG  . LEU   A 1 416 ? -18.02  -13.238 39.894 1    21.953  ? 452 LEU   A CG  1 
ATOM   3332 C  CD1 . LEU   A 1 416 ? -18.698 -14.589 39.842 1    20.201  ? 452 LEU   A CD1 1 
ATOM   3333 C  CD2 . LEU   A 1 416 ? -16.67  -13.506 40.593 1    21.715  ? 452 LEU   A CD2 1 
ATOM   3334 N  N   . ASP   A 1 417 ? -17.993 -10.247 36.053 1    29.853  ? 453 ASP   A N   1 
ATOM   3335 C  CA  . ASP   A 1 417 ? -17.639 -9.736  34.725 1    34.138  ? 453 ASP   A CA  1 
ATOM   3336 C  C   . ASP   A 1 417 ? -17.041 -8.328  34.754 1    27.714  ? 453 ASP   A C   1 
ATOM   3337 O  O   . ASP   A 1 417 ? -15.948 -8.125  34.299 1    38.098  ? 453 ASP   A O   1 
ATOM   3338 C  CB  . ASP   A 1 417 ? -18.734 -9.886  33.692 1    45.197  ? 453 ASP   A CB  1 
ATOM   3339 C  CG  . ASP   A 1 417 ? -18.883 -11.317 33.22  1    65.857  ? 453 ASP   A CG  1 
ATOM   3340 O  OD1 . ASP   A 1 417 ? -17.853 -12.04  33.213 1    76.65   ? 453 ASP   A OD1 1 
ATOM   3341 O  OD2 . ASP   A 1 417 ? -20.017 -11.686 32.872 1    92.495  ? 453 ASP   A OD2 1 
ATOM   3342 N  N   . LYS   A 1 418 ? -17.68  -7.375  35.412 1    23.36   ? 454 LYS   A N   1 
ATOM   3343 C  CA  . LYS   A 1 418 ? -17.348 -5.983  35.217 1    20.972  ? 454 LYS   A CA  1 
ATOM   3344 C  C   . LYS   A 1 418 ? -16.216 -5.553  36.13  1    22.878  ? 454 LYS   A C   1 
ATOM   3345 O  O   . LYS   A 1 418 ? -15.351 -4.836  35.677 1    30.662  ? 454 LYS   A O   1 
ATOM   3346 C  CB  . LYS   A 1 418 ? -18.631 -5.155  35.388 1    19.881  ? 454 LYS   A CB  1 
ATOM   3347 C  CG  . LYS   A 1 418 ? -19.815 -5.597  34.523 1    22.641  ? 454 LYS   A CG  1 
ATOM   3348 C  CD  . LYS   A 1 418 ? -19.425 -5.433  33.028 1    23.774  ? 454 LYS   A CD  1 
ATOM   3349 C  CE  . LYS   A 1 418 ? -20.622 -5.576  32.075 1    21.857  ? 454 LYS   A CE  1 
ATOM   3350 N  NZ  . LYS   A 1 418 ? -20.296 -5.308  30.675 1    20.785  ? 454 LYS   A NZ  1 
ATOM   3351 N  N   . ILE   A 1 419 ? -16.28  -5.887  37.424 1    22.43   ? 455 ILE   A N   1 
ATOM   3352 C  CA  . ILE   A 1 419 ? -15.348 -5.342  38.386 1    20.189  ? 455 ILE   A CA  1 
ATOM   3353 C  C   . ILE   A 1 419 ? -14.028 -6.053  38.123 1    20.401  ? 455 ILE   A C   1 
ATOM   3354 O  O   . ILE   A 1 419 ? -12.965 -5.45   38.16  1    25.556  ? 455 ILE   A O   1 
ATOM   3355 C  CB  . ILE   A 1 419 ? -15.828 -5.614  39.829 1    19.344  ? 455 ILE   A CB  1 
ATOM   3356 C  CG1 . ILE   A 1 419 ? -17.132 -4.932  40.195 1    23.478  ? 455 ILE   A CG1 1 
ATOM   3357 C  CG2 . ILE   A 1 419 ? -14.74  -5.327  40.843 1    19.917  ? 455 ILE   A CG2 1 
ATOM   3358 C  CD1 . ILE   A 1 419 ? -17.142 -3.42   40.038 1    25.747  ? 455 ILE   A CD1 1 
ATOM   3359 N  N   . ALA   A 1 420 ? -14.087 -7.374  37.911 1    19.38   ? 456 ALA   A N   1 
ATOM   3360 C  CA  . ALA   A 1 420 ? -12.843 -8.12   37.794 1    19.399  ? 456 ALA   A CA  1 
ATOM   3361 C  C   . ALA   A 1 420 ? -11.988 -7.65   36.617 1    23.245  ? 456 ALA   A C   1 
ATOM   3362 O  O   . ALA   A 1 420 ? -10.778 -7.683  36.754 1    25.055  ? 456 ALA   A O   1 
ATOM   3363 C  CB  . ALA   A 1 420 ? -13.133 -9.573  37.697 1    18.408  ? 456 ALA   A CB  1 
ATOM   3364 N  N   . PHE   A 1 421 ? -12.627 -7.182  35.519 1    20.329  ? 457 PHE   A N   1 
ATOM   3365 C  CA  . PHE   A 1 421 ? -11.964 -6.791  34.306 1    21.808  ? 457 PHE   A CA  1 
ATOM   3366 C  C   . PHE   A 1 421 ? -11.297 -5.418  34.477 1    25.812  ? 457 PHE   A C   1 
ATOM   3367 O  O   . PHE   A 1 421 ? -10.372 -5.047  33.729 1    24.282  ? 457 PHE   A O   1 
ATOM   3368 C  CB  . PHE   A 1 421 ? -13.132 -6.849  33.322 1    23.509  ? 457 PHE   A CB  1 
ATOM   3369 C  CG  . PHE   A 1 421 ? -12.714 -6.4    31.941 1    24.369  ? 457 PHE   A CG  1 
ATOM   3370 C  CD1 . PHE   A 1 421 ? -11.917 -7.219  31.131 1    28.199  ? 457 PHE   A CD1 1 
ATOM   3371 C  CD2 . PHE   A 1 421 ? -13.021 -5.117  31.497 1    25.922  ? 457 PHE   A CD2 1 
ATOM   3372 C  CE1 . PHE   A 1 421 ? -11.475 -6.814  29.869 1    24.992  ? 457 PHE   A CE1 1 
ATOM   3373 C  CE2 . PHE   A 1 421 ? -12.572 -4.704  30.242 1    28.899  ? 457 PHE   A CE2 1 
ATOM   3374 C  CZ  . PHE   A 1 421 ? -11.812 -5.561  29.428 1    29.761  ? 457 PHE   A CZ  1 
ATOM   3375 N  N   . ILE   A 1 422 ? -11.796 -4.624  35.421 1    22.775  ? 458 ILE   A N   1 
ATOM   3376 C  CA  . ILE   A 1 422 ? -11.27  -3.279  35.596 1    22.143  ? 458 ILE   A CA  1 
ATOM   3377 C  C   . ILE   A 1 422 ? -9.734  -3.318  35.669 1    28.26   ? 458 ILE   A C   1 
ATOM   3378 O  O   . ILE   A 1 422 ? -9.116  -2.782  34.755 1    31.538  ? 458 ILE   A O   1 
ATOM   3379 C  CB  . ILE   A 1 422 ? -11.942 -2.598  36.788 1    26.52   ? 458 ILE   A CB  1 
ATOM   3380 C  CG1 . ILE   A 1 422 ? -13.37  -2.133  36.438 1    28.791  ? 458 ILE   A CG1 1 
ATOM   3381 C  CG2 . ILE   A 1 422 ? -11.108 -1.445  37.36  1    23.9    ? 458 ILE   A CG2 1 
ATOM   3382 C  CD1 . ILE   A 1 422 ? -13.359 -1.013  35.4   1    34.04   ? 458 ILE   A CD1 1 
ATOM   3383 N  N   . PRO   A 1 423 ? -9.045  -3.998  36.637 1    23.958  ? 459 PRO   A N   1 
ATOM   3384 C  CA  . PRO   A 1 423 ? -7.584  -4.054  36.609 1    25.265  ? 459 PRO   A CA  1 
ATOM   3385 C  C   . PRO   A 1 423 ? -6.99   -4.713  35.364 1    20.971  ? 459 PRO   A C   1 
ATOM   3386 O  O   . PRO   A 1 423 ? -5.847  -4.441  35.001 1    20.924  ? 459 PRO   A O   1 
ATOM   3387 C  CB  . PRO   A 1 423 ? -7.132  -4.734  37.956 1    21.756  ? 459 PRO   A CB  1 
ATOM   3388 C  CG  . PRO   A 1 423 ? -8.379  -5.578  38.277 1    25.921  ? 459 PRO   A CG  1 
ATOM   3389 C  CD  . PRO   A 1 423 ? -9.584  -4.755  37.784 1    24.695  ? 459 PRO   A CD  1 
ATOM   3390 N  N   . PHE   A 1 424 ? -7.716  -5.657  34.762 1    20.56   ? 460 PHE   A N   1 
ATOM   3391 C  CA  . PHE   A 1 424 ? -7.098  -6.288  33.614 1    22.016  ? 460 PHE   A CA  1 
ATOM   3392 C  C   . PHE   A 1 424 ? -6.982  -5.234  32.517 1    23.447  ? 460 PHE   A C   1 
ATOM   3393 O  O   . PHE   A 1 424 ? -5.891  -4.986  31.986 1    27.253  ? 460 PHE   A O   1 
ATOM   3394 C  CB  . PHE   A 1 424 ? -7.693  -7.649  33.241 1    23.579  ? 460 PHE   A CB  1 
ATOM   3395 C  CG  . PHE   A 1 424 ? -7.085  -8.255  31.989 1    20.72   ? 460 PHE   A CG  1 
ATOM   3396 C  CD1 . PHE   A 1 424 ? -5.96   -9.077  32.069 1    20.952  ? 460 PHE   A CD1 1 
ATOM   3397 C  CD2 . PHE   A 1 424 ? -7.616  -7.94   30.734 1    20.726  ? 460 PHE   A CD2 1 
ATOM   3398 C  CE1 . PHE   A 1 424 ? -5.398  -9.584  30.898 1    20.088  ? 460 PHE   A CE1 1 
ATOM   3399 C  CE2 . PHE   A 1 424 ? -7.052  -8.439  29.572 1    17.76   ? 460 PHE   A CE2 1 
ATOM   3400 C  CZ  . PHE   A 1 424 ? -5.962  -9.297  29.669 1    17.706  ? 460 PHE   A CZ  1 
ATOM   3401 N  N   . SER   A 1 425 ? -8.102  -4.563  32.263 1    21.939  ? 461 SER   A N   1 
ATOM   3402 C  CA  . SER   A 1 425 ? -8.23   -3.689  31.112 1    24.043  ? 461 SER   A CA  1 
ATOM   3403 C  C   . SER   A 1 425 ? -7.309  -2.484  31.317 1    22.571  ? 461 SER   A C   1 
ATOM   3404 O  O   . SER   A 1 425 ? -6.805  -1.895  30.354 1    18.355  ? 461 SER   A O   1 
ATOM   3405 C  CB  . SER   A 1 425 ? -9.628  -3.27   30.912 1    21.921  ? 461 SER   A CB  1 
ATOM   3406 O  OG  . SER   A 1 425 ? -10.065 -2.673  32.132 1    30.1    ? 461 SER   A OG  1 
ATOM   3407 N  N   . TYR   A 1 426 ? -7.06   -2.17   32.587 1    19.695  ? 462 TYR   A N   1 
ATOM   3408 C  CA  . TYR   A 1 426 ? -6.162  -1.086  32.902 1    23.058  ? 462 TYR   A CA  1 
ATOM   3409 C  C   . TYR   A 1 426 ? -4.689  -1.459  32.626 1    27.144  ? 462 TYR   A C   1 
ATOM   3410 O  O   . TYR   A 1 426 ? -3.914  -0.603  32.188 1    28.085  ? 462 TYR   A O   1 
ATOM   3411 C  CB  . TYR   A 1 426 ? -6.334  -0.792  34.384 1    25.928  ? 462 TYR   A CB  1 
ATOM   3412 C  CG  . TYR   A 1 426 ? -5.558  0.451   34.813 1    31.348  ? 462 TYR   A CG  1 
ATOM   3413 C  CD1 . TYR   A 1 426 ? -5.948  1.703   34.356 1    30.97   ? 462 TYR   A CD1 1 
ATOM   3414 C  CD2 . TYR   A 1 426 ? -4.452  0.365   35.668 1    30.225  ? 462 TYR   A CD2 1 
ATOM   3415 C  CE1 . TYR   A 1 426 ? -5.252  2.847   34.719 1    28.206  ? 462 TYR   A CE1 1 
ATOM   3416 C  CE2 . TYR   A 1 426 ? -3.767  1.498   36.061 1    26.628  ? 462 TYR   A CE2 1 
ATOM   3417 C  CZ  . TYR   A 1 426 ? -4.175  2.74    35.578 1    27.307  ? 462 TYR   A CZ  1 
ATOM   3418 O  OH  . TYR   A 1 426 ? -3.56   3.903   35.912 1    23.282  ? 462 TYR   A OH  1 
ATOM   3419 N  N   . LEU   A 1 427 ? -4.273  -2.72   32.889 1    26.682  ? 463 LEU   A N   1 
ATOM   3420 C  CA  . LEU   A 1 427 ? -2.845  -3.032  32.929 1    24.513  ? 463 LEU   A CA  1 
ATOM   3421 C  C   . LEU   A 1 427 ? -2.219  -3.258  31.552 1    26.502  ? 463 LEU   A C   1 
ATOM   3422 O  O   . LEU   A 1 427 ? -1.038  -2.921  31.374 1    23.2    ? 463 LEU   A O   1 
ATOM   3423 C  CB  . LEU   A 1 427 ? -2.438  -4.093  33.929 1    21.374  ? 463 LEU   A CB  1 
ATOM   3424 C  CG  . LEU   A 1 427 ? -2.799  -5.53   33.537 1    21.211  ? 463 LEU   A CG  1 
ATOM   3425 C  CD1 . LEU   A 1 427 ? -1.707  -6.149  32.692 1    18.721  ? 463 LEU   A CD1 1 
ATOM   3426 C  CD2 . LEU   A 1 427 ? -2.935  -6.2    34.875 1    19.8    ? 463 LEU   A CD2 1 
ATOM   3427 N  N   . VAL   A 1 428 ? -3.013  -3.75   30.575 1    28.041  ? 464 VAL   A N   1 
ATOM   3428 C  CA  . VAL   A 1 428 ? -2.498  -4.074  29.247 1    23.048  ? 464 VAL   A CA  1 
ATOM   3429 C  C   . VAL   A 1 428 ? -1.67   -2.938  28.617 1    20.61   ? 464 VAL   A C   1 
ATOM   3430 O  O   . VAL   A 1 428 ? -0.501  -3.107  28.271 1    20.053  ? 464 VAL   A O   1 
ATOM   3431 C  CB  . VAL   A 1 428 ? -3.574  -4.622  28.297 1    22.292  ? 464 VAL   A CB  1 
ATOM   3432 C  CG1 . VAL   A 1 428 ? -3.052  -4.801  26.856 1    20.329  ? 464 VAL   A CG1 1 
ATOM   3433 C  CG2 . VAL   A 1 428 ? -4.183  -5.88   28.88  1    16.581  ? 464 VAL   A CG2 1 
ATOM   3434 N  N   . ASP   A 1 429 ? -2.261  -1.761  28.454 1    23.894  ? 465 ASP   A N   1 
ATOM   3435 C  CA  . ASP   A 1 429 ? -1.594  -0.653  27.774 1    20.577  ? 465 ASP   A CA  1 
ATOM   3436 C  C   . ASP   A 1 429 ? -0.594  0.006   28.724 1    25.948  ? 465 ASP   A C   1 
ATOM   3437 O  O   . ASP   A 1 429 ? 0.323   0.703   28.264 1    25.354  ? 465 ASP   A O   1 
ATOM   3438 C  CB  . ASP   A 1 429 ? -2.567  0.288   27.082 1    23.653  ? 465 ASP   A CB  1 
ATOM   3439 C  CG  . ASP   A 1 429 ? -3.133  -0.248  25.766 1    28.102  ? 465 ASP   A CG  1 
ATOM   3440 O  OD1 . ASP   A 1 429 ? -2.576  -1.23   25.275 1    28.076  ? 465 ASP   A OD1 1 
ATOM   3441 O  OD2 . ASP   A 1 429 ? -4.081  0.359   25.2   1    26.217  ? 465 ASP   A OD2 1 
ATOM   3442 N  N   . GLN   A 1 430 ? -0.729  -0.257  30.042 1    22.296  ? 466 GLN   A N   1 
ATOM   3443 C  CA  . GLN   A 1 430 ? 0.304   0.248   30.928 1    20.531  ? 466 GLN   A CA  1 
ATOM   3444 C  C   . GLN   A 1 430 ? 1.593   -0.464  30.551 1    21.426  ? 466 GLN   A C   1 
ATOM   3445 O  O   . GLN   A 1 430 ? 2.681   0.129   30.587 1    28.13   ? 466 GLN   A O   1 
ATOM   3446 C  CB  . GLN   A 1 430 ? 0.194   0.064   32.456 1    20.721  ? 466 GLN   A CB  1 
ATOM   3447 C  CG  . GLN   A 1 430 ? -0.964  0.722   33.193 1    23.5    ? 466 GLN   A CG  1 
ATOM   3448 C  CD  . GLN   A 1 430 ? -1.145  2.217   32.978 1    30.064  ? 466 GLN   A CD  1 
ATOM   3449 O  OE1 . GLN   A 1 430 ? -0.196  3.005   32.957 1    28.918  ? 466 GLN   A OE1 1 
ATOM   3450 N  NE2 . GLN   A 1 430 ? -2.4    2.647   32.842 1    33.39   ? 466 GLN   A NE2 1 
ATOM   3451 N  N   . TRP   A 1 431 ? 1.473   -1.767  30.316 1    19.711  ? 467 TRP   A N   1 
ATOM   3452 C  CA  . TRP   A 1 431 ? 2.613   -2.538  29.871 1    20.252  ? 467 TRP   A CA  1 
ATOM   3453 C  C   . TRP   A 1 431 ? 3.025   -2.007  28.497 1    21.526  ? 467 TRP   A C   1 
ATOM   3454 O  O   . TRP   A 1 431 ? 4.212   -1.66   28.348 1    17.826  ? 467 TRP   A O   1 
ATOM   3455 C  CB  . TRP   A 1 431 ? 2.37    -4.067  29.928 1    20.935  ? 467 TRP   A CB  1 
ATOM   3456 C  CG  . TRP   A 1 431 ? 3.527   -4.917  29.452 1    22.395  ? 467 TRP   A CG  1 
ATOM   3457 C  CD1 . TRP   A 1 431 ? 4.575   -5.416  30.177 1    25.135  ? 467 TRP   A CD1 1 
ATOM   3458 C  CD2 . TRP   A 1 431 ? 3.734   -5.395  28.105 1    20.58   ? 467 TRP   A CD2 1 
ATOM   3459 N  NE1 . TRP   A 1 431 ? 5.436   -6.15   29.384 1    24.762  ? 467 TRP   A NE1 1 
ATOM   3460 C  CE2 . TRP   A 1 431 ? 4.932   -6.159  28.105 1    23.58   ? 467 TRP   A CE2 1 
ATOM   3461 C  CE3 . TRP   A 1 431 ? 3.016   -5.248  26.911 1    21.787  ? 467 TRP   A CE3 1 
ATOM   3462 C  CZ2 . TRP   A 1 431 ? 5.428   -6.772  26.952 1    21.116  ? 467 TRP   A CZ2 1 
ATOM   3463 C  CZ3 . TRP   A 1 431 ? 3.534   -5.8    25.753 1    22.212  ? 467 TRP   A CZ3 1 
ATOM   3464 C  CH2 . TRP   A 1 431 ? 4.717   -6.556  25.787 1    23.166  ? 467 TRP   A CH2 1 
ATOM   3465 N  N   . ARG   A 1 432 ? 2.059   -1.898  27.532 1    24.177  ? 468 ARG   A N   1 
ATOM   3466 C  CA  . ARG   A 1 432 ? 2.489   -1.603  26.159 1    25.225  ? 468 ARG   A CA  1 
ATOM   3467 C  C   . ARG   A 1 432 ? 3.064   -0.185  26.094 1    28.085  ? 468 ARG   A C   1 
ATOM   3468 O  O   . ARG   A 1 432 ? 3.982   0.036   25.314 1    23.035  ? 468 ARG   A O   1 
ATOM   3469 C  CB  . ARG   A 1 432 ? 1.492   -1.667  25.003 1    23.986  ? 468 ARG   A CB  1 
ATOM   3470 C  CG  . ARG   A 1 432 ? 0.985   -3.064  24.691 1    31.115  ? 468 ARG   A CG  1 
ATOM   3471 C  CD  . ARG   A 1 432 ? 0.336   -3.267  23.292 1    29.592  ? 468 ARG   A CD  1 
ATOM   3472 N  NE  . ARG   A 1 432 ? -1.073  -2.902  23.445 1    23.87   ? 468 ARG   A NE  1 
ATOM   3473 C  CZ  . ARG   A 1 432 ? -2.062  -3.514  22.823 1    23.642  ? 468 ARG   A CZ  1 
ATOM   3474 N  NH1 . ARG   A 1 432 ? -1.8    -4.204  21.719 1    21.805  ? 468 ARG   A NH1 1 
ATOM   3475 N  NH2 . ARG   A 1 432 ? -3.325  -3.336  23.243 1    21.329  ? 468 ARG   A NH2 1 
ATOM   3476 N  N   . TRP   A 1 433 ? 2.505   0.758   26.888 1    24.368  ? 469 TRP   A N   1 
ATOM   3477 C  CA  . TRP   A 1 433 ? 2.999   2.136   26.842 1    29.892  ? 469 TRP   A CA  1 
ATOM   3478 C  C   . TRP   A 1 433 ? 4.48    2.202   27.179 1    32.595  ? 469 TRP   A C   1 
ATOM   3479 O  O   . TRP   A 1 433 ? 5.207   3.027   26.613 1    36.143  ? 469 TRP   A O   1 
ATOM   3480 C  CB  . TRP   A 1 433 ? 2.22    3.15    27.715 1    23.351  ? 469 TRP   A CB  1 
ATOM   3481 C  CG  . TRP   A 1 433 ? 0.811   3.444   27.256 1    21.863  ? 469 TRP   A CG  1 
ATOM   3482 C  CD1 . TRP   A 1 433 ? 0.236   3.22    26.028 1    20.438  ? 469 TRP   A CD1 1 
ATOM   3483 C  CD2 . TRP   A 1 433 ? -0.249  3.949   28.099 1    22.931  ? 469 TRP   A CD2 1 
ATOM   3484 N  NE1 . TRP   A 1 433 ? -1.078  3.585   26.016 1    19.844  ? 469 TRP   A NE1 1 
ATOM   3485 C  CE2 . TRP   A 1 433 ? -1.409  4.023   27.288 1    23.303  ? 469 TRP   A CE2 1 
ATOM   3486 C  CE3 . TRP   A 1 433 ? -0.312  4.311   29.453 1    22.409  ? 469 TRP   A CE3 1 
ATOM   3487 C  CZ2 . TRP   A 1 433 ? -2.631  4.459   27.802 1    22.33   ? 469 TRP   A CZ2 1 
ATOM   3488 C  CZ3 . TRP   A 1 433 ? -1.526  4.737   29.95  1    23.139  ? 469 TRP   A CZ3 1 
ATOM   3489 C  CH2 . TRP   A 1 433 ? -2.663  4.806   29.134 1    23.089  ? 469 TRP   A CH2 1 
ATOM   3490 N  N   . ARG   A 1 434 ? 4.885   1.334   28.107 1    27.991  ? 470 ARG   A N   1 
ATOM   3491 C  CA  . ARG   A 1 434 ? 6.235   1.291   28.643 1    25.249  ? 470 ARG   A CA  1 
ATOM   3492 C  C   . ARG   A 1 434 ? 7.166   0.561   27.693 1    23.163  ? 470 ARG   A C   1 
ATOM   3493 O  O   . ARG   A 1 434 ? 8.379   0.792   27.713 1    20.683  ? 470 ARG   A O   1 
ATOM   3494 C  CB  . ARG   A 1 434 ? 6.277   0.731   30.077 1    22.273  ? 470 ARG   A CB  1 
ATOM   3495 C  CG  . ARG   A 1 434 ? 5.84    1.89    30.994 1    22.332  ? 470 ARG   A CG  1 
ATOM   3496 C  CD  . ARG   A 1 434 ? 5.615   1.485   32.478 1    30.595  ? 470 ARG   A CD  1 
ATOM   3497 N  NE  . ARG   A 1 434 ? 6.789   0.785   33.042 1    39.969  ? 470 ARG   A NE  1 
ATOM   3498 C  CZ  . ARG   A 1 434 ? 6.793   -0.411  33.67  1    41.529  ? 470 ARG   A CZ  1 
ATOM   3499 N  NH1 . ARG   A 1 434 ? 5.677   -1.064  33.979 1    42.198  ? 470 ARG   A NH1 1 
ATOM   3500 N  NH2 . ARG   A 1 434 ? 7.936   -0.952  34.008 1    39.028  ? 470 ARG   A NH2 1 
ATOM   3501 N  N   . VAL   A 1 435 ? 6.589   -0.361  26.923 1    22.448  ? 471 VAL   A N   1 
ATOM   3502 C  CA  . VAL   A 1 435 ? 7.357   -1.062  25.908 1    23.929  ? 471 VAL   A CA  1 
ATOM   3503 C  C   . VAL   A 1 435 ? 7.659   -0.065  24.788 1    22.928  ? 471 VAL   A C   1 
ATOM   3504 O  O   . VAL   A 1 435 ? 8.786   0.034   24.324 1    23.538  ? 471 VAL   A O   1 
ATOM   3505 C  CB  . VAL   A 1 435 ? 6.653   -2.337  25.365 1    21.049  ? 471 VAL   A CB  1 
ATOM   3506 C  CG1 . VAL   A 1 435 ? 7.433   -3.029  24.223 1    16.43   ? 471 VAL   A CG1 1 
ATOM   3507 C  CG2 . VAL   A 1 435 ? 6.358   -3.299  26.488 1    20.51   ? 471 VAL   A CG2 1 
ATOM   3508 N  N   . PHE   A 1 436 ? 6.628   0.68    24.382 1    21.195  ? 472 PHE   A N   1 
ATOM   3509 C  CA  . PHE   A 1 436 ? 6.732   1.665   23.31  1    24.174  ? 472 PHE   A CA  1 
ATOM   3510 C  C   . PHE   A 1 436 ? 7.731   2.794   23.623 1    25.448  ? 472 PHE   A C   1 
ATOM   3511 O  O   . PHE   A 1 436 ? 8.481   3.198   22.722 1    20.694  ? 472 PHE   A O   1 
ATOM   3512 C  CB  . PHE   A 1 436 ? 5.31    2.103   22.927 1    19.161  ? 472 PHE   A CB  1 
ATOM   3513 C  CG  . PHE   A 1 436 ? 4.448   1.084   22.186 1    19.229  ? 472 PHE   A CG  1 
ATOM   3514 C  CD1 . PHE   A 1 436 ? 5.021   0.07    21.396 1    18.691  ? 472 PHE   A CD1 1 
ATOM   3515 C  CD2 . PHE   A 1 436 ? 3.055   1.189   22.205 1    20.152  ? 472 PHE   A CD2 1 
ATOM   3516 C  CE1 . PHE   A 1 436 ? 4.235   -0.824  20.685 1    17.226  ? 472 PHE   A CE1 1 
ATOM   3517 C  CE2 . PHE   A 1 436 ? 2.251   0.357   21.436 1    17.966  ? 472 PHE   A CE2 1 
ATOM   3518 C  CZ  . PHE   A 1 436 ? 2.854   -0.649  20.673 1    19.817  ? 472 PHE   A CZ  1 
ATOM   3519 N  N   . ASP   A 1 437 ? 7.698   3.342   24.87  1    24.026  ? 473 ASP   A N   1 
ATOM   3520 C  CA  . ASP   A 1 437 ? 8.58    4.442   25.287 1    22.112  ? 473 ASP   A CA  1 
ATOM   3521 C  C   . ASP   A 1 437 ? 9.954   3.923   25.722 1    24.184  ? 473 ASP   A C   1 
ATOM   3522 O  O   . ASP   A 1 437 ? 10.821  4.708   26.014 1    30.753  ? 473 ASP   A O   1 
ATOM   3523 C  CB  . ASP   A 1 437 ? 7.951   5.356   26.335 1    22.361  ? 473 ASP   A CB  1 
ATOM   3524 C  CG  . ASP   A 1 437 ? 7.962   4.866   27.792 1    27.534  ? 473 ASP   A CG  1 
ATOM   3525 O  OD1 . ASP   A 1 437 ? 8.734   3.934   28.14  1    27.77   ? 473 ASP   A OD1 1 
ATOM   3526 O  OD2 . ASP   A 1 437 ? 7.23    5.44    28.605 1    32.893  ? 473 ASP   A OD2 1 
ATOM   3527 N  N   . GLY   A 1 438 ? 10.168  2.602   25.781 1    29.334  ? 474 GLY   A N   1 
ATOM   3528 C  CA  . GLY   A 1 438 ? 11.504  2.05    25.943 1    24.981  ? 474 GLY   A CA  1 
ATOM   3529 C  C   . GLY   A 1 438 ? 11.949  1.926   27.414 1    22.862  ? 474 GLY   A C   1 
ATOM   3530 O  O   . GLY   A 1 438 ? 13.124  1.73    27.647 1    29.257  ? 474 GLY   A O   1 
ATOM   3531 N  N   . SER   A 1 439 ? 11.059  2.027   28.401 1    23.328  ? 475 SER   A N   1 
ATOM   3532 C  CA  . SER   A 1 439 ? 11.351  1.716   29.809 1    27.524  ? 475 SER   A CA  1 
ATOM   3533 C  C   . SER   A 1 439 ? 11.376  0.202   30.073 1    29.328  ? 475 SER   A C   1 
ATOM   3534 O  O   . SER   A 1 439 ? 11.965  -0.215  31.05  1    31.197  ? 475 SER   A O   1 
ATOM   3535 C  CB  . SER   A 1 439 ? 10.317  2.302   30.738 1    26.198  ? 475 SER   A CB  1 
ATOM   3536 O  OG  . SER   A 1 439 ? 9.762   3.476   30.181 1    40.497  ? 475 SER   A OG  1 
ATOM   3537 N  N   . ILE   A 1 440 ? 10.629  -0.582  29.274 1    29.854  ? 476 ILE   A N   1 
ATOM   3538 C  CA  . ILE   A 1 440 ? 10.678  -2.039  29.174 1    26.821  ? 476 ILE   A CA  1 
ATOM   3539 C  C   . ILE   A 1 440 ? 11.271  -2.46   27.814 1    28.23   ? 476 ILE   A C   1 
ATOM   3540 O  O   . ILE   A 1 440 ? 10.883  -1.937  26.746 1    27.117  ? 476 ILE   A O   1 
ATOM   3541 C  CB  . ILE   A 1 440 ? 9.256   -2.591  29.261 1    25.054  ? 476 ILE   A CB  1 
ATOM   3542 C  CG1 . ILE   A 1 440 ? 8.449   -2.022  30.43  1    25.846  ? 476 ILE   A CG1 1 
ATOM   3543 C  CG2 . ILE   A 1 440 ? 9.268   -4.105  29.187 1    22.737  ? 476 ILE   A CG2 1 
ATOM   3544 C  CD1 . ILE   A 1 440 ? 7.088   -2.687  30.584 1    23.426  ? 476 ILE   A CD1 1 
ATOM   3545 N  N   . THR   A 1 441 ? 12.229  -3.407  27.883 1    26.512  ? 477 THR   A N   1 
ATOM   3546 C  CA  . THR   A 1 441 ? 12.971  -3.963  26.756 1    24.81   ? 477 THR   A CA  1 
ATOM   3547 C  C   . THR   A 1 441 ? 12.668  -5.457  26.679 1    29.073  ? 477 THR   A C   1 
ATOM   3548 O  O   . THR   A 1 441 ? 12.031  -6.063  27.591 1    28.92   ? 477 THR   A O   1 
ATOM   3549 C  CB  . THR   A 1 441 ? 14.484  -3.698  26.845 1    24.604  ? 477 THR   A CB  1 
ATOM   3550 O  OG1 . THR   A 1 441 ? 15.089  -4.732  27.605 1    26.42   ? 477 THR   A OG1 1 
ATOM   3551 C  CG2 . THR   A 1 441 ? 14.896  -2.406  27.524 1    25.374  ? 477 THR   A CG2 1 
ATOM   3552 N  N   . LYS   A 1 442 ? 13.151  -6.066  25.584 1    28.562  ? 478 LYS   A N   1 
ATOM   3553 C  CA  . LYS   A 1 442 ? 12.946  -7.502  25.419 1    30.831  ? 478 LYS   A CA  1 
ATOM   3554 C  C   . LYS   A 1 442 ? 13.627  -8.304  26.523 1    26.054  ? 478 LYS   A C   1 
ATOM   3555 O  O   . LYS   A 1 442 ? 13.303  -9.462  26.646 1    38.022  ? 478 LYS   A O   1 
ATOM   3556 C  CB  . LYS   A 1 442 ? 13.376  -8.062  24.058 1    36.662  ? 478 LYS   A CB  1 
ATOM   3557 C  CG  . LYS   A 1 442 ? 14.89   -8.16   23.869 1    36.599  ? 478 LYS   A CG  1 
ATOM   3558 C  CD  . LYS   A 1 442 ? 15.201  -8.867  22.55  1    47.365  ? 478 LYS   A CD  1 
ATOM   3559 C  CE  . LYS   A 1 442 ? 16.634  -9.258  22.239 1    45.469  ? 478 LYS   A CE  1 
ATOM   3560 N  NZ  . LYS   A 1 442 ? 16.804  -9.055  20.797 1    41.938  ? 478 LYS   A NZ  1 
ATOM   3561 N  N   . GLU   A 1 443 ? 14.567  -7.745  27.308 1    25.11   ? 479 GLU   A N   1 
ATOM   3562 C  CA  . GLU   A 1 443 ? 15.171  -8.517  28.381 1    28.009  ? 479 GLU   A CA  1 
ATOM   3563 C  C   . GLU   A 1 443 ? 14.171  -8.586  29.546 1    30.379  ? 479 GLU   A C   1 
ATOM   3564 O  O   . GLU   A 1 443 ? 14.318  -9.396  30.455 1    34.926  ? 479 GLU   A O   1 
ATOM   3565 C  CB  . GLU   A 1 443 ? 16.396  -7.886  29.048 1    28.887  ? 479 GLU   A CB  1 
ATOM   3566 C  CG  . GLU   A 1 443 ? 17.435  -7.229  28.142 1    38.534  ? 479 GLU   A CG  1 
ATOM   3567 C  CD  . GLU   A 1 443 ? 18.338  -6.249  28.928 1    52.665  ? 479 GLU   A CD  1 
ATOM   3568 O  OE1 . GLU   A 1 443 ? 17.997  -5.081  29.409 1    39.653  ? 479 GLU   A OE1 1 
ATOM   3569 O  OE2 . GLU   A 1 443 ? 19.485  -6.729  29.096 1    64.696  ? 479 GLU   A OE2 1 
ATOM   3570 N  N   . ASN   A 1 444 ? 13.134  -7.765  29.467 1    26.045  ? 480 ASN   A N   1 
ATOM   3571 C  CA  . ASN   A 1 444 ? 12.239  -7.445  30.552 1    33.383  ? 480 ASN   A CA  1 
ATOM   3572 C  C   . ASN   A 1 444 ? 10.759  -7.725  30.293 1    29.994  ? 480 ASN   A C   1 
ATOM   3573 O  O   . ASN   A 1 444 ? 9.981   -7.589  31.236 1    25.788  ? 480 ASN   A O   1 
ATOM   3574 C  CB  . ASN   A 1 444 ? 12.083  -5.933  30.534 1    37.756  ? 480 ASN   A CB  1 
ATOM   3575 C  CG  . ASN   A 1 444 ? 12.913  -5.432  31.654 1    43.565  ? 480 ASN   A CG  1 
ATOM   3576 O  OD1 . ASN   A 1 444 ? 13.589  -6.264  32.266 1    49.645  ? 480 ASN   A OD1 1 
ATOM   3577 N  ND2 . ASN   A 1 444 ? 12.852  -4.143  31.923 1    48.996  ? 480 ASN   A ND2 1 
ATOM   3578 N  N   . TYR   A 1 445 ? 10.366  -7.968  29.024 1    25.321  ? 481 TYR   A N   1 
ATOM   3579 C  CA  . TYR   A 1 445 ? 8.958   -8.066  28.649 1    25.947  ? 481 TYR   A CA  1 
ATOM   3580 C  C   . TYR   A 1 445 ? 8.107   -8.749  29.735 1    25.356  ? 481 TYR   A C   1 
ATOM   3581 O  O   . TYR   A 1 445 ? 7.192   -8.145  30.281 1    26.215  ? 481 TYR   A O   1 
ATOM   3582 C  CB  . TYR   A 1 445 ? 8.835   -8.835  27.335 1    24.253  ? 481 TYR   A CB  1 
ATOM   3583 C  CG  . TYR   A 1 445 ? 9.236   -8.129  26.044 1    24.059  ? 481 TYR   A CG  1 
ATOM   3584 C  CD1 . TYR   A 1 445 ? 9.354   -6.744  25.968 1    24.595  ? 481 TYR   A CD1 1 
ATOM   3585 C  CD2 . TYR   A 1 445 ? 9.409   -8.857  24.876 1    23.854  ? 481 TYR   A CD2 1 
ATOM   3586 C  CE1 . TYR   A 1 445 ? 9.673   -6.113  24.788 1    21.988  ? 481 TYR   A CE1 1 
ATOM   3587 C  CE2 . TYR   A 1 445 ? 9.687   -8.235  23.674 1    27.31   ? 481 TYR   A CE2 1 
ATOM   3588 C  CZ  . TYR   A 1 445 ? 9.85    -6.873  23.651 1    24.82   ? 481 TYR   A CZ  1 
ATOM   3589 O  OH  . TYR   A 1 445 ? 10.125  -6.339  22.466 1    25.933  ? 481 TYR   A OH  1 
ATOM   3590 N  N   . ASN   A 1 446 ? 8.464   -9.973  30.082 1    26.957  ? 482 ASN   A N   1 
ATOM   3591 C  CA  . ASN   A 1 446 ? 7.573   -10.901 30.74  1    31.712  ? 482 ASN   A CA  1 
ATOM   3592 C  C   . ASN   A 1 446 ? 7.551   -10.547 32.215 1    31.026  ? 482 ASN   A C   1 
ATOM   3593 O  O   . ASN   A 1 446 ? 6.464   -10.423 32.776 1    27.389  ? 482 ASN   A O   1 
ATOM   3594 C  CB  . ASN   A 1 446 ? 7.993   -12.362 30.563 1    30.07   ? 482 ASN   A CB  1 
ATOM   3595 C  CG  . ASN   A 1 446 ? 6.78    -13.279 30.487 1    37.34   ? 482 ASN   A CG  1 
ATOM   3596 O  OD1 . ASN   A 1 446 ? 5.949   -13.162 29.567 1    38.046  ? 482 ASN   A OD1 1 
ATOM   3597 N  ND2 . ASN   A 1 446 ? 6.658   -14.211 31.429 1    28.272  ? 482 ASN   A ND2 1 
ATOM   3598 N  N   . GLN   A 1 447 ? 8.743   -10.387 32.815 1    25.212  ? 483 GLN   A N   1 
ATOM   3599 C  CA  . GLN   A 1 447 ? 8.834   -9.99   34.214 1    28.085  ? 483 GLN   A CA  1 
ATOM   3600 C  C   . GLN   A 1 447 ? 7.991   -8.733  34.472 1    28.434  ? 483 GLN   A C   1 
ATOM   3601 O  O   . GLN   A 1 447 ? 7.396   -8.573  35.532 1    34.215  ? 483 GLN   A O   1 
ATOM   3602 C  CB  . GLN   A 1 447 ? 10.241  -9.802  34.813 1    31.771  ? 483 GLN   A CB  1 
ATOM   3603 C  CG  . GLN   A 1 447 ? 11.243  -10.959 34.649 1    35.049  ? 483 GLN   A CG  1 
ATOM   3604 C  CD  . GLN   A 1 447 ? 11.981  -11.087 33.313 1    39.348  ? 483 GLN   A CD  1 
ATOM   3605 O  OE1 . GLN   A 1 447 ? 11.498  -10.762 32.21  1    31.834  ? 483 GLN   A OE1 1 
ATOM   3606 N  NE2 . GLN   A 1 447 ? 13.171  -11.679 33.38  1    41.85   ? 483 GLN   A NE2 1 
ATOM   3607 N  N   . GLU   A 1 448 ? 7.938   -7.812  33.525 1    22.645  ? 484 GLU   A N   1 
ATOM   3608 C  CA  . GLU   A 1 448 ? 7.238   -6.563  33.819 1    27.893  ? 484 GLU   A CA  1 
ATOM   3609 C  C   . GLU   A 1 448 ? 5.73    -6.752  33.567 1    26.181  ? 484 GLU   A C   1 
ATOM   3610 O  O   . GLU   A 1 448 ? 4.888   -5.991  34.051 1    26.127  ? 484 GLU   A O   1 
ATOM   3611 C  CB  . GLU   A 1 448 ? 7.707   -5.425  32.886 1    30.381  ? 484 GLU   A CB  1 
ATOM   3612 C  CG  . GLU   A 1 448 ? 9.047   -4.783  33.235 1    36.689  ? 484 GLU   A CG  1 
ATOM   3613 C  CD  . GLU   A 1 448 ? 9.2     -4.293  34.673 1    42.612  ? 484 GLU   A CD  1 
ATOM   3614 O  OE1 . GLU   A 1 448 ? 8.58    -3.28   35.056 1    45.462  ? 484 GLU   A OE1 1 
ATOM   3615 O  OE2 . GLU   A 1 448 ? 9.91    -4.973  35.44  1    56.017  ? 484 GLU   A OE2 1 
ATOM   3616 N  N   . TRP   A 1 449 ? 5.418   -7.76   32.748 1    21.84   ? 485 TRP   A N   1 
ATOM   3617 C  CA  . TRP   A 1 449 ? 4.049   -8.158  32.554 1    23.178  ? 485 TRP   A CA  1 
ATOM   3618 C  C   . TRP   A 1 449 ? 3.546   -8.746  33.877 1    24.548  ? 485 TRP   A C   1 
ATOM   3619 O  O   . TRP   A 1 449 ? 2.479   -8.388  34.356 1    28.221  ? 485 TRP   A O   1 
ATOM   3620 C  CB  . TRP   A 1 449 ? 3.959   -9.156  31.399 1    18.495  ? 485 TRP   A CB  1 
ATOM   3621 C  CG  . TRP   A 1 449 ? 2.571   -9.686  31.219 1    20.009  ? 485 TRP   A CG  1 
ATOM   3622 C  CD1 . TRP   A 1 449 ? 2.159   -10.926 31.598 1    23.007  ? 485 TRP   A CD1 1 
ATOM   3623 C  CD2 . TRP   A 1 449 ? 1.434   -9.064  30.584 1    18.606  ? 485 TRP   A CD2 1 
ATOM   3624 N  NE1 . TRP   A 1 449 ? 0.858   -11.144 31.211 1    23.099  ? 485 TRP   A NE1 1 
ATOM   3625 C  CE2 . TRP   A 1 449 ? 0.395   -10.025 30.574 1    19.542  ? 485 TRP   A CE2 1 
ATOM   3626 C  CE3 . TRP   A 1 449 ? 1.198   -7.828  29.973 1    20.191  ? 485 TRP   A CE3 1 
ATOM   3627 C  CZ2 . TRP   A 1 449 ? -0.86   -9.77   30.036 1    17.689  ? 485 TRP   A CZ2 1 
ATOM   3628 C  CZ3 . TRP   A 1 449 ? -0.031  -7.579  29.383 1    22.658  ? 485 TRP   A CZ3 1 
ATOM   3629 C  CH2 . TRP   A 1 449 ? -1.047  -8.552  29.411 1    20.863  ? 485 TRP   A CH2 1 
ATOM   3630 N  N   . TRP   A 1 450 ? 4.373   -9.554  34.517 1    21.294  ? 486 TRP   A N   1 
ATOM   3631 C  CA  . TRP   A 1 450 ? 4.001   -10.154 35.789 1    24.717  ? 486 TRP   A CA  1 
ATOM   3632 C  C   . TRP   A 1 450 ? 3.927   -9.151  36.937 1    22.534  ? 486 TRP   A C   1 
ATOM   3633 O  O   . TRP   A 1 450 ? 3.024   -9.271  37.77  1    22.615  ? 486 TRP   A O   1 
ATOM   3634 C  CB  . TRP   A 1 450 ? 4.655   -11.533 36.094 1    22.441  ? 486 TRP   A CB  1 
ATOM   3635 C  CG  . TRP   A 1 450 ? 3.983   -12.565 35.219 1    23.463  ? 486 TRP   A CG  1 
ATOM   3636 C  CD1 . TRP   A 1 450 ? 4.415   -12.999 34.002 1    18.825  ? 486 TRP   A CD1 1 
ATOM   3637 C  CD2 . TRP   A 1 450 ? 2.669   -13.167 35.415 1    22.588  ? 486 TRP   A CD2 1 
ATOM   3638 N  NE1 . TRP   A 1 450 ? 3.48    -13.85  33.452 1    19.587  ? 486 TRP   A NE1 1 
ATOM   3639 C  CE2 . TRP   A 1 450 ? 2.399   -13.958 34.278 1    19.348  ? 486 TRP   A CE2 1 
ATOM   3640 C  CE3 . TRP   A 1 450 ? 1.705   -13.12  36.426 1    24.292  ? 486 TRP   A CE3 1 
ATOM   3641 C  CZ2 . TRP   A 1 450 ? 1.235   -14.697 34.137 1    21.489  ? 486 TRP   A CZ2 1 
ATOM   3642 C  CZ3 . TRP   A 1 450 ? 0.545   -13.873 36.289 1    24.352  ? 486 TRP   A CZ3 1 
ATOM   3643 C  CH2 . TRP   A 1 450 ? 0.298   -14.626 35.145 1    21.124  ? 486 TRP   A CH2 1 
ATOM   3644 N  N   . SER   A 1 451 ? 4.76    -8.103  36.923 1    27.576  ? 487 SER   A N   1 
ATOM   3645 C  CA  . SER   A 1 451 ? 4.651   -7.09   37.971 1    29.81   ? 487 SER   A CA  1 
ATOM   3646 C  C   . SER   A 1 451 ? 3.26    -6.476  37.959 1    25.994  ? 487 SER   A C   1 
ATOM   3647 O  O   . SER   A 1 451 ? 2.712   -6.175  39.021 1    25.748  ? 487 SER   A O   1 
ATOM   3648 C  CB  . SER   A 1 451 ? 5.649   -5.991  37.823 1    33.554  ? 487 SER   A CB  1 
ATOM   3649 O  OG  . SER   A 1 451 ? 6.89    -6.606  38.09  1    40.615  ? 487 SER   A OG  1 
ATOM   3650 N  N   . LEU   A 1 452 ? 2.748   -6.244  36.743 1    23.916  ? 488 LEU   A N   1 
ATOM   3651 C  CA  . LEU   A 1 452 ? 1.485   -5.534  36.606 1    22.136  ? 488 LEU   A CA  1 
ATOM   3652 C  C   . LEU   A 1 452 ? 0.299   -6.431  36.989 1    22.972  ? 488 LEU   A C   1 
ATOM   3653 O  O   . LEU   A 1 452 ? -0.576  -5.977  37.731 1    22.206  ? 488 LEU   A O   1 
ATOM   3654 C  CB  . LEU   A 1 452 ? 1.373   -4.912  35.228 1    20.604  ? 488 LEU   A CB  1 
ATOM   3655 C  CG  . LEU   A 1 452 ? 2.355   -3.755  35.005 1    23.643  ? 488 LEU   A CG  1 
ATOM   3656 C  CD1 . LEU   A 1 452 ? 2.4     -3.344  33.536 1    20.366  ? 488 LEU   A CD1 1 
ATOM   3657 C  CD2 . LEU   A 1 452 ? 2.015   -2.562  35.895 1    17.415  ? 488 LEU   A CD2 1 
ATOM   3658 N  N   . ARG   A 1 453 ? 0.367   -7.715  36.587 1    20.398  ? 489 ARG   A N   1 
ATOM   3659 C  CA  . ARG   A 1 453 ? -0.633  -8.736  36.873 1    21.525  ? 489 ARG   A CA  1 
ATOM   3660 C  C   . ARG   A 1 453 ? -0.794  -8.872  38.393 1    21.717  ? 489 ARG   A C   1 
ATOM   3661 O  O   . ARG   A 1 453 ? -1.928  -8.855  38.909 1    22.478  ? 489 ARG   A O   1 
ATOM   3662 C  CB  . ARG   A 1 453 ? -0.233  -9.982  36.07  1    19.652  ? 489 ARG   A CB  1 
ATOM   3663 C  CG  . ARG   A 1 453 ? -0.243  -9.787  34.544 1    21.155  ? 489 ARG   A CG  1 
ATOM   3664 C  CD  . ARG   A 1 453 ? -1.617  -10.179 33.992 1    17.91   ? 489 ARG   A CD  1 
ATOM   3665 N  NE  . ARG   A 1 453 ? -1.843  -11.631 34.088 1    17.058  ? 489 ARG   A NE  1 
ATOM   3666 C  CZ  . ARG   A 1 453 ? -2.943  -12.308 33.845 1    19.182  ? 489 ARG   A CZ  1 
ATOM   3667 N  NH1 . ARG   A 1 453 ? -2.835  -13.574 33.451 1    20.385  ? 489 ARG   A NH1 1 
ATOM   3668 N  NH2 . ARG   A 1 453 ? -4.13   -11.72  33.874 1    18.527  ? 489 ARG   A NH2 1 
ATOM   3669 N  N   . LEU   A 1 454 ? 0.354   -8.959  39.087 1    21.469  ? 490 LEU   A N   1 
ATOM   3670 C  CA  . LEU   A 1 454 ? 0.443   -8.967  40.533 1    24.001  ? 490 LEU   A CA  1 
ATOM   3671 C  C   . LEU   A 1 454 ? -0.067  -7.643  41.14  1    26.412  ? 490 LEU   A C   1 
ATOM   3672 O  O   . LEU   A 1 454 ? -0.954  -7.641  41.995 1    24.497  ? 490 LEU   A O   1 
ATOM   3673 C  CB  . LEU   A 1 454 ? 1.856   -9.334  40.986 1    24.272  ? 490 LEU   A CB  1 
ATOM   3674 C  CG  . LEU   A 1 454 ? 2.111   -9.149  42.489 1    27.483  ? 490 LEU   A CG  1 
ATOM   3675 C  CD1 . LEU   A 1 454 ? 1.123   -10.016 43.306 1    21.63   ? 490 LEU   A CD1 1 
ATOM   3676 C  CD2 . LEU   A 1 454 ? 3.583   -9.479  42.837 1    26.221  ? 490 LEU   A CD2 1 
ATOM   3677 N  N   . LYS   A 1 455 ? 0.454   -6.492  40.713 1    24.524  ? 491 LYS   A N   1 
ATOM   3678 C  CA  . LYS   A 1 455 ? 0.118   -5.278  41.437 1    27.33   ? 491 LYS   A CA  1 
ATOM   3679 C  C   . LYS   A 1 455 ? -1.342  -4.829  41.205 1    25.951  ? 491 LYS   A C   1 
ATOM   3680 O  O   . LYS   A 1 455 ? -2.033  -4.425  42.141 1    26.045  ? 491 LYS   A O   1 
ATOM   3681 C  CB  . LYS   A 1 455 ? 1.239   -4.269  41.175 1    33.949  ? 491 LYS   A CB  1 
ATOM   3682 C  CG  . LYS   A 1 455 ? 0.771   -2.83   41.231 1    31.262  ? 491 LYS   A CG  1 
ATOM   3683 C  CD  . LYS   A 1 455 ? 1.855   -1.88   40.73  1    39.634  ? 491 LYS   A CD  1 
ATOM   3684 C  CE  . LYS   A 1 455 ? 1.25    -0.47   40.886 1    46.224  ? 491 LYS   A CE  1 
ATOM   3685 N  NZ  . LYS   A 1 455 ? 2.007   0.595   40.214 1    44.103  ? 491 LYS   A NZ  1 
ATOM   3686 N  N   . TYR   A 1 456 ? -1.845  -4.91   39.976 1    26.551  ? 492 TYR   A N   1 
ATOM   3687 C  CA  . TYR   A 1 456 ? -3.215  -4.509  39.678 1    22.224  ? 492 TYR   A CA  1 
ATOM   3688 C  C   . TYR   A 1 456 ? -4.195  -5.62   40.013 1    26.54   ? 492 TYR   A C   1 
ATOM   3689 O  O   . TYR   A 1 456 ? -5.195  -5.349  40.678 1    23.673  ? 492 TYR   A O   1 
ATOM   3690 C  CB  . TYR   A 1 456 ? -3.27   -4.105  38.215 1    26.05   ? 492 TYR   A CB  1 
ATOM   3691 C  CG  . TYR   A 1 456 ? -2.58   -2.765  38.075 1    32.242  ? 492 TYR   A CG  1 
ATOM   3692 C  CD1 . TYR   A 1 456 ? -2.936  -1.707  38.912 1    35.798  ? 492 TYR   A CD1 1 
ATOM   3693 C  CD2 . TYR   A 1 456 ? -1.504  -2.581  37.195 1    36.68   ? 492 TYR   A CD2 1 
ATOM   3694 C  CE1 . TYR   A 1 456 ? -2.26   -0.493  38.86  1    40.925  ? 492 TYR   A CE1 1 
ATOM   3695 C  CE2 . TYR   A 1 456 ? -0.83   -1.364  37.115 1    33.859  ? 492 TYR   A CE2 1 
ATOM   3696 C  CZ  . TYR   A 1 456 ? -1.231  -0.319  37.943 1    39.383  ? 492 TYR   A CZ  1 
ATOM   3697 O  OH  . TYR   A 1 456 ? -0.649  0.903   37.91  1    37.357  ? 492 TYR   A OH  1 
ATOM   3698 N  N   . GLN   A 1 457 ? -3.934  -6.848  39.5   1    28.095  ? 493 GLN   A N   1 
ATOM   3699 C  CA  . GLN   A 1 457 ? -4.95   -7.901  39.547 1    22.603  ? 493 GLN   A CA  1 
ATOM   3700 C  C   . GLN   A 1 457 ? -4.797  -8.791  40.76  1    22.258  ? 493 GLN   A C   1 
ATOM   3701 O  O   . GLN   A 1 457 ? -5.771  -9.472  41.017 1    19.322  ? 493 GLN   A O   1 
ATOM   3702 C  CB  . GLN   A 1 457 ? -5.075  -8.943  38.434 1    20.428  ? 493 GLN   A CB  1 
ATOM   3703 C  CG  . GLN   A 1 457 ? -5.596  -8.273  37.174 1    21.552  ? 493 GLN   A CG  1 
ATOM   3704 C  CD  . GLN   A 1 457 ? -5.648  -9.147  35.956 1    19.55   ? 493 GLN   A CD  1 
ATOM   3705 O  OE1 . GLN   A 1 457 ? -4.672  -9.309  35.206 1    20.671  ? 493 GLN   A OE1 1 
ATOM   3706 N  NE2 . GLN   A 1 457 ? -6.849  -9.64   35.731 1    16.096  ? 493 GLN   A NE2 1 
ATOM   3707 N  N   . GLY   A 1 458 ? -3.635  -8.791  41.452 1    20.366  ? 494 GLY   A N   1 
ATOM   3708 C  CA  . GLY   A 1 458 ? -3.393  -9.708  42.582 1    22.407  ? 494 GLY   A CA  1 
ATOM   3709 C  C   . GLY   A 1 458 ? -3.391  -11.202 42.153 1    23.948  ? 494 GLY   A C   1 
ATOM   3710 O  O   . GLY   A 1 458 ? -3.981  -12.084 42.825 1    19.178  ? 494 GLY   A O   1 
ATOM   3711 N  N   . LEU   A 1 459 ? -2.744  -11.491 40.999 1    21.901  ? 495 LEU   A N   1 
ATOM   3712 C  CA  . LEU   A 1 459 ? -2.628  -12.855 40.494 1    20.551  ? 495 LEU   A CA  1 
ATOM   3713 C  C   . LEU   A 1 459 ? -1.149  -13.263 40.447 1    20.069  ? 495 LEU   A C   1 
ATOM   3714 O  O   . LEU   A 1 459 ? -0.293  -12.398 40.317 1    21.453  ? 495 LEU   A O   1 
ATOM   3715 C  CB  . LEU   A 1 459 ? -3.15   -12.815 39.067 1    18.455  ? 495 LEU   A CB  1 
ATOM   3716 C  CG  . LEU   A 1 459 ? -4.567  -12.347 38.796 1    18.931  ? 495 LEU   A CG  1 
ATOM   3717 C  CD1 . LEU   A 1 459 ? -4.986  -12.519 37.297 1    16.641  ? 495 LEU   A CD1 1 
ATOM   3718 C  CD2 . LEU   A 1 459 ? -5.471  -12.969 39.828 1    17.589  ? 495 LEU   A CD2 1 
ATOM   3719 N  N   A CYS   A 1 460 ? -0.887  -14.581 40.491 0.5  20.489  ? 496 CYS   A N   1 
ATOM   3720 N  N   B CYS   A 1 460 ? -0.838  -14.565 40.52  0.5  21.911  ? 496 CYS   A N   1 
ATOM   3721 C  CA  A CYS   A 1 460 ? 0.451   -15.135 40.312 0.5  23.925  ? 496 CYS   A CA  1 
ATOM   3722 C  CA  B CYS   A 1 460 ? 0.521   -15.052 40.291 0.5  26.444  ? 496 CYS   A CA  1 
ATOM   3723 C  C   A CYS   A 1 460 ? 0.378   -16.198 39.222 0.5  26.981  ? 496 CYS   A C   1 
ATOM   3724 C  C   B CYS   A 1 460 ? 0.408   -16.173 39.256 0.5  28.668  ? 496 CYS   A C   1 
ATOM   3725 O  O   A CYS   A 1 460 ? -0.682  -16.815 39.023 0.5  22.532  ? 496 CYS   A O   1 
ATOM   3726 O  O   B CYS   A 1 460 ? -0.659  -16.796 39.123 0.5  24.131  ? 496 CYS   A O   1 
ATOM   3727 C  CB  A CYS   A 1 460 ? 1.1     -15.68  41.599 0.5  22.776  ? 496 CYS   A CB  1 
ATOM   3728 C  CB  B CYS   A 1 460 ? 1.289   -15.453 41.572 0.5  28.408  ? 496 CYS   A CB  1 
ATOM   3729 S  SG  A CYS   A 1 460 ? 0.135   -16.901 42.527 0.5  25.567  ? 496 CYS   A SG  1 
ATOM   3730 S  SG  B CYS   A 1 460 ? 2.505   -14.244 42.212 0.5  35.937  ? 496 CYS   A SG  1 
ATOM   3731 N  N   . PRO   A 1 461 ? 1.492   -16.442 38.485 1    27.274  ? 497 PRO   A N   1 
ATOM   3732 C  CA  . PRO   A 1 461 ? 1.474   -17.481 37.466 1    26.781  ? 497 PRO   A CA  1 
ATOM   3733 C  C   . PRO   A 1 461 ? 1.424   -18.824 38.209 1    26.139  ? 497 PRO   A C   1 
ATOM   3734 O  O   . PRO   A 1 461 ? 2.034   -18.948 39.254 1    26.402  ? 497 PRO   A O   1 
ATOM   3735 C  CB  . PRO   A 1 461 ? 2.783   -17.203 36.704 1    29.305  ? 497 PRO   A CB  1 
ATOM   3736 C  CG  . PRO   A 1 461 ? 3.741   -16.614 37.747 1    35.701  ? 497 PRO   A CG  1 
ATOM   3737 C  CD  . PRO   A 1 461 ? 2.792   -15.736 38.585 1    33.388  ? 497 PRO   A CD  1 
ATOM   3738 N  N   . PRO   A 1 462 ? 0.634   -19.84  37.779 1    24.232  ? 498 PRO   A N   1 
ATOM   3739 C  CA  . PRO   A 1 462 ? 0.677   -21.128 38.452 1    23.595  ? 498 PRO   A CA  1 
ATOM   3740 C  C   . PRO   A 1 462 ? 2.003   -21.892 38.271 1    28.339  ? 498 PRO   A C   1 
ATOM   3741 O  O   . PRO   A 1 462 ? 2.314   -22.731 39.099 1    28.101  ? 498 PRO   A O   1 
ATOM   3742 C  CB  . PRO   A 1 462 ? -0.549  -21.875 37.89  1    19.834  ? 498 PRO   A CB  1 
ATOM   3743 C  CG  . PRO   A 1 462 ? -0.687  -21.297 36.516 1    21.729  ? 498 PRO   A CG  1 
ATOM   3744 C  CD  . PRO   A 1 462 ? -0.305  -19.811 36.617 1    23.081  ? 498 PRO   A CD  1 
ATOM   3745 N  N   . VAL   A 1 463 ? 2.798   -21.562 37.236 1    27.511  ? 499 VAL   A N   1 
ATOM   3746 C  CA  . VAL   A 1 463 ? 4.079   -22.179 36.903 1    28.547  ? 499 VAL   A CA  1 
ATOM   3747 C  C   . VAL   A 1 463 ? 5.109   -21.063 36.823 1    28.842  ? 499 VAL   A C   1 
ATOM   3748 O  O   . VAL   A 1 463 ? 4.802   -20.008 36.308 1    30.707  ? 499 VAL   A O   1 
ATOM   3749 C  CB  . VAL   A 1 463 ? 3.887   -22.797 35.505 1    33.619  ? 499 VAL   A CB  1 
ATOM   3750 C  CG1 . VAL   A 1 463 ? 5.233   -23.15  34.869 1    34.867  ? 499 VAL   A CG1 1 
ATOM   3751 C  CG2 . VAL   A 1 463 ? 2.944   -23.99  35.54  1    29.892  ? 499 VAL   A CG2 1 
ATOM   3752 N  N   . PRO   A 1 464 ? 6.313   -21.145 37.417 1    35.251  ? 500 PRO   A N   1 
ATOM   3753 C  CA  . PRO   A 1 464 ? 7.313   -20.103 37.196 1    31.655  ? 500 PRO   A CA  1 
ATOM   3754 C  C   . PRO   A 1 464 ? 7.565   -19.861 35.703 1    34.712  ? 500 PRO   A C   1 
ATOM   3755 O  O   . PRO   A 1 464 ? 7.632   -20.798 34.889 1    38.579  ? 500 PRO   A O   1 
ATOM   3756 C  CB  . PRO   A 1 464 ? 8.54    -20.818 37.884 1    36.049  ? 500 PRO   A CB  1 
ATOM   3757 C  CG  . PRO   A 1 464 ? 7.935   -21.455 39.092 1    35.808  ? 500 PRO   A CG  1 
ATOM   3758 C  CD  . PRO   A 1 464 ? 6.731   -22.136 38.426 1    38.023  ? 500 PRO   A CD  1 
ATOM   3759 N  N   . ARG   A 1 465 ? 7.71    -18.584 35.34  1    31.417  ? 501 ARG   A N   1 
ATOM   3760 C  CA  . ARG   A 1 465 ? 7.994   -18.207 33.965 1    33.424  ? 501 ARG   A CA  1 
ATOM   3761 C  C   . ARG   A 1 465 ? 9.511   -18.254 33.749 1    35.867  ? 501 ARG   A C   1 
ATOM   3762 O  O   . ARG   A 1 465 ? 10.323  -18.056 34.662 1    36.841  ? 501 ARG   A O   1 
ATOM   3763 C  CB  . ARG   A 1 465 ? 7.47    -16.771 33.779 1    32.398  ? 501 ARG   A CB  1 
ATOM   3764 C  CG  . ARG   A 1 465 ? 6.176   -16.355 34.468 1    29.513  ? 501 ARG   A CG  1 
ATOM   3765 C  CD  . ARG   A 1 465 ? 5.026   -17.371 34.189 1    30.455  ? 501 ARG   A CD  1 
ATOM   3766 N  NE  . ARG   A 1 465 ? 4.716   -17.62  32.763 1    28.235  ? 501 ARG   A NE  1 
ATOM   3767 C  CZ  . ARG   A 1 465 ? 4.682   -18.809 32.191 1    29.176  ? 501 ARG   A CZ  1 
ATOM   3768 N  NH1 . ARG   A 1 465 ? 4.914   -19.899 32.926 1    30.283  ? 501 ARG   A NH1 1 
ATOM   3769 N  NH2 . ARG   A 1 465 ? 4.469   -18.888 30.889 1    25.93   ? 501 ARG   A NH2 1 
ATOM   3770 N  N   . THR   A 1 466 ? 9.917   -18.52  32.514 1    38.75   ? 502 THR   A N   1 
ATOM   3771 C  CA  . THR   A 1 466 ? 11.347  -18.57  32.232 1    37.62   ? 502 THR   A CA  1 
ATOM   3772 C  C   . THR   A 1 466 ? 11.608  -17.712 30.998 1    38.312  ? 502 THR   A C   1 
ATOM   3773 O  O   . THR   A 1 466 ? 10.702  -17.463 30.175 1    36.044  ? 502 THR   A O   1 
ATOM   3774 C  CB  . THR   A 1 466 ? 11.823  -20.023 32.034 1    39.462  ? 502 THR   A CB  1 
ATOM   3775 O  OG1 . THR   A 1 466 ? 10.943  -20.655 31.103 1    44.916  ? 502 THR   A OG1 1 
ATOM   3776 C  CG2 . THR   A 1 466 ? 11.753  -20.865 33.304 1    33.291  ? 502 THR   A CG2 1 
ATOM   3777 N  N   . GLN   A 1 467 ? 12.866  -17.306 30.867 1    35      ? 503 GLN   A N   1 
ATOM   3778 C  CA  . GLN   A 1 467 ? 13.275  -16.541 29.711 1    40.98   ? 503 GLN   A CA  1 
ATOM   3779 C  C   . GLN   A 1 467 ? 12.836  -17.374 28.524 1    40.663  ? 503 GLN   A C   1 
ATOM   3780 O  O   . GLN   A 1 467 ? 12.924  -18.606 28.529 1    42.257  ? 503 GLN   A O   1 
ATOM   3781 C  CB  . GLN   A 1 467 ? 14.77   -16.218 29.599 1    39.853  ? 503 GLN   A CB  1 
ATOM   3782 C  CG  . GLN   A 1 467 ? 15.032  -14.961 28.778 1    46.349  ? 503 GLN   A CG  1 
ATOM   3783 C  CD  . GLN   A 1 467 ? 14.45   -13.711 29.422 1    55.246  ? 503 GLN   A CD  1 
ATOM   3784 O  OE1 . GLN   A 1 467 ? 14.206  -13.644 30.634 1    56.906  ? 503 GLN   A OE1 1 
ATOM   3785 N  NE2 . GLN   A 1 467 ? 14.247  -12.676 28.622 1    57.488  ? 503 GLN   A NE2 1 
ATOM   3786 N  N   . GLY   A 1 468 ? 12.331  -16.69  27.518 1    33.237  ? 504 GLY   A N   1 
ATOM   3787 C  CA  . GLY   A 1 468 ? 11.716  -17.508 26.495 1    29.165  ? 504 GLY   A CA  1 
ATOM   3788 C  C   . GLY   A 1 468 ? 10.194  -17.383 26.597 1    27.253  ? 504 GLY   A C   1 
ATOM   3789 O  O   . GLY   A 1 468 ? 9.551   -17.482 25.583 1    27.056  ? 504 GLY   A O   1 
ATOM   3790 N  N   . ASP   A 1 469 ? 9.612   -17.123 27.783 1    24.849  ? 505 ASP   A N   1 
ATOM   3791 C  CA  . ASP   A 1 469 ? 8.166   -16.906 27.845 1    25.761  ? 505 ASP   A CA  1 
ATOM   3792 C  C   . ASP   A 1 469 ? 7.844   -15.476 27.392 1    25.457  ? 505 ASP   A C   1 
ATOM   3793 O  O   . ASP   A 1 469 ? 8.617   -14.549 27.632 1    26.336  ? 505 ASP   A O   1 
ATOM   3794 C  CB  . ASP   A 1 469 ? 7.615   -17.267 29.232 1    24.941  ? 505 ASP   A CB  1 
ATOM   3795 C  CG  . ASP   A 1 469 ? 7.713   -18.742 29.597 1    26.497  ? 505 ASP   A CG  1 
ATOM   3796 O  OD1 . ASP   A 1 469 ? 7.712   -19.574 28.621 1    28.242  ? 505 ASP   A OD1 1 
ATOM   3797 O  OD2 . ASP   A 1 469 ? 7.831   -19.055 30.826 1    26.273  ? 505 ASP   A OD2 1 
ATOM   3798 N  N   . PHE   A 1 470 ? 6.698   -15.297 26.718 1    23.65   ? 506 PHE   A N   1 
ATOM   3799 C  CA  . PHE   A 1 470 ? 6.151   -13.977 26.402 1    21.052  ? 506 PHE   A CA  1 
ATOM   3800 C  C   . PHE   A 1 470 ? 4.627   -14.102 26.528 1    22.597  ? 506 PHE   A C   1 
ATOM   3801 O  O   . PHE   A 1 470 ? 3.913   -14.341 25.535 1    16.25   ? 506 PHE   A O   1 
ATOM   3802 C  CB  . PHE   A 1 470 ? 6.616   -13.696 24.967 1    20.252  ? 506 PHE   A CB  1 
ATOM   3803 C  CG  . PHE   A 1 470 ? 6.188   -12.328 24.464 1    22.749  ? 506 PHE   A CG  1 
ATOM   3804 C  CD1 . PHE   A 1 470 ? 6.622   -11.151 25.11  1    20.959  ? 506 PHE   A CD1 1 
ATOM   3805 C  CD2 . PHE   A 1 470 ? 5.403   -12.216 23.306 1    22.153  ? 506 PHE   A CD2 1 
ATOM   3806 C  CE1 . PHE   A 1 470 ? 6.231   -9.892  24.657 1    18.211  ? 506 PHE   A CE1 1 
ATOM   3807 C  CE2 . PHE   A 1 470 ? 5.016   -10.959 22.846 1    20.821  ? 506 PHE   A CE2 1 
ATOM   3808 C  CZ  . PHE   A 1 470 ? 5.421   -9.797  23.541 1    22.444  ? 506 PHE   A CZ  1 
ATOM   3809 N  N   . ASP   A 1 471 ? 4.16    -14.119 27.796 1    20.844  ? 507 ASP   A N   1 
ATOM   3810 C  CA  . ASP   A 1 471 ? 2.745   -14.234 28.108 1    18.685  ? 507 ASP   A CA  1 
ATOM   3811 C  C   . ASP   A 1 471 ? 1.918   -13.155 27.373 1    20.868  ? 507 ASP   A C   1 
ATOM   3812 O  O   . ASP   A 1 471 ? 0.842   -13.419 26.824 1    20.21   ? 507 ASP   A O   1 
ATOM   3813 C  CB  . ASP   A 1 471 ? 2.683   -14.394 29.61  1    20.773  ? 507 ASP   A CB  1 
ATOM   3814 C  CG  . ASP   A 1 471 ? 3.453   -15.618 30.094 1    24.244  ? 507 ASP   A CG  1 
ATOM   3815 O  OD1 . ASP   A 1 471 ? 3.425   -16.674 29.396 1    24.723  ? 507 ASP   A OD1 1 
ATOM   3816 O  OD2 . ASP   A 1 471 ? 4.057   -15.54  31.182 1    26.716  ? 507 ASP   A OD2 1 
ATOM   3817 N  N   . PRO   A 1 472 ? 2.379   -11.889 27.218 1    20.103  ? 508 PRO   A N   1 
ATOM   3818 C  CA  . PRO   A 1 472 ? 1.568   -10.912 26.492 1    21.029  ? 508 PRO   A CA  1 
ATOM   3819 C  C   . PRO   A 1 472 ? 1.164   -11.359 25.101 1    22.136  ? 508 PRO   A C   1 
ATOM   3820 O  O   . PRO   A 1 472 ? 0.04    -11.092 24.669 1    25.004  ? 508 PRO   A O   1 
ATOM   3821 C  CB  . PRO   A 1 472 ? 2.422   -9.614  26.482 1    18.9    ? 508 PRO   A CB  1 
ATOM   3822 C  CG  . PRO   A 1 472 ? 3.258   -9.801  27.751 1    19.81   ? 508 PRO   A CG  1 
ATOM   3823 C  CD  . PRO   A 1 472 ? 3.601   -11.3   27.803 1    17.806  ? 508 PRO   A CD  1 
ATOM   3824 N  N   . GLY   A 1 473 ? 2.059   -12.061 24.404 1    21.769  ? 509 GLY   A N   1 
ATOM   3825 C  CA  . GLY   A 1 473 ? 1.668   -12.48  23.071 1    20.979  ? 509 GLY   A CA  1 
ATOM   3826 C  C   . GLY   A 1 473 ? 0.58    -13.555 23.143 1    22.916  ? 509 GLY   A C   1 
ATOM   3827 O  O   . GLY   A 1 473 ? 0.087   -14.046 22.125 1    25.736  ? 509 GLY   A O   1 
ATOM   3828 N  N   . ALA   A 1 474 ? 0.187   -13.955 24.357 1    22.006  ? 510 ALA   A N   1 
ATOM   3829 C  CA  . ALA   A 1 474 ? -0.861  -14.959 24.441 1    22.997  ? 510 ALA   A CA  1 
ATOM   3830 C  C   . ALA   A 1 474 ? -2.258  -14.326 24.539 1    20.901  ? 510 ALA   A C   1 
ATOM   3831 O  O   . ALA   A 1 474 ? -3.28   -14.999 24.668 1    20.453  ? 510 ALA   A O   1 
ATOM   3832 C  CB  . ALA   A 1 474 ? -0.526  -15.907 25.567 1    24.001  ? 510 ALA   A CB  1 
ATOM   3833 N  N   . LYS   A 1 475 ? -2.305  -12.997 24.438 1    22.024  ? 511 LYS   A N   1 
ATOM   3834 C  CA  . LYS   A 1 475 ? -3.574  -12.286 24.443 1    20.743  ? 511 LYS   A CA  1 
ATOM   3835 C  C   . LYS   A 1 475 ? -3.726  -11.596 23.086 1    21.426  ? 511 LYS   A C   1 
ATOM   3836 O  O   . LYS   A 1 475 ? -2.852  -10.817 22.679 1    24.62   ? 511 LYS   A O   1 
ATOM   3837 C  CB  . LYS   A 1 475 ? -3.584  -11.339 25.65  1    16.837  ? 511 LYS   A CB  1 
ATOM   3838 C  CG  . LYS   A 1 475 ? -4.717  -10.31  25.588 1    17.759  ? 511 LYS   A CG  1 
ATOM   3839 C  CD  . LYS   A 1 475 ? -6.066  -10.986 25.835 1    21.069  ? 511 LYS   A CD  1 
ATOM   3840 C  CE  . LYS   A 1 475 ? -7.317  -10.105 25.602 1    24.823  ? 511 LYS   A CE  1 
ATOM   3841 N  NZ  . LYS   A 1 475 ? -8.589  -10.847 25.639 1    25.906  ? 511 LYS   A NZ  1 
ATOM   3842 N  N   . PHE   A 1 476 ? -4.895  -11.796 22.473 1    25.066  ? 512 PHE   A N   1 
ATOM   3843 C  CA  . PHE   A 1 476 ? -5.178  -11.47  21.073 1    22.613  ? 512 PHE   A CA  1 
ATOM   3844 C  C   . PHE   A 1 476 ? -4.65   -10.104 20.635 1    18.82   ? 512 PHE   A C   1 
ATOM   3845 O  O   . PHE   A 1 476 ? -4.009  -10.016 19.608 1    26.269  ? 512 PHE   A O   1 
ATOM   3846 C  CB  . PHE   A 1 476 ? -6.699  -11.455 20.825 1    18.417  ? 512 PHE   A CB  1 
ATOM   3847 C  CG  . PHE   A 1 476 ? -7.134  -11.018 19.423 1    17.969  ? 512 PHE   A CG  1 
ATOM   3848 C  CD1 . PHE   A 1 476 ? -6.997  -11.885 18.329 1    19.378  ? 512 PHE   A CD1 1 
ATOM   3849 C  CD2 . PHE   A 1 476 ? -7.688  -9.75   19.185 1    19.099  ? 512 PHE   A CD2 1 
ATOM   3850 C  CE1 . PHE   A 1 476 ? -7.438  -11.512 17.03  1    19.305  ? 512 PHE   A CE1 1 
ATOM   3851 C  CE2 . PHE   A 1 476 ? -8.116  -9.361  17.888 1    23.149  ? 512 PHE   A CE2 1 
ATOM   3852 C  CZ  . PHE   A 1 476 ? -7.989  -10.24  16.802 1    19.555  ? 512 PHE   A CZ  1 
ATOM   3853 N  N   . HIS   A 1 477 ? -5.047  -9.053  21.344 1    16.572  ? 513 HIS   A N   1 
ATOM   3854 C  CA  . HIS   A 1 477 ? -4.831  -7.641  21.058 1    18.594  ? 513 HIS   A CA  1 
ATOM   3855 C  C   . HIS   A 1 477 ? -3.341  -7.293  21.027 1    21.67   ? 513 HIS   A C   1 
ATOM   3856 O  O   . HIS   A 1 477 ? -2.971  -6.196  20.578 1    20.09   ? 513 HIS   A O   1 
ATOM   3857 C  CB  . HIS   A 1 477 ? -5.446  -6.794  22.185 1    15.619  ? 513 HIS   A CB  1 
ATOM   3858 C  CG  . HIS   A 1 477 ? -6.891  -7.04   22.255 1    18.528  ? 513 HIS   A CG  1 
ATOM   3859 N  ND1 . HIS   A 1 477 ? -7.452  -8.238  22.64  1    21.351  ? 513 HIS   A ND1 1 
ATOM   3860 C  CD2 . HIS   A 1 477 ? -7.905  -6.244  21.862 1    19.632  ? 513 HIS   A CD2 1 
ATOM   3861 C  CE1 . HIS   A 1 477 ? -8.769  -8.142  22.517 1    21.721  ? 513 HIS   A CE1 1 
ATOM   3862 N  NE2 . HIS   A 1 477 ? -9.049  -6.925  22.03  1    18.17   ? 513 HIS   A NE2 1 
ATOM   3863 N  N   . ILE   A 1 478 ? -2.501  -8.194  21.565 1    20.948  ? 514 ILE   A N   1 
ATOM   3864 C  CA  . ILE   A 1 478 ? -1.09   -7.856  21.577 1    22.254  ? 514 ILE   A CA  1 
ATOM   3865 C  C   . ILE   A 1 478 ? -0.536  -8.175  20.182 1    23.372  ? 514 ILE   A C   1 
ATOM   3866 O  O   . ILE   A 1 478 ? -0.004  -7.321  19.528 1    21.592  ? 514 ILE   A O   1 
ATOM   3867 C  CB  . ILE   A 1 478 ? -0.368  -8.581  22.727 1    19.55   ? 514 ILE   A CB  1 
ATOM   3868 C  CG1 . ILE   A 1 478 ? -0.901  -8.22   24.095 1    19.072  ? 514 ILE   A CG1 1 
ATOM   3869 C  CG2 . ILE   A 1 478 ? 1.134   -8.408  22.649 1    19.9    ? 514 ILE   A CG2 1 
ATOM   3870 C  CD1 . ILE   A 1 478 ? -0.448  -6.875  24.499 1    19.867  ? 514 ILE   A CD1 1 
ATOM   3871 N  N   . PRO   A 1 479 ? -0.608  -9.417  19.677 1    26.079  ? 515 PRO   A N   1 
ATOM   3872 C  CA  . PRO   A 1 479 ? -0.207  -9.701  18.307 1    29.666  ? 515 PRO   A CA  1 
ATOM   3873 C  C   . PRO   A 1 479 ? -0.96   -8.931  17.219 1    27.435  ? 515 PRO   A C   1 
ATOM   3874 O  O   . PRO   A 1 479 ? -0.372  -8.621  16.18  1    29.264  ? 515 PRO   A O   1 
ATOM   3875 C  CB  . PRO   A 1 479 ? -0.386  -11.221 18.137 1    27.05   ? 515 PRO   A CB  1 
ATOM   3876 C  CG  . PRO   A 1 479 ? -0.724  -11.779 19.496 1    23.581  ? 515 PRO   A CG  1 
ATOM   3877 C  CD  . PRO   A 1 479 ? -0.967  -10.633 20.414 1    24.567  ? 515 PRO   A CD  1 
ATOM   3878 N  N   . SER   A 1 480 ? -2.227  -8.595  17.47  1    25.321  ? 516 SER   A N   1 
ATOM   3879 C  CA  . SER   A 1 480 ? -3.042  -7.934  16.452 1    26.733  ? 516 SER   A CA  1 
ATOM   3880 C  C   . SER   A 1 480 ? -2.845  -6.426  16.54  1    23.533  ? 516 SER   A C   1 
ATOM   3881 O  O   . SER   A 1 480 ? -3.55   -5.727  15.85  1    22.026  ? 516 SER   A O   1 
ATOM   3882 C  CB  . SER   A 1 480 ? -4.518  -8.212  16.608 1    26.198  ? 516 SER   A CB  1 
ATOM   3883 O  OG  . SER   A 1 480 ? -4.762  -9.587  16.44  1    37.659  ? 516 SER   A OG  1 
ATOM   3884 N  N   . SER   A 1 481 ? -2.101  -5.955  17.554 1    22.965  ? 517 SER   A N   1 
ATOM   3885 C  CA  . SER   A 1 481 ? -1.814  -4.539  17.692 1    25.86   ? 517 SER   A CA  1 
ATOM   3886 C  C   . SER   A 1 481 ? -3.123  -3.739  17.787 1    23.478  ? 517 SER   A C   1 
ATOM   3887 O  O   . SER   A 1 481 ? -3.353  -2.791  17.082 1    21.07   ? 517 SER   A O   1 
ATOM   3888 C  CB  . SER   A 1 481 ? -0.975  -4.117  16.525 1    24.584  ? 517 SER   A CB  1 
ATOM   3889 O  OG  . SER   A 1 481 ? -0.332  -2.876  16.74  1    28.569  ? 517 SER   A OG  1 
ATOM   3890 N  N   . VAL   A 1 482 ? -4      -4.105  18.701 1    23.414  ? 518 VAL   A N   1 
ATOM   3891 C  CA  . VAL   A 1 482 ? -5.218  -3.347  18.894 1    21.39   ? 518 VAL   A CA  1 
ATOM   3892 C  C   . VAL   A 1 482 ? -5.129  -2.712  20.275 1    21.355  ? 518 VAL   A C   1 
ATOM   3893 O  O   . VAL   A 1 482 ? -4.807  -3.403  21.218 1    18.171  ? 518 VAL   A O   1 
ATOM   3894 C  CB  . VAL   A 1 482 ? -6.462  -4.238  18.83  1    22.24   ? 518 VAL   A CB  1 
ATOM   3895 C  CG1 . VAL   A 1 482 ? -7.678  -3.408  19.288 1    22.611  ? 518 VAL   A CG1 1 
ATOM   3896 C  CG2 . VAL   A 1 482 ? -6.639  -4.751  17.403 1    20.482  ? 518 VAL   A CG2 1 
ATOM   3897 N  N   . PRO   A 1 483 ? -5.29   -1.377  20.419 1    21.257  ? 519 PRO   A N   1 
ATOM   3898 C  CA  . PRO   A 1 483 ? -5.119  -0.74   21.735 1    20.381  ? 519 PRO   A CA  1 
ATOM   3899 C  C   . PRO   A 1 483 ? -6.166  -1.23   22.737 1    20.15   ? 519 PRO   A C   1 
ATOM   3900 O  O   . PRO   A 1 483 ? -7.236  -1.661  22.366 1    19.413  ? 519 PRO   A O   1 
ATOM   3901 C  CB  . PRO   A 1 483 ? -5.18   0.749   21.424 1    19.516  ? 519 PRO   A CB  1 
ATOM   3902 C  CG  . PRO   A 1 483 ? -4.81   0.85    19.922 1    20.118  ? 519 PRO   A CG  1 
ATOM   3903 C  CD  . PRO   A 1 483 ? -5.371  -0.43   19.289 1    19.581  ? 519 PRO   A CD  1 
ATOM   3904 N  N   . TYR   A 1 484 ? -5.819  -1.254  24.013 1    21.02   ? 520 TYR   A N   1 
ATOM   3905 C  CA  . TYR   A 1 484 ? -6.666  -1.934  24.968 1    22.993  ? 520 TYR   A CA  1 
ATOM   3906 C  C   . TYR   A 1 484 ? -7.302  -0.961  25.972 1    22.863  ? 520 TYR   A C   1 
ATOM   3907 O  O   . TYR   A 1 484 ? -8.256  -1.311  26.626 1    26.311  ? 520 TYR   A O   1 
ATOM   3908 C  CB  . TYR   A 1 484 ? -5.844  -3.048  25.65  1    25.41   ? 520 TYR   A CB  1 
ATOM   3909 C  CG  . TYR   A 1 484 ? -6.745  -4.197  26.078 1    23.235  ? 520 TYR   A CG  1 
ATOM   3910 C  CD1 . TYR   A 1 484 ? -7.106  -5.179  25.168 1    23.256  ? 520 TYR   A CD1 1 
ATOM   3911 C  CD2 . TYR   A 1 484 ? -7.285  -4.239  27.348 1    25.243  ? 520 TYR   A CD2 1 
ATOM   3912 C  CE1 . TYR   A 1 484 ? -8.041  -6.154  25.477 1    26.758  ? 520 TYR   A CE1 1 
ATOM   3913 C  CE2 . TYR   A 1 484 ? -8.198  -5.217  27.698 1    29.724  ? 520 TYR   A CE2 1 
ATOM   3914 C  CZ  . TYR   A 1 484 ? -8.572  -6.177  26.766 1    30.662  ? 520 TYR   A CZ  1 
ATOM   3915 O  OH  . TYR   A 1 484 ? -9.43   -7.165  27.142 1    25.066  ? 520 TYR   A OH  1 
ATOM   3916 N  N   . ILE   A 1 485 ? -6.743  0.219   26.204 1    20.854  ? 521 ILE   A N   1 
ATOM   3917 C  CA  . ILE   A 1 485 ? -7.267  1.082   27.262 1    20.436  ? 521 ILE   A CA  1 
ATOM   3918 C  C   . ILE   A 1 485 ? -8.749  1.405   26.947 1    23.954  ? 521 ILE   A C   1 
ATOM   3919 O  O   . ILE   A 1 485 ? -9.589  1.468   27.858 1    27.277  ? 521 ILE   A O   1 
ATOM   3920 C  CB  . ILE   A 1 485 ? -6.319  2.284   27.457 1    18.962  ? 521 ILE   A CB  1 
ATOM   3921 C  CG1 . ILE   A 1 485 ? -6.434  3.049   28.789 1    19.843  ? 521 ILE   A CG1 1 
ATOM   3922 C  CG2 . ILE   A 1 485 ? -6.4    3.212   26.236 1    20.489  ? 521 ILE   A CG2 1 
ATOM   3923 C  CD1 . ILE   A 1 485 ? -6.239  2.232   30.064 1    22.29   ? 521 ILE   A CD1 1 
ATOM   3924 N  N   . ARG   A 1 486 ? -9.119  1.423   25.655 1    19.245  ? 522 ARG   A N   1 
ATOM   3925 C  CA  . ARG   A 1 486 ? -10.496 1.583   25.24  1    20.177  ? 522 ARG   A CA  1 
ATOM   3926 C  C   . ARG   A 1 486 ? -11.463 0.79    26.146 1    20.736  ? 522 ARG   A C   1 
ATOM   3927 O  O   . ARG   A 1 486 ? -12.544 1.274   26.47  1    22.388  ? 522 ARG   A O   1 
ATOM   3928 C  CB  . ARG   A 1 486 ? -10.721 1.21    23.763 1    19.371  ? 522 ARG   A CB  1 
ATOM   3929 C  CG  . ARG   A 1 486 ? -10.164 -0.166  23.43  1    22.383  ? 522 ARG   A CG  1 
ATOM   3930 C  CD  . ARG   A 1 486 ? -10.213 -0.43   21.917 1    19.598  ? 522 ARG   A CD  1 
ATOM   3931 N  NE  . ARG   A 1 486 ? -9.49   0.665   21.271 1    23.259  ? 522 ARG   A NE  1 
ATOM   3932 C  CZ  . ARG   A 1 486 ? -9.178  0.815   19.959 1    19.982  ? 522 ARG   A CZ  1 
ATOM   3933 N  NH1 . ARG   A 1 486 ? -9.46   -0.175  19.124 1    14.043  ? 522 ARG   A NH1 1 
ATOM   3934 N  NH2 . ARG   A 1 486 ? -8.585  1.951   19.554 1    15.421  ? 522 ARG   A NH2 1 
ATOM   3935 N  N   . TYR   A 1 487 ? -11.111 -0.439  26.517 1    19.181  ? 523 TYR   A N   1 
ATOM   3936 C  CA  . TYR   A 1 487 ? -12.04  -1.31   27.201 1    19.71   ? 523 TYR   A CA  1 
ATOM   3937 C  C   . TYR   A 1 487 ? -12.117 -0.874  28.668 1    22.934  ? 523 TYR   A C   1 
ATOM   3938 O  O   . TYR   A 1 487 ? -13.114 -1.127  29.36  1    19.674  ? 523 TYR   A O   1 
ATOM   3939 C  CB  . TYR   A 1 487 ? -11.503 -2.749  27.091 1    20.614  ? 523 TYR   A CB  1 
ATOM   3940 C  CG  . TYR   A 1 487 ? -11.425 -3.3    25.672 1    18.797  ? 523 TYR   A CG  1 
ATOM   3941 C  CD1 . TYR   A 1 487 ? -12.604 -3.547  24.965 1    21.228  ? 523 TYR   A CD1 1 
ATOM   3942 C  CD2 . TYR   A 1 487 ? -10.209 -3.513  25.018 1    17.81   ? 523 TYR   A CD2 1 
ATOM   3943 C  CE1 . TYR   A 1 487 ? -12.584 -3.99   23.655 1    19.973  ? 523 TYR   A CE1 1 
ATOM   3944 C  CE2 . TYR   A 1 487 ? -10.181 -3.967  23.7   1    18.147  ? 523 TYR   A CE2 1 
ATOM   3945 C  CZ  . TYR   A 1 487 ? -11.372 -4.183  23.026 1    16.518  ? 523 TYR   A CZ  1 
ATOM   3946 O  OH  . TYR   A 1 487 ? -11.485 -4.684  21.789 1    20.126  ? 523 TYR   A OH  1 
ATOM   3947 N  N   . PHE   A 1 488 ? -11.063 -0.203  29.164 1    19.981  ? 524 PHE   A N   1 
ATOM   3948 C  CA  . PHE   A 1 488 ? -11.159 0.268   30.537 1    21.196  ? 524 PHE   A CA  1 
ATOM   3949 C  C   . PHE   A 1 488 ? -12.168 1.436   30.568 1    28.133  ? 524 PHE   A C   1 
ATOM   3950 O  O   . PHE   A 1 488 ? -13.076 1.505   31.433 1    25.602  ? 524 PHE   A O   1 
ATOM   3951 C  CB  . PHE   A 1 488 ? -9.77   0.725   30.971 1    17.276  ? 524 PHE   A CB  1 
ATOM   3952 C  CG  . PHE   A 1 488 ? -9.754  1.394   32.333 1    15.257  ? 524 PHE   A CG  1 
ATOM   3953 C  CD1 . PHE   A 1 488 ? -9.684  0.655   33.493 1    14.809  ? 524 PHE   A CD1 1 
ATOM   3954 C  CD2 . PHE   A 1 488 ? -9.821  2.769   32.441 1    17.853  ? 524 PHE   A CD2 1 
ATOM   3955 C  CE1 . PHE   A 1 488 ? -9.65   1.275   34.726 1    16.67   ? 524 PHE   A CE1 1 
ATOM   3956 C  CE2 . PHE   A 1 488 ? -9.809  3.399   33.69  1    16.913  ? 524 PHE   A CE2 1 
ATOM   3957 C  CZ  . PHE   A 1 488 ? -9.706  2.659   34.827 1    15.838  ? 524 PHE   A CZ  1 
ATOM   3958 N  N   . VAL   A 1 489 ? -12.037 2.336   29.566 1    26.41   ? 525 VAL   A N   1 
ATOM   3959 C  CA  . VAL   A 1 489 ? -12.884 3.519   29.462 1    24.008  ? 525 VAL   A CA  1 
ATOM   3960 C  C   . VAL   A 1 489 ? -14.332 3.023   29.312 1    26.587  ? 525 VAL   A C   1 
ATOM   3961 O  O   . VAL   A 1 489 ? -15.207 3.401   30.11  1    24.365  ? 525 VAL   A O   1 
ATOM   3962 C  CB  . VAL   A 1 489 ? -12.397 4.438   28.321 1    21.574  ? 525 VAL   A CB  1 
ATOM   3963 C  CG1 . VAL   A 1 489 ? -13.325 5.635   28.082 1    17.424  ? 525 VAL   A CG1 1 
ATOM   3964 C  CG2 . VAL   A 1 489 ? -10.927 4.866   28.502 1    17.081  ? 525 VAL   A CG2 1 
ATOM   3965 N  N   . SER   A 1 490 ? -14.515 2.052   28.406 1    20.448  ? 526 SER   A N   1 
ATOM   3966 C  CA  . SER   A 1 490 ? -15.802 1.4     28.209 1    25.15   ? 526 SER   A CA  1 
ATOM   3967 C  C   . SER   A 1 490 ? -16.486 0.978   29.53  1    23.405  ? 526 SER   A C   1 
ATOM   3968 O  O   . SER   A 1 490 ? -17.64  1.251   29.751 1    21.272  ? 526 SER   A O   1 
ATOM   3969 C  CB  . SER   A 1 490 ? -15.64  0.21    27.308 1    23.91   ? 526 SER   A CB  1 
ATOM   3970 O  OG  . SER   A 1 490 ? -16.955 -0.248  27.073 1    34.017  ? 526 SER   A OG  1 
ATOM   3971 N  N   . PHE   A 1 491 ? -15.808 0.203   30.363 1    24.12   ? 527 PHE   A N   1 
ATOM   3972 C  CA  . PHE   A 1 491 ? -16.365 -0.388  31.568 1    24.693  ? 527 PHE   A CA  1 
ATOM   3973 C  C   . PHE   A 1 491 ? -16.809 0.688   32.548 1    23.19   ? 527 PHE   A C   1 
ATOM   3974 O  O   . PHE   A 1 491 ? -17.878 0.531   33.128 1    26.44   ? 527 PHE   A O   1 
ATOM   3975 C  CB  . PHE   A 1 491 ? -15.478 -1.5    32.156 1    24.504  ? 527 PHE   A CB  1 
ATOM   3976 C  CG  . PHE   A 1 491 ? -15.736 -2.852  31.501 1    24.005  ? 527 PHE   A CG  1 
ATOM   3977 C  CD1 . PHE   A 1 491 ? -15.762 -2.967  30.104 1    27.171  ? 527 PHE   A CD1 1 
ATOM   3978 C  CD2 . PHE   A 1 491 ? -15.97  -3.988  32.269 1    24.656  ? 527 PHE   A CD2 1 
ATOM   3979 C  CE1 . PHE   A 1 491 ? -16.009 -4.199  29.488 1    29.438  ? 527 PHE   A CE1 1 
ATOM   3980 C  CE2 . PHE   A 1 491 ? -16.252 -5.219  31.668 1    31.493  ? 527 PHE   A CE2 1 
ATOM   3981 C  CZ  . PHE   A 1 491 ? -16.281 -5.323  30.272 1    31.044  ? 527 PHE   A CZ  1 
ATOM   3982 N  N   . ILE   A 1 492 ? -16.046 1.799   32.668 1    27.832  ? 528 ILE   A N   1 
ATOM   3983 C  CA  . ILE   A 1 492 ? -16.515 2.942   33.451 1    26.894  ? 528 ILE   A CA  1 
ATOM   3984 C  C   . ILE   A 1 492 ? -17.721 3.638   32.809 1    28.205  ? 528 ILE   A C   1 
ATOM   3985 O  O   . ILE   A 1 492 ? -18.725 3.862   33.48  1    28.22   ? 528 ILE   A O   1 
ATOM   3986 C  CB  . ILE   A 1 492 ? -15.379 3.9     33.817 1    32.172  ? 528 ILE   A CB  1 
ATOM   3987 C  CG1 . ILE   A 1 492 ? -14.522 3.279   34.876 1    33.046  ? 528 ILE   A CG1 1 
ATOM   3988 C  CG2 . ILE   A 1 492 ? -15.884 5.281   34.271 1    32.31   ? 528 ILE   A CG2 1 
ATOM   3989 C  CD1 . ILE   A 1 492 ? -13.327 2.618   34.266 1    43.551  ? 528 ILE   A CD1 1 
ATOM   3990 N  N   . ILE   A 1 493 ? -17.662 3.93    31.505 1    25.988  ? 529 ILE   A N   1 
ATOM   3991 C  CA  . ILE   A 1 493 ? -18.594 4.908   30.964 1    25.699  ? 529 ILE   A CA  1 
ATOM   3992 C  C   . ILE   A 1 493 ? -19.928 4.228   30.631 1    27.479  ? 529 ILE   A C   1 
ATOM   3993 O  O   . ILE   A 1 493 ? -20.963 4.901   30.501 1    30.842  ? 529 ILE   A O   1 
ATOM   3994 C  CB  . ILE   A 1 493 ? -18.014 5.676   29.75  1    27.581  ? 529 ILE   A CB  1 
ATOM   3995 C  CG1 . ILE   A 1 493 ? -17.8   4.773   28.526 1    20.534  ? 529 ILE   A CG1 1 
ATOM   3996 C  CG2 . ILE   A 1 493 ? -16.764 6.508   30.111 1    23.216  ? 529 ILE   A CG2 1 
ATOM   3997 C  CD1 . ILE   A 1 493 ? -17.316 5.596   27.346 1    26.639  ? 529 ILE   A CD1 1 
ATOM   3998 N  N   . GLN   A 1 494 ? -19.889 2.903   30.462 1    22.046  ? 530 GLN   A N   1 
ATOM   3999 C  CA  . GLN   A 1 494 ? -21.096 2.151   30.179 1    28.277  ? 530 GLN   A CA  1 
ATOM   4000 C  C   . GLN   A 1 494 ? -22.076 2.247   31.371 1    30.633  ? 530 GLN   A C   1 
ATOM   4001 O  O   . GLN   A 1 494 ? -23.274 2.419   31.145 1    25.875  ? 530 GLN   A O   1 
ATOM   4002 C  CB  . GLN   A 1 494 ? -20.707 0.741   29.718 1    28.714  ? 530 GLN   A CB  1 
ATOM   4003 C  CG  . GLN   A 1 494 ? -20.267 -0.211  30.838 1    32.079  ? 530 GLN   A CG  1 
ATOM   4004 C  CD  . GLN   A 1 494 ? -19.917 -1.608  30.34  1    33.857  ? 530 GLN   A CD  1 
ATOM   4005 O  OE1 . GLN   A 1 494 ? -20.46  -2.615  30.829 1    25.203  ? 530 GLN   A OE1 1 
ATOM   4006 N  NE2 . GLN   A 1 494 ? -19.051 -1.686  29.325 1    27.959  ? 530 GLN   A NE2 1 
ATOM   4007 N  N   . PHE   A 1 495 ? -21.566 2.197   32.622 1    24.34   ? 531 PHE   A N   1 
ATOM   4008 C  CA  . PHE   A 1 495 ? -22.379 2.46    33.792 1    25.35   ? 531 PHE   A CA  1 
ATOM   4009 C  C   . PHE   A 1 495 ? -22.937 3.889   33.751 1    29.864  ? 531 PHE   A C   1 
ATOM   4010 O  O   . PHE   A 1 495 ? -24.137 4.113   33.971 1    25.613  ? 531 PHE   A O   1 
ATOM   4011 C  CB  . PHE   A 1 495 ? -21.555 2.142   35.05  1    23.273  ? 531 PHE   A CB  1 
ATOM   4012 C  CG  . PHE   A 1 495 ? -21.43  0.627   35.134 1    27.401  ? 531 PHE   A CG  1 
ATOM   4013 C  CD1 . PHE   A 1 495 ? -22.493 -0.153  35.609 1    25.942  ? 531 PHE   A CD1 1 
ATOM   4014 C  CD2 . PHE   A 1 495 ? -20.292 -0.032  34.657 1    29.474  ? 531 PHE   A CD2 1 
ATOM   4015 C  CE1 . PHE   A 1 495 ? -22.442 -1.552  35.617 1    27.911  ? 531 PHE   A CE1 1 
ATOM   4016 C  CE2 . PHE   A 1 495 ? -20.252 -1.437  34.645 1    30.013  ? 531 PHE   A CE2 1 
ATOM   4017 C  CZ  . PHE   A 1 495 ? -21.319 -2.192  35.139 1    29.064  ? 531 PHE   A CZ  1 
ATOM   4018 N  N   . GLN   A 1 496 ? -22.063 4.871   33.5   1    21.388  ? 532 GLN   A N   1 
ATOM   4019 C  CA  . GLN   A 1 496 ? -22.602 6.206   33.451 1    21.403  ? 532 GLN   A CA  1 
ATOM   4020 C  C   . GLN   A 1 496 ? -23.692 6.276   32.407 1    21.18   ? 532 GLN   A C   1 
ATOM   4021 O  O   . GLN   A 1 496 ? -24.662 6.985   32.606 1    26.776  ? 532 GLN   A O   1 
ATOM   4022 C  CB  . GLN   A 1 496 ? -21.576 7.194   32.888 1    26.075  ? 532 GLN   A CB  1 
ATOM   4023 C  CG  . GLN   A 1 496 ? -20.488 7.507   33.915 1    30.476  ? 532 GLN   A CG  1 
ATOM   4024 C  CD  . GLN   A 1 496 ? -19.427 8.465   33.449 1    28.304  ? 532 GLN   A CD  1 
ATOM   4025 O  OE1 . GLN   A 1 496 ? -18.384 8.005   32.993 1    30.726  ? 532 GLN   A OE1 1 
ATOM   4026 N  NE2 . GLN   A 1 496 ? -19.639 9.768   33.652 1    25.998  ? 532 GLN   A NE2 1 
ATOM   4027 N  N   . PHE   A 1 497 ? -23.503 5.639   31.261 1    20.66   ? 533 PHE   A N   1 
ATOM   4028 C  CA  . PHE   A 1 497 ? -24.517 5.791   30.238 1    22.785  ? 533 PHE   A CA  1 
ATOM   4029 C  C   . PHE   A 1 497 ? -25.806 5.109   30.701 1    25.245  ? 533 PHE   A C   1 
ATOM   4030 O  O   . PHE   A 1 497 ? -26.907 5.544   30.386 1    25.764  ? 533 PHE   A O   1 
ATOM   4031 C  CB  . PHE   A 1 497 ? -24.19  5.183   28.871 1    22.187  ? 533 PHE   A CB  1 
ATOM   4032 C  CG  . PHE   A 1 497 ? -22.981 5.766   28.184 1    25.168  ? 533 PHE   A CG  1 
ATOM   4033 C  CD1 . PHE   A 1 497 ? -22.493 7.002   28.555 1    25.166  ? 533 PHE   A CD1 1 
ATOM   4034 C  CD2 . PHE   A 1 497 ? -22.37  5.084   27.136 1    24.243  ? 533 PHE   A CD2 1 
ATOM   4035 C  CE1 . PHE   A 1 497 ? -21.451 7.592   27.844 1    29.969  ? 533 PHE   A CE1 1 
ATOM   4036 C  CE2 . PHE   A 1 497 ? -21.327 5.66    26.431 1    28.799  ? 533 PHE   A CE2 1 
ATOM   4037 C  CZ  . PHE   A 1 497 ? -20.851 6.915   26.8   1    31.256  ? 533 PHE   A CZ  1 
ATOM   4038 N  N   . HIS   A 1 498 ? -25.646 3.945   31.316 1    26.286  ? 534 HIS   A N   1 
ATOM   4039 C  CA  . HIS   A 1 498 ? -26.754 3.113   31.736 1    28.143  ? 534 HIS   A CA  1 
ATOM   4040 C  C   . HIS   A 1 498 ? -27.558 3.862   32.789 1    26.615  ? 534 HIS   A C   1 
ATOM   4041 O  O   . HIS   A 1 498 ? -28.783 3.972   32.692 1    27.31   ? 534 HIS   A O   1 
ATOM   4042 C  CB  . HIS   A 1 498 ? -26.21  1.825   32.344 1    24.702  ? 534 HIS   A CB  1 
ATOM   4043 C  CG  . HIS   A 1 498 ? -27.243 0.962   32.93  1    29.878  ? 534 HIS   A CG  1 
ATOM   4044 N  ND1 . HIS   A 1 498 ? -28.122 0.278   32.114 1    26.798  ? 534 HIS   A ND1 1 
ATOM   4045 C  CD2 . HIS   A 1 498 ? -27.514 0.591   34.244 1    29.512  ? 534 HIS   A CD2 1 
ATOM   4046 C  CE1 . HIS   A 1 498 ? -28.879 -0.505  32.905 1    28.466  ? 534 HIS   A CE1 1 
ATOM   4047 N  NE2 . HIS   A 1 498 ? -28.532 -0.316  34.19  1    29.696  ? 534 HIS   A NE2 1 
ATOM   4048 N  N   . GLU   A 1 499 ? -26.826 4.523   33.679 1    26.656  ? 535 GLU   A N   1 
ATOM   4049 C  CA  . GLU   A 1 499 ? -27.444 5.334   34.715 1    29.427  ? 535 GLU   A CA  1 
ATOM   4050 C  C   . GLU   A 1 499 ? -28.295 6.449   34.112 1    33.926  ? 535 GLU   A C   1 
ATOM   4051 O  O   . GLU   A 1 499 ? -29.398 6.688   34.611 1    34.893  ? 535 GLU   A O   1 
ATOM   4052 C  CB  . GLU   A 1 499 ? -26.427 5.984   35.645 1    29.561  ? 535 GLU   A CB  1 
ATOM   4053 C  CG  . GLU   A 1 499 ? -27.099 6.771   36.769 1    35.358  ? 535 GLU   A CG  1 
ATOM   4054 C  CD  . GLU   A 1 499 ? -26.059 7.544   37.548 1    36.374  ? 535 GLU   A CD  1 
ATOM   4055 O  OE1 . GLU   A 1 499 ? -25.412 8.386   36.913 1    38.239  ? 535 GLU   A OE1 1 
ATOM   4056 O  OE2 . GLU   A 1 499 ? -25.845 7.268   38.755 1    44.141  ? 535 GLU   A OE2 1 
ATOM   4057 N  N   . ALA   A 1 500 ? -27.762 7.114   33.069 1    32.629  ? 536 ALA   A N   1 
ATOM   4058 C  CA  . ALA   A 1 500 ? -28.445 8.219   32.408 1    33.114  ? 536 ALA   A CA  1 
ATOM   4059 C  C   . ALA   A 1 500 ? -29.629 7.707   31.602 1    32.378  ? 536 ALA   A C   1 
ATOM   4060 O  O   . ALA   A 1 500 ? -30.67  8.357   31.58  1    35.807  ? 536 ALA   A O   1 
ATOM   4061 C  CB  . ALA   A 1 500 ? -27.526 9.061   31.558 1    25.05   ? 536 ALA   A CB  1 
ATOM   4062 N  N   . LEU   A 1 501 ? -29.482 6.544   30.967 1    28.374  ? 537 LEU   A N   1 
ATOM   4063 C  CA  . LEU   A 1 501 ? -30.552 6.131   30.074 1    30.479  ? 537 LEU   A CA  1 
ATOM   4064 C  C   . LEU   A 1 501 ? -31.724 5.651   30.939 1    32.706  ? 537 LEU   A C   1 
ATOM   4065 O  O   . LEU   A 1 501 ? -32.857 5.734   30.491 1    31.763  ? 537 LEU   A O   1 
ATOM   4066 C  CB  . LEU   A 1 501 ? -30.206 5.14    28.959 1    29.757  ? 537 LEU   A CB  1 
ATOM   4067 C  CG  . LEU   A 1 501 ? -28.949 5.43    28.134 1    32.967  ? 537 LEU   A CG  1 
ATOM   4068 C  CD1 . LEU   A 1 501 ? -28.672 4.259   27.202 1    24.274  ? 537 LEU   A CD1 1 
ATOM   4069 C  CD2 . LEU   A 1 501 ? -29.115 6.714   27.343 1    33.049  ? 537 LEU   A CD2 1 
ATOM   4070 N  N   . CYS   A 1 502 ? -31.435 5.252   32.189 1    28.924  ? 538 CYS   A N   1 
ATOM   4071 C  CA  . CYS   A 1 502 ? -32.433 4.754   33.114 1    31.958  ? 538 CYS   A CA  1 
ATOM   4072 C  C   . CYS   A 1 502 ? -33.302 5.893   33.628 1    33.244  ? 538 CYS   A C   1 
ATOM   4073 O  O   . CYS   A 1 502 ? -34.53  5.79    33.634 1    39.627  ? 538 CYS   A O   1 
ATOM   4074 C  CB  . CYS   A 1 502 ? -31.794 3.961   34.234 1    32.673  ? 538 CYS   A CB  1 
ATOM   4075 S  SG  . CYS   A 1 502 ? -31.052 2.44    33.582 1    34.605  ? 538 CYS   A SG  1 
ATOM   4076 N  N   . GLN   A 1 503 ? -32.652 7       33.956 1    32.851  ? 539 GLN   A N   1 
ATOM   4077 C  CA  . GLN   A 1 503 ? -33.305 8.244   34.33  1    39.064  ? 539 GLN   A CA  1 
ATOM   4078 C  C   . GLN   A 1 503 ? -34.138 8.771   33.152 1    40.992  ? 539 GLN   A C   1 
ATOM   4079 O  O   . GLN   A 1 503 ? -35.288 9.106   33.364 1    40.175  ? 539 GLN   A O   1 
ATOM   4080 C  CB  . GLN   A 1 503 ? -32.288 9.199   34.958 1    43.199  ? 539 GLN   A CB  1 
ATOM   4081 C  CG  . GLN   A 1 503 ? -32.7   10.67   34.951 1    63.296  ? 539 GLN   A CG  1 
ATOM   4082 C  CD  . GLN   A 1 503 ? -31.493 11.586  35.01  1    92.264  ? 539 GLN   A CD  1 
ATOM   4083 O  OE1 . GLN   A 1 503 ? -30.593 11.533  34.156 1    99.828  ? 539 GLN   A OE1 1 
ATOM   4084 N  NE2 . GLN   A 1 503 ? -31.442 12.423  36.037 1    95.941  ? 539 GLN   A NE2 1 
ATOM   4085 N  N   . ALA   A 1 504 ? -33.6   8.797   31.915 1    35.608  ? 540 ALA   A N   1 
ATOM   4086 C  CA  . ALA   A 1 504 ? -34.422 9.207   30.784 1    34.728  ? 540 ALA   A CA  1 
ATOM   4087 C  C   . ALA   A 1 504 ? -35.668 8.331   30.683 1    41.46   ? 540 ALA   A C   1 
ATOM   4088 O  O   . ALA   A 1 504 ? -36.737 8.847   30.318 1    36.182  ? 540 ALA   A O   1 
ATOM   4089 C  CB  . ALA   A 1 504 ? -33.678 9.146   29.465 1    30.571  ? 540 ALA   A CB  1 
ATOM   4090 N  N   . ALA   A 1 505 ? -35.491 7.008   30.919 1    41.893  ? 541 ALA   A N   1 
ATOM   4091 C  CA  . ALA   A 1 505 ? -36.56  6.039   30.696 1    41.297  ? 541 ALA   A CA  1 
ATOM   4092 C  C   . ALA   A 1 505 ? -37.594 6.075   31.825 1    39.97   ? 541 ALA   A C   1 
ATOM   4093 O  O   . ALA   A 1 505 ? -38.546 5.318   31.783 1    41.908  ? 541 ALA   A O   1 
ATOM   4094 C  CB  . ALA   A 1 505 ? -36.009 4.645   30.507 1    33.309  ? 541 ALA   A CB  1 
ATOM   4095 N  N   . GLY   A 1 506 ? -37.391 6.93    32.837 1    44.719  ? 542 GLY   A N   1 
ATOM   4096 C  CA  . GLY   A 1 506 ? -38.264 6.98    34.014 1    45.678  ? 542 GLY   A CA  1 
ATOM   4097 C  C   . GLY   A 1 506 ? -38.063 5.852   35.046 1    49.556  ? 542 GLY   A C   1 
ATOM   4098 O  O   . GLY   A 1 506 ? -39.029 5.372   35.645 1    44.698  ? 542 GLY   A O   1 
ATOM   4099 N  N   . HIS   A 1 507 ? -36.822 5.412   35.317 1    43.947  ? 543 HIS   A N   1 
ATOM   4100 C  CA  . HIS   A 1 507 ? -36.718 4.259   36.202 1    40.199  ? 543 HIS   A CA  1 
ATOM   4101 C  C   . HIS   A 1 507 ? -36.486 4.771   37.621 1    40.704  ? 543 HIS   A C   1 
ATOM   4102 O  O   . HIS   A 1 507 ? -35.843 5.802   37.778 1    35.907  ? 543 HIS   A O   1 
ATOM   4103 C  CB  . HIS   A 1 507 ? -35.692 3.256   35.672 1    41.807  ? 543 HIS   A CB  1 
ATOM   4104 C  CG  . HIS   A 1 507 ? -35.223 2.295   36.697 1    48.502  ? 543 HIS   A CG  1 
ATOM   4105 N  ND1 . HIS   A 1 507 ? -35.856 1.087   36.94  1    48.599  ? 543 HIS   A ND1 1 
ATOM   4106 C  CD2 . HIS   A 1 507 ? -34.184 2.379   37.572 1    50.954  ? 543 HIS   A CD2 1 
ATOM   4107 C  CE1 . HIS   A 1 507 ? -35.23  0.465   37.931 1    41.042  ? 543 HIS   A CE1 1 
ATOM   4108 N  NE2 . HIS   A 1 507 ? -34.205 1.234   38.327 1    51.408  ? 543 HIS   A NE2 1 
ATOM   4109 N  N   . THR   A 1 508 ? -36.955 4.048   38.659 1    44.66   ? 544 THR   A N   1 
ATOM   4110 C  CA  . THR   A 1 508 ? -36.681 4.544   40.011 1    49.721  ? 544 THR   A CA  1 
ATOM   4111 C  C   . THR   A 1 508 ? -36.227 3.41    40.934 1    56.674  ? 544 THR   A C   1 
ATOM   4112 O  O   . THR   A 1 508 ? -36.456 2.218   40.711 1    43.352  ? 544 THR   A O   1 
ATOM   4113 C  CB  . THR   A 1 508 ? -37.859 5.304   40.629 1    61.237  ? 544 THR   A CB  1 
ATOM   4114 O  OG1 . THR   A 1 508 ? -38.89  4.324   40.743 1    61.936  ? 544 THR   A OG1 1 
ATOM   4115 C  CG2 . THR   A 1 508 ? -38.308 6.544   39.86  1    60.59   ? 544 THR   A CG2 1 
ATOM   4116 N  N   . GLY   A 1 509 ? -35.6   3.797   42.037 1    63.056  ? 545 GLY   A N   1 
ATOM   4117 C  CA  . GLY   A 1 509 ? -34.986 2.746   42.812 1    54.298  ? 545 GLY   A CA  1 
ATOM   4118 C  C   . GLY   A 1 509 ? -33.705 2.301   42.125 1    49.886  ? 545 GLY   A C   1 
ATOM   4119 O  O   . GLY   A 1 509 ? -33.188 2.981   41.232 1    43.468  ? 545 GLY   A O   1 
ATOM   4120 N  N   . PRO   A 1 510 ? -33.203 1.117   42.524 1    50.094  ? 546 PRO   A N   1 
ATOM   4121 C  CA  . PRO   A 1 510 ? -31.775 0.819   42.467 1    38.852  ? 546 PRO   A CA  1 
ATOM   4122 C  C   . PRO   A 1 510 ? -31.426 0.597   41.005 1    41.226  ? 546 PRO   A C   1 
ATOM   4123 O  O   . PRO   A 1 510 ? -32.161 -0.039  40.221 1    34.198  ? 546 PRO   A O   1 
ATOM   4124 C  CB  . PRO   A 1 510 ? -31.729 -0.469  43.264 1    37.283  ? 546 PRO   A CB  1 
ATOM   4125 C  CG  . PRO   A 1 510 ? -32.974 -0.393  44.15  1    36.5    ? 546 PRO   A CG  1 
ATOM   4126 C  CD  . PRO   A 1 510 ? -34.002 0.014   43.088 1    46.814  ? 546 PRO   A CD  1 
ATOM   4127 N  N   . LEU   A 1 511 ? -30.271 1.16    40.669 1    34.457  ? 547 LEU   A N   1 
ATOM   4128 C  CA  . LEU   A 1 511 ? -29.848 1.29    39.287 1    34.225  ? 547 LEU   A CA  1 
ATOM   4129 C  C   . LEU   A 1 511 ? -29.759 -0.095  38.641 1    33.907  ? 547 LEU   A C   1 
ATOM   4130 O  O   . LEU   A 1 511 ? -29.966 -0.242  37.452 1    34.73   ? 547 LEU   A O   1 
ATOM   4131 C  CB  . LEU   A 1 511 ? -28.5   2.03    39.298 1    28.175  ? 547 LEU   A CB  1 
ATOM   4132 C  CG  . LEU   A 1 511 ? -27.85  2.007   37.925 1    32.261  ? 547 LEU   A CG  1 
ATOM   4133 C  CD1 . LEU   A 1 511 ? -28.987 2.551   37.01  1    31.584  ? 547 LEU   A CD1 1 
ATOM   4134 C  CD2 . LEU   A 1 511 ? -26.532 2.783   37.821 1    28.045  ? 547 LEU   A CD2 1 
ATOM   4135 N  N   . HIS   A 1 512 ? -29.412 -1.12   39.43  1    38.211  ? 548 HIS   A N   1 
ATOM   4136 C  CA  . HIS   A 1 512 ? -29.192 -2.451  38.888 1    32.728  ? 548 HIS   A CA  1 
ATOM   4137 C  C   . HIS   A 1 512 ? -30.504 -3.161  38.581 1    35.731  ? 548 HIS   A C   1 
ATOM   4138 O  O   . HIS   A 1 512 ? -30.458 -4.281  38.116 1    34.987  ? 548 HIS   A O   1 
ATOM   4139 C  CB  . HIS   A 1 512 ? -28.411 -3.329  39.868 1    34.255  ? 548 HIS   A CB  1 
ATOM   4140 C  CG  . HIS   A 1 512 ? -29.209 -3.797  41.046 1    32.33   ? 548 HIS   A CG  1 
ATOM   4141 N  ND1 . HIS   A 1 512 ? -29.31  -3.056  42.212 1    35.879  ? 548 HIS   A ND1 1 
ATOM   4142 C  CD2 . HIS   A 1 512 ? -29.906 -4.954  41.26  1    27.746  ? 548 HIS   A CD2 1 
ATOM   4143 C  CE1 . HIS   A 1 512 ? -30.062 -3.727  43.101 1    34.404  ? 548 HIS   A CE1 1 
ATOM   4144 N  NE2 . HIS   A 1 512 ? -30.44  -4.881  42.541 1    32.317  ? 548 HIS   A NE2 1 
ATOM   4145 N  N   . LYS   A 1 513 ? -31.654 -2.523  38.828 1    44.615  ? 549 LYS   A N   1 
ATOM   4146 C  CA  . LYS   A 1 513 ? -32.915 -3.152  38.478 1    48.541  ? 549 LYS   A CA  1 
ATOM   4147 C  C   . LYS   A 1 513 ? -33.319 -2.618  37.11  1    38.838  ? 549 LYS   A C   1 
ATOM   4148 O  O   . LYS   A 1 513 ? -34.236 -3.13   36.466 1    31.503  ? 549 LYS   A O   1 
ATOM   4149 C  CB  . LYS   A 1 513 ? -33.99  -2.946  39.557 1    51.619  ? 549 LYS   A CB  1 
ATOM   4150 C  CG  . LYS   A 1 513 ? -33.69  -3.594  40.917 1    62.581  ? 549 LYS   A CG  1 
ATOM   4151 C  CD  . LYS   A 1 513 ? -33.451 -5.102  40.858 1    78.916  ? 549 LYS   A CD  1 
ATOM   4152 C  CE  . LYS   A 1 513 ? -34.632 -6.035  40.726 1    76.672  ? 549 LYS   A CE  1 
ATOM   4153 N  NZ  . LYS   A 1 513 ? -35.087 -6.49   42.04  1    74.025  ? 549 LYS   A NZ  1 
ATOM   4154 N  N   . CYS   A 1 514 ? -32.597 -1.598  36.648 1    35.826  ? 550 CYS   A N   1 
ATOM   4155 C  CA  . CYS   A 1 514 ? -33.052 -0.95   35.424 1    36.917  ? 550 CYS   A CA  1 
ATOM   4156 C  C   . CYS   A 1 514 ? -32.976 -1.885  34.214 1    36.376  ? 550 CYS   A C   1 
ATOM   4157 O  O   . CYS   A 1 514 ? -32.01  -2.64   34.033 1    40.245  ? 550 CYS   A O   1 
ATOM   4158 C  CB  . CYS   A 1 514 ? -32.491 0.453   35.253 1    32.985  ? 550 CYS   A CB  1 
ATOM   4159 S  SG  . CYS   A 1 514 ? -32.578 1.055   33.536 1    40.12   ? 550 CYS   A SG  1 
ATOM   4160 N  N   . ASP   A 1 515 ? -34.032 -1.812  33.399 1    26.603  ? 551 ASP   A N   1 
ATOM   4161 C  CA  . ASP   A 1 515 ? -34.113 -2.472  32.111 1    26.182  ? 551 ASP   A CA  1 
ATOM   4162 C  C   . ASP   A 1 515 ? -34.688 -1.46   31.122 1    30.55   ? 551 ASP   A C   1 
ATOM   4163 O  O   . ASP   A 1 515 ? -35.862 -1.073  31.215 1    27.451  ? 551 ASP   A O   1 
ATOM   4164 C  CB  . ASP   A 1 515 ? -34.883 -3.794  32.124 1    21.912  ? 551 ASP   A CB  1 
ATOM   4165 C  CG  . ASP   A 1 515 ? -35.038 -4.39   30.727 1    29.753  ? 551 ASP   A CG  1 
ATOM   4166 O  OD1 . ASP   A 1 515 ? -34.649 -3.682  29.758 1    30.593  ? 551 ASP   A OD1 1 
ATOM   4167 O  OD2 . ASP   A 1 515 ? -35.572 -5.54   30.571 1    32.635  ? 551 ASP   A OD2 1 
ATOM   4168 N  N   . ILE   A 1 516 ? -33.871 -1.063  30.14  1    25.799  ? 552 ILE   A N   1 
ATOM   4169 C  CA  . ILE   A 1 516 ? -34.273 0.065   29.313 1    27.09   ? 552 ILE   A CA  1 
ATOM   4170 C  C   . ILE   A 1 516 ? -34.914 -0.469  28.039 1    27.61   ? 552 ILE   A C   1 
ATOM   4171 O  O   . ILE   A 1 516 ? -34.976 0.243   27.051 1    33.011  ? 552 ILE   A O   1 
ATOM   4172 C  CB  . ILE   A 1 516 ? -33.073 0.97    28.933 1    28.242  ? 552 ILE   A CB  1 
ATOM   4173 C  CG1 . ILE   A 1 516 ? -32.13  0.26    27.955 1    21.565  ? 552 ILE   A CG1 1 
ATOM   4174 C  CG2 . ILE   A 1 516 ? -32.366 1.54    30.172 1    23.101  ? 552 ILE   A CG2 1 
ATOM   4175 C  CD1 . ILE   A 1 516 ? -31.106 1.185   27.373 1    29.848  ? 552 ILE   A CD1 1 
ATOM   4176 N  N   . TYR   A 1 517 ? -35.31  -1.735  28.022 1    26.647  ? 553 TYR   A N   1 
ATOM   4177 C  CA  . TYR   A 1 517 ? -35.921 -2.272  26.822 1    28.956  ? 553 TYR   A CA  1 
ATOM   4178 C  C   . TYR   A 1 517 ? -37.108 -1.386  26.425 1    29.123  ? 553 TYR   A C   1 
ATOM   4179 O  O   . TYR   A 1 517 ? -37.969 -1.099  27.251 1    34.841  ? 553 TYR   A O   1 
ATOM   4180 C  CB  . TYR   A 1 517 ? -36.296 -3.736  27.11  1    29.702  ? 553 TYR   A CB  1 
ATOM   4181 C  CG  . TYR   A 1 517 ? -36.934 -4.373  25.882 1    34.882  ? 553 TYR   A CG  1 
ATOM   4182 C  CD1 . TYR   A 1 517 ? -36.137 -4.754  24.807 1    33.263  ? 553 TYR   A CD1 1 
ATOM   4183 C  CD2 . TYR   A 1 517 ? -38.316 -4.536  25.767 1    32.459  ? 553 TYR   A CD2 1 
ATOM   4184 C  CE1 . TYR   A 1 517 ? -36.677 -5.332  23.678 1    34.144  ? 553 TYR   A CE1 1 
ATOM   4185 C  CE2 . TYR   A 1 517 ? -38.873 -5.07   24.614 1    34.188  ? 553 TYR   A CE2 1 
ATOM   4186 C  CZ  . TYR   A 1 517 ? -38.05  -5.461  23.561 1    34.718  ? 553 TYR   A CZ  1 
ATOM   4187 O  OH  . TYR   A 1 517 ? -38.511 -6.052  22.407 1    28.404  ? 553 TYR   A OH  1 
ATOM   4188 N  N   . GLN   A 1 518 ? -37.132 -0.961  25.15  1    31.159  ? 554 GLN   A N   1 
ATOM   4189 C  CA  . GLN   A 1 518 ? -38.22  -0.262  24.479 1    27.368  ? 554 GLN   A CA  1 
ATOM   4190 C  C   . GLN   A 1 518 ? -38.279 1.216   24.868 1    26.366  ? 554 GLN   A C   1 
ATOM   4191 O  O   . GLN   A 1 518 ? -39.211 1.913   24.473 1    31.232  ? 554 GLN   A O   1 
ATOM   4192 C  CB  . GLN   A 1 518 ? -39.618 -0.888  24.633 1    34.103  ? 554 GLN   A CB  1 
ATOM   4193 C  CG  . GLN   A 1 518 ? -40.522 -0.8    23.4   1    38.385  ? 554 GLN   A CG  1 
ATOM   4194 C  CD  . GLN   A 1 518 ? -41.912 -1.405  23.577 1    41.738  ? 554 GLN   A CD  1 
ATOM   4195 O  OE1 . GLN   A 1 518 ? -42.11  -2.63   23.595 1    42.993  ? 554 GLN   A OE1 1 
ATOM   4196 N  NE2 . GLN   A 1 518 ? -42.918 -0.541  23.605 1    29.925  ? 554 GLN   A NE2 1 
ATOM   4197 N  N   . SER   A 1 519 ? -37.352 1.726   25.683 1    22.404  ? 555 SER   A N   1 
ATOM   4198 C  CA  . SER   A 1 519 ? -37.321 3.179   25.885 1    24.717  ? 555 SER   A CA  1 
ATOM   4199 C  C   . SER   A 1 519 ? -36.879 3.945   24.625 1    27.313  ? 555 SER   A C   1 
ATOM   4200 O  O   . SER   A 1 519 ? -35.737 3.861   24.182 1    30.326  ? 555 SER   A O   1 
ATOM   4201 C  CB  . SER   A 1 519 ? -36.444 3.526   27.034 1    24.984  ? 555 SER   A CB  1 
ATOM   4202 O  OG  . SER   A 1 519 ? -36.494 4.916   27.241 1    32.663  ? 555 SER   A OG  1 
ATOM   4203 N  N   . LYS   A 1 520 ? -37.796 4.7     24.023 1    31.304  ? 556 LYS   A N   1 
ATOM   4204 C  CA  . LYS   A 1 520 ? -37.499 5.605   22.922 1    33.455  ? 556 LYS   A CA  1 
ATOM   4205 C  C   . LYS   A 1 520 ? -36.733 6.818   23.441 1    30.157  ? 556 LYS   A C   1 
ATOM   4206 O  O   . LYS   A 1 520 ? -36.012 7.422   22.676 1    29.09   ? 556 LYS   A O   1 
ATOM   4207 C  CB  . LYS   A 1 520 ? -38.704 6.147   22.127 1    33.336  ? 556 LYS   A CB  1 
ATOM   4208 C  CG  . LYS   A 1 520 ? -39.611 5.051   21.528 1    39.944  ? 556 LYS   A CG  1 
ATOM   4209 C  CD  . LYS   A 1 520 ? -38.954 3.942   20.691 1    38.115  ? 556 LYS   A CD  1 
ATOM   4210 C  CE  . LYS   A 1 520 ? -39.894 2.962   19.985 1    33.381  ? 556 LYS   A CE  1 
ATOM   4211 N  NZ  . LYS   A 1 520 ? -40.154 1.661   20.622 1    32.813  ? 556 LYS   A NZ  1 
ATOM   4212 N  N   . GLU   A 1 521 ? -36.867 7.171   24.727 1    29.749  ? 557 GLU   A N   1 
ATOM   4213 C  CA  . GLU   A 1 521 ? -36.103 8.287   25.267 1    31.681  ? 557 GLU   A CA  1 
ATOM   4214 C  C   . GLU   A 1 521 ? -34.614 7.944   25.307 1    33.923  ? 557 GLU   A C   1 
ATOM   4215 O  O   . GLU   A 1 521 ? -33.775 8.802   24.99  1    29.154  ? 557 GLU   A O   1 
ATOM   4216 C  CB  . GLU   A 1 521 ? -36.591 8.826   26.608 1    40.135  ? 557 GLU   A CB  1 
ATOM   4217 C  CG  . GLU   A 1 521 ? -37.959 9.511   26.516 1    50.785  ? 557 GLU   A CG  1 
ATOM   4218 C  CD  . GLU   A 1 521 ? -39.155 8.584   26.308 1    56.343  ? 557 GLU   A CD  1 
ATOM   4219 O  OE1 . GLU   A 1 521 ? -39.057 7.314   26.232 1    50.103  ? 557 GLU   A OE1 1 
ATOM   4220 O  OE2 . GLU   A 1 521 ? -40.242 9.186   26.222 1    59.562  ? 557 GLU   A OE2 1 
ATOM   4221 N  N   . ALA   A 1 522 ? -34.332 6.687   25.683 1    32.174  ? 558 ALA   A N   1 
ATOM   4222 C  CA  . ALA   A 1 522 ? -32.977 6.182   25.767 1    32.385  ? 558 ALA   A CA  1 
ATOM   4223 C  C   . ALA   A 1 522 ? -32.401 6.047   24.363 1    31.688  ? 558 ALA   A C   1 
ATOM   4224 O  O   . ALA   A 1 522 ? -31.309 6.539   24.12  1    31.85   ? 558 ALA   A O   1 
ATOM   4225 C  CB  . ALA   A 1 522 ? -32.917 4.913   26.543 1    30.477  ? 558 ALA   A CB  1 
ATOM   4226 N  N   . GLY   A 1 523 ? -33.17  5.539   23.404 1    25.388  ? 559 GLY   A N   1 
ATOM   4227 C  CA  . GLY   A 1 523 ? -32.61  5.48    22.054 1    25.113  ? 559 GLY   A CA  1 
ATOM   4228 C  C   . GLY   A 1 523 ? -32.126 6.834   21.525 1    29.741  ? 559 GLY   A C   1 
ATOM   4229 O  O   . GLY   A 1 523 ? -30.982 7       21.077 1    30.735  ? 559 GLY   A O   1 
ATOM   4230 N  N   . GLN   A 1 524 ? -32.968 7.847   21.697 1    32.215  ? 560 GLN   A N   1 
ATOM   4231 C  CA  . GLN   A 1 524 ? -32.688 9.213   21.279 1    35.422  ? 560 GLN   A CA  1 
ATOM   4232 C  C   . GLN   A 1 524 ? -31.357 9.747   21.861 1    35.163  ? 560 GLN   A C   1 
ATOM   4233 O  O   . GLN   A 1 524 ? -30.577 10.382  21.17  1    37.532  ? 560 GLN   A O   1 
ATOM   4234 C  CB  . GLN   A 1 524 ? -33.979 9.977   21.627 1    39.553  ? 560 GLN   A CB  1 
ATOM   4235 C  CG  . GLN   A 1 524 ? -34.108 11.364  21.006 1    51.062  ? 560 GLN   A CG  1 
ATOM   4236 C  CD  . GLN   A 1 524 ? -34.043 11.342  19.484 1    66.18   ? 560 GLN   A CD  1 
ATOM   4237 O  OE1 . GLN   A 1 524 ? -32.965 11.253  18.866 1    57.976  ? 560 GLN   A OE1 1 
ATOM   4238 N  NE2 . GLN   A 1 524 ? -35.215 11.442  18.864 1    63.911  ? 560 GLN   A NE2 1 
ATOM   4239 N  N   . ARG   A 1 525 ? -31.076 9.544   23.147 1    32.399  ? 561 ARG   A N   1 
ATOM   4240 C  CA  . ARG   A 1 525 ? -29.829 10.042  23.707 1    37.589  ? 561 ARG   A CA  1 
ATOM   4241 C  C   . ARG   A 1 525 ? -28.646 9.404   22.977 1    36.161  ? 561 ARG   A C   1 
ATOM   4242 O  O   . ARG   A 1 525 ? -27.699 10.07   22.547 1    31.355  ? 561 ARG   A O   1 
ATOM   4243 C  CB  . ARG   A 1 525 ? -29.752 9.559   25.161 1    41.407  ? 561 ARG   A CB  1 
ATOM   4244 C  CG  . ARG   A 1 525 ? -30.74  10.287  26.058 1    37.171  ? 561 ARG   A CG  1 
ATOM   4245 C  CD  . ARG   A 1 525 ? -30.166 11.63   26.46  1    38.324  ? 561 ARG   A CD  1 
ATOM   4246 N  NE  . ARG   A 1 525 ? -31.05  12.189  27.483 1    45.368  ? 561 ARG   A NE  1 
ATOM   4247 C  CZ  . ARG   A 1 525 ? -30.987 12.157  28.802 1    43.33   ? 561 ARG   A CZ  1 
ATOM   4248 N  NH1 . ARG   A 1 525 ? -30.164 11.385  29.478 1    44.793  ? 561 ARG   A NH1 1 
ATOM   4249 N  NH2 . ARG   A 1 525 ? -31.847 12.889  29.459 1    46.149  ? 561 ARG   A NH2 1 
ATOM   4250 N  N   . LEU   A 1 526 ? -28.737 8.08    22.824 1    32.106  ? 562 LEU   A N   1 
ATOM   4251 C  CA  . LEU   A 1 526 ? -27.661 7.331   22.221 1    33.434  ? 562 LEU   A CA  1 
ATOM   4252 C  C   . LEU   A 1 526 ? -27.437 7.79    20.773 1    35.133  ? 562 LEU   A C   1 
ATOM   4253 O  O   . LEU   A 1 526 ? -26.296 8.086   20.419 1    40.266  ? 562 LEU   A O   1 
ATOM   4254 C  CB  . LEU   A 1 526 ? -27.941 5.832   22.361 1    34.601  ? 562 LEU   A CB  1 
ATOM   4255 C  CG  . LEU   A 1 526 ? -27.469 5.131   23.639 1    40.364  ? 562 LEU   A CG  1 
ATOM   4256 C  CD1 . LEU   A 1 526 ? -27.383 3.654   23.339 1    39.049  ? 562 LEU   A CD1 1 
ATOM   4257 C  CD2 . LEU   A 1 526 ? -26.068 5.633   24.054 1    45.541  ? 562 LEU   A CD2 1 
ATOM   4258 N  N   . ALA   A 1 527 ? -28.506 7.807   19.95  1    31.565  ? 563 ALA   A N   1 
ATOM   4259 C  CA  . ALA   A 1 527 ? -28.481 8.144   18.525 1    29.397  ? 563 ALA   A CA  1 
ATOM   4260 C  C   . ALA   A 1 527 ? -27.855 9.526   18.346 1    31.231  ? 563 ALA   A C   1 
ATOM   4261 O  O   . ALA   A 1 527 ? -26.972 9.696   17.503 1    30.76   ? 563 ALA   A O   1 
ATOM   4262 C  CB  . ALA   A 1 527 ? -29.905 8.144   17.905 1    24.16   ? 563 ALA   A CB  1 
ATOM   4263 N  N   . THR   A 1 528 ? -28.28  10.526  19.134 1    29.778  ? 564 THR   A N   1 
ATOM   4264 C  CA  . THR   A 1 528 ? -27.704 11.838  18.829 1    38.432  ? 564 THR   A CA  1 
ATOM   4265 C  C   . THR   A 1 528 ? -26.206 11.838  19.188 1    39.881  ? 564 THR   A C   1 
ATOM   4266 O  O   . THR   A 1 528 ? -25.408 12.355  18.421 1    41.061  ? 564 THR   A O   1 
ATOM   4267 C  CB  . THR   A 1 528 ? -28.495 13.049  19.366 1    43.633  ? 564 THR   A CB  1 
ATOM   4268 O  OG1 . THR   A 1 528 ? -28.597 12.948  20.779 1    46.703  ? 564 THR   A OG1 1 
ATOM   4269 C  CG2 . THR   A 1 528 ? -29.936 13.144  18.873 1    47.875  ? 564 THR   A CG2 1 
ATOM   4270 N  N   . ALA   A 1 529 ? -25.813 11.213  20.326 1    36.104  ? 565 ALA   A N   1 
ATOM   4271 C  CA  . ALA   A 1 529 ? -24.411 10.987  20.657 1    29.073  ? 565 ALA   A CA  1 
ATOM   4272 C  C   . ALA   A 1 529 ? -23.672 10.3    19.496 1    28.141  ? 565 ALA   A C   1 
ATOM   4273 O  O   . ALA   A 1 529 ? -22.664 10.794  18.976 1    26.998  ? 565 ALA   A O   1 
ATOM   4274 C  CB  . ALA   A 1 529 ? -24.291 10.197  21.944 1    25.537  ? 565 ALA   A CB  1 
ATOM   4275 N  N   . MET   A 1 530 ? -24.188 9.173   19.039 1    21.594  ? 566 MET   A N   1 
ATOM   4276 C  CA  . MET   A 1 530 ? -23.456 8.448   18.006 1    25.004  ? 566 MET   A CA  1 
ATOM   4277 C  C   . MET   A 1 530 ? -23.389 9.212   16.668 1    29.464  ? 566 MET   A C   1 
ATOM   4278 O  O   . MET   A 1 530 ? -22.5   8.948   15.868 1    33.051  ? 566 MET   A O   1 
ATOM   4279 C  CB  . MET   A 1 530 ? -24.1   7.067   17.796 1    24.28   ? 566 MET   A CB  1 
ATOM   4280 C  CG  . MET   A 1 530 ? -23.841 6.046   18.887 1    26.406  ? 566 MET   A CG  1 
ATOM   4281 S  SD  . MET   A 1 530 ? -24.449 4.389   18.52  1    27.887  ? 566 MET   A SD  1 
ATOM   4282 C  CE  . MET   A 1 530 ? -26.087 4.748   19.169 1    23.438  ? 566 MET   A CE  1 
ATOM   4283 N  N   . LYS   A 1 531 ? -24.341 10.106  16.353 1    31.01   ? 567 LYS   A N   1 
ATOM   4284 C  CA  . LYS   A 1 531 ? -24.341 10.765  15.046 1    31.666  ? 567 LYS   A CA  1 
ATOM   4285 C  C   . LYS   A 1 531 ? -23.146 11.716  14.914 1    31.441  ? 567 LYS   A C   1 
ATOM   4286 O  O   . LYS   A 1 531 ? -22.748 12.087  13.821 1    34.024  ? 567 LYS   A O   1 
ATOM   4287 C  CB  . LYS   A 1 531 ? -25.643 11.504  14.684 1    30.099  ? 567 LYS   A CB  1 
ATOM   4288 C  CG  . LYS   A 1 531 ? -26.772 10.527  14.353 1    41.316  ? 567 LYS   A CG  1 
ATOM   4289 C  CD  . LYS   A 1 531 ? -28.16  10.901  13.827 1    57.095  ? 567 LYS   A CD  1 
ATOM   4290 C  CE  . LYS   A 1 531 ? -28.964 9.742   13.22  1    63.259  ? 567 LYS   A CE  1 
ATOM   4291 N  NZ  . LYS   A 1 531 ? -29.709 8.863   14.14  1    57.975  ? 567 LYS   A NZ  1 
ATOM   4292 N  N   . LEU   A 1 532 ? -22.614 12.173  16.04  1    30.823  ? 568 LEU   A N   1 
ATOM   4293 C  CA  . LEU   A 1 532 ? -21.507 13.105  16.075 1    32.91   ? 568 LEU   A CA  1 
ATOM   4294 C  C   . LEU   A 1 532 ? -20.23  12.451  15.523 1    32.472  ? 568 LEU   A C   1 
ATOM   4295 O  O   . LEU   A 1 532 ? -19.302 13.159  15.114 1    24.394  ? 568 LEU   A O   1 
ATOM   4296 C  CB  . LEU   A 1 532 ? -21.299 13.555  17.519 1    30.76   ? 568 LEU   A CB  1 
ATOM   4297 C  CG  . LEU   A 1 532 ? -22.353 14.483  18.131 1    38.319  ? 568 LEU   A CG  1 
ATOM   4298 C  CD1 . LEU   A 1 532 ? -21.882 14.841  19.566 1    30.739  ? 568 LEU   A CD1 1 
ATOM   4299 C  CD2 . LEU   A 1 532 ? -22.621 15.725  17.253 1    31.446  ? 568 LEU   A CD2 1 
ATOM   4300 N  N   . GLY   A 1 533 ? -20.15  11.116  15.608 1    25.673  ? 569 GLY   A N   1 
ATOM   4301 C  CA  . GLY   A 1 533 ? -18.952 10.431  15.178 1    24.234  ? 569 GLY   A CA  1 
ATOM   4302 C  C   . GLY   A 1 533 ? -17.737 10.943  15.94  1    27.253  ? 569 GLY   A C   1 
ATOM   4303 O  O   . GLY   A 1 533 ? -17.778 11.113  17.163 1    21.289  ? 569 GLY   A O   1 
ATOM   4304 N  N   . PHE   A 1 534 ? -16.668 11.217  15.183 1    30.957  ? 570 PHE   A N   1 
ATOM   4305 C  CA  . PHE   A 1 534 ? -15.477 11.818  15.757 1    27.706  ? 570 PHE   A CA  1 
ATOM   4306 C  C   . PHE   A 1 534 ? -15.428 13.32   15.452 1    30.328  ? 570 PHE   A C   1 
ATOM   4307 O  O   . PHE   A 1 534 ? -14.323 13.878  15.379 1    35.294  ? 570 PHE   A O   1 
ATOM   4308 C  CB  . PHE   A 1 534 ? -14.291 10.971  15.269 1    24.536  ? 570 PHE   A CB  1 
ATOM   4309 C  CG  . PHE   A 1 534 ? -12.941 11.285  15.894 1    26.113  ? 570 PHE   A CG  1 
ATOM   4310 C  CD1 . PHE   A 1 534 ? -12.707 11.07   17.256 1    25.265  ? 570 PHE   A CD1 1 
ATOM   4311 C  CD2 . PHE   A 1 534 ? -11.862 11.71   15.113 1    32.748  ? 570 PHE   A CD2 1 
ATOM   4312 C  CE1 . PHE   A 1 534 ? -11.451 11.284  17.841 1    26.245  ? 570 PHE   A CE1 1 
ATOM   4313 C  CE2 . PHE   A 1 534 ? -10.583 11.933  15.688 1    30.914  ? 570 PHE   A CE2 1 
ATOM   4314 C  CZ  . PHE   A 1 534 ? -10.388 11.74   17.058 1    33.529  ? 570 PHE   A CZ  1 
ATOM   4315 N  N   . SER   A 1 535 ? -16.597 13.985  15.315 1    28.859  ? 571 SER   A N   1 
ATOM   4316 C  CA  . SER   A 1 535 ? -16.66  15.364  14.81  1    31.357  ? 571 SER   A CA  1 
ATOM   4317 C  C   . SER   A 1 535 ? -16.402 16.416  15.881 1    33.997  ? 571 SER   A C   1 
ATOM   4318 O  O   . SER   A 1 535 ? -15.995 17.524  15.528 1    39.696  ? 571 SER   A O   1 
ATOM   4319 C  CB  . SER   A 1 535 ? -17.909 15.688  14.048 1    32.876  ? 571 SER   A CB  1 
ATOM   4320 O  OG  . SER   A 1 535 ? -19.044 15.691  14.905 1    38.233  ? 571 SER   A OG  1 
ATOM   4321 N  N   . ARG   A 1 536 ? -16.616 16.058  17.162 1    31.205  ? 572 ARG   A N   1 
ATOM   4322 C  CA  . ARG   A 1 536 ? -16.533 16.981  18.289 1    29.598  ? 572 ARG   A CA  1 
ATOM   4323 C  C   . ARG   A 1 536 ? -15.685 16.391  19.407 1    28.184  ? 572 ARG   A C   1 
ATOM   4324 O  O   . ARG   A 1 536 ? -15.66  15.184  19.589 1    35.336  ? 572 ARG   A O   1 
ATOM   4325 C  CB  . ARG   A 1 536 ? -17.948 17.242  18.821 1    30.185  ? 572 ARG   A CB  1 
ATOM   4326 C  CG  . ARG   A 1 536 ? -18.929 17.944  17.878 1    37.036  ? 572 ARG   A CG  1 
ATOM   4327 C  CD  . ARG   A 1 536 ? -18.606 19.278  17.203 1    39.032  ? 572 ARG   A CD  1 
ATOM   4328 N  NE  . ARG   A 1 536 ? -18.29  20.308  18.205 1    61.881  ? 572 ARG   A NE  1 
ATOM   4329 C  CZ  . ARG   A 1 536 ? -17.416 21.352  18.155 1    56.349  ? 572 ARG   A CZ  1 
ATOM   4330 N  NH1 . ARG   A 1 536 ? -16.883 21.741  17.006 1    41.699  ? 572 ARG   A NH1 1 
ATOM   4331 N  NH2 . ARG   A 1 536 ? -17.137 22.037  19.264 1    44.357  ? 572 ARG   A NH2 1 
ATOM   4332 N  N   . PRO   A 1 537 ? -15.024 17.187  20.264 1    33.006  ? 573 PRO   A N   1 
ATOM   4333 C  CA  . PRO   A 1 537 ? -14.35  16.614  21.436 1    32.481  ? 573 PRO   A CA  1 
ATOM   4334 C  C   . PRO   A 1 537 ? -15.319 15.713  22.207 1    29.411  ? 573 PRO   A C   1 
ATOM   4335 O  O   . PRO   A 1 537 ? -16.492 16.056  22.363 1    26.416  ? 573 PRO   A O   1 
ATOM   4336 C  CB  . PRO   A 1 537 ? -13.899 17.867  22.28  1    30.173  ? 573 PRO   A CB  1 
ATOM   4337 C  CG  . PRO   A 1 537 ? -13.892 19.039  21.304 1    27.052  ? 573 PRO   A CG  1 
ATOM   4338 C  CD  . PRO   A 1 537 ? -14.989 18.669  20.268 1    31.846  ? 573 PRO   A CD  1 
ATOM   4339 N  N   . TRP   A 1 538 ? -14.825 14.557  22.693 1    28.569  ? 574 TRP   A N   1 
ATOM   4340 C  CA  . TRP   A 1 538 ? -15.708 13.56   23.284 1    26.195  ? 574 TRP   A CA  1 
ATOM   4341 C  C   . TRP   A 1 538 ? -16.54  14.066  24.475 1    29.777  ? 574 TRP   A C   1 
ATOM   4342 O  O   . TRP   A 1 538 ? -17.635 13.52   24.677 1    27.203  ? 574 TRP   A O   1 
ATOM   4343 C  CB  . TRP   A 1 538 ? -14.944 12.297  23.66  1    21.626  ? 574 TRP   A CB  1 
ATOM   4344 C  CG  . TRP   A 1 538 ? -13.984 12.437  24.797 1    18.881  ? 574 TRP   A CG  1 
ATOM   4345 C  CD1 . TRP   A 1 538 ? -12.617 12.418  24.668 1    20.191  ? 574 TRP   A CD1 1 
ATOM   4346 C  CD2 . TRP   A 1 538 ? -14.275 12.452  26.213 1    18.433  ? 574 TRP   A CD2 1 
ATOM   4347 N  NE1 . TRP   A 1 538 ? -12.037 12.457  25.903 1    20.065  ? 574 TRP   A NE1 1 
ATOM   4348 C  CE2 . TRP   A 1 538 ? -13.016 12.492  26.872 1    16.63   ? 574 TRP   A CE2 1 
ATOM   4349 C  CE3 . TRP   A 1 538 ? -15.457 12.402  26.985 1    16.972  ? 574 TRP   A CE3 1 
ATOM   4350 C  CZ2 . TRP   A 1 538 ? -12.896 12.555  28.254 1    13.726  ? 574 TRP   A CZ2 1 
ATOM   4351 C  CZ3 . TRP   A 1 538 ? -15.335 12.443  28.358 1    15.936  ? 574 TRP   A CZ3 1 
ATOM   4352 C  CH2 . TRP   A 1 538 ? -14.075 12.536  28.971 1    16.153  ? 574 TRP   A CH2 1 
ATOM   4353 N  N   . PRO   A 1 539 ? -16.129 15.088  25.302 1    32.632  ? 575 PRO   A N   1 
ATOM   4354 C  CA  . PRO   A 1 539 ? -16.943 15.48   26.465 1    32.75   ? 575 PRO   A CA  1 
ATOM   4355 C  C   . PRO   A 1 539 ? -18.315 15.942  25.975 1    32.212  ? 575 PRO   A C   1 
ATOM   4356 O  O   . PRO   A 1 539 ? -19.267 15.915  26.743 1    27.051  ? 575 PRO   A O   1 
ATOM   4357 C  CB  . PRO   A 1 539 ? -16.141 16.58   27.114 1    23.923  ? 575 PRO   A CB  1 
ATOM   4358 C  CG  . PRO   A 1 539 ? -14.722 16.165  26.733 1    25.437  ? 575 PRO   A CG  1 
ATOM   4359 C  CD  . PRO   A 1 539 ? -14.876 15.872  25.25  1    24.752  ? 575 PRO   A CD  1 
ATOM   4360 N  N   . GLU   A 1 540 ? -18.399 16.28   24.671 1    27.098  ? 576 GLU   A N   1 
ATOM   4361 C  CA  . GLU   A 1 540 ? -19.647 16.813  24.134 1    30.713  ? 576 GLU   A CA  1 
ATOM   4362 C  C   . GLU   A 1 540 ? -20.622 15.668  23.949 1    33.082  ? 576 GLU   A C   1 
ATOM   4363 O  O   . GLU   A 1 540 ? -21.765 15.806  24.364 1    35.418  ? 576 GLU   A O   1 
ATOM   4364 C  CB  . GLU   A 1 540 ? -19.624 17.675  22.869 1    31.334  ? 576 GLU   A CB  1 
ATOM   4365 C  CG  . GLU   A 1 540 ? -19.142 19.107  23.107 1    38.967  ? 576 GLU   A CG  1 
ATOM   4366 C  CD  . GLU   A 1 540 ? -18.768 19.934  21.846 1    51.994  ? 576 GLU   A CD  1 
ATOM   4367 O  OE1 . GLU   A 1 540 ? -19.463 19.731  20.782 1    36.278  ? 576 GLU   A OE1 1 
ATOM   4368 O  OE2 . GLU   A 1 540 ? -17.821 20.817  21.935 1    51.905  ? 576 GLU   A OE2 1 
ATOM   4369 N  N   . ALA   A 1 541 ? -20.131 14.525  23.42  1    31.629  ? 577 ALA   A N   1 
ATOM   4370 C  CA  . ALA   A 1 541 ? -20.965 13.341  23.424 1    29.32   ? 577 ALA   A CA  1 
ATOM   4371 C  C   . ALA   A 1 541 ? -21.237 12.875  24.861 1    28.21   ? 577 ALA   A C   1 
ATOM   4372 O  O   . ALA   A 1 541 ? -22.337 12.454  25.157 1    28.919  ? 577 ALA   A O   1 
ATOM   4373 C  CB  . ALA   A 1 541 ? -20.399 12.268  22.529 1    26.845  ? 577 ALA   A CB  1 
ATOM   4374 N  N   . MET   A 1 542 ? -20.272 12.982  25.777 1    23.696  ? 578 MET   A N   1 
ATOM   4375 C  CA  . MET   A 1 542 ? -20.575 12.506  27.11  1    22.491  ? 578 MET   A CA  1 
ATOM   4376 C  C   . MET   A 1 542 ? -21.783 13.262  27.661 1    26.599  ? 578 MET   A C   1 
ATOM   4377 O  O   . MET   A 1 542 ? -22.665 12.648  28.294 1    24.333  ? 578 MET   A O   1 
ATOM   4378 C  CB  . MET   A 1 542 ? -19.417 12.784  28.062 1    22.864  ? 578 MET   A CB  1 
ATOM   4379 C  CG  . MET   A 1 542 ? -19.743 12.438  29.535 1    21.538  ? 578 MET   A CG  1 
ATOM   4380 S  SD  . MET   A 1 542 ? -19.961 10.658  29.764 1    29.815  ? 578 MET   A SD  1 
ATOM   4381 C  CE  . MET   A 1 542 ? -18.308 9.95    29.514 1    23.47   ? 578 MET   A CE  1 
ATOM   4382 N  N   . GLN   A 1 543 ? -21.76  14.6    27.43  1    28.424  ? 579 GLN   A N   1 
ATOM   4383 C  CA  . GLN   A 1 543 ? -22.707 15.609  27.896 1    33.686  ? 579 GLN   A CA  1 
ATOM   4384 C  C   . GLN   A 1 543 ? -24.073 15.385  27.253 1    31.891  ? 579 GLN   A C   1 
ATOM   4385 O  O   . GLN   A 1 543 ? -25.051 15.293  27.968 1    36.979  ? 579 GLN   A O   1 
ATOM   4386 C  CB  . GLN   A 1 543 ? -22.202 17.047  27.75  1    47.265  ? 579 GLN   A CB  1 
ATOM   4387 C  CG  . GLN   A 1 543 ? -22.98  18.105  28.545 1    52.534  ? 579 GLN   A CG  1 
ATOM   4388 C  CD  . GLN   A 1 543 ? -22.199 19.397  28.722 1    61.08   ? 579 GLN   A CD  1 
ATOM   4389 O  OE1 . GLN   A 1 543 ? -21.018 19.42   29.09  1    68.967  ? 579 GLN   A OE1 1 
ATOM   4390 N  NE2 . GLN   A 1 543 ? -22.835 20.519  28.429 1    80.779  ? 579 GLN   A NE2 1 
ATOM   4391 N  N   . LEU   A 1 544 ? -24.131 15.154  25.939 1    27.515  ? 580 LEU   A N   1 
ATOM   4392 C  CA  . LEU   A 1 544 ? -25.376 14.744  25.326 1    34.946  ? 580 LEU   A CA  1 
ATOM   4393 C  C   . LEU   A 1 544 ? -25.982 13.516  26.024 1    39.675  ? 580 LEU   A C   1 
ATOM   4394 O  O   . LEU   A 1 544 ? -27.205 13.424  26.134 1    40.406  ? 580 LEU   A O   1 
ATOM   4395 C  CB  . LEU   A 1 544 ? -25.136 14.438  23.849 1    33.752  ? 580 LEU   A CB  1 
ATOM   4396 C  CG  . LEU   A 1 544 ? -25.024 15.637  22.904 1    43.195  ? 580 LEU   A CG  1 
ATOM   4397 C  CD1 . LEU   A 1 544 ? -24.658 15.057  21.563 1    31.161  ? 580 LEU   A CD1 1 
ATOM   4398 C  CD2 . LEU   A 1 544 ? -26.365 16.386  22.763 1    47.789  ? 580 LEU   A CD2 1 
ATOM   4399 N  N   . ILE   A 1 545 ? -25.164 12.508  26.375 1    31.553  ? 581 ILE   A N   1 
ATOM   4400 C  CA  . ILE   A 1 545 ? -25.802 11.305  26.865 1    32.417  ? 581 ILE   A CA  1 
ATOM   4401 C  C   . ILE   A 1 545 ? -26.187 11.501  28.34  1    32.951  ? 581 ILE   A C   1 
ATOM   4402 O  O   . ILE   A 1 545 ? -27.19  10.929  28.777 1    27.753  ? 581 ILE   A O   1 
ATOM   4403 C  CB  . ILE   A 1 545 ? -24.96  10.022  26.652 1    29.694  ? 581 ILE   A CB  1 
ATOM   4404 C  CG1 . ILE   A 1 545 ? -24.774 9.617   25.199 1    26.303  ? 581 ILE   A CG1 1 
ATOM   4405 C  CG2 . ILE   A 1 545 ? -25.596 8.857   27.394 1    25.591  ? 581 ILE   A CG2 1 
ATOM   4406 C  CD1 . ILE   A 1 545 ? -23.492 8.82    25.019 1    20.744  ? 581 ILE   A CD1 1 
ATOM   4407 N  N   . THR   A 1 546 ? -25.364 12.245  29.103 1    27.097  ? 582 THR   A N   1 
ATOM   4408 C  CA  . THR   A 1 546 ? -25.374 12.067  30.542 1    25.853  ? 582 THR   A CA  1 
ATOM   4409 C  C   . THR   A 1 546 ? -25.603 13.386  31.275 1    28.348  ? 582 THR   A C   1 
ATOM   4410 O  O   . THR   A 1 546 ? -25.568 13.371  32.488 1    27.012  ? 582 THR   A O   1 
ATOM   4411 C  CB  . THR   A 1 546 ? -24.081 11.433  31.061 1    27.305  ? 582 THR   A CB  1 
ATOM   4412 O  OG1 . THR   A 1 546 ? -23.049 12.436  31.045 1    23.439  ? 582 THR   A OG1 1 
ATOM   4413 C  CG2 . THR   A 1 546 ? -23.76  10.065  30.449 1    23.575  ? 582 THR   A CG2 1 
ATOM   4414 N  N   . GLY   A 1 547 ? -25.816 14.514  30.582 1    27.132  ? 583 GLY   A N   1 
ATOM   4415 C  CA  . GLY   A 1 547 ? -25.972 15.775  31.291 1    28.066  ? 583 GLY   A CA  1 
ATOM   4416 C  C   . GLY   A 1 547 ? -24.698 16.403  31.864 1    32.644  ? 583 GLY   A C   1 
ATOM   4417 O  O   . GLY   A 1 547 ? -24.726 17.548  32.334 1    38.988  ? 583 GLY   A O   1 
ATOM   4418 N  N   . GLN   A 1 548 ? -23.551 15.726  31.807 1    30.284  ? 584 GLN   A N   1 
ATOM   4419 C  CA  . GLN   A 1 548 ? -22.35  16.424  32.241 1    30.876  ? 584 GLN   A CA  1 
ATOM   4420 C  C   . GLN   A 1 548 ? -21.234 15.975  31.314 1    31.062  ? 584 GLN   A C   1 
ATOM   4421 O  O   . GLN   A 1 548 ? -21.518 15.084  30.53  1    31.55   ? 584 GLN   A O   1 
ATOM   4422 C  CB  . GLN   A 1 548 ? -22.084 16.25   33.741 1    27.771  ? 584 GLN   A CB  1 
ATOM   4423 C  CG  . GLN   A 1 548 ? -21.991 14.797  34.186 1    29.642  ? 584 GLN   A CG  1 
ATOM   4424 C  CD  . GLN   A 1 548 ? -20.643 14.149  33.894 1    31.382  ? 584 GLN   A CD  1 
ATOM   4425 O  OE1 . GLN   A 1 548 ? -19.598 14.645  34.301 1    30.284  ? 584 GLN   A OE1 1 
ATOM   4426 N  NE2 . GLN   A 1 548 ? -20.645 13.027  33.183 1    31.394  ? 584 GLN   A NE2 1 
ATOM   4427 N  N   . PRO   A 1 549 ? -19.994 16.545  31.353 1    32.849  ? 585 PRO   A N   1 
ATOM   4428 C  CA  . PRO   A 1 549 ? -18.927 16.17   30.409 1    34.189  ? 585 PRO   A CA  1 
ATOM   4429 C  C   . PRO   A 1 549 ? -17.778 15.279  30.904 1    32.188  ? 585 PRO   A C   1 
ATOM   4430 O  O   . PRO   A 1 549 ? -16.819 15.063  30.181 1    29.365  ? 585 PRO   A O   1 
ATOM   4431 C  CB  . PRO   A 1 549 ? -18.389 17.637  30.17  1    38.127  ? 585 PRO   A CB  1 
ATOM   4432 C  CG  . PRO   A 1 549 ? -18.295 18.239  31.619 1    31.039  ? 585 PRO   A CG  1 
ATOM   4433 C  CD  . PRO   A 1 549 ? -19.556 17.655  32.232 1    30.849  ? 585 PRO   A CD  1 
ATOM   4434 N  N   . GLN   A 1 550 ? -17.793 14.817  32.156 1    32.738  ? 586 GLN   A N   1 
ATOM   4435 C  CA  . GLN   A 1 550 ? -16.632 14.069  32.632 1    33.469  ? 586 GLN   A CA  1 
ATOM   4436 C  C   . GLN   A 1 550 ? -16.847 12.547  32.657 1    29.842  ? 586 GLN   A C   1 
ATOM   4437 O  O   . GLN   A 1 550 ? -17.959 12.039  32.683 1    26.389  ? 586 GLN   A O   1 
ATOM   4438 C  CB  . GLN   A 1 550 ? -16.376 14.429  34.083 1    38.152  ? 586 GLN   A CB  1 
ATOM   4439 C  CG  . GLN   A 1 550 ? -16.459 15.914  34.377 1    41.866  ? 586 GLN   A CG  1 
ATOM   4440 C  CD  . GLN   A 1 550 ? -15.348 16.265  35.336 1    61.644  ? 586 GLN   A CD  1 
ATOM   4441 O  OE1 . GLN   A 1 550 ? -14.199 16.402  34.899 1    85.185  ? 586 GLN   A OE1 1 
ATOM   4442 N  NE2 . GLN   A 1 550 ? -15.641 16.34   36.634 1    44.121  ? 586 GLN   A NE2 1 
ATOM   4443 N  N   . MET   A 1 551 ? -15.746 11.797  32.637 1    33.083  ? 587 MET   A N   1 
ATOM   4444 C  CA  . MET   A 1 551 ? -15.776 10.381  32.962 1    30.576  ? 587 MET   A CA  1 
ATOM   4445 C  C   . MET   A 1 551 ? -15.851 10.258  34.494 1    27.381  ? 587 MET   A C   1 
ATOM   4446 O  O   . MET   A 1 551 ? -15.156 10.969  35.2   1    25.075  ? 587 MET   A O   1 
ATOM   4447 C  CB  . MET   A 1 551 ? -14.454 9.753   32.485 1    26.12   ? 587 MET   A CB  1 
ATOM   4448 C  CG  . MET   A 1 551 ? -14.366 9.418   30.992 1    25.259  ? 587 MET   A CG  1 
ATOM   4449 S  SD  . MET   A 1 551 ? -12.854 8.445   30.732 1    27.08   ? 587 MET   A SD  1 
ATOM   4450 C  CE  . MET   A 1 551 ? -11.709 9.784   31.142 1    28.881  ? 587 MET   A CE  1 
ATOM   4451 N  N   . SER   A 1 552 ? -16.605 9.289   35.023 1    28.688  ? 588 SER   A N   1 
ATOM   4452 C  CA  . SER   A 1 552 ? -16.824 9.19    36.472 1    31.761  ? 588 SER   A CA  1 
ATOM   4453 C  C   . SER   A 1 552 ? -17.185 7.753   36.851 1    30.576  ? 588 SER   A C   1 
ATOM   4454 O  O   . SER   A 1 552 ? -18.104 7.159   36.255 1    24.905  ? 588 SER   A O   1 
ATOM   4455 C  CB  . SER   A 1 552 ? -17.969 10.111  36.907 1    34.061  ? 588 SER   A CB  1 
ATOM   4456 O  OG  . SER   A 1 552 ? -18.202 10.068  38.313 1    38.023  ? 588 SER   A OG  1 
ATOM   4457 N  N   . ALA   A 1 553 ? -16.473 7.229   37.866 1    29.621  ? 589 ALA   A N   1 
ATOM   4458 C  CA  . ALA   A 1 553 ? -16.747 5.943   38.492 1    26.392  ? 589 ALA   A CA  1 
ATOM   4459 C  C   . ALA   A 1 553 ? -18.086 5.884   39.258 1    28.706  ? 589 ALA   A C   1 
ATOM   4460 O  O   . ALA   A 1 553 ? -18.592 4.796   39.513 1    33.427  ? 589 ALA   A O   1 
ATOM   4461 C  CB  . ALA   A 1 553 ? -15.607 5.649   39.408 1    22.043  ? 589 ALA   A CB  1 
ATOM   4462 N  N   . SER   A 1 554 ? -18.689 7.014   39.638 1    23.867  ? 590 SER   A N   1 
ATOM   4463 C  CA  . SER   A 1 554 ? -19.76  6.945   40.63  1    28.977  ? 590 SER   A CA  1 
ATOM   4464 C  C   . SER   A 1 554 ? -21.002 6.163   40.159 1    27.984  ? 590 SER   A C   1 
ATOM   4465 O  O   . SER   A 1 554 ? -21.698 5.557   40.965 1    26.963  ? 590 SER   A O   1 
ATOM   4466 C  CB  . SER   A 1 554 ? -20.105 8.344   41.189 1    31.221  ? 590 SER   A CB  1 
ATOM   4467 O  OG  . SER   A 1 554 ? -20.9   9.014   40.217 1    38.108  ? 590 SER   A OG  1 
ATOM   4468 N  N   . ALA   A 1 555 ? -21.243 6.027   38.848 1    24.856  ? 591 ALA   A N   1 
ATOM   4469 C  CA  . ALA   A 1 555 ? -22.392 5.257   38.429 1    20.283  ? 591 ALA   A CA  1 
ATOM   4470 C  C   . ALA   A 1 555 ? -22.107 3.75    38.614 1    26.913  ? 591 ALA   A C   1 
ATOM   4471 O  O   . ALA   A 1 555 ? -22.968 2.946   39.051 1    26.487  ? 591 ALA   A O   1 
ATOM   4472 C  CB  . ALA   A 1 555 ? -22.728 5.656   36.991 1    17.956  ? 591 ALA   A CB  1 
ATOM   4473 N  N   . MET   A 1 556 ? -20.876 3.345   38.275 1    24.201  ? 592 MET   A N   1 
ATOM   4474 C  CA  . MET   A 1 556 ? -20.492 1.977   38.538 1    26.117  ? 592 MET   A CA  1 
ATOM   4475 C  C   . MET   A 1 556 ? -20.555 1.728   40.053 1    26.479  ? 592 MET   A C   1 
ATOM   4476 O  O   . MET   A 1 556 ? -21.076 0.714   40.494 1    32.054  ? 592 MET   A O   1 
ATOM   4477 C  CB  . MET   A 1 556 ? -19.066 1.674   38.046 1    24.722  ? 592 MET   A CB  1 
ATOM   4478 C  CG  . MET   A 1 556 ? -18.786 0.215   37.886 1    25.51   ? 592 MET   A CG  1 
ATOM   4479 S  SD  . MET   A 1 556 ? -17.164 -0.097  37.154 1    29.933  ? 592 MET   A SD  1 
ATOM   4480 C  CE  . MET   A 1 556 ? -17.119 -1.861  36.803 1    31.047  ? 592 MET   A CE  1 
ATOM   4481 N  N   . LEU   A 1 557 ? -19.996 2.609   40.865 1    24.64   ? 593 LEU   A N   1 
ATOM   4482 C  CA  . LEU   A 1 557 ? -19.968 2.321   42.301 1    26.657  ? 593 LEU   A CA  1 
ATOM   4483 C  C   . LEU   A 1 557 ? -21.382 2.184   42.821 1    25.692  ? 593 LEU   A C   1 
ATOM   4484 O  O   . LEU   A 1 557 ? -21.596 1.511   43.821 1    29.913  ? 593 LEU   A O   1 
ATOM   4485 C  CB  . LEU   A 1 557 ? -19.294 3.397   43.15  1    22.74   ? 593 LEU   A CB  1 
ATOM   4486 C  CG  . LEU   A 1 557 ? -17.784 3.452   42.923 1    30.284  ? 593 LEU   A CG  1 
ATOM   4487 C  CD1 . LEU   A 1 557 ? -17.122 4.512   43.803 1    24.577  ? 593 LEU   A CD1 1 
ATOM   4488 C  CD2 . LEU   A 1 557 ? -17.224 2.054   43.106 1    31.51   ? 593 LEU   A CD2 1 
ATOM   4489 N  N   . SER   A 1 558 ? -22.296 2.944   42.215 1    26.117  ? 594 SER   A N   1 
ATOM   4490 C  CA  . SER   A 1 558 ? -23.621 3.057   42.772 1    28.097  ? 594 SER   A CA  1 
ATOM   4491 C  C   . SER   A 1 558 ? -24.423 1.87    42.264 1    29.441  ? 594 SER   A C   1 
ATOM   4492 O  O   . SER   A 1 558 ? -25.139 1.27    43.031 1    34.044  ? 594 SER   A O   1 
ATOM   4493 C  CB  . SER   A 1 558 ? -24.219 4.361   42.448 1    31.15   ? 594 SER   A CB  1 
ATOM   4494 O  OG  . SER   A 1 558 ? -25.588 4.109   42.2   1    35.599  ? 594 SER   A OG  1 
ATOM   4495 N  N   . TYR   A 1 559 ? -24.172 1.435   41.031 1    25.164  ? 595 TYR   A N   1 
ATOM   4496 C  CA  . TYR   A 1 559 ? -24.752 0.182   40.599 1    26.03   ? 595 TYR   A CA  1 
ATOM   4497 C  C   . TYR   A 1 559 ? -24.39  -0.999  41.505 1    28.599  ? 595 TYR   A C   1 
ATOM   4498 O  O   . TYR   A 1 559 ? -25.253 -1.86   41.685 1    27.301  ? 595 TYR   A O   1 
ATOM   4499 C  CB  . TYR   A 1 559 ? -24.273 -0.158  39.186 1    22.944  ? 595 TYR   A CB  1 
ATOM   4500 C  CG  . TYR   A 1 559 ? -24.766 -1.48   38.602 1    18.569  ? 595 TYR   A CG  1 
ATOM   4501 C  CD1 . TYR   A 1 559 ? -24.158 -2.701  38.892 1    17.871  ? 595 TYR   A CD1 1 
ATOM   4502 C  CD2 . TYR   A 1 559 ? -25.738 -1.466  37.61  1    19.321  ? 595 TYR   A CD2 1 
ATOM   4503 C  CE1 . TYR   A 1 559 ? -24.556 -3.886  38.28  1    17.113  ? 595 TYR   A CE1 1 
ATOM   4504 C  CE2 . TYR   A 1 559 ? -26.168 -2.623  36.995 1    21.371  ? 595 TYR   A CE2 1 
ATOM   4505 C  CZ  . TYR   A 1 559 ? -25.586 -3.827  37.352 1    21.51   ? 595 TYR   A CZ  1 
ATOM   4506 O  OH  . TYR   A 1 559 ? -26.077 -4.872  36.658 1    26.878  ? 595 TYR   A OH  1 
ATOM   4507 N  N   . PHE   A 1 560 ? -23.133 -1.081  42.015 1    27.757  ? 596 PHE   A N   1 
ATOM   4508 C  CA  . PHE   A 1 560 ? -22.644 -2.248  42.771 1    28.937  ? 596 PHE   A CA  1 
ATOM   4509 C  C   . PHE   A 1 560 ? -22.73  -2.054  44.308 1    32.098  ? 596 PHE   A C   1 
ATOM   4510 O  O   . PHE   A 1 560 ? -22.237 -2.878  45.099 1    28.834  ? 596 PHE   A O   1 
ATOM   4511 C  CB  . PHE   A 1 560 ? -21.244 -2.753  42.338 1    22.446  ? 596 PHE   A CB  1 
ATOM   4512 C  CG  . PHE   A 1 560 ? -21.212 -3.492  41.001 1    21.295  ? 596 PHE   A CG  1 
ATOM   4513 C  CD1 . PHE   A 1 560 ? -21.625 -4.823  40.911 1    18.832  ? 596 PHE   A CD1 1 
ATOM   4514 C  CD2 . PHE   A 1 560 ? -20.716 -2.872  39.848 1    19.937  ? 596 PHE   A CD2 1 
ATOM   4515 C  CE1 . PHE   A 1 560 ? -21.609 -5.502  39.696 1    22.724  ? 596 PHE   A CE1 1 
ATOM   4516 C  CE2 . PHE   A 1 560 ? -20.678 -3.553  38.625 1    23.114  ? 596 PHE   A CE2 1 
ATOM   4517 C  CZ  . PHE   A 1 560 ? -21.082 -4.892  38.544 1    21.33   ? 596 PHE   A CZ  1 
ATOM   4518 N  N   . LYS   A 1 561 ? -23.299 -0.925  44.762 1    36.859  ? 597 LYS   A N   1 
ATOM   4519 C  CA  . LYS   A 1 561 ? -23.247 -0.488  46.157 1    33.588  ? 597 LYS   A CA  1 
ATOM   4520 C  C   . LYS   A 1 561 ? -23.803 -1.562  47.101 1    33.519  ? 597 LYS   A C   1 
ATOM   4521 O  O   . LYS   A 1 561 ? -23.172 -1.848  48.129 1    40.64   ? 597 LYS   A O   1 
ATOM   4522 C  CB  . LYS   A 1 561 ? -23.815 0.942   46.231 1    39.123  ? 597 LYS   A CB  1 
ATOM   4523 C  CG  . LYS   A 1 561 ? -24.541 1.426   47.485 1    52.633  ? 597 LYS   A CG  1 
ATOM   4524 C  CD  . LYS   A 1 561 ? -23.62  1.635   48.684 1    61.341  ? 597 LYS   A CD  1 
ATOM   4525 C  CE  . LYS   A 1 561 ? -24.297 1.989   49.983 1    64.678  ? 597 LYS   A CE  1 
ATOM   4526 N  NZ  . LYS   A 1 561 ? -23.281 1.934   51.044 1    65.345  ? 597 LYS   A NZ  1 
ATOM   4527 N  N   . PRO   A 1 562 ? -24.974 -2.19   46.832 1    28.027  ? 598 PRO   A N   1 
ATOM   4528 C  CA  . PRO   A 1 562 ? -25.437 -3.341  47.628 1    32.185  ? 598 PRO   A CA  1 
ATOM   4529 C  C   . PRO   A 1 562 ? -24.467 -4.516  47.721 1    32.733  ? 598 PRO   A C   1 
ATOM   4530 O  O   . PRO   A 1 562 ? -24.342 -5.134  48.784 1    37.508  ? 598 PRO   A O   1 
ATOM   4531 C  CB  . PRO   A 1 562 ? -26.827 -3.781  47.097 1    26.922  ? 598 PRO   A CB  1 
ATOM   4532 C  CG  . PRO   A 1 562 ? -27.259 -2.623  46.19  1    28.446  ? 598 PRO   A CG  1 
ATOM   4533 C  CD  . PRO   A 1 562 ? -25.968 -1.835  45.801 1    30.933  ? 598 PRO   A CD  1 
ATOM   4534 N  N   . LEU   A 1 563 ? -23.776 -4.808  46.618 1    28.856  ? 599 LEU   A N   1 
ATOM   4535 C  CA  . LEU   A 1 563 ? -22.776 -5.854  46.673 1    25.988  ? 599 LEU   A CA  1 
ATOM   4536 C  C   . LEU   A 1 563 ? -21.583 -5.425  47.528 1    25.975  ? 599 LEU   A C   1 
ATOM   4537 O  O   . LEU   A 1 563 ? -21.041 -6.247  48.259 1    30.781  ? 599 LEU   A O   1 
ATOM   4538 C  CB  . LEU   A 1 563 ? -22.314 -6.273  45.282 1    32.426  ? 599 LEU   A CB  1 
ATOM   4539 C  CG  . LEU   A 1 563 ? -21.276 -7.4    45.321 1    37.866  ? 599 LEU   A CG  1 
ATOM   4540 C  CD1 . LEU   A 1 563 ? -22.078 -8.636  45.63  1    32.98   ? 599 LEU   A CD1 1 
ATOM   4541 C  CD2 . LEU   A 1 563 ? -20.524 -7.575  44.054 1    36.733  ? 599 LEU   A CD2 1 
ATOM   4542 N  N   . LEU   A 1 564 ? -21.142 -4.167  47.427 1    23.791  ? 600 LEU   A N   1 
ATOM   4543 C  CA  . LEU   A 1 564 ? -20.007 -3.727  48.245 1    25.699  ? 600 LEU   A CA  1 
ATOM   4544 C  C   . LEU   A 1 564 ? -20.351 -3.808  49.762 1    32.531  ? 600 LEU   A C   1 
ATOM   4545 O  O   . LEU   A 1 564 ? -19.512 -4.196  50.597 1    28.316  ? 600 LEU   A O   1 
ATOM   4546 C  CB  . LEU   A 1 564 ? -19.503 -2.341  47.807 1    21.044  ? 600 LEU   A CB  1 
ATOM   4547 C  CG  . LEU   A 1 564 ? -18.476 -1.587  48.676 1    22.668  ? 600 LEU   A CG  1 
ATOM   4548 C  CD1 . LEU   A 1 564 ? -17.085 -2.155  48.479 1    25.393  ? 600 LEU   A CD1 1 
ATOM   4549 C  CD2 . LEU   A 1 564 ? -18.401 -0.1    48.409 1    20.281  ? 600 LEU   A CD2 1 
ATOM   4550 N  N   . ASP   A 1 565 ? -21.597 -3.467  50.128 1    28.877  ? 601 ASP   A N   1 
ATOM   4551 C  CA  . ASP   A 1 565 ? -22.012 -3.573  51.516 1    31.65   ? 601 ASP   A CA  1 
ATOM   4552 C  C   . ASP   A 1 565 ? -21.953 -5.045  51.892 1    32.092  ? 601 ASP   A C   1 
ATOM   4553 O  O   . ASP   A 1 565 ? -21.529 -5.384  52.991 1    27.585  ? 601 ASP   A O   1 
ATOM   4554 C  CB  . ASP   A 1 565 ? -23.402 -3.009  51.772 1    23.526  ? 601 ASP   A CB  1 
ATOM   4555 C  CG  . ASP   A 1 565 ? -23.431 -1.508  51.607 1    28.348  ? 601 ASP   A CG  1 
ATOM   4556 O  OD1 . ASP   A 1 565 ? -22.32  -0.956  51.748 1    28.591  ? 601 ASP   A OD1 1 
ATOM   4557 O  OD2 . ASP   A 1 565 ? -24.524 -0.934  51.246 1    30.209  ? 601 ASP   A OD2 1 
ATOM   4558 N  N   . TRP   A 1 566 ? -22.345 -5.898  50.947 1    28.627  ? 602 TRP   A N   1 
ATOM   4559 C  CA  . TRP   A 1 566 ? -22.442 -7.308  51.307 1    33.376  ? 602 TRP   A CA  1 
ATOM   4560 C  C   . TRP   A 1 566 ? -21.044 -7.92   51.476 1    32.031  ? 602 TRP   A C   1 
ATOM   4561 O  O   . TRP   A 1 566 ? -20.816 -8.658  52.442 1    30.295  ? 602 TRP   A O   1 
ATOM   4562 C  CB  . TRP   A 1 566 ? -23.312 -8.08   50.309 1    28.362  ? 602 TRP   A CB  1 
ATOM   4563 C  CG  . TRP   A 1 566 ? -23.516 -9.51   50.725 1    36.416  ? 602 TRP   A CG  1 
ATOM   4564 C  CD1 . TRP   A 1 566 ? -24.516 -10.032 51.508 1    35.528  ? 602 TRP   A CD1 1 
ATOM   4565 C  CD2 . TRP   A 1 566 ? -22.666 -10.611 50.344 1    33.463  ? 602 TRP   A CD2 1 
ATOM   4566 N  NE1 . TRP   A 1 566 ? -24.336 -11.377 51.654 1    40.077  ? 602 TRP   A NE1 1 
ATOM   4567 C  CE2 . TRP   A 1 566 ? -23.208 -11.764 50.966 1    37.024  ? 602 TRP   A CE2 1 
ATOM   4568 C  CE3 . TRP   A 1 566 ? -21.515 -10.725 49.545 1    29.393  ? 602 TRP   A CE3 1 
ATOM   4569 C  CZ2 . TRP   A 1 566 ? -22.612 -13.023 50.817 1    34.554  ? 602 TRP   A CZ2 1 
ATOM   4570 C  CZ3 . TRP   A 1 566 ? -20.931 -11.967 49.372 1    26.783  ? 602 TRP   A CZ3 1 
ATOM   4571 C  CH2 . TRP   A 1 566 ? -21.471 -13.094 50.027 1    39.486  ? 602 TRP   A CH2 1 
ATOM   4572 N  N   . LEU   A 1 567 ? -20.097 -7.503  50.607 1    26.834  ? 603 LEU   A N   1 
ATOM   4573 C  CA  . LEU   A 1 567 ? -18.765 -8.072  50.579 1    25.957  ? 603 LEU   A CA  1 
ATOM   4574 C  C   . LEU   A 1 567 ? -18.004 -7.686  51.83  1    24.112  ? 603 LEU   A C   1 
ATOM   4575 O  O   . LEU   A 1 567 ? -17.356 -8.523  52.419 1    25.509  ? 603 LEU   A O   1 
ATOM   4576 C  CB  . LEU   A 1 567 ? -17.995 -7.682  49.337 1    24.552  ? 603 LEU   A CB  1 
ATOM   4577 C  CG  . LEU   A 1 567 ? -18.547 -8.346  48.089 1    28.823  ? 603 LEU   A CG  1 
ATOM   4578 C  CD1 . LEU   A 1 567 ? -18.146 -7.437  46.989 1    27.557  ? 603 LEU   A CD1 1 
ATOM   4579 C  CD2 . LEU   A 1 567 ? -17.976 -9.781  47.948 1    24.462  ? 603 LEU   A CD2 1 
ATOM   4580 N  N   . ARG   A 1 568 ? -18.144 -6.447  52.235 1    25.493  ? 604 ARG   A N   1 
ATOM   4581 C  CA  . ARG   A 1 568 ? -17.491 -5.932  53.429 1    31.691  ? 604 ARG   A CA  1 
ATOM   4582 C  C   . ARG   A 1 568 ? -17.931 -6.715  54.66  1    27.213  ? 604 ARG   A C   1 
ATOM   4583 O  O   . ARG   A 1 568 ? -17.1   -7.139  55.451 1    28.939  ? 604 ARG   A O   1 
ATOM   4584 C  CB  . ARG   A 1 568 ? -17.881 -4.472  53.694 1    32.475  ? 604 ARG   A CB  1 
ATOM   4585 C  CG  . ARG   A 1 568 ? -17.225 -3.437  52.8   1    34.759  ? 604 ARG   A CG  1 
ATOM   4586 C  CD  . ARG   A 1 568 ? -17.099 -2.148  53.594 1    50.227  ? 604 ARG   A CD  1 
ATOM   4587 N  NE  . ARG   A 1 568 ? -15.975 -1.413  52.999 1    61.248  ? 604 ARG   A NE  1 
ATOM   4588 C  CZ  . ARG   A 1 568 ? -16.121 -0.373  52.165 1    63.77   ? 604 ARG   A CZ  1 
ATOM   4589 N  NH1 . ARG   A 1 568 ? -17.362 -0.028  51.785 1    45.024  ? 604 ARG   A NH1 1 
ATOM   4590 N  NH2 . ARG   A 1 568 ? -15.028 0.283   51.735 1    46.083  ? 604 ARG   A NH2 1 
ATOM   4591 N  N   . THR   A 1 569 ? -19.232 -6.89   54.811 1    28.862  ? 605 THR   A N   1 
ATOM   4592 C  CA  . THR   A 1 569 ? -19.806 -7.607  55.952 1    33.9    ? 605 THR   A CA  1 
ATOM   4593 C  C   . THR   A 1 569 ? -19.333 -9.066  55.956 1    31.398  ? 605 THR   A C   1 
ATOM   4594 O  O   . THR   A 1 569 ? -18.97  -9.612  56.999 1    28.437  ? 605 THR   A O   1 
ATOM   4595 C  CB  . THR   A 1 569 ? -21.341 -7.452  55.971 1    31.369  ? 605 THR   A CB  1 
ATOM   4596 O  OG1 . THR   A 1 569 ? -21.549 -6.035  56.167 1    30.485  ? 605 THR   A OG1 1 
ATOM   4597 C  CG2 . THR   A 1 569 ? -22.002 -8.324  57.029 1    24.518  ? 605 THR   A CG2 1 
ATOM   4598 N  N   . GLU   A 1 570 ? -19.285 -9.684  54.769 1    34.358  ? 606 GLU   A N   1 
ATOM   4599 C  CA  . GLU   A 1 570 ? -18.929 -11.097 54.641 1    33.707  ? 606 GLU   A CA  1 
ATOM   4600 C  C   . GLU   A 1 570 ? -17.43  -11.312 54.895 1    30.894  ? 606 GLU   A C   1 
ATOM   4601 O  O   . GLU   A 1 570 ? -17.06  -12.146 55.694 1    30.324  ? 606 GLU   A O   1 
ATOM   4602 C  CB  . GLU   A 1 570 ? -19.382 -11.559 53.253 1    33.778  ? 606 GLU   A CB  1 
ATOM   4603 C  CG  . GLU   A 1 570 ? -18.791 -12.914 52.875 1    36.147  ? 606 GLU   A CG  1 
ATOM   4604 C  CD  . GLU   A 1 570 ? -19.551 -14.022 53.596 1    40.222  ? 606 GLU   A CD  1 
ATOM   4605 O  OE1 . GLU   A 1 570 ? -20.533 -13.756 54.366 1    34.006  ? 606 GLU   A OE1 1 
ATOM   4606 O  OE2 . GLU   A 1 570 ? -19.148 -15.188 53.352 1    37.755  ? 606 GLU   A OE2 1 
ATOM   4607 N  N   . ASN   A 1 571 ? -16.577 -10.544 54.204 1    29.024  ? 607 ASN   A N   1 
ATOM   4608 C  CA  . ASN   A 1 571 ? -15.134 -10.524 54.365 1    27.741  ? 607 ASN   A CA  1 
ATOM   4609 C  C   . ASN   A 1 571 ? -14.769 -10.2   55.804 1    29.089  ? 607 ASN   A C   1 
ATOM   4610 O  O   . ASN   A 1 571 ? -13.788 -10.705 56.323 1    37.493  ? 607 ASN   A O   1 
ATOM   4611 C  CB  . ASN   A 1 571 ? -14.42  -9.576  53.389 1    24.649  ? 607 ASN   A CB  1 
ATOM   4612 C  CG  . ASN   A 1 571 ? -14.454 -10.031 51.939 1    29.574  ? 607 ASN   A CG  1 
ATOM   4613 O  OD1 . ASN   A 1 571 ? -14.759 -11.197 51.635 1    28.376  ? 607 ASN   A OD1 1 
ATOM   4614 N  ND2 . ASN   A 1 571 ? -14.177 -9.128  51.003 1    25.812  ? 607 ASN   A ND2 1 
ATOM   4615 N  N   . GLU   A 1 572 ? -15.557 -9.383  56.477 1    35.588  ? 608 GLU   A N   1 
ATOM   4616 C  CA  . GLU   A 1 572 ? -15.177 -9.013  57.839 1    39.74   ? 608 GLU   A CA  1 
ATOM   4617 C  C   . GLU   A 1 572 ? -15.474 -10.147 58.824 1    31.232  ? 608 GLU   A C   1 
ATOM   4618 O  O   . GLU   A 1 572 ? -14.716 -10.389 59.768 1    31.053  ? 608 GLU   A O   1 
ATOM   4619 C  CB  . GLU   A 1 572 ? -15.725 -7.617  58.147 1    47.977  ? 608 GLU   A CB  1 
ATOM   4620 C  CG  . GLU   A 1 572 ? -15.439 -7.108  59.555 1    63.688  ? 608 GLU   A CG  1 
ATOM   4621 C  CD  . GLU   A 1 572 ? -16.361 -5.927  59.834 1    75.699  ? 608 GLU   A CD  1 
ATOM   4622 O  OE1 . GLU   A 1 572 ? -16.107 -4.771  59.327 1    59.714  ? 608 GLU   A OE1 1 
ATOM   4623 O  OE2 . GLU   A 1 572 ? -17.379 -6.239  60.535 1    50.415  ? 608 GLU   A OE2 1 
ATOM   4624 N  N   . LEU   A 1 573 ? -16.548 -10.878 58.55  1    28.729  ? 609 LEU   A N   1 
ATOM   4625 C  CA  . LEU   A 1 573 ? -16.952 -11.998 59.393 1    31.197  ? 609 LEU   A CA  1 
ATOM   4626 C  C   . LEU   A 1 573 ? -15.844 -13.04  59.41  1    33.981  ? 609 LEU   A C   1 
ATOM   4627 O  O   . LEU   A 1 573 ? -15.616 -13.747 60.413 1    27.078  ? 609 LEU   A O   1 
ATOM   4628 C  CB  . LEU   A 1 573 ? -18.104 -12.542 58.57  1    28.677  ? 609 LEU   A CB  1 
ATOM   4629 C  CG  . LEU   A 1 573 ? -18.976 -13.623 59.172 1    40.878  ? 609 LEU   A CG  1 
ATOM   4630 C  CD1 . LEU   A 1 573 ? -19.573 -12.942 60.353 1    47.5    ? 609 LEU   A CD1 1 
ATOM   4631 C  CD2 . LEU   A 1 573 ? -20.067 -13.891 58.164 1    39.469  ? 609 LEU   A CD2 1 
ATOM   4632 N  N   . HIS   A 1 574 ? -15.217 -13.178 58.224 1    28.311  ? 610 HIS   A N   1 
ATOM   4633 C  CA  . HIS   A 1 574 ? -14.272 -14.244 58.02  1    23.232  ? 610 HIS   A CA  1 
ATOM   4634 C  C   . HIS   A 1 574 ? -12.861 -13.807 58.367 1    23.755  ? 610 HIS   A C   1 
ATOM   4635 O  O   . HIS   A 1 574 ? -11.99  -14.658 58.35  1    34.284  ? 610 HIS   A O   1 
ATOM   4636 C  CB  . HIS   A 1 574 ? -14.412 -14.841 56.632 1    22.643  ? 610 HIS   A CB  1 
ATOM   4637 C  CG  . HIS   A 1 574 ? -15.725 -15.468 56.385 1    28.5    ? 610 HIS   A CG  1 
ATOM   4638 N  ND1 . HIS   A 1 574 ? -16.178 -16.516 57.153 1    29.728  ? 610 HIS   A ND1 1 
ATOM   4639 C  CD2 . HIS   A 1 574 ? -16.675 -15.274 55.416 1    31.153  ? 610 HIS   A CD2 1 
ATOM   4640 C  CE1 . HIS   A 1 574 ? -17.387 -16.89  56.715 1    32.064  ? 610 HIS   A CE1 1 
ATOM   4641 N  NE2 . HIS   A 1 574 ? -17.682 -16.191 55.634 1    32.335  ? 610 HIS   A NE2 1 
ATOM   4642 N  N   . GLY   A 1 575 ? -12.652 -12.516 58.641 1    22.831  ? 611 GLY   A N   1 
ATOM   4643 C  CA  . GLY   A 1 575 ? -11.342 -11.974 58.981 1    24.716  ? 611 GLY   A CA  1 
ATOM   4644 C  C   . GLY   A 1 575 ? -10.428 -11.73  57.782 1    27.555  ? 611 GLY   A C   1 
ATOM   4645 O  O   . GLY   A 1 575 ? -9.211  -11.731 57.942 1    32.28   ? 611 GLY   A O   1 
ATOM   4646 N  N   . GLU   A 1 576 ? -10.978 -11.557 56.578 1    25.183  ? 612 GLU   A N   1 
ATOM   4647 C  CA  . GLU   A 1 576 ? -10.105 -11.501 55.408 1    27.471  ? 612 GLU   A CA  1 
ATOM   4648 C  C   . GLU   A 1 576 ? -9.057  -10.381 55.528 1    32.333  ? 612 GLU   A C   1 
ATOM   4649 O  O   . GLU   A 1 576 ? -9.35   -9.267  55.962 1    31.435  ? 612 GLU   A O   1 
ATOM   4650 C  CB  . GLU   A 1 576 ? -10.883 -11.329 54.101 1    22.34   ? 612 GLU   A CB  1 
ATOM   4651 C  CG  . GLU   A 1 576 ? -11.91  -12.413 53.836 1    21.553  ? 612 GLU   A CG  1 
ATOM   4652 C  CD  . GLU   A 1 576 ? -11.455 -13.861 53.757 1    23.91   ? 612 GLU   A CD  1 
ATOM   4653 O  OE1 . GLU   A 1 576 ? -10.207 -14.136 53.897 1    21.871  ? 612 GLU   A OE1 1 
ATOM   4654 O  OE2 . GLU   A 1 576 ? -12.394 -14.721 53.691 1    24.447  ? 612 GLU   A OE2 1 
ATOM   4655 N  N   . LYS   A 1 577 ? -7.81   -10.649 55.122 1    36.668  ? 613 LYS   A N   1 
ATOM   4656 C  CA  . LYS   A 1 577 ? -6.879  -9.54   54.915 1    35.975  ? 613 LYS   A CA  1 
ATOM   4657 C  C   . LYS   A 1 577 ? -6.922  -9.149  53.437 1    36.999  ? 613 LYS   A C   1 
ATOM   4658 O  O   . LYS   A 1 577 ? -6.432  -9.897  52.575 1    34.296  ? 613 LYS   A O   1 
ATOM   4659 C  CB  . LYS   A 1 577 ? -5.42   -9.845  55.296 1    42.871  ? 613 LYS   A CB  1 
ATOM   4660 C  CG  . LYS   A 1 577 ? -5.136  -9.987  56.779 1    56.444  ? 613 LYS   A CG  1 
ATOM   4661 C  CD  . LYS   A 1 577 ? -3.666  -9.74   57.123 1    69.053  ? 613 LYS   A CD  1 
ATOM   4662 C  CE  . LYS   A 1 577 ? -3.253  -10.229 58.512 1    77.225  ? 613 LYS   A CE  1 
ATOM   4663 N  NZ  . LYS   A 1 577 ? -4.161  -9.82   59.592 1    57.736  ? 613 LYS   A NZ  1 
ATOM   4664 N  N   . LEU   A 1 578 ? -7.572  -8.008  53.157 1    33.033  ? 614 LEU   A N   1 
ATOM   4665 C  CA  . LEU   A 1 578 ? -7.732  -7.512  51.803 1    29.68   ? 614 LEU   A CA  1 
ATOM   4666 C  C   . LEU   A 1 578 ? -6.341  -7.308  51.225 1    30.18   ? 614 LEU   A C   1 
ATOM   4667 O  O   . LEU   A 1 578 ? -5.475  -6.942  51.967 1    27.658  ? 614 LEU   A O   1 
ATOM   4668 C  CB  . LEU   A 1 578 ? -8.485  -6.195  51.866 1    23.362  ? 614 LEU   A CB  1 
ATOM   4669 C  CG  . LEU   A 1 578 ? -9.985  -6.279  52.185 1    26.12   ? 614 LEU   A CG  1 
ATOM   4670 C  CD1 . LEU   A 1 578 ? -10.564 -4.923  51.858 1    25.524  ? 614 LEU   A CD1 1 
ATOM   4671 C  CD2 . LEU   A 1 578 ? -10.911 -7.34   51.553 1    26.099  ? 614 LEU   A CD2 1 
ATOM   4672 N  N   . GLY   A 1 579 ? -6.126  -7.554  49.92  1    33.834  ? 615 GLY   A N   1 
ATOM   4673 C  CA  . GLY   A 1 579 ? -4.819  -7.338  49.327 1    25.327  ? 615 GLY   A CA  1 
ATOM   4674 C  C   . GLY   A 1 579 ? -3.927  -8.586  49.37  1    29.024  ? 615 GLY   A C   1 
ATOM   4675 O  O   . GLY   A 1 579 ? -4.393  -9.716  49.638 1    26.751  ? 615 GLY   A O   1 
ATOM   4676 N  N   . TRP   A 1 580 ? -2.645  -8.347  49.051 1    25.535  ? 616 TRP   A N   1 
ATOM   4677 C  CA  . TRP   A 1 580 ? -1.593  -9.344  48.899 1    40.714  ? 616 TRP   A CA  1 
ATOM   4678 C  C   . TRP   A 1 580 ? -0.254  -8.624  49.012 1    40.182  ? 616 TRP   A C   1 
ATOM   4679 O  O   . TRP   A 1 580 ? -0.247  -7.447  48.75  1    46.805  ? 616 TRP   A O   1 
ATOM   4680 C  CB  . TRP   A 1 580 ? -1.711  -9.998  47.519 1    26.403  ? 616 TRP   A CB  1 
ATOM   4681 C  CG  . TRP   A 1 580 ? -1.785  -8.947  46.455 1    30.489  ? 616 TRP   A CG  1 
ATOM   4682 C  CD1 . TRP   A 1 580 ? -0.768  -8.308  45.779 1    30.162  ? 616 TRP   A CD1 1 
ATOM   4683 C  CD2 . TRP   A 1 580 ? -3.017  -8.441  45.909 1    29.989  ? 616 TRP   A CD2 1 
ATOM   4684 N  NE1 . TRP   A 1 580 ? -1.278  -7.424  44.85  1    28.278  ? 616 TRP   A NE1 1 
ATOM   4685 C  CE2 . TRP   A 1 580 ? -2.658  -7.492  44.909 1    29.616  ? 616 TRP   A CE2 1 
ATOM   4686 C  CE3 . TRP   A 1 580 ? -4.366  -8.718  46.161 1    28.937  ? 616 TRP   A CE3 1 
ATOM   4687 C  CZ2 . TRP   A 1 580 ? -3.633  -6.793  44.199 1    30.074  ? 616 TRP   A CZ2 1 
ATOM   4688 C  CZ3 . TRP   A 1 580 ? -5.325  -8.058  45.423 1    28.58   ? 616 TRP   A CZ3 1 
ATOM   4689 C  CH2 . TRP   A 1 580 ? -4.961  -7.111  44.455 1    31.539  ? 616 TRP   A CH2 1 
ATOM   4690 N  N   . PRO   A 1 581 ? 0.911   -9.246  49.334 1    74.057  ? 617 PRO   A N   1 
ATOM   4691 C  CA  . PRO   A 1 581 ? 2.113   -8.465  49.691 1    82.794  ? 617 PRO   A CA  1 
ATOM   4692 C  C   . PRO   A 1 581 ? 3.078   -7.951  48.586 1    73.627  ? 617 PRO   A C   1 
ATOM   4693 O  O   . PRO   A 1 581 ? 2.691   -7.523  47.459 1    61.7    ? 617 PRO   A O   1 
ATOM   4694 C  CB  . PRO   A 1 581 ? 2.808   -9.438  50.694 1    86.689  ? 617 PRO   A CB  1 
ATOM   4695 C  CG  . PRO   A 1 581 ? 2.441   -10.842 50.198 1    82.942  ? 617 PRO   A CG  1 
ATOM   4696 C  CD  . PRO   A 1 581 ? 1.174   -10.702 49.343 1    81.126  ? 617 PRO   A CD  1 
HETATM 4697 C  C1  . NAG   B 2 .   ? -17.805 24.204  7.811  1    47.683  ? 1   NAG   B C1  1 
HETATM 4698 C  C2  . NAG   B 2 .   ? -19.202 24.804  8.061  1    48.613  ? 1   NAG   B C2  1 
HETATM 4699 C  C3  . NAG   B 2 .   ? -20.225 23.698  8.349  1    44.905  ? 1   NAG   B C3  1 
HETATM 4700 C  C4  . NAG   B 2 .   ? -20.159 22.587  7.305  1    46.189  ? 1   NAG   B C4  1 
HETATM 4701 C  C5  . NAG   B 2 .   ? -18.727 22.09   7.228  1    45.096  ? 1   NAG   B C5  1 
HETATM 4702 C  C6  . NAG   B 2 .   ? -18.57  20.907  6.304  1    41.648  ? 1   NAG   B C6  1 
HETATM 4703 C  C7  . NAG   B 2 .   ? -19.798 26.974  8.877  1    78.543  ? 1   NAG   B C7  1 
HETATM 4704 C  C8  . NAG   B 2 .   ? -21.062 27.41   9.575  1    70.687  ? 1   NAG   B C8  1 
HETATM 4705 N  N2  . NAG   B 2 .   ? -19.312 25.755  9.149  1    58.138  ? 1   NAG   B N2  1 
HETATM 4706 O  O3  . NAG   B 2 .   ? -21.553 24.178  8.487  1    43.103  ? 1   NAG   B O3  1 
HETATM 4707 O  O4  . NAG   B 2 .   ? -20.935 21.444  7.667  1    48.743  ? 1   NAG   B O4  1 
HETATM 4708 O  O5  . NAG   B 2 .   ? -17.883 23.185  6.803  1    39.242  ? 1   NAG   B O5  1 
HETATM 4709 O  O6  . NAG   B 2 .   ? -18.969 21.278  4.983  1    44.783  ? 1   NAG   B O6  1 
HETATM 4710 O  O7  . NAG   B 2 .   ? -19.24  27.686  8.049  1    73.859  ? 1   NAG   B O7  1 
HETATM 4711 C  C1  . NAG   B 2 .   ? -22.068 21.02   6.991  1    51.436  ? 2   NAG   B C1  1 
HETATM 4712 C  C2  . NAG   B 2 .   ? -22.476 19.694  7.611  1    57.388  ? 2   NAG   B C2  1 
HETATM 4713 C  C3  . NAG   B 2 .   ? -23.79  19.22   6.988  1    60.855  ? 2   NAG   B C3  1 
HETATM 4714 C  C4  . NAG   B 2 .   ? -24.882 20.267  7.096  1    62.647  ? 2   NAG   B C4  1 
HETATM 4715 C  C5  . NAG   B 2 .   ? -24.335 21.595  6.577  1    70.243  ? 2   NAG   B C5  1 
HETATM 4716 C  C6  . NAG   B 2 .   ? -25.272 22.772  6.711  1    59.019  ? 2   NAG   B C6  1 
HETATM 4717 C  C7  . NAG   B 2 .   ? -20.659 18.117  8.258  1    56.857  ? 2   NAG   B C7  1 
HETATM 4718 C  C8  . NAG   B 2 .   ? -19.941 16.899  7.759  1    52.823  ? 2   NAG   B C8  1 
HETATM 4719 N  N2  . NAG   B 2 .   ? -21.398 18.76   7.351  1    67.618  ? 2   NAG   B N2  1 
HETATM 4720 O  O3  . NAG   B 2 .   ? -24.286 17.985  7.491  1    69.234  ? 2   NAG   B O3  1 
HETATM 4721 O  O4  . NAG   B 2 .   ? -25.907 19.789  6.218  1    71.688  ? 2   NAG   B O4  1 
HETATM 4722 O  O5  . NAG   B 2 .   ? -23.094 21.967  7.223  1    62.77   ? 2   NAG   B O5  1 
HETATM 4723 O  O6  . NAG   B 2 .   ? -24.926 23.658  5.63   1    58.836  ? 2   NAG   B O6  1 
HETATM 4724 O  O7  . NAG   B 2 .   ? -20.556 18.514  9.413  1    54.593  ? 2   NAG   B O7  1 
HETATM 4725 C  C1  . BMA   B 2 .   ? -27.071 19.137  6.625  1    82.184  ? 3   BMA   B C1  1 
HETATM 4726 C  C2  . BMA   B 2 .   ? -28.265 20.067  6.379  1    86.703  ? 3   BMA   B C2  1 
HETATM 4727 C  C3  . BMA   B 2 .   ? -29.581 19.365  6.776  1    73.057  ? 3   BMA   B C3  1 
HETATM 4728 C  C4  . BMA   B 2 .   ? -29.711 18.07   5.98   1    76.046  ? 3   BMA   B C4  1 
HETATM 4729 C  C5  . BMA   B 2 .   ? -28.449 17.156  6.183  1    80.562  ? 3   BMA   B C5  1 
HETATM 4730 C  C6  . BMA   B 2 .   ? -28.415 15.919  5.309  1    76.847  ? 3   BMA   B C6  1 
HETATM 4731 O  O2  . BMA   B 2 .   ? -28.26  20.488  5.01   1    86.79   ? 3   BMA   B O2  1 
HETATM 4732 O  O3  . BMA   B 2 .   ? -30.734 20.2    6.605  1    56.286  ? 3   BMA   B O3  1 
HETATM 4733 O  O4  . BMA   B 2 .   ? -30.927 17.433  6.339  1    68.292  ? 3   BMA   B O4  1 
HETATM 4734 O  O5  . BMA   B 2 .   ? -27.22  17.91   5.896  1    80.112  ? 3   BMA   B O5  1 
HETATM 4735 O  O6  . BMA   B 2 .   ? -27.07  15.574  5.017  1    89.661  ? 3   BMA   B O6  1 
HETATM 4736 C  C1  . FUC   B 2 .   ? -19.47  20.201  4.251  0.89 46.818  ? 4   FUC   B C1  1 
HETATM 4737 C  C2  . FUC   B 2 .   ? -20.309 20.754  3.097  0.89 49.13   ? 4   FUC   B C2  1 
HETATM 4738 C  C3  . FUC   B 2 .   ? -19.569 21.697  2.235  0.89 45.352  ? 4   FUC   B C3  1 
HETATM 4739 C  C4  . FUC   B 2 .   ? -18.165 21.211  1.865  0.89 39.809  ? 4   FUC   B C4  1 
HETATM 4740 C  C5  . FUC   B 2 .   ? -17.435 20.513  3.019  0.89 43.282  ? 4   FUC   B C5  1 
HETATM 4741 C  C6  . FUC   B 2 .   ? -16.226 19.729  2.539  0.89 34.32   ? 4   FUC   B C6  1 
HETATM 4742 O  O2  . FUC   B 2 .   ? -21.458 21.487  3.513  0.89 58.242  ? 4   FUC   B O2  1 
HETATM 4743 O  O3  . FUC   B 2 .   ? -20.428 21.717  1.107  0.89 38.504  ? 4   FUC   B O3  1 
HETATM 4744 O  O4  . FUC   B 2 .   ? -18.254 20.299  0.791  0.89 38.885  ? 4   FUC   B O4  1 
HETATM 4745 O  O5  . FUC   B 2 .   ? -18.3   19.58   3.733  0.89 41.981  ? 4   FUC   B O5  1 
HETATM 4746 ZN ZN  . ZN    C 3 .   ? -15.454 -3.931  20.732 1    25.838  ? 701 ZN    A ZN  1 
HETATM 4747 CL CL  . CL    D 4 .   ? -7.775  2.991   22.752 1    27.409  ? 702 CL    A CL  1 
HETATM 4748 CL CL  . CL    E 4 .   ? -0.629  -14.056 31.273 1    24.813  ? 703 CL    A CL  1 
HETATM 4749 C  C11 . A1IJY F 5 .   ? -13.879 -5.223  16.716 1    32.156  ? 704 A1IJY A C11 1 
HETATM 4750 O  O01 . A1IJY F 5 .   ? -11.77  -8.262  21.941 1    24.419  ? 704 A1IJY A O01 1 
HETATM 4751 C  C02 . A1IJY F 5 .   ? -12.905 -7.991  22.202 1    24.419  ? 704 A1IJY A C02 1 
HETATM 4752 C  C03 . A1IJY F 5 .   ? -14.02  -8.129  21.176 1    24.295  ? 704 A1IJY A C03 1 
HETATM 4753 N  N04 . A1IJY F 5 .   ? -13.417 -8.15   19.853 1    23.17   ? 704 A1IJY A N04 1 
HETATM 4754 C  C05 . A1IJY F 5 .   ? -12.925 -6.908  19.456 1    28.487  ? 704 A1IJY A C05 1 
HETATM 4755 C  C06 . A1IJY F 5 .   ? -12.62  -6.956  17.915 1    28.544  ? 704 A1IJY A C06 1 
HETATM 4756 C  C07 . A1IJY F 5 .   ? -11.112 -7.29   17.566 1    30.263  ? 704 A1IJY A C07 1 
HETATM 4757 C  C08 . A1IJY F 5 .   ? -10.402 -5.867  17.727 1    30.213  ? 704 A1IJY A C08 1 
HETATM 4758 C  C09 . A1IJY F 5 .   ? -11.415 -4.888  17.728 1    23.908  ? 704 A1IJY A C09 1 
HETATM 4759 N  N10 . A1IJY F 5 .   ? -12.739 -5.729  17.45  1    26.35   ? 704 A1IJY A N10 1 
HETATM 4760 C  C12 . A1IJY F 5 .   ? -13.838 -3.74   16.293 1    31.484  ? 704 A1IJY A C12 1 
HETATM 4761 C  C13 . A1IJY F 5 .   ? -13.661 -2.714  17.298 1    28.56   ? 704 A1IJY A C13 1 
HETATM 4762 C  C14 . A1IJY F 5 .   ? -13.62  -1.348  16.944 1    24.303  ? 704 A1IJY A C14 1 
HETATM 4763 C  C15 . A1IJY F 5 .   ? -13.805 -1.064  15.542 1    33.692  ? 704 A1IJY A C15 1 
HETATM 4764 C  C16 . A1IJY F 5 .   ? -13.89  0.348   14.906 1    34.401  ? 704 A1IJY A C16 1 
HETATM 4765 O  O17 . A1IJY F 5 .   ? -14.179 0.348   13.708 1    40.152  ? 704 A1IJY A O17 1 
HETATM 4766 O  O18 . A1IJY F 5 .   ? -13.836 1.467   15.463 1    37.168  ? 704 A1IJY A O18 1 
HETATM 4767 C  C19 . A1IJY F 5 .   ? -14.009 -2.079  14.563 1    30.124  ? 704 A1IJY A C19 1 
HETATM 4768 C  C20 . A1IJY F 5 .   ? -13.992 -3.434  14.941 1    31.044  ? 704 A1IJY A C20 1 
HETATM 4769 O  O21 . A1IJY F 5 .   ? -14.844 -5.91   16.475 1    29.227  ? 704 A1IJY A O21 1 
HETATM 4770 C  C22 . A1IJY F 5 .   ? -13.99  -5.867  19.887 1    31.405  ? 704 A1IJY A C22 1 
HETATM 4771 O  O23 . A1IJY F 5 .   ? -13.66  -4.867  20.623 1    35.418  ? 704 A1IJY A O23 1 
HETATM 4772 O  O24 . A1IJY F 5 .   ? -15.19  -5.949  19.507 1    28.062  ? 704 A1IJY A O24 1 
HETATM 4773 C  C25 . A1IJY F 5 .   ? -14.493 -9.588  21.399 1    21.282  ? 704 A1IJY A C25 1 
HETATM 4774 N  N26 . A1IJY F 5 .   ? -13.267 -7.614  23.513 1    21.475  ? 704 A1IJY A N26 1 
HETATM 4775 C  C27 . A1IJY F 5 .   ? -14.787 -7.314  23.77  1    21.011  ? 704 A1IJY A C27 1 
HETATM 4776 C  C28 . A1IJY F 5 .   ? -14.827 -6.907  25.133 1    25.01   ? 704 A1IJY A C28 1 
HETATM 4777 C  C29 . A1IJY F 5 .   ? -13.497 -7.321  25.848 1    21.166  ? 704 A1IJY A C29 1 
HETATM 4778 C  C30 . A1IJY F 5 .   ? -12.469 -7.495  24.653 1    20.908  ? 704 A1IJY A C30 1 
HETATM 4779 C  C31 . A1IJY F 5 .   ? -11.692 -8.785  25.001 1    26.342  ? 704 A1IJY A C31 1 
HETATM 4780 O  O32 . A1IJY F 5 .   ? -10.54  -8.883  25.464 1    31.86   ? 704 A1IJY A O32 1 
HETATM 4781 O  O33 . A1IJY F 5 .   ? -12.17  -9.929  24.859 1    32.59   ? 704 A1IJY A O33 1 
HETATM 4782 O  O   . HOH   G 6 .   ? -6.826  10.245  -6.144 1    28.551  ? 801 HOH   A O   1 
HETATM 4783 O  O   . HOH   G 6 .   ? -10.693 13.201  31.083 1    38.96   ? 802 HOH   A O   1 
HETATM 4784 O  O   . HOH   G 6 .   ? -22.373 -12.224 54.753 1    38.347  ? 803 HOH   A O   1 
HETATM 4785 O  O   . HOH   G 6 .   ? -27.971 -1.008  42.285 1    30.856  ? 804 HOH   A O   1 
HETATM 4786 O  O   . HOH   G 6 .   ? -10.852 -31.188 33.572 1    26.556  ? 805 HOH   A O   1 
HETATM 4787 O  O   . HOH   G 6 .   ? 1.801   -30.809 37.566 1    25.929  ? 806 HOH   A O   1 
HETATM 4788 O  O   . HOH   G 6 .   ? -1.205  -22.517 50.934 1    30.587  ? 807 HOH   A O   1 
HETATM 4789 O  O   . HOH   G 6 .   ? -27.827 -4.681  34.746 1    32.047  ? 808 HOH   A O   1 
HETATM 4790 O  O   . HOH   G 6 .   ? -10.336 -21.404 35.308 1    31.313  ? 809 HOH   A O   1 
HETATM 4791 O  O   . HOH   G 6 .   ? -19.896 9.869   18.689 1    32.488  ? 810 HOH   A O   1 
HETATM 4792 O  O   . HOH   G 6 .   ? -13.021 1.319   20.085 1    25.674  ? 811 HOH   A O   1 
HETATM 4793 O  O   . HOH   G 6 .   ? 9.17    7.797   23.825 1    26.777  ? 812 HOH   A O   1 
HETATM 4794 O  O   . HOH   G 6 .   ? -11.674 -22.684 38.739 1    24.781  ? 813 HOH   A O   1 
HETATM 4795 O  O   . HOH   G 6 .   ? -31.341 -8.657  23.032 1    30.601  ? 814 HOH   A O   1 
HETATM 4796 O  O   . HOH   G 6 .   ? -11.501 -6.388  -2.38  1    52.572  ? 815 HOH   A O   1 
HETATM 4797 O  O   . HOH   G 6 .   ? -10.886 -18.196 28.327 1    18.225  ? 816 HOH   A O   1 
HETATM 4798 O  O   . HOH   G 6 .   ? -29.778 -3      35.257 1    37.326  ? 817 HOH   A O   1 
HETATM 4799 O  O   . HOH   G 6 .   ? -16.597 7.358   -3.68  1    41.729  ? 818 HOH   A O   1 
HETATM 4800 O  O   . HOH   G 6 .   ? -14.271 0.366   45.009 1    51.394  ? 819 HOH   A O   1 
HETATM 4801 O  O   . HOH   G 6 .   ? 14.925  2.476   25.954 1    31.556  ? 820 HOH   A O   1 
HETATM 4802 O  O   . HOH   G 6 .   ? -11.212 -12.335 24.763 1    29.033  ? 821 HOH   A O   1 
HETATM 4803 O  O   . HOH   G 6 .   ? 8.245   -10.081 37.463 1    37.919  ? 822 HOH   A O   1 
HETATM 4804 O  O   . HOH   G 6 .   ? -7.044  17.11   29.758 1    36.582  ? 823 HOH   A O   1 
HETATM 4805 O  O   . HOH   G 6 .   ? -14.219 4.343   46.12  1    27.871  ? 824 HOH   A O   1 
HETATM 4806 O  O   . HOH   G 6 .   ? 4.55    -17.307 26.585 1    18.723  ? 825 HOH   A O   1 
HETATM 4807 O  O   . HOH   G 6 .   ? 0.893   -4.769  20.361 1    24.046  ? 826 HOH   A O   1 
HETATM 4808 O  O   . HOH   G 6 .   ? -28.894 -19.309 50.661 1    39.246  ? 827 HOH   A O   1 
HETATM 4809 O  O   . HOH   G 6 .   ? -14.073 0.574   11.097 1    29.397  ? 828 HOH   A O   1 
HETATM 4810 O  O   . HOH   G 6 .   ? -4.768  -0.715  29.196 1    28.69   ? 829 HOH   A O   1 
HETATM 4811 O  O   . HOH   G 6 .   ? -1.328  -8.269  13.762 1    31.142  ? 830 HOH   A O   1 
HETATM 4812 O  O   . HOH   G 6 .   ? 11.812  2.594   16.252 1    23.842  ? 831 HOH   A O   1 
HETATM 4813 O  O   . HOH   G 6 .   ? -17.449 -2.956  -3.829 1    49.853  ? 832 HOH   A O   1 
HETATM 4814 O  O   . HOH   G 6 .   ? -8.484  -14.525 21.431 1    32.298  ? 833 HOH   A O   1 
HETATM 4815 O  O   . HOH   G 6 .   ? -22.536 -5.649  29.304 1    35.953  ? 834 HOH   A O   1 
HETATM 4816 O  O   . HOH   G 6 .   ? -29.647 -3.153  15.107 1    24.751  ? 835 HOH   A O   1 
HETATM 4817 O  O   . HOH   G 6 .   ? -9.157  -13.954 51.201 1    21.094  ? 836 HOH   A O   1 
HETATM 4818 O  O   . HOH   G 6 .   ? -7.721  -13.244 54.165 1    24.961  ? 837 HOH   A O   1 
HETATM 4819 O  O   . HOH   G 6 .   ? -12.768 17.708  -7.491 1    37.808  ? 838 HOH   A O   1 
HETATM 4820 O  O   . HOH   G 6 .   ? -16.031 2.579   10.731 1    24.595  ? 839 HOH   A O   1 
HETATM 4821 O  O   . HOH   G 6 .   ? 11.166  -1.866  24.088 1    19.325  ? 840 HOH   A O   1 
HETATM 4822 O  O   . HOH   G 6 .   ? -8.242  -18.029 34.956 1    13.551  ? 841 HOH   A O   1 
HETATM 4823 O  O   . HOH   G 6 .   ? -1.508  -13.472 28.102 1    18.813  ? 842 HOH   A O   1 
HETATM 4824 O  O   . HOH   G 6 .   ? -36.193 -0.685  34.503 1    35.587  ? 843 HOH   A O   1 
HETATM 4825 O  O   . HOH   G 6 .   ? -16.909 -2.811  26.302 1    25.376  ? 844 HOH   A O   1 
HETATM 4826 O  O   . HOH   G 6 .   ? -5.19   12.206  24.525 1    29.978  ? 845 HOH   A O   1 
HETATM 4827 O  O   . HOH   G 6 .   ? -26.96  -2.311  15.573 1    34.498  ? 846 HOH   A O   1 
HETATM 4828 O  O   . HOH   G 6 .   ? 4.215   5.307   25.228 1    16.276  ? 847 HOH   A O   1 
HETATM 4829 O  O   . HOH   G 6 .   ? -40.684 5.69    24.826 1    47.25   ? 848 HOH   A O   1 
HETATM 4830 O  O   . HOH   G 6 .   ? -0.602  -24.713 15.181 1    38.283  ? 849 HOH   A O   1 
HETATM 4831 O  O   . HOH   G 6 .   ? -19.835 2.873   5.886  1    27.426  ? 850 HOH   A O   1 
HETATM 4832 O  O   . HOH   G 6 .   ? -19.22  4.694   36.265 1    26.282  ? 851 HOH   A O   1 
HETATM 4833 O  O   . HOH   G 6 .   ? -17.073 3.137   -0.765 1    42.323  ? 852 HOH   A O   1 
HETATM 4834 O  O   . HOH   G 6 .   ? -3.148  2.874   24.421 1    24.832  ? 853 HOH   A O   1 
HETATM 4835 O  O   . HOH   G 6 .   ? -19.36  5.773   2.205  1    44.693  ? 854 HOH   A O   1 
HETATM 4836 O  O   . HOH   G 6 .   ? -8.669  -9.273  37.715 1    18.029  ? 855 HOH   A O   1 
HETATM 4837 O  O   . HOH   G 6 .   ? -23.696 8.153   40.163 1    36.22   ? 856 HOH   A O   1 
HETATM 4838 O  O   . HOH   G 6 .   ? -3.679  -9.987  52.25  1    50.156  ? 857 HOH   A O   1 
HETATM 4839 O  O   . HOH   G 6 .   ? -35.451 6.525   19.756 1    30.551  ? 858 HOH   A O   1 
HETATM 4840 O  O   . HOH   G 6 .   ? -4.5    -16.126 33.214 1    29.304  ? 859 HOH   A O   1 
HETATM 4841 O  O   . HOH   G 6 .   ? -16.688 -21.097 23.416 1    35.252  ? 860 HOH   A O   1 
HETATM 4842 O  O   . HOH   G 6 .   ? -29.221 -0.498  29.734 1    25.876  ? 861 HOH   A O   1 
HETATM 4843 O  O   . HOH   G 6 .   ? -19.073 4.116   -1.078 1    35.874  ? 862 HOH   A O   1 
HETATM 4844 O  O   . HOH   G 6 .   ? -17.731 13.587  18.333 1    30.019  ? 863 HOH   A O   1 
HETATM 4845 O  O   . HOH   G 6 .   ? 4.592   -7.375  3.318  1    37.843  ? 864 HOH   A O   1 
HETATM 4846 O  O   . HOH   G 6 .   ? -8.056  -8.624  48.3   1    23.134  ? 865 HOH   A O   1 
HETATM 4847 O  O   . HOH   G 6 .   ? -14.875 -14.09  52.714 1    21.339  ? 866 HOH   A O   1 
HETATM 4848 O  O   . HOH   G 6 .   ? -12.642 7.19    18.349 1    31.749  ? 867 HOH   A O   1 
HETATM 4849 O  O   . HOH   G 6 .   ? -5.095  4.691   23.149 1    28.395  ? 868 HOH   A O   1 
HETATM 4850 O  O   . HOH   G 6 .   ? -25.054 -4.819  5.564  1    43.219  ? 869 HOH   A O   1 
HETATM 4851 O  O   . HOH   G 6 .   ? 2.718   4.11    14.763 1    24.428  ? 870 HOH   A O   1 
HETATM 4852 O  O   . HOH   G 6 .   ? -20.342 -1.9    21.192 1    29.281  ? 871 HOH   A O   1 
HETATM 4853 O  O   . HOH   G 6 .   ? -11.984 14.344  21.707 1    32.752  ? 872 HOH   A O   1 
HETATM 4854 O  O   . HOH   G 6 .   ? 9.929   6.06    19.46  1    29.632  ? 873 HOH   A O   1 
HETATM 4855 O  O   . HOH   G 6 .   ? -20.528 0.136   5.003  1    27.795  ? 874 HOH   A O   1 
HETATM 4856 O  O   . HOH   G 6 .   ? -20.115 3.82    8.417  1    24.012  ? 875 HOH   A O   1 
HETATM 4857 O  O   . HOH   G 6 .   ? -24.745 9.205   34.342 1    23.481  ? 876 HOH   A O   1 
HETATM 4858 O  O   . HOH   G 6 .   ? -14.213 16.031  30.257 1    21.535  ? 877 HOH   A O   1 
HETATM 4859 O  O   . HOH   G 6 .   ? -23.311 -17.395 9.6    1    41.487  ? 878 HOH   A O   1 
HETATM 4860 O  O   . HOH   G 6 .   ? 11.885  -9.152  16.279 1    36.885  ? 879 HOH   A O   1 
HETATM 4861 O  O   . HOH   G 6 .   ? 5.554   8.355   25.771 1    30.136  ? 880 HOH   A O   1 
HETATM 4862 O  O   . HOH   G 6 .   ? -14.895 -0.235  -3.899 1    53.662  ? 881 HOH   A O   1 
HETATM 4863 O  O   . HOH   G 6 .   ? -21.586 6.402   43.64  1    24.999  ? 882 HOH   A O   1 
HETATM 4864 O  O   . HOH   G 6 .   ? -27.554 -20.117 13.588 1    50.022  ? 883 HOH   A O   1 
HETATM 4865 O  O   . HOH   G 6 .   ? -18.497 -3.986  0.141  1    37.21   ? 884 HOH   A O   1 
HETATM 4866 O  O   . HOH   G 6 .   ? -10.917 15.926  27.051 1    28.856  ? 885 HOH   A O   1 
HETATM 4867 O  O   . HOH   G 6 .   ? -36.143 -19.191 25.051 1    41.791  ? 886 HOH   A O   1 
HETATM 4868 O  O   . HOH   G 6 .   ? -24.174 -7.485  30.888 1    28.205  ? 887 HOH   A O   1 
HETATM 4869 O  O   . HOH   G 6 .   ? -11.063 15.7    24.087 1    34.332  ? 888 HOH   A O   1 
HETATM 4870 O  O   . HOH   G 6 .   ? -13.773 -5.728  53.942 1    43.397  ? 889 HOH   A O   1 
HETATM 4871 O  O   . HOH   G 6 .   ? -24.286 9.607   9.566  1    34.9    ? 890 HOH   A O   1 
HETATM 4872 O  O   . HOH   G 6 .   ? 12.836  -11.897 20.033 1    39.044  ? 891 HOH   A O   1 
HETATM 4873 O  O   . HOH   G 6 .   ? 12.207  -3.348  19.978 1    21.775  ? 892 HOH   A O   1 
HETATM 4874 O  O   . HOH   G 6 .   ? -11.044 -2.44   19.765 1    36.394  ? 893 HOH   A O   1 
HETATM 4875 O  O   . HOH   G 6 .   ? -11.445 11.677  21.214 1    26.953  ? 894 HOH   A O   1 
HETATM 4876 O  O   . HOH   G 6 .   ? -19.765 -9.033  59.666 1    30.578  ? 895 HOH   A O   1 
HETATM 4877 O  O   . HOH   G 6 .   ? -20.588 -23.076 26.43  1    28.515  ? 896 HOH   A O   1 
HETATM 4878 O  O   . HOH   G 6 .   ? 10.646  4.939   22.096 1    28.142  ? 897 HOH   A O   1 
HETATM 4879 O  O   . HOH   G 6 .   ? -3.459  -19.541 53.512 1    31.851  ? 898 HOH   A O   1 
HETATM 4880 O  O   . HOH   G 6 .   ? -26.563 -4.948  50.589 1    26.545  ? 899 HOH   A O   1 
HETATM 4881 O  O   . HOH   G 6 .   ? -13.164 -19.601 29.231 1    20.998  ? 900 HOH   A O   1 
HETATM 4882 O  O   . HOH   G 6 .   ? -0.863  11.973  22.984 1    26.486  ? 901 HOH   A O   1 
HETATM 4883 O  O   . HOH   G 6 .   ? -0.27   -8.701  51.905 1    50.948  ? 902 HOH   A O   1 
HETATM 4884 O  O   . HOH   G 6 .   ? 7.632   -16.887 37.67  1    30.834  ? 903 HOH   A O   1 
HETATM 4885 O  O   . HOH   G 6 .   ? 8.398   12.96   16.152 1    34.707  ? 904 HOH   A O   1 
HETATM 4886 O  O   . HOH   G 6 .   ? -12.186 -13.435 27.246 1    28.384  ? 905 HOH   A O   1 
HETATM 4887 O  O   . HOH   G 6 .   ? -13.236 -2.037  52.05  1    35.845  ? 906 HOH   A O   1 
HETATM 4888 O  O   . HOH   G 6 .   ? -13.181 13.157  32.569 1    26.018  ? 907 HOH   A O   1 
HETATM 4889 O  O   . HOH   G 6 .   ? -16.488 -16.02  52.532 1    28.763  ? 908 HOH   A O   1 
HETATM 4890 O  O   . HOH   G 6 .   ? -14.62  -16.691 33.849 1    21.83   ? 909 HOH   A O   1 
HETATM 4891 O  O   . HOH   G 6 .   ? -13.989 -13.739 20.33  1    29.565  ? 910 HOH   A O   1 
HETATM 4892 O  O   . HOH   G 6 .   ? -22.273 10.409  34.736 1    21.235  ? 911 HOH   A O   1 
HETATM 4893 O  O   . HOH   G 6 .   ? -15.986 -4.995  -0.268 1    37.179  ? 912 HOH   A O   1 
HETATM 4894 O  O   . HOH   G 6 .   ? 11.131  -11.178 29.335 1    37.301  ? 913 HOH   A O   1 
HETATM 4895 O  O   . HOH   G 6 .   ? -14.37  9.05    28.019 1    25.358  ? 914 HOH   A O   1 
HETATM 4896 O  O   . HOH   G 6 .   ? -22.918 -24.004 21.085 1    36.485  ? 915 HOH   A O   1 
HETATM 4897 O  O   . HOH   G 6 .   ? 0.874   -20.915 15.768 1    32.531  ? 916 HOH   A O   1 
HETATM 4898 O  O   . HOH   G 6 .   ? 11.378  -3.683  22.673 1    21.375  ? 917 HOH   A O   1 
HETATM 4899 O  O   . HOH   G 6 .   ? -8.052  -27.432 52.435 1    25.704  ? 918 HOH   A O   1 
HETATM 4900 O  O   . HOH   G 6 .   ? -16.99  14.42   -1.393 1    35.591  ? 919 HOH   A O   1 
HETATM 4901 O  O   . HOH   G 6 .   ? -4.464  -21.83  53.057 1    27.263  ? 920 HOH   A O   1 
HETATM 4902 O  O   . HOH   G 6 .   ? 11.698  2.177   19.261 1    18.599  ? 921 HOH   A O   1 
HETATM 4903 O  O   . HOH   G 6 .   ? -31.425 6.202   14.895 1    36.839  ? 922 HOH   A O   1 
HETATM 4904 O  O   . HOH   G 6 .   ? 0.796   -24.158 17.669 1    35.673  ? 923 HOH   A O   1 
HETATM 4905 O  O   . HOH   G 6 .   ? -19.929 -0.942  -2.979 1    40.576  ? 924 HOH   A O   1 
HETATM 4906 O  O   . HOH   G 6 .   ? -19.111 -21.697 16.057 1    35.111  ? 925 HOH   A O   1 
HETATM 4907 O  O   . HOH   G 6 .   ? -16.049 -17.239 49.841 1    26.431  ? 926 HOH   A O   1 
HETATM 4908 O  O   . HOH   G 6 .   ? -14.171 -11.666 28.536 1    38.283  ? 927 HOH   A O   1 
HETATM 4909 O  O   . HOH   G 6 .   ? -23.136 -9.967  54.094 1    32.173  ? 928 HOH   A O   1 
HETATM 4910 O  O   . HOH   G 6 .   ? -22.805 -3.109  -0.198 1    39.194  ? 929 HOH   A O   1 
HETATM 4911 O  O   . HOH   G 6 .   ? -20.789 -3.146  55.018 1    43.616  ? 930 HOH   A O   1 
HETATM 4912 O  O   . HOH   G 6 .   ? -16.81  26.199  11.089 1    41.551  ? 931 HOH   A O   1 
HETATM 4913 O  O   . HOH   G 6 .   ? 1       7.083   14.088 1    32.701  ? 932 HOH   A O   1 
HETATM 4914 O  O   . HOH   G 6 .   ? -13.425 -31.074 35.94  1    39.612  ? 933 HOH   A O   1 
HETATM 4915 O  O   . HOH   G 6 .   ? -27.102 -12.589 34.1   1    40.454  ? 934 HOH   A O   1 
HETATM 4916 O  O   . HOH   G 6 .   ? -10.872 11.13   36.522 1    40.046  ? 935 HOH   A O   1 
HETATM 4917 O  O   . HOH   G 6 .   ? -26.807 11.101  34.342 1    30.673  ? 936 HOH   A O   1 
HETATM 4918 O  O   . HOH   G 6 .   ? -11.045 -10.608 14.062 1    34.365  ? 937 HOH   A O   1 
HETATM 4919 O  O   . HOH   G 6 .   ? 3.258   11.739  25.824 1    49.741  ? 938 HOH   A O   1 
HETATM 4920 O  O   . HOH   G 6 .   ? -17.759 11.306  -0.82  1    39.948  ? 939 HOH   A O   1 
HETATM 4921 O  O   . HOH   G 6 .   ? -18.809 -11.841 27.533 1    32.539  ? 940 HOH   A O   1 
HETATM 4922 O  O   . HOH   G 6 .   ? 6.385   -7.696  41.194 1    30.524  ? 941 HOH   A O   1 
HETATM 4923 O  O   . HOH   G 6 .   ? 2.48    -17.28  10.618 1    43.901  ? 942 HOH   A O   1 
HETATM 4924 O  O   . HOH   G 6 .   ? 3.034   -5.42   2.286  1    43.244  ? 943 HOH   A O   1 
HETATM 4925 O  O   . HOH   G 6 .   ? -9.088  -11.449 -0.693 1    34.2    ? 944 HOH   A O   1 
HETATM 4926 O  O   . HOH   G 6 .   ? -12.009 -7.045  55.343 1    39.106  ? 945 HOH   A O   1 
HETATM 4927 O  O   . HOH   G 6 .   ? -3.14   6.439   -4.634 1    35.912  ? 946 HOH   A O   1 
HETATM 4928 O  O   . HOH   G 6 .   ? -16.967 14.916  1.479  1    39.166  ? 947 HOH   A O   1 
HETATM 4929 O  O   . HOH   G 6 .   ? -0.612  -20.154 53.217 1    39.224  ? 948 HOH   A O   1 
HETATM 4930 O  O   . HOH   G 6 .   ? 2.865   0.949   35.08  1    32.957  ? 949 HOH   A O   1 
HETATM 4931 O  O   . HOH   G 6 .   ? -16.036 29.01   9.536  1    41.424  ? 950 HOH   A O   1 
HETATM 4932 O  O   . HOH   G 6 .   ? -6.588  -14.1   56.61  1    28.333  ? 951 HOH   A O   1 
HETATM 4933 O  O   . HOH   G 6 .   ? -8.674  17.724  27.692 1    32.551  ? 952 HOH   A O   1 
HETATM 4934 O  O   . HOH   G 6 .   ? -14.873 -20.012 22.057 1    29.788  ? 953 HOH   A O   1 
HETATM 4935 O  O   . HOH   G 6 .   ? -12.902 -32.136 34.098 1    34.18   ? 954 HOH   A O   1 
HETATM 4936 O  O   . HOH   G 6 .   ? 5.884   10.882  25.938 1    30.507  ? 955 HOH   A O   1 
HETATM 4937 O  O   . HOH   G 6 .   ? 2.327   -20.969 13.772 1    37.493  ? 956 HOH   A O   1 
HETATM 4938 O  O   . HOH   G 6 .   ? -15.952 2.51    47.356 1    38.047  ? 957 HOH   A O   1 
HETATM 4939 O  O   . HOH   G 6 .   ? -11.956 15.604  29.621 1    24.424  ? 958 HOH   A O   1 
# 
