data_9EBX
# 
_entry.id   9EBX 
# 
_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   9EBX         pdb_00009ebx 10.2210/pdb9ebx/pdb 
WWPDB D_1000289871 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-03-19 
_pdbx_audit_revision_history.part_number         ? 
# 
_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_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9EBX 
_pdbx_database_status.recvd_initial_deposition_date   2024-11-13 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_database_related.db_name        PDB 
_pdbx_database_related.details        '9EBW contains the same protein complexed with lactate' 
_pdbx_database_related.db_id          9EBW 
_pdbx_database_related.content_type   unspecified 
# 
loop_
_pdbx_contact_author.id 
_pdbx_contact_author.email 
_pdbx_contact_author.name_first 
_pdbx_contact_author.name_last 
_pdbx_contact_author.name_mi 
_pdbx_contact_author.role 
_pdbx_contact_author.identifier_ORCID 
2 katherine.davis@emory.edu   Katherine Davis  M 'principal investigator/group leader' 0000-0002-0258-8907 
3 gary_yellen@hms.harvard.edu Gary      Yellen ? 'principal investigator/group leader' 0000-0003-4228-7866 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Horwitz, S.M.'  1 0000-0002-5407-7674 
'Ambarian, J.A.' 2 0000-0002-1465-8423 
'Waidmann, L.'   3 0000-0002-9579-9622 
'Davis, K.M.'    4 0000-0002-0258-8907 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Proc.Natl.Acad.Sci.USA 
_citation.journal_id_ASTM           PNASA6 
_citation.journal_id_CSD            0040 
_citation.journal_id_ISSN           1091-6490 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            122 
_citation.language                  ? 
_citation.page_first                e2426324122 
_citation.page_last                 e2426324122 
_citation.title                     'State-dependent motion of a genetically encoded fluorescent biosensor.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1073/pnas.2426324122 
_citation.pdbx_database_id_PubMed   40048274 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Rosen, P.C.'    1 0000-0001-7414-454X 
primary 'Horwitz, S.M.'  2 ?                   
primary 'Brooks, D.J.'   3 ?                   
primary 'Kim, E.'        4 ?                   
primary 'Ambarian, J.A.' 5 ?                   
primary 'Waidmann, L.'   6 ?                   
primary 'Davis, K.M.'    7 ?                   
primary 'Yellen, G.'     8 0000-0003-4228-7866 
# 
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 'Green fluorescent protein,Methyl-accepting chemotaxis transducer (TlpC)' 58440.969 1 ? ? ? 
;mTurquoise GFP (residues 10-153 and 428-515) attached to lactate binding protein TlpC (residues 159-421) by two separate linkers, one from residues 154-158 and another from residues 425-427
;
2 water   nat water                                                                     18.015    9 ? ? ? ? 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   yes 
_entity_poly.pdbx_seq_one_letter_code       
;MKHHHHHHHVSKGEELFTGVVPILVELDGDVNGHKFSVSGEGEGDATYGKLTLKFICTTGKLPVPWPTLVTTL(SWG)VQ
CFARYPDHMKQHDFFKSAMPEGYVQERTIFFKDDGNYKTRAEVKFEGDTLVNRIELKGIDFKEDGNILGHKLEYNSSGRT
GIDPFTESVLQSQATELLQKKAQLVSFKIQGIMKRIFMGANTLEKFLSDENSAINDTLKRRMLSEFLLANPHVLLVSAIY
TNNNERVITAMSMDSKIAYPNTTLNENMTNQIRSLKSITHSDPYYKEVNGDKIYGMDITLPLMGKNQNAIGALNFFLNID
AFYTDVVGKKKSNTFLMGKDGRLLINPNREIQDKILSAINPDRRVAKAVEYYNQNEAGTLSYHSLSGNTETFLAIQPFDF
FEEKGNNGNHWRWAIGKYVNKSLVFSSHSNVYITADKQKNGIKANFKIRHNIEDGGVQLADHYQQNTPIGDGPVLLPDNH
YLSTQSKLSKDPNEKRDHMVLLEFVTAAGITLGMDELYQ
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MKHHHHHHHVSKGEELFTGVVPILVELDGDVNGHKFSVSGEGEGDATYGKLTLKFICTTGKLPVPWPTLVTTLSWGVQCF
ARYPDHMKQHDFFKSAMPEGYVQERTIFFKDDGNYKTRAEVKFEGDTLVNRIELKGIDFKEDGNILGHKLEYNSSGRTGI
DPFTESVLQSQATELLQKKAQLVSFKIQGIMKRIFMGANTLEKFLSDENSAINDTLKRRMLSEFLLANPHVLLVSAIYTN
NNERVITAMSMDSKIAYPNTTLNENMTNQIRSLKSITHSDPYYKEVNGDKIYGMDITLPLMGKNQNAIGALNFFLNIDAF
YTDVVGKKKSNTFLMGKDGRLLINPNREIQDKILSAINPDRRVAKAVEYYNQNEAGTLSYHSLSGNTETFLAIQPFDFFE
EKGNNGNHWRWAIGKYVNKSLVFSSHSNVYITADKQKNGIKANFKIRHNIEDGGVQLADHYQQNTPIGDGPVLLPDNHYL
STQSKLSKDPNEKRDHMVLLEFVTAAGITLGMDELYQ
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
_pdbx_entity_nonpoly.entity_id   2 
_pdbx_entity_nonpoly.name        water 
_pdbx_entity_nonpoly.comp_id     HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   LYS n 
1 3   HIS n 
1 4   HIS n 
1 5   HIS n 
1 6   HIS n 
1 7   HIS n 
1 8   HIS n 
1 9   HIS n 
1 10  VAL n 
1 11  SER n 
1 12  LYS n 
1 13  GLY n 
1 14  GLU n 
1 15  GLU n 
1 16  LEU n 
1 17  PHE n 
1 18  THR n 
1 19  GLY n 
1 20  VAL n 
1 21  VAL n 
1 22  PRO n 
1 23  ILE n 
1 24  LEU n 
1 25  VAL n 
1 26  GLU n 
1 27  LEU n 
1 28  ASP n 
1 29  GLY n 
1 30  ASP n 
1 31  VAL n 
1 32  ASN n 
1 33  GLY n 
1 34  HIS n 
1 35  LYS n 
1 36  PHE n 
1 37  SER n 
1 38  VAL n 
1 39  SER n 
1 40  GLY n 
1 41  GLU n 
1 42  GLY n 
1 43  GLU n 
1 44  GLY n 
1 45  ASP n 
1 46  ALA n 
1 47  THR n 
1 48  TYR n 
1 49  GLY n 
1 50  LYS n 
1 51  LEU n 
1 52  THR n 
1 53  LEU n 
1 54  LYS n 
1 55  PHE n 
1 56  ILE n 
1 57  CYS n 
1 58  THR n 
1 59  THR n 
1 60  GLY n 
1 61  LYS n 
1 62  LEU n 
1 63  PRO n 
1 64  VAL n 
1 65  PRO n 
1 66  TRP n 
1 67  PRO n 
1 68  THR n 
1 69  LEU n 
1 70  VAL n 
1 71  THR n 
1 72  THR n 
1 73  LEU n 
1 74  SWG n 
1 75  VAL n 
1 76  GLN n 
1 77  CYS n 
1 78  PHE n 
1 79  ALA n 
1 80  ARG n 
1 81  TYR n 
1 82  PRO n 
1 83  ASP n 
1 84  HIS n 
1 85  MET n 
1 86  LYS n 
1 87  GLN n 
1 88  HIS n 
1 89  ASP n 
1 90  PHE n 
1 91  PHE n 
1 92  LYS n 
1 93  SER n 
1 94  ALA n 
1 95  MET n 
1 96  PRO n 
1 97  GLU n 
1 98  GLY n 
1 99  TYR n 
1 100 VAL n 
1 101 GLN n 
1 102 GLU n 
1 103 ARG n 
1 104 THR n 
1 105 ILE n 
1 106 PHE n 
1 107 PHE n 
1 108 LYS n 
1 109 ASP n 
1 110 ASP n 
1 111 GLY n 
1 112 ASN n 
1 113 TYR n 
1 114 LYS n 
1 115 THR n 
1 116 ARG n 
1 117 ALA n 
1 118 GLU n 
1 119 VAL n 
1 120 LYS n 
1 121 PHE n 
1 122 GLU n 
1 123 GLY n 
1 124 ASP n 
1 125 THR n 
1 126 LEU n 
1 127 VAL n 
1 128 ASN n 
1 129 ARG n 
1 130 ILE n 
1 131 GLU n 
1 132 LEU n 
1 133 LYS n 
1 134 GLY n 
1 135 ILE n 
1 136 ASP n 
1 137 PHE n 
1 138 LYS n 
1 139 GLU n 
1 140 ASP n 
1 141 GLY n 
1 142 ASN n 
1 143 ILE n 
1 144 LEU n 
1 145 GLY n 
1 146 HIS n 
1 147 LYS n 
1 148 LEU n 
1 149 GLU n 
1 150 TYR n 
1 151 ASN n 
1 152 SER n 
1 153 SER n 
1 154 GLY n 
1 155 ARG n 
1 156 THR n 
1 157 GLY n 
1 158 ILE n 
1 159 ASP n 
1 160 PRO n 
1 161 PHE n 
1 162 THR n 
1 163 GLU n 
1 164 SER n 
1 165 VAL n 
1 166 LEU n 
1 167 GLN n 
1 168 SER n 
1 169 GLN n 
1 170 ALA n 
1 171 THR n 
1 172 GLU n 
1 173 LEU n 
1 174 LEU n 
1 175 GLN n 
1 176 LYS n 
1 177 LYS n 
1 178 ALA n 
1 179 GLN n 
1 180 LEU n 
1 181 VAL n 
1 182 SER n 
1 183 PHE n 
1 184 LYS n 
1 185 ILE n 
1 186 GLN n 
1 187 GLY n 
1 188 ILE n 
1 189 MET n 
1 190 LYS n 
1 191 ARG n 
1 192 ILE n 
1 193 PHE n 
1 194 MET n 
1 195 GLY n 
1 196 ALA n 
1 197 ASN n 
1 198 THR n 
1 199 LEU n 
1 200 GLU n 
1 201 LYS n 
1 202 PHE n 
1 203 LEU n 
1 204 SER n 
1 205 ASP n 
1 206 GLU n 
1 207 ASN n 
1 208 SER n 
1 209 ALA n 
1 210 ILE n 
1 211 ASN n 
1 212 ASP n 
1 213 THR n 
1 214 LEU n 
1 215 LYS n 
1 216 ARG n 
1 217 ARG n 
1 218 MET n 
1 219 LEU n 
1 220 SER n 
1 221 GLU n 
1 222 PHE n 
1 223 LEU n 
1 224 LEU n 
1 225 ALA n 
1 226 ASN n 
1 227 PRO n 
1 228 HIS n 
1 229 VAL n 
1 230 LEU n 
1 231 LEU n 
1 232 VAL n 
1 233 SER n 
1 234 ALA n 
1 235 ILE n 
1 236 TYR n 
1 237 THR n 
1 238 ASN n 
1 239 ASN n 
1 240 ASN n 
1 241 GLU n 
1 242 ARG n 
1 243 VAL n 
1 244 ILE n 
1 245 THR n 
1 246 ALA n 
1 247 MET n 
1 248 SER n 
1 249 MET n 
1 250 ASP n 
1 251 SER n 
1 252 LYS n 
1 253 ILE n 
1 254 ALA n 
1 255 TYR n 
1 256 PRO n 
1 257 ASN n 
1 258 THR n 
1 259 THR n 
1 260 LEU n 
1 261 ASN n 
1 262 GLU n 
1 263 ASN n 
1 264 MET n 
1 265 THR n 
1 266 ASN n 
1 267 GLN n 
1 268 ILE n 
1 269 ARG n 
1 270 SER n 
1 271 LEU n 
1 272 LYS n 
1 273 SER n 
1 274 ILE n 
1 275 THR n 
1 276 HIS n 
1 277 SER n 
1 278 ASP n 
1 279 PRO n 
1 280 TYR n 
1 281 TYR n 
1 282 LYS n 
1 283 GLU n 
1 284 VAL n 
1 285 ASN n 
1 286 GLY n 
1 287 ASP n 
1 288 LYS n 
1 289 ILE n 
1 290 TYR n 
1 291 GLY n 
1 292 MET n 
1 293 ASP n 
1 294 ILE n 
1 295 THR n 
1 296 LEU n 
1 297 PRO n 
1 298 LEU n 
1 299 MET n 
1 300 GLY n 
1 301 LYS n 
1 302 ASN n 
1 303 GLN n 
1 304 ASN n 
1 305 ALA n 
1 306 ILE n 
1 307 GLY n 
1 308 ALA n 
1 309 LEU n 
1 310 ASN n 
1 311 PHE n 
1 312 PHE n 
1 313 LEU n 
1 314 ASN n 
1 315 ILE n 
1 316 ASP n 
1 317 ALA n 
1 318 PHE n 
1 319 TYR n 
1 320 THR n 
1 321 ASP n 
1 322 VAL n 
1 323 VAL n 
1 324 GLY n 
1 325 LYS n 
1 326 LYS n 
1 327 LYS n 
1 328 SER n 
1 329 ASN n 
1 330 THR n 
1 331 PHE n 
1 332 LEU n 
1 333 MET n 
1 334 GLY n 
1 335 LYS n 
1 336 ASP n 
1 337 GLY n 
1 338 ARG n 
1 339 LEU n 
1 340 LEU n 
1 341 ILE n 
1 342 ASN n 
1 343 PRO n 
1 344 ASN n 
1 345 ARG n 
1 346 GLU n 
1 347 ILE n 
1 348 GLN n 
1 349 ASP n 
1 350 LYS n 
1 351 ILE n 
1 352 LEU n 
1 353 SER n 
1 354 ALA n 
1 355 ILE n 
1 356 ASN n 
1 357 PRO n 
1 358 ASP n 
1 359 ARG n 
1 360 ARG n 
1 361 VAL n 
1 362 ALA n 
1 363 LYS n 
1 364 ALA n 
1 365 VAL n 
1 366 GLU n 
1 367 TYR n 
1 368 TYR n 
1 369 ASN n 
1 370 GLN n 
1 371 ASN n 
1 372 GLU n 
1 373 ALA n 
1 374 GLY n 
1 375 THR n 
1 376 LEU n 
1 377 SER n 
1 378 TYR n 
1 379 HIS n 
1 380 SER n 
1 381 LEU n 
1 382 SER n 
1 383 GLY n 
1 384 ASN n 
1 385 THR n 
1 386 GLU n 
1 387 THR n 
1 388 PHE n 
1 389 LEU n 
1 390 ALA n 
1 391 ILE n 
1 392 GLN n 
1 393 PRO n 
1 394 PHE n 
1 395 ASP n 
1 396 PHE n 
1 397 PHE n 
1 398 GLU n 
1 399 GLU n 
1 400 LYS n 
1 401 GLY n 
1 402 ASN n 
1 403 ASN n 
1 404 GLY n 
1 405 ASN n 
1 406 HIS n 
1 407 TRP n 
1 408 ARG n 
1 409 TRP n 
1 410 ALA n 
1 411 ILE n 
1 412 GLY n 
1 413 LYS n 
1 414 TYR n 
1 415 VAL n 
1 416 ASN n 
1 417 LYS n 
1 418 SER n 
1 419 LEU n 
1 420 VAL n 
1 421 PHE n 
1 422 SER n 
1 423 SER n 
1 424 HIS n 
1 425 SER n 
1 426 ASN n 
1 427 VAL n 
1 428 TYR n 
1 429 ILE n 
1 430 THR n 
1 431 ALA n 
1 432 ASP n 
1 433 LYS n 
1 434 GLN n 
1 435 LYS n 
1 436 ASN n 
1 437 GLY n 
1 438 ILE n 
1 439 LYS n 
1 440 ALA n 
1 441 ASN n 
1 442 PHE n 
1 443 LYS n 
1 444 ILE n 
1 445 ARG n 
1 446 HIS n 
1 447 ASN n 
1 448 ILE n 
1 449 GLU n 
1 450 ASP n 
1 451 GLY n 
1 452 GLY n 
1 453 VAL n 
1 454 GLN n 
1 455 LEU n 
1 456 ALA n 
1 457 ASP n 
1 458 HIS n 
1 459 TYR n 
1 460 GLN n 
1 461 GLN n 
1 462 ASN n 
1 463 THR n 
1 464 PRO n 
1 465 ILE n 
1 466 GLY n 
1 467 ASP n 
1 468 GLY n 
1 469 PRO n 
1 470 VAL n 
1 471 LEU n 
1 472 LEU n 
1 473 PRO n 
1 474 ASP n 
1 475 ASN n 
1 476 HIS n 
1 477 TYR n 
1 478 LEU n 
1 479 SER n 
1 480 THR n 
1 481 GLN n 
1 482 SER n 
1 483 LYS n 
1 484 LEU n 
1 485 SER n 
1 486 LYS n 
1 487 ASP n 
1 488 PRO n 
1 489 ASN n 
1 490 GLU n 
1 491 LYS n 
1 492 ARG n 
1 493 ASP n 
1 494 HIS n 
1 495 MET n 
1 496 VAL n 
1 497 LEU n 
1 498 LEU n 
1 499 GLU n 
1 500 PHE n 
1 501 VAL n 
1 502 THR n 
1 503 ALA n 
1 504 ALA n 
1 505 GLY n 
1 506 ILE n 
1 507 THR n 
1 508 LEU n 
1 509 GLY n 
1 510 MET n 
1 511 ASP n 
1 512 GLU n 
1 513 LEU n 
1 514 TYR n 
1 515 GLN n 
# 
loop_
_entity_src_gen.entity_id 
_entity_src_gen.pdbx_src_id 
_entity_src_gen.pdbx_alt_source_flag 
_entity_src_gen.pdbx_seq_type 
_entity_src_gen.pdbx_beg_seq_num 
_entity_src_gen.pdbx_end_seq_num 
_entity_src_gen.gene_src_common_name 
_entity_src_gen.gene_src_genus 
_entity_src_gen.pdbx_gene_src_gene 
_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 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 
_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 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 
_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 
1 1 sample 'Biological sequence' 1   158 ? ? GFP     ? ?     ? ? ? ? 'Aequorea victoria'   6100  ? ? ? ? ? ? ? ? 
'Escherichia coli B' 37762 ? ? ? ? ? ? 'BL21(DE3)' OneShot ? ? ? ? ? ? Plasmid ? ? ? ? ? ? 
1 2 sample 'Biological sequence' 159 421 ? ? HP_0082 ? 26695 ? ? ? ? 'Helicobacter pylori' 85962 ? ? ? ? ? ? ? ? 
'Escherichia coli B' 37762 ? ? ? ? ? ? 'BL21(DE3)' OneShot ? ? ? ? ? ? Plasmid ? ? ? ? ? ? 
1 3 sample 'Biological sequence' 422 515 ? ? GFP     ? ?     ? ? ? ? 'Aequorea victoria'   6100  ? ? ? ? ? ? ? ? 
'Escherichia coli B' 37762 ? ? ? ? ? ? 'BL21(DE3)' OneShot ? ? ? ? ? ? Plasmid ? ? ? ? ? ? 
# 
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 
ALA 'L-peptide linking' y ALANINE ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4'     133.103 
CYS 'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE ? 'C2 H5 N O2'     75.067  
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 
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 
SWG 'L-peptide linking' n 
'2-[(4Z)-2-[(1R)-1-amino-2-hydroxy-ethyl]-4-(1H-indol-3-ylmethylidene)-5-oxo-imidazol-1-yl]ethanoic acid' ? 'C16 H16 N4 O4'  
328.323 
THR 'L-peptide linking' y THREONINE ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN ? 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE ? 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE ? 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   ?   ?   ?   A . n 
A 1 2   LYS 2   2   ?   ?   ?   A . n 
A 1 3   HIS 3   3   ?   ?   ?   A . n 
A 1 4   HIS 4   4   ?   ?   ?   A . n 
A 1 5   HIS 5   5   ?   ?   ?   A . n 
A 1 6   HIS 6   6   ?   ?   ?   A . n 
A 1 7   HIS 7   7   ?   ?   ?   A . n 
A 1 8   HIS 8   8   ?   ?   ?   A . n 
A 1 9   HIS 9   9   ?   ?   ?   A . n 
A 1 10  VAL 10  10  ?   ?   ?   A . n 
A 1 11  SER 11  11  ?   ?   ?   A . n 
A 1 12  LYS 12  12  12  LYS LYS A . n 
A 1 13  GLY 13  13  13  GLY GLY A . n 
A 1 14  GLU 14  14  14  GLU GLU A . n 
A 1 15  GLU 15  15  15  GLU GLU A . n 
A 1 16  LEU 16  16  16  LEU LEU A . n 
A 1 17  PHE 17  17  17  PHE PHE A . n 
A 1 18  THR 18  18  18  THR THR A . n 
A 1 19  GLY 19  19  19  GLY GLY A . n 
A 1 20  VAL 20  20  20  VAL VAL A . n 
A 1 21  VAL 21  21  21  VAL VAL A . n 
A 1 22  PRO 22  22  22  PRO PRO A . n 
A 1 23  ILE 23  23  23  ILE ILE A . n 
A 1 24  LEU 24  24  24  LEU LEU A . n 
A 1 25  VAL 25  25  25  VAL VAL A . n 
A 1 26  GLU 26  26  26  GLU GLU A . n 
A 1 27  LEU 27  27  27  LEU LEU A . n 
A 1 28  ASP 28  28  28  ASP ASP A . n 
A 1 29  GLY 29  29  29  GLY GLY A . n 
A 1 30  ASP 30  30  30  ASP ASP A . n 
A 1 31  VAL 31  31  31  VAL VAL A . n 
A 1 32  ASN 32  32  32  ASN ASN A . n 
A 1 33  GLY 33  33  33  GLY GLY A . n 
A 1 34  HIS 34  34  34  HIS HIS A . n 
A 1 35  LYS 35  35  35  LYS LYS A . n 
A 1 36  PHE 36  36  36  PHE PHE A . n 
A 1 37  SER 37  37  37  SER SER A . n 
A 1 38  VAL 38  38  38  VAL VAL A . n 
A 1 39  SER 39  39  39  SER SER A . n 
A 1 40  GLY 40  40  40  GLY GLY A . n 
A 1 41  GLU 41  41  41  GLU GLU A . n 
A 1 42  GLY 42  42  42  GLY GLY A . n 
A 1 43  GLU 43  43  43  GLU GLU A . n 
A 1 44  GLY 44  44  44  GLY GLY A . n 
A 1 45  ASP 45  45  45  ASP ASP A . n 
A 1 46  ALA 46  46  46  ALA ALA A . n 
A 1 47  THR 47  47  47  THR THR A . n 
A 1 48  TYR 48  48  48  TYR TYR A . n 
A 1 49  GLY 49  49  49  GLY GLY A . n 
A 1 50  LYS 50  50  50  LYS LYS A . n 
A 1 51  LEU 51  51  51  LEU LEU A . n 
A 1 52  THR 52  52  52  THR THR A . n 
A 1 53  LEU 53  53  53  LEU LEU A . n 
A 1 54  LYS 54  54  54  LYS LYS A . n 
A 1 55  PHE 55  55  55  PHE PHE A . n 
A 1 56  ILE 56  56  56  ILE ILE A . n 
A 1 57  CYS 57  57  57  CYS CYS A . n 
A 1 58  THR 58  58  58  THR THR A . n 
A 1 59  THR 59  59  59  THR THR A . n 
A 1 60  GLY 60  60  60  GLY GLY A . n 
A 1 61  LYS 61  61  61  LYS LYS A . n 
A 1 62  LEU 62  62  62  LEU LEU A . n 
A 1 63  PRO 63  63  63  PRO PRO A . n 
A 1 64  VAL 64  64  64  VAL VAL A . n 
A 1 65  PRO 65  65  65  PRO PRO A . n 
A 1 66  TRP 66  66  66  TRP TRP A . n 
A 1 67  PRO 67  67  67  PRO PRO A . n 
A 1 68  THR 68  68  68  THR THR A . n 
A 1 69  LEU 69  69  69  LEU LEU A . n 
A 1 70  VAL 70  70  70  VAL VAL A . n 
A 1 71  THR 71  71  71  THR THR A . n 
A 1 72  THR 72  72  72  THR THR A . n 
A 1 73  LEU 73  73  73  LEU LEU A . n 
A 1 74  SWG 74  74  74  SWG SWG A . n 
A 1 75  VAL 75  75  75  VAL VAL A . n 
A 1 76  GLN 76  76  76  GLN GLN A . n 
A 1 77  CYS 77  77  77  CYS CYS A . n 
A 1 78  PHE 78  78  78  PHE PHE A . n 
A 1 79  ALA 79  79  79  ALA ALA A . n 
A 1 80  ARG 80  80  80  ARG ARG A . n 
A 1 81  TYR 81  81  81  TYR TYR A . n 
A 1 82  PRO 82  82  82  PRO PRO A . n 
A 1 83  ASP 83  83  83  ASP ASP A . n 
A 1 84  HIS 84  84  84  HIS HIS A . n 
A 1 85  MET 85  85  85  MET MET A . n 
A 1 86  LYS 86  86  86  LYS LYS A . n 
A 1 87  GLN 87  87  87  GLN GLN A . n 
A 1 88  HIS 88  88  ?   ?   ?   A . n 
A 1 89  ASP 89  89  89  ASP ASP A . n 
A 1 90  PHE 90  90  90  PHE PHE A . n 
A 1 91  PHE 91  91  91  PHE PHE A . n 
A 1 92  LYS 92  92  92  LYS LYS A . n 
A 1 93  SER 93  93  93  SER SER A . n 
A 1 94  ALA 94  94  94  ALA ALA A . n 
A 1 95  MET 95  95  95  MET MET A . n 
A 1 96  PRO 96  96  96  PRO PRO A . n 
A 1 97  GLU 97  97  97  GLU GLU A . n 
A 1 98  GLY 98  98  98  GLY GLY A . n 
A 1 99  TYR 99  99  99  TYR TYR A . n 
A 1 100 VAL 100 100 100 VAL VAL A . n 
A 1 101 GLN 101 101 101 GLN GLN A . n 
A 1 102 GLU 102 102 102 GLU GLU A . n 
A 1 103 ARG 103 103 103 ARG ARG A . n 
A 1 104 THR 104 104 104 THR THR A . n 
A 1 105 ILE 105 105 105 ILE ILE A . n 
A 1 106 PHE 106 106 106 PHE PHE A . n 
A 1 107 PHE 107 107 107 PHE PHE A . n 
A 1 108 LYS 108 108 108 LYS LYS A . n 
A 1 109 ASP 109 109 109 ASP ASP A . n 
A 1 110 ASP 110 110 110 ASP ASP A . n 
A 1 111 GLY 111 111 111 GLY GLY A . n 
A 1 112 ASN 112 112 112 ASN ASN A . n 
A 1 113 TYR 113 113 113 TYR TYR A . n 
A 1 114 LYS 114 114 114 LYS LYS A . n 
A 1 115 THR 115 115 115 THR THR A . n 
A 1 116 ARG 116 116 116 ARG ARG A . n 
A 1 117 ALA 117 117 117 ALA ALA A . n 
A 1 118 GLU 118 118 118 GLU GLU A . n 
A 1 119 VAL 119 119 119 VAL VAL A . n 
A 1 120 LYS 120 120 120 LYS LYS A . n 
A 1 121 PHE 121 121 121 PHE PHE A . n 
A 1 122 GLU 122 122 122 GLU GLU A . n 
A 1 123 GLY 123 123 123 GLY GLY A . n 
A 1 124 ASP 124 124 124 ASP ASP A . n 
A 1 125 THR 125 125 125 THR THR A . n 
A 1 126 LEU 126 126 126 LEU LEU A . n 
A 1 127 VAL 127 127 127 VAL VAL A . n 
A 1 128 ASN 128 128 128 ASN ASN A . n 
A 1 129 ARG 129 129 129 ARG ARG A . n 
A 1 130 ILE 130 130 130 ILE ILE A . n 
A 1 131 GLU 131 131 131 GLU GLU A . n 
A 1 132 LEU 132 132 132 LEU LEU A . n 
A 1 133 LYS 133 133 133 LYS LYS A . n 
A 1 134 GLY 134 134 134 GLY GLY A . n 
A 1 135 ILE 135 135 135 ILE ILE A . n 
A 1 136 ASP 136 136 136 ASP ASP A . n 
A 1 137 PHE 137 137 137 PHE PHE A . n 
A 1 138 LYS 138 138 138 LYS LYS A . n 
A 1 139 GLU 139 139 139 GLU GLU A . n 
A 1 140 ASP 140 140 140 ASP ASP A . n 
A 1 141 GLY 141 141 141 GLY GLY A . n 
A 1 142 ASN 142 142 142 ASN ASN A . n 
A 1 143 ILE 143 143 143 ILE ILE A . n 
A 1 144 LEU 144 144 144 LEU LEU A . n 
A 1 145 GLY 145 145 145 GLY GLY A . n 
A 1 146 HIS 146 146 146 HIS HIS A . n 
A 1 147 LYS 147 147 147 LYS LYS A . n 
A 1 148 LEU 148 148 148 LEU LEU A . n 
A 1 149 GLU 149 149 149 GLU GLU A . n 
A 1 150 TYR 150 150 150 TYR TYR A . n 
A 1 151 ASN 151 151 151 ASN ASN A . n 
A 1 152 SER 152 152 152 SER SER A . n 
A 1 153 SER 153 153 153 SER SER A . n 
A 1 154 GLY 154 154 ?   ?   ?   A . n 
A 1 155 ARG 155 155 ?   ?   ?   A . n 
A 1 156 THR 156 156 ?   ?   ?   A . n 
A 1 157 GLY 157 157 ?   ?   ?   A . n 
A 1 158 ILE 158 158 ?   ?   ?   A . n 
A 1 159 ASP 159 159 ?   ?   ?   A . n 
A 1 160 PRO 160 160 ?   ?   ?   A . n 
A 1 161 PHE 161 161 161 PHE PHE A . n 
A 1 162 THR 162 162 162 THR THR A . n 
A 1 163 GLU 163 163 163 GLU GLU A . n 
A 1 164 SER 164 164 164 SER SER A . n 
A 1 165 VAL 165 165 165 VAL VAL A . n 
A 1 166 LEU 166 166 166 LEU LEU A . n 
A 1 167 GLN 167 167 167 GLN GLN A . n 
A 1 168 SER 168 168 168 SER SER A . n 
A 1 169 GLN 169 169 169 GLN GLN A . n 
A 1 170 ALA 170 170 170 ALA ALA A . n 
A 1 171 THR 171 171 171 THR THR A . n 
A 1 172 GLU 172 172 172 GLU GLU A . n 
A 1 173 LEU 173 173 173 LEU LEU A . n 
A 1 174 LEU 174 174 174 LEU LEU A . n 
A 1 175 GLN 175 175 175 GLN GLN A . n 
A 1 176 LYS 176 176 176 LYS LYS A . n 
A 1 177 LYS 177 177 177 LYS LYS A . n 
A 1 178 ALA 178 178 178 ALA ALA A . n 
A 1 179 GLN 179 179 179 GLN GLN A . n 
A 1 180 LEU 180 180 180 LEU LEU A . n 
A 1 181 VAL 181 181 181 VAL VAL A . n 
A 1 182 SER 182 182 182 SER SER A . n 
A 1 183 PHE 183 183 183 PHE PHE A . n 
A 1 184 LYS 184 184 184 LYS LYS A . n 
A 1 185 ILE 185 185 185 ILE ILE A . n 
A 1 186 GLN 186 186 186 GLN GLN A . n 
A 1 187 GLY 187 187 187 GLY GLY A . n 
A 1 188 ILE 188 188 188 ILE ILE A . n 
A 1 189 MET 189 189 189 MET MET A . n 
A 1 190 LYS 190 190 190 LYS LYS A . n 
A 1 191 ARG 191 191 191 ARG ARG A . n 
A 1 192 ILE 192 192 192 ILE ILE A . n 
A 1 193 PHE 193 193 193 PHE PHE A . n 
A 1 194 MET 194 194 194 MET MET A . n 
A 1 195 GLY 195 195 195 GLY GLY A . n 
A 1 196 ALA 196 196 196 ALA ALA A . n 
A 1 197 ASN 197 197 197 ASN ASN A . n 
A 1 198 THR 198 198 198 THR THR A . n 
A 1 199 LEU 199 199 199 LEU LEU A . n 
A 1 200 GLU 200 200 200 GLU GLU A . n 
A 1 201 LYS 201 201 201 LYS LYS A . n 
A 1 202 PHE 202 202 202 PHE PHE A . n 
A 1 203 LEU 203 203 203 LEU LEU A . n 
A 1 204 SER 204 204 204 SER SER A . n 
A 1 205 ASP 205 205 205 ASP ASP A . n 
A 1 206 GLU 206 206 206 GLU GLU A . n 
A 1 207 ASN 207 207 207 ASN ASN A . n 
A 1 208 SER 208 208 208 SER SER A . n 
A 1 209 ALA 209 209 209 ALA ALA A . n 
A 1 210 ILE 210 210 210 ILE ILE A . n 
A 1 211 ASN 211 211 211 ASN ASN A . n 
A 1 212 ASP 212 212 212 ASP ASP A . n 
A 1 213 THR 213 213 213 THR THR A . n 
A 1 214 LEU 214 214 214 LEU LEU A . n 
A 1 215 LYS 215 215 215 LYS LYS A . n 
A 1 216 ARG 216 216 216 ARG ARG A . n 
A 1 217 ARG 217 217 217 ARG ARG A . n 
A 1 218 MET 218 218 218 MET MET A . n 
A 1 219 LEU 219 219 219 LEU LEU A . n 
A 1 220 SER 220 220 220 SER SER A . n 
A 1 221 GLU 221 221 221 GLU GLU A . n 
A 1 222 PHE 222 222 222 PHE PHE A . n 
A 1 223 LEU 223 223 223 LEU LEU A . n 
A 1 224 LEU 224 224 224 LEU LEU A . n 
A 1 225 ALA 225 225 225 ALA ALA A . n 
A 1 226 ASN 226 226 226 ASN ASN A . n 
A 1 227 PRO 227 227 227 PRO PRO A . n 
A 1 228 HIS 228 228 228 HIS HIS A . n 
A 1 229 VAL 229 229 229 VAL VAL A . n 
A 1 230 LEU 230 230 230 LEU LEU A . n 
A 1 231 LEU 231 231 231 LEU LEU A . n 
A 1 232 VAL 232 232 232 VAL VAL A . n 
A 1 233 SER 233 233 233 SER SER A . n 
A 1 234 ALA 234 234 234 ALA ALA A . n 
A 1 235 ILE 235 235 235 ILE ILE A . n 
A 1 236 TYR 236 236 236 TYR TYR A . n 
A 1 237 THR 237 237 237 THR THR A . n 
A 1 238 ASN 238 238 238 ASN ASN A . n 
A 1 239 ASN 239 239 239 ASN ASN A . n 
A 1 240 ASN 240 240 240 ASN ASN A . n 
A 1 241 GLU 241 241 241 GLU GLU A . n 
A 1 242 ARG 242 242 242 ARG ARG A . n 
A 1 243 VAL 243 243 243 VAL VAL A . n 
A 1 244 ILE 244 244 244 ILE ILE A . n 
A 1 245 THR 245 245 245 THR THR A . n 
A 1 246 ALA 246 246 246 ALA ALA A . n 
A 1 247 MET 247 247 247 MET MET A . n 
A 1 248 SER 248 248 248 SER SER A . n 
A 1 249 MET 249 249 249 MET MET A . n 
A 1 250 ASP 250 250 250 ASP ASP A . n 
A 1 251 SER 251 251 251 SER SER A . n 
A 1 252 LYS 252 252 252 LYS LYS A . n 
A 1 253 ILE 253 253 253 ILE ILE A . n 
A 1 254 ALA 254 254 254 ALA ALA A . n 
A 1 255 TYR 255 255 255 TYR TYR A . n 
A 1 256 PRO 256 256 256 PRO PRO A . n 
A 1 257 ASN 257 257 257 ASN ASN A . n 
A 1 258 THR 258 258 258 THR THR A . n 
A 1 259 THR 259 259 259 THR THR A . n 
A 1 260 LEU 260 260 260 LEU LEU A . n 
A 1 261 ASN 261 261 261 ASN ASN A . n 
A 1 262 GLU 262 262 262 GLU GLU A . n 
A 1 263 ASN 263 263 263 ASN ASN A . n 
A 1 264 MET 264 264 264 MET MET A . n 
A 1 265 THR 265 265 265 THR THR A . n 
A 1 266 ASN 266 266 266 ASN ASN A . n 
A 1 267 GLN 267 267 267 GLN GLN A . n 
A 1 268 ILE 268 268 268 ILE ILE A . n 
A 1 269 ARG 269 269 269 ARG ARG A . n 
A 1 270 SER 270 270 270 SER SER A . n 
A 1 271 LEU 271 271 271 LEU LEU A . n 
A 1 272 LYS 272 272 272 LYS LYS A . n 
A 1 273 SER 273 273 273 SER SER A . n 
A 1 274 ILE 274 274 274 ILE ILE A . n 
A 1 275 THR 275 275 275 THR THR A . n 
A 1 276 HIS 276 276 276 HIS HIS A . n 
A 1 277 SER 277 277 277 SER SER A . n 
A 1 278 ASP 278 278 278 ASP ASP A . n 
A 1 279 PRO 279 279 279 PRO PRO A . n 
A 1 280 TYR 280 280 280 TYR TYR A . n 
A 1 281 TYR 281 281 281 TYR TYR A . n 
A 1 282 LYS 282 282 282 LYS LYS A . n 
A 1 283 GLU 283 283 283 GLU GLU A . n 
A 1 284 VAL 284 284 284 VAL VAL A . n 
A 1 285 ASN 285 285 285 ASN ASN A . n 
A 1 286 GLY 286 286 286 GLY GLY A . n 
A 1 287 ASP 287 287 287 ASP ASP A . n 
A 1 288 LYS 288 288 288 LYS LYS A . n 
A 1 289 ILE 289 289 289 ILE ILE A . n 
A 1 290 TYR 290 290 290 TYR TYR A . n 
A 1 291 GLY 291 291 291 GLY GLY A . n 
A 1 292 MET 292 292 292 MET MET A . n 
A 1 293 ASP 293 293 293 ASP ASP A . n 
A 1 294 ILE 294 294 294 ILE ILE A . n 
A 1 295 THR 295 295 295 THR THR A . n 
A 1 296 LEU 296 296 296 LEU LEU A . n 
A 1 297 PRO 297 297 297 PRO PRO A . n 
A 1 298 LEU 298 298 298 LEU LEU A . n 
A 1 299 MET 299 299 299 MET MET A . n 
A 1 300 GLY 300 300 300 GLY GLY A . n 
A 1 301 LYS 301 301 301 LYS LYS A . n 
A 1 302 ASN 302 302 302 ASN ASN A . n 
A 1 303 GLN 303 303 ?   ?   ?   A . n 
A 1 304 ASN 304 304 ?   ?   ?   A . n 
A 1 305 ALA 305 305 305 ALA ALA A . n 
A 1 306 ILE 306 306 306 ILE ILE A . n 
A 1 307 GLY 307 307 307 GLY GLY A . n 
A 1 308 ALA 308 308 308 ALA ALA A . n 
A 1 309 LEU 309 309 309 LEU LEU A . n 
A 1 310 ASN 310 310 310 ASN ASN A . n 
A 1 311 PHE 311 311 311 PHE PHE A . n 
A 1 312 PHE 312 312 312 PHE PHE A . n 
A 1 313 LEU 313 313 313 LEU LEU A . n 
A 1 314 ASN 314 314 314 ASN ASN A . n 
A 1 315 ILE 315 315 315 ILE ILE A . n 
A 1 316 ASP 316 316 316 ASP ASP A . n 
A 1 317 ALA 317 317 317 ALA ALA A . n 
A 1 318 PHE 318 318 318 PHE PHE A . n 
A 1 319 TYR 319 319 319 TYR TYR A . n 
A 1 320 THR 320 320 320 THR THR A . n 
A 1 321 ASP 321 321 321 ASP ASP A . n 
A 1 322 VAL 322 322 322 VAL VAL A . n 
A 1 323 VAL 323 323 323 VAL VAL A . n 
A 1 324 GLY 324 324 324 GLY GLY A . n 
A 1 325 LYS 325 325 325 LYS LYS A . n 
A 1 326 LYS 326 326 326 LYS LYS A . n 
A 1 327 LYS 327 327 327 LYS LYS A . n 
A 1 328 SER 328 328 328 SER SER A . n 
A 1 329 ASN 329 329 329 ASN ASN A . n 
A 1 330 THR 330 330 330 THR THR A . n 
A 1 331 PHE 331 331 331 PHE PHE A . n 
A 1 332 LEU 332 332 332 LEU LEU A . n 
A 1 333 MET 333 333 333 MET MET A . n 
A 1 334 GLY 334 334 334 GLY GLY A . n 
A 1 335 LYS 335 335 335 LYS LYS A . n 
A 1 336 ASP 336 336 336 ASP ASP A . n 
A 1 337 GLY 337 337 337 GLY GLY A . n 
A 1 338 ARG 338 338 338 ARG ARG A . n 
A 1 339 LEU 339 339 339 LEU LEU A . n 
A 1 340 LEU 340 340 340 LEU LEU A . n 
A 1 341 ILE 341 341 341 ILE ILE A . n 
A 1 342 ASN 342 342 342 ASN ASN A . n 
A 1 343 PRO 343 343 343 PRO PRO A . n 
A 1 344 ASN 344 344 344 ASN ASN A . n 
A 1 345 ARG 345 345 345 ARG ARG A . n 
A 1 346 GLU 346 346 346 GLU GLU A . n 
A 1 347 ILE 347 347 347 ILE ILE A . n 
A 1 348 GLN 348 348 348 GLN GLN A . n 
A 1 349 ASP 349 349 349 ASP ASP A . n 
A 1 350 LYS 350 350 350 LYS LYS A . n 
A 1 351 ILE 351 351 351 ILE ILE A . n 
A 1 352 LEU 352 352 352 LEU LEU A . n 
A 1 353 SER 353 353 353 SER SER A . n 
A 1 354 ALA 354 354 354 ALA ALA A . n 
A 1 355 ILE 355 355 355 ILE ILE A . n 
A 1 356 ASN 356 356 356 ASN ASN A . n 
A 1 357 PRO 357 357 357 PRO PRO A . n 
A 1 358 ASP 358 358 358 ASP ASP A . n 
A 1 359 ARG 359 359 359 ARG ARG A . n 
A 1 360 ARG 360 360 360 ARG ARG A . n 
A 1 361 VAL 361 361 361 VAL VAL A . n 
A 1 362 ALA 362 362 362 ALA ALA A . n 
A 1 363 LYS 363 363 363 LYS LYS A . n 
A 1 364 ALA 364 364 364 ALA ALA A . n 
A 1 365 VAL 365 365 365 VAL VAL A . n 
A 1 366 GLU 366 366 366 GLU GLU A . n 
A 1 367 TYR 367 367 367 TYR TYR A . n 
A 1 368 TYR 368 368 368 TYR TYR A . n 
A 1 369 ASN 369 369 369 ASN ASN A . n 
A 1 370 GLN 370 370 370 GLN GLN A . n 
A 1 371 ASN 371 371 371 ASN ASN A . n 
A 1 372 GLU 372 372 372 GLU GLU A . n 
A 1 373 ALA 373 373 373 ALA ALA A . n 
A 1 374 GLY 374 374 374 GLY GLY A . n 
A 1 375 THR 375 375 375 THR THR A . n 
A 1 376 LEU 376 376 376 LEU LEU A . n 
A 1 377 SER 377 377 377 SER SER A . n 
A 1 378 TYR 378 378 378 TYR TYR A . n 
A 1 379 HIS 379 379 379 HIS HIS A . n 
A 1 380 SER 380 380 380 SER SER A . n 
A 1 381 LEU 381 381 381 LEU LEU A . n 
A 1 382 SER 382 382 382 SER SER A . n 
A 1 383 GLY 383 383 383 GLY GLY A . n 
A 1 384 ASN 384 384 384 ASN ASN A . n 
A 1 385 THR 385 385 385 THR THR A . n 
A 1 386 GLU 386 386 386 GLU GLU A . n 
A 1 387 THR 387 387 387 THR THR A . n 
A 1 388 PHE 388 388 388 PHE PHE A . n 
A 1 389 LEU 389 389 389 LEU LEU A . n 
A 1 390 ALA 390 390 390 ALA ALA A . n 
A 1 391 ILE 391 391 391 ILE ILE A . n 
A 1 392 GLN 392 392 392 GLN GLN A . n 
A 1 393 PRO 393 393 393 PRO PRO A . n 
A 1 394 PHE 394 394 394 PHE PHE A . n 
A 1 395 ASP 395 395 395 ASP ASP A . n 
A 1 396 PHE 396 396 396 PHE PHE A . n 
A 1 397 PHE 397 397 397 PHE PHE A . n 
A 1 398 GLU 398 398 398 GLU GLU A . n 
A 1 399 GLU 399 399 399 GLU GLU A . n 
A 1 400 LYS 400 400 400 LYS LYS A . n 
A 1 401 GLY 401 401 401 GLY GLY A . n 
A 1 402 ASN 402 402 ?   ?   ?   A . n 
A 1 403 ASN 403 403 ?   ?   ?   A . n 
A 1 404 GLY 404 404 ?   ?   ?   A . n 
A 1 405 ASN 405 405 405 ASN ASN A . n 
A 1 406 HIS 406 406 406 HIS HIS A . n 
A 1 407 TRP 407 407 407 TRP TRP A . n 
A 1 408 ARG 408 408 408 ARG ARG A . n 
A 1 409 TRP 409 409 409 TRP TRP A . n 
A 1 410 ALA 410 410 410 ALA ALA A . n 
A 1 411 ILE 411 411 411 ILE ILE A . n 
A 1 412 GLY 412 412 412 GLY GLY A . n 
A 1 413 LYS 413 413 413 LYS LYS A . n 
A 1 414 TYR 414 414 414 TYR TYR A . n 
A 1 415 VAL 415 415 415 VAL VAL A . n 
A 1 416 ASN 416 416 416 ASN ASN A . n 
A 1 417 LYS 417 417 417 LYS LYS A . n 
A 1 418 SER 418 418 418 SER SER A . n 
A 1 419 LEU 419 419 419 LEU LEU A . n 
A 1 420 VAL 420 420 420 VAL VAL A . n 
A 1 421 PHE 421 421 421 PHE PHE A . n 
A 1 422 SER 422 422 422 SER SER A . n 
A 1 423 SER 423 423 423 SER SER A . n 
A 1 424 HIS 424 424 424 HIS HIS A . n 
A 1 425 SER 425 425 425 SER SER A . n 
A 1 426 ASN 426 426 426 ASN ASN A . n 
A 1 427 VAL 427 427 427 VAL VAL A . n 
A 1 428 TYR 428 428 428 TYR TYR A . n 
A 1 429 ILE 429 429 429 ILE ILE A . n 
A 1 430 THR 430 430 430 THR THR A . n 
A 1 431 ALA 431 431 431 ALA ALA A . n 
A 1 432 ASP 432 432 432 ASP ASP A . n 
A 1 433 LYS 433 433 433 LYS LYS A . n 
A 1 434 GLN 434 434 434 GLN GLN A . n 
A 1 435 LYS 435 435 435 LYS LYS A . n 
A 1 436 ASN 436 436 436 ASN ASN A . n 
A 1 437 GLY 437 437 437 GLY GLY A . n 
A 1 438 ILE 438 438 438 ILE ILE A . n 
A 1 439 LYS 439 439 439 LYS LYS A . n 
A 1 440 ALA 440 440 440 ALA ALA A . n 
A 1 441 ASN 441 441 441 ASN ASN A . n 
A 1 442 PHE 442 442 442 PHE PHE A . n 
A 1 443 LYS 443 443 443 LYS LYS A . n 
A 1 444 ILE 444 444 444 ILE ILE A . n 
A 1 445 ARG 445 445 445 ARG ARG A . n 
A 1 446 HIS 446 446 446 HIS HIS A . n 
A 1 447 ASN 447 447 447 ASN ASN A . n 
A 1 448 ILE 448 448 448 ILE ILE A . n 
A 1 449 GLU 449 449 449 GLU GLU A . n 
A 1 450 ASP 450 450 450 ASP ASP A . n 
A 1 451 GLY 451 451 451 GLY GLY A . n 
A 1 452 GLY 452 452 452 GLY GLY A . n 
A 1 453 VAL 453 453 453 VAL VAL A . n 
A 1 454 GLN 454 454 454 GLN GLN A . n 
A 1 455 LEU 455 455 455 LEU LEU A . n 
A 1 456 ALA 456 456 456 ALA ALA A . n 
A 1 457 ASP 457 457 457 ASP ASP A . n 
A 1 458 HIS 458 458 458 HIS HIS A . n 
A 1 459 TYR 459 459 459 TYR TYR A . n 
A 1 460 GLN 460 460 460 GLN GLN A . n 
A 1 461 GLN 461 461 461 GLN GLN A . n 
A 1 462 ASN 462 462 462 ASN ASN A . n 
A 1 463 THR 463 463 463 THR THR A . n 
A 1 464 PRO 464 464 464 PRO PRO A . n 
A 1 465 ILE 465 465 465 ILE ILE A . n 
A 1 466 GLY 466 466 466 GLY GLY A . n 
A 1 467 ASP 467 467 467 ASP ASP A . n 
A 1 468 GLY 468 468 468 GLY GLY A . n 
A 1 469 PRO 469 469 469 PRO PRO A . n 
A 1 470 VAL 470 470 470 VAL VAL A . n 
A 1 471 LEU 471 471 471 LEU LEU A . n 
A 1 472 LEU 472 472 472 LEU LEU A . n 
A 1 473 PRO 473 473 473 PRO PRO A . n 
A 1 474 ASP 474 474 474 ASP ASP A . n 
A 1 475 ASN 475 475 475 ASN ASN A . n 
A 1 476 HIS 476 476 476 HIS HIS A . n 
A 1 477 TYR 477 477 477 TYR TYR A . n 
A 1 478 LEU 478 478 478 LEU LEU A . n 
A 1 479 SER 479 479 479 SER SER A . n 
A 1 480 THR 480 480 480 THR THR A . n 
A 1 481 GLN 481 481 481 GLN GLN A . n 
A 1 482 SER 482 482 482 SER SER A . n 
A 1 483 LYS 483 483 483 LYS LYS A . n 
A 1 484 LEU 484 484 484 LEU LEU A . n 
A 1 485 SER 485 485 485 SER SER A . n 
A 1 486 LYS 486 486 486 LYS LYS A . n 
A 1 487 ASP 487 487 487 ASP ASP A . n 
A 1 488 PRO 488 488 488 PRO PRO A . n 
A 1 489 ASN 489 489 489 ASN ASN A . n 
A 1 490 GLU 490 490 490 GLU GLU A . n 
A 1 491 LYS 491 491 491 LYS LYS A . n 
A 1 492 ARG 492 492 492 ARG ARG A . n 
A 1 493 ASP 493 493 493 ASP ASP A . n 
A 1 494 HIS 494 494 494 HIS HIS A . n 
A 1 495 MET 495 495 495 MET MET A . n 
A 1 496 VAL 496 496 496 VAL VAL A . n 
A 1 497 LEU 497 497 497 LEU LEU A . n 
A 1 498 LEU 498 498 498 LEU LEU A . n 
A 1 499 GLU 499 499 499 GLU GLU A . n 
A 1 500 PHE 500 500 500 PHE PHE A . n 
A 1 501 VAL 501 501 501 VAL VAL A . n 
A 1 502 THR 502 502 502 THR THR A . n 
A 1 503 ALA 503 503 503 ALA ALA A . n 
A 1 504 ALA 504 504 504 ALA ALA A . n 
A 1 505 GLY 505 505 505 GLY GLY A . n 
A 1 506 ILE 506 506 ?   ?   ?   A . n 
A 1 507 THR 507 507 ?   ?   ?   A . n 
A 1 508 LEU 508 508 ?   ?   ?   A . n 
A 1 509 GLY 509 509 ?   ?   ?   A . n 
A 1 510 MET 510 510 ?   ?   ?   A . n 
A 1 511 ASP 511 511 ?   ?   ?   A . n 
A 1 512 GLU 512 512 ?   ?   ?   A . n 
A 1 513 LEU 513 513 ?   ?   ?   A . n 
A 1 514 TYR 514 514 ?   ?   ?   A . n 
A 1 515 GLN 515 515 ?   ?   ?   A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        SWG 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   SWG 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 HOH 1 601 1 HOH HOH A . 
B 2 HOH 2 602 2 HOH HOH A . 
B 2 HOH 3 603 4 HOH HOH A . 
B 2 HOH 4 604 5 HOH HOH A . 
B 2 HOH 5 605 6 HOH HOH A . 
B 2 HOH 6 606 3 HOH HOH A . 
B 2 HOH 7 607 8 HOH HOH A . 
B 2 HOH 8 608 9 HOH HOH A . 
B 2 HOH 9 609 7 HOH HOH A . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1   1 Y 1 A LYS 12  ? CG  ? A LYS 12  CG  
2   1 Y 1 A LYS 12  ? CD  ? A LYS 12  CD  
3   1 Y 1 A LYS 12  ? CE  ? A LYS 12  CE  
4   1 Y 1 A LYS 12  ? NZ  ? A LYS 12  NZ  
5   1 Y 1 A GLU 14  ? CG  ? A GLU 14  CG  
6   1 Y 1 A GLU 14  ? CD  ? A GLU 14  CD  
7   1 Y 1 A GLU 14  ? OE1 ? A GLU 14  OE1 
8   1 Y 1 A GLU 14  ? OE2 ? A GLU 14  OE2 
9   1 Y 1 A GLU 15  ? CG  ? A GLU 15  CG  
10  1 Y 1 A GLU 15  ? CD  ? A GLU 15  CD  
11  1 Y 1 A GLU 15  ? OE1 ? A GLU 15  OE1 
12  1 Y 1 A GLU 15  ? OE2 ? A GLU 15  OE2 
13  1 Y 1 A LEU 16  ? CD2 ? A LEU 16  CD2 
14  1 Y 1 A LYS 35  ? CG  ? A LYS 35  CG  
15  1 Y 1 A LYS 35  ? CD  ? A LYS 35  CD  
16  1 Y 1 A LYS 35  ? CE  ? A LYS 35  CE  
17  1 Y 1 A LYS 35  ? NZ  ? A LYS 35  NZ  
18  1 Y 1 A GLU 41  ? CG  ? A GLU 41  CG  
19  1 Y 1 A GLU 41  ? CD  ? A GLU 41  CD  
20  1 Y 1 A GLU 41  ? OE1 ? A GLU 41  OE1 
21  1 Y 1 A GLU 41  ? OE2 ? A GLU 41  OE2 
22  1 Y 1 A GLU 43  ? CG  ? A GLU 43  CG  
23  1 Y 1 A GLU 43  ? CD  ? A GLU 43  CD  
24  1 Y 1 A GLU 43  ? OE1 ? A GLU 43  OE1 
25  1 Y 1 A GLU 43  ? OE2 ? A GLU 43  OE2 
26  1 Y 1 A TYR 48  ? CG  ? A TYR 48  CG  
27  1 Y 1 A TYR 48  ? CD1 ? A TYR 48  CD1 
28  1 Y 1 A TYR 48  ? CD2 ? A TYR 48  CD2 
29  1 Y 1 A TYR 48  ? CE1 ? A TYR 48  CE1 
30  1 Y 1 A TYR 48  ? CE2 ? A TYR 48  CE2 
31  1 Y 1 A TYR 48  ? CZ  ? A TYR 48  CZ  
32  1 Y 1 A TYR 48  ? OH  ? A TYR 48  OH  
33  1 Y 1 A LYS 50  ? CG  ? A LYS 50  CG  
34  1 Y 1 A LYS 50  ? CD  ? A LYS 50  CD  
35  1 Y 1 A LYS 50  ? CE  ? A LYS 50  CE  
36  1 Y 1 A LYS 50  ? NZ  ? A LYS 50  NZ  
37  1 Y 1 A LEU 51  ? CG  ? A LEU 51  CG  
38  1 Y 1 A LEU 51  ? CD1 ? A LEU 51  CD1 
39  1 Y 1 A LEU 51  ? CD2 ? A LEU 51  CD2 
40  1 Y 1 A ILE 56  ? CD1 ? A ILE 56  CD1 
41  1 Y 1 A LYS 61  ? CG  ? A LYS 61  CG  
42  1 Y 1 A LYS 61  ? CD  ? A LYS 61  CD  
43  1 Y 1 A LYS 61  ? CE  ? A LYS 61  CE  
44  1 Y 1 A LYS 61  ? NZ  ? A LYS 61  NZ  
45  1 Y 1 A ARG 80  ? CZ  ? A ARG 80  CZ  
46  1 Y 1 A ARG 80  ? NH1 ? A ARG 80  NH1 
47  1 Y 1 A ARG 80  ? NH2 ? A ARG 80  NH2 
48  1 Y 1 A ASP 83  ? CG  ? A ASP 83  CG  
49  1 Y 1 A ASP 83  ? OD1 ? A ASP 83  OD1 
50  1 Y 1 A ASP 83  ? OD2 ? A ASP 83  OD2 
51  1 Y 1 A HIS 84  ? CG  ? A HIS 84  CG  
52  1 Y 1 A HIS 84  ? ND1 ? A HIS 84  ND1 
53  1 Y 1 A HIS 84  ? CD2 ? A HIS 84  CD2 
54  1 Y 1 A HIS 84  ? CE1 ? A HIS 84  CE1 
55  1 Y 1 A HIS 84  ? NE2 ? A HIS 84  NE2 
56  1 Y 1 A MET 85  ? CG  ? A MET 85  CG  
57  1 Y 1 A MET 85  ? SD  ? A MET 85  SD  
58  1 Y 1 A MET 85  ? CE  ? A MET 85  CE  
59  1 Y 1 A LYS 86  ? CG  ? A LYS 86  CG  
60  1 Y 1 A LYS 86  ? CD  ? A LYS 86  CD  
61  1 Y 1 A LYS 86  ? CE  ? A LYS 86  CE  
62  1 Y 1 A LYS 86  ? NZ  ? A LYS 86  NZ  
63  1 Y 1 A GLN 87  ? CG  ? A GLN 87  CG  
64  1 Y 1 A GLN 87  ? CD  ? A GLN 87  CD  
65  1 Y 1 A GLN 87  ? OE1 ? A GLN 87  OE1 
66  1 Y 1 A GLN 87  ? NE2 ? A GLN 87  NE2 
67  1 Y 1 A ASP 89  ? CG  ? A ASP 89  CG  
68  1 Y 1 A ASP 89  ? OD1 ? A ASP 89  OD1 
69  1 Y 1 A ASP 89  ? OD2 ? A ASP 89  OD2 
70  1 Y 1 A SER 93  ? OG  ? A SER 93  OG  
71  1 Y 1 A GLU 97  ? CG  ? A GLU 97  CG  
72  1 Y 1 A GLU 97  ? CD  ? A GLU 97  CD  
73  1 Y 1 A GLU 97  ? OE1 ? A GLU 97  OE1 
74  1 Y 1 A GLU 97  ? OE2 ? A GLU 97  OE2 
75  1 Y 1 A LYS 108 ? CE  ? A LYS 108 CE  
76  1 Y 1 A LYS 108 ? NZ  ? A LYS 108 NZ  
77  1 Y 1 A LYS 120 ? NZ  ? A LYS 120 NZ  
78  1 Y 1 A VAL 127 ? CG1 ? A VAL 127 CG1 
79  1 Y 1 A VAL 127 ? CG2 ? A VAL 127 CG2 
80  1 Y 1 A LYS 133 ? CG  ? A LYS 133 CG  
81  1 Y 1 A LYS 133 ? CD  ? A LYS 133 CD  
82  1 Y 1 A LYS 133 ? CE  ? A LYS 133 CE  
83  1 Y 1 A LYS 133 ? NZ  ? A LYS 133 NZ  
84  1 Y 1 A LYS 138 ? CG  ? A LYS 138 CG  
85  1 Y 1 A LYS 138 ? CD  ? A LYS 138 CD  
86  1 Y 1 A LYS 138 ? CE  ? A LYS 138 CE  
87  1 Y 1 A LYS 138 ? NZ  ? A LYS 138 NZ  
88  1 Y 1 A ASP 140 ? CG  ? A ASP 140 CG  
89  1 Y 1 A ASP 140 ? OD1 ? A ASP 140 OD1 
90  1 Y 1 A ASP 140 ? OD2 ? A ASP 140 OD2 
91  1 Y 1 A LYS 147 ? CE  ? A LYS 147 CE  
92  1 Y 1 A LYS 147 ? NZ  ? A LYS 147 NZ  
93  1 Y 1 A SER 153 ? OG  ? A SER 153 OG  
94  1 Y 1 A PHE 161 ? CG  ? A PHE 161 CG  
95  1 Y 1 A PHE 161 ? CD1 ? A PHE 161 CD1 
96  1 Y 1 A PHE 161 ? CD2 ? A PHE 161 CD2 
97  1 Y 1 A PHE 161 ? CE1 ? A PHE 161 CE1 
98  1 Y 1 A PHE 161 ? CE2 ? A PHE 161 CE2 
99  1 Y 1 A PHE 161 ? CZ  ? A PHE 161 CZ  
100 1 Y 1 A VAL 165 ? CG1 ? A VAL 165 CG1 
101 1 Y 1 A VAL 165 ? CG2 ? A VAL 165 CG2 
102 1 Y 1 A LEU 166 ? CG  ? A LEU 166 CG  
103 1 Y 1 A LEU 166 ? CD1 ? A LEU 166 CD1 
104 1 Y 1 A LEU 166 ? CD2 ? A LEU 166 CD2 
105 1 Y 1 A GLN 167 ? CG  ? A GLN 167 CG  
106 1 Y 1 A GLN 167 ? CD  ? A GLN 167 CD  
107 1 Y 1 A GLN 167 ? OE1 ? A GLN 167 OE1 
108 1 Y 1 A GLN 167 ? NE2 ? A GLN 167 NE2 
109 1 Y 1 A SER 168 ? OG  ? A SER 168 OG  
110 1 Y 1 A GLN 169 ? CG  ? A GLN 169 CG  
111 1 Y 1 A GLN 169 ? CD  ? A GLN 169 CD  
112 1 Y 1 A GLN 169 ? OE1 ? A GLN 169 OE1 
113 1 Y 1 A GLN 169 ? NE2 ? A GLN 169 NE2 
114 1 Y 1 A THR 171 ? OG1 ? A THR 171 OG1 
115 1 Y 1 A THR 171 ? CG2 ? A THR 171 CG2 
116 1 Y 1 A GLU 172 ? CG  ? A GLU 172 CG  
117 1 Y 1 A GLU 172 ? CD  ? A GLU 172 CD  
118 1 Y 1 A GLU 172 ? OE1 ? A GLU 172 OE1 
119 1 Y 1 A GLU 172 ? OE2 ? A GLU 172 OE2 
120 1 Y 1 A LEU 173 ? CG  ? A LEU 173 CG  
121 1 Y 1 A LEU 173 ? CD1 ? A LEU 173 CD1 
122 1 Y 1 A LEU 173 ? CD2 ? A LEU 173 CD2 
123 1 Y 1 A LEU 174 ? CG  ? A LEU 174 CG  
124 1 Y 1 A LEU 174 ? CD1 ? A LEU 174 CD1 
125 1 Y 1 A LEU 174 ? CD2 ? A LEU 174 CD2 
126 1 Y 1 A LYS 176 ? CG  ? A LYS 176 CG  
127 1 Y 1 A LYS 176 ? CD  ? A LYS 176 CD  
128 1 Y 1 A LYS 176 ? CE  ? A LYS 176 CE  
129 1 Y 1 A LYS 176 ? NZ  ? A LYS 176 NZ  
130 1 Y 1 A LYS 177 ? CG  ? A LYS 177 CG  
131 1 Y 1 A LYS 177 ? CD  ? A LYS 177 CD  
132 1 Y 1 A LYS 177 ? CE  ? A LYS 177 CE  
133 1 Y 1 A LYS 177 ? NZ  ? A LYS 177 NZ  
134 1 Y 1 A LEU 180 ? CG  ? A LEU 180 CG  
135 1 Y 1 A LEU 180 ? CD1 ? A LEU 180 CD1 
136 1 Y 1 A LEU 180 ? CD2 ? A LEU 180 CD2 
137 1 Y 1 A GLN 186 ? CG  ? A GLN 186 CG  
138 1 Y 1 A GLN 186 ? CD  ? A GLN 186 CD  
139 1 Y 1 A GLN 186 ? OE1 ? A GLN 186 OE1 
140 1 Y 1 A GLN 186 ? NE2 ? A GLN 186 NE2 
141 1 Y 1 A LYS 190 ? CG  ? A LYS 190 CG  
142 1 Y 1 A LYS 190 ? CD  ? A LYS 190 CD  
143 1 Y 1 A LYS 190 ? CE  ? A LYS 190 CE  
144 1 Y 1 A LYS 190 ? NZ  ? A LYS 190 NZ  
145 1 Y 1 A SER 208 ? OG  ? A SER 208 OG  
146 1 Y 1 A THR 213 ? OG1 ? A THR 213 OG1 
147 1 Y 1 A THR 213 ? CG2 ? A THR 213 CG2 
148 1 Y 1 A ARG 217 ? CG  ? A ARG 217 CG  
149 1 Y 1 A ARG 217 ? CD  ? A ARG 217 CD  
150 1 Y 1 A ARG 217 ? NE  ? A ARG 217 NE  
151 1 Y 1 A ARG 217 ? CZ  ? A ARG 217 CZ  
152 1 Y 1 A ARG 217 ? NH1 ? A ARG 217 NH1 
153 1 Y 1 A ARG 217 ? NH2 ? A ARG 217 NH2 
154 1 Y 1 A ASN 239 ? CG  ? A ASN 239 CG  
155 1 Y 1 A ASN 239 ? OD1 ? A ASN 239 OD1 
156 1 Y 1 A ASN 239 ? ND2 ? A ASN 239 ND2 
157 1 Y 1 A GLU 241 ? CG  ? A GLU 241 CG  
158 1 Y 1 A GLU 241 ? CD  ? A GLU 241 CD  
159 1 Y 1 A GLU 241 ? OE1 ? A GLU 241 OE1 
160 1 Y 1 A GLU 241 ? OE2 ? A GLU 241 OE2 
161 1 Y 1 A ASN 257 ? CG  ? A ASN 257 CG  
162 1 Y 1 A ASN 257 ? OD1 ? A ASN 257 OD1 
163 1 Y 1 A ASN 257 ? ND2 ? A ASN 257 ND2 
164 1 Y 1 A ASN 261 ? CG  ? A ASN 261 CG  
165 1 Y 1 A ASN 261 ? OD1 ? A ASN 261 OD1 
166 1 Y 1 A ASN 261 ? ND2 ? A ASN 261 ND2 
167 1 Y 1 A GLU 262 ? CG  ? A GLU 262 CG  
168 1 Y 1 A GLU 262 ? CD  ? A GLU 262 CD  
169 1 Y 1 A GLU 262 ? OE1 ? A GLU 262 OE1 
170 1 Y 1 A GLU 262 ? OE2 ? A GLU 262 OE2 
171 1 Y 1 A ASN 263 ? CG  ? A ASN 263 CG  
172 1 Y 1 A ASN 263 ? OD1 ? A ASN 263 OD1 
173 1 Y 1 A ASN 263 ? ND2 ? A ASN 263 ND2 
174 1 Y 1 A THR 265 ? OG1 ? A THR 265 OG1 
175 1 Y 1 A THR 265 ? CG2 ? A THR 265 CG2 
176 1 Y 1 A GLN 267 ? CG  ? A GLN 267 CG  
177 1 Y 1 A GLN 267 ? CD  ? A GLN 267 CD  
178 1 Y 1 A GLN 267 ? OE1 ? A GLN 267 OE1 
179 1 Y 1 A GLN 267 ? NE2 ? A GLN 267 NE2 
180 1 Y 1 A ILE 268 ? CG1 ? A ILE 268 CG1 
181 1 Y 1 A ILE 268 ? CG2 ? A ILE 268 CG2 
182 1 Y 1 A ILE 268 ? CD1 ? A ILE 268 CD1 
183 1 Y 1 A SER 270 ? OG  ? A SER 270 OG  
184 1 Y 1 A GLU 283 ? CG  ? A GLU 283 CG  
185 1 Y 1 A GLU 283 ? CD  ? A GLU 283 CD  
186 1 Y 1 A GLU 283 ? OE1 ? A GLU 283 OE1 
187 1 Y 1 A GLU 283 ? OE2 ? A GLU 283 OE2 
188 1 Y 1 A VAL 284 ? CG1 ? A VAL 284 CG1 
189 1 Y 1 A VAL 284 ? CG2 ? A VAL 284 CG2 
190 1 Y 1 A ASN 285 ? CG  ? A ASN 285 CG  
191 1 Y 1 A ASN 285 ? OD1 ? A ASN 285 OD1 
192 1 Y 1 A ASN 285 ? ND2 ? A ASN 285 ND2 
193 1 Y 1 A ASP 287 ? CG  ? A ASP 287 CG  
194 1 Y 1 A ASP 287 ? OD1 ? A ASP 287 OD1 
195 1 Y 1 A ASP 287 ? OD2 ? A ASP 287 OD2 
196 1 Y 1 A LYS 301 ? CG  ? A LYS 301 CG  
197 1 Y 1 A LYS 301 ? CD  ? A LYS 301 CD  
198 1 Y 1 A LYS 301 ? CE  ? A LYS 301 CE  
199 1 Y 1 A LYS 301 ? NZ  ? A LYS 301 NZ  
200 1 Y 1 A ASN 302 ? CG  ? A ASN 302 CG  
201 1 Y 1 A ASN 302 ? OD1 ? A ASN 302 OD1 
202 1 Y 1 A ASN 302 ? ND2 ? A ASN 302 ND2 
203 1 Y 1 A ILE 306 ? CD1 ? A ILE 306 CD1 
204 1 Y 1 A THR 320 ? OG1 ? A THR 320 OG1 
205 1 Y 1 A THR 320 ? CG2 ? A THR 320 CG2 
206 1 Y 1 A LYS 325 ? CE  ? A LYS 325 CE  
207 1 Y 1 A LYS 325 ? NZ  ? A LYS 325 NZ  
208 1 Y 1 A LYS 326 ? CG  ? A LYS 326 CG  
209 1 Y 1 A LYS 326 ? CD  ? A LYS 326 CD  
210 1 Y 1 A LYS 326 ? CE  ? A LYS 326 CE  
211 1 Y 1 A LYS 326 ? NZ  ? A LYS 326 NZ  
212 1 Y 1 A LYS 327 ? CG  ? A LYS 327 CG  
213 1 Y 1 A LYS 327 ? CD  ? A LYS 327 CD  
214 1 Y 1 A LYS 327 ? CE  ? A LYS 327 CE  
215 1 Y 1 A LYS 327 ? NZ  ? A LYS 327 NZ  
216 1 Y 1 A ARG 345 ? CG  ? A ARG 345 CG  
217 1 Y 1 A ARG 345 ? CD  ? A ARG 345 CD  
218 1 Y 1 A ARG 345 ? NE  ? A ARG 345 NE  
219 1 Y 1 A ARG 345 ? CZ  ? A ARG 345 CZ  
220 1 Y 1 A ARG 345 ? NH1 ? A ARG 345 NH1 
221 1 Y 1 A ARG 345 ? NH2 ? A ARG 345 NH2 
222 1 Y 1 A GLU 346 ? CG  ? A GLU 346 CG  
223 1 Y 1 A GLU 346 ? CD  ? A GLU 346 CD  
224 1 Y 1 A GLU 346 ? OE1 ? A GLU 346 OE1 
225 1 Y 1 A GLU 346 ? OE2 ? A GLU 346 OE2 
226 1 Y 1 A LYS 350 ? CG  ? A LYS 350 CG  
227 1 Y 1 A LYS 350 ? CD  ? A LYS 350 CD  
228 1 Y 1 A LYS 350 ? CE  ? A LYS 350 CE  
229 1 Y 1 A LYS 350 ? NZ  ? A LYS 350 NZ  
230 1 Y 1 A ARG 359 ? CD  ? A ARG 359 CD  
231 1 Y 1 A ARG 359 ? NE  ? A ARG 359 NE  
232 1 Y 1 A ARG 359 ? CZ  ? A ARG 359 CZ  
233 1 Y 1 A ARG 359 ? NH1 ? A ARG 359 NH1 
234 1 Y 1 A ARG 359 ? NH2 ? A ARG 359 NH2 
235 1 Y 1 A LYS 363 ? CE  ? A LYS 363 CE  
236 1 Y 1 A LYS 363 ? NZ  ? A LYS 363 NZ  
237 1 Y 1 A GLN 370 ? CG  ? A GLN 370 CG  
238 1 Y 1 A GLN 370 ? CD  ? A GLN 370 CD  
239 1 Y 1 A GLN 370 ? OE1 ? A GLN 370 OE1 
240 1 Y 1 A GLN 370 ? NE2 ? A GLN 370 NE2 
241 1 Y 1 A LEU 381 ? CG  ? A LEU 381 CG  
242 1 Y 1 A LEU 381 ? CD1 ? A LEU 381 CD1 
243 1 Y 1 A LEU 381 ? CD2 ? A LEU 381 CD2 
244 1 Y 1 A SER 382 ? OG  ? A SER 382 OG  
245 1 Y 1 A ILE 391 ? CG1 ? A ILE 391 CG1 
246 1 Y 1 A ILE 391 ? CG2 ? A ILE 391 CG2 
247 1 Y 1 A ILE 391 ? CD1 ? A ILE 391 CD1 
248 1 Y 1 A GLU 399 ? CG  ? A GLU 399 CG  
249 1 Y 1 A GLU 399 ? CD  ? A GLU 399 CD  
250 1 Y 1 A GLU 399 ? OE1 ? A GLU 399 OE1 
251 1 Y 1 A GLU 399 ? OE2 ? A GLU 399 OE2 
252 1 Y 1 A LYS 400 ? CG  ? A LYS 400 CG  
253 1 Y 1 A LYS 400 ? CD  ? A LYS 400 CD  
254 1 Y 1 A LYS 400 ? CE  ? A LYS 400 CE  
255 1 Y 1 A LYS 400 ? NZ  ? A LYS 400 NZ  
256 1 Y 1 A ASN 405 ? CG  ? A ASN 405 CG  
257 1 Y 1 A ASN 405 ? OD1 ? A ASN 405 OD1 
258 1 Y 1 A ASN 405 ? ND2 ? A ASN 405 ND2 
259 1 Y 1 A HIS 406 ? CG  ? A HIS 406 CG  
260 1 Y 1 A HIS 406 ? ND1 ? A HIS 406 ND1 
261 1 Y 1 A HIS 406 ? CD2 ? A HIS 406 CD2 
262 1 Y 1 A HIS 406 ? CE1 ? A HIS 406 CE1 
263 1 Y 1 A HIS 406 ? NE2 ? A HIS 406 NE2 
264 1 Y 1 A LYS 413 ? CG  ? A LYS 413 CG  
265 1 Y 1 A LYS 413 ? CD  ? A LYS 413 CD  
266 1 Y 1 A LYS 413 ? CE  ? A LYS 413 CE  
267 1 Y 1 A LYS 413 ? NZ  ? A LYS 413 NZ  
268 1 Y 1 A VAL 415 ? CG1 ? A VAL 415 CG1 
269 1 Y 1 A VAL 415 ? CG2 ? A VAL 415 CG2 
270 1 Y 1 A ASN 416 ? CG  ? A ASN 416 CG  
271 1 Y 1 A ASN 416 ? OD1 ? A ASN 416 OD1 
272 1 Y 1 A ASN 416 ? ND2 ? A ASN 416 ND2 
273 1 Y 1 A LYS 417 ? CG  ? A LYS 417 CG  
274 1 Y 1 A LYS 417 ? CD  ? A LYS 417 CD  
275 1 Y 1 A LYS 417 ? CE  ? A LYS 417 CE  
276 1 Y 1 A LYS 417 ? NZ  ? A LYS 417 NZ  
277 1 Y 1 A SER 418 ? OG  ? A SER 418 OG  
278 1 Y 1 A LEU 419 ? CG  ? A LEU 419 CG  
279 1 Y 1 A LEU 419 ? CD1 ? A LEU 419 CD1 
280 1 Y 1 A LEU 419 ? CD2 ? A LEU 419 CD2 
281 1 Y 1 A ILE 429 ? CG1 ? A ILE 429 CG1 
282 1 Y 1 A ILE 429 ? CG2 ? A ILE 429 CG2 
283 1 Y 1 A ILE 429 ? CD1 ? A ILE 429 CD1 
284 1 Y 1 A ASP 432 ? CG  ? A ASP 432 CG  
285 1 Y 1 A ASP 432 ? OD1 ? A ASP 432 OD1 
286 1 Y 1 A ASP 432 ? OD2 ? A ASP 432 OD2 
287 1 Y 1 A LYS 433 ? CG  ? A LYS 433 CG  
288 1 Y 1 A LYS 433 ? CD  ? A LYS 433 CD  
289 1 Y 1 A LYS 433 ? CE  ? A LYS 433 CE  
290 1 Y 1 A LYS 433 ? NZ  ? A LYS 433 NZ  
291 1 Y 1 A GLN 434 ? CG  ? A GLN 434 CG  
292 1 Y 1 A GLN 434 ? CD  ? A GLN 434 CD  
293 1 Y 1 A GLN 434 ? OE1 ? A GLN 434 OE1 
294 1 Y 1 A GLN 434 ? NE2 ? A GLN 434 NE2 
295 1 Y 1 A ILE 438 ? CD1 ? A ILE 438 CD1 
296 1 Y 1 A LYS 439 ? CG  ? A LYS 439 CG  
297 1 Y 1 A LYS 439 ? CD  ? A LYS 439 CD  
298 1 Y 1 A LYS 439 ? CE  ? A LYS 439 CE  
299 1 Y 1 A LYS 439 ? NZ  ? A LYS 439 NZ  
300 1 Y 1 A ASN 441 ? CG  ? A ASN 441 CG  
301 1 Y 1 A ASN 441 ? OD1 ? A ASN 441 OD1 
302 1 Y 1 A ASN 441 ? ND2 ? A ASN 441 ND2 
303 1 Y 1 A LYS 443 ? CG  ? A LYS 443 CG  
304 1 Y 1 A LYS 443 ? CD  ? A LYS 443 CD  
305 1 Y 1 A LYS 443 ? CE  ? A LYS 443 CE  
306 1 Y 1 A LYS 443 ? NZ  ? A LYS 443 NZ  
307 1 Y 1 A ASP 450 ? CG  ? A ASP 450 CG  
308 1 Y 1 A ASP 450 ? OD1 ? A ASP 450 OD1 
309 1 Y 1 A ASP 450 ? OD2 ? A ASP 450 OD2 
310 1 Y 1 A ILE 465 ? CG1 ? A ILE 465 CG1 
311 1 Y 1 A ILE 465 ? CG2 ? A ILE 465 CG2 
312 1 Y 1 A ILE 465 ? CD1 ? A ILE 465 CD1 
313 1 Y 1 A ASP 467 ? CG  ? A ASP 467 CG  
314 1 Y 1 A ASP 467 ? OD1 ? A ASP 467 OD1 
315 1 Y 1 A ASP 467 ? OD2 ? A ASP 467 OD2 
316 1 Y 1 A VAL 470 ? CG1 ? A VAL 470 CG1 
317 1 Y 1 A VAL 470 ? CG2 ? A VAL 470 CG2 
318 1 Y 1 A LEU 471 ? CG  ? A LEU 471 CG  
319 1 Y 1 A LEU 471 ? CD1 ? A LEU 471 CD1 
320 1 Y 1 A LEU 471 ? CD2 ? A LEU 471 CD2 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX  ? ? ? '1.20.1_4487: 000' 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? 1.19               2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? 0.7.15             3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER  ? ? ? 2.8.3              4 
# 
_cell.angle_alpha                  97.82 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   91.43 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  104.24 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9EBX 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     34.350 
_cell.length_a_esd                 ? 
_cell.length_b                     57.980 
_cell.length_b_esd                 ? 
_cell.length_c                     67.319 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        1 
_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                         9EBX 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                1 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 1' 
_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                   9EBX 
_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             2.22 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          44.6 
_exptl_crystal.description                  'Bright yellow chunky diamond-shaped crystals, 200 x 100 um' 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_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    'magnesium chloride hexahydrate, HEPES, PEG 3350' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            296 
# 
_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 EIGER X 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         2022-07-07 
_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   0.978532 
_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                        'APS BEAMLINE 23-ID-B' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.978532 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   23-ID-B 
_diffrn_source.pdbx_synchrotron_site       APS 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9EBX 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.42 
_reflns.d_resolution_low                               46.13 
_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                                     16566 
_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                           86.92 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                1.9 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          12.56 
_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                                0.04407 
_reflns.pdbx_Rpim_I_all                                0.03116 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.999 
_reflns.pdbx_CC_star                                   1 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.03116 
_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                                    2.42 
_reflns_shell.d_res_low                                     2.507 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.75 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             1775 
_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                               1.9 
_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                               0.5253 
_reflns_shell.pdbx_Rpim_I_all                               0.3715 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.874 
_reflns_shell.pdbx_CC_star                                  0.966 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          92.11 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.3715 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9EBX 
_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                            2.42 
_refine.ls_d_res_low                             46.13 
_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                     16566 
_refine.ls_number_reflns_R_free                  1645 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    86.86 
_refine.ls_percent_reflns_R_free                 9.93 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2386 
_refine.ls_R_factor_R_free                       0.2796 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2340 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.97 
_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       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.10 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 37.03 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.43 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.42 
_refine_hist.d_res_low                        46.13 
_refine_hist.number_atoms_solvent             9 
_refine_hist.number_atoms_total               3527 
_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        3518 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         0 
_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' ? 0.009  ? 3590 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.242  ? 4888 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 15.868 ? 1205 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.060  ? 559  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.015  ? 639  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.42 2.49  . . 157 1304 91.00 . . . . 0.3395 . . . . . . . . . . . 0.3991 
'X-RAY DIFFRACTION' 2.49 2.57  . . 133 1292 91.00 . . . . 0.3228 . . . . . . . . . . . 0.3463 
'X-RAY DIFFRACTION' 2.57 2.66  . . 146 1276 88.00 . . . . 0.3012 . . . . . . . . . . . 0.3733 
'X-RAY DIFFRACTION' 2.66 2.77  . . 125 1218 84.00 . . . . 0.3156 . . . . . . . . . . . 0.4507 
'X-RAY DIFFRACTION' 2.77 2.89  . . 131 1165 82.00 . . . . 0.3381 . . . . . . . . . . . 0.3974 
'X-RAY DIFFRACTION' 2.89 3.04  . . 143 1275 90.00 . . . . 0.2953 . . . . . . . . . . . 0.3784 
'X-RAY DIFFRACTION' 3.04 3.24  . . 148 1287 90.00 . . . . 0.2746 . . . . . . . . . . . 0.3413 
'X-RAY DIFFRACTION' 3.24 3.48  . . 121 1230 85.00 . . . . 0.2867 . . . . . . . . . . . 0.3550 
'X-RAY DIFFRACTION' 3.49 3.84  . . 138 1201 84.00 . . . . 0.2529 . . . . . . . . . . . 0.3032 
'X-RAY DIFFRACTION' 3.84 4.39  . . 121 1121 78.00 . . . . 0.2056 . . . . . . . . . . . 0.2545 
'X-RAY DIFFRACTION' 4.39 5.53  . . 147 1310 92.00 . . . . 0.1905 . . . . . . . . . . . 0.2298 
'X-RAY DIFFRACTION' 5.53 46.13 . . 135 1242 87.00 . . . . 0.1911 . . . . . . . . . . . 0.2053 
# 
_struct.entry_id                     9EBX 
_struct.title                        'Chimeric fluorescence biosensor formed from a lactate-binding protein and GFP' 
_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        9EBX 
_struct_keywords.text            'Biosensor, Binding protein, Chimera, FLUORESCENT PROTEIN' 
_struct_keywords.pdbx_keywords   'FLUORESCENT PROTEIN' 
# 
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 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP GFP_AEQVI    P42212 ? 1 
;SKGEELFTGVVPILVELDGDVNGHKFSVSGEGEGDATYGKLTLKFICTTGKLPVPWPTLVTTFSYGVQCFSRYPDHMKQH
DFFKSAMPEGYVQERTIFFKDDGNYKTRAEVKFEGDTLVNRIELKGIDFKEDGNILGHKLEYNYN
;
2   
2 UNP O24911_HELPY O24911 ? 1 
;SYKVESVLQSQATELLQKKAQLVSFKIQGIMKRIFMGANTLEKFLSDENSAINDTLKRRMLSEFLLANPHVLLVSAIYTN
NNERVITAMSMDSKIAYPNTTLNENMTNQIRSLKSITHSDPYYKEVNGDKIYGMDITLPLMGKNQNAIGALNFFLNIDAF
YTDVVGKKKSNTFLMGKDGRLLINPNREIQDKILSAINPDRRVAKAVEYYNQNEAGTLSYHSLSGNTETFLAIQPFDFFE
EKGNNGNHWRWAIGKYVNKSLVF
;
30  
3 UNP GFP_AEQVI    P42212 ? 1 
;NVYIMADKQKNGIKVNFKIRHNIEDGSVQLADHYQQNTPIGDGPVLLPDNHYLSTQSALSKDPNEKRDHMVLLEFVTAAG
ITHGMDELYK
;
149 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 9EBX A 11  ? 153 ? P42212 2   ? 146 ? 11  153 
2 2 9EBX A 159 ? 421 ? O24911 30  ? 292 ? 159 421 
3 3 9EBX A 426 ? 515 ? P42212 149 ? 238 ? 426 515 
# 
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 9EBX MET A 1   ? UNP P42212 ?   ?   'initiating methionine' 1   1  
1 9EBX LYS A 2   ? UNP P42212 ?   ?   'expression tag'        2   2  
1 9EBX HIS A 3   ? UNP P42212 ?   ?   'expression tag'        3   3  
1 9EBX HIS A 4   ? UNP P42212 ?   ?   'expression tag'        4   4  
1 9EBX HIS A 5   ? UNP P42212 ?   ?   'expression tag'        5   5  
1 9EBX HIS A 6   ? UNP P42212 ?   ?   'expression tag'        6   6  
1 9EBX HIS A 7   ? UNP P42212 ?   ?   'expression tag'        7   7  
1 9EBX HIS A 8   ? UNP P42212 ?   ?   'expression tag'        8   8  
1 9EBX HIS A 9   ? UNP P42212 ?   ?   'expression tag'        9   9  
1 9EBX VAL A 10  ? UNP P42212 ?   ?   'expression tag'        10  10 
1 9EBX LEU A 73  ? UNP P42212 PHE 64  conflict                73  11 
1 9EBX SWG A 74  ? UNP P42212 SER 65  chromophore             74  12 
1 9EBX SWG A 74  ? UNP P42212 TYR 66  chromophore             74  13 
1 9EBX SWG A 74  ? UNP P42212 GLY 67  chromophore             74  14 
1 9EBX ALA A 79  ? UNP P42212 SER 72  conflict                79  15 
1 9EBX SER A 152 ? UNP P42212 TYR 145 conflict                152 16 
1 9EBX SER A 153 ? UNP P42212 ASN 146 conflict                153 17 
1 9EBX GLY A 154 ? UNP P42212 ?   ?   linker                  154 18 
1 9EBX ARG A 155 ? UNP P42212 ?   ?   linker                  155 19 
1 9EBX THR A 156 ? UNP P42212 ?   ?   linker                  156 20 
1 9EBX GLY A 157 ? UNP P42212 ?   ?   linker                  157 21 
1 9EBX ILE A 158 ? UNP P42212 ?   ?   linker                  158 22 
2 9EBX ASP A 159 ? UNP O24911 SER 30  conflict                159 23 
2 9EBX PRO A 160 ? UNP O24911 TYR 31  conflict                160 24 
2 9EBX PHE A 161 ? UNP O24911 LYS 32  conflict                161 25 
2 9EBX THR A 162 ? UNP O24911 VAL 33  conflict                162 26 
2 9EBX SER A 422 ? UNP O24911 ?   ?   linker                  422 27 
2 9EBX SER A 423 ? UNP O24911 ?   ?   linker                  423 28 
2 9EBX HIS A 424 ? UNP O24911 ?   ?   linker                  424 29 
2 9EBX SER A 425 ? UNP O24911 ?   ?   linker                  425 30 
3 9EBX THR A 430 ? UNP P42212 MET 153 conflict                430 31 
3 9EBX ALA A 440 ? UNP P42212 VAL 163 conflict                440 32 
3 9EBX GLY A 452 ? UNP P42212 SER 175 conflict                452 33 
3 9EBX LYS A 483 ? UNP P42212 ALA 206 conflict                483 34 
3 9EBX LEU A 508 ? UNP P42212 HIS 231 conflict                508 35 
3 9EBX GLN A 515 ? UNP P42212 LYS 238 conflict                515 36 
# 
_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 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B 
# 
_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 PRO A 65  ? VAL A 70  ? PRO A 65  VAL A 70  5 ? 6  
HELX_P HELX_P2  AA2 PHE A 90  ? ALA A 94  ? PHE A 90  ALA A 94  1 ? 5  
HELX_P HELX_P3  AA3 LEU A 166 ? SER A 204 ? LEU A 166 SER A 204 1 ? 39 
HELX_P HELX_P4  AA4 ASN A 211 ? ASN A 226 ? ASN A 211 ASN A 226 1 ? 16 
HELX_P HELX_P5  AA5 ASN A 263 ? LEU A 271 ? ASN A 263 LEU A 271 1 ? 9  
HELX_P HELX_P6  AA6 PHE A 318 ? VAL A 323 ? PHE A 318 VAL A 323 1 ? 6  
HELX_P HELX_P7  AA7 LYS A 335 ? GLY A 337 ? LYS A 335 GLY A 337 5 ? 3  
HELX_P HELX_P8  AA8 ASN A 344 ? GLN A 348 ? ASN A 344 GLN A 348 5 ? 5  
HELX_P HELX_P9  AA9 ILE A 351 ? ASN A 356 ? ILE A 351 ASN A 356 1 ? 6  
HELX_P HELX_P10 AB1 ASP A 358 ? VAL A 361 ? ASP A 358 VAL A 361 5 ? 4  
HELX_P HELX_P11 AB2 ALA A 362 ? ASN A 371 ? ALA A 362 ASN A 371 1 ? 10 
# 
_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 
covale1 covale both ? A LEU 73 C  ? ? ? 1_555 A SWG 74 N1 ? ? A LEU 73 A SWG 74 1_555 ? ? ? ? ? ? ? 1.326 ? ? 
covale2 covale both ? A SWG 74 C3 ? ? ? 1_555 A VAL 75 N  ? ? A SWG 74 A VAL 75 1_555 ? ? ? ? ? ? ? 1.340 ? ? 
# 
_struct_conn_type.id          covale 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
_pdbx_modification_feature.ordinal                            1 
_pdbx_modification_feature.label_comp_id                      SWG 
_pdbx_modification_feature.label_asym_id                      A 
_pdbx_modification_feature.label_seq_id                       74 
_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                       SWG 
_pdbx_modification_feature.auth_asym_id                       A 
_pdbx_modification_feature.auth_seq_id                        74 
_pdbx_modification_feature.PDB_ins_code                       ? 
_pdbx_modification_feature.symmetry                           1_555 
_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                'SER, TRP, GLY' 
_pdbx_modification_feature.ref_pcm_id                         1 
_pdbx_modification_feature.ref_comp_id                        SWG 
_pdbx_modification_feature.type                               None 
_pdbx_modification_feature.category                           Chromophore/chromophore-like 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 13 ? 
AA2 ? 6  ? 
AA3 ? 6  ? 
AA4 ? 5  ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1  2  ? anti-parallel 
AA1 2  3  ? anti-parallel 
AA1 3  4  ? anti-parallel 
AA1 4  5  ? anti-parallel 
AA1 5  6  ? anti-parallel 
AA1 6  7  ? parallel      
AA1 7  8  ? anti-parallel 
AA1 8  9  ? anti-parallel 
AA1 9  10 ? anti-parallel 
AA1 10 11 ? anti-parallel 
AA1 11 12 ? anti-parallel 
AA1 12 13 ? anti-parallel 
AA2 1  2  ? anti-parallel 
AA2 2  3  ? anti-parallel 
AA2 3  4  ? anti-parallel 
AA2 4  5  ? anti-parallel 
AA2 5  6  ? anti-parallel 
AA3 1  2  ? anti-parallel 
AA3 2  3  ? anti-parallel 
AA3 3  4  ? anti-parallel 
AA3 4  5  ? anti-parallel 
AA3 5  6  ? anti-parallel 
AA4 1  2  ? anti-parallel 
AA4 2  3  ? anti-parallel 
AA4 3  4  ? anti-parallel 
AA4 4  5  ? 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 502 ? ALA A 504 ? THR A 502 ALA A 504 
AA1 2  ASN A 475 ? SER A 485 ? ASN A 475 SER A 485 
AA1 3  HIS A 494 ? PHE A 500 ? HIS A 494 PHE A 500 
AA1 4  LYS A 50  ? CYS A 57  ? LYS A 50  CYS A 57  
AA1 5  HIS A 34  ? ASP A 45  ? HIS A 34  ASP A 45  
AA1 6  VAL A 20  ? VAL A 31  ? VAL A 20  VAL A 31  
AA1 7  THR A 125 ? ILE A 135 ? THR A 125 ILE A 135 
AA1 8  ASN A 112 ? GLU A 122 ? ASN A 112 GLU A 122 
AA1 9  GLY A 98  ? PHE A 107 ? GLY A 98  PHE A 107 
AA1 10 VAL A 453 ? PRO A 464 ? VAL A 453 PRO A 464 
AA1 11 ILE A 438 ? ASN A 447 ? ILE A 438 ASN A 447 
AA1 12 SER A 423 ? ALA A 431 ? SER A 423 ALA A 431 
AA1 13 ASN A 475 ? SER A 485 ? ASN A 475 SER A 485 
AA2 1  ILE A 253 ? ALA A 254 ? ILE A 253 ALA A 254 
AA2 2  ARG A 242 ? SER A 248 ? ARG A 242 SER A 248 
AA2 3  VAL A 229 ? TYR A 236 ? VAL A 229 TYR A 236 
AA2 4  GLY A 307 ? ASN A 314 ? GLY A 307 ASN A 314 
AA2 5  ASP A 287 ? LEU A 298 ? ASP A 287 LEU A 298 
AA2 6  THR A 275 ? HIS A 276 ? THR A 275 HIS A 276 
AA3 1  ILE A 253 ? ALA A 254 ? ILE A 253 ALA A 254 
AA3 2  ARG A 242 ? SER A 248 ? ARG A 242 SER A 248 
AA3 3  VAL A 229 ? TYR A 236 ? VAL A 229 TYR A 236 
AA3 4  GLY A 307 ? ASN A 314 ? GLY A 307 ASN A 314 
AA3 5  ASP A 287 ? LEU A 298 ? ASP A 287 LEU A 298 
AA3 6  TYR A 280 ? VAL A 284 ? TYR A 280 VAL A 284 
AA4 1  LEU A 339 ? ILE A 341 ? LEU A 339 ILE A 341 
AA4 2  THR A 330 ? MET A 333 ? THR A 330 MET A 333 
AA4 3  ARG A 408 ? LYS A 417 ? ARG A 408 LYS A 417 
AA4 4  GLU A 386 ? ASP A 395 ? GLU A 386 ASP A 395 
AA4 5  GLY A 374 ? HIS A 379 ? GLY A 374 HIS A 379 
# 
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  O ALA A 504 ? O ALA A 504 N TYR A 477 ? N TYR A 477 
AA1 2  3  N GLN A 481 ? N GLN A 481 O PHE A 500 ? O PHE A 500 
AA1 3  4  O MET A 495 ? O MET A 495 N PHE A 55  ? N PHE A 55  
AA1 4  5  O LYS A 50  ? O LYS A 50  N ASP A 45  ? N ASP A 45  
AA1 5  6  O GLY A 42  ? O GLY A 42  N ILE A 23  ? N ILE A 23  
AA1 6  7  N GLU A 26  ? N GLU A 26  O ILE A 130 ? O ILE A 130 
AA1 7  8  O LYS A 133 ? O LYS A 133 N LYS A 114 ? N LYS A 114 
AA1 8  9  O THR A 115 ? O THR A 115 N ARG A 103 ? N ARG A 103 
AA1 9  10 N VAL A 100 ? N VAL A 100 O THR A 463 ? O THR A 463 
AA1 10 11 O GLN A 454 ? O GLN A 454 N HIS A 446 ? N HIS A 446 
AA1 11 12 O LYS A 439 ? O LYS A 439 N THR A 430 ? N THR A 430 
AA1 12 13 N ILE A 429 ? N ILE A 429 O HIS A 476 ? O HIS A 476 
AA2 1  2  O ALA A 254 ? O ALA A 254 N MET A 247 ? N MET A 247 
AA2 2  3  O ARG A 242 ? O ARG A 242 N TYR A 236 ? N TYR A 236 
AA2 3  4  N ILE A 235 ? N ILE A 235 O ALA A 308 ? O ALA A 308 
AA2 4  5  O LEU A 309 ? O LEU A 309 N LEU A 296 ? N LEU A 296 
AA2 5  6  O THR A 295 ? O THR A 295 N THR A 275 ? N THR A 275 
AA3 1  2  O ALA A 254 ? O ALA A 254 N MET A 247 ? N MET A 247 
AA3 2  3  O ARG A 242 ? O ARG A 242 N TYR A 236 ? N TYR A 236 
AA3 3  4  N ILE A 235 ? N ILE A 235 O ALA A 308 ? O ALA A 308 
AA3 4  5  O LEU A 309 ? O LEU A 309 N LEU A 296 ? N LEU A 296 
AA3 5  6  O ILE A 289 ? O ILE A 289 N LYS A 282 ? N LYS A 282 
AA4 1  2  O ILE A 341 ? O ILE A 341 N LEU A 332 ? N LEU A 332 
AA4 2  3  N MET A 333 ? N MET A 333 O ALA A 410 ? O ALA A 410 
AA4 3  4  O LYS A 417 ? O LYS A 417 N GLU A 386 ? N GLU A 386 
AA4 4  5  O LEU A 389 ? O LEU A 389 N LEU A 376 ? N LEU A 376 
# 
_pdbx_entry_details.entry_id                   9EBX 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 PHE A 78  ? ? -86.48  -124.59 
2  1 ALA A 79  ? ? 76.69   137.33  
3  1 MET A 85  ? ? -65.88  97.31   
4  1 GLU A 97  ? ? -112.04 -105.05 
5  1 ASP A 140 ? ? 75.38   -1.22   
6  1 HIS A 146 ? ? 51.17   73.64   
7  1 THR A 162 ? ? 63.59   -79.34  
8  1 SER A 164 ? ? -92.30  -78.03  
9  1 ASN A 238 ? ? -68.29  -83.81  
10 1 GLU A 241 ? ? -55.50  101.22  
11 1 MET A 249 ? ? -97.41  -110.79 
12 1 ASN A 266 ? ? 81.10   -43.50  
13 1 MET A 299 ? ? 65.24   164.48  
14 1 LYS A 301 ? ? -119.36 78.29   
15 1 VAL A 322 ? ? -97.31  -60.50  
16 1 LEU A 381 ? ? 43.23   -127.70 
17 1 TRP A 407 ? ? -117.40 51.92   
18 1 ASP A 432 ? ? -91.21  -113.05 
19 1 LYS A 433 ? ? 148.77  -64.71  
20 1 ASN A 436 ? ? 38.61   48.07   
21 1 ASP A 474 ? ? -93.37  -78.76  
22 1 ASN A 475 ? ? -172.26 103.23  
# 
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 116 ? ? 0.085 'SIDE CHAIN' 
2 1 ARG A 191 ? ? 0.111 'SIDE CHAIN' 
3 1 ARG A 269 ? ? 0.115 'SIDE CHAIN' 
4 1 ARG A 492 ? ? 0.090 'SIDE CHAIN' 
# 
loop_
_pdbx_struct_mod_residue.id 
_pdbx_struct_mod_residue.label_asym_id 
_pdbx_struct_mod_residue.label_comp_id 
_pdbx_struct_mod_residue.label_seq_id 
_pdbx_struct_mod_residue.auth_asym_id 
_pdbx_struct_mod_residue.auth_comp_id 
_pdbx_struct_mod_residue.auth_seq_id 
_pdbx_struct_mod_residue.PDB_ins_code 
_pdbx_struct_mod_residue.parent_comp_id 
_pdbx_struct_mod_residue.details 
1 A SWG 74 A SWG 74 ? SER chromophore 
2 A SWG 74 A SWG 74 ? TYR chromophore 
3 A SWG 74 A SWG 74 ? GLY chromophore 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A MET 1   ? A MET 1   
2  1 Y 1 A LYS 2   ? A LYS 2   
3  1 Y 1 A HIS 3   ? A HIS 3   
4  1 Y 1 A HIS 4   ? A HIS 4   
5  1 Y 1 A HIS 5   ? A HIS 5   
6  1 Y 1 A HIS 6   ? A HIS 6   
7  1 Y 1 A HIS 7   ? A HIS 7   
8  1 Y 1 A HIS 8   ? A HIS 8   
9  1 Y 1 A HIS 9   ? A HIS 9   
10 1 Y 1 A VAL 10  ? A VAL 10  
11 1 Y 1 A SER 11  ? A SER 11  
12 1 Y 1 A HIS 88  ? A HIS 88  
13 1 Y 1 A GLY 154 ? A GLY 154 
14 1 Y 1 A ARG 155 ? A ARG 155 
15 1 Y 1 A THR 156 ? A THR 156 
16 1 Y 1 A GLY 157 ? A GLY 157 
17 1 Y 1 A ILE 158 ? A ILE 158 
18 1 Y 1 A ASP 159 ? A ASP 159 
19 1 Y 1 A PRO 160 ? A PRO 160 
20 1 Y 1 A GLN 303 ? A GLN 303 
21 1 Y 1 A ASN 304 ? A ASN 304 
22 1 Y 1 A ASN 402 ? A ASN 402 
23 1 Y 1 A ASN 403 ? A ASN 403 
24 1 Y 1 A GLY 404 ? A GLY 404 
25 1 Y 1 A ILE 506 ? A ILE 506 
26 1 Y 1 A THR 507 ? A THR 507 
27 1 Y 1 A LEU 508 ? A LEU 508 
28 1 Y 1 A GLY 509 ? A GLY 509 
29 1 Y 1 A MET 510 ? A MET 510 
30 1 Y 1 A ASP 511 ? A ASP 511 
31 1 Y 1 A GLU 512 ? A GLU 512 
32 1 Y 1 A LEU 513 ? A LEU 513 
33 1 Y 1 A TYR 514 ? A TYR 514 
34 1 Y 1 A GLN 515 ? A GLN 515 
# 
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 
ALA N    N N N 1   
ALA CA   C N S 2   
ALA C    C N N 3   
ALA O    O N N 4   
ALA CB   C N N 5   
ALA OXT  O N N 6   
ALA H    H N N 7   
ALA H2   H N N 8   
ALA HA   H N N 9   
ALA HB1  H N N 10  
ALA HB2  H N N 11  
ALA HB3  H N N 12  
ALA HXT  H N N 13  
ARG N    N N N 14  
ARG CA   C N S 15  
ARG C    C N N 16  
ARG O    O N N 17  
ARG CB   C N N 18  
ARG CG   C N N 19  
ARG CD   C N N 20  
ARG NE   N N N 21  
ARG CZ   C N N 22  
ARG NH1  N N N 23  
ARG NH2  N N N 24  
ARG OXT  O N N 25  
ARG H    H N N 26  
ARG H2   H N N 27  
ARG HA   H N N 28  
ARG HB2  H N N 29  
ARG HB3  H N N 30  
ARG HG2  H N N 31  
ARG HG3  H N N 32  
ARG HD2  H N N 33  
ARG HD3  H N N 34  
ARG HE   H N N 35  
ARG HH11 H N N 36  
ARG HH12 H N N 37  
ARG HH21 H N N 38  
ARG HH22 H N N 39  
ARG HXT  H N N 40  
ASN N    N N N 41  
ASN CA   C N S 42  
ASN C    C N N 43  
ASN O    O N N 44  
ASN CB   C N N 45  
ASN CG   C N N 46  
ASN OD1  O N N 47  
ASN ND2  N N N 48  
ASN OXT  O N N 49  
ASN H    H N N 50  
ASN H2   H N N 51  
ASN HA   H N N 52  
ASN HB2  H N N 53  
ASN HB3  H N N 54  
ASN HD21 H N N 55  
ASN HD22 H N N 56  
ASN HXT  H N N 57  
ASP N    N N N 58  
ASP CA   C N S 59  
ASP C    C N N 60  
ASP O    O N N 61  
ASP CB   C N N 62  
ASP CG   C N N 63  
ASP OD1  O N N 64  
ASP OD2  O N N 65  
ASP OXT  O N N 66  
ASP H    H N N 67  
ASP H2   H N N 68  
ASP HA   H N N 69  
ASP HB2  H N N 70  
ASP HB3  H N N 71  
ASP HD2  H N N 72  
ASP HXT  H N N 73  
CYS N    N N N 74  
CYS CA   C N R 75  
CYS C    C N N 76  
CYS O    O N N 77  
CYS CB   C N N 78  
CYS SG   S N N 79  
CYS OXT  O N N 80  
CYS H    H N N 81  
CYS H2   H N N 82  
CYS HA   H N N 83  
CYS HB2  H N N 84  
CYS HB3  H N N 85  
CYS HG   H N N 86  
CYS HXT  H N N 87  
GLN N    N N N 88  
GLN CA   C N S 89  
GLN C    C N N 90  
GLN O    O N N 91  
GLN CB   C N N 92  
GLN CG   C N N 93  
GLN CD   C N N 94  
GLN OE1  O N N 95  
GLN NE2  N N N 96  
GLN OXT  O N N 97  
GLN H    H N N 98  
GLN H2   H N N 99  
GLN HA   H N N 100 
GLN HB2  H N N 101 
GLN HB3  H N N 102 
GLN HG2  H N N 103 
GLN HG3  H N N 104 
GLN HE21 H N N 105 
GLN HE22 H N N 106 
GLN HXT  H N N 107 
GLU N    N N N 108 
GLU CA   C N S 109 
GLU C    C N N 110 
GLU O    O N N 111 
GLU CB   C N N 112 
GLU CG   C N N 113 
GLU CD   C N N 114 
GLU OE1  O N N 115 
GLU OE2  O N N 116 
GLU OXT  O N N 117 
GLU H    H N N 118 
GLU H2   H N N 119 
GLU HA   H N N 120 
GLU HB2  H N N 121 
GLU HB3  H N N 122 
GLU HG2  H N N 123 
GLU HG3  H N N 124 
GLU HE2  H N N 125 
GLU HXT  H N N 126 
GLY N    N N N 127 
GLY CA   C N N 128 
GLY C    C N N 129 
GLY O    O N N 130 
GLY OXT  O N N 131 
GLY H    H N N 132 
GLY H2   H N N 133 
GLY HA2  H N N 134 
GLY HA3  H N N 135 
GLY HXT  H N N 136 
HIS N    N N N 137 
HIS CA   C N S 138 
HIS C    C N N 139 
HIS O    O N N 140 
HIS CB   C N N 141 
HIS CG   C Y N 142 
HIS ND1  N Y N 143 
HIS CD2  C Y N 144 
HIS CE1  C Y N 145 
HIS NE2  N Y N 146 
HIS OXT  O N N 147 
HIS H    H N N 148 
HIS H2   H N N 149 
HIS HA   H N N 150 
HIS HB2  H N N 151 
HIS HB3  H N N 152 
HIS HD1  H N N 153 
HIS HD2  H N N 154 
HIS HE1  H N N 155 
HIS HE2  H N N 156 
HIS HXT  H N N 157 
HOH O    O N N 158 
HOH H1   H N N 159 
HOH H2   H N N 160 
ILE N    N N N 161 
ILE CA   C N S 162 
ILE C    C N N 163 
ILE O    O N N 164 
ILE CB   C N S 165 
ILE CG1  C N N 166 
ILE CG2  C N N 167 
ILE CD1  C N N 168 
ILE OXT  O N N 169 
ILE H    H N N 170 
ILE H2   H N N 171 
ILE HA   H N N 172 
ILE HB   H N N 173 
ILE HG12 H N N 174 
ILE HG13 H N N 175 
ILE HG21 H N N 176 
ILE HG22 H N N 177 
ILE HG23 H N N 178 
ILE HD11 H N N 179 
ILE HD12 H N N 180 
ILE HD13 H N N 181 
ILE HXT  H N N 182 
LEU N    N N N 183 
LEU CA   C N S 184 
LEU C    C N N 185 
LEU O    O N N 186 
LEU CB   C N N 187 
LEU CG   C N N 188 
LEU CD1  C N N 189 
LEU CD2  C N N 190 
LEU OXT  O N N 191 
LEU H    H N N 192 
LEU H2   H N N 193 
LEU HA   H N N 194 
LEU HB2  H N N 195 
LEU HB3  H N N 196 
LEU HG   H N N 197 
LEU HD11 H N N 198 
LEU HD12 H N N 199 
LEU HD13 H N N 200 
LEU HD21 H N N 201 
LEU HD22 H N N 202 
LEU HD23 H N N 203 
LEU HXT  H N N 204 
LYS N    N N N 205 
LYS CA   C N S 206 
LYS C    C N N 207 
LYS O    O N N 208 
LYS CB   C N N 209 
LYS CG   C N N 210 
LYS CD   C N N 211 
LYS CE   C N N 212 
LYS NZ   N N N 213 
LYS OXT  O N N 214 
LYS H    H N N 215 
LYS H2   H N N 216 
LYS HA   H N N 217 
LYS HB2  H N N 218 
LYS HB3  H N N 219 
LYS HG2  H N N 220 
LYS HG3  H N N 221 
LYS HD2  H N N 222 
LYS HD3  H N N 223 
LYS HE2  H N N 224 
LYS HE3  H N N 225 
LYS HZ1  H N N 226 
LYS HZ2  H N N 227 
LYS HZ3  H N N 228 
LYS HXT  H N N 229 
MET N    N N N 230 
MET CA   C N S 231 
MET C    C N N 232 
MET O    O N N 233 
MET CB   C N N 234 
MET CG   C N N 235 
MET SD   S N N 236 
MET CE   C N N 237 
MET OXT  O N N 238 
MET H    H N N 239 
MET H2   H N N 240 
MET HA   H N N 241 
MET HB2  H N N 242 
MET HB3  H N N 243 
MET HG2  H N N 244 
MET HG3  H N N 245 
MET HE1  H N N 246 
MET HE2  H N N 247 
MET HE3  H N N 248 
MET HXT  H N N 249 
PHE N    N N N 250 
PHE CA   C N S 251 
PHE C    C N N 252 
PHE O    O N N 253 
PHE CB   C N N 254 
PHE CG   C Y N 255 
PHE CD1  C Y N 256 
PHE CD2  C Y N 257 
PHE CE1  C Y N 258 
PHE CE2  C Y N 259 
PHE CZ   C Y N 260 
PHE OXT  O N N 261 
PHE H    H N N 262 
PHE H2   H N N 263 
PHE HA   H N N 264 
PHE HB2  H N N 265 
PHE HB3  H N N 266 
PHE HD1  H N N 267 
PHE HD2  H N N 268 
PHE HE1  H N N 269 
PHE HE2  H N N 270 
PHE HZ   H N N 271 
PHE HXT  H N N 272 
PRO N    N N N 273 
PRO CA   C N S 274 
PRO C    C N N 275 
PRO O    O N N 276 
PRO CB   C N N 277 
PRO CG   C N N 278 
PRO CD   C N N 279 
PRO OXT  O N N 280 
PRO H    H N N 281 
PRO HA   H N N 282 
PRO HB2  H N N 283 
PRO HB3  H N N 284 
PRO HG2  H N N 285 
PRO HG3  H N N 286 
PRO HD2  H N N 287 
PRO HD3  H N N 288 
PRO HXT  H N N 289 
SER N    N N N 290 
SER CA   C N S 291 
SER C    C N N 292 
SER O    O N N 293 
SER CB   C N N 294 
SER OG   O N N 295 
SER OXT  O N N 296 
SER H    H N N 297 
SER H2   H N N 298 
SER HA   H N N 299 
SER HB2  H N N 300 
SER HB3  H N N 301 
SER HG   H N N 302 
SER HXT  H N N 303 
SWG CD2  C Y N 304 
SWG CE3  C Y N 305 
SWG CZ3  C Y N 306 
SWG CH2  C Y N 307 
SWG CZ2  C Y N 308 
SWG CE2  C Y N 309 
SWG NE1  N Y N 310 
SWG CD1  C Y N 311 
SWG CG   C Y N 312 
SWG CB2  C N N 313 
SWG CA2  C N N 314 
SWG N2   N N N 315 
SWG C2   C N N 316 
SWG O2   O N N 317 
SWG N3   N N N 318 
SWG CA3  C N N 319 
SWG C3   C N N 320 
SWG O3   O N N 321 
SWG OXT  O N N 322 
SWG C1   C N N 323 
SWG CA1  C N R 324 
SWG N1   N N N 325 
SWG CB1  C N N 326 
SWG OG1  O N N 327 
SWG HE3  H N N 328 
SWG HZ3  H N N 329 
SWG HH2  H N N 330 
SWG HZ2  H N N 331 
SWG HE1  H N N 332 
SWG HD1  H N N 333 
SWG HB2  H N N 334 
SWG HA31 H N N 335 
SWG HA32 H N N 336 
SWG HXT  H N N 337 
SWG HA1  H N N 338 
SWG H    H N N 339 
SWG H2   H N N 340 
SWG HB11 H N N 341 
SWG HB12 H N N 342 
SWG HG1  H N N 343 
THR N    N N N 344 
THR CA   C N S 345 
THR C    C N N 346 
THR O    O N N 347 
THR CB   C N R 348 
THR OG1  O N N 349 
THR CG2  C N N 350 
THR OXT  O N N 351 
THR H    H N N 352 
THR H2   H N N 353 
THR HA   H N N 354 
THR HB   H N N 355 
THR HG1  H N N 356 
THR HG21 H N N 357 
THR HG22 H N N 358 
THR HG23 H N N 359 
THR HXT  H N N 360 
TRP N    N N N 361 
TRP CA   C N S 362 
TRP C    C N N 363 
TRP O    O N N 364 
TRP CB   C N N 365 
TRP CG   C Y N 366 
TRP CD1  C Y N 367 
TRP CD2  C Y N 368 
TRP NE1  N Y N 369 
TRP CE2  C Y N 370 
TRP CE3  C Y N 371 
TRP CZ2  C Y N 372 
TRP CZ3  C Y N 373 
TRP CH2  C Y N 374 
TRP OXT  O N N 375 
TRP H    H N N 376 
TRP H2   H N N 377 
TRP HA   H N N 378 
TRP HB2  H N N 379 
TRP HB3  H N N 380 
TRP HD1  H N N 381 
TRP HE1  H N N 382 
TRP HE3  H N N 383 
TRP HZ2  H N N 384 
TRP HZ3  H N N 385 
TRP HH2  H N N 386 
TRP HXT  H N N 387 
TYR N    N N N 388 
TYR CA   C N S 389 
TYR C    C N N 390 
TYR O    O N N 391 
TYR CB   C N N 392 
TYR CG   C Y N 393 
TYR CD1  C Y N 394 
TYR CD2  C Y N 395 
TYR CE1  C Y N 396 
TYR CE2  C Y N 397 
TYR CZ   C Y N 398 
TYR OH   O N N 399 
TYR OXT  O N N 400 
TYR H    H N N 401 
TYR H2   H N N 402 
TYR HA   H N N 403 
TYR HB2  H N N 404 
TYR HB3  H N N 405 
TYR HD1  H N N 406 
TYR HD2  H N N 407 
TYR HE1  H N N 408 
TYR HE2  H N N 409 
TYR HH   H N N 410 
TYR HXT  H N N 411 
VAL N    N N N 412 
VAL CA   C N S 413 
VAL C    C N N 414 
VAL O    O N N 415 
VAL CB   C N N 416 
VAL CG1  C N N 417 
VAL CG2  C N N 418 
VAL OXT  O N N 419 
VAL H    H N N 420 
VAL H2   H N N 421 
VAL HA   H N N 422 
VAL HB   H N N 423 
VAL HG11 H N N 424 
VAL HG12 H N N 425 
VAL HG13 H N N 426 
VAL HG21 H N N 427 
VAL HG22 H N N 428 
VAL HG23 H N N 429 
VAL HXT  H N N 430 
# 
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 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
HIS N   CA   sing N N 129 
HIS N   H    sing N N 130 
HIS N   H2   sing N N 131 
HIS CA  C    sing N N 132 
HIS CA  CB   sing N N 133 
HIS CA  HA   sing N N 134 
HIS C   O    doub N N 135 
HIS C   OXT  sing N N 136 
HIS CB  CG   sing N N 137 
HIS CB  HB2  sing N N 138 
HIS CB  HB3  sing N N 139 
HIS CG  ND1  sing Y N 140 
HIS CG  CD2  doub Y N 141 
HIS ND1 CE1  doub Y N 142 
HIS ND1 HD1  sing N N 143 
HIS CD2 NE2  sing Y N 144 
HIS CD2 HD2  sing N N 145 
HIS CE1 NE2  sing Y N 146 
HIS CE1 HE1  sing N N 147 
HIS NE2 HE2  sing N N 148 
HIS OXT HXT  sing N N 149 
HOH O   H1   sing N N 150 
HOH O   H2   sing N N 151 
ILE N   CA   sing N N 152 
ILE N   H    sing N N 153 
ILE N   H2   sing N N 154 
ILE CA  C    sing N N 155 
ILE CA  CB   sing N N 156 
ILE CA  HA   sing N N 157 
ILE C   O    doub N N 158 
ILE C   OXT  sing N N 159 
ILE CB  CG1  sing N N 160 
ILE CB  CG2  sing N N 161 
ILE CB  HB   sing N N 162 
ILE CG1 CD1  sing N N 163 
ILE CG1 HG12 sing N N 164 
ILE CG1 HG13 sing N N 165 
ILE CG2 HG21 sing N N 166 
ILE CG2 HG22 sing N N 167 
ILE CG2 HG23 sing N N 168 
ILE CD1 HD11 sing N N 169 
ILE CD1 HD12 sing N N 170 
ILE CD1 HD13 sing N N 171 
ILE OXT HXT  sing N N 172 
LEU N   CA   sing N N 173 
LEU N   H    sing N N 174 
LEU N   H2   sing N N 175 
LEU CA  C    sing N N 176 
LEU CA  CB   sing N N 177 
LEU CA  HA   sing N N 178 
LEU C   O    doub N N 179 
LEU C   OXT  sing N N 180 
LEU CB  CG   sing N N 181 
LEU CB  HB2  sing N N 182 
LEU CB  HB3  sing N N 183 
LEU CG  CD1  sing N N 184 
LEU CG  CD2  sing N N 185 
LEU CG  HG   sing N N 186 
LEU CD1 HD11 sing N N 187 
LEU CD1 HD12 sing N N 188 
LEU CD1 HD13 sing N N 189 
LEU CD2 HD21 sing N N 190 
LEU CD2 HD22 sing N N 191 
LEU CD2 HD23 sing N N 192 
LEU OXT HXT  sing N N 193 
LYS N   CA   sing N N 194 
LYS N   H    sing N N 195 
LYS N   H2   sing N N 196 
LYS CA  C    sing N N 197 
LYS CA  CB   sing N N 198 
LYS CA  HA   sing N N 199 
LYS C   O    doub N N 200 
LYS C   OXT  sing N N 201 
LYS CB  CG   sing N N 202 
LYS CB  HB2  sing N N 203 
LYS CB  HB3  sing N N 204 
LYS CG  CD   sing N N 205 
LYS CG  HG2  sing N N 206 
LYS CG  HG3  sing N N 207 
LYS CD  CE   sing N N 208 
LYS CD  HD2  sing N N 209 
LYS CD  HD3  sing N N 210 
LYS CE  NZ   sing N N 211 
LYS CE  HE2  sing N N 212 
LYS CE  HE3  sing N N 213 
LYS NZ  HZ1  sing N N 214 
LYS NZ  HZ2  sing N N 215 
LYS NZ  HZ3  sing N N 216 
LYS OXT HXT  sing N N 217 
MET N   CA   sing N N 218 
MET N   H    sing N N 219 
MET N   H2   sing N N 220 
MET CA  C    sing N N 221 
MET CA  CB   sing N N 222 
MET CA  HA   sing N N 223 
MET C   O    doub N N 224 
MET C   OXT  sing N N 225 
MET CB  CG   sing N N 226 
MET CB  HB2  sing N N 227 
MET CB  HB3  sing N N 228 
MET CG  SD   sing N N 229 
MET CG  HG2  sing N N 230 
MET CG  HG3  sing N N 231 
MET SD  CE   sing N N 232 
MET CE  HE1  sing N N 233 
MET CE  HE2  sing N N 234 
MET CE  HE3  sing N N 235 
MET OXT HXT  sing N N 236 
PHE N   CA   sing N N 237 
PHE N   H    sing N N 238 
PHE N   H2   sing N N 239 
PHE CA  C    sing N N 240 
PHE CA  CB   sing N N 241 
PHE CA  HA   sing N N 242 
PHE C   O    doub N N 243 
PHE C   OXT  sing N N 244 
PHE CB  CG   sing N N 245 
PHE CB  HB2  sing N N 246 
PHE CB  HB3  sing N N 247 
PHE CG  CD1  doub Y N 248 
PHE CG  CD2  sing Y N 249 
PHE CD1 CE1  sing Y N 250 
PHE CD1 HD1  sing N N 251 
PHE CD2 CE2  doub Y N 252 
PHE CD2 HD2  sing N N 253 
PHE CE1 CZ   doub Y N 254 
PHE CE1 HE1  sing N N 255 
PHE CE2 CZ   sing Y N 256 
PHE CE2 HE2  sing N N 257 
PHE CZ  HZ   sing N N 258 
PHE OXT HXT  sing N N 259 
PRO N   CA   sing N N 260 
PRO N   CD   sing N N 261 
PRO N   H    sing N N 262 
PRO CA  C    sing N N 263 
PRO CA  CB   sing N N 264 
PRO CA  HA   sing N N 265 
PRO C   O    doub N N 266 
PRO C   OXT  sing N N 267 
PRO CB  CG   sing N N 268 
PRO CB  HB2  sing N N 269 
PRO CB  HB3  sing N N 270 
PRO CG  CD   sing N N 271 
PRO CG  HG2  sing N N 272 
PRO CG  HG3  sing N N 273 
PRO CD  HD2  sing N N 274 
PRO CD  HD3  sing N N 275 
PRO OXT HXT  sing N N 276 
SER N   CA   sing N N 277 
SER N   H    sing N N 278 
SER N   H2   sing N N 279 
SER CA  C    sing N N 280 
SER CA  CB   sing N N 281 
SER CA  HA   sing N N 282 
SER C   O    doub N N 283 
SER C   OXT  sing N N 284 
SER CB  OG   sing N N 285 
SER CB  HB2  sing N N 286 
SER CB  HB3  sing N N 287 
SER OG  HG   sing N N 288 
SER OXT HXT  sing N N 289 
SWG CD2 CE3  sing Y N 290 
SWG CD2 CE2  doub Y N 291 
SWG CD2 CG   sing Y N 292 
SWG CE3 CZ3  doub Y N 293 
SWG CZ3 CH2  sing Y N 294 
SWG CH2 CZ2  doub Y N 295 
SWG CZ2 CE2  sing Y N 296 
SWG CE2 NE1  sing Y N 297 
SWG NE1 CD1  sing Y N 298 
SWG CD1 CG   doub Y N 299 
SWG CG  CB2  sing N N 300 
SWG CB2 CA2  doub N N 301 
SWG CA2 N2   sing N N 302 
SWG CA2 C2   sing N N 303 
SWG N2  C1   doub N N 304 
SWG C2  O2   doub N N 305 
SWG C2  N3   sing N N 306 
SWG N3  CA3  sing N Z 307 
SWG N3  C1   sing N N 308 
SWG CA3 C3   sing N N 309 
SWG C3  O3   doub N N 310 
SWG C3  OXT  sing N N 311 
SWG C1  CA1  sing N N 312 
SWG CA1 N1   sing N N 313 
SWG CA1 CB1  sing N N 314 
SWG CB1 OG1  sing N N 315 
SWG CE3 HE3  sing N N 316 
SWG CZ3 HZ3  sing N N 317 
SWG CH2 HH2  sing N N 318 
SWG CZ2 HZ2  sing N N 319 
SWG NE1 HE1  sing N N 320 
SWG CD1 HD1  sing N N 321 
SWG CB2 HB2  sing N N 322 
SWG CA3 HA31 sing N N 323 
SWG CA3 HA32 sing N N 324 
SWG CA1 HA1  sing N N 325 
SWG N1  H    sing N N 326 
SWG N1  H2   sing N N 327 
SWG CB1 HB11 sing N N 328 
SWG CB1 HB12 sing N N 329 
SWG OG1 HG1  sing N N 330 
SWG OXT HXT  sing N N 331 
THR N   CA   sing N N 332 
THR N   H    sing N N 333 
THR N   H2   sing N N 334 
THR CA  C    sing N N 335 
THR CA  CB   sing N N 336 
THR CA  HA   sing N N 337 
THR C   O    doub N N 338 
THR C   OXT  sing N N 339 
THR CB  OG1  sing N N 340 
THR CB  CG2  sing N N 341 
THR CB  HB   sing N N 342 
THR OG1 HG1  sing N N 343 
THR CG2 HG21 sing N N 344 
THR CG2 HG22 sing N N 345 
THR CG2 HG23 sing N N 346 
THR OXT HXT  sing N N 347 
TRP N   CA   sing N N 348 
TRP N   H    sing N N 349 
TRP N   H2   sing N N 350 
TRP CA  C    sing N N 351 
TRP CA  CB   sing N N 352 
TRP CA  HA   sing N N 353 
TRP C   O    doub N N 354 
TRP C   OXT  sing N N 355 
TRP CB  CG   sing N N 356 
TRP CB  HB2  sing N N 357 
TRP CB  HB3  sing N N 358 
TRP CG  CD1  doub Y N 359 
TRP CG  CD2  sing Y N 360 
TRP CD1 NE1  sing Y N 361 
TRP CD1 HD1  sing N N 362 
TRP CD2 CE2  doub Y N 363 
TRP CD2 CE3  sing Y N 364 
TRP NE1 CE2  sing Y N 365 
TRP NE1 HE1  sing N N 366 
TRP CE2 CZ2  sing Y N 367 
TRP CE3 CZ3  doub Y N 368 
TRP CE3 HE3  sing N N 369 
TRP CZ2 CH2  doub Y N 370 
TRP CZ2 HZ2  sing N N 371 
TRP CZ3 CH2  sing Y N 372 
TRP CZ3 HZ3  sing N N 373 
TRP CH2 HH2  sing N N 374 
TRP OXT HXT  sing N N 375 
TYR N   CA   sing N N 376 
TYR N   H    sing N N 377 
TYR N   H2   sing N N 378 
TYR CA  C    sing N N 379 
TYR CA  CB   sing N N 380 
TYR CA  HA   sing N N 381 
TYR C   O    doub N N 382 
TYR C   OXT  sing N N 383 
TYR CB  CG   sing N N 384 
TYR CB  HB2  sing N N 385 
TYR CB  HB3  sing N N 386 
TYR CG  CD1  doub Y N 387 
TYR CG  CD2  sing Y N 388 
TYR CD1 CE1  sing Y N 389 
TYR CD1 HD1  sing N N 390 
TYR CD2 CE2  doub Y N 391 
TYR CD2 HD2  sing N N 392 
TYR CE1 CZ   doub Y N 393 
TYR CE1 HE1  sing N N 394 
TYR CE2 CZ   sing Y N 395 
TYR CE2 HE2  sing N N 396 
TYR CZ  OH   sing N N 397 
TYR OH  HH   sing N N 398 
TYR OXT HXT  sing N N 399 
VAL N   CA   sing N N 400 
VAL N   H    sing N N 401 
VAL N   H2   sing N N 402 
VAL CA  C    sing N N 403 
VAL CA  CB   sing N N 404 
VAL CA  HA   sing N N 405 
VAL C   O    doub N N 406 
VAL C   OXT  sing N N 407 
VAL CB  CG1  sing N N 408 
VAL CB  CG2  sing N N 409 
VAL CB  HB   sing N N 410 
VAL CG1 HG11 sing N N 411 
VAL CG1 HG12 sing N N 412 
VAL CG1 HG13 sing N N 413 
VAL CG2 HG21 sing N N 414 
VAL CG2 HG22 sing N N 415 
VAL CG2 HG23 sing N N 416 
VAL OXT HXT  sing N N 417 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'National Institutes of Health/National Center for Research Resources (NIH/NCRR)' 'United States' R01GM124038 1 
'National Institutes of Health/National Center for Research Resources (NIH/NCRR)' 'United States' F31CA254162 2 
'National Science Foundation (NSF, United States)'                                'United States' 1937971     3 
# 
loop_
_pdbx_initial_refinement_model.id 
_pdbx_initial_refinement_model.entity_id_list 
_pdbx_initial_refinement_model.type 
_pdbx_initial_refinement_model.source_name 
_pdbx_initial_refinement_model.accession_code 
_pdbx_initial_refinement_model.details 
1 1 'experimental model' PDB 5WBF ? 
2 1 'experimental model' PDB 6YLN 
;Due to the chimeric nature of the construct represented in the current entry, the 6YLN model used for molecular replacement was split into two distinct models, one containing residues 1 through 145, and the other containing residues 150 through 238
;
# 
_atom_sites.entry_id                    9EBX 
_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]   0.029112 
_atom_sites.fract_transf_matrix[1][2]   0.007388 
_atom_sites.fract_transf_matrix[1][3]   0.001831 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.017794 
_atom_sites.fract_transf_matrix[2][3]   0.002640 
_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]   0.015022 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
H 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . LYS A 1 12  ? 14.085  22.039  7.362   1.00 91.32  ? 12  LYS A N   1 
ATOM   2    C CA  . LYS A 1 12  ? 12.629  21.993  7.224   1.00 90.91  ? 12  LYS A CA  1 
ATOM   3    C C   . LYS A 1 12  ? 12.160  20.614  6.768   1.00 95.10  ? 12  LYS A C   1 
ATOM   4    O O   . LYS A 1 12  ? 11.277  20.025  7.388   1.00 91.56  ? 12  LYS A O   1 
ATOM   5    C CB  . LYS A 1 12  ? 12.135  23.068  6.239   1.00 84.70  ? 12  LYS A CB  1 
ATOM   6    N N   . GLY A 1 13  ? 12.757  20.113  5.678   1.00 95.47  ? 13  GLY A N   1 
ATOM   7    C CA  . GLY A 1 13  ? 12.384  18.828  5.109   1.00 94.27  ? 13  GLY A CA  1 
ATOM   8    C C   . GLY A 1 13  ? 11.290  18.947  4.053   1.00 94.43  ? 13  GLY A C   1 
ATOM   9    O O   . GLY A 1 13  ? 11.438  18.434  2.946   1.00 93.31  ? 13  GLY A O   1 
ATOM   10   N N   . GLU A 1 14  ? 10.194  19.627  4.416   1.00 95.79  ? 14  GLU A N   1 
ATOM   11   C CA  . GLU A 1 14  ? 9.113   19.925  3.489   1.00 93.85  ? 14  GLU A CA  1 
ATOM   12   C C   . GLU A 1 14  ? 9.619   20.602  2.216   1.00 90.77  ? 14  GLU A C   1 
ATOM   13   O O   . GLU A 1 14  ? 9.037   20.421  1.148   1.00 95.66  ? 14  GLU A O   1 
ATOM   14   C CB  . GLU A 1 14  ? 8.062   20.821  4.165   1.00 85.89  ? 14  GLU A CB  1 
ATOM   15   N N   . GLU A 1 15  ? 10.701  21.382  2.346   1.00 91.05  ? 15  GLU A N   1 
ATOM   16   C CA  . GLU A 1 15  ? 11.326  22.055  1.216   1.00 99.96  ? 15  GLU A CA  1 
ATOM   17   C C   . GLU A 1 15  ? 11.740  21.095  0.101   1.00 101.40 ? 15  GLU A C   1 
ATOM   18   O O   . GLU A 1 15  ? 11.627  21.437  -1.076  1.00 97.81  ? 15  GLU A O   1 
ATOM   19   C CB  . GLU A 1 15  ? 12.556  22.854  1.685   1.00 92.18  ? 15  GLU A CB  1 
ATOM   20   N N   . LEU A 1 16  ? 12.218  19.900  0.479   1.00 98.54  ? 16  LEU A N   1 
ATOM   21   C CA  . LEU A 1 16  ? 12.610  18.885  -0.488  1.00 96.99  ? 16  LEU A CA  1 
ATOM   22   C C   . LEU A 1 16  ? 11.426  18.488  -1.367  1.00 96.21  ? 16  LEU A C   1 
ATOM   23   O O   . LEU A 1 16  ? 11.577  18.351  -2.580  1.00 98.85  ? 16  LEU A O   1 
ATOM   24   C CB  . LEU A 1 16  ? 13.185  17.626  0.199   1.00 94.34  ? 16  LEU A CB  1 
ATOM   25   C CG  . LEU A 1 16  ? 14.607  17.735  0.756   1.00 95.32  ? 16  LEU A CG  1 
ATOM   26   C CD1 . LEU A 1 16  ? 14.611  18.061  2.236   1.00 88.40  ? 16  LEU A CD1 1 
ATOM   27   N N   . PHE A 1 17  ? 10.251  18.314  -0.746  1.00 92.29  ? 17  PHE A N   1 
ATOM   28   C CA  . PHE A 1 17  ? 9.038   17.952  -1.463  1.00 94.40  ? 17  PHE A CA  1 
ATOM   29   C C   . PHE A 1 17  ? 8.285   19.210  -1.890  1.00 96.08  ? 17  PHE A C   1 
ATOM   30   O O   . PHE A 1 17  ? 7.334   19.626  -1.228  1.00 103.75 ? 17  PHE A O   1 
ATOM   31   C CB  . PHE A 1 17  ? 8.120   17.052  -0.607  1.00 90.17  ? 17  PHE A CB  1 
ATOM   32   C CG  . PHE A 1 17  ? 8.794   15.856  0.017   1.00 83.21  ? 17  PHE A CG  1 
ATOM   33   C CD1 . PHE A 1 17  ? 9.453   15.966  1.230   1.00 90.41  ? 17  PHE A CD1 1 
ATOM   34   C CD2 . PHE A 1 17  ? 8.777   14.625  -0.612  1.00 78.99  ? 17  PHE A CD2 1 
ATOM   35   C CE1 . PHE A 1 17  ? 10.072  14.863  1.804   1.00 91.27  ? 17  PHE A CE1 1 
ATOM   36   C CE2 . PHE A 1 17  ? 9.400   13.525  -0.035  1.00 82.31  ? 17  PHE A CE2 1 
ATOM   37   C CZ  . PHE A 1 17  ? 10.045  13.652  1.167   1.00 90.07  ? 17  PHE A CZ  1 
ATOM   38   N N   . THR A 1 18  ? 8.737   19.819  -2.993  1.00 94.21  ? 18  THR A N   1 
ATOM   39   C CA  . THR A 1 18  ? 8.085   20.988  -3.565  1.00 95.59  ? 18  THR A CA  1 
ATOM   40   C C   . THR A 1 18  ? 7.650   20.776  -5.018  1.00 92.15  ? 18  THR A C   1 
ATOM   41   O O   . THR A 1 18  ? 6.880   21.570  -5.554  1.00 88.85  ? 18  THR A O   1 
ATOM   42   C CB  . THR A 1 18  ? 9.006   22.214  -3.400  1.00 87.15  ? 18  THR A CB  1 
ATOM   43   O OG1 . THR A 1 18  ? 8.275   23.390  -3.743  1.00 86.15  ? 18  THR A OG1 1 
ATOM   44   C CG2 . THR A 1 18  ? 10.276  22.124  -4.241  1.00 81.25  ? 18  THR A CG2 1 
ATOM   45   N N   . GLY A 1 19  ? 8.145   19.700  -5.646  1.00 90.77  ? 19  GLY A N   1 
ATOM   46   C CA  . GLY A 1 19  ? 7.732   19.313  -6.985  1.00 86.80  ? 19  GLY A CA  1 
ATOM   47   C C   . GLY A 1 19  ? 7.802   17.798  -7.162  1.00 82.63  ? 19  GLY A C   1 
ATOM   48   O O   . GLY A 1 19  ? 7.516   17.056  -6.228  1.00 85.01  ? 19  GLY A O   1 
ATOM   49   N N   . VAL A 1 20  ? 8.189   17.357  -8.365  1.00 80.74  ? 20  VAL A N   1 
ATOM   50   C CA  . VAL A 1 20  ? 8.360   15.944  -8.660  1.00 72.73  ? 20  VAL A CA  1 
ATOM   51   C C   . VAL A 1 20  ? 9.669   15.445  -8.057  1.00 72.06  ? 20  VAL A C   1 
ATOM   52   O O   . VAL A 1 20  ? 10.726  16.015  -8.312  1.00 77.46  ? 20  VAL A O   1 
ATOM   53   C CB  . VAL A 1 20  ? 8.314   15.686  -10.181 1.00 75.26  ? 20  VAL A CB  1 
ATOM   54   C CG1 . VAL A 1 20  ? 8.687   14.244  -10.517 1.00 64.41  ? 20  VAL A CG1 1 
ATOM   55   C CG2 . VAL A 1 20  ? 6.951   16.050  -10.756 1.00 67.45  ? 20  VAL A CG2 1 
ATOM   56   N N   . VAL A 1 21  ? 9.577   14.382  -7.249  1.00 81.63  ? 21  VAL A N   1 
ATOM   57   C CA  . VAL A 1 21  ? 10.738  13.739  -6.658  1.00 73.27  ? 21  VAL A CA  1 
ATOM   58   C C   . VAL A 1 21  ? 10.777  12.299  -7.157  1.00 66.98  ? 21  VAL A C   1 
ATOM   59   O O   . VAL A 1 21  ? 9.775   11.593  -7.064  1.00 66.29  ? 21  VAL A O   1 
ATOM   60   C CB  . VAL A 1 21  ? 10.690  13.766  -5.122  1.00 75.30  ? 21  VAL A CB  1 
ATOM   61   C CG1 . VAL A 1 21  ? 12.007  13.290  -4.521  1.00 77.02  ? 21  VAL A CG1 1 
ATOM   62   C CG2 . VAL A 1 21  ? 10.309  15.148  -4.601  1.00 75.55  ? 21  VAL A CG2 1 
ATOM   63   N N   . PRO A 1 22  ? 11.916  11.812  -7.699  1.00 66.80  ? 22  PRO A N   1 
ATOM   64   C CA  . PRO A 1 22  ? 12.008  10.421  -8.129  1.00 70.96  ? 22  PRO A CA  1 
ATOM   65   C C   . PRO A 1 22  ? 11.908  9.428   -6.974  1.00 75.31  ? 22  PRO A C   1 
ATOM   66   O O   . PRO A 1 22  ? 12.528  9.624   -5.929  1.00 74.49  ? 22  PRO A O   1 
ATOM   67   C CB  . PRO A 1 22  ? 13.377  10.338  -8.809  1.00 67.68  ? 22  PRO A CB  1 
ATOM   68   C CG  . PRO A 1 22  ? 13.823  11.771  -8.995  1.00 76.87  ? 22  PRO A CG  1 
ATOM   69   C CD  . PRO A 1 22  ? 13.151  12.573  -7.939  1.00 63.67  ? 22  PRO A CD  1 
ATOM   70   N N   . ILE A 1 23  ? 11.124  8.366   -7.194  1.00 71.22  ? 23  ILE A N   1 
ATOM   71   C CA  . ILE A 1 23  ? 10.906  7.322   -6.208  1.00 63.20  ? 23  ILE A CA  1 
ATOM   72   C C   . ILE A 1 23  ? 11.668  6.064   -6.602  1.00 69.22  ? 23  ILE A C   1 
ATOM   73   O O   . ILE A 1 23  ? 11.697  5.697   -7.775  1.00 69.68  ? 23  ILE A O   1 
ATOM   74   C CB  . ILE A 1 23  ? 9.404   6.985   -6.054  1.00 63.51  ? 23  ILE A CB  1 
ATOM   75   C CG1 . ILE A 1 23  ? 8.572   8.245   -5.836  1.00 59.65  ? 23  ILE A CG1 1 
ATOM   76   C CG2 . ILE A 1 23  ? 9.181   5.939   -4.935  1.00 68.34  ? 23  ILE A CG2 1 
ATOM   77   C CD1 . ILE A 1 23  ? 9.051   9.107   -4.766  1.00 61.10  ? 23  ILE A CD1 1 
ATOM   78   N N   . LEU A 1 24  ? 12.258  5.408   -5.598  1.00 68.27  ? 24  LEU A N   1 
ATOM   79   C CA  . LEU A 1 24  ? 12.857  4.097   -5.772  1.00 65.53  ? 24  LEU A CA  1 
ATOM   80   C C   . LEU A 1 24  ? 12.415  3.208   -4.612  1.00 64.18  ? 24  LEU A C   1 
ATOM   81   O O   . LEU A 1 24  ? 12.427  3.640   -3.463  1.00 68.14  ? 24  LEU A O   1 
ATOM   82   C CB  . LEU A 1 24  ? 14.377  4.231   -5.827  1.00 66.39  ? 24  LEU A CB  1 
ATOM   83   C CG  . LEU A 1 24  ? 15.111  3.038   -6.401  1.00 79.10  ? 24  LEU A CG  1 
ATOM   84   C CD1 . LEU A 1 24  ? 14.889  2.937   -7.902  1.00 65.55  ? 24  LEU A CD1 1 
ATOM   85   C CD2 . LEU A 1 24  ? 16.595  3.108   -6.083  1.00 82.55  ? 24  LEU A CD2 1 
ATOM   86   N N   . VAL A 1 25  ? 12.008  1.974   -4.928  1.00 60.69  ? 25  VAL A N   1 
ATOM   87   C CA  . VAL A 1 25  ? 11.534  1.037   -3.925  1.00 55.64  ? 25  VAL A CA  1 
ATOM   88   C C   . VAL A 1 25  ? 12.217  -0.318  -4.091  1.00 62.45  ? 25  VAL A C   1 
ATOM   89   O O   . VAL A 1 25  ? 12.341  -0.809  -5.211  1.00 58.41  ? 25  VAL A O   1 
ATOM   90   C CB  . VAL A 1 25  ? 9.998   0.887   -3.998  1.00 55.57  ? 25  VAL A CB  1 
ATOM   91   C CG1 . VAL A 1 25  ? 9.500   -0.164  -3.008  1.00 61.36  ? 25  VAL A CG1 1 
ATOM   92   C CG2 . VAL A 1 25  ? 9.306   2.227   -3.773  1.00 54.80  ? 25  VAL A CG2 1 
ATOM   93   N N   . GLU A 1 26  ? 12.631  -0.909  -2.959  1.00 62.30  ? 26  GLU A N   1 
ATOM   94   C CA  . GLU A 1 26  ? 13.262  -2.220  -2.917  1.00 52.36  ? 26  GLU A CA  1 
ATOM   95   C C   . GLU A 1 26  ? 12.662  -3.032  -1.770  1.00 59.67  ? 26  GLU A C   1 
ATOM   96   O O   . GLU A 1 26  ? 12.583  -2.545  -0.645  1.00 53.39  ? 26  GLU A O   1 
ATOM   97   C CB  . GLU A 1 26  ? 14.788  -2.101  -2.705  1.00 59.92  ? 26  GLU A CB  1 
ATOM   98   C CG  . GLU A 1 26  ? 15.489  -1.107  -3.618  1.00 66.34  ? 26  GLU A CG  1 
ATOM   99   C CD  . GLU A 1 26  ? 15.520  -1.466  -5.092  1.00 81.15  ? 26  GLU A CD  1 
ATOM   100  O OE1 . GLU A 1 26  ? 15.276  -2.647  -5.434  1.00 78.31  ? 26  GLU A OE1 1 
ATOM   101  O OE2 . GLU A 1 26  ? 15.776  -0.552  -5.910  1.00 82.24  ? 26  GLU A OE2 1 
ATOM   102  N N   . LEU A 1 27  ? 12.257  -4.275  -2.058  1.00 56.03  ? 27  LEU A N   1 
ATOM   103  C CA  . LEU A 1 27  ? 11.590  -5.121  -1.080  1.00 58.75  ? 27  LEU A CA  1 
ATOM   104  C C   . LEU A 1 27  ? 12.241  -6.501  -1.070  1.00 52.27  ? 27  LEU A C   1 
ATOM   105  O O   . LEU A 1 27  ? 12.335  -7.145  -2.112  1.00 55.18  ? 27  LEU A O   1 
ATOM   106  C CB  . LEU A 1 27  ? 10.072  -5.224  -1.405  1.00 49.02  ? 27  LEU A CB  1 
ATOM   107  C CG  . LEU A 1 27  ? 9.184   -5.955  -0.387  1.00 48.08  ? 27  LEU A CG  1 
ATOM   108  C CD1 . LEU A 1 27  ? 7.711   -5.856  -0.752  1.00 51.86  ? 27  LEU A CD1 1 
ATOM   109  C CD2 . LEU A 1 27  ? 9.528   -7.413  -0.274  1.00 60.59  ? 27  LEU A CD2 1 
ATOM   110  N N   . ASP A 1 28  ? 12.692  -6.931  0.117   1.00 57.88  ? 28  ASP A N   1 
ATOM   111  C CA  . ASP A 1 28  ? 13.212  -8.274  0.330   1.00 52.93  ? 28  ASP A CA  1 
ATOM   112  C C   . ASP A 1 28  ? 12.178  -8.995  1.185   1.00 56.91  ? 28  ASP A C   1 
ATOM   113  O O   . ASP A 1 28  ? 11.860  -8.528  2.275   1.00 63.85  ? 28  ASP A O   1 
ATOM   114  C CB  . ASP A 1 28  ? 14.606  -8.240  1.009   1.00 63.03  ? 28  ASP A CB  1 
ATOM   115  C CG  . ASP A 1 28  ? 15.132  -9.583  1.516   1.00 73.92  ? 28  ASP A CG  1 
ATOM   116  O OD1 . ASP A 1 28  ? 15.152  -10.555 0.723   1.00 75.83  ? 28  ASP A OD1 1 
ATOM   117  O OD2 . ASP A 1 28  ? 15.533  -9.657  2.699   1.00 70.97  ? 28  ASP A OD2 1 
ATOM   118  N N   . GLY A 1 29  ? 11.653  -10.117 0.677   1.00 58.82  ? 29  GLY A N   1 
ATOM   119  C CA  . GLY A 1 29  ? 10.462  -10.730 1.240   1.00 53.80  ? 29  GLY A CA  1 
ATOM   120  C C   . GLY A 1 29  ? 10.531  -12.242 1.441   1.00 57.03  ? 29  GLY A C   1 
ATOM   121  O O   . GLY A 1 29  ? 11.083  -12.960 0.610   1.00 60.78  ? 29  GLY A O   1 
ATOM   122  N N   . ASP A 1 30  ? 9.945   -12.703 2.555   1.00 53.40  ? 30  ASP A N   1 
ATOM   123  C CA  . ASP A 1 30  ? 9.750   -14.120 2.823   1.00 57.19  ? 30  ASP A CA  1 
ATOM   124  C C   . ASP A 1 30  ? 8.345   -14.341 3.383   1.00 48.91  ? 30  ASP A C   1 
ATOM   125  O O   . ASP A 1 30  ? 7.974   -13.738 4.388   1.00 50.00  ? 30  ASP A O   1 
ATOM   126  C CB  . ASP A 1 30  ? 10.817  -14.638 3.803   1.00 47.31  ? 30  ASP A CB  1 
ATOM   127  C CG  . ASP A 1 30  ? 10.687  -16.109 4.170   1.00 66.73  ? 30  ASP A CG  1 
ATOM   128  O OD1 . ASP A 1 30  ? 9.715   -16.748 3.727   1.00 71.01  ? 30  ASP A OD1 1 
ATOM   129  O OD2 . ASP A 1 30  ? 11.562  -16.620 4.900   1.00 80.06  ? 30  ASP A OD2 1 
ATOM   130  N N   . VAL A 1 31  ? 7.563   -15.204 2.726   1.00 50.93  ? 31  VAL A N   1 
ATOM   131  C CA  . VAL A 1 31  ? 6.219   -15.519 3.187   1.00 57.12  ? 31  VAL A CA  1 
ATOM   132  C C   . VAL A 1 31  ? 6.044   -17.033 3.287   1.00 62.41  ? 31  VAL A C   1 
ATOM   133  O O   . VAL A 1 31  ? 5.932   -17.710 2.269   1.00 65.27  ? 31  VAL A O   1 
ATOM   134  C CB  . VAL A 1 31  ? 5.145   -14.869 2.279   1.00 52.09  ? 31  VAL A CB  1 
ATOM   135  C CG1 . VAL A 1 31  ? 3.763   -15.458 2.540   1.00 56.44  ? 31  VAL A CG1 1 
ATOM   136  C CG2 . VAL A 1 31  ? 5.125   -13.354 2.453   1.00 46.72  ? 31  VAL A CG2 1 
ATOM   137  N N   . ASN A 1 32  ? 6.000   -17.544 4.526   1.00 56.81  ? 32  ASN A N   1 
ATOM   138  C CA  . ASN A 1 32  ? 6.011   -18.975 4.791   1.00 60.03  ? 32  ASN A CA  1 
ATOM   139  C C   . ASN A 1 32  ? 7.135   -19.663 4.018   1.00 69.27  ? 32  ASN A C   1 
ATOM   140  O O   . ASN A 1 32  ? 6.899   -20.637 3.305   1.00 74.42  ? 32  ASN A O   1 
ATOM   141  C CB  . ASN A 1 32  ? 4.663   -19.637 4.455   1.00 56.40  ? 32  ASN A CB  1 
ATOM   142  C CG  . ASN A 1 32  ? 3.541   -19.293 5.393   1.00 59.76  ? 32  ASN A CG  1 
ATOM   143  O OD1 . ASN A 1 32  ? 3.581   -18.314 6.142   1.00 61.14  ? 32  ASN A OD1 1 
ATOM   144  N ND2 . ASN A 1 32  ? 2.494   -20.104 5.363   1.00 54.33  ? 32  ASN A ND2 1 
ATOM   145  N N   . GLY A 1 33  ? 8.354   -19.134 4.112   1.00 64.71  ? 33  GLY A N   1 
ATOM   146  C CA  . GLY A 1 33  ? 9.492   -19.803 3.454   1.00 66.67  ? 33  GLY A CA  1 
ATOM   147  C C   . GLY A 1 33  ? 9.641   -19.372 2.011   1.00 72.83  ? 33  GLY A C   1 
ATOM   148  O O   . GLY A 1 33  ? 10.723  -19.593 1.435   1.00 66.52  ? 33  GLY A O   1 
ATOM   149  N N   . HIS A 1 34  ? 8.592   -18.778 1.447   1.00 68.24  ? 34  HIS A N   1 
ATOM   150  C CA  . HIS A 1 34  ? 8.620   -18.335 0.032   1.00 62.60  ? 34  HIS A CA  1 
ATOM   151  C C   . HIS A 1 34  ? 9.334   -16.989 -0.054  1.00 60.15  ? 34  HIS A C   1 
ATOM   152  O O   . HIS A 1 34  ? 8.724   -15.948 0.232   1.00 58.08  ? 34  HIS A O   1 
ATOM   153  C CB  . HIS A 1 34  ? 7.198   -18.277 -0.529  1.00 68.21  ? 34  HIS A CB  1 
ATOM   154  C CG  . HIS A 1 34  ? 6.677   -19.583 -1.009  1.00 71.79  ? 34  HIS A CG  1 
ATOM   155  N ND1 . HIS A 1 34  ? 5.709   -20.294 -0.338  1.00 77.46  ? 34  HIS A ND1 1 
ATOM   156  C CD2 . HIS A 1 34  ? 6.981   -20.296 -2.095  1.00 74.81  ? 34  HIS A CD2 1 
ATOM   157  C CE1 . HIS A 1 34  ? 5.447   -21.404 -1.009  1.00 90.38  ? 34  HIS A CE1 1 
ATOM   158  N NE2 . HIS A 1 34  ? 6.208   -21.424 -2.080  1.00 91.83  ? 34  HIS A NE2 1 
ATOM   159  N N   . LYS A 1 35  ? 10.600  -17.023 -0.458  1.00 64.80  ? 35  LYS A N   1 
ATOM   160  C CA  . LYS A 1 35  ? 11.416  -15.790 -0.537  1.00 61.80  ? 35  LYS A CA  1 
ATOM   161  C C   . LYS A 1 35  ? 11.136  -15.093 -1.867  1.00 55.83  ? 35  LYS A C   1 
ATOM   162  O O   . LYS A 1 35  ? 11.022  -15.787 -2.891  1.00 59.23  ? 35  LYS A O   1 
ATOM   163  C CB  . LYS A 1 35  ? 12.895  -16.154 -0.390  1.00 62.44  ? 35  LYS A CB  1 
ATOM   164  N N   . PHE A 1 36  ? 11.053  -13.770 -1.834  1.00 46.96  ? 36  PHE A N   1 
ATOM   165  C CA  . PHE A 1 36  ? 10.703  -13.017 -3.060  1.00 60.57  ? 36  PHE A CA  1 
ATOM   166  C C   . PHE A 1 36  ? 11.317  -11.645 -2.986  1.00 56.93  ? 36  PHE A C   1 
ATOM   167  O O   . PHE A 1 36  ? 11.543  -11.121 -1.891  1.00 56.14  ? 36  PHE A O   1 
ATOM   168  C CB  . PHE A 1 36  ? 9.180   -12.959 -3.217  1.00 52.44  ? 36  PHE A CB  1 
ATOM   169  C CG  . PHE A 1 36  ? 8.400   -12.157 -2.188  1.00 55.95  ? 36  PHE A CG  1 
ATOM   170  C CD1 . PHE A 1 36  ? 8.024   -12.725 -0.979  1.00 51.84  ? 36  PHE A CD1 1 
ATOM   171  C CD2 . PHE A 1 36  ? 8.015   -10.850 -2.451  1.00 57.64  ? 36  PHE A CD2 1 
ATOM   172  C CE1 . PHE A 1 36  ? 7.307   -11.995 -0.051  1.00 56.81  ? 36  PHE A CE1 1 
ATOM   173  C CE2 . PHE A 1 36  ? 7.295   -10.127 -1.519  1.00 55.51  ? 36  PHE A CE2 1 
ATOM   174  C CZ  . PHE A 1 36  ? 6.945   -10.699 -0.323  1.00 58.75  ? 36  PHE A CZ  1 
ATOM   175  N N   . SER A 1 37  ? 11.575  -11.071 -4.152  1.00 47.78  ? 37  SER A N   1 
ATOM   176  C CA  . SER A 1 37  ? 12.203  -9.734  -4.195  1.00 54.36  ? 37  SER A CA  1 
ATOM   177  C C   . SER A 1 37  ? 11.422  -8.835  -5.159  1.00 52.92  ? 37  SER A C   1 
ATOM   178  O O   . SER A 1 37  ? 11.070  -9.308  -6.252  1.00 52.12  ? 37  SER A O   1 
ATOM   179  C CB  . SER A 1 37  ? 13.656  -9.838  -4.550  1.00 55.35  ? 37  SER A CB  1 
ATOM   180  O OG  . SER A 1 37  ? 14.336  -10.706 -3.656  1.00 62.89  ? 37  SER A OG  1 
ATOM   181  N N   . VAL A 1 38  ? 11.141  -7.602  -4.741  1.00 46.76  ? 38  VAL A N   1 
ATOM   182  C CA  . VAL A 1 38  ? 10.339  -6.672  -5.586  1.00 57.10  ? 38  VAL A CA  1 
ATOM   183  C C   . VAL A 1 38  ? 11.082  -5.342  -5.729  1.00 58.78  ? 38  VAL A C   1 
ATOM   184  O O   . VAL A 1 38  ? 11.500  -4.786  -4.704  1.00 61.29  ? 38  VAL A O   1 
ATOM   185  C CB  . VAL A 1 38  ? 8.905   -6.437  -5.070  1.00 55.72  ? 38  VAL A CB  1 
ATOM   186  C CG1 . VAL A 1 38  ? 8.211   -5.297  -5.803  1.00 49.52  ? 38  VAL A CG1 1 
ATOM   187  C CG2 . VAL A 1 38  ? 8.058   -7.699  -5.144  1.00 54.22  ? 38  VAL A CG2 1 
ATOM   188  N N   . SER A 1 39  ? 11.250  -4.875  -6.958  1.00 53.24  ? 39  SER A N   1 
ATOM   189  C CA  . SER A 1 39  ? 11.864  -3.587  -7.241  1.00 52.09  ? 39  SER A CA  1 
ATOM   190  C C   . SER A 1 39  ? 10.836  -2.621  -7.829  1.00 66.52  ? 39  SER A C   1 
ATOM   191  O O   . SER A 1 39  ? 9.954   -3.032  -8.585  1.00 57.58  ? 39  SER A O   1 
ATOM   192  C CB  . SER A 1 39  ? 13.039  -3.755  -8.198  1.00 49.25  ? 39  SER A CB  1 
ATOM   193  O OG  . SER A 1 39  ? 14.060  -4.561  -7.630  1.00 60.62  ? 39  SER A OG  1 
ATOM   194  N N   . GLY A 1 40  ? 10.969  -1.334  -7.482  1.00 66.24  ? 40  GLY A N   1 
ATOM   195  C CA  . GLY A 1 40  ? 10.012  -0.318  -7.887  1.00 48.89  ? 40  GLY A CA  1 
ATOM   196  C C   . GLY A 1 40  ? 10.659  1.021   -8.231  1.00 59.46  ? 40  GLY A C   1 
ATOM   197  O O   . GLY A 1 40  ? 11.706  1.368   -7.689  1.00 61.00  ? 40  GLY A O   1 
ATOM   198  N N   . GLU A 1 41  ? 10.008  1.759   -9.138  1.00 55.63  ? 41  GLU A N   1 
ATOM   199  C CA  . GLU A 1 41  ? 10.473  3.062   -9.587  1.00 64.65  ? 41  GLU A CA  1 
ATOM   200  C C   . GLU A 1 41  ? 9.264   3.925   -9.936  1.00 62.01  ? 41  GLU A C   1 
ATOM   201  O O   . GLU A 1 41  ? 8.198   3.406   -10.265 1.00 59.50  ? 41  GLU A O   1 
ATOM   202  C CB  . GLU A 1 41  ? 11.398  2.937   -10.809 1.00 57.69  ? 41  GLU A CB  1 
ATOM   203  N N   . GLY A 1 42  ? 9.448   5.245   -9.860  1.00 53.41  ? 42  GLY A N   1 
ATOM   204  C CA  . GLY A 1 42  ? 8.368   6.179   -10.112 1.00 55.63  ? 42  GLY A CA  1 
ATOM   205  C C   . GLY A 1 42  ? 8.696   7.588   -9.631  1.00 61.82  ? 42  GLY A C   1 
ATOM   206  O O   . GLY A 1 42  ? 9.859   7.920   -9.412  1.00 61.05  ? 42  GLY A O   1 
ATOM   207  N N   . GLU A 1 43  ? 7.650   8.403   -9.473  1.00 52.60  ? 43  GLU A N   1 
ATOM   208  C CA  . GLU A 1 43  ? 7.805   9.803   -9.120  1.00 61.67  ? 43  GLU A CA  1 
ATOM   209  C C   . GLU A 1 43  ? 6.696   10.211  -8.159  1.00 65.05  ? 43  GLU A C   1 
ATOM   210  O O   . GLU A 1 43  ? 5.551   9.785   -8.305  1.00 62.19  ? 43  GLU A O   1 
ATOM   211  C CB  . GLU A 1 43  ? 7.769   10.687  -10.374 1.00 54.76  ? 43  GLU A CB  1 
ATOM   212  N N   . GLY A 1 44  ? 7.060   11.031  -7.171  1.00 66.81  ? 44  GLY A N   1 
ATOM   213  C CA  . GLY A 1 44  ? 6.102   11.558  -6.215  1.00 74.77  ? 44  GLY A CA  1 
ATOM   214  C C   . GLY A 1 44  ? 6.040   13.081  -6.277  1.00 72.32  ? 44  GLY A C   1 
ATOM   215  O O   . GLY A 1 44  ? 7.075   13.746  -6.249  1.00 75.19  ? 44  GLY A O   1 
ATOM   216  N N   . ASP A 1 45  ? 4.818   13.614  -6.372  1.00 66.37  ? 45  ASP A N   1 
ATOM   217  C CA  . ASP A 1 45  ? 4.595   15.049  -6.327  1.00 73.67  ? 45  ASP A CA  1 
ATOM   218  C C   . ASP A 1 45  ? 3.692   15.382  -5.143  1.00 79.15  ? 45  ASP A C   1 
ATOM   219  O O   . ASP A 1 45  ? 2.493   15.114  -5.177  1.00 83.18  ? 45  ASP A O   1 
ATOM   220  C CB  . ASP A 1 45  ? 3.992   15.544  -7.646  1.00 79.00  ? 45  ASP A CB  1 
ATOM   221  C CG  . ASP A 1 45  ? 3.701   17.029  -7.669  1.00 81.77  ? 45  ASP A CG  1 
ATOM   222  O OD1 . ASP A 1 45  ? 4.492   17.798  -7.077  1.00 83.04  ? 45  ASP A OD1 1 
ATOM   223  O OD2 . ASP A 1 45  ? 2.699   17.426  -8.304  1.00 69.94  ? 45  ASP A OD2 1 
ATOM   224  N N   . ALA A 1 46  ? 4.288   15.975  -4.103  1.00 78.20  ? 46  ALA A N   1 
ATOM   225  C CA  . ALA A 1 46  ? 3.607   16.205  -2.840  1.00 77.03  ? 46  ALA A CA  1 
ATOM   226  C C   . ALA A 1 46  ? 2.900   17.557  -2.772  1.00 84.92  ? 46  ALA A C   1 
ATOM   227  O O   . ALA A 1 46  ? 2.423   17.942  -1.707  1.00 86.93  ? 46  ALA A O   1 
ATOM   228  C CB  . ALA A 1 46  ? 4.598   16.084  -1.694  1.00 78.24  ? 46  ALA A CB  1 
ATOM   229  N N   . THR A 1 47  ? 2.848   18.273  -3.904  1.00 75.55  ? 47  THR A N   1 
ATOM   230  C CA  . THR A 1 47  ? 2.011   19.455  -4.030  1.00 84.28  ? 47  THR A CA  1 
ATOM   231  C C   . THR A 1 47  ? 0.549   19.027  -4.112  1.00 81.62  ? 47  THR A C   1 
ATOM   232  O O   . THR A 1 47  ? -0.275  19.492  -3.331  1.00 92.39  ? 47  THR A O   1 
ATOM   233  C CB  . THR A 1 47  ? 2.435   20.299  -5.239  1.00 82.16  ? 47  THR A CB  1 
ATOM   234  O OG1 . THR A 1 47  ? 3.673   20.939  -4.935  1.00 87.86  ? 47  THR A OG1 1 
ATOM   235  C CG2 . THR A 1 47  ? 1.405   21.351  -5.613  1.00 81.46  ? 47  THR A CG2 1 
ATOM   236  N N   . TYR A 1 48  ? 0.251   18.145  -5.074  1.00 80.43  ? 48  TYR A N   1 
ATOM   237  C CA  . TYR A 1 48  ? -1.075  17.564  -5.224  1.00 87.45  ? 48  TYR A CA  1 
ATOM   238  C C   . TYR A 1 48  ? -1.217  16.284  -4.400  1.00 83.38  ? 48  TYR A C   1 
ATOM   239  O O   . TYR A 1 48  ? -2.330  15.818  -4.160  1.00 90.67  ? 48  TYR A O   1 
ATOM   240  C CB  . TYR A 1 48  ? -1.368  17.281  -6.709  1.00 68.64  ? 48  TYR A CB  1 
ATOM   241  N N   . GLY A 1 49  ? -0.080  15.729  -3.962  1.00 78.34  ? 49  GLY A N   1 
ATOM   242  C CA  . GLY A 1 49  ? -0.055  14.460  -3.255  1.00 79.30  ? 49  GLY A CA  1 
ATOM   243  C C   . GLY A 1 49  ? -0.346  13.294  -4.194  1.00 74.75  ? 49  GLY A C   1 
ATOM   244  O O   . GLY A 1 49  ? -1.179  12.444  -3.890  1.00 79.25  ? 49  GLY A O   1 
ATOM   245  N N   . LYS A 1 50  ? 0.345   13.279  -5.340  1.00 74.31  ? 50  LYS A N   1 
ATOM   246  C CA  . LYS A 1 50  ? 0.168   12.241  -6.341  1.00 68.36  ? 50  LYS A CA  1 
ATOM   247  C C   . LYS A 1 50  ? 1.431   11.392  -6.432  1.00 60.55  ? 50  LYS A C   1 
ATOM   248  O O   . LYS A 1 50  ? 2.541   11.916  -6.359  1.00 57.16  ? 50  LYS A O   1 
ATOM   249  C CB  . LYS A 1 50  ? -0.163  12.847  -7.714  1.00 67.67  ? 50  LYS A CB  1 
ATOM   250  N N   . LEU A 1 51  ? 1.235   10.078  -6.579  1.00 54.70  ? 51  LEU A N   1 
ATOM   251  C CA  . LEU A 1 51  ? 2.325   9.135   -6.757  1.00 62.91  ? 51  LEU A CA  1 
ATOM   252  C C   . LEU A 1 51  ? 1.991   8.241   -7.945  1.00 64.72  ? 51  LEU A C   1 
ATOM   253  O O   . LEU A 1 51  ? 0.855   7.788   -8.081  1.00 63.73  ? 51  LEU A O   1 
ATOM   254  C CB  . LEU A 1 51  ? 2.535   8.281   -5.498  1.00 61.08  ? 51  LEU A CB  1 
ATOM   255  N N   . THR A 1 52  ? 2.994   8.019   -8.803  1.00 53.84  ? 52  THR A N   1 
ATOM   256  C CA  . THR A 1 52  ? 2.871   7.123   -9.939  1.00 53.77  ? 52  THR A CA  1 
ATOM   257  C C   . THR A 1 52  ? 4.069   6.186   -9.883  1.00 60.70  ? 52  THR A C   1 
ATOM   258  O O   . THR A 1 52  ? 5.200   6.606   -10.111 1.00 64.86  ? 52  THR A O   1 
ATOM   259  C CB  . THR A 1 52  ? 2.779   7.901   -11.262 1.00 65.03  ? 52  THR A CB  1 
ATOM   260  O OG1 . THR A 1 52  ? 3.924   8.755   -11.389 1.00 57.13  ? 52  THR A OG1 1 
ATOM   261  C CG2 . THR A 1 52  ? 1.496   8.719   -11.360 1.00 44.81  ? 52  THR A CG2 1 
ATOM   262  N N   . LEU A 1 53  ? 3.807   4.925   -9.536  1.00 60.68  ? 53  LEU A N   1 
ATOM   263  C CA  . LEU A 1 53  ? 4.861   3.956   -9.302  1.00 58.35  ? 53  LEU A CA  1 
ATOM   264  C C   . LEU A 1 53  ? 4.603   2.695   -10.120 1.00 61.12  ? 53  LEU A C   1 
ATOM   265  O O   . LEU A 1 53  ? 3.460   2.373   -10.440 1.00 62.30  ? 53  LEU A O   1 
ATOM   266  C CB  . LEU A 1 53  ? 4.941   3.629   -7.802  1.00 61.63  ? 53  LEU A CB  1 
ATOM   267  C CG  . LEU A 1 53  ? 5.899   4.490   -6.966  1.00 66.64  ? 53  LEU A CG  1 
ATOM   268  C CD1 . LEU A 1 53  ? 5.601   5.969   -7.101  1.00 69.65  ? 53  LEU A CD1 1 
ATOM   269  C CD2 . LEU A 1 53  ? 5.839   4.096   -5.501  1.00 66.72  ? 53  LEU A CD2 1 
ATOM   270  N N   . LYS A 1 54  ? 5.694   2.009   -10.475 1.00 54.89  ? 54  LYS A N   1 
ATOM   271  C CA  . LYS A 1 54  ? 5.621   0.714   -11.126 1.00 53.27  ? 54  LYS A CA  1 
ATOM   272  C C   . LYS A 1 54  ? 6.517   -0.251  -10.359 1.00 55.12  ? 54  LYS A C   1 
ATOM   273  O O   . LYS A 1 54  ? 7.637   0.099   -9.993  1.00 52.98  ? 54  LYS A O   1 
ATOM   274  C CB  . LYS A 1 54  ? 6.030   0.819   -12.598 1.00 47.94  ? 54  LYS A CB  1 
ATOM   275  C CG  . LYS A 1 54  ? 6.205   -0.521  -13.297 1.00 49.18  ? 54  LYS A CG  1 
ATOM   276  C CD  . LYS A 1 54  ? 5.962   -0.423  -14.783 1.00 48.42  ? 54  LYS A CD  1 
ATOM   277  C CE  . LYS A 1 54  ? 6.571   -1.544  -15.584 1.00 52.40  ? 54  LYS A CE  1 
ATOM   278  N NZ  . LYS A 1 54  ? 7.926   -1.185  -16.087 1.00 67.38  ? 54  LYS A NZ  1 
ATOM   279  N N   . PHE A 1 55  ? 5.994   -1.456  -10.112 1.00 51.91  ? 55  PHE A N   1 
ATOM   280  C CA  . PHE A 1 55  ? 6.725   -2.491  -9.404  1.00 61.38  ? 55  PHE A CA  1 
ATOM   281  C C   . PHE A 1 55  ? 6.852   -3.729  -10.286 1.00 55.22  ? 55  PHE A C   1 
ATOM   282  O O   . PHE A 1 55  ? 5.915   -4.080  -11.002 1.00 56.14  ? 55  PHE A O   1 
ATOM   283  C CB  . PHE A 1 55  ? 6.021   -2.825  -8.089  1.00 50.68  ? 55  PHE A CB  1 
ATOM   284  C CG  . PHE A 1 55  ? 5.820   -1.620  -7.200  1.00 55.80  ? 55  PHE A CG  1 
ATOM   285  C CD1 . PHE A 1 55  ? 6.833   -1.173  -6.370  1.00 58.56  ? 55  PHE A CD1 1 
ATOM   286  C CD2 . PHE A 1 55  ? 4.627   -0.920  -7.214  1.00 53.77  ? 55  PHE A CD2 1 
ATOM   287  C CE1 . PHE A 1 55  ? 6.645   -0.062  -5.552  1.00 52.56  ? 55  PHE A CE1 1 
ATOM   288  C CE2 . PHE A 1 55  ? 4.445   0.190   -6.400  1.00 46.62  ? 55  PHE A CE2 1 
ATOM   289  C CZ  . PHE A 1 55  ? 5.454   0.615   -5.579  1.00 50.84  ? 55  PHE A CZ  1 
ATOM   290  N N   . ILE A 1 56  ? 8.029   -4.365  -10.235 1.00 54.40  ? 56  ILE A N   1 
ATOM   291  C CA  . ILE A 1 56  ? 8.266   -5.631  -10.908 1.00 57.42  ? 56  ILE A CA  1 
ATOM   292  C C   . ILE A 1 56  ? 8.816   -6.639  -9.901  1.00 61.37  ? 56  ILE A C   1 
ATOM   293  O O   . ILE A 1 56  ? 9.482   -6.264  -8.939  1.00 67.24  ? 56  ILE A O   1 
ATOM   294  C CB  . ILE A 1 56  ? 9.210   -5.465  -12.130 1.00 68.23  ? 56  ILE A CB  1 
ATOM   295  C CG1 . ILE A 1 56  ? 10.619  -4.935  -11.734 1.00 66.70  ? 56  ILE A CG1 1 
ATOM   296  C CG2 . ILE A 1 56  ? 8.568   -4.588  -13.205 1.00 59.80  ? 56  ILE A CG2 1 
ATOM   297  N N   . CYS A 1 57  ? 8.521   -7.921  -10.131 1.00 58.84  ? 57  CYS A N   1 
ATOM   298  C CA  . CYS A 1 57  ? 9.041   -8.993  -9.301  1.00 60.25  ? 57  CYS A CA  1 
ATOM   299  C C   . CYS A 1 57  ? 10.294  -9.565  -9.958  1.00 69.44  ? 57  CYS A C   1 
ATOM   300  O O   . CYS A 1 57  ? 10.214  -10.163 -11.030 1.00 74.45  ? 57  CYS A O   1 
ATOM   301  C CB  . CYS A 1 57  ? 7.983   -10.065 -9.082  1.00 56.15  ? 57  CYS A CB  1 
ATOM   302  S SG  . CYS A 1 57  ? 8.523   -11.425 -8.023  1.00 67.88  ? 57  CYS A SG  1 
ATOM   303  N N   . THR A 1 58  ? 11.443  -9.373  -9.301  1.00 66.61  ? 58  THR A N   1 
ATOM   304  C CA  . THR A 1 58  ? 12.729  -9.776  -9.850  1.00 61.65  ? 58  THR A CA  1 
ATOM   305  C C   . THR A 1 58  ? 12.998  -11.274 -9.706  1.00 67.15  ? 58  THR A C   1 
ATOM   306  O O   . THR A 1 58  ? 13.905  -11.795 -10.355 1.00 69.76  ? 58  THR A O   1 
ATOM   307  C CB  . THR A 1 58  ? 13.862  -8.979  -9.187  1.00 58.25  ? 58  THR A CB  1 
ATOM   308  O OG1 . THR A 1 58  ? 13.911  -9.304  -7.801  1.00 68.94  ? 58  THR A OG1 1 
ATOM   309  C CG2 . THR A 1 58  ? 13.697  -7.483  -9.339  1.00 45.63  ? 58  THR A CG2 1 
ATOM   310  N N   . THR A 1 59  ? 12.209  -11.950 -8.855  1.00 64.09  ? 59  THR A N   1 
ATOM   311  C CA  . THR A 1 59  ? 12.409  -13.357 -8.539  1.00 58.75  ? 59  THR A CA  1 
ATOM   312  C C   . THR A 1 59  ? 11.537  -14.310 -9.358  1.00 63.99  ? 59  THR A C   1 
ATOM   313  O O   . THR A 1 59  ? 11.626  -15.524 -9.188  1.00 56.23  ? 59  THR A O   1 
ATOM   314  C CB  . THR A 1 59  ? 12.129  -13.590 -7.047  1.00 59.04  ? 59  THR A CB  1 
ATOM   315  O OG1 . THR A 1 59  ? 12.954  -14.656 -6.573  1.00 81.33  ? 59  THR A OG1 1 
ATOM   316  C CG2 . THR A 1 59  ? 10.658  -13.916 -6.765  1.00 59.55  ? 59  THR A CG2 1 
ATOM   317  N N   . GLY A 1 60  ? 10.671  -13.752 -10.215 1.00 65.98  ? 60  GLY A N   1 
ATOM   318  C CA  . GLY A 1 60  ? 9.723   -14.541 -10.989 1.00 63.56  ? 60  GLY A CA  1 
ATOM   319  C C   . GLY A 1 60  ? 8.271   -14.241 -10.621 1.00 67.39  ? 60  GLY A C   1 
ATOM   320  O O   . GLY A 1 60  ? 7.830   -13.101 -10.741 1.00 72.33  ? 60  GLY A O   1 
ATOM   321  N N   . LYS A 1 61  ? 7.541   -15.277 -10.178 1.00 67.09  ? 61  LYS A N   1 
ATOM   322  C CA  . LYS A 1 61  ? 6.132   -15.158 -9.834  1.00 58.46  ? 61  LYS A CA  1 
ATOM   323  C C   . LYS A 1 61  ? 5.974   -14.779 -8.366  1.00 64.98  ? 61  LYS A C   1 
ATOM   324  O O   . LYS A 1 61  ? 6.608   -15.374 -7.498  1.00 74.86  ? 61  LYS A O   1 
ATOM   325  C CB  . LYS A 1 61  ? 5.378   -16.468 -10.106 1.00 55.92  ? 61  LYS A CB  1 
ATOM   326  N N   . LEU A 1 62  ? 5.114   -13.788 -8.106  1.00 65.74  ? 62  LEU A N   1 
ATOM   327  C CA  . LEU A 1 62  ? 4.890   -13.296 -6.758  1.00 61.90  ? 62  LEU A CA  1 
ATOM   328  C C   . LEU A 1 62  ? 4.171   -14.383 -5.961  1.00 64.33  ? 62  LEU A C   1 
ATOM   329  O O   . LEU A 1 62  ? 3.143   -14.893 -6.405  1.00 64.28  ? 62  LEU A O   1 
ATOM   330  C CB  . LEU A 1 62  ? 4.075   -11.989 -6.800  1.00 62.74  ? 62  LEU A CB  1 
ATOM   331  C CG  . LEU A 1 62  ? 4.229   -11.059 -5.599  1.00 60.89  ? 62  LEU A CG  1 
ATOM   332  C CD1 . LEU A 1 62  ? 5.662   -10.590 -5.436  1.00 65.09  ? 62  LEU A CD1 1 
ATOM   333  C CD2 . LEU A 1 62  ? 3.330   -9.841  -5.727  1.00 53.00  ? 62  LEU A CD2 1 
ATOM   334  N N   . PRO A 1 63  ? 4.696   -14.793 -4.780  1.00 58.28  ? 63  PRO A N   1 
ATOM   335  C CA  . PRO A 1 63  ? 4.053   -15.827 -3.977  1.00 56.02  ? 63  PRO A CA  1 
ATOM   336  C C   . PRO A 1 63  ? 2.734   -15.372 -3.362  1.00 55.59  ? 63  PRO A C   1 
ATOM   337  O O   . PRO A 1 63  ? 1.892   -16.196 -3.019  1.00 57.43  ? 63  PRO A O   1 
ATOM   338  C CB  . PRO A 1 63  ? 5.076   -16.130 -2.867  1.00 60.53  ? 63  PRO A CB  1 
ATOM   339  C CG  . PRO A 1 63  ? 6.284   -15.302 -3.167  1.00 60.62  ? 63  PRO A CG  1 
ATOM   340  C CD  . PRO A 1 63  ? 5.905   -14.245 -4.149  1.00 60.46  ? 63  PRO A CD  1 
ATOM   341  N N   . VAL A 1 64  ? 2.607   -14.049 -3.202  1.00 58.41  ? 64  VAL A N   1 
ATOM   342  C CA  . VAL A 1 64  ? 1.414   -13.410 -2.678  1.00 59.93  ? 64  VAL A CA  1 
ATOM   343  C C   . VAL A 1 64  ? 0.789   -12.543 -3.768  1.00 52.44  ? 64  VAL A C   1 
ATOM   344  O O   . VAL A 1 64  ? 1.470   -12.162 -4.711  1.00 53.30  ? 64  VAL A O   1 
ATOM   345  C CB  . VAL A 1 64  ? 1.768   -12.575 -1.435  1.00 58.31  ? 64  VAL A CB  1 
ATOM   346  C CG1 . VAL A 1 64  ? 2.446   -13.438 -0.381  1.00 50.68  ? 64  VAL A CG1 1 
ATOM   347  C CG2 . VAL A 1 64  ? 2.635   -11.369 -1.799  1.00 54.79  ? 64  VAL A CG2 1 
ATOM   348  N N   . PRO A 1 65  ? -0.518  -12.206 -3.685  1.00 57.38  ? 65  PRO A N   1 
ATOM   349  C CA  . PRO A 1 65  ? -1.119  -11.244 -4.602  1.00 55.77  ? 65  PRO A CA  1 
ATOM   350  C C   . PRO A 1 65  ? -0.592  -9.823  -4.420  1.00 52.76  ? 65  PRO A C   1 
ATOM   351  O O   . PRO A 1 65  ? -0.338  -9.388  -3.301  1.00 56.18  ? 65  PRO A O   1 
ATOM   352  C CB  . PRO A 1 65  ? -2.619  -11.331 -4.274  1.00 57.82  ? 65  PRO A CB  1 
ATOM   353  C CG  . PRO A 1 65  ? -2.781  -12.600 -3.483  1.00 60.60  ? 65  PRO A CG  1 
ATOM   354  C CD  . PRO A 1 65  ? -1.493  -12.759 -2.735  1.00 64.68  ? 65  PRO A CD  1 
ATOM   355  N N   . TRP A 1 66  ? -0.464  -9.102  -5.538  1.00 51.57  ? 66  TRP A N   1 
ATOM   356  C CA  . TRP A 1 66  ? 0.046   -7.740  -5.546  1.00 44.27  ? 66  TRP A CA  1 
ATOM   357  C C   . TRP A 1 66  ? -0.713  -6.763  -4.648  1.00 52.70  ? 66  TRP A C   1 
ATOM   358  O O   . TRP A 1 66  ? -0.093  -5.902  -4.029  1.00 50.22  ? 66  TRP A O   1 
ATOM   359  C CB  . TRP A 1 66  ? 0.057   -7.205  -6.976  1.00 42.72  ? 66  TRP A CB  1 
ATOM   360  C CG  . TRP A 1 66  ? 1.218   -7.641  -7.821  1.00 51.25  ? 66  TRP A CG  1 
ATOM   361  C CD1 . TRP A 1 66  ? 1.198   -8.545  -8.841  1.00 47.22  ? 66  TRP A CD1 1 
ATOM   362  C CD2 . TRP A 1 66  ? 2.555   -7.134  -7.760  1.00 51.20  ? 66  TRP A CD2 1 
ATOM   363  N NE1 . TRP A 1 66  ? 2.447   -8.650  -9.405  1.00 46.53  ? 66  TRP A NE1 1 
ATOM   364  C CE2 . TRP A 1 66  ? 3.300   -7.792  -8.763  1.00 52.31  ? 66  TRP A CE2 1 
ATOM   365  C CE3 . TRP A 1 66  ? 3.198   -6.193  -6.954  1.00 48.65  ? 66  TRP A CE3 1 
ATOM   366  C CZ2 . TRP A 1 66  ? 4.655   -7.540  -8.972  1.00 46.47  ? 66  TRP A CZ2 1 
ATOM   367  C CZ3 . TRP A 1 66  ? 4.544   -5.948  -7.162  1.00 51.81  ? 66  TRP A CZ3 1 
ATOM   368  C CH2 . TRP A 1 66  ? 5.255   -6.614  -8.164  1.00 51.20  ? 66  TRP A CH2 1 
ATOM   369  N N   . PRO A 1 67  ? -2.065  -6.818  -4.560  1.00 50.71  ? 67  PRO A N   1 
ATOM   370  C CA  . PRO A 1 67  ? -2.794  -5.892  -3.700  1.00 52.12  ? 67  PRO A CA  1 
ATOM   371  C C   . PRO A 1 67  ? -2.345  -5.911  -2.238  1.00 54.97  ? 67  PRO A C   1 
ATOM   372  O O   . PRO A 1 67  ? -2.417  -4.890  -1.558  1.00 56.53  ? 67  PRO A O   1 
ATOM   373  C CB  . PRO A 1 67  ? -4.258  -6.333  -3.877  1.00 54.34  ? 67  PRO A CB  1 
ATOM   374  C CG  . PRO A 1 67  ? -4.285  -7.022  -5.208  1.00 49.73  ? 67  PRO A CG  1 
ATOM   375  C CD  . PRO A 1 67  ? -2.956  -7.706  -5.325  1.00 46.56  ? 67  PRO A CD  1 
ATOM   376  N N   . THR A 1 68  ? -1.803  -7.041  -1.792  1.00 52.20  ? 68  THR A N   1 
ATOM   377  C CA  . THR A 1 68  ? -1.367  -7.189  -0.385  1.00 50.21  ? 68  THR A CA  1 
ATOM   378  C C   . THR A 1 68  ? -0.116  -6.392  -0.122  1.00 53.78  ? 68  THR A C   1 
ATOM   379  O O   . THR A 1 68  ? 0.153   -6.115  1.054   1.00 51.35  ? 68  THR A O   1 
ATOM   380  C CB  . THR A 1 68  ? -1.130  -8.668  -0.092  1.00 48.04  ? 68  THR A CB  1 
ATOM   381  O OG1 . THR A 1 68  ? 0.033   -9.014  -0.834  1.00 49.35  ? 68  THR A OG1 1 
ATOM   382  C CG2 . THR A 1 68  ? -2.299  -9.541  -0.508  1.00 50.28  ? 68  THR A CG2 1 
ATOM   383  N N   . LEU A 1 69  ? 0.616   -6.008  -1.164  1.00 49.74  ? 69  LEU A N   1 
ATOM   384  C CA  . LEU A 1 69  ? 1.921   -5.338  -0.947  1.00 49.59  ? 69  LEU A CA  1 
ATOM   385  C C   . LEU A 1 69  ? 1.814   -3.822  -1.146  1.00 54.49  ? 69  LEU A C   1 
ATOM   386  O O   . LEU A 1 69  ? 2.787   -3.126  -0.825  1.00 52.80  ? 69  LEU A O   1 
ATOM   387  C CB  . LEU A 1 69  ? 2.927   -5.979  -1.896  1.00 52.39  ? 69  LEU A CB  1 
ATOM   388  C CG  . LEU A 1 69  ? 3.175   -7.476  -1.696  1.00 56.16  ? 69  LEU A CG  1 
ATOM   389  C CD1 . LEU A 1 69  ? 4.249   -7.957  -2.646  1.00 61.67  ? 69  LEU A CD1 1 
ATOM   390  C CD2 . LEU A 1 69  ? 3.578   -7.754  -0.263  1.00 46.76  ? 69  LEU A CD2 1 
ATOM   391  N N   . VAL A 1 70  ? 0.666   -3.329  -1.598  1.00 44.41  ? 70  VAL A N   1 
ATOM   392  C CA  . VAL A 1 70  ? 0.533   -1.875  -1.905  1.00 50.20  ? 70  VAL A CA  1 
ATOM   393  C C   . VAL A 1 70  ? 0.944   -1.045  -0.682  1.00 49.64  ? 70  VAL A C   1 
ATOM   394  O O   . VAL A 1 70  ? 1.841   -0.203  -0.829  1.00 51.27  ? 70  VAL A O   1 
ATOM   395  C CB  . VAL A 1 70  ? -0.885  -1.502  -2.379  1.00 53.84  ? 70  VAL A CB  1 
ATOM   396  C CG1 . VAL A 1 70  ? -1.002  -0.024  -2.722  1.00 41.87  ? 70  VAL A CG1 1 
ATOM   397  C CG2 . VAL A 1 70  ? -1.343  -2.366  -3.544  1.00 49.63  ? 70  VAL A CG2 1 
ATOM   398  N N   . THR A 1 71  ? 0.324   -1.272  0.471   1.00 52.64  ? 71  THR A N   1 
ATOM   399  C CA  . THR A 1 71  ? 0.598   -0.423  1.649   1.00 53.19  ? 71  THR A CA  1 
ATOM   400  C C   . THR A 1 71  ? 2.059   -0.500  2.034   1.00 53.07  ? 71  THR A C   1 
ATOM   401  O O   . THR A 1 71  ? 2.583   0.493   2.548   1.00 54.19  ? 71  THR A O   1 
ATOM   402  C CB  . THR A 1 71  ? -0.325  -0.842  2.789   1.00 60.03  ? 71  THR A CB  1 
ATOM   403  O OG1 . THR A 1 71  ? -0.160  -2.246  2.938   1.00 58.90  ? 71  THR A OG1 1 
ATOM   404  C CG2 . THR A 1 71  ? -1.779  -0.530  2.488   1.00 51.62  ? 71  THR A CG2 1 
ATOM   405  N N   . THR A 1 72  ? 2.723   -1.616  1.776   1.00 42.94  ? 72  THR A N   1 
ATOM   406  C CA  . THR A 1 72  ? 4.122   -1.718  2.223   1.00 57.50  ? 72  THR A CA  1 
ATOM   407  C C   . THR A 1 72  ? 5.001   -1.097  1.161   1.00 51.91  ? 72  THR A C   1 
ATOM   408  O O   . THR A 1 72  ? 5.831   -0.247  1.510   1.00 55.29  ? 72  THR A O   1 
ATOM   409  C CB  . THR A 1 72  ? 4.472   -3.174  2.531   1.00 51.90  ? 72  THR A CB  1 
ATOM   410  O OG1 . THR A 1 72  ? 3.866   -3.965  1.516   1.00 66.63  ? 72  THR A OG1 1 
ATOM   411  C CG2 . THR A 1 72  ? 3.931   -3.617  3.876   1.00 52.19  ? 72  THR A CG2 1 
ATOM   412  N N   . LEU A 1 73  ? 4.793   -1.478  -0.097  1.00 53.50  ? 73  LEU A N   1 
ATOM   413  C CA  . LEU A 1 73  ? 5.582   -0.926  -1.221  1.00 52.01  ? 73  LEU A CA  1 
ATOM   414  C C   . LEU A 1 73  ? 5.382   0.597   -1.303  1.00 56.35  ? 73  LEU A C   1 
ATOM   415  O O   . LEU A 1 73  ? 6.374   1.319   -1.483  1.00 56.74  ? 73  LEU A O   1 
ATOM   416  C CB  . LEU A 1 73  ? 5.150   -1.633  -2.500  1.00 48.61  ? 73  LEU A CB  1 
ATOM   417  C CG  . LEU A 1 73  ? 5.689   -3.048  -2.713  1.00 56.73  ? 73  LEU A CG  1 
ATOM   418  C CD1 . LEU A 1 73  ? 5.016   -3.666  -3.922  1.00 46.09  ? 73  LEU A CD1 1 
ATOM   419  C CD2 . LEU A 1 73  ? 7.186   -2.989  -2.914  1.00 49.63  ? 73  LEU A CD2 1 
HETATM 420  C CD2 . SWG A 1 74  ? -2.244  3.092   1.804   1.00 59.04  ? 74  SWG A CD2 1 
HETATM 421  C CE3 . SWG A 1 74  ? -2.798  3.402   3.051   1.00 67.02  ? 74  SWG A CE3 1 
HETATM 422  C CZ3 . SWG A 1 74  ? -4.158  3.306   3.248   1.00 61.26  ? 74  SWG A CZ3 1 
HETATM 423  C CH2 . SWG A 1 74  ? -4.949  2.901   2.209   1.00 59.05  ? 74  SWG A CH2 1 
HETATM 424  C CZ2 . SWG A 1 74  ? -4.447  2.578   0.946   1.00 61.96  ? 74  SWG A CZ2 1 
HETATM 425  C CE2 . SWG A 1 74  ? -3.078  2.684   0.776   1.00 62.95  ? 74  SWG A CE2 1 
HETATM 426  N NE1 . SWG A 1 74  ? -2.330  2.428   -0.367  1.00 59.91  ? 74  SWG A NE1 1 
HETATM 427  C CD1 . SWG A 1 74  ? -1.026  2.678   -0.028  1.00 60.85  ? 74  SWG A CD1 1 
HETATM 428  C CG  . SWG A 1 74  ? -0.882  3.085   1.262   1.00 60.53  ? 74  SWG A CG  1 
HETATM 429  C CB2 . SWG A 1 74  ? 0.354   3.456   2.015   1.00 59.82  ? 74  SWG A CB2 1 
HETATM 430  C CA2 . SWG A 1 74  ? 1.599   3.291   1.470   1.00 59.19  ? 74  SWG A CA2 1 
HETATM 431  N N2  . SWG A 1 74  ? 1.866   2.909   0.187   1.00 62.08  ? 74  SWG A N2  1 
HETATM 432  C C2  . SWG A 1 74  ? 2.887   3.481   2.116   1.00 65.83  ? 74  SWG A C2  1 
HETATM 433  O O2  . SWG A 1 74  ? 3.135   3.826   3.272   1.00 74.93  ? 74  SWG A O2  1 
HETATM 434  N N3  . SWG A 1 74  ? 3.805   3.201   1.172   1.00 65.02  ? 74  SWG A N3  1 
HETATM 435  C CA3 . SWG A 1 74  ? 5.223   3.207   1.268   1.00 66.52  ? 74  SWG A CA3 1 
HETATM 436  C C3  . SWG A 1 74  ? 6.135   4.326   1.705   1.00 65.51  ? 74  SWG A C3  1 
HETATM 437  O O3  . SWG A 1 74  ? 6.992   3.798   2.408   1.00 73.62  ? 74  SWG A O3  1 
HETATM 438  C C1  . SWG A 1 74  ? 3.200   2.856   0.066   1.00 59.65  ? 74  SWG A C1  1 
HETATM 439  C CA1 . SWG A 1 74  ? 3.887   2.492   -1.201  1.00 60.11  ? 74  SWG A CA1 1 
HETATM 440  N N1  . SWG A 1 74  ? 4.154   1.069   -1.135  1.00 42.55  ? 74  SWG A N1  1 
HETATM 441  C CB1 . SWG A 1 74  ? 3.035   2.783   -2.433  1.00 46.74  ? 74  SWG A CB1 1 
HETATM 442  O OG1 . SWG A 1 74  ? 2.849   4.202   -2.468  1.00 55.77  ? 74  SWG A OG1 1 
ATOM   443  N N   . VAL A 1 75  ? 5.905   5.640   1.830   1.00 71.72  ? 75  VAL A N   1 
ATOM   444  C CA  . VAL A 1 75  ? 6.216   6.731   0.858   1.00 76.76  ? 75  VAL A CA  1 
ATOM   445  C C   . VAL A 1 75  ? 5.162   7.810   1.154   1.00 70.27  ? 75  VAL A C   1 
ATOM   446  O O   . VAL A 1 75  ? 4.784   8.576   0.256   1.00 73.53  ? 75  VAL A O   1 
ATOM   447  C CB  . VAL A 1 75  ? 6.273   6.317   -0.627  1.00 81.05  ? 75  VAL A CB  1 
ATOM   448  C CG1 . VAL A 1 75  ? 6.607   7.485   -1.544  1.00 79.73  ? 75  VAL A CG1 1 
ATOM   449  C CG2 . VAL A 1 75  ? 7.298   5.215   -0.867  1.00 82.40  ? 75  VAL A CG2 1 
ATOM   450  N N   . GLN A 1 76  ? 4.703   7.845   2.402   1.00 73.12  ? 76  GLN A N   1 
ATOM   451  C CA  . GLN A 1 76  ? 3.693   8.843   2.821   1.00 70.31  ? 76  GLN A CA  1 
ATOM   452  C C   . GLN A 1 76  ? 4.444   10.140  3.087   1.00 63.04  ? 76  GLN A C   1 
ATOM   453  O O   . GLN A 1 76  ? 3.797   11.132  3.450   1.00 70.23  ? 76  GLN A O   1 
ATOM   454  C CB  . GLN A 1 76  ? 2.960   8.300   4.047   1.00 71.16  ? 76  GLN A CB  1 
ATOM   455  C CG  . GLN A 1 76  ? 1.871   7.287   3.715   1.00 72.44  ? 76  GLN A CG  1 
ATOM   456  C CD  . GLN A 1 76  ? 1.562   6.349   4.859   1.00 71.97  ? 76  GLN A CD  1 
ATOM   457  O OE1 . GLN A 1 76  ? 0.415   5.939   5.067   1.00 71.06  ? 76  GLN A OE1 1 
ATOM   458  N NE2 . GLN A 1 76  ? 2.590   5.997   5.615   1.00 78.09  ? 76  GLN A NE2 1 
ATOM   459  N N   . CYS A 1 77  ? 5.764   10.109  2.914   1.00 65.24  ? 77  CYS A N   1 
ATOM   460  C CA  . CYS A 1 77  ? 6.586   11.330  3.070   1.00 66.34  ? 77  CYS A CA  1 
ATOM   461  C C   . CYS A 1 77  ? 6.015   12.403  2.142   1.00 85.07  ? 77  CYS A C   1 
ATOM   462  O O   . CYS A 1 77  ? 6.288   13.593  2.362   1.00 86.90  ? 77  CYS A O   1 
ATOM   463  C CB  . CYS A 1 77  ? 8.026   11.032  2.694   1.00 54.59  ? 77  CYS A CB  1 
ATOM   464  S SG  . CYS A 1 77  ? 8.177   9.760   1.418   1.00 89.69  ? 77  CYS A SG  1 
ATOM   465  N N   . PHE A 1 78  ? 5.254   11.984  1.141   1.00 64.48  ? 78  PHE A N   1 
ATOM   466  C CA  . PHE A 1 78  ? 4.604   12.945  0.231   1.00 76.94  ? 78  PHE A CA  1 
ATOM   467  C C   . PHE A 1 78  ? 3.302   13.337  0.854   1.00 84.75  ? 78  PHE A C   1 
ATOM   468  O O   . PHE A 1 78  ? 3.325   13.796  2.005   1.00 85.32  ? 78  PHE A O   1 
ATOM   469  C CB  . PHE A 1 78  ? 4.457   12.183  -1.085  1.00 78.76  ? 78  PHE A CB  1 
ATOM   470  C CG  . PHE A 1 78  ? 5.789   12.016  -1.802  1.00 73.34  ? 78  PHE A CG  1 
ATOM   471  C CD1 . PHE A 1 78  ? 6.290   13.022  -2.617  1.00 76.51  ? 78  PHE A CD1 1 
ATOM   472  C CD2 . PHE A 1 78  ? 6.550   10.868  -1.633  1.00 73.31  ? 78  PHE A CD2 1 
ATOM   473  C CE1 . PHE A 1 78  ? 7.508   12.875  -3.255  1.00 76.52  ? 78  PHE A CE1 1 
ATOM   474  C CE2 . PHE A 1 78  ? 7.768   10.728  -2.274  1.00 78.41  ? 78  PHE A CE2 1 
ATOM   475  C CZ  . PHE A 1 78  ? 8.243   11.729  -3.084  1.00 66.18  ? 78  PHE A CZ  1 
ATOM   476  N N   . ALA A 1 79  ? 2.202   13.165  0.126   1.00 75.69  ? 79  ALA A N   1 
ATOM   477  C CA  . ALA A 1 79  ? 0.861   13.453  0.683   1.00 80.47  ? 79  ALA A CA  1 
ATOM   478  C C   . ALA A 1 79  ? 0.596   14.957  0.723   1.00 83.97  ? 79  ALA A C   1 
ATOM   479  O O   . ALA A 1 79  ? 1.478   15.739  1.119   1.00 87.43  ? 79  ALA A O   1 
ATOM   480  C CB  . ALA A 1 79  ? 0.714   12.832  2.049   1.00 80.72  ? 79  ALA A CB  1 
ATOM   481  N N   . ARG A 1 80  ? -0.616  15.345  0.339   1.00 77.86  ? 80  ARG A N   1 
ATOM   482  C CA  . ARG A 1 80  ? -0.975  16.781  0.298   1.00 84.29  ? 80  ARG A CA  1 
ATOM   483  C C   . ARG A 1 80  ? -1.474  17.209  1.678   1.00 84.91  ? 80  ARG A C   1 
ATOM   484  O O   . ARG A 1 80  ? -2.654  16.958  1.984   1.00 76.95  ? 80  ARG A O   1 
ATOM   485  C CB  . ARG A 1 80  ? -2.037  17.002  -0.783  1.00 79.16  ? 80  ARG A CB  1 
ATOM   486  C CG  . ARG A 1 80  ? -2.286  18.465  -1.116  1.00 82.03  ? 80  ARG A CG  1 
ATOM   487  C CD  . ARG A 1 80  ? -3.628  18.633  -1.801  1.00 80.15  ? 80  ARG A CD  1 
ATOM   488  N NE  . ARG A 1 80  ? -4.338  17.355  -1.914  1.00 88.70  ? 80  ARG A NE  1 
ATOM   489  N N   . TYR A 1 81  ? -0.595  17.808  2.478   1.00 88.99  ? 81  TYR A N   1 
ATOM   490  C CA  . TYR A 1 81  ? -1.008  18.324  3.808   1.00 95.55  ? 81  TYR A CA  1 
ATOM   491  C C   . TYR A 1 81  ? -1.532  19.733  3.601   1.00 86.97  ? 81  TYR A C   1 
ATOM   492  O O   . TYR A 1 81  ? -0.783  20.620  3.151   1.00 81.80  ? 81  TYR A O   1 
ATOM   493  C CB  . TYR A 1 81  ? 0.149   18.332  4.812   1.00 92.60  ? 81  TYR A CB  1 
ATOM   494  C CG  . TYR A 1 81  ? 0.317   17.099  5.686   1.00 90.57  ? 81  TYR A CG  1 
ATOM   495  C CD1 . TYR A 1 81  ? -0.697  16.671  6.533   1.00 90.22  ? 81  TYR A CD1 1 
ATOM   496  C CD2 . TYR A 1 81  ? 1.504   16.380  5.679   1.00 91.04  ? 81  TYR A CD2 1 
ATOM   497  C CE1 . TYR A 1 81  ? -0.541  15.553  7.334   1.00 92.32  ? 81  TYR A CE1 1 
ATOM   498  C CE2 . TYR A 1 81  ? 1.673   15.261  6.475   1.00 99.73  ? 81  TYR A CE2 1 
ATOM   499  C CZ  . TYR A 1 81  ? 0.648   14.847  7.305   1.00 100.64 ? 81  TYR A CZ  1 
ATOM   500  O OH  . TYR A 1 81  ? 0.820   13.744  8.088   1.00 94.83  ? 81  TYR A OH  1 
ATOM   501  N N   . PRO A 1 82  ? -2.817  19.981  3.904   1.00 87.00  ? 82  PRO A N   1 
ATOM   502  C CA  . PRO A 1 82  ? -3.387  21.304  3.739   1.00 90.05  ? 82  PRO A CA  1 
ATOM   503  C C   . PRO A 1 82  ? -2.642  22.312  4.579   1.00 94.56  ? 82  PRO A C   1 
ATOM   504  O O   . PRO A 1 82  ? -1.935  21.922  5.521   1.00 101.14 ? 82  PRO A O   1 
ATOM   505  C CB  . PRO A 1 82  ? -4.814  21.102  4.239   1.00 90.60  ? 82  PRO A CB  1 
ATOM   506  C CG  . PRO A 1 82  ? -5.071  19.633  4.031   1.00 90.51  ? 82  PRO A CG  1 
ATOM   507  C CD  . PRO A 1 82  ? -3.749  18.996  4.405   1.00 93.09  ? 82  PRO A CD  1 
ATOM   508  N N   . ASP A 1 83  ? -2.808  23.596  4.264   1.00 96.65  ? 83  ASP A N   1 
ATOM   509  C CA  . ASP A 1 83  ? -2.160  24.673  5.063   1.00 101.01 ? 83  ASP A CA  1 
ATOM   510  C C   . ASP A 1 83  ? -2.737  24.634  6.480   1.00 99.91  ? 83  ASP A C   1 
ATOM   511  O O   . ASP A 1 83  ? -1.951  24.772  7.437   1.00 97.21  ? 83  ASP A O   1 
ATOM   512  C CB  . ASP A 1 83  ? -2.302  26.020  4.371   1.00 99.92  ? 83  ASP A CB  1 
ATOM   513  N N   . HIS A 1 84  ? -4.054  24.466  6.602   1.00 96.68  ? 84  HIS A N   1 
ATOM   514  C CA  . HIS A 1 84  ? -4.689  24.313  7.931   1.00 87.69  ? 84  HIS A CA  1 
ATOM   515  C C   . HIS A 1 84  ? -3.833  23.341  8.734   1.00 98.54  ? 84  HIS A C   1 
ATOM   516  O O   . HIS A 1 84  ? -3.553  23.606  9.919   1.00 98.80  ? 84  HIS A O   1 
ATOM   517  C CB  . HIS A 1 84  ? -6.090  23.732  7.775   1.00 89.29  ? 84  HIS A CB  1 
ATOM   518  N N   . MET A 1 85  ? -3.419  22.243  8.095   1.00 102.08 ? 85  MET A N   1 
ATOM   519  C CA  . MET A 1 85  ? -2.533  21.258  8.771   1.00 94.65  ? 85  MET A CA  1 
ATOM   520  C C   . MET A 1 85  ? -1.184  21.931  9.042   1.00 92.44  ? 85  MET A C   1 
ATOM   521  O O   . MET A 1 85  ? -0.348  21.967  8.122   1.00 95.80  ? 85  MET A O   1 
ATOM   522  C CB  . MET A 1 85  ? -2.349  19.998  7.924   1.00 86.82  ? 85  MET A CB  1 
ATOM   523  N N   . LYS A 1 86  ? -0.992  22.436  10.261  1.00 96.16  ? 86  LYS A N   1 
ATOM   524  C CA  . LYS A 1 86  ? 0.245   23.171  10.631  1.00 95.64  ? 86  LYS A CA  1 
ATOM   525  C C   . LYS A 1 86  ? 1.470   22.632  9.882   1.00 92.99  ? 86  LYS A C   1 
ATOM   526  O O   . LYS A 1 86  ? 2.209   23.464  9.324   1.00 105.50 ? 86  LYS A O   1 
ATOM   527  C CB  . LYS A 1 86  ? 0.472   23.091  12.144  1.00 95.51  ? 86  LYS A CB  1 
ATOM   528  N N   . GLN A 1 87  ? 1.697   21.324  9.898   1.00 82.98  ? 87  GLN A N   1 
ATOM   529  C CA  . GLN A 1 87  ? 2.930   20.797  9.269   1.00 87.03  ? 87  GLN A CA  1 
ATOM   530  C C   . GLN A 1 87  ? 4.129   21.560  9.844   1.00 84.79  ? 87  GLN A C   1 
ATOM   531  O O   . GLN A 1 87  ? 4.242   21.584  11.087  1.00 91.93  ? 87  GLN A O   1 
ATOM   532  C CB  . GLN A 1 87  ? 2.899   20.950  7.752   1.00 74.85  ? 87  GLN A CB  1 
ATOM   533  N N   . ASP A 1 89  ? 3.097   16.419  10.128  1.00 94.79  ? 89  ASP A N   1 
ATOM   534  C CA  . ASP A 1 89  ? 3.990   16.150  8.969   1.00 93.18  ? 89  ASP A CA  1 
ATOM   535  C C   . ASP A 1 89  ? 5.354   15.683  9.473   1.00 85.49  ? 89  ASP A C   1 
ATOM   536  O O   . ASP A 1 89  ? 6.358   16.373  9.207   1.00 90.10  ? 89  ASP A O   1 
ATOM   537  C CB  . ASP A 1 89  ? 4.137   17.395  8.093   1.00 91.20  ? 89  ASP A CB  1 
ATOM   538  N N   . PHE A 1 90  ? 5.387   14.548  10.160  1.00 82.37  ? 90  PHE A N   1 
ATOM   539  C CA  . PHE A 1 90  ? 6.680   13.988  10.617  1.00 88.41  ? 90  PHE A CA  1 
ATOM   540  C C   . PHE A 1 90  ? 7.400   13.470  9.398   1.00 81.47  ? 90  PHE A C   1 
ATOM   541  O O   . PHE A 1 90  ? 8.635   13.599  9.302   1.00 77.84  ? 90  PHE A O   1 
ATOM   542  C CB  . PHE A 1 90  ? 6.267   12.902  11.614  1.00 82.11  ? 90  PHE A CB  1 
ATOM   543  C CG  . PHE A 1 90  ? 7.273   11.794  11.894  1.00 85.82  ? 90  PHE A CG  1 
ATOM   544  C CD1 . PHE A 1 90  ? 7.335   10.661  11.090  1.00 85.58  ? 90  PHE A CD1 1 
ATOM   545  C CD2 . PHE A 1 90  ? 8.134   11.875  12.980  1.00 81.25  ? 90  PHE A CD2 1 
ATOM   546  C CE1 . PHE A 1 90  ? 8.249   9.656   11.353  1.00 84.75  ? 90  PHE A CE1 1 
ATOM   547  C CE2 . PHE A 1 90  ? 9.042   10.864  13.240  1.00 83.11  ? 90  PHE A CE2 1 
ATOM   548  C CZ  . PHE A 1 90  ? 9.098   9.759   12.427  1.00 86.95  ? 90  PHE A CZ  1 
ATOM   549  N N   . PHE A 1 91  ? 6.636   12.923  8.459   1.00 79.78  ? 91  PHE A N   1 
ATOM   550  C CA  . PHE A 1 91  ? 7.226   12.293  7.255   1.00 79.96  ? 91  PHE A CA  1 
ATOM   551  C C   . PHE A 1 91  ? 8.260   13.194  6.612   1.00 79.34  ? 91  PHE A C   1 
ATOM   552  O O   . PHE A 1 91  ? 9.356   12.714  6.276   1.00 81.99  ? 91  PHE A O   1 
ATOM   553  C CB  . PHE A 1 91  ? 5.989   12.031  6.402   1.00 71.56  ? 91  PHE A CB  1 
ATOM   554  C CG  . PHE A 1 91  ? 5.033   10.983  6.952   1.00 68.73  ? 91  PHE A CG  1 
ATOM   555  C CD1 . PHE A 1 91  ? 5.414   9.651   7.047   1.00 75.30  ? 91  PHE A CD1 1 
ATOM   556  C CD2 . PHE A 1 91  ? 3.754   11.331  7.365   1.00 71.51  ? 91  PHE A CD2 1 
ATOM   557  C CE1 . PHE A 1 91  ? 4.544   8.697   7.545   1.00 66.25  ? 91  PHE A CE1 1 
ATOM   558  C CE2 . PHE A 1 91  ? 2.887   10.372  7.862   1.00 76.44  ? 91  PHE A CE2 1 
ATOM   559  C CZ  . PHE A 1 91  ? 3.283   9.059   7.950   1.00 66.88  ? 91  PHE A CZ  1 
ATOM   560  N N   . LYS A 1 92  ? 7.926   14.468  6.425   1.00 82.58  ? 92  LYS A N   1 
ATOM   561  C CA  . LYS A 1 92  ? 8.855   15.394  5.730   1.00 84.82  ? 92  LYS A CA  1 
ATOM   562  C C   . LYS A 1 92  ? 9.951   15.854  6.698   1.00 87.04  ? 92  LYS A C   1 
ATOM   563  O O   . LYS A 1 92  ? 11.126  15.820  6.310   1.00 90.32  ? 92  LYS A O   1 
ATOM   564  C CB  . LYS A 1 92  ? 8.065   16.582  5.178   1.00 88.25  ? 92  LYS A CB  1 
ATOM   565  C CG  . LYS A 1 92  ? 6.720   16.234  4.565   1.00 84.96  ? 92  LYS A CG  1 
ATOM   566  C CD  . LYS A 1 92  ? 6.552   16.856  3.186   1.00 82.41  ? 92  LYS A CD  1 
ATOM   567  C CE  . LYS A 1 92  ? 5.125   16.949  2.757   1.00 97.61  ? 92  LYS A CE  1 
ATOM   568  N NZ  . LYS A 1 92  ? 4.299   15.909  3.377   1.00 97.79  ? 92  LYS A NZ  1 
ATOM   569  N N   . SER A 1 93  ? 9.575   16.247  7.912   1.00 87.02  ? 93  SER A N   1 
ATOM   570  C CA  . SER A 1 93  ? 10.556  16.743  8.911   1.00 87.94  ? 93  SER A CA  1 
ATOM   571  C C   . SER A 1 93  ? 11.765  15.811  9.004   1.00 90.67  ? 93  SER A C   1 
ATOM   572  O O   . SER A 1 93  ? 12.876  16.317  9.244   1.00 101.13 ? 93  SER A O   1 
ATOM   573  C CB  . SER A 1 93  ? 9.915   16.881  10.257  1.00 87.41  ? 93  SER A CB  1 
ATOM   574  N N   . ALA A 1 94  ? 11.553  14.510  8.842   1.00 91.29  ? 94  ALA A N   1 
ATOM   575  C CA  . ALA A 1 94  ? 12.662  13.553  9.046   1.00 93.23  ? 94  ALA A CA  1 
ATOM   576  C C   . ALA A 1 94  ? 13.364  13.273  7.729   1.00 94.69  ? 94  ALA A C   1 
ATOM   577  O O   . ALA A 1 94  ? 14.443  12.655  7.743   1.00 88.59  ? 94  ALA A O   1 
ATOM   578  C CB  . ALA A 1 94  ? 12.102  12.275  9.602   1.00 85.67  ? 94  ALA A CB  1 
ATOM   579  N N   . MET A 1 95  ? 12.765  13.716  6.628   1.00 93.02  ? 95  MET A N   1 
ATOM   580  C CA  . MET A 1 95  ? 13.333  13.343  5.308   1.00 94.53  ? 95  MET A CA  1 
ATOM   581  C C   . MET A 1 95  ? 14.715  13.959  5.069   1.00 97.96  ? 95  MET A C   1 
ATOM   582  O O   . MET A 1 95  ? 15.477  13.324  4.318   1.00 104.60 ? 95  MET A O   1 
ATOM   583  C CB  . MET A 1 95  ? 12.371  13.643  4.158   1.00 94.66  ? 95  MET A CB  1 
ATOM   584  C CG  . MET A 1 95  ? 12.159  12.414  3.316   1.00 95.52  ? 95  MET A CG  1 
ATOM   585  S SD  . MET A 1 95  ? 13.095  11.058  4.047   1.00 92.88  ? 95  MET A SD  1 
ATOM   586  C CE  . MET A 1 95  ? 11.668  10.216  4.734   1.00 83.16  ? 95  MET A CE  1 
ATOM   587  N N   . PRO A 1 96  ? 15.105  15.137  5.605   1.00 88.38  ? 96  PRO A N   1 
ATOM   588  C CA  . PRO A 1 96  ? 16.476  15.584  5.454   1.00 92.71  ? 96  PRO A CA  1 
ATOM   589  C C   . PRO A 1 96  ? 17.324  14.329  5.631   1.00 99.88  ? 96  PRO A C   1 
ATOM   590  O O   . PRO A 1 96  ? 18.297  14.164  4.872   1.00 101.74 ? 96  PRO A O   1 
ATOM   591  C CB  . PRO A 1 96  ? 16.593  16.580  6.591   1.00 97.14  ? 96  PRO A CB  1 
ATOM   592  C CG  . PRO A 1 96  ? 15.254  17.264  6.601   1.00 96.69  ? 96  PRO A CG  1 
ATOM   593  C CD  . PRO A 1 96  ? 14.283  16.160  6.231   1.00 91.98  ? 96  PRO A CD  1 
ATOM   594  N N   . GLU A 1 97  ? 16.977  13.461  6.592   1.00 102.44 ? 97  GLU A N   1 
ATOM   595  C CA  . GLU A 1 97  ? 17.671  12.157  6.763   1.00 97.92  ? 97  GLU A CA  1 
ATOM   596  C C   . GLU A 1 97  ? 16.701  11.007  6.402   1.00 101.87 ? 97  GLU A C   1 
ATOM   597  O O   . GLU A 1 97  ? 16.452  10.823  5.196   1.00 105.46 ? 97  GLU A O   1 
ATOM   598  C CB  . GLU A 1 97  ? 18.200  12.111  8.194   1.00 95.27  ? 97  GLU A CB  1 
ATOM   599  N N   . GLY A 1 98  ? 16.162  10.275  7.387   1.00 82.80  ? 98  GLY A N   1 
ATOM   600  C CA  . GLY A 1 98  ? 15.280  9.126   7.093   1.00 82.47  ? 98  GLY A CA  1 
ATOM   601  C C   . GLY A 1 98  ? 14.401  8.694   8.263   1.00 91.54  ? 98  GLY A C   1 
ATOM   602  O O   . GLY A 1 98  ? 14.807  8.936   9.415   1.00 91.70  ? 98  GLY A O   1 
ATOM   603  N N   . TYR A 1 99  ? 13.246  8.064   7.990   1.00 83.49  ? 99  TYR A N   1 
ATOM   604  C CA  . TYR A 1 99  ? 12.344  7.552   9.066   1.00 76.39  ? 99  TYR A CA  1 
ATOM   605  C C   . TYR A 1 99  ? 12.115  6.055   8.894   1.00 78.92  ? 99  TYR A C   1 
ATOM   606  O O   . TYR A 1 99  ? 12.280  5.537   7.777   1.00 75.86  ? 99  TYR A O   1 
ATOM   607  C CB  . TYR A 1 99  ? 10.976  8.237   9.159   1.00 71.99  ? 99  TYR A CB  1 
ATOM   608  C CG  . TYR A 1 99  ? 9.978   8.078   8.020   1.00 84.73  ? 99  TYR A CG  1 
ATOM   609  C CD1 . TYR A 1 99  ? 9.277   6.895   7.818   1.00 80.48  ? 99  TYR A CD1 1 
ATOM   610  C CD2 . TYR A 1 99  ? 9.686   9.145   7.184   1.00 81.40  ? 99  TYR A CD2 1 
ATOM   611  C CE1 . TYR A 1 99  ? 8.360   6.765   6.789   1.00 80.44  ? 99  TYR A CE1 1 
ATOM   612  C CE2 . TYR A 1 99  ? 8.773   9.028   6.151   1.00 79.88  ? 99  TYR A CE2 1 
ATOM   613  C CZ  . TYR A 1 99  ? 8.108   7.835   5.951   1.00 76.21  ? 99  TYR A CZ  1 
ATOM   614  O OH  . TYR A 1 99  ? 7.206   7.730   4.935   1.00 77.63  ? 99  TYR A OH  1 
ATOM   615  N N   . VAL A 1 100 ? 11.725  5.379   9.981   1.00 85.32  ? 100 VAL A N   1 
ATOM   616  C CA  . VAL A 1 100 ? 11.509  3.902   9.931   1.00 64.55  ? 100 VAL A CA  1 
ATOM   617  C C   . VAL A 1 100 ? 10.012  3.610   10.017  1.00 65.41  ? 100 VAL A C   1 
ATOM   618  O O   . VAL A 1 100 ? 9.398   4.009   11.013  1.00 71.54  ? 100 VAL A O   1 
ATOM   619  C CB  . VAL A 1 100 ? 12.264  3.128   11.023  1.00 70.75  ? 100 VAL A CB  1 
ATOM   620  C CG1 . VAL A 1 100 ? 12.109  1.622   10.858  1.00 72.37  ? 100 VAL A CG1 1 
ATOM   621  C CG2 . VAL A 1 100 ? 13.737  3.510   11.064  1.00 77.34  ? 100 VAL A CG2 1 
ATOM   622  N N   . GLN A 1 101 ? 9.471   2.944   9.002   1.00 74.66  ? 101 GLN A N   1 
ATOM   623  C CA  . GLN A 1 101 ? 8.065   2.581   8.968   1.00 64.60  ? 101 GLN A CA  1 
ATOM   624  C C   . GLN A 1 101 ? 7.954   1.080   9.209   1.00 67.46  ? 101 GLN A C   1 
ATOM   625  O O   . GLN A 1 101 ? 8.280   0.277   8.337   1.00 71.41  ? 101 GLN A O   1 
ATOM   626  C CB  . GLN A 1 101 ? 7.438   2.978   7.631   1.00 70.49  ? 101 GLN A CB  1 
ATOM   627  C CG  . GLN A 1 101 ? 5.954   2.699   7.566   1.00 65.63  ? 101 GLN A CG  1 
ATOM   628  C CD  . GLN A 1 101 ? 5.285   3.553   6.531   1.00 59.98  ? 101 GLN A CD  1 
ATOM   629  O OE1 . GLN A 1 101 ? 5.302   4.781   6.618   1.00 63.08  ? 101 GLN A OE1 1 
ATOM   630  N NE2 . GLN A 1 101 ? 4.677   2.931   5.540   1.00 60.88  ? 101 GLN A NE2 1 
ATOM   631  N N   . GLU A 1 102 ? 7.528   0.721   10.422  1.00 63.31  ? 102 GLU A N   1 
ATOM   632  C CA  . GLU A 1 102 ? 7.308   -0.667  10.782  1.00 60.93  ? 102 GLU A CA  1 
ATOM   633  C C   . GLU A 1 102 ? 5.807   -0.931  10.807  1.00 60.57  ? 102 GLU A C   1 
ATOM   634  O O   . GLU A 1 102 ? 5.041   -0.098  11.287  1.00 59.14  ? 102 GLU A O   1 
ATOM   635  C CB  . GLU A 1 102 ? 7.974   -0.962  12.126  1.00 64.83  ? 102 GLU A CB  1 
ATOM   636  C CG  . GLU A 1 102 ? 9.488   -1.011  12.013  1.00 66.67  ? 102 GLU A CG  1 
ATOM   637  C CD  . GLU A 1 102 ? 10.238  -0.747  13.300  1.00 70.67  ? 102 GLU A CD  1 
ATOM   638  O OE1 . GLU A 1 102 ? 10.094  0.370   13.847  1.00 73.37  ? 102 GLU A OE1 1 
ATOM   639  O OE2 . GLU A 1 102 ? 10.974  -1.651  13.760  1.00 73.42  ? 102 GLU A OE2 1 
ATOM   640  N N   . ARG A 1 103 ? 5.402   -2.078  10.248  1.00 51.51  ? 103 ARG A N   1 
ATOM   641  C CA  . ARG A 1 103 ? 4.013   -2.499  10.281  1.00 53.86  ? 103 ARG A CA  1 
ATOM   642  C C   . ARG A 1 103 ? 3.860   -3.981  10.598  1.00 53.78  ? 103 ARG A C   1 
ATOM   643  O O   . ARG A 1 103 ? 4.714   -4.793  10.246  1.00 42.83  ? 103 ARG A O   1 
ATOM   644  C CB  . ARG A 1 103 ? 3.294   -2.239  8.943   1.00 50.72  ? 103 ARG A CB  1 
ATOM   645  C CG  . ARG A 1 103 ? 2.789   -0.823  8.754   1.00 54.69  ? 103 ARG A CG  1 
ATOM   646  C CD  . ARG A 1 103 ? 1.645   -0.778  7.760   1.00 63.73  ? 103 ARG A CD  1 
ATOM   647  N NE  . ARG A 1 103 ? 1.375   0.578   7.291   1.00 60.62  ? 103 ARG A NE  1 
ATOM   648  C CZ  . ARG A 1 103 ? 1.666   1.025   6.075   1.00 58.07  ? 103 ARG A CZ  1 
ATOM   649  N NH1 . ARG A 1 103 ? 2.328   0.281   5.205   1.00 60.58  ? 103 ARG A NH1 1 
ATOM   650  N NH2 . ARG A 1 103 ? 1.295   2.254   5.728   1.00 66.80  ? 103 ARG A NH2 1 
ATOM   651  N N   . THR A 1 104 ? 2.742   -4.295  11.264  1.00 48.61  ? 104 THR A N   1 
ATOM   652  C CA  . THR A 1 104 ? 2.202   -5.641  11.328  1.00 46.39  ? 104 THR A CA  1 
ATOM   653  C C   . THR A 1 104 ? 0.847   -5.586  10.629  1.00 49.88  ? 104 THR A C   1 
ATOM   654  O O   . THR A 1 104 ? 0.043   -4.698  10.909  1.00 51.31  ? 104 THR A O   1 
ATOM   655  C CB  . THR A 1 104 ? 2.087   -6.118  12.772  1.00 55.50  ? 104 THR A CB  1 
ATOM   656  O OG1 . THR A 1 104 ? 3.311   -5.838  13.449  1.00 54.04  ? 104 THR A OG1 1 
ATOM   657  C CG2 . THR A 1 104 ? 1.771   -7.602  12.867  1.00 48.19  ? 104 THR A CG2 1 
ATOM   658  N N   . ILE A 1 105 ? 0.609   -6.519  9.704   1.00 52.36  ? 105 ILE A N   1 
ATOM   659  C CA  . ILE A 1 105 ? -0.659  -6.573  8.995   1.00 53.44  ? 105 ILE A CA  1 
ATOM   660  C C   . ILE A 1 105 ? -1.247  -7.964  9.208   1.00 55.02  ? 105 ILE A C   1 
ATOM   661  O O   . ILE A 1 105 ? -0.716  -8.944  8.693   1.00 58.27  ? 105 ILE A O   1 
ATOM   662  C CB  . ILE A 1 105 ? -0.519  -6.223  7.486   1.00 52.85  ? 105 ILE A CB  1 
ATOM   663  C CG1 . ILE A 1 105 ? 0.333   -4.946  7.251   1.00 53.49  ? 105 ILE A CG1 1 
ATOM   664  C CG2 . ILE A 1 105 ? -1.895  -6.098  6.843   1.00 46.88  ? 105 ILE A CG2 1 
ATOM   665  C CD1 . ILE A 1 105 ? 0.840   -4.781  5.815   1.00 45.64  ? 105 ILE A CD1 1 
ATOM   666  N N   . PHE A 1 106 ? -2.336  -8.027  9.985   1.00 55.49  ? 106 PHE A N   1 
ATOM   667  C CA  . PHE A 1 106 ? -3.015  -9.273  10.293  1.00 47.50  ? 106 PHE A CA  1 
ATOM   668  C C   . PHE A 1 106 ? -4.140  -9.498  9.292   1.00 50.02  ? 106 PHE A C   1 
ATOM   669  O O   . PHE A 1 106 ? -5.003  -8.639  9.140   1.00 61.14  ? 106 PHE A O   1 
ATOM   670  C CB  . PHE A 1 106 ? -3.601  -9.239  11.708  1.00 50.09  ? 106 PHE A CB  1 
ATOM   671  C CG  . PHE A 1 106 ? -2.607  -8.960  12.807  1.00 52.70  ? 106 PHE A CG  1 
ATOM   672  C CD1 . PHE A 1 106 ? -1.782  -9.963  13.290  1.00 54.30  ? 106 PHE A CD1 1 
ATOM   673  C CD2 . PHE A 1 106 ? -2.491  -7.691  13.350  1.00 48.29  ? 106 PHE A CD2 1 
ATOM   674  C CE1 . PHE A 1 106 ? -0.868  -9.704  14.304  1.00 44.09  ? 106 PHE A CE1 1 
ATOM   675  C CE2 . PHE A 1 106 ? -1.578  -7.432  14.362  1.00 50.17  ? 106 PHE A CE2 1 
ATOM   676  C CZ  . PHE A 1 106 ? -0.773  -8.441  14.837  1.00 51.30  ? 106 PHE A CZ  1 
ATOM   677  N N   . PHE A 1 107 ? -4.114  -10.653 8.618   1.00 54.67  ? 107 PHE A N   1 
ATOM   678  C CA  . PHE A 1 107 ? -5.175  -11.050 7.708   1.00 48.29  ? 107 PHE A CA  1 
ATOM   679  C C   . PHE A 1 107 ? -6.185  -11.942 8.425   1.00 53.52  ? 107 PHE A C   1 
ATOM   680  O O   . PHE A 1 107 ? -5.803  -12.914 9.075   1.00 56.86  ? 107 PHE A O   1 
ATOM   681  C CB  . PHE A 1 107 ? -4.578  -11.766 6.488   1.00 58.20  ? 107 PHE A CB  1 
ATOM   682  C CG  . PHE A 1 107 ? -3.781  -10.865 5.573   1.00 51.95  ? 107 PHE A CG  1 
ATOM   683  C CD1 . PHE A 1 107 ? -4.405  -10.132 4.577   1.00 59.69  ? 107 PHE A CD1 1 
ATOM   684  C CD2 . PHE A 1 107 ? -2.413  -10.732 5.725   1.00 51.57  ? 107 PHE A CD2 1 
ATOM   685  C CE1 . PHE A 1 107 ? -3.667  -9.298  3.737   1.00 50.93  ? 107 PHE A CE1 1 
ATOM   686  C CE2 . PHE A 1 107 ? -1.680  -9.900  4.889   1.00 54.17  ? 107 PHE A CE2 1 
ATOM   687  C CZ  . PHE A 1 107 ? -2.311  -9.184  3.902   1.00 54.85  ? 107 PHE A CZ  1 
ATOM   688  N N   . LYS A 1 108 ? -7.475  -11.604 8.292   1.00 57.87  ? 108 LYS A N   1 
ATOM   689  C CA  . LYS A 1 108 ? -8.542  -12.323 8.972   1.00 51.24  ? 108 LYS A CA  1 
ATOM   690  C C   . LYS A 1 108 ? -8.520  -13.791 8.550   1.00 63.85  ? 108 LYS A C   1 
ATOM   691  O O   . LYS A 1 108 ? -8.543  -14.094 7.359   1.00 57.13  ? 108 LYS A O   1 
ATOM   692  C CB  . LYS A 1 108 ? -9.909  -11.682 8.669   1.00 59.86  ? 108 LYS A CB  1 
ATOM   693  C CG  . LYS A 1 108 ? -11.017 -12.004 9.682   1.00 66.61  ? 108 LYS A CG  1 
ATOM   694  C CD  . LYS A 1 108 ? -10.927 -11.186 10.974  1.00 60.34  ? 108 LYS A CD  1 
ATOM   695  N N   . ASP A 1 109 ? -8.433  -14.686 9.545   1.00 57.94  ? 109 ASP A N   1 
ATOM   696  C CA  . ASP A 1 109 ? -8.399  -16.126 9.332   1.00 56.42  ? 109 ASP A CA  1 
ATOM   697  C C   . ASP A 1 109 ? -7.203  -16.582 8.496   1.00 59.22  ? 109 ASP A C   1 
ATOM   698  O O   . ASP A 1 109 ? -7.301  -17.558 7.755   1.00 57.84  ? 109 ASP A O   1 
ATOM   699  C CB  . ASP A 1 109 ? -9.707  -16.605 8.671   1.00 61.18  ? 109 ASP A CB  1 
ATOM   700  C CG  . ASP A 1 109 ? -10.971 -16.148 9.362   1.00 66.96  ? 109 ASP A CG  1 
ATOM   701  O OD1 . ASP A 1 109 ? -10.885 -15.708 10.526  1.00 69.46  ? 109 ASP A OD1 1 
ATOM   702  O OD2 . ASP A 1 109 ? -12.045 -16.214 8.733   1.00 74.83  ? 109 ASP A OD2 1 
ATOM   703  N N   . ASP A 1 110 ? -6.072  -15.879 8.629   1.00 56.70  ? 110 ASP A N   1 
ATOM   704  C CA  . ASP A 1 110 ? -4.856  -16.248 7.922   1.00 61.40  ? 110 ASP A CA  1 
ATOM   705  C C   . ASP A 1 110 ? -3.635  -15.675 8.644   1.00 55.13  ? 110 ASP A C   1 
ATOM   706  O O   . ASP A 1 110 ? -3.751  -15.205 9.773   1.00 52.60  ? 110 ASP A O   1 
ATOM   707  C CB  . ASP A 1 110 ? -4.932  -15.779 6.450   1.00 50.80  ? 110 ASP A CB  1 
ATOM   708  C CG  . ASP A 1 110 ? -4.221  -16.705 5.480   1.00 62.14  ? 110 ASP A CG  1 
ATOM   709  O OD1 . ASP A 1 110 ? -3.695  -17.747 5.931   1.00 66.30  ? 110 ASP A OD1 1 
ATOM   710  O OD2 . ASP A 1 110 ? -4.182  -16.387 4.275   1.00 53.59  ? 110 ASP A OD2 1 
ATOM   711  N N   . GLY A 1 111 ? -2.466  -15.735 7.994   1.00 54.32  ? 111 GLY A N   1 
ATOM   712  C CA  . GLY A 1 111 ? -1.214  -15.282 8.582   1.00 53.60  ? 111 GLY A CA  1 
ATOM   713  C C   . GLY A 1 111 ? -1.110  -13.766 8.716   1.00 57.98  ? 111 GLY A C   1 
ATOM   714  O O   . GLY A 1 111 ? -2.083  -13.053 8.464   1.00 63.08  ? 111 GLY A O   1 
ATOM   715  N N   . ASN A 1 112 ? 0.078   -13.290 9.113   1.00 55.07  ? 112 ASN A N   1 
ATOM   716  C CA  . ASN A 1 112 ? 0.339   -11.864 9.227   1.00 57.46  ? 112 ASN A CA  1 
ATOM   717  C C   . ASN A 1 112 ? 1.659   -11.466 8.570   1.00 60.94  ? 112 ASN A C   1 
ATOM   718  O O   . ASN A 1 112 ? 2.621   -12.232 8.603   1.00 58.72  ? 112 ASN A O   1 
ATOM   719  C CB  . ASN A 1 112 ? 0.340   -11.421 10.690  1.00 52.50  ? 112 ASN A CB  1 
ATOM   720  C CG  . ASN A 1 112 ? 1.458   -12.016 11.514  1.00 64.99  ? 112 ASN A CG  1 
ATOM   721  O OD1 . ASN A 1 112 ? 2.480   -11.366 11.775  1.00 68.50  ? 112 ASN A OD1 1 
ATOM   722  N ND2 . ASN A 1 112 ? 1.304   -13.264 11.929  1.00 51.35  ? 112 ASN A ND2 1 
ATOM   723  N N   . TYR A 1 113 ? 1.676   -10.267 7.964   1.00 53.75  ? 113 TYR A N   1 
ATOM   724  C CA  . TYR A 1 113 ? 2.901   -9.644  7.485   1.00 53.10  ? 113 TYR A CA  1 
ATOM   725  C C   . TYR A 1 113 ? 3.519   -8.820  8.607   1.00 44.92  ? 113 TYR A C   1 
ATOM   726  O O   . TYR A 1 113 ? 2.820   -8.062  9.273   1.00 51.37  ? 113 TYR A O   1 
ATOM   727  C CB  . TYR A 1 113 ? 2.681   -8.671  6.295   1.00 45.06  ? 113 TYR A CB  1 
ATOM   728  C CG  . TYR A 1 113 ? 2.296   -9.266  4.959   1.00 43.83  ? 113 TYR A CG  1 
ATOM   729  C CD1 . TYR A 1 113 ? 2.375   -10.631 4.729   1.00 41.02  ? 113 TYR A CD1 1 
ATOM   730  C CD2 . TYR A 1 113 ? 1.852   -8.458  3.921   1.00 49.61  ? 113 TYR A CD2 1 
ATOM   731  C CE1 . TYR A 1 113 ? 2.020   -11.178 3.500   1.00 46.76  ? 113 TYR A CE1 1 
ATOM   732  C CE2 . TYR A 1 113 ? 1.496   -8.992  2.689   1.00 40.79  ? 113 TYR A CE2 1 
ATOM   733  C CZ  . TYR A 1 113 ? 1.575   -10.354 2.483   1.00 46.13  ? 113 TYR A CZ  1 
ATOM   734  O OH  . TYR A 1 113 ? 1.208   -10.883 1.268   1.00 50.65  ? 113 TYR A OH  1 
ATOM   735  N N   . LYS A 1 114 ? 4.836   -8.966  8.775   1.00 50.03  ? 114 LYS A N   1 
ATOM   736  C CA  . LYS A 1 114 ? 5.626   -8.063  9.593   1.00 54.96  ? 114 LYS A CA  1 
ATOM   737  C C   . LYS A 1 114 ? 6.631   -7.379  8.675   1.00 51.38  ? 114 LYS A C   1 
ATOM   738  O O   . LYS A 1 114 ? 7.303   -8.037  7.884   1.00 49.24  ? 114 LYS A O   1 
ATOM   739  C CB  . LYS A 1 114 ? 6.309   -8.804  10.749  1.00 48.74  ? 114 LYS A CB  1 
ATOM   740  C CG  . LYS A 1 114 ? 5.423   -8.884  11.987  1.00 53.63  ? 114 LYS A CG  1 
ATOM   741  C CD  . LYS A 1 114 ? 5.630   -10.156 12.806  1.00 52.51  ? 114 LYS A CD  1 
ATOM   742  C CE  . LYS A 1 114 ? 4.632   -10.261 13.933  1.00 51.10  ? 114 LYS A CE  1 
ATOM   743  N NZ  . LYS A 1 114 ? 4.473   -11.667 14.408  1.00 75.74  ? 114 LYS A NZ  1 
ATOM   744  N N   . THR A 1 115 ? 6.712   -6.052  8.805   1.00 47.71  ? 115 THR A N   1 
ATOM   745  C CA  . THR A 1 115 ? 7.363   -5.207  7.820   1.00 49.06  ? 115 THR A CA  1 
ATOM   746  C C   . THR A 1 115 ? 8.231   -4.147  8.489   1.00 55.15  ? 115 THR A C   1 
ATOM   747  O O   . THR A 1 115 ? 7.798   -3.510  9.446   1.00 58.72  ? 115 THR A O   1 
ATOM   748  C CB  . THR A 1 115 ? 6.270   -4.630  6.922   1.00 49.93  ? 115 THR A CB  1 
ATOM   749  O OG1 . THR A 1 115 ? 6.256   -5.400  5.720   1.00 51.79  ? 115 THR A OG1 1 
ATOM   750  C CG2 . THR A 1 115 ? 6.466   -3.157  6.601   1.00 57.25  ? 115 THR A CG2 1 
ATOM   751  N N   . ARG A 1 116 ? 9.453   -3.980  7.968   1.00 54.76  ? 116 ARG A N   1 
ATOM   752  C CA  . ARG A 1 116 ? 10.362  -2.934  8.410   1.00 61.79  ? 116 ARG A CA  1 
ATOM   753  C C   . ARG A 1 116 ? 10.851  -2.151  7.194   1.00 58.24  ? 116 ARG A C   1 
ATOM   754  O O   . ARG A 1 116 ? 11.410  -2.737  6.267   1.00 54.55  ? 116 ARG A O   1 
ATOM   755  C CB  . ARG A 1 116 ? 11.556  -3.532  9.158   1.00 54.04  ? 116 ARG A CB  1 
ATOM   756  C CG  . ARG A 1 116 ? 12.471  -2.494  9.798   1.00 63.12  ? 116 ARG A CG  1 
ATOM   757  C CD  . ARG A 1 116 ? 13.651  -3.149  10.502  1.00 60.98  ? 116 ARG A CD  1 
ATOM   758  N NE  . ARG A 1 116 ? 14.321  -2.220  11.404  1.00 62.02  ? 116 ARG A NE  1 
ATOM   759  C CZ  . ARG A 1 116 ? 15.057  -1.186  11.014  1.00 74.02  ? 116 ARG A CZ  1 
ATOM   760  N NH1 . ARG A 1 116 ? 15.547  -1.109  9.788   1.00 73.38  ? 116 ARG A NH1 1 
ATOM   761  N NH2 . ARG A 1 116 ? 15.332  -0.219  11.886  1.00 84.14  ? 116 ARG A NH2 1 
ATOM   762  N N   . ALA A 1 117 ? 10.650  -0.828  7.224   1.00 56.73  ? 117 ALA A N   1 
ATOM   763  C CA  . ALA A 1 117 ? 10.996  0.032   6.104   1.00 65.94  ? 117 ALA A CA  1 
ATOM   764  C C   . ALA A 1 117 ? 11.886  1.201   6.519   1.00 67.74  ? 117 ALA A C   1 
ATOM   765  O O   . ALA A 1 117 ? 11.574  1.910   7.473   1.00 66.53  ? 117 ALA A O   1 
ATOM   766  C CB  . ALA A 1 117 ? 9.735   0.562   5.455   1.00 62.53  ? 117 ALA A CB  1 
ATOM   767  N N   . GLU A 1 118 ? 12.991  1.384   5.784   1.00 68.37  ? 118 GLU A N   1 
ATOM   768  C CA  . GLU A 1 118 ? 13.819  2.576   5.885   1.00 73.30  ? 118 GLU A CA  1 
ATOM   769  C C   . GLU A 1 118 ? 13.505  3.509   4.720   1.00 69.70  ? 118 GLU A C   1 
ATOM   770  O O   . GLU A 1 118 ? 13.717  3.150   3.565   1.00 68.38  ? 118 GLU A O   1 
ATOM   771  C CB  . GLU A 1 118 ? 15.313  2.220   5.880   1.00 69.21  ? 118 GLU A CB  1 
ATOM   772  C CG  . GLU A 1 118 ? 15.780  1.576   7.171   1.00 74.52  ? 118 GLU A CG  1 
ATOM   773  C CD  . GLU A 1 118 ? 17.284  1.502   7.336   1.00 84.18  ? 118 GLU A CD  1 
ATOM   774  O OE1 . GLU A 1 118 ? 18.013  1.685   6.335   1.00 90.67  ? 118 GLU A OE1 1 
ATOM   775  O OE2 . GLU A 1 118 ? 17.735  1.279   8.481   1.00 88.43  ? 118 GLU A OE2 1 
ATOM   776  N N   . VAL A 1 119 ? 12.991  4.702   5.043   1.00 74.03  ? 119 VAL A N   1 
ATOM   777  C CA  . VAL A 1 119 ? 12.655  5.700   4.041   1.00 75.23  ? 119 VAL A CA  1 
ATOM   778  C C   . VAL A 1 119 ? 13.649  6.853   4.145   1.00 79.47  ? 119 VAL A C   1 
ATOM   779  O O   . VAL A 1 119 ? 13.526  7.702   5.026   1.00 82.26  ? 119 VAL A O   1 
ATOM   780  C CB  . VAL A 1 119 ? 11.196  6.183   4.193   1.00 77.18  ? 119 VAL A CB  1 
ATOM   781  C CG1 . VAL A 1 119 ? 10.825  7.161   3.078   1.00 71.30  ? 119 VAL A CG1 1 
ATOM   782  C CG2 . VAL A 1 119 ? 10.228  5.004   4.232   1.00 62.55  ? 119 VAL A CG2 1 
ATOM   783  N N   . LYS A 1 120 ? 14.629  6.863   3.231   1.00 81.77  ? 120 LYS A N   1 
ATOM   784  C CA  . LYS A 1 120 ? 15.734  7.807   3.263   1.00 79.85  ? 120 LYS A CA  1 
ATOM   785  C C   . LYS A 1 120 ? 16.053  8.331   1.865   1.00 77.39  ? 120 LYS A C   1 
ATOM   786  O O   . LYS A 1 120 ? 16.067  7.567   0.902   1.00 78.04  ? 120 LYS A O   1 
ATOM   787  C CB  . LYS A 1 120 ? 16.992  7.147   3.874   1.00 78.70  ? 120 LYS A CB  1 
ATOM   788  C CG  . LYS A 1 120 ? 17.206  5.682   3.455   1.00 85.59  ? 120 LYS A CG  1 
ATOM   789  C CD  . LYS A 1 120 ? 18.610  5.123   3.781   1.00 79.28  ? 120 LYS A CD  1 
ATOM   790  C CE  . LYS A 1 120 ? 18.933  5.098   5.257   1.00 73.11  ? 120 LYS A CE  1 
ATOM   791  N N   . PHE A 1 121 ? 16.305  9.643   1.774   1.00 88.36  ? 121 PHE A N   1 
ATOM   792  C CA  . PHE A 1 121 ? 16.809  10.260  0.557   1.00 82.77  ? 121 PHE A CA  1 
ATOM   793  C C   . PHE A 1 121 ? 18.197  9.715   0.234   1.00 78.49  ? 121 PHE A C   1 
ATOM   794  O O   . PHE A 1 121 ? 19.128  9.894   1.013   1.00 83.95  ? 121 PHE A O   1 
ATOM   795  C CB  . PHE A 1 121 ? 16.860  11.800  0.681   1.00 80.92  ? 121 PHE A CB  1 
ATOM   796  C CG  . PHE A 1 121 ? 15.655  12.512  0.115   1.00 83.22  ? 121 PHE A CG  1 
ATOM   797  C CD1 . PHE A 1 121 ? 15.404  12.505  -1.246  1.00 81.42  ? 121 PHE A CD1 1 
ATOM   798  C CD2 . PHE A 1 121 ? 14.775  13.189  0.943   1.00 83.31  ? 121 PHE A CD2 1 
ATOM   799  C CE1 . PHE A 1 121 ? 14.294  13.161  -1.769  1.00 85.51  ? 121 PHE A CE1 1 
ATOM   800  C CE2 . PHE A 1 121 ? 13.664  13.844  0.416   1.00 87.60  ? 121 PHE A CE2 1 
ATOM   801  C CZ  . PHE A 1 121 ? 13.430  13.825  -0.936  1.00 83.59  ? 121 PHE A CZ  1 
ATOM   802  N N   . GLU A 1 122 ? 18.308  9.021   -0.904  1.00 73.08  ? 122 GLU A N   1 
ATOM   803  C CA  . GLU A 1 122 ? 19.586  8.548   -1.404  1.00 79.72  ? 122 GLU A CA  1 
ATOM   804  C C   . GLU A 1 122 ? 19.884  9.329   -2.679  1.00 88.12  ? 122 GLU A C   1 
ATOM   805  O O   . GLU A 1 122 ? 19.390  8.988   -3.752  1.00 81.77  ? 122 GLU A O   1 
ATOM   806  C CB  . GLU A 1 122 ? 19.554  7.036   -1.640  1.00 78.10  ? 122 GLU A CB  1 
ATOM   807  C CG  . GLU A 1 122 ? 19.317  6.255   -0.361  1.00 76.92  ? 122 GLU A CG  1 
ATOM   808  C CD  . GLU A 1 122 ? 19.356  4.748   -0.495  1.00 75.38  ? 122 GLU A CD  1 
ATOM   809  O OE1 . GLU A 1 122 ? 19.729  4.241   -1.578  1.00 81.49  ? 122 GLU A OE1 1 
ATOM   810  O OE2 . GLU A 1 122 ? 19.001  4.068   0.492   1.00 83.40  ? 122 GLU A OE2 1 
ATOM   811  N N   . GLY A 1 123 ? 20.682  10.395  -2.528  1.00 87.57  ? 123 GLY A N   1 
ATOM   812  C CA  . GLY A 1 123 ? 20.837  11.405  -3.561  1.00 79.14  ? 123 GLY A CA  1 
ATOM   813  C C   . GLY A 1 123 ? 19.635  12.345  -3.579  1.00 83.67  ? 123 GLY A C   1 
ATOM   814  O O   . GLY A 1 123 ? 19.262  12.888  -2.541  1.00 83.30  ? 123 GLY A O   1 
ATOM   815  N N   . ASP A 1 124 ? 19.051  12.530  -4.771  1.00 85.36  ? 124 ASP A N   1 
ATOM   816  C CA  . ASP A 1 124 ? 17.811  13.271  -4.939  1.00 84.63  ? 124 ASP A CA  1 
ATOM   817  C C   . ASP A 1 124 ? 16.607  12.332  -5.008  1.00 85.66  ? 124 ASP A C   1 
ATOM   818  O O   . ASP A 1 124 ? 15.464  12.784  -4.977  1.00 86.63  ? 124 ASP A O   1 
ATOM   819  C CB  . ASP A 1 124 ? 17.864  14.141  -6.210  1.00 89.98  ? 124 ASP A CB  1 
ATOM   820  C CG  . ASP A 1 124 ? 18.099  13.378  -7.503  1.00 93.18  ? 124 ASP A CG  1 
ATOM   821  O OD1 . ASP A 1 124 ? 18.519  12.202  -7.431  1.00 89.36  ? 124 ASP A OD1 1 
ATOM   822  O OD2 . ASP A 1 124 ? 17.849  13.952  -8.585  1.00 88.96  ? 124 ASP A OD2 1 
ATOM   823  N N   . THR A 1 125 ? 16.884  11.026  -5.117  1.00 83.64  ? 125 THR A N   1 
ATOM   824  C CA  . THR A 1 125 ? 15.853  10.009  -5.235  1.00 85.67  ? 125 THR A CA  1 
ATOM   825  C C   . THR A 1 125 ? 15.446  9.480   -3.861  1.00 81.82  ? 125 THR A C   1 
ATOM   826  O O   . THR A 1 125 ? 16.294  9.034   -3.091  1.00 82.03  ? 125 THR A O   1 
ATOM   827  C CB  . THR A 1 125 ? 16.360  8.873   -6.138  1.00 88.27  ? 125 THR A CB  1 
ATOM   828  O OG1 . THR A 1 125 ? 17.560  8.335   -5.578  1.00 88.64  ? 125 THR A OG1 1 
ATOM   829  C CG2 . THR A 1 125 ? 16.635  9.332   -7.565  1.00 73.49  ? 125 THR A CG2 1 
ATOM   830  N N   . LEU A 1 126 ? 14.141  9.527   -3.568  1.00 82.77  ? 126 LEU A N   1 
ATOM   831  C CA  . LEU A 1 126 ? 13.607  9.003   -2.321  1.00 76.66  ? 126 LEU A CA  1 
ATOM   832  C C   . LEU A 1 126 ? 13.501  7.484   -2.434  1.00 72.26  ? 126 LEU A C   1 
ATOM   833  O O   . LEU A 1 126 ? 12.781  6.976   -3.291  1.00 66.04  ? 126 LEU A O   1 
ATOM   834  C CB  . LEU A 1 126 ? 12.239  9.634   -2.020  1.00 70.05  ? 126 LEU A CB  1 
ATOM   835  C CG  . LEU A 1 126 ? 11.665  9.415   -0.617  1.00 81.99  ? 126 LEU A CG  1 
ATOM   836  C CD1 . LEU A 1 126 ? 11.289  7.958   -0.373  1.00 85.84  ? 126 LEU A CD1 1 
ATOM   837  C CD2 . LEU A 1 126 ? 12.627  9.886   0.451   1.00 75.55  ? 126 LEU A CD2 1 
ATOM   838  N N   . VAL A 1 127 ? 14.228  6.780   -1.554  1.00 64.34  ? 127 VAL A N   1 
ATOM   839  C CA  . VAL A 1 127 ? 14.363  5.334   -1.616  1.00 65.44  ? 127 VAL A CA  1 
ATOM   840  C C   . VAL A 1 127 ? 13.697  4.649   -0.423  1.00 76.78  ? 127 VAL A C   1 
ATOM   841  O O   . VAL A 1 127 ? 14.113  4.847   0.719   1.00 72.86  ? 127 VAL A O   1 
ATOM   842  C CB  . VAL A 1 127 ? 15.858  4.941   -1.698  1.00 69.62  ? 127 VAL A CB  1 
ATOM   843  N N   . ASN A 1 128 ? 12.665  3.841   -0.707  1.00 70.57  ? 128 ASN A N   1 
ATOM   844  C CA  . ASN A 1 128 ? 12.002  3.017   0.292   1.00 55.88  ? 128 ASN A CA  1 
ATOM   845  C C   . ASN A 1 128 ? 12.570  1.599   0.273   1.00 60.93  ? 128 ASN A C   1 
ATOM   846  O O   . ASN A 1 128 ? 12.376  0.871   -0.696  1.00 65.93  ? 128 ASN A O   1 
ATOM   847  C CB  . ASN A 1 128 ? 10.495  2.974   0.019   1.00 56.15  ? 128 ASN A CB  1 
ATOM   848  C CG  . ASN A 1 128 ? 9.673   2.353   1.125   1.00 62.21  ? 128 ASN A CG  1 
ATOM   849  O OD1 . ASN A 1 128 ? 10.109  2.231   2.273   1.00 67.29  ? 128 ASN A OD1 1 
ATOM   850  N ND2 . ASN A 1 128 ? 8.443   1.961   0.809   1.00 57.78  ? 128 ASN A ND2 1 
ATOM   851  N N   . ARG A 1 129 ? 13.252  1.207   1.357   1.00 64.61  ? 129 ARG A N   1 
ATOM   852  C CA  . ARG A 1 129 ? 13.934  -0.078  1.429   1.00 64.67  ? 129 ARG A CA  1 
ATOM   853  C C   . ARG A 1 129 ? 13.267  -0.985  2.464   1.00 61.19  ? 129 ARG A C   1 
ATOM   854  O O   . ARG A 1 129 ? 13.314  -0.701  3.659   1.00 61.04  ? 129 ARG A O   1 
ATOM   855  C CB  . ARG A 1 129 ? 15.418  0.140   1.767   1.00 60.40  ? 129 ARG A CB  1 
ATOM   856  C CG  . ARG A 1 129 ? 16.013  1.349   1.057   1.00 70.23  ? 129 ARG A CG  1 
ATOM   857  C CD  . ARG A 1 129 ? 17.498  1.503   1.295   1.00 76.05  ? 129 ARG A CD  1 
ATOM   858  N NE  . ARG A 1 129 ? 18.267  0.446   0.649   1.00 80.92  ? 129 ARG A NE  1 
ATOM   859  C CZ  . ARG A 1 129 ? 18.940  0.585   -0.488  1.00 85.66  ? 129 ARG A CZ  1 
ATOM   860  N NH1 . ARG A 1 129 ? 18.764  1.636   -1.274  1.00 81.31  ? 129 ARG A NH1 1 
ATOM   861  N NH2 . ARG A 1 129 ? 19.793  -0.367  -0.859  1.00 92.09  ? 129 ARG A NH2 1 
ATOM   862  N N   . ILE A 1 130 ? 12.662  -2.082  1.988   1.00 58.81  ? 130 ILE A N   1 
ATOM   863  C CA  . ILE A 1 130 ? 11.772  -2.904  2.794   1.00 46.66  ? 130 ILE A CA  1 
ATOM   864  C C   . ILE A 1 130 ? 12.317  -4.300  3.078   1.00 55.04  ? 130 ILE A C   1 
ATOM   865  O O   . ILE A 1 130 ? 12.772  -4.990  2.167   1.00 48.30  ? 130 ILE A O   1 
ATOM   866  C CB  . ILE A 1 130 ? 10.404  -3.081  2.087   1.00 51.67  ? 130 ILE A CB  1 
ATOM   867  C CG1 . ILE A 1 130 ? 9.883   -1.776  1.462   1.00 58.44  ? 130 ILE A CG1 1 
ATOM   868  C CG2 . ILE A 1 130 ? 9.383   -3.691  3.031   1.00 49.22  ? 130 ILE A CG2 1 
ATOM   869  C CD1 . ILE A 1 130 ? 9.785   -0.704  2.385   1.00 66.62  ? 130 ILE A CD1 1 
ATOM   870  N N   . GLU A 1 131 ? 12.201  -4.730  4.339   1.00 41.70  ? 131 GLU A N   1 
ATOM   871  C CA  . GLU A 1 131 ? 12.255  -6.145  4.669   1.00 53.27  ? 131 GLU A CA  1 
ATOM   872  C C   . GLU A 1 131 ? 10.848  -6.598  5.052   1.00 54.12  ? 131 GLU A C   1 
ATOM   873  O O   . GLU A 1 131 ? 10.157  -5.911  5.803   1.00 55.05  ? 131 GLU A O   1 
ATOM   874  C CB  . GLU A 1 131 ? 13.259  -6.417  5.799   1.00 52.17  ? 131 GLU A CB  1 
ATOM   875  C CG  . GLU A 1 131 ? 14.690  -6.063  5.420   1.00 71.90  ? 131 GLU A CG  1 
ATOM   876  C CD  . GLU A 1 131 ? 15.734  -6.415  6.464   1.00 84.10  ? 131 GLU A CD  1 
ATOM   877  O OE1 . GLU A 1 131 ? 15.593  -5.956  7.621   1.00 73.18  ? 131 GLU A OE1 1 
ATOM   878  O OE2 . GLU A 1 131 ? 16.697  -7.142  6.125   1.00 84.39  ? 131 GLU A OE2 1 
ATOM   879  N N   . LEU A 1 132 ? 10.433  -7.757  4.530   1.00 52.56  ? 132 LEU A N   1 
ATOM   880  C CA  . LEU A 1 132 ? 9.103   -8.284  4.789   1.00 48.43  ? 132 LEU A CA  1 
ATOM   881  C C   . LEU A 1 132 ? 9.160   -9.766  5.145   1.00 53.67  ? 132 LEU A C   1 
ATOM   882  O O   . LEU A 1 132 ? 9.705   -10.571 4.387   1.00 50.06  ? 132 LEU A O   1 
ATOM   883  C CB  . LEU A 1 132 ? 8.200   -8.054  3.564   1.00 56.59  ? 132 LEU A CB  1 
ATOM   884  C CG  . LEU A 1 132 ? 6.731   -8.465  3.715   1.00 49.64  ? 132 LEU A CG  1 
ATOM   885  C CD1 . LEU A 1 132 ? 5.846   -7.694  2.752   1.00 40.00  ? 132 LEU A CD1 1 
ATOM   886  C CD2 . LEU A 1 132 ? 6.535   -9.959  3.481   1.00 46.25  ? 132 LEU A CD2 1 
ATOM   887  N N   . LYS A 1 133 ? 8.577   -10.095 6.307   1.00 51.94  ? 133 LYS A N   1 
ATOM   888  C CA  . LYS A 1 133 ? 8.416   -11.467 6.761   1.00 50.47  ? 133 LYS A CA  1 
ATOM   889  C C   . LYS A 1 133 ? 6.931   -11.778 6.932   1.00 49.01  ? 133 LYS A C   1 
ATOM   890  O O   . LYS A 1 133 ? 6.198   -11.012 7.557   1.00 52.67  ? 133 LYS A O   1 
ATOM   891  C CB  . LYS A 1 133 ? 9.171   -11.703 8.091   1.00 52.34  ? 133 LYS A CB  1 
ATOM   892  N N   . GLY A 1 134 ? 6.500   -12.915 6.374   1.00 49.55  ? 134 GLY A N   1 
ATOM   893  C CA  . GLY A 1 134 ? 5.132   -13.383 6.529   1.00 55.25  ? 134 GLY A CA  1 
ATOM   894  C C   . GLY A 1 134 ? 5.066   -14.818 7.046   1.00 58.86  ? 134 GLY A C   1 
ATOM   895  O O   . GLY A 1 134 ? 5.611   -15.723 6.420   1.00 63.40  ? 134 GLY A O   1 
ATOM   896  N N   . ILE A 1 135 ? 4.387   -15.010 8.184   1.00 53.92  ? 135 ILE A N   1 
ATOM   897  C CA  . ILE A 1 135 ? 4.207   -16.329 8.774   1.00 65.28  ? 135 ILE A CA  1 
ATOM   898  C C   . ILE A 1 135 ? 2.731   -16.668 8.968   1.00 59.36  ? 135 ILE A C   1 
ATOM   899  O O   . ILE A 1 135 ? 1.879   -15.788 8.908   1.00 62.15  ? 135 ILE A O   1 
ATOM   900  C CB  . ILE A 1 135 ? 4.956   -16.445 10.126  1.00 63.99  ? 135 ILE A CB  1 
ATOM   901  C CG1 . ILE A 1 135 ? 4.483   -15.360 11.125  1.00 59.25  ? 135 ILE A CG1 1 
ATOM   902  C CG2 . ILE A 1 135 ? 6.469   -16.411 9.909   1.00 60.24  ? 135 ILE A CG2 1 
ATOM   903  C CD1 . ILE A 1 135 ? 4.954   -15.555 12.505  1.00 63.61  ? 135 ILE A CD1 1 
ATOM   904  N N   . ASP A 1 136 ? 2.463   -17.958 9.213   1.00 69.27  ? 136 ASP A N   1 
ATOM   905  C CA  . ASP A 1 136 ? 1.154   -18.458 9.604   1.00 59.23  ? 136 ASP A CA  1 
ATOM   906  C C   . ASP A 1 136 ? 0.118   -18.354 8.488   1.00 64.03  ? 136 ASP A C   1 
ATOM   907  O O   . ASP A 1 136 ? -1.078  -18.308 8.757   1.00 65.53  ? 136 ASP A O   1 
ATOM   908  C CB  . ASP A 1 136 ? 0.644   -17.725 10.865  1.00 64.43  ? 136 ASP A CB  1 
ATOM   909  C CG  . ASP A 1 136 ? 1.480   -17.942 12.107  1.00 63.90  ? 136 ASP A CG  1 
ATOM   910  O OD1 . ASP A 1 136 ? 2.323   -18.862 12.102  1.00 67.13  ? 136 ASP A OD1 1 
ATOM   911  O OD2 . ASP A 1 136 ? 1.295   -17.187 13.082  1.00 63.16  ? 136 ASP A OD2 1 
ATOM   912  N N   . PHE A 1 137 ? 0.577   -18.335 7.233   1.00 63.15  ? 137 PHE A N   1 
ATOM   913  C CA  . PHE A 1 137 ? -0.331  -18.239 6.103   1.00 68.50  ? 137 PHE A CA  1 
ATOM   914  C C   . PHE A 1 137 ? -0.762  -19.634 5.661   1.00 66.70  ? 137 PHE A C   1 
ATOM   915  O O   . PHE A 1 137 ? 0.008   -20.586 5.766   1.00 61.88  ? 137 PHE A O   1 
ATOM   916  C CB  . PHE A 1 137 ? 0.306   -17.453 4.953   1.00 63.65  ? 137 PHE A CB  1 
ATOM   917  C CG  . PHE A 1 137 ? 0.345   -15.967 5.199   1.00 59.73  ? 137 PHE A CG  1 
ATOM   918  C CD1 . PHE A 1 137 ? -0.787  -15.189 5.026   1.00 62.90  ? 137 PHE A CD1 1 
ATOM   919  C CD2 . PHE A 1 137 ? 1.508   -15.347 5.621   1.00 59.47  ? 137 PHE A CD2 1 
ATOM   920  C CE1 . PHE A 1 137 ? -0.750  -13.819 5.259   1.00 54.64  ? 137 PHE A CE1 1 
ATOM   921  C CE2 . PHE A 1 137 ? 1.539   -13.978 5.853   1.00 60.33  ? 137 PHE A CE2 1 
ATOM   922  C CZ  . PHE A 1 137 ? 0.412   -13.223 5.669   1.00 59.45  ? 137 PHE A CZ  1 
ATOM   923  N N   . LYS A 1 138 ? -2.007  -19.729 5.177   1.00 68.14  ? 138 LYS A N   1 
ATOM   924  C CA  . LYS A 1 138 ? -2.594  -20.989 4.750   1.00 64.01  ? 138 LYS A CA  1 
ATOM   925  C C   . LYS A 1 138 ? -2.402  -21.176 3.248   1.00 68.35  ? 138 LYS A C   1 
ATOM   926  O O   . LYS A 1 138 ? -2.996  -20.453 2.450   1.00 75.77  ? 138 LYS A O   1 
ATOM   927  C CB  . LYS A 1 138 ? -4.095  -21.031 5.105   1.00 60.53  ? 138 LYS A CB  1 
ATOM   928  N N   . GLU A 1 139 ? -1.553  -22.140 2.869   1.00 71.80  ? 139 GLU A N   1 
ATOM   929  C CA  . GLU A 1 139 ? -1.435  -22.552 1.479   1.00 76.15  ? 139 GLU A CA  1 
ATOM   930  C C   . GLU A 1 139 ? -2.812  -23.001 0.998   1.00 79.17  ? 139 GLU A C   1 
ATOM   931  O O   . GLU A 1 139 ? -3.509  -23.723 1.707   1.00 86.12  ? 139 GLU A O   1 
ATOM   932  C CB  . GLU A 1 139 ? -0.413  -23.688 1.315   1.00 75.78  ? 139 GLU A CB  1 
ATOM   933  C CG  . GLU A 1 139 ? 1.035   -23.250 1.445   1.00 84.28  ? 139 GLU A CG  1 
ATOM   934  C CD  . GLU A 1 139 ? 1.669   -22.632 0.210   1.00 85.37  ? 139 GLU A CD  1 
ATOM   935  O OE1 . GLU A 1 139 ? 1.043   -22.646 -0.874  1.00 89.49  ? 139 GLU A OE1 1 
ATOM   936  O OE2 . GLU A 1 139 ? 2.808   -22.127 0.336   1.00 78.21  ? 139 GLU A OE2 1 
ATOM   937  N N   . ASP A 1 140 ? -3.200  -22.543 -0.198  1.00 71.00  ? 140 ASP A N   1 
ATOM   938  C CA  . ASP A 1 140 ? -4.537  -22.771 -0.727  1.00 80.16  ? 140 ASP A CA  1 
ATOM   939  C C   . ASP A 1 140 ? -5.581  -21.878 -0.054  1.00 82.97  ? 140 ASP A C   1 
ATOM   940  O O   . ASP A 1 140 ? -6.757  -21.924 -0.410  1.00 94.00  ? 140 ASP A O   1 
ATOM   941  C CB  . ASP A 1 140 ? -4.937  -24.256 -0.605  1.00 92.48  ? 140 ASP A CB  1 
ATOM   942  N N   . GLY A 1 141 ? -5.142  -21.059 0.911   1.00 75.72  ? 141 GLY A N   1 
ATOM   943  C CA  . GLY A 1 141 ? -5.954  -19.976 1.436   1.00 62.44  ? 141 GLY A CA  1 
ATOM   944  C C   . GLY A 1 141 ? -6.077  -18.851 0.410   1.00 72.66  ? 141 GLY A C   1 
ATOM   945  O O   . GLY A 1 141 ? -5.752  -19.036 -0.762  1.00 63.31  ? 141 GLY A O   1 
ATOM   946  N N   . ASN A 1 142 ? -6.545  -17.685 0.864   1.00 69.83  ? 142 ASN A N   1 
ATOM   947  C CA  . ASN A 1 142 ? -6.799  -16.561 -0.022  1.00 65.86  ? 142 ASN A CA  1 
ATOM   948  C C   . ASN A 1 142 ? -5.506  -16.022 -0.625  1.00 66.39  ? 142 ASN A C   1 
ATOM   949  O O   . ASN A 1 142 ? -5.414  -15.838 -1.837  1.00 65.48  ? 142 ASN A O   1 
ATOM   950  C CB  . ASN A 1 142 ? -7.556  -15.440 0.719   1.00 66.25  ? 142 ASN A CB  1 
ATOM   951  C CG  . ASN A 1 142 ? -9.053  -15.653 0.776   1.00 61.68  ? 142 ASN A CG  1 
ATOM   952  O OD1 . ASN A 1 142 ? -9.630  -16.433 0.018   1.00 60.31  ? 142 ASN A OD1 1 
ATOM   953  N ND2 . ASN A 1 142 ? -9.719  -14.947 1.667   1.00 58.37  ? 142 ASN A ND2 1 
ATOM   954  N N   . ILE A 1 143 ? -4.512  -15.797 0.238   1.00 61.95  ? 143 ILE A N   1 
ATOM   955  C CA  . ILE A 1 143 ? -3.296  -15.097 -0.138  1.00 58.96  ? 143 ILE A CA  1 
ATOM   956  C C   . ILE A 1 143 ? -2.353  -16.009 -0.916  1.00 58.84  ? 143 ILE A C   1 
ATOM   957  O O   . ILE A 1 143 ? -2.065  -15.750 -2.079  1.00 63.02  ? 143 ILE A O   1 
ATOM   958  C CB  . ILE A 1 143 ? -2.672  -14.500 1.137   1.00 54.69  ? 143 ILE A CB  1 
ATOM   959  C CG1 . ILE A 1 143 ? -3.667  -13.521 1.790   1.00 61.28  ? 143 ILE A CG1 1 
ATOM   960  C CG2 . ILE A 1 143 ? -1.326  -13.830 0.874   1.00 52.64  ? 143 ILE A CG2 1 
ATOM   961  C CD1 . ILE A 1 143 ? -3.335  -13.151 3.132   1.00 66.34  ? 143 ILE A CD1 1 
ATOM   962  N N   . LEU A 1 144 ? -1.893  -17.088 -0.272  1.00 71.40  ? 144 LEU A N   1 
ATOM   963  C CA  . LEU A 1 144 ? -0.974  -18.027 -0.898  1.00 64.32  ? 144 LEU A CA  1 
ATOM   964  C C   . LEU A 1 144 ? -1.641  -18.788 -2.040  1.00 64.26  ? 144 LEU A C   1 
ATOM   965  O O   . LEU A 1 144 ? -0.982  -19.140 -3.015  1.00 68.38  ? 144 LEU A O   1 
ATOM   966  C CB  . LEU A 1 144 ? -0.439  -19.015 0.146   1.00 69.61  ? 144 LEU A CB  1 
ATOM   967  C CG  . LEU A 1 144 ? 0.621   -18.462 1.090   1.00 69.36  ? 144 LEU A CG  1 
ATOM   968  C CD1 . LEU A 1 144 ? 0.991   -19.477 2.155   1.00 62.23  ? 144 LEU A CD1 1 
ATOM   969  C CD2 . LEU A 1 144 ? 1.862   -18.035 0.327   1.00 67.46  ? 144 LEU A CD2 1 
ATOM   970  N N   . GLY A 1 145 ? -2.952  -19.028 -1.910  1.00 66.06  ? 145 GLY A N   1 
ATOM   971  C CA  . GLY A 1 145 ? -3.730  -19.674 -2.955  1.00 70.96  ? 145 GLY A CA  1 
ATOM   972  C C   . GLY A 1 145 ? -4.234  -18.737 -4.053  1.00 66.48  ? 145 GLY A C   1 
ATOM   973  O O   . GLY A 1 145 ? -4.959  -19.177 -4.942  1.00 67.05  ? 145 GLY A O   1 
ATOM   974  N N   . HIS A 1 146 ? -3.850  -17.454 -3.981  1.00 65.46  ? 146 HIS A N   1 
ATOM   975  C CA  . HIS A 1 146 ? -4.120  -16.486 -5.035  1.00 62.90  ? 146 HIS A CA  1 
ATOM   976  C C   . HIS A 1 146 ? -5.597  -16.496 -5.420  1.00 59.22  ? 146 HIS A C   1 
ATOM   977  O O   . HIS A 1 146 ? -5.966  -17.016 -6.471  1.00 66.60  ? 146 HIS A O   1 
ATOM   978  C CB  . HIS A 1 146 ? -3.231  -16.758 -6.269  1.00 59.14  ? 146 HIS A CB  1 
ATOM   979  C CG  . HIS A 1 146 ? -1.793  -16.364 -6.113  1.00 63.09  ? 146 HIS A CG  1 
ATOM   980  N ND1 . HIS A 1 146 ? -1.387  -15.050 -6.243  1.00 57.31  ? 146 HIS A ND1 1 
ATOM   981  C CD2 . HIS A 1 146 ? -0.703  -17.132 -5.885  1.00 64.65  ? 146 HIS A CD2 1 
ATOM   982  C CE1 . HIS A 1 146 ? -0.073  -15.053 -6.068  1.00 62.33  ? 146 HIS A CE1 1 
ATOM   983  N NE2 . HIS A 1 146 ? 0.379   -16.290 -5.851  1.00 60.46  ? 146 HIS A NE2 1 
ATOM   984  N N   . LYS A 1 147 ? -6.429  -15.932 -4.536  1.00 65.04  ? 147 LYS A N   1 
ATOM   985  C CA  . LYS A 1 147 ? -7.870  -15.889 -4.726  1.00 55.76  ? 147 LYS A CA  1 
ATOM   986  C C   . LYS A 1 147 ? -8.413  -14.463 -4.645  1.00 68.54  ? 147 LYS A C   1 
ATOM   987  O O   . LYS A 1 147 ? -9.626  -14.266 -4.625  1.00 71.48  ? 147 LYS A O   1 
ATOM   988  C CB  . LYS A 1 147 ? -8.558  -16.773 -3.673  1.00 56.38  ? 147 LYS A CB  1 
ATOM   989  C CG  . LYS A 1 147 ? -8.054  -18.219 -3.645  1.00 66.95  ? 147 LYS A CG  1 
ATOM   990  C CD  . LYS A 1 147 ? -8.628  -19.036 -2.494  1.00 60.67  ? 147 LYS A CD  1 
ATOM   991  N N   . LEU A 1 148 ? -7.508  -13.476 -4.629  1.00 63.19  ? 148 LEU A N   1 
ATOM   992  C CA  . LEU A 1 148 ? -7.878  -12.077 -4.489  1.00 70.04  ? 148 LEU A CA  1 
ATOM   993  C C   . LEU A 1 148 ? -7.943  -11.411 -5.860  1.00 67.04  ? 148 LEU A C   1 
ATOM   994  O O   . LEU A 1 148 ? -7.242  -11.817 -6.783  1.00 66.16  ? 148 LEU A O   1 
ATOM   995  C CB  . LEU A 1 148 ? -6.864  -11.322 -3.611  1.00 60.10  ? 148 LEU A CB  1 
ATOM   996  C CG  . LEU A 1 148 ? -6.842  -11.683 -2.123  1.00 69.18  ? 148 LEU A CG  1 
ATOM   997  C CD1 . LEU A 1 148 ? -6.059  -12.954 -1.856  1.00 68.37  ? 148 LEU A CD1 1 
ATOM   998  C CD2 . LEU A 1 148 ? -6.255  -10.562 -1.301  1.00 68.36  ? 148 LEU A CD2 1 
ATOM   999  N N   . GLU A 1 149 ? -8.795  -10.387 -5.976  1.00 71.41  ? 149 GLU A N   1 
ATOM   1000 C CA  . GLU A 1 149 ? -8.870  -9.581  -7.184  1.00 68.78  ? 149 GLU A CA  1 
ATOM   1001 C C   . GLU A 1 149 ? -7.729  -8.574  -7.212  1.00 63.18  ? 149 GLU A C   1 
ATOM   1002 O O   . GLU A 1 149 ? -7.174  -8.237  -6.171  1.00 64.72  ? 149 GLU A O   1 
ATOM   1003 C CB  . GLU A 1 149 ? -10.185 -8.811  -7.276  1.00 60.37  ? 149 GLU A CB  1 
ATOM   1004 C CG  . GLU A 1 149 ? -11.389 -9.662  -7.602  1.00 71.38  ? 149 GLU A CG  1 
ATOM   1005 C CD  . GLU A 1 149 ? -12.531 -8.843  -8.166  1.00 75.21  ? 149 GLU A CD  1 
ATOM   1006 O OE1 . GLU A 1 149 ? -12.805 -7.754  -7.610  1.00 67.71  ? 149 GLU A OE1 1 
ATOM   1007 O OE2 . GLU A 1 149 ? -13.149 -9.285  -9.162  1.00 77.17  ? 149 GLU A OE2 1 
ATOM   1008 N N   . TYR A 1 150 ? -7.426  -8.076  -8.415  1.00 65.06  ? 150 TYR A N   1 
ATOM   1009 C CA  . TYR A 1 150 ? -6.342  -7.133  -8.620  1.00 55.02  ? 150 TYR A CA  1 
ATOM   1010 C C   . TYR A 1 150 ? -6.851  -5.720  -8.905  1.00 65.73  ? 150 TYR A C   1 
ATOM   1011 O O   . TYR A 1 150 ? -6.489  -4.777  -8.204  1.00 72.58  ? 150 TYR A O   1 
ATOM   1012 C CB  . TYR A 1 150 ? -5.462  -7.620  -9.770  1.00 60.70  ? 150 TYR A CB  1 
ATOM   1013 C CG  . TYR A 1 150 ? -4.348  -6.661  -10.093 1.00 57.67  ? 150 TYR A CG  1 
ATOM   1014 C CD1 . TYR A 1 150 ? -3.170  -6.660  -9.359  1.00 54.13  ? 150 TYR A CD1 1 
ATOM   1015 C CD2 . TYR A 1 150 ? -4.494  -5.711  -11.094 1.00 49.68  ? 150 TYR A CD2 1 
ATOM   1016 C CE1 . TYR A 1 150 ? -2.150  -5.763  -9.638  1.00 56.21  ? 150 TYR A CE1 1 
ATOM   1017 C CE2 . TYR A 1 150 ? -3.485  -4.805  -11.379 1.00 55.91  ? 150 TYR A CE2 1 
ATOM   1018 C CZ  . TYR A 1 150 ? -2.312  -4.836  -10.652 1.00 54.86  ? 150 TYR A CZ  1 
ATOM   1019 O OH  . TYR A 1 150 ? -1.318  -3.943  -10.942 1.00 59.98  ? 150 TYR A OH  1 
ATOM   1020 N N   . ASN A 1 151 ? -7.676  -5.585  -9.951  1.00 70.12  ? 151 ASN A N   1 
ATOM   1021 C CA  . ASN A 1 151 ? -8.132  -4.285  -10.421 1.00 75.74  ? 151 ASN A CA  1 
ATOM   1022 C C   . ASN A 1 151 ? -9.511  -3.932  -9.864  1.00 82.86  ? 151 ASN A C   1 
ATOM   1023 O O   . ASN A 1 151 ? -10.099 -4.706  -9.110  1.00 69.87  ? 151 ASN A O   1 
ATOM   1024 C CB  . ASN A 1 151 ? -8.152  -4.238  -11.969 1.00 70.35  ? 151 ASN A CB  1 
ATOM   1025 C CG  . ASN A 1 151 ? -9.295  -5.001  -12.613 1.00 88.09  ? 151 ASN A CG  1 
ATOM   1026 O OD1 . ASN A 1 151 ? -9.894  -5.906  -12.023 1.00 93.43  ? 151 ASN A OD1 1 
ATOM   1027 N ND2 . ASN A 1 151 ? -9.616  -4.662  -13.859 1.00 88.80  ? 151 ASN A ND2 1 
ATOM   1028 N N   . SER A 1 152 ? -10.021 -2.764  -10.273 1.00 85.96  ? 152 SER A N   1 
ATOM   1029 C CA  . SER A 1 152 ? -11.320 -2.268  -9.845  1.00 88.45  ? 152 SER A CA  1 
ATOM   1030 C C   . SER A 1 152 ? -12.480 -2.970  -10.552 1.00 86.24  ? 152 SER A C   1 
ATOM   1031 O O   . SER A 1 152 ? -13.303 -2.319  -11.193 1.00 86.24  ? 152 SER A O   1 
ATOM   1032 C CB  . SER A 1 152 ? -11.395 -0.762  -10.093 1.00 85.65  ? 152 SER A CB  1 
ATOM   1033 O OG  . SER A 1 152 ? -10.254 -0.100  -9.574  1.00 78.62  ? 152 SER A OG  1 
ATOM   1034 N N   . SER A 1 153 ? -12.554 -4.299  -10.402 1.00 84.13  ? 153 SER A N   1 
ATOM   1035 C CA  . SER A 1 153 ? -13.503 -5.124  -11.137 1.00 89.55  ? 153 SER A CA  1 
ATOM   1036 C C   . SER A 1 153 ? -13.384 -4.913  -12.651 1.00 90.06  ? 153 SER A C   1 
ATOM   1037 O O   . SER A 1 153 ? -13.014 -5.833  -13.378 1.00 89.43  ? 153 SER A O   1 
ATOM   1038 C CB  . SER A 1 153 ? -14.936 -4.852  -10.682 1.00 86.72  ? 153 SER A CB  1 
ATOM   1039 N N   . PHE A 1 161 ? -10.902 -2.690  -23.356 1.00 102.59 ? 161 PHE A N   1 
ATOM   1040 C CA  . PHE A 1 161 ? -11.786 -1.644  -23.874 1.00 108.98 ? 161 PHE A CA  1 
ATOM   1041 C C   . PHE A 1 161 ? -11.525 -0.331  -23.134 1.00 116.08 ? 161 PHE A C   1 
ATOM   1042 O O   . PHE A 1 161 ? -10.479 -0.178  -22.506 1.00 111.68 ? 161 PHE A O   1 
ATOM   1043 C CB  . PHE A 1 161 ? -13.257 -2.090  -23.756 1.00 103.96 ? 161 PHE A CB  1 
ATOM   1044 N N   . THR A 1 162 ? -12.473 0.613   -23.237 1.00 114.94 ? 162 THR A N   1 
ATOM   1045 C CA  . THR A 1 162 ? -12.440 1.883   -22.523 1.00 115.81 ? 162 THR A CA  1 
ATOM   1046 C C   . THR A 1 162 ? -11.247 2.740   -22.948 1.00 112.33 ? 162 THR A C   1 
ATOM   1047 O O   . THR A 1 162 ? -11.410 3.659   -23.747 1.00 113.29 ? 162 THR A O   1 
ATOM   1048 C CB  . THR A 1 162 ? -12.505 1.682   -20.989 1.00 113.25 ? 162 THR A CB  1 
ATOM   1049 O OG1 . THR A 1 162 ? -11.234 1.268   -20.490 1.00 108.45 ? 162 THR A OG1 1 
ATOM   1050 C CG2 . THR A 1 162 ? -13.575 0.675   -20.583 1.00 112.43 ? 162 THR A CG2 1 
ATOM   1051 N N   . GLU A 1 163 ? -10.054 2.435   -22.417 1.00 112.16 ? 163 GLU A N   1 
ATOM   1052 C CA  . GLU A 1 163 ? -8.855  3.190   -22.747 1.00 111.23 ? 163 GLU A CA  1 
ATOM   1053 C C   . GLU A 1 163 ? -8.483  3.044   -24.223 1.00 110.22 ? 163 GLU A C   1 
ATOM   1054 O O   . GLU A 1 163 ? -7.871  3.944   -24.795 1.00 108.00 ? 163 GLU A O   1 
ATOM   1055 C CB  . GLU A 1 163 ? -7.650  2.794   -21.859 1.00 112.51 ? 163 GLU A CB  1 
ATOM   1056 C CG  . GLU A 1 163 ? -7.204  1.337   -21.939 1.00 112.82 ? 163 GLU A CG  1 
ATOM   1057 C CD  . GLU A 1 163 ? -7.713  0.416   -20.845 1.00 115.61 ? 163 GLU A CD  1 
ATOM   1058 O OE1 . GLU A 1 163 ? -8.368  0.906   -19.898 1.00 119.97 ? 163 GLU A OE1 1 
ATOM   1059 O OE2 . GLU A 1 163 ? -7.446  -0.805  -20.934 1.00 105.38 ? 163 GLU A OE2 1 
ATOM   1060 N N   . SER A 1 164 ? -8.857  1.908   -24.828 1.00 107.45 ? 164 SER A N   1 
ATOM   1061 C CA  . SER A 1 164 ? -8.607  1.660   -26.239 1.00 106.73 ? 164 SER A CA  1 
ATOM   1062 C C   . SER A 1 164 ? -9.782  2.095   -27.113 1.00 107.65 ? 164 SER A C   1 
ATOM   1063 O O   . SER A 1 164 ? -9.735  3.159   -27.726 1.00 103.37 ? 164 SER A O   1 
ATOM   1064 C CB  . SER A 1 164 ? -8.280  0.186   -26.473 1.00 100.86 ? 164 SER A CB  1 
ATOM   1065 O OG  . SER A 1 164 ? -8.222  -0.121  -27.857 1.00 100.96 ? 164 SER A OG  1 
ATOM   1066 N N   . VAL A 1 165 ? -10.837 1.270   -27.147 1.00 108.46 ? 165 VAL A N   1 
ATOM   1067 C CA  . VAL A 1 165 ? -11.922 1.430   -28.104 1.00 105.60 ? 165 VAL A CA  1 
ATOM   1068 C C   . VAL A 1 165 ? -12.648 2.764   -27.950 1.00 105.73 ? 165 VAL A C   1 
ATOM   1069 O O   . VAL A 1 165 ? -12.975 3.406   -28.946 1.00 101.17 ? 165 VAL A O   1 
ATOM   1070 C CB  . VAL A 1 165 ? -12.924 0.259   -27.999 1.00 105.89 ? 165 VAL A CB  1 
ATOM   1071 N N   . LEU A 1 166 ? -12.886 3.174   -26.698 1.00 108.69 ? 166 LEU A N   1 
ATOM   1072 C CA  . LEU A 1 166 ? -13.635 4.388   -26.415 1.00 104.98 ? 166 LEU A CA  1 
ATOM   1073 C C   . LEU A 1 166 ? -12.722 5.612   -26.386 1.00 103.89 ? 166 LEU A C   1 
ATOM   1074 O O   . LEU A 1 166 ? -12.929 6.546   -27.156 1.00 105.17 ? 166 LEU A O   1 
ATOM   1075 C CB  . LEU A 1 166 ? -14.391 4.257   -25.082 1.00 113.99 ? 166 LEU A CB  1 
ATOM   1076 N N   . GLN A 1 167 ? -11.706 5.591   -25.511 1.00 109.21 ? 167 GLN A N   1 
ATOM   1077 C CA  . GLN A 1 167 ? -10.882 6.764   -25.257 1.00 105.34 ? 167 GLN A CA  1 
ATOM   1078 C C   . GLN A 1 167 ? -10.144 7.243   -26.505 1.00 99.89  ? 167 GLN A C   1 
ATOM   1079 O O   . GLN A 1 167 ? -10.164 8.434   -26.809 1.00 101.59 ? 167 GLN A O   1 
ATOM   1080 C CB  . GLN A 1 167 ? -9.868  6.491   -24.136 1.00 102.68 ? 167 GLN A CB  1 
ATOM   1081 N N   . SER A 1 168 ? -9.503  6.311   -27.224 1.00 98.33  ? 168 SER A N   1 
ATOM   1082 C CA  . SER A 1 168 ? -8.754  6.650   -28.425 1.00 98.94  ? 168 SER A CA  1 
ATOM   1083 C C   . SER A 1 168 ? -9.666  7.211   -29.514 1.00 96.76  ? 168 SER A C   1 
ATOM   1084 O O   . SER A 1 168 ? -9.390  8.275   -30.063 1.00 96.03  ? 168 SER A O   1 
ATOM   1085 C CB  . SER A 1 168 ? -7.983  5.443   -28.952 1.00 96.89  ? 168 SER A CB  1 
ATOM   1086 N N   . GLN A 1 169 ? -10.760 6.497   -29.804 1.00 98.61  ? 169 GLN A N   1 
ATOM   1087 C CA  . GLN A 1 169 ? -11.714 6.922   -30.816 1.00 97.23  ? 169 GLN A CA  1 
ATOM   1088 C C   . GLN A 1 169 ? -12.478 8.177   -30.394 1.00 97.42  ? 169 GLN A C   1 
ATOM   1089 O O   . GLN A 1 169 ? -12.880 8.967   -31.246 1.00 95.72  ? 169 GLN A O   1 
ATOM   1090 C CB  . GLN A 1 169 ? -12.706 5.792   -31.134 1.00 96.41  ? 169 GLN A CB  1 
ATOM   1091 N N   . ALA A 1 170 ? -12.681 8.348   -29.079 1.00 95.53  ? 170 ALA A N   1 
ATOM   1092 C CA  . ALA A 1 170 ? -13.324 9.539   -28.546 1.00 93.10  ? 170 ALA A CA  1 
ATOM   1093 C C   . ALA A 1 170 ? -12.455 10.768  -28.799 1.00 96.11  ? 170 ALA A C   1 
ATOM   1094 O O   . ALA A 1 170 ? -12.938 11.780  -29.304 1.00 98.67  ? 170 ALA A O   1 
ATOM   1095 C CB  . ALA A 1 170 ? -13.605 9.390   -27.061 1.00 90.20  ? 170 ALA A CB  1 
ATOM   1096 N N   . THR A 1 171 ? -11.169 10.656  -28.445 1.00 96.28  ? 171 THR A N   1 
ATOM   1097 C CA  . THR A 1 171 ? -10.194 11.700  -28.718 1.00 96.40  ? 171 THR A CA  1 
ATOM   1098 C C   . THR A 1 171 ? -9.994  11.890  -30.221 1.00 89.88  ? 171 THR A C   1 
ATOM   1099 O O   . THR A 1 171 ? -9.814  13.012  -30.684 1.00 86.47  ? 171 THR A O   1 
ATOM   1100 C CB  . THR A 1 171 ? -8.862  11.387  -28.015 1.00 96.26  ? 171 THR A CB  1 
ATOM   1101 N N   . GLU A 1 172 ? -10.031 10.784  -30.975 1.00 89.03  ? 172 GLU A N   1 
ATOM   1102 C CA  . GLU A 1 172 ? -9.910  10.836  -32.424 1.00 87.51  ? 172 GLU A CA  1 
ATOM   1103 C C   . GLU A 1 172 ? -10.989 11.732  -33.028 1.00 86.70  ? 172 GLU A C   1 
ATOM   1104 O O   . GLU A 1 172 ? -10.689 12.597  -33.848 1.00 94.54  ? 172 GLU A O   1 
ATOM   1105 C CB  . GLU A 1 172 ? -9.990  9.428   -33.037 1.00 89.95  ? 172 GLU A CB  1 
ATOM   1106 N N   . LEU A 1 173 ? -12.242 11.519  -32.606 1.00 86.57  ? 173 LEU A N   1 
ATOM   1107 C CA  . LEU A 1 173 ? -13.359 12.334  -33.059 1.00 87.45  ? 173 LEU A CA  1 
ATOM   1108 C C   . LEU A 1 173 ? -13.210 13.775  -32.578 1.00 87.82  ? 173 LEU A C   1 
ATOM   1109 O O   . LEU A 1 173 ? -13.541 14.709  -33.305 1.00 83.17  ? 173 LEU A O   1 
ATOM   1110 C CB  . LEU A 1 173 ? -14.688 11.756  -32.553 1.00 96.39  ? 173 LEU A CB  1 
ATOM   1111 N N   . LEU A 1 174 ? -12.704 13.941  -31.349 1.00 87.91  ? 174 LEU A N   1 
ATOM   1112 C CA  . LEU A 1 174 ? -12.494 15.257  -30.765 1.00 84.50  ? 174 LEU A CA  1 
ATOM   1113 C C   . LEU A 1 174 ? -11.702 16.183  -31.688 1.00 87.83  ? 174 LEU A C   1 
ATOM   1114 O O   . LEU A 1 174 ? -12.047 17.356  -31.821 1.00 83.58  ? 174 LEU A O   1 
ATOM   1115 C CB  . LEU A 1 174 ? -11.761 15.137  -29.424 1.00 78.44  ? 174 LEU A CB  1 
ATOM   1116 N N   . GLN A 1 175 ? -10.653 15.641  -32.325 1.00 77.36  ? 175 GLN A N   1 
ATOM   1117 C CA  . GLN A 1 175 ? -9.768  16.424  -33.174 1.00 80.82  ? 175 GLN A CA  1 
ATOM   1118 C C   . GLN A 1 175 ? -10.396 16.842  -34.503 1.00 82.97  ? 175 GLN A C   1 
ATOM   1119 O O   . GLN A 1 175 ? -10.208 17.974  -34.941 1.00 81.69  ? 175 GLN A O   1 
ATOM   1120 C CB  . GLN A 1 175 ? -8.466  15.657  -33.454 1.00 81.62  ? 175 GLN A CB  1 
ATOM   1121 C CG  . GLN A 1 175 ? -7.471  15.706  -32.306 1.00 82.41  ? 175 GLN A CG  1 
ATOM   1122 C CD  . GLN A 1 175 ? -6.105  15.232  -32.742 1.00 81.90  ? 175 GLN A CD  1 
ATOM   1123 O OE1 . GLN A 1 175 ? -5.118  15.979  -32.698 1.00 72.56  ? 175 GLN A OE1 1 
ATOM   1124 N NE2 . GLN A 1 175 ? -6.019  13.983  -33.182 1.00 76.35  ? 175 GLN A NE2 1 
ATOM   1125 N N   . LYS A 1 176 ? -11.117 15.917  -35.149 1.00 84.44  ? 176 LYS A N   1 
ATOM   1126 C CA  . LYS A 1 176 ? -11.857 16.228  -36.364 1.00 75.02  ? 176 LYS A CA  1 
ATOM   1127 C C   . LYS A 1 176 ? -12.848 17.361  -36.111 1.00 71.16  ? 176 LYS A C   1 
ATOM   1128 O O   . LYS A 1 176 ? -12.968 18.272  -36.927 1.00 79.27  ? 176 LYS A O   1 
ATOM   1129 C CB  . LYS A 1 176 ? -12.601 14.991  -36.892 1.00 78.38  ? 176 LYS A CB  1 
ATOM   1130 N N   . LYS A 1 177 ? -13.543 17.293  -34.968 1.00 74.03  ? 177 LYS A N   1 
ATOM   1131 C CA  . LYS A 1 177 ? -14.477 18.328  -34.554 1.00 78.65  ? 177 LYS A CA  1 
ATOM   1132 C C   . LYS A 1 177 ? -13.748 19.626  -34.218 1.00 71.44  ? 177 LYS A C   1 
ATOM   1133 O O   . LYS A 1 177 ? -14.215 20.708  -34.567 1.00 80.49  ? 177 LYS A O   1 
ATOM   1134 C CB  . LYS A 1 177 ? -15.303 17.862  -33.341 1.00 78.90  ? 177 LYS A CB  1 
ATOM   1135 N N   . ALA A 1 178 ? -12.599 19.504  -33.544 1.00 76.49  ? 178 ALA A N   1 
ATOM   1136 C CA  . ALA A 1 178 ? -11.775 20.651  -33.192 1.00 71.73  ? 178 ALA A CA  1 
ATOM   1137 C C   . ALA A 1 178 ? -11.155 21.308  -34.424 1.00 67.99  ? 178 ALA A C   1 
ATOM   1138 O O   . ALA A 1 178 ? -10.911 22.512  -34.427 1.00 62.76  ? 178 ALA A O   1 
ATOM   1139 C CB  . ALA A 1 178 ? -10.687 20.232  -32.222 1.00 65.61  ? 178 ALA A CB  1 
ATOM   1140 N N   . GLN A 1 179 ? -10.895 20.503  -35.461 1.00 67.84  ? 179 GLN A N   1 
ATOM   1141 C CA  . GLN A 1 179 ? -10.438 21.016  -36.741 1.00 74.45  ? 179 GLN A CA  1 
ATOM   1142 C C   . GLN A 1 179 ? -11.585 21.722  -37.463 1.00 76.85  ? 179 GLN A C   1 
ATOM   1143 O O   . GLN A 1 179 ? -11.390 22.799  -38.023 1.00 77.97  ? 179 GLN A O   1 
ATOM   1144 C CB  . GLN A 1 179 ? -9.870  19.882  -37.611 1.00 81.26  ? 179 GLN A CB  1 
ATOM   1145 C CG  . GLN A 1 179 ? -8.820  20.355  -38.610 1.00 77.66  ? 179 GLN A CG  1 
ATOM   1146 C CD  . GLN A 1 179 ? -8.253  19.220  -39.426 1.00 81.71  ? 179 GLN A CD  1 
ATOM   1147 O OE1 . GLN A 1 179 ? -8.713  18.076  -39.353 1.00 89.39  ? 179 GLN A OE1 1 
ATOM   1148 N NE2 . GLN A 1 179 ? -7.234  19.510  -40.223 1.00 79.94  ? 179 GLN A NE2 1 
ATOM   1149 N N   . LEU A 1 180 ? -12.778 21.107  -37.428 1.00 75.98  ? 180 LEU A N   1 
ATOM   1150 C CA  . LEU A 1 180 ? -13.955 21.636  -38.102 1.00 78.63  ? 180 LEU A CA  1 
ATOM   1151 C C   . LEU A 1 180 ? -14.289 23.050  -37.631 1.00 74.11  ? 180 LEU A C   1 
ATOM   1152 O O   . LEU A 1 180 ? -14.485 23.944  -38.451 1.00 76.99  ? 180 LEU A O   1 
ATOM   1153 C CB  . LEU A 1 180 ? -15.170 20.721  -37.876 1.00 83.33  ? 180 LEU A CB  1 
ATOM   1154 N N   . VAL A 1 181 ? -14.332 23.244  -36.308 1.00 74.40  ? 181 VAL A N   1 
ATOM   1155 C CA  . VAL A 1 181 ? -14.612 24.549  -35.731 1.00 72.57  ? 181 VAL A CA  1 
ATOM   1156 C C   . VAL A 1 181 ? -13.499 25.524  -36.117 1.00 72.32  ? 181 VAL A C   1 
ATOM   1157 O O   . VAL A 1 181 ? -13.777 26.615  -36.611 1.00 60.54  ? 181 VAL A O   1 
ATOM   1158 C CB  . VAL A 1 181 ? -14.811 24.448  -34.194 1.00 72.35  ? 181 VAL A CB  1 
ATOM   1159 C CG1 . VAL A 1 181 ? -14.978 25.823  -33.557 1.00 77.53  ? 181 VAL A CG1 1 
ATOM   1160 C CG2 . VAL A 1 181 ? -16.000 23.555  -33.852 1.00 54.31  ? 181 VAL A CG2 1 
ATOM   1161 N N   . SER A 1 182 ? -12.244 25.099  -35.907 1.00 65.57  ? 182 SER A N   1 
ATOM   1162 C CA  . SER A 1 182 ? -11.067 25.866  -36.291 1.00 65.53  ? 182 SER A CA  1 
ATOM   1163 C C   . SER A 1 182 ? -11.203 26.561  -37.646 1.00 67.23  ? 182 SER A C   1 
ATOM   1164 O O   . SER A 1 182 ? -10.965 27.762  -37.755 1.00 59.02  ? 182 SER A O   1 
ATOM   1165 C CB  . SER A 1 182 ? -9.838  24.959  -36.298 1.00 64.14  ? 182 SER A CB  1 
ATOM   1166 O OG  . SER A 1 182 ? -8.705  25.589  -36.875 1.00 70.41  ? 182 SER A OG  1 
ATOM   1167 N N   . PHE A 1 183 ? -11.586 25.794  -38.673 1.00 69.41  ? 183 PHE A N   1 
ATOM   1168 C CA  . PHE A 1 183 ? -11.811 26.345  -39.999 1.00 72.23  ? 183 PHE A CA  1 
ATOM   1169 C C   . PHE A 1 183 ? -12.785 27.517  -39.922 1.00 65.36  ? 183 PHE A C   1 
ATOM   1170 O O   . PHE A 1 183 ? -12.476 28.614  -40.376 1.00 67.74  ? 183 PHE A O   1 
ATOM   1171 C CB  . PHE A 1 183 ? -12.354 25.277  -40.965 1.00 74.40  ? 183 PHE A CB  1 
ATOM   1172 C CG  . PHE A 1 183 ? -11.427 24.110  -41.218 1.00 75.62  ? 183 PHE A CG  1 
ATOM   1173 C CD1 . PHE A 1 183 ? -10.149 24.312  -41.711 1.00 74.83  ? 183 PHE A CD1 1 
ATOM   1174 C CD2 . PHE A 1 183 ? -11.843 22.809  -40.981 1.00 77.16  ? 183 PHE A CD2 1 
ATOM   1175 C CE1 . PHE A 1 183 ? -9.300  23.233  -41.948 1.00 79.33  ? 183 PHE A CE1 1 
ATOM   1176 C CE2 . PHE A 1 183 ? -10.996 21.735  -41.225 1.00 70.91  ? 183 PHE A CE2 1 
ATOM   1177 C CZ  . PHE A 1 183 ? -9.730  21.953  -41.708 1.00 80.92  ? 183 PHE A CZ  1 
ATOM   1178 N N   . LYS A 1 184 ? -13.949 27.273  -39.309 1.00 67.63  ? 184 LYS A N   1 
ATOM   1179 C CA  . LYS A 1 184 ? -14.993 28.276  -39.184 1.00 59.53  ? 184 LYS A CA  1 
ATOM   1180 C C   . LYS A 1 184 ? -14.461 29.568  -38.567 1.00 64.14  ? 184 LYS A C   1 
ATOM   1181 O O   . LYS A 1 184 ? -14.692 30.646  -39.110 1.00 67.28  ? 184 LYS A O   1 
ATOM   1182 C CB  . LYS A 1 184 ? -16.162 27.730  -38.345 1.00 52.96  ? 184 LYS A CB  1 
ATOM   1183 C CG  . LYS A 1 184 ? -17.427 28.548  -38.463 1.00 72.02  ? 184 LYS A CG  1 
ATOM   1184 C CD  . LYS A 1 184 ? -18.664 27.815  -37.929 1.00 80.62  ? 184 LYS A CD  1 
ATOM   1185 C CE  . LYS A 1 184 ? -18.983 28.152  -36.495 1.00 77.40  ? 184 LYS A CE  1 
ATOM   1186 N NZ  . LYS A 1 184 ? -19.487 29.549  -36.366 1.00 78.16  ? 184 LYS A NZ  1 
ATOM   1187 N N   . ILE A 1 185 ? -13.723 29.440  -37.455 1.00 66.23  ? 185 ILE A N   1 
ATOM   1188 C CA  . ILE A 1 185 ? -13.249 30.590  -36.700 1.00 58.71  ? 185 ILE A CA  1 
ATOM   1189 C C   . ILE A 1 185 ? -12.248 31.387  -37.534 1.00 59.17  ? 185 ILE A C   1 
ATOM   1190 O O   . ILE A 1 185 ? -12.189 32.610  -37.430 1.00 63.51  ? 185 ILE A O   1 
ATOM   1191 C CB  . ILE A 1 185 ? -12.640 30.196  -35.322 1.00 69.76  ? 185 ILE A CB  1 
ATOM   1192 C CG1 . ILE A 1 185 ? -13.482 29.143  -34.582 1.00 62.60  ? 185 ILE A CG1 1 
ATOM   1193 C CG2 . ILE A 1 185 ? -12.437 31.424  -34.435 1.00 66.26  ? 185 ILE A CG2 1 
ATOM   1194 C CD1 . ILE A 1 185 ? -14.977 29.474  -34.486 1.00 66.41  ? 185 ILE A CD1 1 
ATOM   1195 N N   . GLN A 1 186 ? -11.469 30.682  -38.363 1.00 57.22  ? 186 GLN A N   1 
ATOM   1196 C CA  . GLN A 1 186 ? -10.551 31.325  -39.291 1.00 59.36  ? 186 GLN A CA  1 
ATOM   1197 C C   . GLN A 1 186 ? -11.321 32.003  -40.427 1.00 62.33  ? 186 GLN A C   1 
ATOM   1198 O O   . GLN A 1 186 ? -10.859 32.993  -40.996 1.00 59.44  ? 186 GLN A O   1 
ATOM   1199 C CB  . GLN A 1 186 ? -9.538  30.301  -39.845 1.00 59.37  ? 186 GLN A CB  1 
ATOM   1200 N N   . GLY A 1 187 ? -12.496 31.449  -40.753 1.00 62.85  ? 187 GLY A N   1 
ATOM   1201 C CA  . GLY A 1 187 ? -13.415 32.054  -41.703 1.00 63.56  ? 187 GLY A CA  1 
ATOM   1202 C C   . GLY A 1 187 ? -13.928 33.423  -41.257 1.00 60.62  ? 187 GLY A C   1 
ATOM   1203 O O   . GLY A 1 187 ? -13.865 34.387  -42.018 1.00 59.09  ? 187 GLY A O   1 
ATOM   1204 N N   . ILE A 1 188 ? -14.437 33.501  -40.021 1.00 57.79  ? 188 ILE A N   1 
ATOM   1205 C CA  . ILE A 1 188 ? -14.955 34.755  -39.499 1.00 59.08  ? 188 ILE A CA  1 
ATOM   1206 C C   . ILE A 1 188 ? -13.849 35.805  -39.565 1.00 63.57  ? 188 ILE A C   1 
ATOM   1207 O O   . ILE A 1 188 ? -14.047 36.884  -40.116 1.00 62.16  ? 188 ILE A O   1 
ATOM   1208 C CB  . ILE A 1 188 ? -15.544 34.633  -38.062 1.00 57.96  ? 188 ILE A CB  1 
ATOM   1209 C CG1 . ILE A 1 188 ? -16.801 33.720  -38.017 1.00 68.33  ? 188 ILE A CG1 1 
ATOM   1210 C CG2 . ILE A 1 188 ? -15.859 36.004  -37.467 1.00 54.59  ? 188 ILE A CG2 1 
ATOM   1211 C CD1 . ILE A 1 188 ? -16.587 32.372  -37.364 1.00 61.82  ? 188 ILE A CD1 1 
ATOM   1212 N N   . MET A 1 189 ? -12.678 35.466  -39.014 1.00 65.71  ? 189 MET A N   1 
ATOM   1213 C CA  . MET A 1 189 ? -11.568 36.401  -38.923 1.00 62.67  ? 189 MET A CA  1 
ATOM   1214 C C   . MET A 1 189 ? -11.071 36.822  -40.305 1.00 61.61  ? 189 MET A C   1 
ATOM   1215 O O   . MET A 1 189 ? -10.640 37.959  -40.493 1.00 62.48  ? 189 MET A O   1 
ATOM   1216 C CB  . MET A 1 189 ? -10.423 35.767  -38.120 1.00 59.96  ? 189 MET A CB  1 
ATOM   1217 C CG  . MET A 1 189 ? -10.764 35.525  -36.656 1.00 51.86  ? 189 MET A CG  1 
ATOM   1218 S SD  . MET A 1 189 ? -11.230 36.992  -35.705 1.00 63.85  ? 189 MET A SD  1 
ATOM   1219 C CE  . MET A 1 189 ? -10.089 38.187  -36.330 1.00 54.76  ? 189 MET A CE  1 
ATOM   1220 N N   . LYS A 1 190 ? -11.139 35.894  -41.268 1.00 60.22  ? 190 LYS A N   1 
ATOM   1221 C CA  . LYS A 1 190 ? -10.778 36.189  -42.645 1.00 65.36  ? 190 LYS A CA  1 
ATOM   1222 C C   . LYS A 1 190 ? -11.659 37.301  -43.214 1.00 67.27  ? 190 LYS A C   1 
ATOM   1223 O O   . LYS A 1 190 ? -11.158 38.214  -43.866 1.00 60.59  ? 190 LYS A O   1 
ATOM   1224 C CB  . LYS A 1 190 ? -10.881 34.922  -43.510 1.00 72.80  ? 190 LYS A CB  1 
ATOM   1225 N N   . ARG A 1 191 ? -12.968 37.225  -42.942 1.00 63.90  ? 191 ARG A N   1 
ATOM   1226 C CA  . ARG A 1 191 ? -13.913 38.244  -43.368 1.00 65.63  ? 191 ARG A CA  1 
ATOM   1227 C C   . ARG A 1 191 ? -13.637 39.596  -42.714 1.00 63.30  ? 191 ARG A C   1 
ATOM   1228 O O   . ARG A 1 191 ? -13.761 40.630  -43.366 1.00 72.14  ? 191 ARG A O   1 
ATOM   1229 C CB  . ARG A 1 191 ? -15.359 37.814  -43.047 1.00 69.26  ? 191 ARG A CB  1 
ATOM   1230 C CG  . ARG A 1 191 ? -15.831 36.566  -43.791 1.00 71.01  ? 191 ARG A CG  1 
ATOM   1231 C CD  . ARG A 1 191 ? -17.331 36.298  -43.640 1.00 70.33  ? 191 ARG A CD  1 
ATOM   1232 N NE  . ARG A 1 191 ? -17.695 35.629  -42.393 1.00 70.81  ? 191 ARG A NE  1 
ATOM   1233 C CZ  . ARG A 1 191 ? -17.944 36.239  -41.238 1.00 70.37  ? 191 ARG A CZ  1 
ATOM   1234 N NH1 . ARG A 1 191 ? -17.457 37.438  -40.963 1.00 71.67  ? 191 ARG A NH1 1 
ATOM   1235 N NH2 . ARG A 1 191 ? -18.690 35.620  -40.327 1.00 64.11  ? 191 ARG A NH2 1 
ATOM   1236 N N   . ILE A 1 192 ? -13.270 39.577  -41.427 1.00 61.29  ? 192 ILE A N   1 
ATOM   1237 C CA  . ILE A 1 192 ? -13.052 40.797  -40.665 1.00 60.81  ? 192 ILE A CA  1 
ATOM   1238 C C   . ILE A 1 192 ? -11.801 41.530  -41.151 1.00 58.76  ? 192 ILE A C   1 
ATOM   1239 O O   . ILE A 1 192 ? -11.855 42.721  -41.441 1.00 52.69  ? 192 ILE A O   1 
ATOM   1240 C CB  . ILE A 1 192 ? -12.986 40.489  -39.140 1.00 69.96  ? 192 ILE A CB  1 
ATOM   1241 C CG1 . ILE A 1 192 ? -14.292 39.843  -38.637 1.00 62.43  ? 192 ILE A CG1 1 
ATOM   1242 C CG2 . ILE A 1 192 ? -12.657 41.747  -38.327 1.00 69.59  ? 192 ILE A CG2 1 
ATOM   1243 C CD1 . ILE A 1 192 ? -14.197 39.215  -37.277 1.00 49.47  ? 192 ILE A CD1 1 
ATOM   1244 N N   . PHE A 1 193 ? -10.673 40.814  -41.233 1.00 59.58  ? 193 PHE A N   1 
ATOM   1245 C CA  . PHE A 1 193 ? -9.433  41.393  -41.734 1.00 60.36  ? 193 PHE A CA  1 
ATOM   1246 C C   . PHE A 1 193 ? -9.574  41.886  -43.171 1.00 66.03  ? 193 PHE A C   1 
ATOM   1247 O O   . PHE A 1 193 ? -8.924  42.851  -43.568 1.00 73.05  ? 193 PHE A O   1 
ATOM   1248 C CB  . PHE A 1 193 ? -8.268  40.390  -41.656 1.00 58.68  ? 193 PHE A CB  1 
ATOM   1249 C CG  . PHE A 1 193 ? -7.682  40.260  -40.277 1.00 65.42  ? 193 PHE A CG  1 
ATOM   1250 C CD1 . PHE A 1 193 ? -7.089  41.345  -39.655 1.00 57.79  ? 193 PHE A CD1 1 
ATOM   1251 C CD2 . PHE A 1 193 ? -7.744  39.059  -39.589 1.00 60.95  ? 193 PHE A CD2 1 
ATOM   1252 C CE1 . PHE A 1 193 ? -6.563  41.229  -38.375 1.00 62.27  ? 193 PHE A CE1 1 
ATOM   1253 C CE2 . PHE A 1 193 ? -7.217  38.947  -38.313 1.00 58.72  ? 193 PHE A CE2 1 
ATOM   1254 C CZ  . PHE A 1 193 ? -6.628  40.031  -37.713 1.00 58.83  ? 193 PHE A CZ  1 
ATOM   1255 N N   . MET A 1 194 ? -10.433 41.214  -43.941 1.00 64.42  ? 194 MET A N   1 
ATOM   1256 C CA  . MET A 1 194 ? -10.686 41.583  -45.323 1.00 61.95  ? 194 MET A CA  1 
ATOM   1257 C C   . MET A 1 194 ? -11.401 42.933  -45.373 1.00 60.42  ? 194 MET A C   1 
ATOM   1258 O O   . MET A 1 194 ? -11.063 43.790  -46.187 1.00 63.84  ? 194 MET A O   1 
ATOM   1259 C CB  . MET A 1 194 ? -11.498 40.458  -45.970 1.00 63.99  ? 194 MET A CB  1 
ATOM   1260 C CG  . MET A 1 194 ? -11.447 40.422  -47.463 1.00 83.84  ? 194 MET A CG  1 
ATOM   1261 S SD  . MET A 1 194 ? -11.340 38.698  -48.019 1.00 92.83  ? 194 MET A SD  1 
ATOM   1262 C CE  . MET A 1 194 ? -12.911 38.081  -47.456 1.00 89.79  ? 194 MET A CE  1 
ATOM   1263 N N   . GLY A 1 195 ? -12.374 43.124  -44.472 1.00 60.04  ? 195 GLY A N   1 
ATOM   1264 C CA  . GLY A 1 195 ? -13.047 44.405  -44.324 1.00 52.25  ? 195 GLY A CA  1 
ATOM   1265 C C   . GLY A 1 195 ? -12.108 45.510  -43.846 1.00 60.97  ? 195 GLY A C   1 
ATOM   1266 O O   . GLY A 1 195 ? -12.220 46.657  -44.277 1.00 62.98  ? 195 GLY A O   1 
ATOM   1267 N N   . ALA A 1 196 ? -11.189 45.140  -42.946 1.00 59.16  ? 196 ALA A N   1 
ATOM   1268 C CA  . ALA A 1 196 ? -10.201 46.055  -42.402 1.00 58.18  ? 196 ALA A CA  1 
ATOM   1269 C C   . ALA A 1 196 ? -9.200  46.518  -43.460 1.00 52.33  ? 196 ALA A C   1 
ATOM   1270 O O   . ALA A 1 196 ? -8.627  47.599  -43.343 1.00 56.23  ? 196 ALA A O   1 
ATOM   1271 C CB  . ALA A 1 196 ? -9.472  45.387  -41.240 1.00 58.64  ? 196 ALA A CB  1 
ATOM   1272 N N   . ASN A 1 197 ? -8.986  45.681  -44.481 1.00 56.88  ? 197 ASN A N   1 
ATOM   1273 C CA  . ASN A 1 197 ? -8.186  46.053  -45.636 1.00 61.61  ? 197 ASN A CA  1 
ATOM   1274 C C   . ASN A 1 197 ? -8.815  47.216  -46.403 1.00 61.67  ? 197 ASN A C   1 
ATOM   1275 O O   . ASN A 1 197 ? -8.133  48.185  -46.731 1.00 62.37  ? 197 ASN A O   1 
ATOM   1276 C CB  . ASN A 1 197 ? -8.000  44.844  -46.556 1.00 62.91  ? 197 ASN A CB  1 
ATOM   1277 C CG  . ASN A 1 197 ? -6.996  45.065  -47.670 1.00 69.46  ? 197 ASN A CG  1 
ATOM   1278 O OD1 . ASN A 1 197 ? -5.850  45.483  -47.442 1.00 68.23  ? 197 ASN A OD1 1 
ATOM   1279 N ND2 . ASN A 1 197 ? -7.399  44.781  -48.900 1.00 69.49  ? 197 ASN A ND2 1 
ATOM   1280 N N   . THR A 1 198 ? -10.127 47.119  -46.662 1.00 61.12  ? 198 THR A N   1 
ATOM   1281 C CA  . THR A 1 198 ? -10.825 48.115  -47.463 1.00 58.86  ? 198 THR A CA  1 
ATOM   1282 C C   . THR A 1 198 ? -10.879 49.454  -46.728 1.00 57.91  ? 198 THR A C   1 
ATOM   1283 O O   . THR A 1 198 ? -10.638 50.497  -47.328 1.00 57.10  ? 198 THR A O   1 
ATOM   1284 C CB  . THR A 1 198 ? -12.238 47.643  -47.872 1.00 68.67  ? 198 THR A CB  1 
ATOM   1285 O OG1 . THR A 1 198 ? -13.175 47.979  -46.848 1.00 70.64  ? 198 THR A OG1 1 
ATOM   1286 C CG2 . THR A 1 198 ? -12.296 46.140  -48.180 1.00 64.71  ? 198 THR A CG2 1 
ATOM   1287 N N   . LEU A 1 199 ? -11.180 49.409  -45.424 1.00 71.98  ? 199 LEU A N   1 
ATOM   1288 C CA  . LEU A 1 199 ? -11.202 50.603  -44.592 1.00 66.22  ? 199 LEU A CA  1 
ATOM   1289 C C   . LEU A 1 199 ? -9.855  51.317  -44.508 1.00 65.88  ? 199 LEU A C   1 
ATOM   1290 O O   . LEU A 1 199 ? -9.797  52.543  -44.524 1.00 62.05  ? 199 LEU A O   1 
ATOM   1291 C CB  . LEU A 1 199 ? -11.656 50.255  -43.167 1.00 68.33  ? 199 LEU A CB  1 
ATOM   1292 C CG  . LEU A 1 199 ? -13.127 50.456  -42.882 1.00 70.11  ? 199 LEU A CG  1 
ATOM   1293 C CD1 . LEU A 1 199 ? -13.418 50.234  -41.418 1.00 60.26  ? 199 LEU A CD1 1 
ATOM   1294 C CD2 . LEU A 1 199 ? -13.584 51.854  -43.312 1.00 61.25  ? 199 LEU A CD2 1 
ATOM   1295 N N   . GLU A 1 200 ? -8.776  50.538  -44.387 1.00 66.24  ? 200 GLU A N   1 
ATOM   1296 C CA  . GLU A 1 200 ? -7.434  51.093  -44.360 1.00 62.83  ? 200 GLU A CA  1 
ATOM   1297 C C   . GLU A 1 200 ? -7.197  51.950  -45.601 1.00 60.79  ? 200 GLU A C   1 
ATOM   1298 O O   . GLU A 1 200 ? -6.749  53.090  -45.494 1.00 58.59  ? 200 GLU A O   1 
ATOM   1299 C CB  . GLU A 1 200 ? -6.398  49.968  -44.287 1.00 69.54  ? 200 GLU A CB  1 
ATOM   1300 C CG  . GLU A 1 200 ? -4.957  50.444  -44.292 1.00 67.04  ? 200 GLU A CG  1 
ATOM   1301 C CD  . GLU A 1 200 ? -4.028  49.492  -45.012 1.00 81.11  ? 200 GLU A CD  1 
ATOM   1302 O OE1 . GLU A 1 200 ? -4.203  49.321  -46.241 1.00 83.36  ? 200 GLU A OE1 1 
ATOM   1303 O OE2 . GLU A 1 200 ? -3.136  48.909  -44.353 1.00 93.14  ? 200 GLU A OE2 1 
ATOM   1304 N N   . LYS A 1 201 ? -7.512  51.383  -46.772 1.00 61.80  ? 201 LYS A N   1 
ATOM   1305 C CA  . LYS A 1 201 ? -7.353  52.083  -48.038 1.00 65.79  ? 201 LYS A CA  1 
ATOM   1306 C C   . LYS A 1 201 ? -8.125  53.399  -48.024 1.00 58.21  ? 201 LYS A C   1 
ATOM   1307 O O   . LYS A 1 201 ? -7.561  54.458  -48.293 1.00 60.60  ? 201 LYS A O   1 
ATOM   1308 C CB  . LYS A 1 201 ? -7.860  51.233  -49.210 1.00 63.37  ? 201 LYS A CB  1 
ATOM   1309 C CG  . LYS A 1 201 ? -7.158  49.913  -49.426 1.00 59.37  ? 201 LYS A CG  1 
ATOM   1310 C CD  . LYS A 1 201 ? -7.942  49.060  -50.392 1.00 61.23  ? 201 LYS A CD  1 
ATOM   1311 C CE  . LYS A 1 201 ? -7.465  47.642  -50.448 1.00 73.86  ? 201 LYS A CE  1 
ATOM   1312 N NZ  . LYS A 1 201 ? -8.407  46.799  -51.230 1.00 72.22  ? 201 LYS A NZ  1 
ATOM   1313 N N   . PHE A 1 202 ? -9.424  53.302  -47.712 1.00 54.29  ? 202 PHE A N   1 
ATOM   1314 C CA  . PHE A 1 202 ? -10.299 54.457  -47.636 1.00 50.88  ? 202 PHE A CA  1 
ATOM   1315 C C   . PHE A 1 202 ? -9.765  55.491  -46.650 1.00 54.78  ? 202 PHE A C   1 
ATOM   1316 O O   . PHE A 1 202 ? -9.579  56.651  -47.007 1.00 61.24  ? 202 PHE A O   1 
ATOM   1317 C CB  . PHE A 1 202 ? -11.717 54.029  -47.225 1.00 51.74  ? 202 PHE A CB  1 
ATOM   1318 C CG  . PHE A 1 202 ? -12.621 55.194  -46.921 1.00 57.74  ? 202 PHE A CG  1 
ATOM   1319 C CD1 . PHE A 1 202 ? -13.286 55.860  -47.935 1.00 63.09  ? 202 PHE A CD1 1 
ATOM   1320 C CD2 . PHE A 1 202 ? -12.767 55.655  -45.627 1.00 57.99  ? 202 PHE A CD2 1 
ATOM   1321 C CE1 . PHE A 1 202 ? -14.109 56.948  -47.648 1.00 66.59  ? 202 PHE A CE1 1 
ATOM   1322 C CE2 . PHE A 1 202 ? -13.583 56.741  -45.345 1.00 59.01  ? 202 PHE A CE2 1 
ATOM   1323 C CZ  . PHE A 1 202 ? -14.250 57.383  -46.355 1.00 57.77  ? 202 PHE A CZ  1 
ATOM   1324 N N   . LEU A 1 203 ? -9.522  55.048  -45.410 1.00 66.23  ? 203 LEU A N   1 
ATOM   1325 C CA  . LEU A 1 203 ? -9.160  55.941  -44.319 1.00 61.96  ? 203 LEU A CA  1 
ATOM   1326 C C   . LEU A 1 203 ? -7.778  56.571  -44.478 1.00 58.39  ? 203 LEU A C   1 
ATOM   1327 O O   . LEU A 1 203 ? -7.566  57.696  -44.029 1.00 56.44  ? 203 LEU A O   1 
ATOM   1328 C CB  . LEU A 1 203 ? -9.221  55.185  -42.984 1.00 61.93  ? 203 LEU A CB  1 
ATOM   1329 C CG  . LEU A 1 203 ? -10.616 54.862  -42.474 1.00 61.67  ? 203 LEU A CG  1 
ATOM   1330 C CD1 . LEU A 1 203 ? -10.548 54.096  -41.167 1.00 59.17  ? 203 LEU A CD1 1 
ATOM   1331 C CD2 . LEU A 1 203 ? -11.440 56.128  -42.294 1.00 59.70  ? 203 LEU A CD2 1 
ATOM   1332 N N   . SER A 1 204 ? -6.854  55.846  -45.123 1.00 56.50  ? 204 SER A N   1 
ATOM   1333 C CA  . SER A 1 204 ? -5.505  56.341  -45.352 1.00 56.10  ? 204 SER A CA  1 
ATOM   1334 C C   . SER A 1 204 ? -5.446  57.422  -46.433 1.00 60.37  ? 204 SER A C   1 
ATOM   1335 O O   . SER A 1 204 ? -4.378  57.961  -46.715 1.00 50.04  ? 204 SER A O   1 
ATOM   1336 C CB  . SER A 1 204 ? -4.574  55.182  -45.702 1.00 57.30  ? 204 SER A CB  1 
ATOM   1337 O OG  . SER A 1 204 ? -5.063  54.438  -46.806 1.00 67.00  ? 204 SER A OG  1 
ATOM   1338 N N   . ASP A 1 205 ? -6.605  57.724  -47.035 1.00 60.80  ? 205 ASP A N   1 
ATOM   1339 C CA  . ASP A 1 205 ? -6.739  58.807  -47.995 1.00 60.15  ? 205 ASP A CA  1 
ATOM   1340 C C   . ASP A 1 205 ? -6.906  60.142  -47.270 1.00 63.45  ? 205 ASP A C   1 
ATOM   1341 O O   . ASP A 1 205 ? -7.959  60.408  -46.691 1.00 62.84  ? 205 ASP A O   1 
ATOM   1342 C CB  . ASP A 1 205 ? -7.940  58.520  -48.907 1.00 63.01  ? 205 ASP A CB  1 
ATOM   1343 C CG  . ASP A 1 205 ? -8.071  59.407  -50.119 1.00 59.04  ? 205 ASP A CG  1 
ATOM   1344 O OD1 . ASP A 1 205 ? -7.368  60.432  -50.184 1.00 59.76  ? 205 ASP A OD1 1 
ATOM   1345 O OD2 . ASP A 1 205 ? -8.872  59.070  -51.009 1.00 66.78  ? 205 ASP A OD2 1 
ATOM   1346 N N   . GLU A 1 206 ? -5.863  60.982  -47.333 1.00 61.86  ? 206 GLU A N   1 
ATOM   1347 C CA  . GLU A 1 206 ? -5.832  62.256  -46.631 1.00 54.63  ? 206 GLU A CA  1 
ATOM   1348 C C   . GLU A 1 206 ? -6.479  63.414  -47.391 1.00 66.74  ? 206 GLU A C   1 
ATOM   1349 O O   . GLU A 1 206 ? -6.100  64.566  -47.194 1.00 74.13  ? 206 GLU A O   1 
ATOM   1350 C CB  . GLU A 1 206 ? -4.374  62.646  -46.334 1.00 63.79  ? 206 GLU A CB  1 
ATOM   1351 C CG  . GLU A 1 206 ? -3.659  61.761  -45.336 1.00 70.28  ? 206 GLU A CG  1 
ATOM   1352 C CD  . GLU A 1 206 ? -2.352  62.362  -44.853 1.00 77.30  ? 206 GLU A CD  1 
ATOM   1353 O OE1 . GLU A 1 206 ? -1.409  62.492  -45.670 1.00 69.36  ? 206 GLU A OE1 1 
ATOM   1354 O OE2 . GLU A 1 206 ? -2.285  62.732  -43.658 1.00 75.08  ? 206 GLU A OE2 1 
ATOM   1355 N N   . ASN A 1 207 ? -7.458  63.118  -48.253 1.00 67.06  ? 207 ASN A N   1 
ATOM   1356 C CA  . ASN A 1 207 ? -8.075  64.143  -49.077 1.00 57.70  ? 207 ASN A CA  1 
ATOM   1357 C C   . ASN A 1 207 ? -9.043  64.999  -48.261 1.00 61.83  ? 207 ASN A C   1 
ATOM   1358 O O   . ASN A 1 207 ? -9.986  64.481  -47.665 1.00 61.46  ? 207 ASN A O   1 
ATOM   1359 C CB  . ASN A 1 207 ? -8.786  63.510  -50.269 1.00 66.04  ? 207 ASN A CB  1 
ATOM   1360 C CG  . ASN A 1 207 ? -9.169  64.515  -51.336 1.00 63.07  ? 207 ASN A CG  1 
ATOM   1361 O OD1 . ASN A 1 207 ? -10.007 65.405  -51.119 1.00 59.73  ? 207 ASN A OD1 1 
ATOM   1362 N ND2 . ASN A 1 207 ? -8.565  64.393  -52.515 1.00 54.45  ? 207 ASN A ND2 1 
ATOM   1363 N N   . SER A 1 208 ? -8.803  66.316  -48.275 1.00 70.03  ? 208 SER A N   1 
ATOM   1364 C CA  . SER A 1 208 ? -9.597  67.291  -47.541 1.00 62.76  ? 208 SER A CA  1 
ATOM   1365 C C   . SER A 1 208 ? -11.111 67.150  -47.677 1.00 66.64  ? 208 SER A C   1 
ATOM   1366 O O   . SER A 1 208 ? -11.834 67.337  -46.701 1.00 76.38  ? 208 SER A O   1 
ATOM   1367 C CB  . SER A 1 208 ? -9.229  68.699  -47.993 1.00 66.92  ? 208 SER A CB  1 
ATOM   1368 N N   . ALA A 1 209 ? -11.579 66.842  -48.893 1.00 59.17  ? 209 ALA A N   1 
ATOM   1369 C CA  . ALA A 1 209 ? -13.003 66.830  -49.194 1.00 60.68  ? 209 ALA A CA  1 
ATOM   1370 C C   . ALA A 1 209 ? -13.735 65.595  -48.671 1.00 58.61  ? 209 ALA A C   1 
ATOM   1371 O O   . ALA A 1 209 ? -14.966 65.564  -48.682 1.00 65.10  ? 209 ALA A O   1 
ATOM   1372 C CB  . ALA A 1 209 ? -13.215 66.949  -50.696 1.00 64.10  ? 209 ALA A CB  1 
ATOM   1373 N N   . ILE A 1 210 ? -12.979 64.578  -48.233 1.00 65.27  ? 210 ILE A N   1 
ATOM   1374 C CA  . ILE A 1 210 ? -13.563 63.413  -47.587 1.00 65.83  ? 210 ILE A CA  1 
ATOM   1375 C C   . ILE A 1 210 ? -13.947 63.806  -46.162 1.00 65.93  ? 210 ILE A C   1 
ATOM   1376 O O   . ILE A 1 210 ? -13.111 63.780  -45.259 1.00 68.76  ? 210 ILE A O   1 
ATOM   1377 C CB  . ILE A 1 210 ? -12.618 62.184  -47.621 1.00 63.99  ? 210 ILE A CB  1 
ATOM   1378 C CG1 . ILE A 1 210 ? -12.227 61.822  -49.061 1.00 63.48  ? 210 ILE A CG1 1 
ATOM   1379 C CG2 . ILE A 1 210 ? -13.245 60.980  -46.902 1.00 66.08  ? 210 ILE A CG2 1 
ATOM   1380 C CD1 . ILE A 1 210 ? -11.429 60.553  -49.196 1.00 55.66  ? 210 ILE A CD1 1 
ATOM   1381 N N   . ASN A 1 211 ? -15.220 64.180  -45.984 1.00 55.87  ? 211 ASN A N   1 
ATOM   1382 C CA  . ASN A 1 211 ? -15.737 64.586  -44.686 1.00 63.27  ? 211 ASN A CA  1 
ATOM   1383 C C   . ASN A 1 211 ? -15.810 63.421  -43.698 1.00 59.99  ? 211 ASN A C   1 
ATOM   1384 O O   . ASN A 1 211 ? -15.690 62.257  -44.079 1.00 54.89  ? 211 ASN A O   1 
ATOM   1385 C CB  . ASN A 1 211 ? -17.116 65.240  -44.832 1.00 53.93  ? 211 ASN A CB  1 
ATOM   1386 C CG  . ASN A 1 211 ? -18.059 64.461  -45.709 1.00 71.75  ? 211 ASN A CG  1 
ATOM   1387 O OD1 . ASN A 1 211 ? -17.947 64.469  -46.949 1.00 71.86  ? 211 ASN A OD1 1 
ATOM   1388 N ND2 . ASN A 1 211 ? -19.015 63.787  -45.097 1.00 62.07  ? 211 ASN A ND2 1 
ATOM   1389 N N   . ASP A 1 212 ? -16.015 63.757  -42.420 1.00 56.11  ? 212 ASP A N   1 
ATOM   1390 C CA  . ASP A 1 212 ? -16.136 62.759  -41.372 1.00 64.93  ? 212 ASP A CA  1 
ATOM   1391 C C   . ASP A 1 212 ? -17.455 61.991  -41.443 1.00 65.06  ? 212 ASP A C   1 
ATOM   1392 O O   . ASP A 1 212 ? -17.486 60.803  -41.127 1.00 65.95  ? 212 ASP A O   1 
ATOM   1393 C CB  . ASP A 1 212 ? -15.960 63.400  -39.990 1.00 59.19  ? 212 ASP A CB  1 
ATOM   1394 C CG  . ASP A 1 212 ? -14.535 63.782  -39.646 1.00 64.68  ? 212 ASP A CG  1 
ATOM   1395 O OD1 . ASP A 1 212 ? -13.617 63.482  -40.462 1.00 60.77  ? 212 ASP A OD1 1 
ATOM   1396 O OD2 . ASP A 1 212 ? -14.328 64.377  -38.566 1.00 71.23  ? 212 ASP A OD2 1 
ATOM   1397 N N   . THR A 1 213 ? -18.536 62.655  -41.873 1.00 52.42  ? 213 THR A N   1 
ATOM   1398 C CA  . THR A 1 213 ? -19.822 61.983  -41.994 1.00 51.74  ? 213 THR A CA  1 
ATOM   1399 C C   . THR A 1 213 ? -19.732 60.786  -42.939 1.00 57.42  ? 213 THR A C   1 
ATOM   1400 O O   . THR A 1 213 ? -20.457 59.809  -42.766 1.00 62.21  ? 213 THR A O   1 
ATOM   1401 C CB  . THR A 1 213 ? -20.947 62.943  -42.436 1.00 46.89  ? 213 THR A CB  1 
ATOM   1402 N N   . LEU A 1 214 ? -18.829 60.869  -43.927 1.00 58.86  ? 214 LEU A N   1 
ATOM   1403 C CA  . LEU A 1 214 ? -18.616 59.793  -44.884 1.00 58.78  ? 214 LEU A CA  1 
ATOM   1404 C C   . LEU A 1 214 ? -17.668 58.725  -44.336 1.00 59.72  ? 214 LEU A C   1 
ATOM   1405 O O   . LEU A 1 214 ? -17.778 57.550  -44.686 1.00 54.32  ? 214 LEU A O   1 
ATOM   1406 C CB  . LEU A 1 214 ? -18.065 60.380  -46.195 1.00 56.31  ? 214 LEU A CB  1 
ATOM   1407 C CG  . LEU A 1 214 ? -17.758 59.378  -47.303 1.00 54.22  ? 214 LEU A CG  1 
ATOM   1408 C CD1 . LEU A 1 214 ? -18.994 58.577  -47.679 1.00 59.91  ? 214 LEU A CD1 1 
ATOM   1409 C CD2 . LEU A 1 214 ? -17.200 60.078  -48.522 1.00 57.45  ? 214 LEU A CD2 1 
ATOM   1410 N N   . LYS A 1 215 ? -16.726 59.145  -43.483 1.00 57.96  ? 215 LYS A N   1 
ATOM   1411 C CA  . LYS A 1 215 ? -15.885 58.207  -42.758 1.00 59.30  ? 215 LYS A CA  1 
ATOM   1412 C C   . LYS A 1 215 ? -16.732 57.370  -41.802 1.00 57.05  ? 215 LYS A C   1 
ATOM   1413 O O   . LYS A 1 215 ? -16.537 56.162  -41.702 1.00 50.59  ? 215 LYS A O   1 
ATOM   1414 C CB  . LYS A 1 215 ? -14.766 58.933  -41.998 1.00 54.21  ? 215 LYS A CB  1 
ATOM   1415 C CG  . LYS A 1 215 ? -13.816 59.684  -42.897 1.00 49.51  ? 215 LYS A CG  1 
ATOM   1416 C CD  . LYS A 1 215 ? -12.550 60.107  -42.193 1.00 60.34  ? 215 LYS A CD  1 
ATOM   1417 C CE  . LYS A 1 215 ? -11.738 61.065  -43.029 1.00 63.81  ? 215 LYS A CE  1 
ATOM   1418 N NZ  . LYS A 1 215 ? -12.455 62.351  -43.235 1.00 72.88  ? 215 LYS A NZ  1 
ATOM   1419 N N   . ARG A 1 216 ? -17.699 58.015  -41.138 1.00 56.30  ? 216 ARG A N   1 
ATOM   1420 C CA  . ARG A 1 216 ? -18.594 57.321  -40.225 1.00 58.60  ? 216 ARG A CA  1 
ATOM   1421 C C   . ARG A 1 216 ? -19.385 56.227  -40.936 1.00 58.83  ? 216 ARG A C   1 
ATOM   1422 O O   . ARG A 1 216 ? -19.629 55.171  -40.354 1.00 60.95  ? 216 ARG A O   1 
ATOM   1423 C CB  . ARG A 1 216 ? -19.559 58.299  -39.535 1.00 47.86  ? 216 ARG A CB  1 
ATOM   1424 C CG  . ARG A 1 216 ? -18.848 59.314  -38.652 1.00 54.24  ? 216 ARG A CG  1 
ATOM   1425 C CD  . ARG A 1 216 ? -19.781 60.099  -37.757 1.00 50.97  ? 216 ARG A CD  1 
ATOM   1426 N NE  . ARG A 1 216 ? -19.582 61.533  -37.940 1.00 70.93  ? 216 ARG A NE  1 
ATOM   1427 C CZ  . ARG A 1 216 ? -18.823 62.307  -37.174 1.00 76.20  ? 216 ARG A CZ  1 
ATOM   1428 N NH1 . ARG A 1 216 ? -18.172 61.824  -36.128 1.00 86.67  ? 216 ARG A NH1 1 
ATOM   1429 N NH2 . ARG A 1 216 ? -18.708 63.599  -37.471 1.00 77.64  ? 216 ARG A NH2 1 
ATOM   1430 N N   . ARG A 1 217 ? -19.773 56.483  -42.193 1.00 53.09  ? 217 ARG A N   1 
ATOM   1431 C CA  . ARG A 1 217 ? -20.535 55.512  -42.963 1.00 56.43  ? 217 ARG A CA  1 
ATOM   1432 C C   . ARG A 1 217 ? -19.690 54.275  -43.253 1.00 49.42  ? 217 ARG A C   1 
ATOM   1433 O O   . ARG A 1 217 ? -20.162 53.153  -43.092 1.00 47.83  ? 217 ARG A O   1 
ATOM   1434 C CB  . ARG A 1 217 ? -21.062 56.115  -44.278 1.00 54.13  ? 217 ARG A CB  1 
ATOM   1435 N N   . MET A 1 218 ? -18.437 54.495  -43.670 1.00 54.92  ? 218 MET A N   1 
ATOM   1436 C CA  . MET A 1 218 ? -17.520 53.408  -43.975 1.00 49.59  ? 218 MET A CA  1 
ATOM   1437 C C   . MET A 1 218 ? -17.202 52.603  -42.715 1.00 58.25  ? 218 MET A C   1 
ATOM   1438 O O   . MET A 1 218 ? -17.057 51.383  -42.774 1.00 51.00  ? 218 MET A O   1 
ATOM   1439 C CB  . MET A 1 218 ? -16.218 53.962  -44.588 1.00 55.41  ? 218 MET A CB  1 
ATOM   1440 C CG  . MET A 1 218 ? -16.372 54.511  -46.003 1.00 59.09  ? 218 MET A CG  1 
ATOM   1441 S SD  . MET A 1 218 ? -17.016 53.341  -47.229 1.00 61.89  ? 218 MET A SD  1 
ATOM   1442 C CE  . MET A 1 218 ? -16.162 51.853  -46.773 1.00 70.38  ? 218 MET A CE  1 
ATOM   1443 N N   . LEU A 1 219 ? -17.089 53.300  -41.577 1.00 48.99  ? 219 LEU A N   1 
ATOM   1444 C CA  . LEU A 1 219 ? -16.902 52.643  -40.294 1.00 54.30  ? 219 LEU A CA  1 
ATOM   1445 C C   . LEU A 1 219 ? -18.123 51.794  -39.961 1.00 52.29  ? 219 LEU A C   1 
ATOM   1446 O O   . LEU A 1 219 ? -17.984 50.655  -39.526 1.00 51.19  ? 219 LEU A O   1 
ATOM   1447 C CB  . LEU A 1 219 ? -16.641 53.670  -39.182 1.00 48.27  ? 219 LEU A CB  1 
ATOM   1448 C CG  . LEU A 1 219 ? -15.318 54.443  -39.313 1.00 52.32  ? 219 LEU A CG  1 
ATOM   1449 C CD1 . LEU A 1 219 ? -15.131 55.403  -38.163 1.00 53.02  ? 219 LEU A CD1 1 
ATOM   1450 C CD2 . LEU A 1 219 ? -14.137 53.504  -39.406 1.00 55.22  ? 219 LEU A CD2 1 
ATOM   1451 N N   . SER A 1 220 ? -19.316 52.346  -40.206 1.00 51.77  ? 220 SER A N   1 
ATOM   1452 C CA  . SER A 1 220 ? -20.554 51.645  -39.911 1.00 46.05  ? 220 SER A CA  1 
ATOM   1453 C C   . SER A 1 220 ? -20.714 50.366  -40.728 1.00 48.34  ? 220 SER A C   1 
ATOM   1454 O O   . SER A 1 220 ? -21.170 49.356  -40.200 1.00 60.36  ? 220 SER A O   1 
ATOM   1455 C CB  . SER A 1 220 ? -21.748 52.563  -40.123 1.00 56.17  ? 220 SER A CB  1 
ATOM   1456 O OG  . SER A 1 220 ? -21.682 53.683  -39.257 1.00 57.30  ? 220 SER A OG  1 
ATOM   1457 N N   . GLU A 1 221 ? -20.318 50.401  -42.006 1.00 51.73  ? 221 GLU A N   1 
ATOM   1458 C CA  . GLU A 1 221 ? -20.490 49.248  -42.878 1.00 56.91  ? 221 GLU A CA  1 
ATOM   1459 C C   . GLU A 1 221 ? -19.601 48.087  -42.444 1.00 51.61  ? 221 GLU A C   1 
ATOM   1460 O O   . GLU A 1 221 ? -20.062 46.947  -42.399 1.00 58.72  ? 221 GLU A O   1 
ATOM   1461 C CB  . GLU A 1 221 ? -20.229 49.599  -44.356 1.00 50.18  ? 221 GLU A CB  1 
ATOM   1462 C CG  . GLU A 1 221 ? -21.178 50.666  -44.882 1.00 66.33  ? 221 GLU A CG  1 
ATOM   1463 C CD  . GLU A 1 221 ? -21.393 50.697  -46.386 1.00 86.09  ? 221 GLU A CD  1 
ATOM   1464 O OE1 . GLU A 1 221 ? -20.986 49.734  -47.078 1.00 96.10  ? 221 GLU A OE1 1 
ATOM   1465 O OE2 . GLU A 1 221 ? -21.968 51.698  -46.875 1.00 72.47  ? 221 GLU A OE2 1 
ATOM   1466 N N   . PHE A 1 222 ? -18.338 48.392  -42.117 1.00 51.44  ? 222 PHE A N   1 
ATOM   1467 C CA  . PHE A 1 222 ? -17.414 47.403  -41.582 1.00 49.22  ? 222 PHE A CA  1 
ATOM   1468 C C   . PHE A 1 222 ? -18.045 46.644  -40.418 1.00 42.02  ? 222 PHE A C   1 
ATOM   1469 O O   . PHE A 1 222 ? -18.036 45.417  -40.405 1.00 49.08  ? 222 PHE A O   1 
ATOM   1470 C CB  . PHE A 1 222 ? -16.104 48.064  -41.133 1.00 50.20  ? 222 PHE A CB  1 
ATOM   1471 C CG  . PHE A 1 222 ? -15.179 47.138  -40.376 1.00 58.26  ? 222 PHE A CG  1 
ATOM   1472 C CD1 . PHE A 1 222 ? -14.689 45.985  -40.967 1.00 51.61  ? 222 PHE A CD1 1 
ATOM   1473 C CD2 . PHE A 1 222 ? -14.810 47.416  -39.071 1.00 48.59  ? 222 PHE A CD2 1 
ATOM   1474 C CE1 . PHE A 1 222 ? -13.841 45.139  -40.272 1.00 56.60  ? 222 PHE A CE1 1 
ATOM   1475 C CE2 . PHE A 1 222 ? -13.952 46.571  -38.381 1.00 52.19  ? 222 PHE A CE2 1 
ATOM   1476 C CZ  . PHE A 1 222 ? -13.471 45.438  -38.985 1.00 52.05  ? 222 PHE A CZ  1 
ATOM   1477 N N   . LEU A 1 223 ? -18.605 47.391  -39.459 1.00 42.13  ? 223 LEU A N   1 
ATOM   1478 C CA  . LEU A 1 223 ? -19.346 46.811  -38.351 1.00 42.90  ? 223 LEU A CA  1 
ATOM   1479 C C   . LEU A 1 223 ? -20.540 45.997  -38.846 1.00 56.68  ? 223 LEU A C   1 
ATOM   1480 O O   . LEU A 1 223 ? -20.696 44.839  -38.465 1.00 50.17  ? 223 LEU A O   1 
ATOM   1481 C CB  . LEU A 1 223 ? -19.846 47.905  -37.389 1.00 43.57  ? 223 LEU A CB  1 
ATOM   1482 C CG  . LEU A 1 223 ? -18.776 48.716  -36.661 1.00 52.04  ? 223 LEU A CG  1 
ATOM   1483 C CD1 . LEU A 1 223 ? -19.412 49.753  -35.750 1.00 48.81  ? 223 LEU A CD1 1 
ATOM   1484 C CD2 . LEU A 1 223 ? -17.838 47.816  -35.865 1.00 44.12  ? 223 LEU A CD2 1 
ATOM   1485 N N   . LEU A 1 224 ? -21.375 46.596  -39.703 1.00 47.41  ? 224 LEU A N   1 
ATOM   1486 C CA  . LEU A 1 224 ? -22.577 45.921  -40.168 1.00 42.49  ? 224 LEU A CA  1 
ATOM   1487 C C   . LEU A 1 224 ? -22.268 44.579  -40.827 1.00 42.21  ? 224 LEU A C   1 
ATOM   1488 O O   . LEU A 1 224 ? -23.052 43.640  -40.709 1.00 57.97  ? 224 LEU A O   1 
ATOM   1489 C CB  . LEU A 1 224 ? -23.369 46.796  -41.155 1.00 61.15  ? 224 LEU A CB  1 
ATOM   1490 C CG  . LEU A 1 224 ? -24.189 47.947  -40.569 1.00 57.04  ? 224 LEU A CG  1 
ATOM   1491 C CD1 . LEU A 1 224 ? -25.276 48.382  -41.552 1.00 70.95  ? 224 LEU A CD1 1 
ATOM   1492 C CD2 . LEU A 1 224 ? -24.812 47.582  -39.232 1.00 50.64  ? 224 LEU A CD2 1 
ATOM   1493 N N   . ALA A 1 225 ? -21.121 44.491  -41.509 1.00 43.09  ? 225 ALA A N   1 
ATOM   1494 C CA  . ALA A 1 225 ? -20.722 43.260  -42.171 1.00 49.73  ? 225 ALA A CA  1 
ATOM   1495 C C   . ALA A 1 225 ? -20.045 42.273  -41.219 1.00 59.23  ? 225 ALA A C   1 
ATOM   1496 O O   . ALA A 1 225 ? -19.826 41.117  -41.582 1.00 67.12  ? 225 ALA A O   1 
ATOM   1497 C CB  . ALA A 1 225 ? -19.806 43.583  -43.343 1.00 40.46  ? 225 ALA A CB  1 
ATOM   1498 N N   . ASN A 1 226 ? -19.720 42.729  -40.001 1.00 52.12  ? 226 ASN A N   1 
ATOM   1499 C CA  . ASN A 1 226 ? -18.976 41.927  -39.040 1.00 50.92  ? 226 ASN A CA  1 
ATOM   1500 C C   . ASN A 1 226 ? -19.455 42.167  -37.611 1.00 50.23  ? 226 ASN A C   1 
ATOM   1501 O O   . ASN A 1 226 ? -18.887 42.998  -36.901 1.00 50.59  ? 226 ASN A O   1 
ATOM   1502 C CB  . ASN A 1 226 ? -17.498 42.252  -39.140 1.00 48.60  ? 226 ASN A CB  1 
ATOM   1503 C CG  . ASN A 1 226 ? -16.967 42.036  -40.524 1.00 59.45  ? 226 ASN A CG  1 
ATOM   1504 O OD1 . ASN A 1 226 ? -16.800 40.891  -40.971 1.00 59.66  ? 226 ASN A OD1 1 
ATOM   1505 N ND2 . ASN A 1 226 ? -16.707 43.134  -41.235 1.00 53.23  ? 226 ASN A ND2 1 
ATOM   1506 N N   . PRO A 1 227 ? -20.497 41.440  -37.142 1.00 45.65  ? 227 PRO A N   1 
ATOM   1507 C CA  . PRO A 1 227 ? -21.059 41.671  -35.815 1.00 43.58  ? 227 PRO A CA  1 
ATOM   1508 C C   . PRO A 1 227 ? -20.190 41.146  -34.668 1.00 64.10  ? 227 PRO A C   1 
ATOM   1509 O O   . PRO A 1 227 ? -20.455 41.431  -33.499 1.00 57.91  ? 227 PRO A O   1 
ATOM   1510 C CB  . PRO A 1 227 ? -22.419 40.967  -35.890 1.00 42.34  ? 227 PRO A CB  1 
ATOM   1511 C CG  . PRO A 1 227 ? -22.242 39.890  -36.916 1.00 51.42  ? 227 PRO A CG  1 
ATOM   1512 C CD  . PRO A 1 227 ? -21.159 40.347  -37.871 1.00 52.19  ? 227 PRO A CD  1 
ATOM   1513 N N   . HIS A 1 228 ? -19.137 40.389  -35.002 1.00 51.57  ? 228 HIS A N   1 
ATOM   1514 C CA  . HIS A 1 228 ? -18.130 40.032  -34.017 1.00 62.77  ? 228 HIS A CA  1 
ATOM   1515 C C   . HIS A 1 228 ? -17.215 41.204  -33.661 1.00 60.31  ? 228 HIS A C   1 
ATOM   1516 O O   . HIS A 1 228 ? -16.407 41.085  -32.742 1.00 54.77  ? 228 HIS A O   1 
ATOM   1517 C CB  . HIS A 1 228 ? -17.280 38.843  -34.493 1.00 58.89  ? 228 HIS A CB  1 
ATOM   1518 C CG  . HIS A 1 228 ? -18.031 37.552  -34.607 1.00 63.38  ? 228 HIS A CG  1 
ATOM   1519 N ND1 . HIS A 1 228 ? -18.772 37.246  -35.730 1.00 69.09  ? 228 HIS A ND1 1 
ATOM   1520 C CD2 . HIS A 1 228 ? -18.101 36.515  -33.746 1.00 63.61  ? 228 HIS A CD2 1 
ATOM   1521 C CE1 . HIS A 1 228 ? -19.285 36.043  -35.512 1.00 69.34  ? 228 HIS A CE1 1 
ATOM   1522 N NE2 . HIS A 1 228 ? -18.903 35.567  -34.325 1.00 63.57  ? 228 HIS A NE2 1 
ATOM   1523 N N   . VAL A 1 229 ? -17.328 42.322  -34.392 1.00 52.84  ? 229 VAL A N   1 
ATOM   1524 C CA  . VAL A 1 229 ? -16.610 43.535  -34.034 1.00 54.30  ? 229 VAL A CA  1 
ATOM   1525 C C   . VAL A 1 229 ? -17.542 44.480  -33.282 1.00 54.44  ? 229 VAL A C   1 
ATOM   1526 O O   . VAL A 1 229 ? -18.536 44.935  -33.833 1.00 55.95  ? 229 VAL A O   1 
ATOM   1527 C CB  . VAL A 1 229 ? -15.994 44.233  -35.262 1.00 43.33  ? 229 VAL A CB  1 
ATOM   1528 C CG1 . VAL A 1 229 ? -15.189 45.453  -34.844 1.00 41.95  ? 229 VAL A CG1 1 
ATOM   1529 C CG2 . VAL A 1 229 ? -15.137 43.272  -36.075 1.00 44.60  ? 229 VAL A CG2 1 
ATOM   1530 N N   . LEU A 1 230 ? -17.205 44.767  -32.020 1.00 59.77  ? 230 LEU A N   1 
ATOM   1531 C CA  . LEU A 1 230 ? -17.974 45.681  -31.191 1.00 55.37  ? 230 LEU A CA  1 
ATOM   1532 C C   . LEU A 1 230 ? -17.820 47.140  -31.614 1.00 50.35  ? 230 LEU A C   1 
ATOM   1533 O O   . LEU A 1 230 ? -18.782 47.909  -31.583 1.00 51.19  ? 230 LEU A O   1 
ATOM   1534 C CB  . LEU A 1 230 ? -17.509 45.534  -29.740 1.00 40.75  ? 230 LEU A CB  1 
ATOM   1535 C CG  . LEU A 1 230 ? -18.171 46.436  -28.712 1.00 50.68  ? 230 LEU A CG  1 
ATOM   1536 C CD1 . LEU A 1 230 ? -19.617 45.991  -28.431 1.00 41.69  ? 230 LEU A CD1 1 
ATOM   1537 C CD2 . LEU A 1 230 ? -17.353 46.471  -27.418 1.00 42.54  ? 230 LEU A CD2 1 
ATOM   1538 N N   . LEU A 1 231 ? -16.591 47.514  -31.987 1.00 46.95  ? 231 LEU A N   1 
ATOM   1539 C CA  . LEU A 1 231 ? -16.214 48.911  -32.078 1.00 43.47  ? 231 LEU A CA  1 
ATOM   1540 C C   . LEU A 1 231 ? -15.096 49.083  -33.102 1.00 54.90  ? 231 LEU A C   1 
ATOM   1541 O O   . LEU A 1 231 ? -14.320 48.159  -33.339 1.00 49.60  ? 231 LEU A O   1 
ATOM   1542 C CB  . LEU A 1 231 ? -15.818 49.385  -30.670 1.00 47.18  ? 231 LEU A CB  1 
ATOM   1543 C CG  . LEU A 1 231 ? -15.158 50.748  -30.543 1.00 58.20  ? 231 LEU A CG  1 
ATOM   1544 C CD1 . LEU A 1 231 ? -15.521 51.408  -29.229 1.00 70.14  ? 231 LEU A CD1 1 
ATOM   1545 C CD2 . LEU A 1 231 ? -13.649 50.648  -30.619 1.00 51.31  ? 231 LEU A CD2 1 
ATOM   1546 N N   . VAL A 1 232 ? -15.064 50.262  -33.734 1.00 45.45  ? 232 VAL A N   1 
ATOM   1547 C CA  . VAL A 1 232 ? -14.033 50.601  -34.699 1.00 42.24  ? 232 VAL A CA  1 
ATOM   1548 C C   . VAL A 1 232 ? -13.720 52.084  -34.546 1.00 49.18  ? 232 VAL A C   1 
ATOM   1549 O O   . VAL A 1 232 ? -14.582 52.851  -34.127 1.00 49.73  ? 232 VAL A O   1 
ATOM   1550 C CB  . VAL A 1 232 ? -14.427 50.246  -36.151 1.00 47.98  ? 232 VAL A CB  1 
ATOM   1551 C CG1 . VAL A 1 232 ? -15.569 51.125  -36.664 1.00 39.62  ? 232 VAL A CG1 1 
ATOM   1552 C CG2 . VAL A 1 232 ? -13.219 50.334  -37.075 1.00 51.27  ? 232 VAL A CG2 1 
ATOM   1553 N N   . SER A 1 233 ? -12.475 52.459  -34.867 1.00 49.23  ? 233 SER A N   1 
ATOM   1554 C CA  . SER A 1 233 ? -12.019 53.832  -34.740 1.00 50.81  ? 233 SER A CA  1 
ATOM   1555 C C   . SER A 1 233 ? -11.015 54.218  -35.824 1.00 54.17  ? 233 SER A C   1 
ATOM   1556 O O   . SER A 1 233 ? -10.087 53.471  -36.123 1.00 53.61  ? 233 SER A O   1 
ATOM   1557 C CB  . SER A 1 233 ? -11.394 54.064  -33.369 1.00 52.40  ? 233 SER A CB  1 
ATOM   1558 O OG  . SER A 1 233 ? -12.358 53.993  -32.332 1.00 51.42  ? 233 SER A OG  1 
ATOM   1559 N N   . ALA A 1 234 ? -11.230 55.394  -36.419 1.00 52.73  ? 234 ALA A N   1 
ATOM   1560 C CA  . ALA A 1 234 ? -10.240 56.024  -37.270 1.00 54.62  ? 234 ALA A CA  1 
ATOM   1561 C C   . ALA A 1 234 ? -9.509  57.016  -36.378 1.00 46.25  ? 234 ALA A C   1 
ATOM   1562 O O   . ALA A 1 234 ? -10.122 57.926  -35.834 1.00 47.76  ? 234 ALA A O   1 
ATOM   1563 C CB  . ALA A 1 234 ? -10.896 56.713  -38.452 1.00 48.35  ? 234 ALA A CB  1 
ATOM   1564 N N   . ILE A 1 235 ? -8.210  56.795  -36.179 1.00 55.70  ? 235 ILE A N   1 
ATOM   1565 C CA  . ILE A 1 235 ? -7.414  57.701  -35.371 1.00 60.47  ? 235 ILE A CA  1 
ATOM   1566 C C   . ILE A 1 235 ? -6.488  58.454  -36.319 1.00 57.78  ? 235 ILE A C   1 
ATOM   1567 O O   . ILE A 1 235 ? -5.869  57.846  -37.189 1.00 59.47  ? 235 ILE A O   1 
ATOM   1568 C CB  . ILE A 1 235 ? -6.645  56.982  -34.253 1.00 55.49  ? 235 ILE A CB  1 
ATOM   1569 C CG1 . ILE A 1 235 ? -7.490  55.862  -33.617 1.00 56.18  ? 235 ILE A CG1 1 
ATOM   1570 C CG2 . ILE A 1 235 ? -6.158  57.997  -33.214 1.00 58.95  ? 235 ILE A CG2 1 
ATOM   1571 C CD1 . ILE A 1 235 ? -6.821  55.140  -32.484 1.00 47.95  ? 235 ILE A CD1 1 
ATOM   1572 N N   . TYR A 1 236 ? -6.440  59.781  -36.155 1.00 54.34  ? 236 TYR A N   1 
ATOM   1573 C CA  . TYR A 1 236 ? -5.599  60.638  -36.970 1.00 63.00  ? 236 TYR A CA  1 
ATOM   1574 C C   . TYR A 1 236 ? -4.611  61.375  -36.073 1.00 62.85  ? 236 TYR A C   1 
ATOM   1575 O O   . TYR A 1 236 ? -5.003  61.962  -35.067 1.00 69.59  ? 236 TYR A O   1 
ATOM   1576 C CB  . TYR A 1 236 ? -6.459  61.609  -37.787 1.00 57.36  ? 236 TYR A CB  1 
ATOM   1577 C CG  . TYR A 1 236 ? -7.181  60.914  -38.914 1.00 59.02  ? 236 TYR A CG  1 
ATOM   1578 C CD1 . TYR A 1 236 ? -6.480  60.333  -39.961 1.00 63.66  ? 236 TYR A CD1 1 
ATOM   1579 C CD2 . TYR A 1 236 ? -8.565  60.808  -38.920 1.00 60.50  ? 236 TYR A CD2 1 
ATOM   1580 C CE1 . TYR A 1 236 ? -7.138  59.677  -40.994 1.00 56.25  ? 236 TYR A CE1 1 
ATOM   1581 C CE2 . TYR A 1 236 ? -9.234  60.155  -39.948 1.00 51.64  ? 236 TYR A CE2 1 
ATOM   1582 C CZ  . TYR A 1 236 ? -8.517  59.592  -40.984 1.00 48.34  ? 236 TYR A CZ  1 
ATOM   1583 O OH  . TYR A 1 236 ? -9.168  58.944  -41.998 1.00 65.88  ? 236 TYR A OH  1 
ATOM   1584 N N   . THR A 1 237 ? -3.328  61.295  -36.442 1.00 71.18  ? 237 THR A N   1 
ATOM   1585 C CA  . THR A 1 237 ? -2.247  61.927  -35.700 1.00 79.39  ? 237 THR A CA  1 
ATOM   1586 C C   . THR A 1 237 ? -1.474  62.923  -36.561 1.00 78.38  ? 237 THR A C   1 
ATOM   1587 O O   . THR A 1 237 ? -0.499  63.512  -36.107 1.00 79.05  ? 237 THR A O   1 
ATOM   1588 C CB  . THR A 1 237 ? -1.322  60.842  -35.164 1.00 71.49  ? 237 THR A CB  1 
ATOM   1589 O OG1 . THR A 1 237 ? -0.884  60.040  -36.265 1.00 65.40  ? 237 THR A OG1 1 
ATOM   1590 C CG2 . THR A 1 237 ? -2.000  59.962  -34.124 1.00 63.79  ? 237 THR A CG2 1 
ATOM   1591 N N   . ASN A 1 238 ? -1.935  63.115  -37.801 1.00 80.83  ? 238 ASN A N   1 
ATOM   1592 C CA  . ASN A 1 238 ? -1.228  63.922  -38.783 1.00 90.62  ? 238 ASN A CA  1 
ATOM   1593 C C   . ASN A 1 238 ? -1.233  65.401  -38.398 1.00 89.56  ? 238 ASN A C   1 
ATOM   1594 O O   . ASN A 1 238 ? -0.271  65.884  -37.805 1.00 92.79  ? 238 ASN A O   1 
ATOM   1595 C CB  . ASN A 1 238 ? -1.817  63.691  -40.190 1.00 82.42  ? 238 ASN A CB  1 
ATOM   1596 C CG  . ASN A 1 238 ? -3.321  63.535  -40.197 1.00 83.77  ? 238 ASN A CG  1 
ATOM   1597 O OD1 . ASN A 1 238 ? -3.961  63.461  -39.141 1.00 79.61  ? 238 ASN A OD1 1 
ATOM   1598 N ND2 . ASN A 1 238 ? -3.917  63.477  -41.380 1.00 90.04  ? 238 ASN A ND2 1 
ATOM   1599 N N   . ASN A 1 239 ? -2.315  66.109  -38.743 1.00 90.56  ? 239 ASN A N   1 
ATOM   1600 C CA  . ASN A 1 239 ? -2.462  67.521  -38.426 1.00 92.71  ? 239 ASN A CA  1 
ATOM   1601 C C   . ASN A 1 239 ? -3.803  67.796  -37.748 1.00 87.76  ? 239 ASN A C   1 
ATOM   1602 O O   . ASN A 1 239 ? -3.867  68.566  -36.791 1.00 87.29  ? 239 ASN A O   1 
ATOM   1603 C CB  . ASN A 1 239 ? -2.307  68.367  -39.690 1.00 89.78  ? 239 ASN A CB  1 
ATOM   1604 N N   . ASN A 1 240 ? -4.869  67.163  -38.255 1.00 90.89  ? 240 ASN A N   1 
ATOM   1605 C CA  . ASN A 1 240 ? -6.192  67.255  -37.657 1.00 90.08  ? 240 ASN A CA  1 
ATOM   1606 C C   . ASN A 1 240 ? -6.376  66.165  -36.603 1.00 87.87  ? 240 ASN A C   1 
ATOM   1607 O O   . ASN A 1 240 ? -7.165  65.243  -36.797 1.00 86.54  ? 240 ASN A O   1 
ATOM   1608 C CB  . ASN A 1 240 ? -7.278  67.128  -38.729 1.00 89.90  ? 240 ASN A CB  1 
ATOM   1609 C CG  . ASN A 1 240 ? -7.062  67.991  -39.936 1.00 92.34  ? 240 ASN A CG  1 
ATOM   1610 O OD1 . ASN A 1 240 ? -7.072  67.507  -41.075 1.00 93.28  ? 240 ASN A OD1 1 
ATOM   1611 N ND2 . ASN A 1 240 ? -6.868  69.283  -39.721 1.00 102.96 ? 240 ASN A ND2 1 
ATOM   1612 N N   . GLU A 1 241 ? -5.646  66.290  -35.487 1.00 87.64  ? 241 GLU A N   1 
ATOM   1613 C CA  . GLU A 1 241 ? -5.627  65.273  -34.447 1.00 76.63  ? 241 GLU A CA  1 
ATOM   1614 C C   . GLU A 1 241 ? -7.030  64.950  -33.935 1.00 72.40  ? 241 GLU A C   1 
ATOM   1615 O O   . GLU A 1 241 ? -7.586  65.699  -33.136 1.00 76.11  ? 241 GLU A O   1 
ATOM   1616 C CB  . GLU A 1 241 ? -4.738  65.727  -33.277 1.00 84.23  ? 241 GLU A CB  1 
ATOM   1617 N N   . ARG A 1 242 ? -7.593  63.828  -34.406 1.00 68.63  ? 242 ARG A N   1 
ATOM   1618 C CA  . ARG A 1 242 ? -8.936  63.416  -34.027 1.00 73.08  ? 242 ARG A CA  1 
ATOM   1619 C C   . ARG A 1 242 ? -9.116  61.901  -34.105 1.00 70.12  ? 242 ARG A C   1 
ATOM   1620 O O   . ARG A 1 242 ? -8.299  61.203  -34.706 1.00 64.74  ? 242 ARG A O   1 
ATOM   1621 C CB  . ARG A 1 242 ? -9.978  64.124  -34.920 1.00 68.41  ? 242 ARG A CB  1 
ATOM   1622 C CG  . ARG A 1 242 ? -10.002 63.651  -36.370 1.00 63.61  ? 242 ARG A CG  1 
ATOM   1623 C CD  . ARG A 1 242 ? -10.619 64.701  -37.294 1.00 72.80  ? 242 ARG A CD  1 
ATOM   1624 N NE  . ARG A 1 242 ? -10.746 64.250  -38.678 1.00 64.40  ? 242 ARG A NE  1 
ATOM   1625 C CZ  . ARG A 1 242 ? -9.729  63.971  -39.486 1.00 62.25  ? 242 ARG A CZ  1 
ATOM   1626 N NH1 . ARG A 1 242 ? -8.475  64.021  -39.068 1.00 67.24  ? 242 ARG A NH1 1 
ATOM   1627 N NH2 . ARG A 1 242 ? -9.978  63.626  -40.747 1.00 66.37  ? 242 ARG A NH2 1 
ATOM   1628 N N   . VAL A 1 243 ? -10.200 61.418  -33.481 1.00 60.59  ? 243 VAL A N   1 
ATOM   1629 C CA  . VAL A 1 243 ? -10.589 60.016  -33.515 1.00 58.72  ? 243 VAL A CA  1 
ATOM   1630 C C   . VAL A 1 243 ? -12.068 59.918  -33.878 1.00 61.51  ? 243 VAL A C   1 
ATOM   1631 O O   . VAL A 1 243 ? -12.905 60.555  -33.243 1.00 67.52  ? 243 VAL A O   1 
ATOM   1632 C CB  . VAL A 1 243 ? -10.293 59.285  -32.174 1.00 67.68  ? 243 VAL A CB  1 
ATOM   1633 C CG1 . VAL A 1 243 ? -10.732 60.106  -30.971 1.00 74.40  ? 243 VAL A CG1 1 
ATOM   1634 C CG2 . VAL A 1 243 ? -10.925 57.896  -32.137 1.00 56.63  ? 243 VAL A CG2 1 
ATOM   1635 N N   . ILE A 1 244 ? -12.369 59.117  -34.908 1.00 58.88  ? 244 ILE A N   1 
ATOM   1636 C CA  . ILE A 1 244 ? -13.735 58.860  -35.329 1.00 52.98  ? 244 ILE A CA  1 
ATOM   1637 C C   . ILE A 1 244 ? -14.101 57.422  -34.973 1.00 50.42  ? 244 ILE A C   1 
ATOM   1638 O O   . ILE A 1 244 ? -13.601 56.488  -35.595 1.00 58.03  ? 244 ILE A O   1 
ATOM   1639 C CB  . ILE A 1 244 ? -13.910 59.116  -36.848 1.00 62.51  ? 244 ILE A CB  1 
ATOM   1640 C CG1 . ILE A 1 244 ? -13.270 60.446  -37.296 1.00 60.79  ? 244 ILE A CG1 1 
ATOM   1641 C CG2 . ILE A 1 244 ? -15.378 59.043  -37.244 1.00 61.26  ? 244 ILE A CG2 1 
ATOM   1642 C CD1 . ILE A 1 244 ? -13.779 61.664  -36.577 1.00 64.06  ? 244 ILE A CD1 1 
ATOM   1643 N N   . THR A 1 245 ? -14.981 57.258  -33.977 1.00 48.20  ? 245 THR A N   1 
ATOM   1644 C CA  . THR A 1 245 ? -15.394 55.944  -33.510 1.00 53.46  ? 245 THR A CA  1 
ATOM   1645 C C   . THR A 1 245 ? -16.846 55.628  -33.866 1.00 51.64  ? 245 THR A C   1 
ATOM   1646 O O   . THR A 1 245 ? -17.724 56.464  -33.678 1.00 54.41  ? 245 THR A O   1 
ATOM   1647 C CB  . THR A 1 245 ? -15.198 55.861  -31.990 1.00 54.05  ? 245 THR A CB  1 
ATOM   1648 O OG1 . THR A 1 245 ? -13.840 56.179  -31.676 1.00 62.96  ? 245 THR A OG1 1 
ATOM   1649 C CG2 . THR A 1 245 ? -15.542 54.495  -31.428 1.00 42.21  ? 245 THR A CG2 1 
ATOM   1650 N N   . ALA A 1 246 ? -17.082 54.407  -34.365 1.00 49.40  ? 246 ALA A N   1 
ATOM   1651 C CA  . ALA A 1 246 ? -18.413 53.826  -34.439 1.00 46.47  ? 246 ALA A CA  1 
ATOM   1652 C C   . ALA A 1 246 ? -18.501 52.574  -33.566 1.00 47.08  ? 246 ALA A C   1 
ATOM   1653 O O   . ALA A 1 246 ? -17.641 51.699  -33.638 1.00 52.90  ? 246 ALA A O   1 
ATOM   1654 C CB  . ALA A 1 246 ? -18.763 53.482  -35.873 1.00 47.24  ? 246 ALA A CB  1 
ATOM   1655 N N   . MET A 1 247 ? -19.561 52.491  -32.755 1.00 52.46  ? 247 MET A N   1 
ATOM   1656 C CA  . MET A 1 247 ? -19.763 51.369  -31.855 1.00 54.75  ? 247 MET A CA  1 
ATOM   1657 C C   . MET A 1 247 ? -21.107 50.711  -32.155 1.00 59.47  ? 247 MET A C   1 
ATOM   1658 O O   . MET A 1 247 ? -22.117 51.396  -32.318 1.00 56.34  ? 247 MET A O   1 
ATOM   1659 C CB  . MET A 1 247 ? -19.734 51.853  -30.409 1.00 53.67  ? 247 MET A CB  1 
ATOM   1660 C CG  . MET A 1 247 ? -19.621 50.740  -29.415 1.00 47.46  ? 247 MET A CG  1 
ATOM   1661 S SD  . MET A 1 247 ? -19.695 51.241  -27.667 1.00 67.58  ? 247 MET A SD  1 
ATOM   1662 C CE  . MET A 1 247 ? -20.494 52.808  -27.757 1.00 72.44  ? 247 MET A CE  1 
ATOM   1663 N N   . SER A 1 248 ? -21.099 49.374  -32.206 1.00 55.76  ? 248 SER A N   1 
ATOM   1664 C CA  . SER A 1 248 ? -22.273 48.589  -32.549 1.00 53.55  ? 248 SER A CA  1 
ATOM   1665 C C   . SER A 1 248 ? -22.947 48.022  -31.299 1.00 66.47  ? 248 SER A C   1 
ATOM   1666 O O   . SER A 1 248 ? -22.383 47.170  -30.612 1.00 64.67  ? 248 SER A O   1 
ATOM   1667 C CB  . SER A 1 248 ? -21.878 47.472  -33.507 1.00 46.12  ? 248 SER A CB  1 
ATOM   1668 O OG  . SER A 1 248 ? -22.967 46.609  -33.778 1.00 61.55  ? 248 SER A OG  1 
ATOM   1669 N N   . MET A 1 249 ? -24.166 48.502  -31.022 1.00 66.63  ? 249 MET A N   1 
ATOM   1670 C CA  . MET A 1 249 ? -24.889 48.144  -29.813 1.00 64.85  ? 249 MET A CA  1 
ATOM   1671 C C   . MET A 1 249 ? -25.868 47.018  -30.149 1.00 68.81  ? 249 MET A C   1 
ATOM   1672 O O   . MET A 1 249 ? -25.439 45.903  -30.435 1.00 73.96  ? 249 MET A O   1 
ATOM   1673 C CB  . MET A 1 249 ? -25.567 49.404  -29.234 1.00 63.61  ? 249 MET A CB  1 
ATOM   1674 C CG  . MET A 1 249 ? -24.570 50.447  -28.761 1.00 67.95  ? 249 MET A CG  1 
ATOM   1675 S SD  . MET A 1 249 ? -25.334 51.950  -28.109 1.00 95.75  ? 249 MET A SD  1 
ATOM   1676 C CE  . MET A 1 249 ? -24.975 51.759  -26.373 1.00 77.79  ? 249 MET A CE  1 
ATOM   1677 N N   . ASP A 1 250 ? -27.176 47.306  -30.129 1.00 65.44  ? 250 ASP A N   1 
ATOM   1678 C CA  . ASP A 1 250 ? -28.193 46.293  -30.366 1.00 71.98  ? 250 ASP A CA  1 
ATOM   1679 C C   . ASP A 1 250 ? -28.990 46.676  -31.610 1.00 67.03  ? 250 ASP A C   1 
ATOM   1680 O O   . ASP A 1 250 ? -30.044 47.300  -31.508 1.00 65.34  ? 250 ASP A O   1 
ATOM   1681 C CB  . ASP A 1 250 ? -29.119 46.145  -29.142 1.00 69.96  ? 250 ASP A CB  1 
ATOM   1682 C CG  . ASP A 1 250 ? -28.396 45.892  -27.832 1.00 77.41  ? 250 ASP A CG  1 
ATOM   1683 O OD1 . ASP A 1 250 ? -27.655 44.883  -27.745 1.00 71.91  ? 250 ASP A OD1 1 
ATOM   1684 O OD2 . ASP A 1 250 ? -28.573 46.701  -26.892 1.00 71.23  ? 250 ASP A OD2 1 
ATOM   1685 N N   . SER A 1 251 ? -28.456 46.304  -32.781 1.00 54.30  ? 251 SER A N   1 
ATOM   1686 C CA  . SER A 1 251 ? -28.964 46.756  -34.068 1.00 65.23  ? 251 SER A CA  1 
ATOM   1687 C C   . SER A 1 251 ? -28.734 48.250  -34.285 1.00 52.98  ? 251 SER A C   1 
ATOM   1688 O O   . SER A 1 251 ? -29.173 48.797  -35.290 1.00 59.15  ? 251 SER A O   1 
ATOM   1689 C CB  . SER A 1 251 ? -30.448 46.424  -34.227 1.00 61.78  ? 251 SER A CB  1 
ATOM   1690 O OG  . SER A 1 251 ? -31.280 47.181  -33.361 1.00 60.62  ? 251 SER A OG  1 
ATOM   1691 N N   . LYS A 1 252 ? -28.018 48.890  -33.352 1.00 50.85  ? 252 LYS A N   1 
ATOM   1692 C CA  . LYS A 1 252 ? -27.790 50.322  -33.379 1.00 44.82  ? 252 LYS A CA  1 
ATOM   1693 C C   . LYS A 1 252 ? -26.299 50.621  -33.517 1.00 54.21  ? 252 LYS A C   1 
ATOM   1694 O O   . LYS A 1 252 ? -25.470 50.033  -32.825 1.00 53.80  ? 252 LYS A O   1 
ATOM   1695 C CB  . LYS A 1 252 ? -28.337 50.972  -32.105 1.00 46.50  ? 252 LYS A CB  1 
ATOM   1696 C CG  . LYS A 1 252 ? -29.712 50.466  -31.699 1.00 52.31  ? 252 LYS A CG  1 
ATOM   1697 C CD  . LYS A 1 252 ? -30.459 51.401  -30.748 1.00 63.77  ? 252 LYS A CD  1 
ATOM   1698 C CE  . LYS A 1 252 ? -29.709 51.753  -29.482 1.00 70.63  ? 252 LYS A CE  1 
ATOM   1699 N NZ  . LYS A 1 252 ? -29.544 50.585  -28.589 1.00 76.55  ? 252 LYS A NZ  1 
ATOM   1700 N N   . ILE A 1 253 ? -25.964 51.525  -34.443 1.00 51.83  ? 253 ILE A N   1 
ATOM   1701 C CA  . ILE A 1 253 ? -24.619 52.058  -34.537 1.00 50.61  ? 253 ILE A CA  1 
ATOM   1702 C C   . ILE A 1 253 ? -24.657 53.465  -33.950 1.00 55.11  ? 253 ILE A C   1 
ATOM   1703 O O   . ILE A 1 253 ? -25.550 54.248  -34.261 1.00 60.23  ? 253 ILE A O   1 
ATOM   1704 C CB  . ILE A 1 253 ? -24.043 52.018  -35.970 1.00 50.49  ? 253 ILE A CB  1 
ATOM   1705 C CG1 . ILE A 1 253 ? -23.562 50.600  -36.375 1.00 49.86  ? 253 ILE A CG1 1 
ATOM   1706 C CG2 . ILE A 1 253 ? -22.881 53.014  -36.120 1.00 50.95  ? 253 ILE A CG2 1 
ATOM   1707 C CD1 . ILE A 1 253 ? -24.630 49.512  -36.466 1.00 55.63  ? 253 ILE A CD1 1 
ATOM   1708 N N   . ALA A 1 254 ? -23.686 53.753  -33.076 1.00 60.52  ? 254 ALA A N   1 
ATOM   1709 C CA  . ALA A 1 254 ? -23.525 55.063  -32.467 1.00 65.42  ? 254 ALA A CA  1 
ATOM   1710 C C   . ALA A 1 254 ? -22.086 55.542  -32.652 1.00 60.75  ? 254 ALA A C   1 
ATOM   1711 O O   . ALA A 1 254 ? -21.183 54.736  -32.879 1.00 55.04  ? 254 ALA A O   1 
ATOM   1712 C CB  . ALA A 1 254 ? -23.881 55.005  -30.987 1.00 68.17  ? 254 ALA A CB  1 
ATOM   1713 N N   . TYR A 1 255 ? -21.889 56.860  -32.527 1.00 59.97  ? 255 TYR A N   1 
ATOM   1714 C CA  . TYR A 1 255 ? -20.600 57.489  -32.773 1.00 55.88  ? 255 TYR A CA  1 
ATOM   1715 C C   . TYR A 1 255 ? -20.120 58.255  -31.543 1.00 69.45  ? 255 TYR A C   1 
ATOM   1716 O O   . TYR A 1 255 ? -20.278 59.474  -31.474 1.00 69.12  ? 255 TYR A O   1 
ATOM   1717 C CB  . TYR A 1 255 ? -20.686 58.422  -33.987 1.00 57.37  ? 255 TYR A CB  1 
ATOM   1718 C CG  . TYR A 1 255 ? -21.180 57.715  -35.225 1.00 47.68  ? 255 TYR A CG  1 
ATOM   1719 C CD1 . TYR A 1 255 ? -20.351 56.866  -35.943 1.00 46.00  ? 255 TYR A CD1 1 
ATOM   1720 C CD2 . TYR A 1 255 ? -22.494 57.860  -35.653 1.00 60.10  ? 255 TYR A CD2 1 
ATOM   1721 C CE1 . TYR A 1 255 ? -20.808 56.198  -37.075 1.00 53.80  ? 255 TYR A CE1 1 
ATOM   1722 C CE2 . TYR A 1 255 ? -22.962 57.202  -36.786 1.00 64.01  ? 255 TYR A CE2 1 
ATOM   1723 C CZ  . TYR A 1 255 ? -22.117 56.370  -37.494 1.00 56.39  ? 255 TYR A CZ  1 
ATOM   1724 O OH  . TYR A 1 255 ? -22.590 55.714  -38.602 1.00 56.44  ? 255 TYR A OH  1 
ATOM   1725 N N   . PRO A 1 256 ? -19.514 57.560  -30.548 1.00 70.80  ? 256 PRO A N   1 
ATOM   1726 C CA  . PRO A 1 256 ? -18.993 58.213  -29.353 1.00 68.68  ? 256 PRO A CA  1 
ATOM   1727 C C   . PRO A 1 256 ? -17.843 59.176  -29.638 1.00 74.12  ? 256 PRO A C   1 
ATOM   1728 O O   . PRO A 1 256 ? -17.029 58.930  -30.527 1.00 73.67  ? 256 PRO A O   1 
ATOM   1729 C CB  . PRO A 1 256 ? -18.509 57.037  -28.488 1.00 74.29  ? 256 PRO A CB  1 
ATOM   1730 C CG  . PRO A 1 256 ? -19.093 55.815  -29.102 1.00 68.24  ? 256 PRO A CG  1 
ATOM   1731 C CD  . PRO A 1 256 ? -19.285 56.106  -30.541 1.00 59.07  ? 256 PRO A CD  1 
ATOM   1732 N N   . ASN A 1 257 ? -17.783 60.264  -28.864 1.00 77.23  ? 257 ASN A N   1 
ATOM   1733 C CA  . ASN A 1 257 ? -16.764 61.285  -29.044 1.00 78.87  ? 257 ASN A CA  1 
ATOM   1734 C C   . ASN A 1 257 ? -15.551 60.969  -28.174 1.00 86.29  ? 257 ASN A C   1 
ATOM   1735 O O   . ASN A 1 257 ? -15.416 61.503  -27.076 1.00 90.68  ? 257 ASN A O   1 
ATOM   1736 C CB  . ASN A 1 257 ? -17.323 62.677  -28.726 1.00 86.95  ? 257 ASN A CB  1 
ATOM   1737 N N   . THR A 1 258 ? -14.681 60.085  -28.681 1.00 87.35  ? 258 THR A N   1 
ATOM   1738 C CA  . THR A 1 258 ? -13.473 59.684  -27.977 1.00 85.95  ? 258 THR A CA  1 
ATOM   1739 C C   . THR A 1 258 ? -12.460 60.826  -27.996 1.00 93.06  ? 258 THR A C   1 
ATOM   1740 O O   . THR A 1 258 ? -12.404 61.590  -28.956 1.00 101.46 ? 258 THR A O   1 
ATOM   1741 C CB  . THR A 1 258 ? -12.891 58.401  -28.596 1.00 85.44  ? 258 THR A CB  1 
ATOM   1742 O OG1 . THR A 1 258 ? -13.925 57.423  -28.726 1.00 84.18  ? 258 THR A OG1 1 
ATOM   1743 C CG2 . THR A 1 258 ? -11.740 57.822  -27.772 1.00 83.25  ? 258 THR A CG2 1 
ATOM   1744 N N   . THR A 1 259 ? -11.671 60.935  -26.921 1.00 103.04 ? 259 THR A N   1 
ATOM   1745 C CA  . THR A 1 259 ? -10.656 61.970  -26.796 1.00 103.76 ? 259 THR A CA  1 
ATOM   1746 C C   . THR A 1 259 ? -9.271  61.340  -26.916 1.00 103.99 ? 259 THR A C   1 
ATOM   1747 O O   . THR A 1 259 ? -9.072  60.194  -26.515 1.00 103.18 ? 259 THR A O   1 
ATOM   1748 C CB  . THR A 1 259 ? -10.831 62.733  -25.477 1.00 101.08 ? 259 THR A CB  1 
ATOM   1749 O OG1 . THR A 1 259 ? -12.204 63.098  -25.331 1.00 98.62  ? 259 THR A OG1 1 
ATOM   1750 C CG2 . THR A 1 259 ? -9.964  63.981  -25.404 1.00 97.66  ? 259 THR A CG2 1 
ATOM   1751 N N   . LEU A 1 260 ? -8.321  62.109  -27.461 1.00 106.53 ? 260 LEU A N   1 
ATOM   1752 C CA  . LEU A 1 260 ? -6.983  61.611  -27.735 1.00 110.28 ? 260 LEU A CA  1 
ATOM   1753 C C   . LEU A 1 260 ? -6.098  61.691  -26.493 1.00 108.03 ? 260 LEU A C   1 
ATOM   1754 O O   . LEU A 1 260 ? -6.134  62.679  -25.762 1.00 110.85 ? 260 LEU A O   1 
ATOM   1755 C CB  . LEU A 1 260 ? -6.335  62.407  -28.877 1.00 103.28 ? 260 LEU A CB  1 
ATOM   1756 C CG  . LEU A 1 260 ? -7.120  62.426  -30.189 1.00 87.87  ? 260 LEU A CG  1 
ATOM   1757 C CD1 . LEU A 1 260 ? -7.921  63.719  -30.344 1.00 84.56  ? 260 LEU A CD1 1 
ATOM   1758 C CD2 . LEU A 1 260 ? -6.199  62.209  -31.378 1.00 84.85  ? 260 LEU A CD2 1 
ATOM   1759 N N   . ASN A 1 261 ? -5.305  60.637  -26.273 1.00 107.23 ? 261 ASN A N   1 
ATOM   1760 C CA  . ASN A 1 261 ? -4.341  60.602  -25.185 1.00 106.72 ? 261 ASN A CA  1 
ATOM   1761 C C   . ASN A 1 261 ? -2.939  60.860  -25.730 1.00 110.54 ? 261 ASN A C   1 
ATOM   1762 O O   . ASN A 1 261 ? -2.585  60.360  -26.794 1.00 111.40 ? 261 ASN A O   1 
ATOM   1763 C CB  . ASN A 1 261 ? -4.396  59.263  -24.451 1.00 106.40 ? 261 ASN A CB  1 
ATOM   1764 N N   . GLU A 1 262 ? -2.151  61.643  -24.981 1.00 114.25 ? 262 GLU A N   1 
ATOM   1765 C CA  . GLU A 1 262 ? -0.788  61.983  -25.363 1.00 108.22 ? 262 GLU A CA  1 
ATOM   1766 C C   . GLU A 1 262 ? 0.107   60.751  -25.479 1.00 104.75 ? 262 GLU A C   1 
ATOM   1767 O O   . GLU A 1 262 ? 1.089   60.772  -26.218 1.00 99.44  ? 262 GLU A O   1 
ATOM   1768 C CB  . GLU A 1 262 ? -0.178  62.964  -24.348 1.00 106.70 ? 262 GLU A CB  1 
ATOM   1769 N N   . ASN A 1 263 ? -0.234  59.694  -24.728 1.00 108.43 ? 263 ASN A N   1 
ATOM   1770 C CA  . ASN A 1 263 ? 0.457   58.416  -24.805 1.00 105.82 ? 263 ASN A CA  1 
ATOM   1771 C C   . ASN A 1 263 ? -0.022  57.583  -25.993 1.00 105.06 ? 263 ASN A C   1 
ATOM   1772 O O   . ASN A 1 263 ? 0.789   56.979  -26.691 1.00 101.68 ? 263 ASN A O   1 
ATOM   1773 C CB  . ASN A 1 263 ? 0.278   57.628  -23.502 1.00 104.37 ? 263 ASN A CB  1 
ATOM   1774 N N   . MET A 1 264 ? -1.344  57.553  -26.208 1.00 106.09 ? 264 MET A N   1 
ATOM   1775 C CA  . MET A 1 264 ? -1.933  56.833  -27.326 1.00 95.49  ? 264 MET A CA  1 
ATOM   1776 C C   . MET A 1 264 ? -1.472  57.478  -28.630 1.00 94.89  ? 264 MET A C   1 
ATOM   1777 O O   . MET A 1 264 ? -1.099  56.780  -29.569 1.00 94.36  ? 264 MET A O   1 
ATOM   1778 C CB  . MET A 1 264 ? -3.467  56.841  -27.230 1.00 97.13  ? 264 MET A CB  1 
ATOM   1779 C CG  . MET A 1 264 ? -4.019  56.051  -26.045 1.00 106.97 ? 264 MET A CG  1 
ATOM   1780 S SD  . MET A 1 264 ? -3.664  54.272  -26.089 1.00 112.02 ? 264 MET A SD  1 
ATOM   1781 C CE  . MET A 1 264 ? -5.169  53.630  -25.383 1.00 86.45  ? 264 MET A CE  1 
ATOM   1782 N N   . THR A 1 265 ? -1.508  58.817  -28.668 1.00 95.19  ? 265 THR A N   1 
ATOM   1783 C CA  . THR A 1 265 ? -0.842  59.588  -29.706 1.00 93.58  ? 265 THR A CA  1 
ATOM   1784 C C   . THR A 1 265 ? 0.664   59.496  -29.475 1.00 97.74  ? 265 THR A C   1 
ATOM   1785 O O   . THR A 1 265 ? 1.105   59.349  -28.339 1.00 100.69 ? 265 THR A O   1 
ATOM   1786 C CB  . THR A 1 265 ? -1.334  61.044  -29.724 1.00 94.75  ? 265 THR A CB  1 
ATOM   1787 N N   . ASN A 1 266 ? 1.438   59.574  -30.565 1.00 92.43  ? 266 ASN A N   1 
ATOM   1788 C CA  . ASN A 1 266 ? 2.870   59.301  -30.562 1.00 93.89  ? 266 ASN A CA  1 
ATOM   1789 C C   . ASN A 1 266 ? 3.139   57.796  -30.625 1.00 84.46  ? 266 ASN A C   1 
ATOM   1790 O O   . ASN A 1 266 ? 4.021   57.359  -31.361 1.00 81.35  ? 266 ASN A O   1 
ATOM   1791 C CB  . ASN A 1 266 ? 3.627   59.936  -29.366 1.00 99.63  ? 266 ASN A CB  1 
ATOM   1792 C CG  . ASN A 1 266 ? 3.745   61.442  -29.435 1.00 98.79  ? 266 ASN A CG  1 
ATOM   1793 O OD1 . ASN A 1 266 ? 4.202   62.009  -30.434 1.00 103.45 ? 266 ASN A OD1 1 
ATOM   1794 N ND2 . ASN A 1 266 ? 3.348   62.127  -28.372 1.00 95.18  ? 266 ASN A ND2 1 
ATOM   1795 N N   . GLN A 1 267 ? 2.388   57.006  -29.847 1.00 77.26  ? 267 GLN A N   1 
ATOM   1796 C CA  . GLN A 1 267 ? 2.413   55.558  -29.991 1.00 84.27  ? 267 GLN A CA  1 
ATOM   1797 C C   . GLN A 1 267 ? 1.832   55.159  -31.347 1.00 80.79  ? 267 GLN A C   1 
ATOM   1798 O O   . GLN A 1 267 ? 2.366   54.274  -32.014 1.00 77.46  ? 267 GLN A O   1 
ATOM   1799 C CB  . GLN A 1 267 ? 1.646   54.864  -28.853 1.00 88.43  ? 267 GLN A CB  1 
ATOM   1800 N N   . ILE A 1 268 ? 0.743   55.829  -31.749 1.00 74.99  ? 268 ILE A N   1 
ATOM   1801 C CA  . ILE A 1 268 ? 0.148   55.621  -33.060 1.00 71.53  ? 268 ILE A CA  1 
ATOM   1802 C C   . ILE A 1 268 ? 1.089   56.148  -34.140 1.00 72.97  ? 268 ILE A C   1 
ATOM   1803 O O   . ILE A 1 268 ? 1.280   55.496  -35.164 1.00 75.28  ? 268 ILE A O   1 
ATOM   1804 C CB  . ILE A 1 268 ? -1.262  56.263  -33.162 1.00 68.43  ? 268 ILE A CB  1 
ATOM   1805 N N   . ARG A 1 269 ? 1.683   57.324  -33.896 1.00 76.58  ? 269 ARG A N   1 
ATOM   1806 C CA  . ARG A 1 269 ? 2.724   57.864  -34.760 1.00 77.69  ? 269 ARG A CA  1 
ATOM   1807 C C   . ARG A 1 269 ? 3.895   56.899  -34.952 1.00 76.77  ? 269 ARG A C   1 
ATOM   1808 O O   . ARG A 1 269 ? 4.542   56.912  -35.999 1.00 73.58  ? 269 ARG A O   1 
ATOM   1809 C CB  . ARG A 1 269 ? 3.279   59.190  -34.203 1.00 84.42  ? 269 ARG A CB  1 
ATOM   1810 C CG  . ARG A 1 269 ? 2.275   60.338  -34.166 1.00 84.77  ? 269 ARG A CG  1 
ATOM   1811 C CD  . ARG A 1 269 ? 2.948   61.659  -33.832 1.00 88.32  ? 269 ARG A CD  1 
ATOM   1812 N NE  . ARG A 1 269 ? 2.005   62.772  -33.847 1.00 88.67  ? 269 ARG A NE  1 
ATOM   1813 C CZ  . ARG A 1 269 ? 1.094   63.015  -32.911 1.00 88.98  ? 269 ARG A CZ  1 
ATOM   1814 N NH1 . ARG A 1 269 ? 1.252   62.603  -31.663 1.00 92.52  ? 269 ARG A NH1 1 
ATOM   1815 N NH2 . ARG A 1 269 ? 0.015   63.729  -33.227 1.00 102.02 ? 269 ARG A NH2 1 
ATOM   1816 N N   . SER A 1 270 ? 4.163   56.072  -33.932 1.00 67.02  ? 270 SER A N   1 
ATOM   1817 C CA  . SER A 1 270 ? 5.267   55.126  -33.971 1.00 67.10  ? 270 SER A CA  1 
ATOM   1818 C C   . SER A 1 270 ? 4.910   53.785  -34.611 1.00 66.62  ? 270 SER A C   1 
ATOM   1819 O O   . SER A 1 270 ? 5.805   53.072  -35.058 1.00 59.05  ? 270 SER A O   1 
ATOM   1820 C CB  . SER A 1 270 ? 5.811   54.892  -32.564 1.00 61.05  ? 270 SER A CB  1 
ATOM   1821 N N   . LEU A 1 271 ? 3.612   53.444  -34.646 1.00 59.73  ? 271 LEU A N   1 
ATOM   1822 C CA  . LEU A 1 271 ? 3.173   52.142  -35.126 1.00 51.62  ? 271 LEU A CA  1 
ATOM   1823 C C   . LEU A 1 271 ? 3.548   51.960  -36.594 1.00 58.10  ? 271 LEU A C   1 
ATOM   1824 O O   . LEU A 1 271 ? 3.384   52.875  -37.396 1.00 50.49  ? 271 LEU A O   1 
ATOM   1825 C CB  . LEU A 1 271 ? 1.654   51.972  -34.957 1.00 53.32  ? 271 LEU A CB  1 
ATOM   1826 C CG  . LEU A 1 271 ? 1.095   50.576  -35.279 1.00 53.60  ? 271 LEU A CG  1 
ATOM   1827 C CD1 . LEU A 1 271 ? 1.419   49.602  -34.194 1.00 54.51  ? 271 LEU A CD1 1 
ATOM   1828 C CD2 . LEU A 1 271 ? -0.398  50.606  -35.478 1.00 46.34  ? 271 LEU A CD2 1 
ATOM   1829 N N   . LYS A 1 272 ? 4.047   50.764  -36.930 1.00 56.03  ? 272 LYS A N   1 
ATOM   1830 C CA  . LYS A 1 272 ? 4.532   50.472  -38.270 1.00 63.70  ? 272 LYS A CA  1 
ATOM   1831 C C   . LYS A 1 272 ? 3.853   49.263  -38.907 1.00 62.36  ? 272 LYS A C   1 
ATOM   1832 O O   . LYS A 1 272 ? 3.627   49.252  -40.114 1.00 64.79  ? 272 LYS A O   1 
ATOM   1833 C CB  . LYS A 1 272 ? 6.051   50.242  -38.247 1.00 57.16  ? 272 LYS A CB  1 
ATOM   1834 C CG  . LYS A 1 272 ? 6.855   51.465  -37.847 1.00 53.07  ? 272 LYS A CG  1 
ATOM   1835 C CD  . LYS A 1 272 ? 6.861   52.561  -38.890 1.00 64.52  ? 272 LYS A CD  1 
ATOM   1836 C CE  . LYS A 1 272 ? 7.969   53.557  -38.634 1.00 69.18  ? 272 LYS A CE  1 
ATOM   1837 N NZ  . LYS A 1 272 ? 8.062   54.583  -39.706 1.00 82.64  ? 272 LYS A NZ  1 
ATOM   1838 N N   . SER A 1 273 ? 3.547   48.240  -38.103 1.00 57.56  ? 273 SER A N   1 
ATOM   1839 C CA  . SER A 1 273 ? 2.863   47.060  -38.603 1.00 62.06  ? 273 SER A CA  1 
ATOM   1840 C C   . SER A 1 273 ? 1.585   46.783  -37.816 1.00 64.45  ? 273 SER A C   1 
ATOM   1841 O O   . SER A 1 273 ? 1.379   47.342  -36.739 1.00 64.95  ? 273 SER A O   1 
ATOM   1842 C CB  . SER A 1 273 ? 3.789   45.850  -38.565 1.00 60.88  ? 273 SER A CB  1 
ATOM   1843 O OG  . SER A 1 273 ? 4.310   45.641  -37.265 1.00 72.21  ? 273 SER A OG  1 
ATOM   1844 N N   . ILE A 1 274 ? 0.727   45.927  -38.380 1.00 61.03  ? 274 ILE A N   1 
ATOM   1845 C CA  . ILE A 1 274 ? -0.473  45.481  -37.694 1.00 62.07  ? 274 ILE A CA  1 
ATOM   1846 C C   . ILE A 1 274 ? -0.069  44.820  -36.382 1.00 62.41  ? 274 ILE A C   1 
ATOM   1847 O O   . ILE A 1 274 ? 0.929   44.105  -36.328 1.00 65.45  ? 274 ILE A O   1 
ATOM   1848 C CB  . ILE A 1 274 ? -1.336  44.517  -38.540 1.00 54.92  ? 274 ILE A CB  1 
ATOM   1849 C CG1 . ILE A 1 274 ? -2.649  44.167  -37.797 1.00 51.98  ? 274 ILE A CG1 1 
ATOM   1850 C CG2 . ILE A 1 274 ? -0.561  43.261  -38.930 1.00 56.04  ? 274 ILE A CG2 1 
ATOM   1851 C CD1 . ILE A 1 274 ? -3.439  43.068  -38.412 1.00 50.79  ? 274 ILE A CD1 1 
ATOM   1852 N N   . THR A 1 275 ? -0.857  45.081  -35.334 1.00 63.81  ? 275 THR A N   1 
ATOM   1853 C CA  . THR A 1 275 ? -0.651  44.456  -34.040 1.00 62.47  ? 275 THR A CA  1 
ATOM   1854 C C   . THR A 1 275 ? -1.984  44.129  -33.374 1.00 59.37  ? 275 THR A C   1 
ATOM   1855 O O   . THR A 1 275 ? -3.053  44.455  -33.893 1.00 58.53  ? 275 THR A O   1 
ATOM   1856 C CB  . THR A 1 275 ? 0.203   45.356  -33.158 1.00 58.91  ? 275 THR A CB  1 
ATOM   1857 O OG1 . THR A 1 275 ? 0.529   44.637  -31.965 1.00 66.27  ? 275 THR A OG1 1 
ATOM   1858 C CG2 . THR A 1 275 ? -0.494  46.672  -32.818 1.00 52.52  ? 275 THR A CG2 1 
ATOM   1859 N N   . HIS A 1 276 ? -1.895  43.460  -32.223 1.00 52.11  ? 276 HIS A N   1 
ATOM   1860 C CA  . HIS A 1 276 ? -3.051  43.230  -31.381 1.00 57.66  ? 276 HIS A CA  1 
ATOM   1861 C C   . HIS A 1 276 ? -2.642  43.422  -29.925 1.00 62.18  ? 276 HIS A C   1 
ATOM   1862 O O   . HIS A 1 276 ? -1.454  43.471  -29.616 1.00 55.23  ? 276 HIS A O   1 
ATOM   1863 C CB  . HIS A 1 276 ? -3.667  41.845  -31.648 1.00 55.80  ? 276 HIS A CB  1 
ATOM   1864 C CG  . HIS A 1 276 ? -2.861  40.670  -31.186 1.00 55.08  ? 276 HIS A CG  1 
ATOM   1865 N ND1 . HIS A 1 276 ? -2.832  40.295  -29.853 1.00 59.20  ? 276 HIS A ND1 1 
ATOM   1866 C CD2 . HIS A 1 276 ? -2.144  39.780  -31.902 1.00 55.34  ? 276 HIS A CD2 1 
ATOM   1867 C CE1 . HIS A 1 276 ? -2.074  39.211  -29.790 1.00 53.55  ? 276 HIS A CE1 1 
ATOM   1868 N NE2 . HIS A 1 276 ? -1.633  38.867  -31.002 1.00 66.11  ? 276 HIS A NE2 1 
ATOM   1869 N N   . SER A 1 277 ? -3.645  43.580  -29.053 1.00 55.29  ? 277 SER A N   1 
ATOM   1870 C CA  . SER A 1 277 ? -3.413  43.705  -27.627 1.00 47.89  ? 277 SER A CA  1 
ATOM   1871 C C   . SER A 1 277 ? -3.652  42.345  -26.985 1.00 57.03  ? 277 SER A C   1 
ATOM   1872 O O   . SER A 1 277 ? -4.163  41.436  -27.637 1.00 51.97  ? 277 SER A O   1 
ATOM   1873 C CB  . SER A 1 277 ? -4.323  44.754  -27.002 1.00 49.20  ? 277 SER A CB  1 
ATOM   1874 O OG  . SER A 1 277 ? -5.653  44.288  -26.836 1.00 47.97  ? 277 SER A OG  1 
ATOM   1875 N N   . ASP A 1 278 ? -3.264  42.224  -25.711 1.00 50.93  ? 278 ASP A N   1 
ATOM   1876 C CA  . ASP A 1 278 ? -3.657  41.080  -24.906 1.00 55.05  ? 278 ASP A CA  1 
ATOM   1877 C C   . ASP A 1 278 ? -5.163  41.170  -24.680 1.00 53.18  ? 278 ASP A C   1 
ATOM   1878 O O   . ASP A 1 278 ? -5.705  42.265  -24.538 1.00 52.27  ? 278 ASP A O   1 
ATOM   1879 C CB  . ASP A 1 278 ? -2.929  41.040  -23.555 1.00 49.08  ? 278 ASP A CB  1 
ATOM   1880 C CG  . ASP A 1 278 ? -1.456  40.714  -23.637 1.00 52.51  ? 278 ASP A CG  1 
ATOM   1881 O OD1 . ASP A 1 278 ? -1.107  39.691  -24.271 1.00 56.62  ? 278 ASP A OD1 1 
ATOM   1882 O OD2 . ASP A 1 278 ? -0.655  41.464  -23.053 1.00 55.80  ? 278 ASP A OD2 1 
ATOM   1883 N N   . PRO A 1 279 ? -5.889  40.032  -24.631 1.00 51.67  ? 279 PRO A N   1 
ATOM   1884 C CA  . PRO A 1 279 ? -7.311  40.078  -24.324 1.00 43.06  ? 279 PRO A CA  1 
ATOM   1885 C C   . PRO A 1 279 ? -7.587  40.813  -23.016 1.00 52.26  ? 279 PRO A C   1 
ATOM   1886 O O   . PRO A 1 279 ? -6.805  40.711  -22.074 1.00 63.60  ? 279 PRO A O   1 
ATOM   1887 C CB  . PRO A 1 279 ? -7.713  38.602  -24.241 1.00 44.29  ? 279 PRO A CB  1 
ATOM   1888 C CG  . PRO A 1 279 ? -6.632  37.847  -24.938 1.00 55.05  ? 279 PRO A CG  1 
ATOM   1889 C CD  . PRO A 1 279 ? -5.373  38.668  -24.833 1.00 50.93  ? 279 PRO A CD  1 
ATOM   1890 N N   . TYR A 1 280 ? -8.680  41.582  -22.980 1.00 51.18  ? 280 TYR A N   1 
ATOM   1891 C CA  . TYR A 1 280 ? -9.157  42.160  -21.736 1.00 49.43  ? 280 TYR A CA  1 
ATOM   1892 C C   . TYR A 1 280 ? -10.671 42.336  -21.788 1.00 57.53  ? 280 TYR A C   1 
ATOM   1893 O O   . TYR A 1 280 ? -11.277 42.192  -22.849 1.00 60.54  ? 280 TYR A O   1 
ATOM   1894 C CB  . TYR A 1 280 ? -8.449  43.488  -21.421 1.00 49.62  ? 280 TYR A CB  1 
ATOM   1895 C CG  . TYR A 1 280 ? -8.749  44.635  -22.364 1.00 55.74  ? 280 TYR A CG  1 
ATOM   1896 C CD1 . TYR A 1 280 ? -8.264  44.640  -23.667 1.00 59.25  ? 280 TYR A CD1 1 
ATOM   1897 C CD2 . TYR A 1 280 ? -9.501  45.725  -21.948 1.00 54.00  ? 280 TYR A CD2 1 
ATOM   1898 C CE1 . TYR A 1 280 ? -8.527  45.697  -24.533 1.00 55.66  ? 280 TYR A CE1 1 
ATOM   1899 C CE2 . TYR A 1 280 ? -9.769  46.789  -22.802 1.00 55.97  ? 280 TYR A CE2 1 
ATOM   1900 C CZ  . TYR A 1 280 ? -9.285  46.770  -24.098 1.00 57.76  ? 280 TYR A CZ  1 
ATOM   1901 O OH  . TYR A 1 280 ? -9.553  47.826  -24.935 1.00 47.71  ? 280 TYR A OH  1 
ATOM   1902 N N   . TYR A 1 281 ? -11.260 42.616  -20.618 1.00 50.95  ? 281 TYR A N   1 
ATOM   1903 C CA  . TYR A 1 281 ? -12.664 42.969  -20.514 1.00 43.35  ? 281 TYR A CA  1 
ATOM   1904 C C   . TYR A 1 281 ? -12.844 44.468  -20.761 1.00 62.26  ? 281 TYR A C   1 
ATOM   1905 O O   . TYR A 1 281 ? -12.309 45.292  -20.020 1.00 59.93  ? 281 TYR A O   1 
ATOM   1906 C CB  . TYR A 1 281 ? -13.235 42.585  -19.135 1.00 53.28  ? 281 TYR A CB  1 
ATOM   1907 C CG  . TYR A 1 281 ? -13.256 41.097  -18.856 1.00 48.94  ? 281 TYR A CG  1 
ATOM   1908 C CD1 . TYR A 1 281 ? -12.156 40.454  -18.304 1.00 49.97  ? 281 TYR A CD1 1 
ATOM   1909 C CD2 . TYR A 1 281 ? -14.367 40.328  -19.170 1.00 46.66  ? 281 TYR A CD2 1 
ATOM   1910 C CE1 . TYR A 1 281 ? -12.170 39.085  -18.051 1.00 51.04  ? 281 TYR A CE1 1 
ATOM   1911 C CE2 . TYR A 1 281 ? -14.390 38.958  -18.931 1.00 55.73  ? 281 TYR A CE2 1 
ATOM   1912 C CZ  . TYR A 1 281 ? -13.293 38.339  -18.362 1.00 58.19  ? 281 TYR A CZ  1 
ATOM   1913 O OH  . TYR A 1 281 ? -13.327 36.981  -18.128 1.00 56.01  ? 281 TYR A OH  1 
ATOM   1914 N N   . LYS A 1 282 ? -13.603 44.818  -21.807 1.00 51.11  ? 282 LYS A N   1 
ATOM   1915 C CA  . LYS A 1 282 ? -13.927 46.209  -22.069 1.00 53.16  ? 282 LYS A CA  1 
ATOM   1916 C C   . LYS A 1 282 ? -15.131 46.600  -21.217 1.00 57.35  ? 282 LYS A C   1 
ATOM   1917 O O   . LYS A 1 282 ? -16.188 45.974  -21.286 1.00 53.09  ? 282 LYS A O   1 
ATOM   1918 C CB  . LYS A 1 282 ? -14.185 46.459  -23.560 1.00 49.56  ? 282 LYS A CB  1 
ATOM   1919 C CG  . LYS A 1 282 ? -14.538 47.910  -23.878 1.00 61.49  ? 282 LYS A CG  1 
ATOM   1920 C CD  . LYS A 1 282 ? -14.494 48.234  -25.388 1.00 52.08  ? 282 LYS A CD  1 
ATOM   1921 C CE  . LYS A 1 282 ? -13.106 48.522  -25.901 1.00 45.60  ? 282 LYS A CE  1 
ATOM   1922 N NZ  . LYS A 1 282 ? -12.647 49.872  -25.493 1.00 57.46  ? 282 LYS A NZ  1 
ATOM   1923 N N   . GLU A 1 283 ? -14.933 47.640  -20.402 1.00 62.18  ? 283 GLU A N   1 
ATOM   1924 C CA  . GLU A 1 283 ? -15.966 48.180  -19.540 1.00 60.13  ? 283 GLU A CA  1 
ATOM   1925 C C   . GLU A 1 283 ? -16.737 49.239  -20.321 1.00 64.53  ? 283 GLU A C   1 
ATOM   1926 O O   . GLU A 1 283 ? -16.443 50.430  -20.233 1.00 69.14  ? 283 GLU A O   1 
ATOM   1927 C CB  . GLU A 1 283 ? -15.337 48.769  -18.276 1.00 64.46  ? 283 GLU A CB  1 
ATOM   1928 N N   . VAL A 1 284 ? -17.712 48.776  -21.109 1.00 69.89  ? 284 VAL A N   1 
ATOM   1929 C CA  . VAL A 1 284 ? -18.504 49.647  -21.959 1.00 73.81  ? 284 VAL A CA  1 
ATOM   1930 C C   . VAL A 1 284 ? -19.983 49.377  -21.703 1.00 77.42  ? 284 VAL A C   1 
ATOM   1931 O O   . VAL A 1 284 ? -20.350 48.268  -21.317 1.00 68.96  ? 284 VAL A O   1 
ATOM   1932 C CB  . VAL A 1 284 ? -18.137 49.453  -23.448 1.00 66.79  ? 284 VAL A CB  1 
ATOM   1933 N N   . ASN A 1 285 ? -20.807 50.417  -21.899 1.00 87.39  ? 285 ASN A N   1 
ATOM   1934 C CA  . ASN A 1 285 ? -22.256 50.345  -21.762 1.00 85.31  ? 285 ASN A CA  1 
ATOM   1935 C C   . ASN A 1 285 ? -22.739 49.598  -20.518 1.00 86.16  ? 285 ASN A C   1 
ATOM   1936 O O   . ASN A 1 285 ? -23.788 48.957  -20.550 1.00 80.35  ? 285 ASN A O   1 
ATOM   1937 C CB  . ASN A 1 285 ? -22.861 49.704  -23.019 1.00 84.75  ? 285 ASN A CB  1 
ATOM   1938 N N   . GLY A 1 286 ? -21.972 49.703  -19.424 1.00 81.45  ? 286 GLY A N   1 
ATOM   1939 C CA  . GLY A 1 286 ? -22.268 48.988  -18.192 1.00 73.38  ? 286 GLY A CA  1 
ATOM   1940 C C   . GLY A 1 286 ? -22.134 47.471  -18.305 1.00 83.27  ? 286 GLY A C   1 
ATOM   1941 O O   . GLY A 1 286 ? -22.797 46.735  -17.576 1.00 83.22  ? 286 GLY A O   1 
ATOM   1942 N N   . ASP A 1 287 ? -21.258 47.019  -19.213 1.00 84.34  ? 287 ASP A N   1 
ATOM   1943 C CA  . ASP A 1 287 ? -21.043 45.602  -19.458 1.00 79.72  ? 287 ASP A CA  1 
ATOM   1944 C C   . ASP A 1 287 ? -19.554 45.270  -19.487 1.00 68.93  ? 287 ASP A C   1 
ATOM   1945 O O   . ASP A 1 287 ? -18.727 46.139  -19.757 1.00 69.38  ? 287 ASP A O   1 
ATOM   1946 C CB  . ASP A 1 287 ? -21.701 45.191  -20.784 1.00 78.57  ? 287 ASP A CB  1 
ATOM   1947 N N   . LYS A 1 288 ? -19.238 44.003  -19.183 1.00 75.00  ? 288 LYS A N   1 
ATOM   1948 C CA  . LYS A 1 288 ? -17.899 43.455  -19.321 1.00 69.68  ? 288 LYS A CA  1 
ATOM   1949 C C   . LYS A 1 288 ? -17.830 42.578  -20.567 1.00 64.70  ? 288 LYS A C   1 
ATOM   1950 O O   . LYS A 1 288 ? -18.262 41.427  -20.537 1.00 67.37  ? 288 LYS A O   1 
ATOM   1951 C CB  . LYS A 1 288 ? -17.508 42.613  -18.092 1.00 68.28  ? 288 LYS A CB  1 
ATOM   1952 C CG  . LYS A 1 288 ? -16.987 43.416  -16.917 1.00 69.08  ? 288 LYS A CG  1 
ATOM   1953 C CD  . LYS A 1 288 ? -16.351 42.527  -15.867 1.00 67.09  ? 288 LYS A CD  1 
ATOM   1954 C CE  . LYS A 1 288 ? -15.719 43.315  -14.743 1.00 89.54  ? 288 LYS A CE  1 
ATOM   1955 N NZ  . LYS A 1 288 ? -16.712 44.173  -14.039 1.00 85.39  ? 288 LYS A NZ  1 
ATOM   1956 N N   . ILE A 1 289 ? -17.285 43.133  -21.655 1.00 57.03  ? 289 ILE A N   1 
ATOM   1957 C CA  . ILE A 1 289 ? -17.116 42.389  -22.892 1.00 53.95  ? 289 ILE A CA  1 
ATOM   1958 C C   . ILE A 1 289 ? -15.644 42.018  -23.048 1.00 56.56  ? 289 ILE A C   1 
ATOM   1959 O O   . ILE A 1 289 ? -14.776 42.889  -23.046 1.00 50.20  ? 289 ILE A O   1 
ATOM   1960 C CB  . ILE A 1 289 ? -17.648 43.184  -24.109 1.00 61.51  ? 289 ILE A CB  1 
ATOM   1961 C CG1 . ILE A 1 289 ? -19.102 43.683  -23.865 1.00 59.42  ? 289 ILE A CG1 1 
ATOM   1962 C CG2 . ILE A 1 289 ? -17.547 42.349  -25.396 1.00 50.39  ? 289 ILE A CG2 1 
ATOM   1963 C CD1 . ILE A 1 289 ? -19.585 44.698  -24.845 1.00 55.56  ? 289 ILE A CD1 1 
ATOM   1964 N N   . TYR A 1 290 ? -15.385 40.713  -23.174 1.00 60.97  ? 290 TYR A N   1 
ATOM   1965 C CA  . TYR A 1 290 ? -14.042 40.186  -23.331 1.00 54.65  ? 290 TYR A CA  1 
ATOM   1966 C C   . TYR A 1 290 ? -13.607 40.303  -24.786 1.00 46.63  ? 290 TYR A C   1 
ATOM   1967 O O   . TYR A 1 290 ? -14.338 39.886  -25.678 1.00 52.80  ? 290 TYR A O   1 
ATOM   1968 C CB  . TYR A 1 290 ? -13.994 38.718  -22.900 1.00 53.73  ? 290 TYR A CB  1 
ATOM   1969 C CG  . TYR A 1 290 ? -12.605 38.225  -22.567 1.00 50.39  ? 290 TYR A CG  1 
ATOM   1970 C CD1 . TYR A 1 290 ? -11.914 38.724  -21.474 1.00 51.85  ? 290 TYR A CD1 1 
ATOM   1971 C CD2 . TYR A 1 290 ? -11.983 37.255  -23.343 1.00 53.06  ? 290 TYR A CD2 1 
ATOM   1972 C CE1 . TYR A 1 290 ? -10.636 38.275  -21.159 1.00 54.34  ? 290 TYR A CE1 1 
ATOM   1973 C CE2 . TYR A 1 290 ? -10.704 36.795  -23.038 1.00 56.64  ? 290 TYR A CE2 1 
ATOM   1974 C CZ  . TYR A 1 290 ? -10.034 37.308  -21.942 1.00 53.91  ? 290 TYR A CZ  1 
ATOM   1975 O OH  . TYR A 1 290 ? -8.776  36.867  -21.613 1.00 57.80  ? 290 TYR A OH  1 
ATOM   1976 N N   . GLY A 1 291 ? -12.413 40.861  -25.012 1.00 49.06  ? 291 GLY A N   1 
ATOM   1977 C CA  . GLY A 1 291 ? -11.860 40.948  -26.353 1.00 45.09  ? 291 GLY A CA  1 
ATOM   1978 C C   . GLY A 1 291 ? -10.450 41.533  -26.418 1.00 56.53  ? 291 GLY A C   1 
ATOM   1979 O O   . GLY A 1 291 ? -9.801  41.718  -25.391 1.00 46.34  ? 291 GLY A O   1 
ATOM   1980 N N   . MET A 1 292 ? -9.995  41.821  -27.645 1.00 47.57  ? 292 MET A N   1 
ATOM   1981 C CA  . MET A 1 292 ? -8.722  42.485  -27.864 1.00 47.24  ? 292 MET A CA  1 
ATOM   1982 C C   . MET A 1 292 ? -8.871  43.567  -28.927 1.00 54.24  ? 292 MET A C   1 
ATOM   1983 O O   . MET A 1 292 ? -9.779  43.516  -29.755 1.00 58.35  ? 292 MET A O   1 
ATOM   1984 C CB  . MET A 1 292 ? -7.635  41.494  -28.316 1.00 53.79  ? 292 MET A CB  1 
ATOM   1985 C CG  . MET A 1 292 ? -8.088  40.560  -29.412 1.00 61.12  ? 292 MET A CG  1 
ATOM   1986 S SD  . MET A 1 292 ? -6.723  39.659  -30.166 1.00 57.18  ? 292 MET A SD  1 
ATOM   1987 C CE  . MET A 1 292 ? -6.275  38.588  -28.801 1.00 56.75  ? 292 MET A CE  1 
ATOM   1988 N N   . ASP A 1 293 ? -7.951  44.536  -28.890 1.00 55.01  ? 293 ASP A N   1 
ATOM   1989 C CA  . ASP A 1 293 ? -7.864  45.555  -29.918 1.00 51.54  ? 293 ASP A CA  1 
ATOM   1990 C C   . ASP A 1 293 ? -6.926  45.080  -31.022 1.00 61.47  ? 293 ASP A C   1 
ATOM   1991 O O   . ASP A 1 293 ? -5.899  44.472  -30.731 1.00 55.87  ? 293 ASP A O   1 
ATOM   1992 C CB  . ASP A 1 293 ? -7.376  46.867  -29.327 1.00 50.12  ? 293 ASP A CB  1 
ATOM   1993 C CG  . ASP A 1 293 ? -8.372  47.467  -28.378 1.00 52.49  ? 293 ASP A CG  1 
ATOM   1994 O OD1 . ASP A 1 293 ? -9.500  47.765  -28.818 1.00 50.65  ? 293 ASP A OD1 1 
ATOM   1995 O OD2 . ASP A 1 293 ? -8.030  47.630  -27.191 1.00 60.34  ? 293 ASP A OD2 1 
ATOM   1996 N N   . ILE A 1 294 ? -7.330  45.333  -32.275 1.00 49.15  ? 294 ILE A N   1 
ATOM   1997 C CA  . ILE A 1 294 ? -6.515  45.085  -33.452 1.00 55.89  ? 294 ILE A CA  1 
ATOM   1998 C C   . ILE A 1 294 ? -6.199  46.441  -34.073 1.00 55.04  ? 294 ILE A C   1 
ATOM   1999 O O   . ILE A 1 294 ? -7.113  47.141  -34.497 1.00 48.06  ? 294 ILE A O   1 
ATOM   2000 C CB  . ILE A 1 294 ? -7.248  44.177  -34.459 1.00 55.83  ? 294 ILE A CB  1 
ATOM   2001 C CG1 . ILE A 1 294 ? -7.673  42.840  -33.820 1.00 46.99  ? 294 ILE A CG1 1 
ATOM   2002 C CG2 . ILE A 1 294 ? -6.417  43.955  -35.734 1.00 43.67  ? 294 ILE A CG2 1 
ATOM   2003 C CD1 . ILE A 1 294 ? -6.574  42.038  -33.333 1.00 56.13  ? 294 ILE A CD1 1 
ATOM   2004 N N   . THR A 1 295 ? -4.911  46.811  -34.111 1.00 56.60  ? 295 THR A N   1 
ATOM   2005 C CA  . THR A 1 295 ? -4.518  48.111  -34.629 1.00 49.29  ? 295 THR A CA  1 
ATOM   2006 C C   . THR A 1 295 ? -3.737  47.933  -35.927 1.00 49.10  ? 295 THR A C   1 
ATOM   2007 O O   . THR A 1 295 ? -2.756  47.196  -35.975 1.00 55.74  ? 295 THR A O   1 
ATOM   2008 C CB  . THR A 1 295 ? -3.743  48.900  -33.583 1.00 55.28  ? 295 THR A CB  1 
ATOM   2009 O OG1 . THR A 1 295 ? -4.275  48.628  -32.292 1.00 55.89  ? 295 THR A OG1 1 
ATOM   2010 C CG2 . THR A 1 295 ? -3.785  50.396  -33.841 1.00 45.51  ? 295 THR A CG2 1 
ATOM   2011 N N   . LEU A 1 296 ? -4.225  48.592  -36.984 1.00 59.51  ? 296 LEU A N   1 
ATOM   2012 C CA  . LEU A 1 296 ? -3.566  48.630  -38.276 1.00 50.59  ? 296 LEU A CA  1 
ATOM   2013 C C   . LEU A 1 296 ? -3.073  50.058  -38.469 1.00 57.10  ? 296 LEU A C   1 
ATOM   2014 O O   . LEU A 1 296 ? -3.828  51.003  -38.241 1.00 51.26  ? 296 LEU A O   1 
ATOM   2015 C CB  . LEU A 1 296 ? -4.523  48.276  -39.417 1.00 49.81  ? 296 LEU A CB  1 
ATOM   2016 C CG  . LEU A 1 296 ? -4.868  46.815  -39.614 1.00 60.85  ? 296 LEU A CG  1 
ATOM   2017 C CD1 . LEU A 1 296 ? -5.868  46.327  -38.577 1.00 60.30  ? 296 LEU A CD1 1 
ATOM   2018 C CD2 . LEU A 1 296 ? -5.425  46.583  -41.013 1.00 55.97  ? 296 LEU A CD2 1 
ATOM   2019 N N   . PRO A 1 297 ? -1.807  50.266  -38.896 1.00 49.39  ? 297 PRO A N   1 
ATOM   2020 C CA  . PRO A 1 297 ? -1.343  51.600  -39.238 1.00 52.59  ? 297 PRO A CA  1 
ATOM   2021 C C   . PRO A 1 297 ? -1.900  52.055  -40.581 1.00 52.93  ? 297 PRO A C   1 
ATOM   2022 O O   . PRO A 1 297 ? -2.041  51.245  -41.495 1.00 47.80  ? 297 PRO A O   1 
ATOM   2023 C CB  . PRO A 1 297 ? 0.179   51.442  -39.260 1.00 48.53  ? 297 PRO A CB  1 
ATOM   2024 C CG  . PRO A 1 297 ? 0.400   50.022  -39.644 1.00 51.51  ? 297 PRO A CG  1 
ATOM   2025 C CD  . PRO A 1 297 ? -0.784  49.230  -39.113 1.00 55.65  ? 297 PRO A CD  1 
ATOM   2026 N N   . LEU A 1 298 ? -2.238  53.345  -40.672 1.00 50.48  ? 298 LEU A N   1 
ATOM   2027 C CA  . LEU A 1 298 ? -2.659  53.947  -41.926 1.00 64.55  ? 298 LEU A CA  1 
ATOM   2028 C C   . LEU A 1 298 ? -1.446  54.609  -42.578 1.00 58.98  ? 298 LEU A C   1 
ATOM   2029 O O   . LEU A 1 298 ? -1.025  55.686  -42.162 1.00 61.35  ? 298 LEU A O   1 
ATOM   2030 C CB  . LEU A 1 298 ? -3.784  54.953  -41.665 1.00 59.06  ? 298 LEU A CB  1 
ATOM   2031 C CG  . LEU A 1 298 ? -5.058  54.363  -41.035 1.00 62.96  ? 298 LEU A CG  1 
ATOM   2032 C CD1 . LEU A 1 298 ? -6.070  55.450  -40.728 1.00 51.46  ? 298 LEU A CD1 1 
ATOM   2033 C CD2 . LEU A 1 298 ? -5.684  53.303  -41.927 1.00 53.73  ? 298 LEU A CD2 1 
ATOM   2034 N N   . MET A 1 299 ? -0.884  53.933  -43.590 1.00 58.27  ? 299 MET A N   1 
ATOM   2035 C CA  . MET A 1 299 ? 0.342   54.357  -44.251 1.00 78.91  ? 299 MET A CA  1 
ATOM   2036 C C   . MET A 1 299 ? 1.500   54.284  -43.252 1.00 86.58  ? 299 MET A C   1 
ATOM   2037 O O   . MET A 1 299 ? 1.285   54.127  -42.051 1.00 86.79  ? 299 MET A O   1 
ATOM   2038 C CB  . MET A 1 299 ? 0.133   55.759  -44.905 1.00 81.99  ? 299 MET A CB  1 
ATOM   2039 C CG  . MET A 1 299 ? 1.354   56.658  -44.929 1.00 93.33  ? 299 MET A CG  1 
ATOM   2040 S SD  . MET A 1 299 ? 1.039   58.273  -45.692 1.00 111.87 ? 299 MET A SD  1 
ATOM   2041 C CE  . MET A 1 299 ? 0.390   57.781  -47.276 1.00 92.18  ? 299 MET A CE  1 
ATOM   2042 N N   . GLY A 1 300 ? 2.737   54.327  -43.759 1.00 94.67  ? 300 GLY A N   1 
ATOM   2043 C CA  . GLY A 1 300 ? 3.912   54.273  -42.904 1.00 102.16 ? 300 GLY A CA  1 
ATOM   2044 C C   . GLY A 1 300 ? 5.215   54.628  -43.617 1.00 97.77  ? 300 GLY A C   1 
ATOM   2045 O O   . GLY A 1 300 ? 6.094   53.781  -43.759 1.00 99.99  ? 300 GLY A O   1 
ATOM   2046 N N   . LYS A 1 301 ? 5.320   55.889  -44.056 1.00 95.73  ? 301 LYS A N   1 
ATOM   2047 C CA  . LYS A 1 301 ? 6.533   56.407  -44.667 1.00 99.21  ? 301 LYS A CA  1 
ATOM   2048 C C   . LYS A 1 301 ? 7.057   57.574  -43.833 1.00 109.75 ? 301 LYS A C   1 
ATOM   2049 O O   . LYS A 1 301 ? 6.859   58.735  -44.190 1.00 109.08 ? 301 LYS A O   1 
ATOM   2050 C CB  . LYS A 1 301 ? 6.272   56.836  -46.121 1.00 84.64  ? 301 LYS A CB  1 
ATOM   2051 N N   . ASN A 1 302 ? 7.716   57.239  -42.713 1.00 105.97 ? 302 ASN A N   1 
ATOM   2052 C CA  . ASN A 1 302 ? 8.295   58.215  -41.802 1.00 102.98 ? 302 ASN A CA  1 
ATOM   2053 C C   . ASN A 1 302 ? 7.256   59.225  -41.310 1.00 102.91 ? 302 ASN A C   1 
ATOM   2054 O O   . ASN A 1 302 ? 6.107   58.862  -41.067 1.00 97.98  ? 302 ASN A O   1 
ATOM   2055 C CB  . ASN A 1 302 ? 9.473   58.943  -42.462 1.00 99.84  ? 302 ASN A CB  1 
ATOM   2056 N N   . ALA A 1 305 ? 2.540   57.697  -41.712 1.00 84.44  ? 305 ALA A N   1 
ATOM   2057 C CA  . ALA A 1 305 ? 1.828   57.464  -40.459 1.00 74.97  ? 305 ALA A CA  1 
ATOM   2058 C C   . ALA A 1 305 ? 0.796   58.561  -40.212 1.00 74.69  ? 305 ALA A C   1 
ATOM   2059 O O   . ALA A 1 305 ? 1.030   59.471  -39.418 1.00 73.67  ? 305 ALA A O   1 
ATOM   2060 C CB  . ALA A 1 305 ? 2.812   57.389  -39.302 1.00 82.26  ? 305 ALA A CB  1 
ATOM   2061 N N   . ILE A 1 306 ? -0.344  58.460  -40.910 1.00 63.55  ? 306 ILE A N   1 
ATOM   2062 C CA  . ILE A 1 306 ? -1.417  59.435  -40.790 1.00 75.63  ? 306 ILE A CA  1 
ATOM   2063 C C   . ILE A 1 306 ? -2.195  59.156  -39.505 1.00 72.15  ? 306 ILE A C   1 
ATOM   2064 O O   . ILE A 1 306 ? -2.808  60.055  -38.930 1.00 71.39  ? 306 ILE A O   1 
ATOM   2065 C CB  . ILE A 1 306 ? -2.356  59.436  -42.037 1.00 72.46  ? 306 ILE A CB  1 
ATOM   2066 C CG1 . ILE A 1 306 ? -3.476  58.388  -41.927 1.00 74.72  ? 306 ILE A CG1 1 
ATOM   2067 C CG2 . ILE A 1 306 ? -1.578  59.261  -43.340 1.00 75.32  ? 306 ILE A CG2 1 
ATOM   2068 N N   . GLY A 1 307 ? -2.156  57.888  -39.076 1.00 71.37  ? 307 GLY A N   1 
ATOM   2069 C CA  . GLY A 1 307 ? -2.886  57.423  -37.912 1.00 65.24  ? 307 GLY A CA  1 
ATOM   2070 C C   . GLY A 1 307 ? -3.061  55.909  -37.965 1.00 60.14  ? 307 GLY A C   1 
ATOM   2071 O O   . GLY A 1 307 ? -2.220  55.209  -38.527 1.00 52.22  ? 307 GLY A O   1 
ATOM   2072 N N   . ALA A 1 308 ? -4.168  55.421  -37.392 1.00 59.41  ? 308 ALA A N   1 
ATOM   2073 C CA  . ALA A 1 308 ? -4.433  53.994  -37.323 1.00 47.83  ? 308 ALA A CA  1 
ATOM   2074 C C   . ALA A 1 308 ? -5.925  53.675  -37.346 1.00 52.76  ? 308 ALA A C   1 
ATOM   2075 O O   . ALA A 1 308 ? -6.739  54.394  -36.767 1.00 51.93  ? 308 ALA A O   1 
ATOM   2076 C CB  . ALA A 1 308 ? -3.805  53.407  -36.072 1.00 50.66  ? 308 ALA A CB  1 
ATOM   2077 N N   . LEU A 1 309 ? -6.258  52.582  -38.040 1.00 57.72  ? 309 LEU A N   1 
ATOM   2078 C CA  . LEU A 1 309 ? -7.529  51.901  -37.881 1.00 55.76  ? 309 LEU A CA  1 
ATOM   2079 C C   . LEU A 1 309 ? -7.412  50.874  -36.758 1.00 57.38  ? 309 LEU A C   1 
ATOM   2080 O O   . LEU A 1 309 ? -6.672  49.896  -36.880 1.00 50.75  ? 309 LEU A O   1 
ATOM   2081 C CB  . LEU A 1 309 ? -7.930  51.209  -39.186 1.00 52.74  ? 309 LEU A CB  1 
ATOM   2082 C CG  . LEU A 1 309 ? -9.004  50.132  -39.061 1.00 51.84  ? 309 LEU A CG  1 
ATOM   2083 C CD1 . LEU A 1 309 ? -10.262 50.688  -38.446 1.00 57.53  ? 309 LEU A CD1 1 
ATOM   2084 C CD2 . LEU A 1 309 ? -9.296  49.520  -40.402 1.00 53.12  ? 309 LEU A CD2 1 
ATOM   2085 N N   . ASN A 1 310 ? -8.158  51.118  -35.673 1.00 54.92  ? 310 ASN A N   1 
ATOM   2086 C CA  . ASN A 1 310 ? -8.265  50.187  -34.563 1.00 51.88  ? 310 ASN A CA  1 
ATOM   2087 C C   . ASN A 1 310 ? -9.710  49.726  -34.394 1.00 49.18  ? 310 ASN A C   1 
ATOM   2088 O O   . ASN A 1 310 ? -10.631 50.539  -34.446 1.00 53.23  ? 310 ASN A O   1 
ATOM   2089 C CB  . ASN A 1 310 ? -7.778  50.834  -33.277 1.00 57.14  ? 310 ASN A CB  1 
ATOM   2090 C CG  . ASN A 1 310 ? -7.782  49.883  -32.103 1.00 52.02  ? 310 ASN A CG  1 
ATOM   2091 O OD1 . ASN A 1 310 ? -7.064  48.878  -32.088 1.00 56.93  ? 310 ASN A OD1 1 
ATOM   2092 N ND2 . ASN A 1 310 ? -8.588  50.168  -31.099 1.00 46.85  ? 310 ASN A ND2 1 
ATOM   2093 N N   . PHE A 1 311 ? -9.901  48.415  -34.204 1.00 47.15  ? 311 PHE A N   1 
ATOM   2094 C CA  . PHE A 1 311 ? -11.200 47.889  -33.819 1.00 54.17  ? 311 PHE A CA  1 
ATOM   2095 C C   . PHE A 1 311 ? -11.078 46.954  -32.617 1.00 49.71  ? 311 PHE A C   1 
ATOM   2096 O O   . PHE A 1 311 ? -10.042 46.328  -32.405 1.00 42.63  ? 311 PHE A O   1 
ATOM   2097 C CB  . PHE A 1 311 ? -11.900 47.173  -34.984 1.00 45.52  ? 311 PHE A CB  1 
ATOM   2098 C CG  . PHE A 1 311 ? -11.129 46.053  -35.636 1.00 46.12  ? 311 PHE A CG  1 
ATOM   2099 C CD1 . PHE A 1 311 ? -10.168 46.318  -36.594 1.00 52.95  ? 311 PHE A CD1 1 
ATOM   2100 C CD2 . PHE A 1 311 ? -11.378 44.733  -35.304 1.00 50.13  ? 311 PHE A CD2 1 
ATOM   2101 C CE1 . PHE A 1 311 ? -9.474  45.283  -37.208 1.00 57.37  ? 311 PHE A CE1 1 
ATOM   2102 C CE2 . PHE A 1 311 ? -10.674 43.700  -35.914 1.00 53.03  ? 311 PHE A CE2 1 
ATOM   2103 C CZ  . PHE A 1 311 ? -9.729  43.981  -36.863 1.00 52.66  ? 311 PHE A CZ  1 
ATOM   2104 N N   . PHE A 1 312 ? -12.154 46.889  -31.828 1.00 40.26  ? 312 PHE A N   1 
ATOM   2105 C CA  . PHE A 1 312 ? -12.214 46.005  -30.680 1.00 44.16  ? 312 PHE A CA  1 
ATOM   2106 C C   . PHE A 1 312 ? -12.938 44.720  -31.064 1.00 42.21  ? 312 PHE A C   1 
ATOM   2107 O O   . PHE A 1 312 ? -14.149 44.730  -31.286 1.00 40.59  ? 312 PHE A O   1 
ATOM   2108 C CB  . PHE A 1 312 ? -12.905 46.679  -29.499 1.00 47.36  ? 312 PHE A CB  1 
ATOM   2109 C CG  . PHE A 1 312 ? -12.888 45.813  -28.267 1.00 48.34  ? 312 PHE A CG  1 
ATOM   2110 C CD1 . PHE A 1 312 ? -11.723 45.644  -27.535 1.00 46.28  ? 312 PHE A CD1 1 
ATOM   2111 C CD2 . PHE A 1 312 ? -14.030 45.133  -27.858 1.00 46.61  ? 312 PHE A CD2 1 
ATOM   2112 C CE1 . PHE A 1 312 ? -11.710 44.837  -26.401 1.00 51.99  ? 312 PHE A CE1 1 
ATOM   2113 C CE2 . PHE A 1 312 ? -14.011 44.322  -26.727 1.00 43.65  ? 312 PHE A CE2 1 
ATOM   2114 C CZ  . PHE A 1 312 ? -12.856 44.178  -26.008 1.00 48.49  ? 312 PHE A CZ  1 
ATOM   2115 N N   . LEU A 1 313 ? -12.172 43.626  -31.136 1.00 44.47  ? 313 LEU A N   1 
ATOM   2116 C CA  . LEU A 1 313 ? -12.712 42.317  -31.459 1.00 41.08  ? 313 LEU A CA  1 
ATOM   2117 C C   . LEU A 1 313 ? -13.396 41.768  -30.216 1.00 48.85  ? 313 LEU A C   1 
ATOM   2118 O O   . LEU A 1 313 ? -12.744 41.589  -29.190 1.00 49.90  ? 313 LEU A O   1 
ATOM   2119 C CB  . LEU A 1 313 ? -11.604 41.365  -31.919 1.00 44.32  ? 313 LEU A CB  1 
ATOM   2120 C CG  . LEU A 1 313 ? -12.037 39.945  -32.217 1.00 50.73  ? 313 LEU A CG  1 
ATOM   2121 C CD1 . LEU A 1 313 ? -13.061 39.909  -33.336 1.00 57.08  ? 313 LEU A CD1 1 
ATOM   2122 C CD2 . LEU A 1 313 ? -10.856 39.092  -32.579 1.00 47.62  ? 313 LEU A CD2 1 
ATOM   2123 N N   . ASN A 1 314 ? -14.711 41.540  -30.332 1.00 48.61  ? 314 ASN A N   1 
ATOM   2124 C CA  . ASN A 1 314 ? -15.525 40.968  -29.273 1.00 46.80  ? 314 ASN A CA  1 
ATOM   2125 C C   . ASN A 1 314 ? -15.351 39.450  -29.283 1.00 49.13  ? 314 ASN A C   1 
ATOM   2126 O O   . ASN A 1 314 ? -15.898 38.758  -30.139 1.00 47.47  ? 314 ASN A O   1 
ATOM   2127 C CB  . ASN A 1 314 ? -17.002 41.386  -29.467 1.00 51.30  ? 314 ASN A CB  1 
ATOM   2128 C CG  . ASN A 1 314 ? -17.976 40.857  -28.435 1.00 47.62  ? 314 ASN A CG  1 
ATOM   2129 O OD1 . ASN A 1 314 ? -17.653 40.015  -27.597 1.00 55.20  ? 314 ASN A OD1 1 
ATOM   2130 N ND2 . ASN A 1 314 ? -19.203 41.338  -28.486 1.00 44.39  ? 314 ASN A ND2 1 
ATOM   2131 N N   . ILE A 1 315 ? -14.557 38.944  -28.334 1.00 55.15  ? 315 ILE A N   1 
ATOM   2132 C CA  . ILE A 1 315 ? -14.282 37.519  -28.239 1.00 50.59  ? 315 ILE A CA  1 
ATOM   2133 C C   . ILE A 1 315 ? -15.507 36.782  -27.702 1.00 47.73  ? 315 ILE A C   1 
ATOM   2134 O O   . ILE A 1 315 ? -15.785 35.660  -28.119 1.00 46.53  ? 315 ILE A O   1 
ATOM   2135 C CB  . ILE A 1 315 ? -12.999 37.274  -27.402 1.00 52.36  ? 315 ILE A CB  1 
ATOM   2136 C CG1 . ILE A 1 315 ? -11.753 37.678  -28.216 1.00 53.49  ? 315 ILE A CG1 1 
ATOM   2137 C CG2 . ILE A 1 315 ? -12.894 35.832  -26.910 1.00 49.87  ? 315 ILE A CG2 1 
ATOM   2138 C CD1 . ILE A 1 315 ? -10.403 37.565  -27.448 1.00 53.44  ? 315 ILE A CD1 1 
ATOM   2139 N N   . ASP A 1 316 ? -16.252 37.431  -26.798 1.00 53.35  ? 316 ASP A N   1 
ATOM   2140 C CA  . ASP A 1 316 ? -17.483 36.860  -26.273 1.00 54.55  ? 316 ASP A CA  1 
ATOM   2141 C C   . ASP A 1 316 ? -18.454 36.474  -27.389 1.00 55.61  ? 316 ASP A C   1 
ATOM   2142 O O   . ASP A 1 316 ? -19.217 35.524  -27.232 1.00 60.67  ? 316 ASP A O   1 
ATOM   2143 C CB  . ASP A 1 316 ? -18.174 37.813  -25.276 1.00 49.15  ? 316 ASP A CB  1 
ATOM   2144 C CG  . ASP A 1 316 ? -17.499 37.890  -23.918 1.00 58.45  ? 316 ASP A CG  1 
ATOM   2145 O OD1 . ASP A 1 316 ? -17.051 36.836  -23.418 1.00 55.53  ? 316 ASP A OD1 1 
ATOM   2146 O OD2 . ASP A 1 316 ? -17.458 38.996  -23.334 1.00 57.84  ? 316 ASP A OD2 1 
ATOM   2147 N N   . ALA A 1 317 ? -18.391 37.188  -28.522 1.00 51.75  ? 317 ALA A N   1 
ATOM   2148 C CA  . ALA A 1 317 ? -19.266 36.922  -29.654 1.00 54.68  ? 317 ALA A CA  1 
ATOM   2149 C C   . ALA A 1 317 ? -18.955 35.622  -30.397 1.00 58.25  ? 317 ALA A C   1 
ATOM   2150 O O   . ALA A 1 317 ? -19.753 35.183  -31.219 1.00 54.03  ? 317 ALA A O   1 
ATOM   2151 C CB  . ALA A 1 317 ? -19.215 38.086  -30.632 1.00 51.86  ? 317 ALA A CB  1 
ATOM   2152 N N   . PHE A 1 318 ? -17.794 35.015  -30.121 1.00 54.88  ? 318 PHE A N   1 
ATOM   2153 C CA  . PHE A 1 318 ? -17.441 33.739  -30.726 1.00 59.20  ? 318 PHE A CA  1 
ATOM   2154 C C   . PHE A 1 318 ? -17.933 32.540  -29.918 1.00 62.69  ? 318 PHE A C   1 
ATOM   2155 O O   . PHE A 1 318 ? -17.675 31.397  -30.293 1.00 66.35  ? 318 PHE A O   1 
ATOM   2156 C CB  . PHE A 1 318 ? -15.918 33.634  -30.913 1.00 63.33  ? 318 PHE A CB  1 
ATOM   2157 C CG  . PHE A 1 318 ? -15.413 34.580  -31.959 1.00 51.13  ? 318 PHE A CG  1 
ATOM   2158 C CD1 . PHE A 1 318 ? -15.279 35.929  -31.686 1.00 54.26  ? 318 PHE A CD1 1 
ATOM   2159 C CD2 . PHE A 1 318 ? -15.125 34.133  -33.234 1.00 56.81  ? 318 PHE A CD2 1 
ATOM   2160 C CE1 . PHE A 1 318 ? -14.842 36.808  -32.660 1.00 54.23  ? 318 PHE A CE1 1 
ATOM   2161 C CE2 . PHE A 1 318 ? -14.683 35.016  -34.209 1.00 51.76  ? 318 PHE A CE2 1 
ATOM   2162 C CZ  . PHE A 1 318 ? -14.545 36.347  -33.917 1.00 55.12  ? 318 PHE A CZ  1 
ATOM   2163 N N   . TYR A 1 319 ? -18.642 32.815  -28.815 1.00 57.03  ? 319 TYR A N   1 
ATOM   2164 C CA  . TYR A 1 319 ? -19.082 31.774  -27.902 1.00 64.95  ? 319 TYR A CA  1 
ATOM   2165 C C   . TYR A 1 319 ? -19.807 30.655  -28.641 1.00 66.46  ? 319 TYR A C   1 
ATOM   2166 O O   . TYR A 1 319 ? -19.404 29.497  -28.549 1.00 67.52  ? 319 TYR A O   1 
ATOM   2167 C CB  . TYR A 1 319 ? -19.973 32.361  -26.800 1.00 62.31  ? 319 TYR A CB  1 
ATOM   2168 C CG  . TYR A 1 319 ? -20.314 31.359  -25.725 1.00 58.93  ? 319 TYR A CG  1 
ATOM   2169 C CD1 . TYR A 1 319 ? -21.406 30.511  -25.857 1.00 54.66  ? 319 TYR A CD1 1 
ATOM   2170 C CD2 . TYR A 1 319 ? -19.521 31.228  -24.594 1.00 65.56  ? 319 TYR A CD2 1 
ATOM   2171 C CE1 . TYR A 1 319 ? -21.721 29.581  -24.874 1.00 71.59  ? 319 TYR A CE1 1 
ATOM   2172 C CE2 . TYR A 1 319 ? -19.820 30.294  -23.606 1.00 69.04  ? 319 TYR A CE2 1 
ATOM   2173 C CZ  . TYR A 1 319 ? -20.923 29.473  -23.749 1.00 74.97  ? 319 TYR A CZ  1 
ATOM   2174 O OH  . TYR A 1 319 ? -21.224 28.555  -22.775 1.00 71.64  ? 319 TYR A OH  1 
ATOM   2175 N N   . THR A 1 320 ? -20.858 31.018  -29.387 1.00 55.72  ? 320 THR A N   1 
ATOM   2176 C CA  . THR A 1 320 ? -21.686 30.029  -30.060 1.00 63.37  ? 320 THR A CA  1 
ATOM   2177 C C   . THR A 1 320 ? -20.907 29.388  -31.206 1.00 62.52  ? 320 THR A C   1 
ATOM   2178 O O   . THR A 1 320 ? -21.147 28.230  -31.547 1.00 66.08  ? 320 THR A O   1 
ATOM   2179 C CB  . THR A 1 320 ? -23.028 30.636  -30.522 1.00 68.21  ? 320 THR A CB  1 
ATOM   2180 N N   . ASP A 1 321 ? -19.963 30.143  -31.780 1.00 57.46  ? 321 ASP A N   1 
ATOM   2181 C CA  . ASP A 1 321 ? -19.083 29.619  -32.811 1.00 59.27  ? 321 ASP A CA  1 
ATOM   2182 C C   . ASP A 1 321 ? -18.136 28.534  -32.289 1.00 69.85  ? 321 ASP A C   1 
ATOM   2183 O O   . ASP A 1 321 ? -17.804 27.604  -33.024 1.00 74.32  ? 321 ASP A O   1 
ATOM   2184 C CB  . ASP A 1 321 ? -18.283 30.768  -33.452 1.00 67.88  ? 321 ASP A CB  1 
ATOM   2185 C CG  . ASP A 1 321 ? -19.117 31.840  -34.148 1.00 69.99  ? 321 ASP A CG  1 
ATOM   2186 O OD1 . ASP A 1 321 ? -20.351 31.664  -34.252 1.00 70.69  ? 321 ASP A OD1 1 
ATOM   2187 O OD2 . ASP A 1 321 ? -18.534 32.850  -34.592 1.00 69.05  ? 321 ASP A OD2 1 
ATOM   2188 N N   . VAL A 1 322 ? -17.725 28.640  -31.015 1.00 64.39  ? 322 VAL A N   1 
ATOM   2189 C CA  . VAL A 1 322 ? -16.755 27.724  -30.429 1.00 65.24  ? 322 VAL A CA  1 
ATOM   2190 C C   . VAL A 1 322 ? -17.416 26.602  -29.632 1.00 67.10  ? 322 VAL A C   1 
ATOM   2191 O O   . VAL A 1 322 ? -17.233 25.424  -29.936 1.00 63.98  ? 322 VAL A O   1 
ATOM   2192 C CB  . VAL A 1 322 ? -15.748 28.507  -29.554 1.00 55.82  ? 322 VAL A CB  1 
ATOM   2193 C CG1 . VAL A 1 322 ? -15.014 27.588  -28.580 1.00 62.41  ? 322 VAL A CG1 1 
ATOM   2194 C CG2 . VAL A 1 322 ? -14.761 29.289  -30.421 1.00 53.89  ? 322 VAL A CG2 1 
ATOM   2195 N N   . VAL A 1 323 ? -18.166 26.982  -28.593 1.00 65.47  ? 323 VAL A N   1 
ATOM   2196 C CA  . VAL A 1 323 ? -18.862 26.024  -27.751 1.00 61.50  ? 323 VAL A CA  1 
ATOM   2197 C C   . VAL A 1 323 ? -19.966 25.304  -28.521 1.00 61.45  ? 323 VAL A C   1 
ATOM   2198 O O   . VAL A 1 323 ? -20.108 24.091  -28.403 1.00 62.94  ? 323 VAL A O   1 
ATOM   2199 C CB  . VAL A 1 323 ? -19.412 26.730  -26.489 1.00 67.48  ? 323 VAL A CB  1 
ATOM   2200 C CG1 . VAL A 1 323 ? -20.515 25.914  -25.814 1.00 61.41  ? 323 VAL A CG1 1 
ATOM   2201 C CG2 . VAL A 1 323 ? -18.284 27.046  -25.516 1.00 69.92  ? 323 VAL A CG2 1 
ATOM   2202 N N   . GLY A 1 324 ? -20.741 26.064  -29.306 1.00 75.44  ? 324 GLY A N   1 
ATOM   2203 C CA  . GLY A 1 324 ? -21.902 25.537  -30.006 1.00 65.37  ? 324 GLY A CA  1 
ATOM   2204 C C   . GLY A 1 324 ? -23.196 26.147  -29.476 1.00 66.16  ? 324 GLY A C   1 
ATOM   2205 O O   . GLY A 1 324 ? -23.175 26.909  -28.512 1.00 69.96  ? 324 GLY A O   1 
ATOM   2206 N N   . LYS A 1 325 ? -24.317 25.800  -30.116 1.00 76.39  ? 325 LYS A N   1 
ATOM   2207 C CA  . LYS A 1 325 ? -25.622 26.302  -29.714 1.00 70.99  ? 325 LYS A CA  1 
ATOM   2208 C C   . LYS A 1 325 ? -26.091 25.608  -28.437 1.00 73.57  ? 325 LYS A C   1 
ATOM   2209 O O   . LYS A 1 325 ? -26.932 26.143  -27.719 1.00 74.17  ? 325 LYS A O   1 
ATOM   2210 C CB  . LYS A 1 325 ? -26.663 26.123  -30.838 1.00 78.92  ? 325 LYS A CB  1 
ATOM   2211 C CG  . LYS A 1 325 ? -26.536 27.121  -32.000 1.00 72.94  ? 325 LYS A CG  1 
ATOM   2212 C CD  . LYS A 1 325 ? -25.344 26.856  -32.917 1.00 73.92  ? 325 LYS A CD  1 
ATOM   2213 N N   . LYS A 1 326 ? -25.545 24.411  -28.178 1.00 79.76  ? 326 LYS A N   1 
ATOM   2214 C CA  . LYS A 1 326 ? -25.717 23.719  -26.909 1.00 75.55  ? 326 LYS A CA  1 
ATOM   2215 C C   . LYS A 1 326 ? -24.396 23.720  -26.145 1.00 74.51  ? 326 LYS A C   1 
ATOM   2216 O O   . LYS A 1 326 ? -23.327 23.819  -26.746 1.00 62.44  ? 326 LYS A O   1 
ATOM   2217 C CB  . LYS A 1 326 ? -26.198 22.274  -27.125 1.00 70.04  ? 326 LYS A CB  1 
ATOM   2218 N N   . LYS A 1 327 ? -24.490 23.610  -24.814 1.00 74.45  ? 327 LYS A N   1 
ATOM   2219 C CA  . LYS A 1 327 ? -23.319 23.538  -23.956 1.00 77.07  ? 327 LYS A CA  1 
ATOM   2220 C C   . LYS A 1 327 ? -22.524 22.276  -24.288 1.00 76.03  ? 327 LYS A C   1 
ATOM   2221 O O   . LYS A 1 327 ? -23.079 21.177  -24.292 1.00 78.20  ? 327 LYS A O   1 
ATOM   2222 C CB  . LYS A 1 327 ? -23.725 23.540  -22.471 1.00 73.75  ? 327 LYS A CB  1 
ATOM   2223 N N   . SER A 1 328 ? -21.230 22.457  -24.582 1.00 72.28  ? 328 SER A N   1 
ATOM   2224 C CA  . SER A 1 328 ? -20.342 21.359  -24.930 1.00 72.76  ? 328 SER A CA  1 
ATOM   2225 C C   . SER A 1 328 ? -18.971 21.570  -24.295 1.00 73.31  ? 328 SER A C   1 
ATOM   2226 O O   . SER A 1 328 ? -18.662 22.663  -23.825 1.00 69.22  ? 328 SER A O   1 
ATOM   2227 C CB  . SER A 1 328 ? -20.194 21.227  -26.444 1.00 70.19  ? 328 SER A CB  1 
ATOM   2228 O OG  . SER A 1 328 ? -19.289 22.185  -26.966 1.00 63.02  ? 328 SER A OG  1 
ATOM   2229 N N   . ASN A 1 329 ? -18.158 20.515  -24.344 1.00 76.39  ? 329 ASN A N   1 
ATOM   2230 C CA  . ASN A 1 329 ? -16.807 20.564  -23.731 1.00 76.31  ? 329 ASN A CA  1 
ATOM   2231 C C   . ASN A 1 329 ? -15.812 21.106  -24.758 1.00 72.60  ? 329 ASN A C   1 
ATOM   2232 O O   . ASN A 1 329 ? -15.004 20.315  -25.271 1.00 71.34  ? 329 ASN A O   1 
ATOM   2233 C CB  . ASN A 1 329 ? -16.442 19.194  -23.180 1.00 80.02  ? 329 ASN A CB  1 
ATOM   2234 C CG  . ASN A 1 329 ? -17.142 18.890  -21.879 1.00 78.60  ? 329 ASN A CG  1 
ATOM   2235 O OD1 . ASN A 1 329 ? -17.629 19.804  -21.205 1.00 76.90  ? 329 ASN A OD1 1 
ATOM   2236 N ND2 . ASN A 1 329 ? -17.194 17.621  -21.505 1.00 67.04  ? 329 ASN A ND2 1 
ATOM   2237 N N   . THR A 1 330 ? -15.883 22.406  -25.042 1.00 73.48  ? 330 THR A N   1 
ATOM   2238 C CA  . THR A 1 330 ? -14.994 23.033  -26.033 1.00 66.88  ? 330 THR A CA  1 
ATOM   2239 C C   . THR A 1 330 ? -14.538 24.350  -25.473 1.00 65.94  ? 330 THR A C   1 
ATOM   2240 O O   . THR A 1 330 ? -15.347 25.018  -24.827 1.00 67.00  ? 330 THR A O   1 
ATOM   2241 C CB  . THR A 1 330 ? -15.734 23.234  -27.352 1.00 62.01  ? 330 THR A CB  1 
ATOM   2242 O OG1 . THR A 1 330 ? -16.688 22.186  -27.483 1.00 67.24  ? 330 THR A OG1 1 
ATOM   2243 C CG2 . THR A 1 330 ? -14.795 23.195  -28.544 1.00 68.48  ? 330 THR A CG2 1 
ATOM   2244 N N   . PHE A 1 331 ? -13.287 24.725  -25.726 1.00 67.02  ? 331 PHE A N   1 
ATOM   2245 C CA  . PHE A 1 331 ? -12.822 26.056  -25.270 1.00 65.47  ? 331 PHE A CA  1 
ATOM   2246 C C   . PHE A 1 331 ? -11.956 26.714  -26.323 1.00 57.58  ? 331 PHE A C   1 
ATOM   2247 O O   . PHE A 1 331 ? -11.454 26.015  -27.216 1.00 61.74  ? 331 PHE A O   1 
ATOM   2248 C CB  . PHE A 1 331 ? -12.050 25.906  -23.959 1.00 67.20  ? 331 PHE A CB  1 
ATOM   2249 C CG  . PHE A 1 331 ? -10.746 25.122  -24.007 1.00 68.85  ? 331 PHE A CG  1 
ATOM   2250 C CD1 . PHE A 1 331 ? -9.579  25.694  -24.498 1.00 61.31  ? 331 PHE A CD1 1 
ATOM   2251 C CD2 . PHE A 1 331 ? -10.686 23.823  -23.522 1.00 67.08  ? 331 PHE A CD2 1 
ATOM   2252 C CE1 . PHE A 1 331 ? -8.398  24.975  -24.530 1.00 67.19  ? 331 PHE A CE1 1 
ATOM   2253 C CE2 . PHE A 1 331 ? -9.500  23.112  -23.549 1.00 66.55  ? 331 PHE A CE2 1 
ATOM   2254 C CZ  . PHE A 1 331 ? -8.360  23.689  -24.053 1.00 71.22  ? 331 PHE A CZ  1 
ATOM   2255 N N   . LEU A 1 332 ? -11.801 28.034  -26.223 1.00 55.75  ? 332 LEU A N   1 
ATOM   2256 C CA  . LEU A 1 332 ? -10.876 28.755  -27.128 1.00 56.02  ? 332 LEU A CA  1 
ATOM   2257 C C   . LEU A 1 332 ? -9.665  29.145  -26.287 1.00 53.89  ? 332 LEU A C   1 
ATOM   2258 O O   . LEU A 1 332 ? -9.853  29.707  -25.197 1.00 60.13  ? 332 LEU A O   1 
ATOM   2259 C CB  . LEU A 1 332 ? -11.495 29.984  -27.781 1.00 51.42  ? 332 LEU A CB  1 
ATOM   2260 C CG  . LEU A 1 332 ? -10.578 30.775  -28.718 1.00 52.55  ? 332 LEU A CG  1 
ATOM   2261 C CD1 . LEU A 1 332 ? -10.362 30.024  -30.018 1.00 53.70  ? 332 LEU A CD1 1 
ATOM   2262 C CD2 . LEU A 1 332 ? -11.153 32.150  -28.982 1.00 60.20  ? 332 LEU A CD2 1 
ATOM   2263 N N   . MET A 1 333 ? -8.474  28.870  -26.791 1.00 48.83  ? 333 MET A N   1 
ATOM   2264 C CA  . MET A 1 333 ? -7.274  29.120  -26.010 1.00 57.69  ? 333 MET A CA  1 
ATOM   2265 C C   . MET A 1 333 ? -6.388  30.150  -26.706 1.00 55.23  ? 333 MET A C   1 
ATOM   2266 O O   . MET A 1 333 ? -6.185  30.085  -27.916 1.00 59.37  ? 333 MET A O   1 
ATOM   2267 C CB  . MET A 1 333 ? -6.500  27.816  -25.810 1.00 56.13  ? 333 MET A CB  1 
ATOM   2268 C CG  . MET A 1 333 ? -5.455  27.902  -24.721 1.00 64.82  ? 333 MET A CG  1 
ATOM   2269 S SD  . MET A 1 333 ? -4.095  26.704  -24.855 1.00 74.11  ? 333 MET A SD  1 
ATOM   2270 C CE  . MET A 1 333 ? -4.846  25.370  -25.753 1.00 70.09  ? 333 MET A CE  1 
ATOM   2271 N N   . GLY A 1 334 ? -5.869  31.099  -25.922 1.00 50.87  ? 334 GLY A N   1 
ATOM   2272 C CA  . GLY A 1 334 ? -4.952  32.111  -26.417 1.00 48.50  ? 334 GLY A CA  1 
ATOM   2273 C C   . GLY A 1 334 ? -3.522  31.858  -25.944 1.00 62.40  ? 334 GLY A C   1 
ATOM   2274 O O   . GLY A 1 334 ? -3.176  30.730  -25.598 1.00 62.24  ? 334 GLY A O   1 
ATOM   2275 N N   . LYS A 1 335 ? -2.716  32.928  -25.925 1.00 56.47  ? 335 LYS A N   1 
ATOM   2276 C CA  . LYS A 1 335 ? -1.303  32.841  -25.596 1.00 60.25  ? 335 LYS A CA  1 
ATOM   2277 C C   . LYS A 1 335 ? -1.139  32.426  -24.135 1.00 70.28  ? 335 LYS A C   1 
ATOM   2278 O O   . LYS A 1 335 ? -1.976  32.765  -23.297 1.00 66.42  ? 335 LYS A O   1 
ATOM   2279 C CB  . LYS A 1 335 ? -0.598  34.187  -25.853 1.00 56.43  ? 335 LYS A CB  1 
ATOM   2280 C CG  . LYS A 1 335 ? 0.866   34.049  -26.265 1.00 66.90  ? 335 LYS A CG  1 
ATOM   2281 C CD  . LYS A 1 335 ? 1.630   35.369  -26.238 1.00 65.36  ? 335 LYS A CD  1 
ATOM   2282 C CE  . LYS A 1 335 ? 2.210   35.672  -24.875 1.00 77.47  ? 335 LYS A CE  1 
ATOM   2283 N NZ  . LYS A 1 335 ? 2.798   37.039  -24.808 1.00 82.61  ? 335 LYS A NZ  1 
ATOM   2284 N N   . ASP A 1 336 ? -0.060  31.679  -23.859 1.00 68.26  ? 336 ASP A N   1 
ATOM   2285 C CA  . ASP A 1 336 ? 0.232   31.135  -22.539 1.00 71.45  ? 336 ASP A CA  1 
ATOM   2286 C C   . ASP A 1 336 ? -0.912  30.282  -21.994 1.00 68.29  ? 336 ASP A C   1 
ATOM   2287 O O   . ASP A 1 336 ? -1.079  30.155  -20.783 1.00 75.18  ? 336 ASP A O   1 
ATOM   2288 C CB  . ASP A 1 336 ? 0.578   32.260  -21.543 1.00 67.62  ? 336 ASP A CB  1 
ATOM   2289 C CG  . ASP A 1 336 ? 1.729   33.144  -21.977 1.00 73.23  ? 336 ASP A CG  1 
ATOM   2290 O OD1 . ASP A 1 336 ? 2.777   32.595  -22.394 1.00 79.44  ? 336 ASP A OD1 1 
ATOM   2291 O OD2 . ASP A 1 336 ? 1.594   34.383  -21.879 1.00 73.62  ? 336 ASP A OD2 1 
ATOM   2292 N N   . GLY A 1 337 ? -1.682  29.679  -22.904 1.00 65.30  ? 337 GLY A N   1 
ATOM   2293 C CA  . GLY A 1 337 ? -2.847  28.897  -22.532 1.00 65.54  ? 337 GLY A CA  1 
ATOM   2294 C C   . GLY A 1 337 ? -3.906  29.662  -21.741 1.00 62.43  ? 337 GLY A C   1 
ATOM   2295 O O   . GLY A 1 337 ? -4.506  29.103  -20.826 1.00 67.69  ? 337 GLY A O   1 
ATOM   2296 N N   . ARG A 1 338 ? -4.132  30.933  -22.103 1.00 58.93  ? 338 ARG A N   1 
ATOM   2297 C CA  . ARG A 1 338 ? -5.209  31.715  -21.512 1.00 57.41  ? 338 ARG A CA  1 
ATOM   2298 C C   . ARG A 1 338 ? -6.527  31.148  -22.031 1.00 56.75  ? 338 ARG A C   1 
ATOM   2299 O O   . ARG A 1 338 ? -6.611  30.757  -23.193 1.00 57.04  ? 338 ARG A O   1 
ATOM   2300 C CB  . ARG A 1 338 ? -5.079  33.201  -21.868 1.00 62.82  ? 338 ARG A CB  1 
ATOM   2301 C CG  . ARG A 1 338 ? -5.965  34.139  -21.050 1.00 63.69  ? 338 ARG A CG  1 
ATOM   2302 C CD  . ARG A 1 338 ? -5.307  34.591  -19.765 1.00 67.96  ? 338 ARG A CD  1 
ATOM   2303 N NE  . ARG A 1 338 ? -4.165  35.463  -20.019 1.00 75.35  ? 338 ARG A NE  1 
ATOM   2304 C CZ  . ARG A 1 338 ? -3.320  35.886  -19.088 1.00 75.74  ? 338 ARG A CZ  1 
ATOM   2305 N NH1 . ARG A 1 338 ? -3.536  35.656  -17.803 1.00 78.03  ? 338 ARG A NH1 1 
ATOM   2306 N NH2 . ARG A 1 338 ? -2.233  36.559  -19.453 1.00 66.82  ? 338 ARG A NH2 1 
ATOM   2307 N N   . LEU A 1 339 ? -7.537  31.070  -21.155 1.00 62.41  ? 339 LEU A N   1 
ATOM   2308 C CA  . LEU A 1 339 ? -8.866  30.638  -21.560 1.00 63.89  ? 339 LEU A CA  1 
ATOM   2309 C C   . LEU A 1 339 ? -9.669  31.838  -22.056 1.00 63.79  ? 339 LEU A C   1 
ATOM   2310 O O   . LEU A 1 339 ? -10.147 32.645  -21.260 1.00 61.75  ? 339 LEU A O   1 
ATOM   2311 C CB  . LEU A 1 339 ? -9.592  29.903  -20.422 1.00 58.67  ? 339 LEU A CB  1 
ATOM   2312 C CG  . LEU A 1 339 ? -9.697  28.394  -20.612 1.00 65.05  ? 339 LEU A CG  1 
ATOM   2313 C CD1 . LEU A 1 339 ? -8.329  27.733  -20.670 1.00 67.29  ? 339 LEU A CD1 1 
ATOM   2314 C CD2 . LEU A 1 339 ? -10.532 27.772  -19.517 1.00 74.89  ? 339 LEU A CD2 1 
ATOM   2315 N N   . LEU A 1 340 ? -9.785  31.941  -23.388 1.00 60.81  ? 340 LEU A N   1 
ATOM   2316 C CA  . LEU A 1 340 ? -10.468 33.047  -24.037 1.00 60.82  ? 340 LEU A CA  1 
ATOM   2317 C C   . LEU A 1 340 ? -11.972 32.805  -24.036 1.00 59.57  ? 340 LEU A C   1 
ATOM   2318 O O   . LEU A 1 340 ? -12.734 33.681  -23.634 1.00 69.79  ? 340 LEU A O   1 
ATOM   2319 C CB  . LEU A 1 340 ? -9.956  33.218  -25.472 1.00 54.62  ? 340 LEU A CB  1 
ATOM   2320 C CG  . LEU A 1 340 ? -8.457  33.457  -25.612 1.00 57.29  ? 340 LEU A CG  1 
ATOM   2321 C CD1 . LEU A 1 340 ? -8.076  33.730  -27.056 1.00 49.37  ? 340 LEU A CD1 1 
ATOM   2322 C CD2 . LEU A 1 340 ? -7.997  34.602  -24.742 1.00 58.95  ? 340 LEU A CD2 1 
ATOM   2323 N N   . ILE A 1 341 ? -12.379 31.612  -24.490 1.00 61.48  ? 341 ILE A N   1 
ATOM   2324 C CA  . ILE A 1 341 ? -13.762 31.169  -24.407 1.00 57.17  ? 341 ILE A CA  1 
ATOM   2325 C C   . ILE A 1 341 ? -13.813 29.816  -23.706 1.00 61.59  ? 341 ILE A C   1 
ATOM   2326 O O   . ILE A 1 341 ? -13.010 28.933  -24.005 1.00 60.15  ? 341 ILE A O   1 
ATOM   2327 C CB  . ILE A 1 341 ? -14.440 31.080  -25.802 1.00 62.12  ? 341 ILE A CB  1 
ATOM   2328 C CG1 . ILE A 1 341 ? -14.496 32.448  -26.506 1.00 60.51  ? 341 ILE A CG1 1 
ATOM   2329 C CG2 . ILE A 1 341 ? -15.841 30.459  -25.699 1.00 60.01  ? 341 ILE A CG2 1 
ATOM   2330 C CD1 . ILE A 1 341 ? -15.529 33.420  -25.900 1.00 65.24  ? 341 ILE A CD1 1 
ATOM   2331 N N   . ASN A 1 342 ? -14.788 29.667  -22.800 1.00 69.37  ? 342 ASN A N   1 
ATOM   2332 C CA  . ASN A 1 342 ? -14.976 28.447  -22.032 1.00 61.58  ? 342 ASN A CA  1 
ATOM   2333 C C   . ASN A 1 342 ? -16.408 28.373  -21.498 1.00 71.77  ? 342 ASN A C   1 
ATOM   2334 O O   . ASN A 1 342 ? -16.924 29.364  -20.985 1.00 70.35  ? 342 ASN A O   1 
ATOM   2335 C CB  . ASN A 1 342 ? -13.968 28.409  -20.884 1.00 71.62  ? 342 ASN A CB  1 
ATOM   2336 C CG  . ASN A 1 342 ? -14.070 27.174  -20.029 1.00 69.07  ? 342 ASN A CG  1 
ATOM   2337 O OD1 . ASN A 1 342 ? -14.596 27.213  -18.922 1.00 67.31  ? 342 ASN A OD1 1 
ATOM   2338 N ND2 . ASN A 1 342 ? -13.577 26.053  -20.525 1.00 66.07  ? 342 ASN A ND2 1 
ATOM   2339 N N   . PRO A 1 343 ? -17.098 27.210  -21.586 1.00 74.96  ? 343 PRO A N   1 
ATOM   2340 C CA  . PRO A 1 343 ? -18.452 27.078  -21.051 1.00 70.30  ? 343 PRO A CA  1 
ATOM   2341 C C   . PRO A 1 343 ? -18.612 27.631  -19.635 1.00 73.02  ? 343 PRO A C   1 
ATOM   2342 O O   . PRO A 1 343 ? -19.614 28.278  -19.334 1.00 75.38  ? 343 PRO A O   1 
ATOM   2343 C CB  . PRO A 1 343 ? -18.705 25.572  -21.110 1.00 56.98  ? 343 PRO A CB  1 
ATOM   2344 C CG  . PRO A 1 343 ? -17.835 25.090  -22.223 1.00 67.56  ? 343 PRO A CG  1 
ATOM   2345 C CD  . PRO A 1 343 ? -16.611 25.972  -22.214 1.00 68.56  ? 343 PRO A CD  1 
ATOM   2346 N N   . ASN A 1 344 ? -17.616 27.375  -18.779 1.00 66.99  ? 344 ASN A N   1 
ATOM   2347 C CA  . ASN A 1 344 ? -17.537 27.988  -17.462 1.00 76.31  ? 344 ASN A CA  1 
ATOM   2348 C C   . ASN A 1 344 ? -16.989 29.410  -17.587 1.00 74.85  ? 344 ASN A C   1 
ATOM   2349 O O   . ASN A 1 344 ? -15.784 29.599  -17.756 1.00 74.43  ? 344 ASN A O   1 
ATOM   2350 C CB  . ASN A 1 344 ? -16.657 27.133  -16.526 1.00 80.49  ? 344 ASN A CB  1 
ATOM   2351 C CG  . ASN A 1 344 ? -16.516 27.660  -15.113 1.00 72.39  ? 344 ASN A CG  1 
ATOM   2352 O OD1 . ASN A 1 344 ? -16.357 28.861  -14.867 1.00 82.78  ? 344 ASN A OD1 1 
ATOM   2353 N ND2 . ASN A 1 344 ? -16.566 26.764  -14.143 1.00 77.73  ? 344 ASN A ND2 1 
ATOM   2354 N N   . ARG A 1 345 ? -17.886 30.401  -17.484 1.00 79.83  ? 345 ARG A N   1 
ATOM   2355 C CA  . ARG A 1 345 ? -17.531 31.806  -17.628 1.00 79.13  ? 345 ARG A CA  1 
ATOM   2356 C C   . ARG A 1 345 ? -16.632 32.315  -16.502 1.00 70.88  ? 345 ARG A C   1 
ATOM   2357 O O   . ARG A 1 345 ? -15.796 33.192  -16.720 1.00 70.39  ? 345 ARG A O   1 
ATOM   2358 C CB  . ARG A 1 345 ? -18.800 32.668  -17.689 1.00 77.21  ? 345 ARG A CB  1 
ATOM   2359 N N   . GLU A 1 346 ? -16.798 31.747  -15.303 1.00 74.19  ? 346 GLU A N   1 
ATOM   2360 C CA  . GLU A 1 346 ? -16.043 32.173  -14.134 1.00 81.08  ? 346 GLU A CA  1 
ATOM   2361 C C   . GLU A 1 346 ? -14.547 31.872  -14.229 1.00 78.36  ? 346 GLU A C   1 
ATOM   2362 O O   . GLU A 1 346 ? -13.772 32.364  -13.412 1.00 87.91  ? 346 GLU A O   1 
ATOM   2363 C CB  . GLU A 1 346 ? -16.619 31.518  -12.864 1.00 79.97  ? 346 GLU A CB  1 
ATOM   2364 N N   . ILE A 1 347 ? -14.146 31.068  -15.224 1.00 74.78  ? 347 ILE A N   1 
ATOM   2365 C CA  . ILE A 1 347 ? -12.745 30.739  -15.441 1.00 76.45  ? 347 ILE A CA  1 
ATOM   2366 C C   . ILE A 1 347 ? -12.123 31.472  -16.633 1.00 70.91  ? 347 ILE A C   1 
ATOM   2367 O O   . ILE A 1 347 ? -10.916 31.392  -16.845 1.00 62.04  ? 347 ILE A O   1 
ATOM   2368 C CB  . ILE A 1 347 ? -12.649 29.191  -15.561 1.00 84.96  ? 347 ILE A CB  1 
ATOM   2369 C CG1 . ILE A 1 347 ? -13.066 28.506  -14.237 1.00 81.31  ? 347 ILE A CG1 1 
ATOM   2370 C CG2 . ILE A 1 347 ? -11.272 28.704  -15.995 1.00 81.51  ? 347 ILE A CG2 1 
ATOM   2371 C CD1 . ILE A 1 347 ? -12.244 28.889  -13.032 1.00 84.26  ? 347 ILE A CD1 1 
ATOM   2372 N N   . GLN A 1 348 ? -12.940 32.211  -17.398 1.00 76.27  ? 348 GLN A N   1 
ATOM   2373 C CA  . GLN A 1 348 ? -12.443 32.989  -18.525 1.00 59.17  ? 348 GLN A CA  1 
ATOM   2374 C C   . GLN A 1 348 ? -11.324 33.930  -18.080 1.00 65.03  ? 348 GLN A C   1 
ATOM   2375 O O   . GLN A 1 348 ? -11.364 34.461  -16.972 1.00 79.76  ? 348 GLN A O   1 
ATOM   2376 C CB  . GLN A 1 348 ? -13.583 33.798  -19.175 1.00 67.42  ? 348 GLN A CB  1 
ATOM   2377 C CG  . GLN A 1 348 ? -13.146 34.622  -20.395 1.00 59.10  ? 348 GLN A CG  1 
ATOM   2378 C CD  . GLN A 1 348 ? -14.297 35.339  -21.075 1.00 59.38  ? 348 GLN A CD  1 
ATOM   2379 O OE1 . GLN A 1 348 ? -14.855 36.310  -20.556 1.00 47.42  ? 348 GLN A OE1 1 
ATOM   2380 N NE2 . GLN A 1 348 ? -14.658 34.898  -22.265 1.00 47.55  ? 348 GLN A NE2 1 
ATOM   2381 N N   . ASP A 1 349 ? -10.336 34.123  -18.964 1.00 51.24  ? 349 ASP A N   1 
ATOM   2382 C CA  . ASP A 1 349 ? -9.171  34.955  -18.700 1.00 60.63  ? 349 ASP A CA  1 
ATOM   2383 C C   . ASP A 1 349 ? -8.291  34.414  -17.574 1.00 64.18  ? 349 ASP A C   1 
ATOM   2384 O O   . ASP A 1 349 ? -7.687  35.191  -16.838 1.00 64.57  ? 349 ASP A O   1 
ATOM   2385 C CB  . ASP A 1 349 ? -9.590  36.402  -18.378 1.00 57.26  ? 349 ASP A CB  1 
ATOM   2386 C CG  . ASP A 1 349 ? -8.449  37.398  -18.381 1.00 58.57  ? 349 ASP A CG  1 
ATOM   2387 O OD1 . ASP A 1 349 ? -7.694  37.434  -19.378 1.00 57.76  ? 349 ASP A OD1 1 
ATOM   2388 O OD2 . ASP A 1 349 ? -8.315  38.142  -17.393 1.00 59.22  ? 349 ASP A OD2 1 
ATOM   2389 N N   . LYS A 1 350 ? -8.218  33.081  -17.466 1.00 54.25  ? 350 LYS A N   1 
ATOM   2390 C CA  . LYS A 1 350 ? -7.335  32.415  -16.520 1.00 63.78  ? 350 LYS A CA  1 
ATOM   2391 C C   . LYS A 1 350 ? -6.466  31.420  -17.286 1.00 67.84  ? 350 LYS A C   1 
ATOM   2392 O O   . LYS A 1 350 ? -6.894  30.871  -18.298 1.00 73.32  ? 350 LYS A O   1 
ATOM   2393 C CB  . LYS A 1 350 ? -8.134  31.703  -15.414 1.00 52.16  ? 350 LYS A CB  1 
ATOM   2394 N N   . ILE A 1 351 ? -5.235  31.207  -16.806 1.00 75.78  ? 351 ILE A N   1 
ATOM   2395 C CA  . ILE A 1 351 ? -4.307  30.301  -17.464 1.00 72.55  ? 351 ILE A CA  1 
ATOM   2396 C C   . ILE A 1 351 ? -4.663  28.860  -17.102 1.00 74.81  ? 351 ILE A C   1 
ATOM   2397 O O   . ILE A 1 351 ? -4.948  28.560  -15.944 1.00 75.36  ? 351 ILE A O   1 
ATOM   2398 C CB  . ILE A 1 351 ? -2.848  30.669  -17.117 1.00 69.85  ? 351 ILE A CB  1 
ATOM   2399 C CG1 . ILE A 1 351 ? -2.523  32.090  -17.615 1.00 68.00  ? 351 ILE A CG1 1 
ATOM   2400 C CG2 . ILE A 1 351 ? -1.861  29.635  -17.678 1.00 71.12  ? 351 ILE A CG2 1 
ATOM   2401 C CD1 . ILE A 1 351 ? -1.322  32.695  -16.986 1.00 80.90  ? 351 ILE A CD1 1 
ATOM   2402 N N   . LEU A 1 352 ? -4.654  27.983  -18.114 1.00 68.50  ? 352 LEU A N   1 
ATOM   2403 C CA  . LEU A 1 352 ? -5.094  26.605  -17.959 1.00 72.73  ? 352 LEU A CA  1 
ATOM   2404 C C   . LEU A 1 352 ? -4.196  25.837  -16.990 1.00 73.30  ? 352 LEU A C   1 
ATOM   2405 O O   . LEU A 1 352 ? -4.689  25.089  -16.152 1.00 69.99  ? 352 LEU A O   1 
ATOM   2406 C CB  . LEU A 1 352 ? -5.120  25.926  -19.340 1.00 62.39  ? 352 LEU A CB  1 
ATOM   2407 C CG  . LEU A 1 352 ? -5.710  24.521  -19.395 1.00 68.95  ? 352 LEU A CG  1 
ATOM   2408 C CD1 . LEU A 1 352 ? -7.225  24.550  -19.243 1.00 65.95  ? 352 LEU A CD1 1 
ATOM   2409 C CD2 . LEU A 1 352 ? -5.321  23.821  -20.683 1.00 59.37  ? 352 LEU A CD2 1 
ATOM   2410 N N   . SER A 1 353 ? -2.877  26.036  -17.114 1.00 78.18  ? 353 SER A N   1 
ATOM   2411 C CA  . SER A 1 353 ? -1.903  25.432  -16.218 1.00 68.21  ? 353 SER A CA  1 
ATOM   2412 C C   . SER A 1 353 ? -2.086  25.890  -14.774 1.00 75.33  ? 353 SER A C   1 
ATOM   2413 O O   . SER A 1 353 ? -1.848  25.121  -13.845 1.00 77.22  ? 353 SER A O   1 
ATOM   2414 C CB  . SER A 1 353 ? -0.483  25.759  -16.667 1.00 60.35  ? 353 SER A CB  1 
ATOM   2415 O OG  . SER A 1 353 ? -0.271  25.407  -18.022 1.00 69.66  ? 353 SER A OG  1 
ATOM   2416 N N   . ALA A 1 354 ? -2.502  27.150  -14.604 1.00 70.86  ? 354 ALA A N   1 
ATOM   2417 C CA  . ALA A 1 354 ? -2.697  27.736  -13.288 1.00 75.56  ? 354 ALA A CA  1 
ATOM   2418 C C   . ALA A 1 354 ? -3.829  27.064  -12.514 1.00 77.70  ? 354 ALA A C   1 
ATOM   2419 O O   . ALA A 1 354 ? -3.685  26.776  -11.327 1.00 80.72  ? 354 ALA A O   1 
ATOM   2420 C CB  . ALA A 1 354 ? -2.970  29.225  -13.419 1.00 69.33  ? 354 ALA A CB  1 
ATOM   2421 N N   . ILE A 1 355 ? -4.949  26.816  -13.202 1.00 73.08  ? 355 ILE A N   1 
ATOM   2422 C CA  . ILE A 1 355 ? -6.150  26.295  -12.568 1.00 79.75  ? 355 ILE A CA  1 
ATOM   2423 C C   . ILE A 1 355 ? -6.104  24.781  -12.358 1.00 78.44  ? 355 ILE A C   1 
ATOM   2424 O O   . ILE A 1 355 ? -6.643  24.288  -11.371 1.00 75.90  ? 355 ILE A O   1 
ATOM   2425 C CB  . ILE A 1 355 ? -7.430  26.728  -13.345 1.00 73.81  ? 355 ILE A CB  1 
ATOM   2426 C CG1 . ILE A 1 355 ? -7.359  26.380  -14.853 1.00 76.72  ? 355 ILE A CG1 1 
ATOM   2427 C CG2 . ILE A 1 355 ? -7.713  28.215  -13.129 1.00 71.04  ? 355 ILE A CG2 1 
ATOM   2428 C CD1 . ILE A 1 355 ? -8.599  26.737  -15.624 1.00 73.50  ? 355 ILE A CD1 1 
ATOM   2429 N N   . ASN A 1 356 ? -5.457  24.052  -13.278 1.00 78.24  ? 356 ASN A N   1 
ATOM   2430 C CA  . ASN A 1 356 ? -5.333  22.605  -13.168 1.00 79.83  ? 356 ASN A CA  1 
ATOM   2431 C C   . ASN A 1 356 ? -3.987  22.185  -12.579 1.00 72.04  ? 356 ASN A C   1 
ATOM   2432 O O   . ASN A 1 356 ? -2.943  22.634  -13.044 1.00 74.05  ? 356 ASN A O   1 
ATOM   2433 C CB  . ASN A 1 356 ? -5.514  21.948  -14.530 1.00 74.36  ? 356 ASN A CB  1 
ATOM   2434 C CG  . ASN A 1 356 ? -6.883  22.147  -15.104 1.00 64.90  ? 356 ASN A CG  1 
ATOM   2435 O OD1 . ASN A 1 356 ? -7.897  21.925  -14.444 1.00 66.48  ? 356 ASN A OD1 1 
ATOM   2436 N ND2 . ASN A 1 356 ? -6.948  22.574  -16.348 1.00 83.60  ? 356 ASN A ND2 1 
ATOM   2437 N N   . PRO A 1 357 ? -3.957  21.296  -11.560 1.00 76.31  ? 357 PRO A N   1 
ATOM   2438 C CA  . PRO A 1 357 ? -2.700  20.933  -10.909 1.00 80.84  ? 357 PRO A CA  1 
ATOM   2439 C C   . PRO A 1 357 ? -1.788  20.052  -11.762 1.00 74.16  ? 357 PRO A C   1 
ATOM   2440 O O   . PRO A 1 357 ? -0.603  20.342  -11.905 1.00 74.59  ? 357 PRO A O   1 
ATOM   2441 C CB  . PRO A 1 357 ? -3.155  20.206  -9.638  1.00 77.97  ? 357 PRO A CB  1 
ATOM   2442 C CG  . PRO A 1 357 ? -4.537  19.696  -9.947  1.00 72.33  ? 357 PRO A CG  1 
ATOM   2443 C CD  . PRO A 1 357 ? -5.129  20.607  -10.992 1.00 84.37  ? 357 PRO A CD  1 
ATOM   2444 N N   . ASP A 1 358 ? -2.361  18.984  -12.328 1.00 73.62  ? 358 ASP A N   1 
ATOM   2445 C CA  . ASP A 1 358 ? -1.597  17.992  -13.064 1.00 65.26  ? 358 ASP A CA  1 
ATOM   2446 C C   . ASP A 1 358 ? -0.733  18.672  -14.122 1.00 61.18  ? 358 ASP A C   1 
ATOM   2447 O O   . ASP A 1 358 ? -1.254  19.285  -15.050 1.00 73.08  ? 358 ASP A O   1 
ATOM   2448 C CB  . ASP A 1 358 ? -2.551  16.965  -13.690 1.00 67.86  ? 358 ASP A CB  1 
ATOM   2449 C CG  . ASP A 1 358 ? -1.894  15.702  -14.192 1.00 65.79  ? 358 ASP A CG  1 
ATOM   2450 O OD1 . ASP A 1 358 ? -0.655  15.688  -14.316 1.00 70.05  ? 358 ASP A OD1 1 
ATOM   2451 O OD2 . ASP A 1 358 ? -2.621  14.721  -14.455 1.00 60.02  ? 358 ASP A OD2 1 
ATOM   2452 N N   . ARG A 1 359 ? 0.590   18.545  -13.962 1.00 70.57  ? 359 ARG A N   1 
ATOM   2453 C CA  . ARG A 1 359 ? 1.563   19.243  -14.788 1.00 61.80  ? 359 ARG A CA  1 
ATOM   2454 C C   . ARG A 1 359 ? 1.586   18.769  -16.240 1.00 67.77  ? 359 ARG A C   1 
ATOM   2455 O O   . ARG A 1 359 ? 2.338   19.307  -17.050 1.00 67.21  ? 359 ARG A O   1 
ATOM   2456 C CB  . ARG A 1 359 ? 2.985   19.094  -14.188 1.00 68.69  ? 359 ARG A CB  1 
ATOM   2457 C CG  . ARG A 1 359 ? 3.608   17.695  -14.314 1.00 64.79  ? 359 ARG A CG  1 
ATOM   2458 N N   . ARG A 1 360 ? 0.775   17.753  -16.556 1.00 61.30  ? 360 ARG A N   1 
ATOM   2459 C CA  . ARG A 1 360 ? 0.641   17.276  -17.921 1.00 60.30  ? 360 ARG A CA  1 
ATOM   2460 C C   . ARG A 1 360 ? -0.179  18.241  -18.781 1.00 71.61  ? 360 ARG A C   1 
ATOM   2461 O O   . ARG A 1 360 ? -0.168  18.135  -20.007 1.00 55.44  ? 360 ARG A O   1 
ATOM   2462 C CB  . ARG A 1 360 ? 0.008   15.875  -17.918 1.00 70.39  ? 360 ARG A CB  1 
ATOM   2463 C CG  . ARG A 1 360 ? 0.818   14.822  -17.142 1.00 66.28  ? 360 ARG A CG  1 
ATOM   2464 C CD  . ARG A 1 360 ? 0.198   13.432  -17.228 1.00 54.10  ? 360 ARG A CD  1 
ATOM   2465 N NE  . ARG A 1 360 ? -1.097  13.352  -16.561 1.00 57.04  ? 360 ARG A NE  1 
ATOM   2466 C CZ  . ARG A 1 360 ? -1.924  12.317  -16.651 1.00 61.67  ? 360 ARG A CZ  1 
ATOM   2467 N NH1 . ARG A 1 360 ? -1.700  11.325  -17.498 1.00 59.01  ? 360 ARG A NH1 1 
ATOM   2468 N NH2 . ARG A 1 360 ? -3.018  12.290  -15.893 1.00 61.98  ? 360 ARG A NH2 1 
ATOM   2469 N N   . VAL A 1 361 ? -0.879  19.183  -18.127 1.00 66.17  ? 361 VAL A N   1 
ATOM   2470 C CA  . VAL A 1 361 ? -1.668  20.199  -18.811 1.00 71.55  ? 361 VAL A CA  1 
ATOM   2471 C C   . VAL A 1 361 ? -0.807  21.237  -19.531 1.00 70.38  ? 361 VAL A C   1 
ATOM   2472 O O   . VAL A 1 361 ? -1.305  21.953  -20.398 1.00 60.78  ? 361 VAL A O   1 
ATOM   2473 C CB  . VAL A 1 361 ? -2.631  20.908  -17.825 1.00 77.63  ? 361 VAL A CB  1 
ATOM   2474 C CG1 . VAL A 1 361 ? -1.868  21.798  -16.848 1.00 78.89  ? 361 VAL A CG1 1 
ATOM   2475 C CG2 . VAL A 1 361 ? -3.695  21.713  -18.570 1.00 69.84  ? 361 VAL A CG2 1 
ATOM   2476 N N   . ALA A 1 362 ? 0.479   21.318  -19.157 1.00 67.21  ? 362 ALA A N   1 
ATOM   2477 C CA  . ALA A 1 362 ? 1.436   22.183  -19.833 1.00 60.66  ? 362 ALA A CA  1 
ATOM   2478 C C   . ALA A 1 362 ? 1.714   21.750  -21.273 1.00 67.61  ? 362 ALA A C   1 
ATOM   2479 O O   . ALA A 1 362 ? 2.213   22.542  -22.071 1.00 67.55  ? 362 ALA A O   1 
ATOM   2480 C CB  . ALA A 1 362 ? 2.734   22.229  -19.052 1.00 57.40  ? 362 ALA A CB  1 
ATOM   2481 N N   . LYS A 1 363 ? 1.385   20.492  -21.596 1.00 63.40  ? 363 LYS A N   1 
ATOM   2482 C CA  . LYS A 1 363 ? 1.547   19.963  -22.942 1.00 65.95  ? 363 LYS A CA  1 
ATOM   2483 C C   . LYS A 1 363 ? 0.614   20.637  -23.951 1.00 68.57  ? 363 LYS A C   1 
ATOM   2484 O O   . LYS A 1 363 ? 0.860   20.583  -25.155 1.00 66.51  ? 363 LYS A O   1 
ATOM   2485 C CB  . LYS A 1 363 ? 1.309   18.438  -22.922 1.00 63.20  ? 363 LYS A CB  1 
ATOM   2486 C CG  . LYS A 1 363 ? 1.967   17.687  -24.073 1.00 65.24  ? 363 LYS A CG  1 
ATOM   2487 C CD  . LYS A 1 363 ? 1.853   16.168  -23.940 1.00 59.00  ? 363 LYS A CD  1 
ATOM   2488 N N   . ALA A 1 364 ? -0.456  21.268  -23.448 1.00 68.69  ? 364 ALA A N   1 
ATOM   2489 C CA  . ALA A 1 364 ? -1.397  22.010  -24.272 1.00 72.76  ? 364 ALA A CA  1 
ATOM   2490 C C   . ALA A 1 364 ? -0.778  23.275  -24.862 1.00 73.47  ? 364 ALA A C   1 
ATOM   2491 O O   . ALA A 1 364 ? -0.974  23.574  -26.039 1.00 65.13  ? 364 ALA A O   1 
ATOM   2492 C CB  . ALA A 1 364 ? -2.622  22.383  -23.452 1.00 72.45  ? 364 ALA A CB  1 
ATOM   2493 N N   . VAL A 1 365 ? -0.039  24.013  -24.026 1.00 71.41  ? 365 VAL A N   1 
ATOM   2494 C CA  . VAL A 1 365 ? 0.558   25.274  -24.434 1.00 69.05  ? 365 VAL A CA  1 
ATOM   2495 C C   . VAL A 1 365 ? 1.720   25.009  -25.389 1.00 66.28  ? 365 VAL A C   1 
ATOM   2496 O O   . VAL A 1 365 ? 2.069   25.872  -26.191 1.00 72.30  ? 365 VAL A O   1 
ATOM   2497 C CB  . VAL A 1 365 ? 0.990   26.123  -23.213 1.00 66.11  ? 365 VAL A CB  1 
ATOM   2498 C CG1 . VAL A 1 365 ? 1.381   27.539  -23.635 1.00 73.43  ? 365 VAL A CG1 1 
ATOM   2499 C CG2 . VAL A 1 365 ? -0.110  26.161  -22.150 1.00 67.32  ? 365 VAL A CG2 1 
ATOM   2500 N N   . GLU A 1 366 ? 2.293   23.801  -25.311 1.00 67.74  ? 366 GLU A N   1 
ATOM   2501 C CA  . GLU A 1 366 ? 3.360   23.383  -26.206 1.00 71.53  ? 366 GLU A CA  1 
ATOM   2502 C C   . GLU A 1 366 ? 2.838   23.035  -27.598 1.00 69.85  ? 366 GLU A C   1 
ATOM   2503 O O   . GLU A 1 366 ? 3.425   23.454  -28.594 1.00 73.47  ? 366 GLU A O   1 
ATOM   2504 C CB  . GLU A 1 366 ? 4.116   22.201  -25.591 1.00 71.91  ? 366 GLU A CB  1 
ATOM   2505 C CG  . GLU A 1 366 ? 5.037   22.624  -24.460 1.00 67.62  ? 366 GLU A CG  1 
ATOM   2506 C CD  . GLU A 1 366 ? 5.257   21.558  -23.407 1.00 83.13  ? 366 GLU A CD  1 
ATOM   2507 O OE1 . GLU A 1 366 ? 5.597   20.411  -23.779 1.00 75.46  ? 366 GLU A OE1 1 
ATOM   2508 O OE2 . GLU A 1 366 ? 5.087   21.870  -22.205 1.00 85.00  ? 366 GLU A OE2 1 
ATOM   2509 N N   . TYR A 1 367 ? 1.741   22.266  -27.657 1.00 69.04  ? 367 TYR A N   1 
ATOM   2510 C CA  . TYR A 1 367 ? 1.011   22.055  -28.900 1.00 67.78  ? 367 TYR A CA  1 
ATOM   2511 C C   . TYR A 1 367 ? 0.655   23.391  -29.547 1.00 61.82  ? 367 TYR A C   1 
ATOM   2512 O O   . TYR A 1 367 ? 0.853   23.581  -30.746 1.00 69.90  ? 367 TYR A O   1 
ATOM   2513 C CB  . TYR A 1 367 ? -0.289  21.255  -28.671 1.00 68.45  ? 367 TYR A CB  1 
ATOM   2514 C CG  . TYR A 1 367 ? -0.097  19.796  -28.320 1.00 72.58  ? 367 TYR A CG  1 
ATOM   2515 C CD1 . TYR A 1 367 ? 0.737   18.981  -29.075 1.00 72.02  ? 367 TYR A CD1 1 
ATOM   2516 C CD2 . TYR A 1 367 ? -0.780  19.221  -27.258 1.00 72.87  ? 367 TYR A CD2 1 
ATOM   2517 C CE1 . TYR A 1 367 ? 0.912   17.637  -28.762 1.00 68.92  ? 367 TYR A CE1 1 
ATOM   2518 C CE2 . TYR A 1 367 ? -0.616  17.877  -26.935 1.00 82.09  ? 367 TYR A CE2 1 
ATOM   2519 C CZ  . TYR A 1 367 ? 0.231   17.087  -27.691 1.00 81.80  ? 367 TYR A CZ  1 
ATOM   2520 O OH  . TYR A 1 367 ? 0.392   15.759  -27.381 1.00 74.68  ? 367 TYR A OH  1 
ATOM   2521 N N   . TYR A 1 368 ? 0.115   24.302  -28.727 1.00 64.89  ? 368 TYR A N   1 
ATOM   2522 C CA  . TYR A 1 368 ? -0.222  25.651  -29.149 1.00 69.44  ? 368 TYR A CA  1 
ATOM   2523 C C   . TYR A 1 368 ? 0.956   26.322  -29.850 1.00 59.57  ? 368 TYR A C   1 
ATOM   2524 O O   . TYR A 1 368 ? 0.857   26.655  -31.027 1.00 58.96  ? 368 TYR A O   1 
ATOM   2525 C CB  . TYR A 1 368 ? -0.682  26.472  -27.930 1.00 67.25  ? 368 TYR A CB  1 
ATOM   2526 C CG  . TYR A 1 368 ? -0.847  27.953  -28.185 1.00 67.91  ? 368 TYR A CG  1 
ATOM   2527 C CD1 . TYR A 1 368 ? -1.984  28.452  -28.809 1.00 64.22  ? 368 TYR A CD1 1 
ATOM   2528 C CD2 . TYR A 1 368 ? 0.131   28.857  -27.797 1.00 62.43  ? 368 TYR A CD2 1 
ATOM   2529 C CE1 . TYR A 1 368 ? -2.143  29.815  -29.037 1.00 53.83  ? 368 TYR A CE1 1 
ATOM   2530 C CE2 . TYR A 1 368 ? -0.016  30.221  -28.021 1.00 64.01  ? 368 TYR A CE2 1 
ATOM   2531 C CZ  . TYR A 1 368 ? -1.153  30.697  -28.644 1.00 63.44  ? 368 TYR A CZ  1 
ATOM   2532 O OH  . TYR A 1 368 ? -1.288  32.041  -28.860 1.00 70.35  ? 368 TYR A OH  1 
ATOM   2533 N N   . ASN A 1 369 ? 2.070   26.472  -29.122 1.00 69.09  ? 369 ASN A N   1 
ATOM   2534 C CA  . ASN A 1 369 ? 3.266   27.133  -29.628 1.00 67.09  ? 369 ASN A CA  1 
ATOM   2535 C C   . ASN A 1 369 ? 3.882   26.436  -30.842 1.00 66.67  ? 369 ASN A C   1 
ATOM   2536 O O   . ASN A 1 369 ? 4.396   27.099  -31.741 1.00 78.39  ? 369 ASN A O   1 
ATOM   2537 C CB  . ASN A 1 369 ? 4.329   27.257  -28.520 1.00 69.83  ? 369 ASN A CB  1 
ATOM   2538 C CG  . ASN A 1 369 ? 3.935   28.155  -27.368 1.00 68.12  ? 369 ASN A CG  1 
ATOM   2539 O OD1 . ASN A 1 369 ? 4.047   27.783  -26.196 1.00 71.92  ? 369 ASN A OD1 1 
ATOM   2540 N ND2 . ASN A 1 369 ? 3.489   29.369  -27.667 1.00 63.48  ? 369 ASN A ND2 1 
ATOM   2541 N N   . GLN A 1 370 ? 3.826   25.098  -30.862 1.00 62.62  ? 370 GLN A N   1 
ATOM   2542 C CA  . GLN A 1 370 ? 4.305   24.324  -31.997 1.00 59.59  ? 370 GLN A CA  1 
ATOM   2543 C C   . GLN A 1 370 ? 3.384   24.425  -33.212 1.00 63.91  ? 370 GLN A C   1 
ATOM   2544 O O   . GLN A 1 370 ? 3.814   24.154  -34.332 1.00 66.73  ? 370 GLN A O   1 
ATOM   2545 C CB  . GLN A 1 370 ? 4.458   22.845  -31.608 1.00 57.73  ? 370 GLN A CB  1 
ATOM   2546 N N   . ASN A 1 371 ? 2.118   24.796  -32.969 1.00 63.79  ? 371 ASN A N   1 
ATOM   2547 C CA  . ASN A 1 371 ? 1.076   24.844  -33.986 1.00 69.13  ? 371 ASN A CA  1 
ATOM   2548 C C   . ASN A 1 371 ? 0.739   23.432  -34.466 1.00 70.99  ? 371 ASN A C   1 
ATOM   2549 O O   . ASN A 1 371 ? 0.227   23.255  -35.569 1.00 67.95  ? 371 ASN A O   1 
ATOM   2550 C CB  . ASN A 1 371 ? 1.475   25.766  -35.163 1.00 67.95  ? 371 ASN A CB  1 
ATOM   2551 C CG  . ASN A 1 371 ? 0.308   26.373  -35.932 1.00 72.07  ? 371 ASN A CG  1 
ATOM   2552 O OD1 . ASN A 1 371 ? -0.872  26.062  -35.720 1.00 72.59  ? 371 ASN A OD1 1 
ATOM   2553 N ND2 . ASN A 1 371 ? 0.618   27.271  -36.851 1.00 75.60  ? 371 ASN A ND2 1 
ATOM   2554 N N   . GLU A 1 372 ? 1.001   22.439  -33.603 1.00 70.27  ? 372 GLU A N   1 
ATOM   2555 C CA  . GLU A 1 372 ? 0.796   21.036  -33.926 1.00 70.87  ? 372 GLU A CA  1 
ATOM   2556 C C   . GLU A 1 372 ? -0.373  20.508  -33.097 1.00 71.17  ? 372 GLU A C   1 
ATOM   2557 O O   . GLU A 1 372 ? -0.343  20.586  -31.872 1.00 78.08  ? 372 GLU A O   1 
ATOM   2558 C CB  . GLU A 1 372 ? 2.070   20.226  -33.625 1.00 75.03  ? 372 GLU A CB  1 
ATOM   2559 C CG  . GLU A 1 372 ? 2.246   18.978  -34.477 1.00 80.12  ? 372 GLU A CG  1 
ATOM   2560 C CD  . GLU A 1 372 ? 2.915   19.189  -35.825 1.00 84.08  ? 372 GLU A CD  1 
ATOM   2561 O OE1 . GLU A 1 372 ? 3.120   20.358  -36.228 1.00 77.68  ? 372 GLU A OE1 1 
ATOM   2562 O OE2 . GLU A 1 372 ? 3.255   18.173  -36.475 1.00 78.50  ? 372 GLU A OE2 1 
ATOM   2563 N N   . ALA A 1 373 ? -1.401  19.981  -33.773 1.00 68.58  ? 373 ALA A N   1 
ATOM   2564 C CA  . ALA A 1 373 ? -2.535  19.377  -33.093 1.00 73.27  ? 373 ALA A CA  1 
ATOM   2565 C C   . ALA A 1 373 ? -2.114  18.084  -32.396 1.00 76.81  ? 373 ALA A C   1 
ATOM   2566 O O   . ALA A 1 373 ? -1.364  17.282  -32.951 1.00 73.66  ? 373 ALA A O   1 
ATOM   2567 C CB  . ALA A 1 373 ? -3.668  19.102  -34.068 1.00 64.96  ? 373 ALA A CB  1 
ATOM   2568 N N   . GLY A 1 374 ? -2.614  17.900  -31.171 1.00 72.48  ? 374 GLY A N   1 
ATOM   2569 C CA  . GLY A 1 374 ? -2.288  16.732  -30.375 1.00 78.54  ? 374 GLY A CA  1 
ATOM   2570 C C   . GLY A 1 374 ? -3.236  16.570  -29.193 1.00 78.55  ? 374 GLY A C   1 
ATOM   2571 O O   . GLY A 1 374 ? -4.014  17.474  -28.892 1.00 79.02  ? 374 GLY A O   1 
ATOM   2572 N N   . THR A 1 375 ? -3.159  15.401  -28.548 1.00 74.70  ? 375 THR A N   1 
ATOM   2573 C CA  . THR A 1 375 ? -3.997  15.084  -27.405 1.00 72.22  ? 375 THR A CA  1 
ATOM   2574 C C   . THR A 1 375 ? -3.155  15.096  -26.136 1.00 72.81  ? 375 THR A C   1 
ATOM   2575 O O   . THR A 1 375 ? -1.929  15.038  -26.207 1.00 77.56  ? 375 THR A O   1 
ATOM   2576 C CB  . THR A 1 375 ? -4.678  13.736  -27.610 1.00 75.43  ? 375 THR A CB  1 
ATOM   2577 O OG1 . THR A 1 375 ? -3.675  12.730  -27.753 1.00 72.13  ? 375 THR A OG1 1 
ATOM   2578 C CG2 . THR A 1 375 ? -5.587  13.727  -28.825 1.00 71.90  ? 375 THR A CG2 1 
ATOM   2579 N N   . LEU A 1 376 ? -3.829  15.222  -24.990 1.00 72.34  ? 376 LEU A N   1 
ATOM   2580 C CA  . LEU A 1 376 ? -3.146  15.198  -23.671 1.00 58.55  ? 376 LEU A CA  1 
ATOM   2581 C C   . LEU A 1 376 ? -4.158  14.693  -22.632 1.00 72.32  ? 376 LEU A C   1 
ATOM   2582 O O   . LEU A 1 376 ? -5.366  14.879  -22.855 1.00 66.56  ? 376 LEU A O   1 
ATOM   2583 C CB  . LEU A 1 376 ? -2.583  16.564  -23.287 1.00 56.56  ? 376 LEU A CB  1 
ATOM   2584 C CG  . LEU A 1 376 ? -3.573  17.723  -23.181 1.00 71.11  ? 376 LEU A CG  1 
ATOM   2585 C CD1 . LEU A 1 376 ? -3.308  18.444  -21.877 1.00 64.06  ? 376 LEU A CD1 1 
ATOM   2586 C CD2 . LEU A 1 376 ? -3.336  18.652  -24.353 1.00 70.20  ? 376 LEU A CD2 1 
ATOM   2587 N N   . SER A 1 377 ? -3.685  14.055  -21.560 1.00 64.76  ? 377 SER A N   1 
ATOM   2588 C CA  . SER A 1 377 ? -4.598  13.594  -20.483 1.00 67.59  ? 377 SER A CA  1 
ATOM   2589 C C   . SER A 1 377 ? -4.173  14.220  -19.156 1.00 67.12  ? 377 SER A C   1 
ATOM   2590 O O   . SER A 1 377 ? -2.964  14.370  -18.939 1.00 68.22  ? 377 SER A O   1 
ATOM   2591 C CB  . SER A 1 377 ? -4.615  12.110  -20.369 1.00 68.15  ? 377 SER A CB  1 
ATOM   2592 O OG  . SER A 1 377 ? -4.659  11.728  -19.003 1.00 79.16  ? 377 SER A OG  1 
ATOM   2593 N N   . TYR A 1 378 ? -5.144  14.570  -18.319 1.00 63.77  ? 378 TYR A N   1 
ATOM   2594 C CA  . TYR A 1 378 ? -4.817  15.209  -17.020 1.00 71.15  ? 378 TYR A CA  1 
ATOM   2595 C C   . TYR A 1 378 ? -5.830  14.790  -15.968 1.00 77.05  ? 378 TYR A C   1 
ATOM   2596 O O   . TYR A 1 378 ? -6.980  14.463  -16.312 1.00 79.27  ? 378 TYR A O   1 
ATOM   2597 C CB  . TYR A 1 378 ? -4.661  16.730  -17.113 1.00 73.99  ? 378 TYR A CB  1 
ATOM   2598 C CG  . TYR A 1 378 ? -5.692  17.568  -17.853 1.00 80.00  ? 378 TYR A CG  1 
ATOM   2599 C CD1 . TYR A 1 378 ? -5.761  17.569  -19.239 1.00 77.79  ? 378 TYR A CD1 1 
ATOM   2600 C CD2 . TYR A 1 378 ? -6.548  18.414  -17.160 1.00 81.85  ? 378 TYR A CD2 1 
ATOM   2601 C CE1 . TYR A 1 378 ? -6.683  18.352  -19.911 1.00 80.10  ? 378 TYR A CE1 1 
ATOM   2602 C CE2 . TYR A 1 378 ? -7.470  19.206  -17.820 1.00 76.11  ? 378 TYR A CE2 1 
ATOM   2603 C CZ  . TYR A 1 378 ? -7.535  19.176  -19.200 1.00 77.71  ? 378 TYR A CZ  1 
ATOM   2604 O OH  . TYR A 1 378 ? -8.449  19.945  -19.857 1.00 87.02  ? 378 TYR A OH  1 
ATOM   2605 N N   . HIS A 1 379 ? -5.402  14.800  -14.708 1.00 69.40  ? 379 HIS A N   1 
ATOM   2606 C CA  . HIS A 1 379 ? -6.282  14.331  -13.607 1.00 77.66  ? 379 HIS A CA  1 
ATOM   2607 C C   . HIS A 1 379 ? -6.950  15.518  -12.910 1.00 82.54  ? 379 HIS A C   1 
ATOM   2608 O O   . HIS A 1 379 ? -6.396  16.627  -12.944 1.00 84.78  ? 379 HIS A O   1 
ATOM   2609 C CB  . HIS A 1 379 ? -5.483  13.458  -12.633 1.00 76.90  ? 379 HIS A CB  1 
ATOM   2610 C CG  . HIS A 1 379 ? -5.261  12.063  -13.106 1.00 70.60  ? 379 HIS A CG  1 
ATOM   2611 N ND1 . HIS A 1 379 ? -4.019  11.468  -13.120 1.00 58.80  ? 379 HIS A ND1 1 
ATOM   2612 C CD2 . HIS A 1 379 ? -6.114  11.149  -13.574 1.00 71.93  ? 379 HIS A CD2 1 
ATOM   2613 C CE1 . HIS A 1 379 ? -4.133  10.236  -13.589 1.00 56.55  ? 379 HIS A CE1 1 
ATOM   2614 N NE2 . HIS A 1 379 ? -5.397  10.022  -13.869 1.00 59.13  ? 379 HIS A NE2 1 
ATOM   2615 N N   . SER A 1 380 ? -8.106  15.279  -12.284 1.00 83.54  ? 380 SER A N   1 
ATOM   2616 C CA  . SER A 1 380 ? -8.860  16.346  -11.645 1.00 88.95  ? 380 SER A CA  1 
ATOM   2617 C C   . SER A 1 380 ? -8.437  16.560  -10.194 1.00 97.15  ? 380 SER A C   1 
ATOM   2618 O O   . SER A 1 380 ? -8.593  15.663  -9.367  1.00 99.22  ? 380 SER A O   1 
ATOM   2619 C CB  . SER A 1 380 ? -10.354 16.044  -11.686 1.00 87.28  ? 380 SER A CB  1 
ATOM   2620 O OG  . SER A 1 380 ? -10.683 14.979  -10.809 1.00 91.68  ? 380 SER A OG  1 
ATOM   2621 N N   . LEU A 1 381 ? -7.912  17.758  -9.900  1.00 95.96  ? 381 LEU A N   1 
ATOM   2622 C CA  . LEU A 1 381 ? -7.549  18.145  -8.545  1.00 100.32 ? 381 LEU A CA  1 
ATOM   2623 C C   . LEU A 1 381 ? -6.834  16.989  -7.846  1.00 99.28  ? 381 LEU A C   1 
ATOM   2624 O O   . LEU A 1 381 ? -5.861  16.460  -8.380  1.00 102.51 ? 381 LEU A O   1 
ATOM   2625 C CB  . LEU A 1 381 ? -8.816  18.588  -7.789  1.00 102.09 ? 381 LEU A CB  1 
ATOM   2626 N N   . SER A 1 382 ? -7.313  16.616  -6.651  1.00 104.03 ? 382 SER A N   1 
ATOM   2627 C CA  . SER A 1 382 ? -6.924  15.375  -5.999  1.00 98.65  ? 382 SER A CA  1 
ATOM   2628 C C   . SER A 1 382 ? -8.096  14.395  -5.910  1.00 99.80  ? 382 SER A C   1 
ATOM   2629 O O   . SER A 1 382 ? -8.005  13.377  -5.223  1.00 102.94 ? 382 SER A O   1 
ATOM   2630 C CB  . SER A 1 382 ? -6.361  15.665  -4.610  1.00 98.41  ? 382 SER A CB  1 
ATOM   2631 N N   . GLY A 1 383 ? -9.188  14.702  -6.627  1.00 92.62  ? 383 GLY A N   1 
ATOM   2632 C CA  . GLY A 1 383 ? -10.375 13.862  -6.654  1.00 92.01  ? 383 GLY A CA  1 
ATOM   2633 C C   . GLY A 1 383 ? -10.239 12.686  -7.619  1.00 97.41  ? 383 GLY A C   1 
ATOM   2634 O O   . GLY A 1 383 ? -9.139  12.176  -7.818  1.00 96.80  ? 383 GLY A O   1 
ATOM   2635 N N   . ASN A 1 384 ? -11.363 12.264  -8.217  1.00 88.83  ? 384 ASN A N   1 
ATOM   2636 C CA  . ASN A 1 384 ? -11.369 11.128  -9.127  1.00 90.39  ? 384 ASN A CA  1 
ATOM   2637 C C   . ASN A 1 384 ? -12.027 11.500  -10.455 1.00 84.62  ? 384 ASN A C   1 
ATOM   2638 O O   . ASN A 1 384 ? -13.236 11.348  -10.619 1.00 84.47  ? 384 ASN A O   1 
ATOM   2639 C CB  . ASN A 1 384 ? -12.090 9.900   -8.516  1.00 89.57  ? 384 ASN A CB  1 
ATOM   2640 C CG  . ASN A 1 384 ? -12.422 10.020  -7.053  1.00 81.56  ? 384 ASN A CG  1 
ATOM   2641 O OD1 . ASN A 1 384 ? -11.598 10.403  -6.223  1.00 85.55  ? 384 ASN A OD1 1 
ATOM   2642 N ND2 . ASN A 1 384 ? -13.657 9.702   -6.716  1.00 82.99  ? 384 ASN A ND2 1 
ATOM   2643 N N   . THR A 1 385 ? -11.215 11.997  -11.393 1.00 86.22  ? 385 THR A N   1 
ATOM   2644 C CA  . THR A 1 385 ? -11.656 12.242  -12.758 1.00 84.22  ? 385 THR A CA  1 
ATOM   2645 C C   . THR A 1 385 ? -10.449 12.520  -13.652 1.00 81.64  ? 385 THR A C   1 
ATOM   2646 O O   . THR A 1 385 ? -9.556  13.277  -13.277 1.00 79.98  ? 385 THR A O   1 
ATOM   2647 C CB  . THR A 1 385 ? -12.708 13.376  -12.806 1.00 88.53  ? 385 THR A CB  1 
ATOM   2648 O OG1 . THR A 1 385 ? -14.009 12.820  -12.578 1.00 81.76  ? 385 THR A OG1 1 
ATOM   2649 C CG2 . THR A 1 385 ? -12.718 14.124  -14.138 1.00 81.06  ? 385 THR A CG2 1 
ATOM   2650 N N   . GLU A 1 386 ? -10.438 11.890  -14.833 1.00 79.91  ? 386 GLU A N   1 
ATOM   2651 C CA  . GLU A 1 386 ? -9.403  12.107  -15.829 1.00 75.31  ? 386 GLU A CA  1 
ATOM   2652 C C   . GLU A 1 386 ? -10.055 12.655  -17.095 1.00 82.85  ? 386 GLU A C   1 
ATOM   2653 O O   . GLU A 1 386 ? -10.910 11.996  -17.686 1.00 81.73  ? 386 GLU A O   1 
ATOM   2654 C CB  . GLU A 1 386 ? -8.640  10.802  -16.118 1.00 81.42  ? 386 GLU A CB  1 
ATOM   2655 C CG  . GLU A 1 386 ? -7.569  10.932  -17.193 1.00 76.13  ? 386 GLU A CG  1 
ATOM   2656 C CD  . GLU A 1 386 ? -6.503  9.851   -17.169 1.00 81.49  ? 386 GLU A CD  1 
ATOM   2657 O OE1 . GLU A 1 386 ? -6.858  8.656   -17.289 1.00 81.58  ? 386 GLU A OE1 1 
ATOM   2658 O OE2 . GLU A 1 386 ? -5.307  10.203  -17.035 1.00 69.53  ? 386 GLU A OE2 1 
ATOM   2659 N N   . THR A 1 387 ? -9.648  13.869  -17.491 1.00 82.87  ? 387 THR A N   1 
ATOM   2660 C CA  . THR A 1 387 ? -10.163 14.503  -18.694 1.00 84.02  ? 387 THR A CA  1 
ATOM   2661 C C   . THR A 1 387 ? -9.192  14.266  -19.846 1.00 74.95  ? 387 THR A C   1 
ATOM   2662 O O   . THR A 1 387 ? -8.004  14.554  -19.723 1.00 72.99  ? 387 THR A O   1 
ATOM   2663 C CB  . THR A 1 387 ? -10.411 16.011  -18.491 1.00 79.91  ? 387 THR A CB  1 
ATOM   2664 O OG1 . THR A 1 387 ? -9.220  16.731  -18.795 1.00 83.64  ? 387 THR A OG1 1 
ATOM   2665 C CG2 . THR A 1 387 ? -10.877 16.348  -17.081 1.00 83.44  ? 387 THR A CG2 1 
ATOM   2666 N N   . PHE A 1 388 ? -9.715  13.730  -20.954 1.00 77.30  ? 388 PHE A N   1 
ATOM   2667 C CA  . PHE A 1 388 ? -8.941  13.529  -22.165 1.00 69.51  ? 388 PHE A CA  1 
ATOM   2668 C C   . PHE A 1 388 ? -9.150  14.743  -23.064 1.00 78.93  ? 388 PHE A C   1 
ATOM   2669 O O   . PHE A 1 388 ? -10.278 15.035  -23.461 1.00 80.46  ? 388 PHE A O   1 
ATOM   2670 C CB  . PHE A 1 388 ? -9.352  12.239  -22.885 1.00 80.47  ? 388 PHE A CB  1 
ATOM   2671 C CG  . PHE A 1 388 ? -9.132  10.970  -22.087 1.00 84.77  ? 388 PHE A CG  1 
ATOM   2672 C CD1 . PHE A 1 388 ? -9.929  10.671  -20.993 1.00 74.03  ? 388 PHE A CD1 1 
ATOM   2673 C CD2 . PHE A 1 388 ? -8.132  10.077  -22.434 1.00 89.11  ? 388 PHE A CD2 1 
ATOM   2674 C CE1 . PHE A 1 388 ? -9.729  9.504   -20.267 1.00 86.20  ? 388 PHE A CE1 1 
ATOM   2675 C CE2 . PHE A 1 388 ? -7.934  8.912   -21.702 1.00 91.13  ? 388 PHE A CE2 1 
ATOM   2676 C CZ  . PHE A 1 388 ? -8.733  8.632   -20.625 1.00 86.83  ? 388 PHE A CZ  1 
ATOM   2677 N N   . LEU A 1 389 ? -8.050  15.446  -23.365 1.00 76.47  ? 389 LEU A N   1 
ATOM   2678 C CA  . LEU A 1 389 ? -8.104  16.698  -24.101 1.00 70.82  ? 389 LEU A CA  1 
ATOM   2679 C C   . LEU A 1 389 ? -7.495  16.547  -25.489 1.00 64.04  ? 389 LEU A C   1 
ATOM   2680 O O   . LEU A 1 389 ? -6.484  15.872  -25.656 1.00 69.47  ? 389 LEU A O   1 
ATOM   2681 C CB  . LEU A 1 389 ? -7.370  17.792  -23.308 1.00 70.10  ? 389 LEU A CB  1 
ATOM   2682 C CG  . LEU A 1 389 ? -7.197  19.150  -23.995 1.00 73.47  ? 389 LEU A CG  1 
ATOM   2683 C CD1 . LEU A 1 389 ? -8.542  19.768  -24.394 1.00 70.59  ? 389 LEU A CD1 1 
ATOM   2684 C CD2 . LEU A 1 389 ? -6.447  20.108  -23.095 1.00 66.75  ? 389 LEU A CD2 1 
ATOM   2685 N N   . ALA A 1 390 ? -8.152  17.165  -26.477 1.00 73.36  ? 390 ALA A N   1 
ATOM   2686 C CA  . ALA A 1 390 ? -7.574  17.391  -27.790 1.00 67.38  ? 390 ALA A CA  1 
ATOM   2687 C C   . ALA A 1 390 ? -7.461  18.897  -28.004 1.00 63.11  ? 390 ALA A C   1 
ATOM   2688 O O   . ALA A 1 390 ? -8.355  19.641  -27.615 1.00 65.33  ? 390 ALA A O   1 
ATOM   2689 C CB  . ALA A 1 390 ? -8.424  16.751  -28.868 1.00 72.06  ? 390 ALA A CB  1 
ATOM   2690 N N   . ILE A 1 391 ? -6.340  19.330  -28.593 1.00 70.12  ? 391 ILE A N   1 
ATOM   2691 C CA  . ILE A 1 391 ? -6.067  20.735  -28.835 1.00 61.69  ? 391 ILE A CA  1 
ATOM   2692 C C   . ILE A 1 391 ? -5.745  20.901  -30.316 1.00 67.28  ? 391 ILE A C   1 
ATOM   2693 O O   . ILE A 1 391 ? -5.072  20.055  -30.902 1.00 63.11  ? 391 ILE A O   1 
ATOM   2694 C CB  . ILE A 1 391 ? -4.925  21.247  -27.932 1.00 74.15  ? 391 ILE A CB  1 
ATOM   2695 N N   . GLN A 1 392 ? -6.249  21.994  -30.905 1.00 68.47  ? 392 GLN A N   1 
ATOM   2696 C CA  . GLN A 1 392 ? -6.111  22.259  -32.328 1.00 65.70  ? 392 GLN A CA  1 
ATOM   2697 C C   . GLN A 1 392 ? -5.681  23.710  -32.528 1.00 65.52  ? 392 GLN A C   1 
ATOM   2698 O O   . GLN A 1 392 ? -6.525  24.602  -32.620 1.00 66.44  ? 392 GLN A O   1 
ATOM   2699 C CB  . GLN A 1 392 ? -7.435  21.973  -33.067 1.00 65.83  ? 392 GLN A CB  1 
ATOM   2700 C CG  . GLN A 1 392 ? -7.380  22.211  -34.580 1.00 67.44  ? 392 GLN A CG  1 
ATOM   2701 C CD  . GLN A 1 392 ? -6.447  21.249  -35.283 1.00 71.09  ? 392 GLN A CD  1 
ATOM   2702 O OE1 . GLN A 1 392 ? -6.668  20.032  -35.296 1.00 81.26  ? 392 GLN A OE1 1 
ATOM   2703 N NE2 . GLN A 1 392 ? -5.382  21.766  -35.887 1.00 59.20  ? 392 GLN A NE2 1 
ATOM   2704 N N   . PRO A 1 393 ? -4.359  23.990  -32.590 1.00 61.57  ? 393 PRO A N   1 
ATOM   2705 C CA  . PRO A 1 393 ? -3.883  25.343  -32.856 1.00 62.99  ? 393 PRO A CA  1 
ATOM   2706 C C   . PRO A 1 393 ? -4.171  25.809  -34.280 1.00 62.38  ? 393 PRO A C   1 
ATOM   2707 O O   . PRO A 1 393 ? -4.285  24.991  -35.191 1.00 57.83  ? 393 PRO A O   1 
ATOM   2708 C CB  . PRO A 1 393 ? -2.369  25.262  -32.585 1.00 61.02  ? 393 PRO A CB  1 
ATOM   2709 C CG  . PRO A 1 393 ? -2.115  23.875  -31.993 1.00 64.72  ? 393 PRO A CG  1 
ATOM   2710 C CD  . PRO A 1 393 ? -3.270  23.017  -32.399 1.00 69.03  ? 393 PRO A CD  1 
ATOM   2711 N N   . PHE A 1 394 ? -4.291  27.131  -34.450 1.00 54.74  ? 394 PHE A N   1 
ATOM   2712 C CA  . PHE A 1 394 ? -4.455  27.736  -35.763 1.00 66.95  ? 394 PHE A CA  1 
ATOM   2713 C C   . PHE A 1 394 ? -4.117  29.223  -35.711 1.00 56.29  ? 394 PHE A C   1 
ATOM   2714 O O   . PHE A 1 394 ? -4.348  29.879  -34.698 1.00 57.82  ? 394 PHE A O   1 
ATOM   2715 C CB  . PHE A 1 394 ? -5.893  27.539  -36.304 1.00 60.58  ? 394 PHE A CB  1 
ATOM   2716 C CG  . PHE A 1 394 ? -6.992  28.222  -35.522 1.00 58.34  ? 394 PHE A CG  1 
ATOM   2717 C CD1 . PHE A 1 394 ? -7.381  27.749  -34.281 1.00 61.42  ? 394 PHE A CD1 1 
ATOM   2718 C CD2 . PHE A 1 394 ? -7.641  29.334  -36.032 1.00 64.54  ? 394 PHE A CD2 1 
ATOM   2719 C CE1 . PHE A 1 394 ? -8.400  28.373  -33.566 1.00 57.52  ? 394 PHE A CE1 1 
ATOM   2720 C CE2 . PHE A 1 394 ? -8.658  29.958  -35.312 1.00 64.34  ? 394 PHE A CE2 1 
ATOM   2721 C CZ  . PHE A 1 394 ? -9.030  29.473  -34.084 1.00 57.65  ? 394 PHE A CZ  1 
ATOM   2722 N N   . ASP A 1 395 ? -3.570  29.746  -36.813 1.00 59.12  ? 395 ASP A N   1 
ATOM   2723 C CA  . ASP A 1 395 ? -3.328  31.175  -36.934 1.00 72.13  ? 395 ASP A CA  1 
ATOM   2724 C C   . ASP A 1 395 ? -4.533  31.847  -37.585 1.00 58.20  ? 395 ASP A C   1 
ATOM   2725 O O   . ASP A 1 395 ? -4.979  31.421  -38.647 1.00 57.81  ? 395 ASP A O   1 
ATOM   2726 C CB  . ASP A 1 395 ? -2.032  31.465  -37.712 1.00 64.82  ? 395 ASP A CB  1 
ATOM   2727 C CG  . ASP A 1 395 ? -0.792  31.045  -36.941 1.00 72.34  ? 395 ASP A CG  1 
ATOM   2728 O OD1 . ASP A 1 395 ? -0.459  29.841  -36.962 1.00 74.18  ? 395 ASP A OD1 1 
ATOM   2729 O OD2 . ASP A 1 395 ? -0.182  31.914  -36.277 1.00 70.68  ? 395 ASP A OD2 1 
ATOM   2730 N N   . PHE A 1 396 ? -5.063  32.880  -36.916 1.00 56.47  ? 396 PHE A N   1 
ATOM   2731 C CA  . PHE A 1 396 ? -6.222  33.613  -37.402 1.00 67.01  ? 396 PHE A CA  1 
ATOM   2732 C C   . PHE A 1 396 ? -5.823  34.859  -38.191 1.00 68.42  ? 396 PHE A C   1 
ATOM   2733 O O   . PHE A 1 396 ? -6.682  35.640  -38.591 1.00 65.54  ? 396 PHE A O   1 
ATOM   2734 C CB  . PHE A 1 396 ? -7.158  33.973  -36.228 1.00 63.06  ? 396 PHE A CB  1 
ATOM   2735 C CG  . PHE A 1 396 ? -6.673  35.024  -35.255 1.00 57.26  ? 396 PHE A CG  1 
ATOM   2736 C CD1 . PHE A 1 396 ? -6.897  36.368  -35.492 1.00 65.19  ? 396 PHE A CD1 1 
ATOM   2737 C CD2 . PHE A 1 396 ? -6.012  34.665  -34.095 1.00 60.88  ? 396 PHE A CD2 1 
ATOM   2738 C CE1 . PHE A 1 396 ? -6.461  37.333  -34.589 1.00 58.51  ? 396 PHE A CE1 1 
ATOM   2739 C CE2 . PHE A 1 396 ? -5.576  35.633  -33.197 1.00 63.36  ? 396 PHE A CE2 1 
ATOM   2740 C CZ  . PHE A 1 396 ? -5.803  36.961  -33.451 1.00 57.10  ? 396 PHE A CZ  1 
ATOM   2741 N N   . PHE A 1 397 ? -4.511  35.036  -38.391 1.00 63.69  ? 397 PHE A N   1 
ATOM   2742 C CA  . PHE A 1 397 ? -3.970  36.066  -39.259 1.00 57.97  ? 397 PHE A CA  1 
ATOM   2743 C C   . PHE A 1 397 ? -2.598  35.594  -39.728 1.00 72.70  ? 397 PHE A C   1 
ATOM   2744 O O   . PHE A 1 397 ? -1.667  35.501  -38.931 1.00 70.87  ? 397 PHE A O   1 
ATOM   2745 C CB  . PHE A 1 397 ? -3.864  37.409  -38.537 1.00 52.36  ? 397 PHE A CB  1 
ATOM   2746 C CG  . PHE A 1 397 ? -3.377  38.536  -39.417 1.00 69.05  ? 397 PHE A CG  1 
ATOM   2747 C CD1 . PHE A 1 397 ? -4.201  39.090  -40.382 1.00 67.41  ? 397 PHE A CD1 1 
ATOM   2748 C CD2 . PHE A 1 397 ? -2.087  39.028  -39.292 1.00 71.58  ? 397 PHE A CD2 1 
ATOM   2749 C CE1 . PHE A 1 397 ? -3.750  40.126  -41.191 1.00 62.42  ? 397 PHE A CE1 1 
ATOM   2750 C CE2 . PHE A 1 397 ? -1.643  40.065  -40.106 1.00 65.50  ? 397 PHE A CE2 1 
ATOM   2751 C CZ  . PHE A 1 397 ? -2.475  40.604  -41.049 1.00 65.19  ? 397 PHE A CZ  1 
ATOM   2752 N N   . GLU A 1 398 ? -2.489  35.295  -41.025 1.00 82.91  ? 398 GLU A N   1 
ATOM   2753 C CA  . GLU A 1 398 ? -1.332  34.596  -41.563 1.00 89.05  ? 398 GLU A CA  1 
ATOM   2754 C C   . GLU A 1 398 ? -0.213  35.534  -42.006 1.00 85.28  ? 398 GLU A C   1 
ATOM   2755 O O   . GLU A 1 398 ? 0.956   35.167  -41.932 1.00 91.02  ? 398 GLU A O   1 
ATOM   2756 C CB  . GLU A 1 398 ? -1.793  33.714  -42.729 1.00 91.02  ? 398 GLU A CB  1 
ATOM   2757 C CG  . GLU A 1 398 ? -2.654  32.551  -42.267 1.00 86.63  ? 398 GLU A CG  1 
ATOM   2758 C CD  . GLU A 1 398 ? -3.873  32.294  -43.126 1.00 103.60 ? 398 GLU A CD  1 
ATOM   2759 O OE1 . GLU A 1 398 ? -3.709  32.084  -44.349 1.00 107.64 ? 398 GLU A OE1 1 
ATOM   2760 O OE2 . GLU A 1 398 ? -4.997  32.311  -42.574 1.00 107.22 ? 398 GLU A OE2 1 
ATOM   2761 N N   . GLU A 1 399 ? -0.584  36.744  -42.443 1.00 78.11  ? 399 GLU A N   1 
ATOM   2762 C CA  . GLU A 1 399 ? 0.353   37.674  -43.055 1.00 86.99  ? 399 GLU A CA  1 
ATOM   2763 C C   . GLU A 1 399 ? 1.583   37.959  -42.193 1.00 92.14  ? 399 GLU A C   1 
ATOM   2764 O O   . GLU A 1 399 ? 2.711   37.772  -42.648 1.00 90.44  ? 399 GLU A O   1 
ATOM   2765 C CB  . GLU A 1 399 ? -0.356  38.997  -43.392 1.00 85.47  ? 399 GLU A CB  1 
ATOM   2766 N N   . LYS A 1 400 ? 1.357   38.401  -40.948 1.00 87.22  ? 400 LYS A N   1 
ATOM   2767 C CA  . LYS A 1 400 ? 2.439   38.824  -40.071 1.00 83.85  ? 400 LYS A CA  1 
ATOM   2768 C C   . LYS A 1 400 ? 2.984   37.638  -39.277 1.00 84.58  ? 400 LYS A C   1 
ATOM   2769 O O   . LYS A 1 400 ? 2.220   36.915  -38.641 1.00 86.98  ? 400 LYS A O   1 
ATOM   2770 C CB  . LYS A 1 400 ? 1.962   39.929  -39.115 1.00 77.50  ? 400 LYS A CB  1 
ATOM   2771 N N   . GLY A 1 401 ? 4.310   37.454  -39.325 1.00 84.82  ? 401 GLY A N   1 
ATOM   2772 C CA  . GLY A 1 401 ? 4.972   36.367  -38.621 1.00 87.68  ? 401 GLY A CA  1 
ATOM   2773 C C   . GLY A 1 401 ? 6.363   36.087  -39.154 1.00 86.06  ? 401 GLY A C   1 
ATOM   2774 O O   . GLY A 1 401 ? 6.527   35.753  -40.328 1.00 83.81  ? 401 GLY A O   1 
ATOM   2775 N N   . ASN A 1 405 ? 3.267   32.778  -35.019 1.00 69.57  ? 405 ASN A N   1 
ATOM   2776 C CA  . ASN A 1 405 ? 3.796   33.126  -33.701 1.00 74.12  ? 405 ASN A CA  1 
ATOM   2777 C C   . ASN A 1 405 ? 2.803   33.975  -32.906 1.00 72.59  ? 405 ASN A C   1 
ATOM   2778 O O   . ASN A 1 405 ? 2.216   33.498  -31.937 1.00 69.10  ? 405 ASN A O   1 
ATOM   2779 C CB  . ASN A 1 405 ? 5.157   33.844  -33.835 1.00 74.88  ? 405 ASN A CB  1 
ATOM   2780 N N   . HIS A 1 406 ? 2.591   35.221  -33.348 1.00 79.61  ? 406 HIS A N   1 
ATOM   2781 C CA  . HIS A 1 406 ? 1.862   36.210  -32.566 1.00 78.10  ? 406 HIS A CA  1 
ATOM   2782 C C   . HIS A 1 406 ? 0.353   36.242  -32.820 1.00 76.05  ? 406 HIS A C   1 
ATOM   2783 O O   . HIS A 1 406 ? -0.382  36.838  -32.034 1.00 68.28  ? 406 HIS A O   1 
ATOM   2784 C CB  . HIS A 1 406 ? 2.458   37.609  -32.823 1.00 75.61  ? 406 HIS A CB  1 
ATOM   2785 N N   . TRP A 1 407 ? -0.110  35.603  -33.906 1.00 70.71  ? 407 TRP A N   1 
ATOM   2786 C CA  . TRP A 1 407 ? -1.525  35.606  -34.257 1.00 71.74  ? 407 TRP A CA  1 
ATOM   2787 C C   . TRP A 1 407 ? -2.148  34.211  -34.240 1.00 68.66  ? 407 TRP A C   1 
ATOM   2788 O O   . TRP A 1 407 ? -2.796  33.812  -35.204 1.00 66.80  ? 407 TRP A O   1 
ATOM   2789 C CB  . TRP A 1 407 ? -1.738  36.239  -35.644 1.00 53.12  ? 407 TRP A CB  1 
ATOM   2790 C CG  . TRP A 1 407 ? -1.209  37.632  -35.769 1.00 63.70  ? 407 TRP A CG  1 
ATOM   2791 C CD1 . TRP A 1 407 ? 0.077   38.007  -36.016 1.00 66.57  ? 407 TRP A CD1 1 
ATOM   2792 C CD2 . TRP A 1 407 ? -1.960  38.840  -35.625 1.00 61.57  ? 407 TRP A CD2 1 
ATOM   2793 N NE1 . TRP A 1 407 ? 0.171   39.376  -36.047 1.00 64.22  ? 407 TRP A NE1 1 
ATOM   2794 C CE2 . TRP A 1 407 ? -1.067  39.914  -35.811 1.00 59.81  ? 407 TRP A CE2 1 
ATOM   2795 C CE3 . TRP A 1 407 ? -3.305  39.119  -35.361 1.00 62.57  ? 407 TRP A CE3 1 
ATOM   2796 C CZ2 . TRP A 1 407 ? -1.477  41.244  -35.738 1.00 62.34  ? 407 TRP A CZ2 1 
ATOM   2797 C CZ3 . TRP A 1 407 ? -3.711  40.436  -35.291 1.00 55.91  ? 407 TRP A CZ3 1 
ATOM   2798 C CH2 . TRP A 1 407 ? -2.804  41.481  -35.473 1.00 54.20  ? 407 TRP A CH2 1 
ATOM   2799 N N   . ARG A 1 408 ? -1.967  33.487  -33.129 1.00 66.69  ? 408 ARG A N   1 
ATOM   2800 C CA  . ARG A 1 408 ? -2.378  32.095  -33.037 1.00 63.70  ? 408 ARG A CA  1 
ATOM   2801 C C   . ARG A 1 408 ? -3.341  31.856  -31.877 1.00 58.82  ? 408 ARG A C   1 
ATOM   2802 O O   . ARG A 1 408 ? -3.155  32.393  -30.788 1.00 66.15  ? 408 ARG A O   1 
ATOM   2803 C CB  . ARG A 1 408 ? -1.142  31.186  -32.901 1.00 64.33  ? 408 ARG A CB  1 
ATOM   2804 C CG  . ARG A 1 408 ? -1.457  29.695  -32.932 1.00 59.18  ? 408 ARG A CG  1 
ATOM   2805 C CD  . ARG A 1 408 ? -0.382  28.883  -33.631 1.00 56.38  ? 408 ARG A CD  1 
ATOM   2806 N NE  . ARG A 1 408 ? 0.950   29.139  -33.089 1.00 68.17  ? 408 ARG A NE  1 
ATOM   2807 C CZ  . ARG A 1 408 ? 2.040   29.362  -33.817 1.00 74.15  ? 408 ARG A CZ  1 
ATOM   2808 N NH1 . ARG A 1 408 ? 1.991   29.432  -35.138 1.00 59.92  ? 408 ARG A NH1 1 
ATOM   2809 N NH2 . ARG A 1 408 ? 3.212   29.505  -33.204 1.00 69.81  ? 408 ARG A NH2 1 
ATOM   2810 N N   . TRP A 1 409 ? -4.384  31.064  -32.152 1.00 55.96  ? 409 TRP A N   1 
ATOM   2811 C CA  . TRP A 1 409 ? -5.302  30.572  -31.139 1.00 60.03  ? 409 TRP A CA  1 
ATOM   2812 C C   . TRP A 1 409 ? -5.286  29.048  -31.189 1.00 58.68  ? 409 TRP A C   1 
ATOM   2813 O O   . TRP A 1 409 ? -4.583  28.459  -32.009 1.00 55.96  ? 409 TRP A O   1 
ATOM   2814 C CB  . TRP A 1 409 ? -6.738  31.091  -31.363 1.00 51.96  ? 409 TRP A CB  1 
ATOM   2815 C CG  . TRP A 1 409 ? -6.977  32.528  -30.996 1.00 57.59  ? 409 TRP A CG  1 
ATOM   2816 C CD1 . TRP A 1 409 ? -6.168  33.343  -30.260 1.00 57.50  ? 409 TRP A CD1 1 
ATOM   2817 C CD2 . TRP A 1 409 ? -8.110  33.321  -31.370 1.00 46.42  ? 409 TRP A CD2 1 
ATOM   2818 N NE1 . TRP A 1 409 ? -6.730  34.593  -30.149 1.00 56.52  ? 409 TRP A NE1 1 
ATOM   2819 C CE2 . TRP A 1 409 ? -7.925  34.606  -30.820 1.00 50.86  ? 409 TRP A CE2 1 
ATOM   2820 C CE3 . TRP A 1 409 ? -9.264  33.070  -32.120 1.00 58.44  ? 409 TRP A CE3 1 
ATOM   2821 C CZ2 . TRP A 1 409 ? -8.849  35.633  -30.998 1.00 56.99  ? 409 TRP A CZ2 1 
ATOM   2822 C CZ3 . TRP A 1 409 ? -10.178 34.089  -32.291 1.00 61.84  ? 409 TRP A CZ3 1 
ATOM   2823 C CH2 . TRP A 1 409 ? -9.967  35.353  -31.734 1.00 57.73  ? 409 TRP A CH2 1 
ATOM   2824 N N   . ALA A 1 410 ? -6.072  28.426  -30.307 1.00 49.20  ? 410 ALA A N   1 
ATOM   2825 C CA  . ALA A 1 410 ? -6.338  27.001  -30.388 1.00 59.93  ? 410 ALA A CA  1 
ATOM   2826 C C   . ALA A 1 410 ? -7.745  26.682  -29.888 1.00 60.90  ? 410 ALA A C   1 
ATOM   2827 O O   . ALA A 1 410 ? -8.317  27.429  -29.093 1.00 60.93  ? 410 ALA A O   1 
ATOM   2828 C CB  . ALA A 1 410 ? -5.305  26.232  -29.586 1.00 57.99  ? 410 ALA A CB  1 
ATOM   2829 N N   . ILE A 1 411 ? -8.292  25.564  -30.374 1.00 59.47  ? 411 ILE A N   1 
ATOM   2830 C CA  . ILE A 1 411 ? -9.531  25.018  -29.851 1.00 56.15  ? 411 ILE A CA  1 
ATOM   2831 C C   . ILE A 1 411 ? -9.228  23.712  -29.125 1.00 66.39  ? 411 ILE A C   1 
ATOM   2832 O O   . ILE A 1 411 ? -8.640  22.802  -29.706 1.00 72.18  ? 411 ILE A O   1 
ATOM   2833 C CB  . ILE A 1 411 ? -10.564 24.810  -30.972 1.00 66.51  ? 411 ILE A CB  1 
ATOM   2834 C CG1 . ILE A 1 411 ? -11.050 26.167  -31.527 1.00 65.50  ? 411 ILE A CG1 1 
ATOM   2835 C CG2 . ILE A 1 411 ? -11.737 23.943  -30.489 1.00 61.59  ? 411 ILE A CG2 1 
ATOM   2836 C CD1 . ILE A 1 411 ? -11.582 26.097  -32.836 1.00 65.61  ? 411 ILE A CD1 1 
ATOM   2837 N N   . GLY A 1 412 ? -9.631  23.643  -27.853 1.00 59.57  ? 412 GLY A N   1 
ATOM   2838 C CA  . GLY A 1 412 ? -9.599  22.401  -27.101 1.00 70.93  ? 412 GLY A CA  1 
ATOM   2839 C C   . GLY A 1 412 ? -10.985 21.773  -26.965 1.00 69.45  ? 412 GLY A C   1 
ATOM   2840 O O   . GLY A 1 412 ? -11.925 22.443  -26.544 1.00 67.15  ? 412 GLY A O   1 
ATOM   2841 N N   . LYS A 1 413 ? -11.093 20.494  -27.352 1.00 69.00  ? 413 LYS A N   1 
ATOM   2842 C CA  . LYS A 1 413 ? -12.293 19.702  -27.132 1.00 72.47  ? 413 LYS A CA  1 
ATOM   2843 C C   . LYS A 1 413 ? -11.958 18.567  -26.166 1.00 79.83  ? 413 LYS A C   1 
ATOM   2844 O O   . LYS A 1 413 ? -11.208 17.655  -26.515 1.00 76.76  ? 413 LYS A O   1 
ATOM   2845 C CB  . LYS A 1 413 ? -12.846 19.148  -28.457 1.00 72.34  ? 413 LYS A CB  1 
ATOM   2846 N N   . TYR A 1 414 ? -12.530 18.633  -24.955 1.00 66.57  ? 414 TYR A N   1 
ATOM   2847 C CA  . TYR A 1 414 ? -12.160 17.738  -23.869 1.00 79.09  ? 414 TYR A CA  1 
ATOM   2848 C C   . TYR A 1 414 ? -13.281 16.756  -23.534 1.00 84.34  ? 414 TYR A C   1 
ATOM   2849 O O   . TYR A 1 414 ? -14.442 16.991  -23.865 1.00 77.73  ? 414 TYR A O   1 
ATOM   2850 C CB  . TYR A 1 414 ? -11.740 18.520  -22.602 1.00 75.43  ? 414 TYR A CB  1 
ATOM   2851 C CG  . TYR A 1 414 ? -12.671 19.637  -22.178 1.00 78.79  ? 414 TYR A CG  1 
ATOM   2852 C CD1 . TYR A 1 414 ? -12.708 20.839  -22.870 1.00 76.77  ? 414 TYR A CD1 1 
ATOM   2853 C CD2 . TYR A 1 414 ? -13.500 19.498  -21.072 1.00 82.85  ? 414 TYR A CD2 1 
ATOM   2854 C CE1 . TYR A 1 414 ? -13.556 21.871  -22.482 1.00 75.19  ? 414 TYR A CE1 1 
ATOM   2855 C CE2 . TYR A 1 414 ? -14.354 20.523  -20.675 1.00 73.41  ? 414 TYR A CE2 1 
ATOM   2856 C CZ  . TYR A 1 414 ? -14.377 21.709  -21.383 1.00 77.61  ? 414 TYR A CZ  1 
ATOM   2857 O OH  . TYR A 1 414 ? -15.214 22.729  -20.999 1.00 89.19  ? 414 TYR A OH  1 
ATOM   2858 N N   . VAL A 1 415 ? -12.898 15.647  -22.888 1.00 75.22  ? 415 VAL A N   1 
ATOM   2859 C CA  . VAL A 1 415 ? -13.835 14.627  -22.442 1.00 76.28  ? 415 VAL A CA  1 
ATOM   2860 C C   . VAL A 1 415 ? -13.444 14.185  -21.034 1.00 80.67  ? 415 VAL A C   1 
ATOM   2861 O O   . VAL A 1 415 ? -12.454 13.478  -20.861 1.00 79.27  ? 415 VAL A O   1 
ATOM   2862 C CB  . VAL A 1 415 ? -13.884 13.428  -23.416 1.00 71.29  ? 415 VAL A CB  1 
ATOM   2863 N N   . ASN A 1 416 ? -14.228 14.627  -20.041 1.00 73.00  ? 416 ASN A N   1 
ATOM   2864 C CA  . ASN A 1 416 ? -14.000 14.289  -18.645 1.00 79.13  ? 416 ASN A CA  1 
ATOM   2865 C C   . ASN A 1 416 ? -14.563 12.905  -18.323 1.00 86.09  ? 416 ASN A C   1 
ATOM   2866 O O   . ASN A 1 416 ? -15.697 12.593  -18.680 1.00 85.42  ? 416 ASN A O   1 
ATOM   2867 C CB  . ASN A 1 416 ? -14.616 15.343  -17.725 1.00 73.18  ? 416 ASN A CB  1 
ATOM   2868 N N   . LYS A 1 417 ? -13.754 12.082  -17.646 1.00 83.20  ? 417 LYS A N   1 
ATOM   2869 C CA  . LYS A 1 417 ? -14.137 10.723  -17.300 1.00 85.40  ? 417 LYS A CA  1 
ATOM   2870 C C   . LYS A 1 417 ? -13.891 10.469  -15.815 1.00 88.68  ? 417 LYS A C   1 
ATOM   2871 O O   . LYS A 1 417 ? -12.854 10.859  -15.283 1.00 80.78  ? 417 LYS A O   1 
ATOM   2872 C CB  . LYS A 1 417 ? -13.350 9.711   -18.150 1.00 91.06  ? 417 LYS A CB  1 
ATOM   2873 N N   . SER A 1 418 ? -14.859 9.817   -15.160 1.00 88.87  ? 418 SER A N   1 
ATOM   2874 C CA  . SER A 1 418 ? -14.742 9.471   -13.753 1.00 88.39  ? 418 SER A CA  1 
ATOM   2875 C C   . SER A 1 418 ? -13.765 8.310   -13.583 1.00 91.96  ? 418 SER A C   1 
ATOM   2876 O O   . SER A 1 418 ? -13.905 7.281   -14.242 1.00 92.16  ? 418 SER A O   1 
ATOM   2877 C CB  . SER A 1 418 ? -16.105 9.117   -13.163 1.00 75.36  ? 418 SER A CB  1 
ATOM   2878 N N   . LEU A 1 419 ? -12.774 8.492   -12.701 1.00 86.14  ? 419 LEU A N   1 
ATOM   2879 C CA  . LEU A 1 419 ? -11.739 7.496   -12.473 1.00 82.38  ? 419 LEU A CA  1 
ATOM   2880 C C   . LEU A 1 419 ? -12.100 6.616   -11.279 1.00 88.65  ? 419 LEU A C   1 
ATOM   2881 O O   . LEU A 1 419 ? -12.022 7.059   -10.135 1.00 92.60  ? 419 LEU A O   1 
ATOM   2882 C CB  . LEU A 1 419 ? -10.381 8.185   -12.239 1.00 75.75  ? 419 LEU A CB  1 
ATOM   2883 N N   . VAL A 1 420 ? -12.506 5.370   -11.560 1.00 84.38  ? 420 VAL A N   1 
ATOM   2884 C CA  . VAL A 1 420 ? -12.839 4.408   -10.520 1.00 86.46  ? 420 VAL A CA  1 
ATOM   2885 C C   . VAL A 1 420 ? -11.566 3.837   -9.899  1.00 80.88  ? 420 VAL A C   1 
ATOM   2886 O O   . VAL A 1 420 ? -10.792 3.163   -10.574 1.00 86.08  ? 420 VAL A O   1 
ATOM   2887 C CB  . VAL A 1 420 ? -13.762 3.266   -11.030 1.00 91.58  ? 420 VAL A CB  1 
ATOM   2888 C CG1 . VAL A 1 420 ? -13.124 2.462   -12.166 1.00 91.77  ? 420 VAL A CG1 1 
ATOM   2889 C CG2 . VAL A 1 420 ? -14.175 2.347   -9.882  1.00 85.09  ? 420 VAL A CG2 1 
ATOM   2890 N N   . PHE A 1 421 ? -11.372 4.112   -8.602  1.00 84.73  ? 421 PHE A N   1 
ATOM   2891 C CA  . PHE A 1 421 ? -10.219 3.631   -7.858  1.00 78.61  ? 421 PHE A CA  1 
ATOM   2892 C C   . PHE A 1 421 ? -10.445 2.224   -7.310  1.00 78.00  ? 421 PHE A C   1 
ATOM   2893 O O   . PHE A 1 421 ? -11.585 1.790   -7.152  1.00 75.24  ? 421 PHE A O   1 
ATOM   2894 C CB  . PHE A 1 421 ? -9.893  4.594   -6.707  1.00 78.45  ? 421 PHE A CB  1 
ATOM   2895 C CG  . PHE A 1 421 ? -9.049  5.781   -7.100  1.00 77.36  ? 421 PHE A CG  1 
ATOM   2896 C CD1 . PHE A 1 421 ? -7.693  5.641   -7.327  1.00 75.33  ? 421 PHE A CD1 1 
ATOM   2897 C CD2 . PHE A 1 421 ? -9.611  7.036   -7.237  1.00 79.34  ? 421 PHE A CD2 1 
ATOM   2898 C CE1 . PHE A 1 421 ? -6.913  6.732   -7.680  1.00 72.80  ? 421 PHE A CE1 1 
ATOM   2899 C CE2 . PHE A 1 421 ? -8.827  8.128   -7.588  1.00 78.88  ? 421 PHE A CE2 1 
ATOM   2900 C CZ  . PHE A 1 421 ? -7.483  7.968   -7.808  1.00 80.31  ? 421 PHE A CZ  1 
ATOM   2901 N N   . SER A 1 422 ? -9.338  1.529   -7.018  1.00 76.00  ? 422 SER A N   1 
ATOM   2902 C CA  . SER A 1 422 ? -9.377  0.172   -6.499  1.00 74.71  ? 422 SER A CA  1 
ATOM   2903 C C   . SER A 1 422 ? -9.708  0.194   -5.011  1.00 74.47  ? 422 SER A C   1 
ATOM   2904 O O   . SER A 1 422 ? -10.760 -0.292  -4.604  1.00 85.71  ? 422 SER A O   1 
ATOM   2905 C CB  . SER A 1 422 ? -8.054  -0.555  -6.751  1.00 73.17  ? 422 SER A CB  1 
ATOM   2906 O OG  . SER A 1 422 ? -7.735  -0.632  -8.132  1.00 64.47  ? 422 SER A OG  1 
ATOM   2907 N N   . SER A 1 423 ? -8.814  0.794   -4.217  1.00 74.25  ? 423 SER A N   1 
ATOM   2908 C CA  . SER A 1 423 ? -8.948  0.815   -2.769  1.00 76.77  ? 423 SER A CA  1 
ATOM   2909 C C   . SER A 1 423 ? -9.165  2.229   -2.241  1.00 78.73  ? 423 SER A C   1 
ATOM   2910 O O   . SER A 1 423 ? -8.780  3.205   -2.882  1.00 80.16  ? 423 SER A O   1 
ATOM   2911 C CB  . SER A 1 423 ? -7.708  0.219   -2.105  1.00 79.82  ? 423 SER A CB  1 
ATOM   2912 O OG  . SER A 1 423 ? -7.452  -1.105  -2.544  1.00 84.82  ? 423 SER A OG  1 
ATOM   2913 N N   . HIS A 1 424 ? -9.799  2.313   -1.067  1.00 78.50  ? 424 HIS A N   1 
ATOM   2914 C CA  . HIS A 1 424 ? -9.843  3.531   -0.274  1.00 76.34  ? 424 HIS A CA  1 
ATOM   2915 C C   . HIS A 1 424 ? -9.757  3.170   1.206   1.00 75.22  ? 424 HIS A C   1 
ATOM   2916 O O   . HIS A 1 424 ? -10.390 2.212   1.650   1.00 84.53  ? 424 HIS A O   1 
ATOM   2917 C CB  . HIS A 1 424 ? -11.127 4.335   -0.534  1.00 68.72  ? 424 HIS A CB  1 
ATOM   2918 C CG  . HIS A 1 424 ? -11.284 5.530   0.360   1.00 73.93  ? 424 HIS A CG  1 
ATOM   2919 N ND1 . HIS A 1 424 ? -12.070 5.482   1.504   1.00 79.87  ? 424 HIS A ND1 1 
ATOM   2920 C CD2 . HIS A 1 424 ? -10.718 6.754   0.277   1.00 74.22  ? 424 HIS A CD2 1 
ATOM   2921 C CE1 . HIS A 1 424 ? -11.977 6.678   2.064   1.00 75.84  ? 424 HIS A CE1 1 
ATOM   2922 N NE2 . HIS A 1 424 ? -11.172 7.479   1.354   1.00 82.31  ? 424 HIS A NE2 1 
ATOM   2923 N N   . SER A 1 425 ? -8.970  3.942   1.964   1.00 67.86  ? 425 SER A N   1 
ATOM   2924 C CA  . SER A 1 425 ? -9.002  3.858   3.414   1.00 75.11  ? 425 SER A CA  1 
ATOM   2925 C C   . SER A 1 425 ? -8.470  5.138   4.052   1.00 78.45  ? 425 SER A C   1 
ATOM   2926 O O   . SER A 1 425 ? -7.598  5.798   3.489   1.00 75.80  ? 425 SER A O   1 
ATOM   2927 C CB  . SER A 1 425 ? -8.209  2.654   3.909   1.00 68.93  ? 425 SER A CB  1 
ATOM   2928 O OG  . SER A 1 425 ? -8.510  2.386   5.269   1.00 70.08  ? 425 SER A OG  1 
ATOM   2929 N N   . ASN A 1 426 ? -9.020  5.470   5.227   1.00 71.53  ? 426 ASN A N   1 
ATOM   2930 C CA  . ASN A 1 426 ? -8.575  6.606   6.015   1.00 65.94  ? 426 ASN A CA  1 
ATOM   2931 C C   . ASN A 1 426 ? -7.598  6.149   7.098   1.00 74.88  ? 426 ASN A C   1 
ATOM   2932 O O   . ASN A 1 426 ? -7.974  5.407   8.005   1.00 80.06  ? 426 ASN A O   1 
ATOM   2933 C CB  . ASN A 1 426 ? -9.781  7.321   6.612   1.00 70.38  ? 426 ASN A CB  1 
ATOM   2934 C CG  . ASN A 1 426 ? -10.700 7.907   5.562   1.00 70.32  ? 426 ASN A CG  1 
ATOM   2935 O OD1 . ASN A 1 426 ? -10.350 8.026   4.383   1.00 70.77  ? 426 ASN A OD1 1 
ATOM   2936 N ND2 . ASN A 1 426 ? -11.895 8.298   5.965   1.00 71.77  ? 426 ASN A ND2 1 
ATOM   2937 N N   . VAL A 1 427 ? -6.340  6.593   6.977   1.00 74.29  ? 427 VAL A N   1 
ATOM   2938 C CA  . VAL A 1 427 ? -5.263  6.194   7.869   1.00 69.36  ? 427 VAL A CA  1 
ATOM   2939 C C   . VAL A 1 427 ? -5.187  7.129   9.075   1.00 79.29  ? 427 VAL A C   1 
ATOM   2940 O O   . VAL A 1 427 ? -4.527  8.165   9.017   1.00 83.45  ? 427 VAL A O   1 
ATOM   2941 C CB  . VAL A 1 427 ? -3.915  6.171   7.100   1.00 76.11  ? 427 VAL A CB  1 
ATOM   2942 C CG1 . VAL A 1 427 ? -2.736  5.886   8.031   1.00 72.33  ? 427 VAL A CG1 1 
ATOM   2943 C CG2 . VAL A 1 427 ? -3.954  5.179   5.944   1.00 72.84  ? 427 VAL A CG2 1 
ATOM   2944 N N   . TYR A 1 428 ? -5.869  6.749   10.153  1.00 76.12  ? 428 TYR A N   1 
ATOM   2945 C CA  . TYR A 1 428 ? -5.913  7.600   11.369  1.00 76.44  ? 428 TYR A CA  1 
ATOM   2946 C C   . TYR A 1 428 ? -4.553  7.572   12.042  1.00 79.16  ? 428 TYR A C   1 
ATOM   2947 O O   . TYR A 1 428 ? -4.157  6.530   12.591  1.00 78.79  ? 428 TYR A O   1 
ATOM   2948 C CB  . TYR A 1 428 ? -7.092  7.094   12.200  1.00 68.25  ? 428 TYR A CB  1 
ATOM   2949 C CG  . TYR A 1 428 ? -8.428  7.582   11.663  1.00 73.76  ? 428 TYR A CG  1 
ATOM   2950 C CD1 . TYR A 1 428 ? -8.921  8.832   12.009  1.00 79.65  ? 428 TYR A CD1 1 
ATOM   2951 C CD2 . TYR A 1 428 ? -9.182  6.804   10.796  1.00 78.01  ? 428 TYR A CD2 1 
ATOM   2952 C CE1 . TYR A 1 428 ? -10.132 9.288   11.520  1.00 80.46  ? 428 TYR A CE1 1 
ATOM   2953 C CE2 . TYR A 1 428 ? -10.394 7.249   10.299  1.00 78.10  ? 428 TYR A CE2 1 
ATOM   2954 C CZ  . TYR A 1 428 ? -10.870 8.495   10.662  1.00 79.88  ? 428 TYR A CZ  1 
ATOM   2955 O OH  . TYR A 1 428 ? -12.064 8.946   10.181  1.00 88.04  ? 428 TYR A OH  1 
ATOM   2956 N N   . ILE A 1 429 ? -3.856  8.707   12.005  1.00 74.59  ? 429 ILE A N   1 
ATOM   2957 C CA  . ILE A 1 429 ? -2.482  8.767   12.574  1.00 83.94  ? 429 ILE A CA  1 
ATOM   2958 C C   . ILE A 1 429 ? -2.514  9.509   13.915  1.00 89.13  ? 429 ILE A C   1 
ATOM   2959 O O   . ILE A 1 429 ? -3.124  10.592  13.978  1.00 95.83  ? 429 ILE A O   1 
ATOM   2960 C CB  . ILE A 1 429 ? -1.524  9.449   11.582  1.00 88.73  ? 429 ILE A CB  1 
ATOM   2961 N N   . THR A 1 430 ? -1.883  8.938   14.938  1.00 76.61  ? 430 THR A N   1 
ATOM   2962 C CA  . THR A 1 430 ? -1.802  9.605   16.248  1.00 81.37  ? 430 THR A CA  1 
ATOM   2963 C C   . THR A 1 430 ? -0.345  9.790   16.571  1.00 82.27  ? 430 THR A C   1 
ATOM   2964 O O   . THR A 1 430 ? 0.465   8.947   16.161  1.00 74.81  ? 430 THR A O   1 
ATOM   2965 C CB  . THR A 1 430 ? -2.503  8.781   17.326  1.00 73.08  ? 430 THR A CB  1 
ATOM   2966 O OG1 . THR A 1 430 ? -1.692  7.623   17.491  1.00 79.00  ? 430 THR A OG1 1 
ATOM   2967 C CG2 . THR A 1 430 ? -3.916  8.388   16.936  1.00 79.40  ? 430 THR A CG2 1 
ATOM   2968 N N   . ALA A 1 431 ? -0.022  10.848  17.302  1.00 81.19  ? 431 ALA A N   1 
ATOM   2969 C CA  . ALA A 1 431 ? 1.374   11.088  17.715  1.00 81.14  ? 431 ALA A CA  1 
ATOM   2970 C C   . ALA A 1 431 ? 1.793   10.072  18.769  1.00 76.11  ? 431 ALA A C   1 
ATOM   2971 O O   . ALA A 1 431 ? 0.955   9.640   19.578  1.00 68.67  ? 431 ALA A O   1 
ATOM   2972 C CB  . ALA A 1 431 ? 1.501   12.479  18.260  1.00 77.61  ? 431 ALA A CB  1 
ATOM   2973 N N   . ASP A 1 432 ? 3.066   9.701   18.751  1.00 80.90  ? 432 ASP A N   1 
ATOM   2974 C CA  . ASP A 1 432 ? 3.585   8.801   19.804  1.00 79.95  ? 432 ASP A CA  1 
ATOM   2975 C C   . ASP A 1 432 ? 4.115   9.692   20.919  1.00 82.95  ? 432 ASP A C   1 
ATOM   2976 O O   . ASP A 1 432 ? 3.279   10.403  21.513  1.00 80.96  ? 432 ASP A O   1 
ATOM   2977 C CB  . ASP A 1 432 ? 4.677   7.894   19.275  1.00 88.89  ? 432 ASP A CB  1 
ATOM   2978 N N   . LYS A 1 433 ? 5.432   9.685   21.136  1.00 91.80  ? 433 LYS A N   1 
ATOM   2979 C CA  . LYS A 1 433 ? 6.085   10.512  22.185  1.00 89.77  ? 433 LYS A CA  1 
ATOM   2980 C C   . LYS A 1 433 ? 7.310   9.748   22.675  1.00 90.48  ? 433 LYS A C   1 
ATOM   2981 O O   . LYS A 1 433 ? 8.441   10.228  22.472  1.00 93.79  ? 433 LYS A O   1 
ATOM   2982 C CB  . LYS A 1 433 ? 5.301   10.703  23.483  1.00 106.98 ? 433 LYS A CB  1 
ATOM   2983 N N   . GLN A 1 434 ? 7.073   8.594   23.293  1.00 84.84  ? 434 GLN A N   1 
ATOM   2984 C CA  . GLN A 1 434 ? 8.181   7.762   23.806  1.00 90.27  ? 434 GLN A CA  1 
ATOM   2985 C C   . GLN A 1 434 ? 9.267   7.620   22.743  1.00 88.41  ? 434 GLN A C   1 
ATOM   2986 O O   . GLN A 1 434 ? 10.447  7.751   23.103  1.00 86.89  ? 434 GLN A O   1 
ATOM   2987 C CB  . GLN A 1 434 ? 7.604   6.389   24.127  1.00 87.99  ? 434 GLN A CB  1 
ATOM   2988 N N   . LYS A 1 435 ? 8.880   7.363   21.492  1.00 92.44  ? 435 LYS A N   1 
ATOM   2989 C CA  . LYS A 1 435 ? 9.885   7.098   20.431  1.00 88.08  ? 435 LYS A CA  1 
ATOM   2990 C C   . LYS A 1 435 ? 10.014  8.303   19.496  1.00 87.89  ? 435 LYS A C   1 
ATOM   2991 O O   . LYS A 1 435 ? 10.430  8.094   18.345  1.00 97.26  ? 435 LYS A O   1 
ATOM   2992 C CB  . LYS A 1 435 ? 9.455   5.848   19.662  1.00 83.43  ? 435 LYS A CB  1 
ATOM   2993 C CG  . LYS A 1 435 ? 9.215   4.615   20.516  1.00 88.00  ? 435 LYS A CG  1 
ATOM   2994 C CD  . LYS A 1 435 ? 7.908   3.902   20.196  1.00 81.72  ? 435 LYS A CD  1 
ATOM   2995 C CE  . LYS A 1 435 ? 6.814   4.853   19.839  1.00 86.61  ? 435 LYS A CE  1 
ATOM   2996 N NZ  . LYS A 1 435 ? 6.167   5.388   21.038  1.00 90.65  ? 435 LYS A NZ  1 
ATOM   2997 N N   . ASN A 1 436 ? 9.684   9.505   19.974  1.00 93.45  ? 436 ASN A N   1 
ATOM   2998 C CA  . ASN A 1 436 ? 9.723   10.728  19.124  1.00 89.85  ? 436 ASN A CA  1 
ATOM   2999 C C   . ASN A 1 436 ? 9.224   10.366  17.726  1.00 90.74  ? 436 ASN A C   1 
ATOM   3000 O O   . ASN A 1 436 ? 9.873   10.746  16.740  1.00 88.90  ? 436 ASN A O   1 
ATOM   3001 C CB  . ASN A 1 436 ? 11.106  11.365  19.088  1.00 86.90  ? 436 ASN A CB  1 
ATOM   3002 C CG  . ASN A 1 436 ? 11.035  12.836  18.764  1.00 88.92  ? 436 ASN A CG  1 
ATOM   3003 O OD1 . ASN A 1 436 ? 9.982   13.460  18.939  1.00 84.08  ? 436 ASN A OD1 1 
ATOM   3004 N ND2 . ASN A 1 436 ? 12.133  13.402  18.286  1.00 81.89  ? 436 ASN A ND2 1 
ATOM   3005 N N   . GLY A 1 437 ? 8.094   9.670   17.655  1.00 92.55  ? 437 GLY A N   1 
ATOM   3006 C CA  . GLY A 1 437 ? 7.609   9.221   16.347  1.00 80.87  ? 437 GLY A CA  1 
ATOM   3007 C C   . GLY A 1 437 ? 6.112   9.338   16.243  1.00 81.11  ? 437 GLY A C   1 
ATOM   3008 O O   . GLY A 1 437 ? 5.520   10.125  17.002  1.00 84.98  ? 437 GLY A O   1 
ATOM   3009 N N   . ILE A 1 438 ? 5.524   8.579   15.325  1.00 76.43  ? 438 ILE A N   1 
ATOM   3010 C CA  . ILE A 1 438 ? 4.057   8.650   15.111  1.00 72.45  ? 438 ILE A CA  1 
ATOM   3011 C C   . ILE A 1 438 ? 3.545   7.215   14.980  1.00 75.75  ? 438 ILE A C   1 
ATOM   3012 O O   . ILE A 1 438 ? 4.366   6.307   14.742  1.00 78.54  ? 438 ILE A O   1 
ATOM   3013 C CB  . ILE A 1 438 ? 3.744   9.502   13.871  1.00 84.98  ? 438 ILE A CB  1 
ATOM   3014 C CG1 . ILE A 1 438 ? 2.353   10.125  13.942  1.00 89.18  ? 438 ILE A CG1 1 
ATOM   3015 C CG2 . ILE A 1 438 ? 3.935   8.706   12.580  1.00 82.54  ? 438 ILE A CG2 1 
ATOM   3016 N N   . LYS A 1 439 ? 2.245   7.029   15.165  1.00 71.63  ? 439 LYS A N   1 
ATOM   3017 C CA  . LYS A 1 439 ? 1.657   5.676   15.088  1.00 71.44  ? 439 LYS A CA  1 
ATOM   3018 C C   . LYS A 1 439 ? 0.315   5.763   14.366  1.00 72.15  ? 439 LYS A C   1 
ATOM   3019 O O   . LYS A 1 439 ? -0.323  6.825   14.417  1.00 80.14  ? 439 LYS A O   1 
ATOM   3020 C CB  . LYS A 1 439 ? 1.432   5.118   16.494  1.00 80.56  ? 439 LYS A CB  1 
ATOM   3021 N N   . ALA A 1 440 ? -0.096  4.670   13.739  1.00 64.43  ? 440 ALA A N   1 
ATOM   3022 C CA  . ALA A 1 440 ? -1.340  4.739   12.957  1.00 65.27  ? 440 ALA A CA  1 
ATOM   3023 C C   . ALA A 1 440 ? -1.993  3.368   12.874  1.00 61.43  ? 440 ALA A C   1 
ATOM   3024 O O   . ALA A 1 440 ? -1.293  2.350   12.964  1.00 62.98  ? 440 ALA A O   1 
ATOM   3025 C CB  . ALA A 1 440 ? -1.032  5.290   11.589  1.00 71.38  ? 440 ALA A CB  1 
ATOM   3026 N N   . ASN A 1 441 ? -3.309  3.361   12.726  1.00 70.64  ? 441 ASN A N   1 
ATOM   3027 C CA  . ASN A 1 441 ? -4.052  2.124   12.561  1.00 63.22  ? 441 ASN A CA  1 
ATOM   3028 C C   . ASN A 1 441 ? -5.137  2.331   11.507  1.00 70.44  ? 441 ASN A C   1 
ATOM   3029 O O   . ASN A 1 441 ? -5.826  3.348   11.520  1.00 69.67  ? 441 ASN A O   1 
ATOM   3030 C CB  . ASN A 1 441 ? -4.663  1.681   13.885  1.00 61.30  ? 441 ASN A CB  1 
ATOM   3031 N N   . PHE A 1 442 ? -5.268  1.367   10.589  1.00 63.46  ? 442 PHE A N   1 
ATOM   3032 C CA  . PHE A 1 442 ? -6.303  1.414   9.570   1.00 57.01  ? 442 PHE A CA  1 
ATOM   3033 C C   . PHE A 1 442 ? -6.590  0.024   9.005   1.00 59.18  ? 442 PHE A C   1 
ATOM   3034 O O   . PHE A 1 442 ? -5.758  -0.876  9.098   1.00 60.83  ? 442 PHE A O   1 
ATOM   3035 C CB  . PHE A 1 442 ? -5.909  2.373   8.437   1.00 62.81  ? 442 PHE A CB  1 
ATOM   3036 C CG  . PHE A 1 442 ? -4.694  1.955   7.642   1.00 58.88  ? 442 PHE A CG  1 
ATOM   3037 C CD1 . PHE A 1 442 ? -3.416  2.194   8.119   1.00 55.67  ? 442 PHE A CD1 1 
ATOM   3038 C CD2 . PHE A 1 442 ? -4.832  1.309   6.426   1.00 53.93  ? 442 PHE A CD2 1 
ATOM   3039 C CE1 . PHE A 1 442 ? -2.303  1.799   7.391   1.00 51.86  ? 442 PHE A CE1 1 
ATOM   3040 C CE2 . PHE A 1 442 ? -3.722  0.914   5.705   1.00 51.42  ? 442 PHE A CE2 1 
ATOM   3041 C CZ  . PHE A 1 442 ? -2.462  1.164   6.187   1.00 57.83  ? 442 PHE A CZ  1 
ATOM   3042 N N   . LYS A 1 443 ? -7.782  -0.131  8.418   1.00 59.83  ? 443 LYS A N   1 
ATOM   3043 C CA  . LYS A 1 443 ? -8.206  -1.395  7.838   1.00 52.28  ? 443 LYS A CA  1 
ATOM   3044 C C   . LYS A 1 443 ? -8.302  -1.275  6.320   1.00 64.54  ? 443 LYS A C   1 
ATOM   3045 O O   . LYS A 1 443 ? -8.713  -0.240  5.799   1.00 72.38  ? 443 LYS A O   1 
ATOM   3046 C CB  . LYS A 1 443 ? -9.556  -1.833  8.425   1.00 60.78  ? 443 LYS A CB  1 
ATOM   3047 N N   . ILE A 1 444 ? -7.897  -2.346  5.630   1.00 63.97  ? 444 ILE A N   1 
ATOM   3048 C CA  . ILE A 1 444 ? -8.035  -2.467  4.189   1.00 62.69  ? 444 ILE A CA  1 
ATOM   3049 C C   . ILE A 1 444 ? -8.859  -3.718  3.893   1.00 69.47  ? 444 ILE A C   1 
ATOM   3050 O O   . ILE A 1 444 ? -8.640  -4.762  4.502   1.00 60.55  ? 444 ILE A O   1 
ATOM   3051 C CB  . ILE A 1 444 ? -6.640  -2.500  3.512   1.00 63.13  ? 444 ILE A CB  1 
ATOM   3052 C CG1 . ILE A 1 444 ? -6.050  -1.085  3.367   1.00 70.64  ? 444 ILE A CG1 1 
ATOM   3053 C CG2 . ILE A 1 444 ? -6.678  -3.215  2.159   1.00 60.33  ? 444 ILE A CG2 1 
ATOM   3054 C CD1 . ILE A 1 444 ? -6.722  -0.209  2.283   1.00 73.12  ? 444 ILE A CD1 1 
ATOM   3055 N N   . ARG A 1 445 ? -9.806  -3.590  2.954   1.00 69.78  ? 445 ARG A N   1 
ATOM   3056 C CA  . ARG A 1 445 ? -10.661 -4.693  2.547   1.00 68.85  ? 445 ARG A CA  1 
ATOM   3057 C C   . ARG A 1 445 ? -10.288 -5.126  1.132   1.00 72.60  ? 445 ARG A C   1 
ATOM   3058 O O   . ARG A 1 445 ? -10.431 -4.349  0.188   1.00 71.15  ? 445 ARG A O   1 
ATOM   3059 C CB  . ARG A 1 445 ? -12.147 -4.284  2.609   1.00 71.57  ? 445 ARG A CB  1 
ATOM   3060 C CG  . ARG A 1 445 ? -12.635 -3.970  4.017   1.00 75.79  ? 445 ARG A CG  1 
ATOM   3061 C CD  . ARG A 1 445 ? -14.058 -3.426  4.056   1.00 74.68  ? 445 ARG A CD  1 
ATOM   3062 N NE  . ARG A 1 445 ? -15.058 -4.485  4.160   1.00 85.27  ? 445 ARG A NE  1 
ATOM   3063 C CZ  . ARG A 1 445 ? -16.145 -4.587  3.402   1.00 80.19  ? 445 ARG A CZ  1 
ATOM   3064 N NH1 . ARG A 1 445 ? -16.386 -3.738  2.415   1.00 77.66  ? 445 ARG A NH1 1 
ATOM   3065 N NH2 . ARG A 1 445 ? -17.012 -5.567  3.640   1.00 74.70  ? 445 ARG A NH2 1 
ATOM   3066 N N   . HIS A 1 446 ? -9.804  -6.369  1.005   1.00 59.97  ? 446 HIS A N   1 
ATOM   3067 C CA  . HIS A 1 446 ? -9.456  -6.940  -0.285  1.00 56.14  ? 446 HIS A CA  1 
ATOM   3068 C C   . HIS A 1 446 ? -10.590 -7.812  -0.821  1.00 59.45  ? 446 HIS A C   1 
ATOM   3069 O O   . HIS A 1 446 ? -11.059 -8.709  -0.126  1.00 65.70  ? 446 HIS A O   1 
ATOM   3070 C CB  . HIS A 1 446 ? -8.177  -7.767  -0.178  1.00 45.62  ? 446 HIS A CB  1 
ATOM   3071 C CG  . HIS A 1 446 ? -6.935  -6.980  0.116   1.00 54.15  ? 446 HIS A CG  1 
ATOM   3072 N ND1 . HIS A 1 446 ? -6.110  -7.301  1.181   1.00 61.90  ? 446 HIS A ND1 1 
ATOM   3073 C CD2 . HIS A 1 446 ? -6.394  -5.935  -0.549  1.00 56.35  ? 446 HIS A CD2 1 
ATOM   3074 C CE1 . HIS A 1 446 ? -5.105  -6.436  1.141   1.00 54.45  ? 446 HIS A CE1 1 
ATOM   3075 N NE2 . HIS A 1 446 ? -5.239  -5.592  0.112   1.00 54.59  ? 446 HIS A NE2 1 
ATOM   3076 N N   . ASN A 1 447 ? -11.019 -7.544  -2.062  1.00 62.90  ? 447 ASN A N   1 
ATOM   3077 C CA  . ASN A 1 447 ? -12.060 -8.330  -2.707  1.00 66.54  ? 447 ASN A CA  1 
ATOM   3078 C C   . ASN A 1 447 ? -11.526 -9.688  -3.159  1.00 63.35  ? 447 ASN A C   1 
ATOM   3079 O O   . ASN A 1 447 ? -10.425 -9.771  -3.700  1.00 61.10  ? 447 ASN A O   1 
ATOM   3080 C CB  . ASN A 1 447 ? -12.656 -7.579  -3.912  1.00 73.21  ? 447 ASN A CB  1 
ATOM   3081 C CG  . ASN A 1 447 ? -13.591 -6.445  -3.542  1.00 73.07  ? 447 ASN A CG  1 
ATOM   3082 O OD1 . ASN A 1 447 ? -14.594 -6.634  -2.856  1.00 74.27  ? 447 ASN A OD1 1 
ATOM   3083 N ND2 . ASN A 1 447 ? -13.288 -5.241  -3.991  1.00 64.38  ? 447 ASN A ND2 1 
ATOM   3084 N N   . ILE A 1 448 ? -12.327 -10.739 -2.938  1.00 59.39  ? 448 ILE A N   1 
ATOM   3085 C CA  . ILE A 1 448 ? -12.003 -12.089 -3.371  1.00 61.57  ? 448 ILE A CA  1 
ATOM   3086 C C   . ILE A 1 448 ? -12.628 -12.366 -4.737  1.00 70.90  ? 448 ILE A C   1 
ATOM   3087 O O   . ILE A 1 448 ? -13.762 -11.963 -4.993  1.00 77.10  ? 448 ILE A O   1 
ATOM   3088 C CB  . ILE A 1 448 ? -12.469 -13.130 -2.313  1.00 68.25  ? 448 ILE A CB  1 
ATOM   3089 C CG1 . ILE A 1 448 ? -11.892 -12.824 -0.909  1.00 61.31  ? 448 ILE A CG1 1 
ATOM   3090 C CG2 . ILE A 1 448 ? -12.124 -14.568 -2.734  1.00 62.88  ? 448 ILE A CG2 1 
ATOM   3091 C CD1 . ILE A 1 448 ? -12.457 -13.716 0.208   1.00 46.93  ? 448 ILE A CD1 1 
ATOM   3092 N N   . GLU A 1 449 ? -11.871 -13.053 -5.606  1.00 74.92  ? 449 GLU A N   1 
ATOM   3093 C CA  . GLU A 1 449 ? -12.360 -13.501 -6.902  1.00 73.10  ? 449 GLU A CA  1 
ATOM   3094 C C   . GLU A 1 449 ? -13.580 -14.401 -6.728  1.00 79.54  ? 449 GLU A C   1 
ATOM   3095 O O   . GLU A 1 449 ? -13.521 -15.378 -5.984  1.00 76.69  ? 449 GLU A O   1 
ATOM   3096 C CB  . GLU A 1 449 ? -11.266 -14.271 -7.666  1.00 75.59  ? 449 GLU A CB  1 
ATOM   3097 C CG  . GLU A 1 449 ? -10.339 -13.396 -8.491  1.00 71.75  ? 449 GLU A CG  1 
ATOM   3098 C CD  . GLU A 1 449 ? -10.848 -13.089 -9.884  1.00 80.32  ? 449 GLU A CD  1 
ATOM   3099 O OE1 . GLU A 1 449 ? -11.066 -14.050 -10.657 1.00 81.32  ? 449 GLU A OE1 1 
ATOM   3100 O OE2 . GLU A 1 449 ? -11.026 -11.892 -10.207 1.00 79.12  ? 449 GLU A OE2 1 
ATOM   3101 N N   . ASP A 1 450 ? -14.675 -14.052 -7.418  1.00 74.05  ? 450 ASP A N   1 
ATOM   3102 C CA  . ASP A 1 450 ? -15.911 -14.817 -7.363  1.00 64.49  ? 450 ASP A CA  1 
ATOM   3103 C C   . ASP A 1 450 ? -16.274 -15.155 -5.919  1.00 74.35  ? 450 ASP A C   1 
ATOM   3104 O O   . ASP A 1 450 ? -16.354 -16.327 -5.555  1.00 82.49  ? 450 ASP A O   1 
ATOM   3105 C CB  . ASP A 1 450 ? -15.782 -16.098 -8.212  1.00 60.27  ? 450 ASP A CB  1 
ATOM   3106 N N   . GLY A 1 451 ? -16.475 -14.116 -5.098  1.00 74.42  ? 451 GLY A N   1 
ATOM   3107 C CA  . GLY A 1 451 ? -16.665 -14.299 -3.667  1.00 65.09  ? 451 GLY A CA  1 
ATOM   3108 C C   . GLY A 1 451 ? -16.801 -12.997 -2.879  1.00 64.81  ? 451 GLY A C   1 
ATOM   3109 O O   . GLY A 1 451 ? -17.327 -12.012 -3.391  1.00 65.75  ? 451 GLY A O   1 
ATOM   3110 N N   . GLY A 1 452 ? -16.310 -13.014 -1.633  1.00 60.37  ? 452 GLY A N   1 
ATOM   3111 C CA  . GLY A 1 452 ? -16.502 -11.922 -0.691  1.00 62.15  ? 452 GLY A CA  1 
ATOM   3112 C C   . GLY A 1 452 ? -15.228 -11.123 -0.424  1.00 61.89  ? 452 GLY A C   1 
ATOM   3113 O O   . GLY A 1 452 ? -14.513 -10.778 -1.359  1.00 63.65  ? 452 GLY A O   1 
ATOM   3114 N N   . VAL A 1 453 ? -14.954 -10.848 0.859   1.00 63.35  ? 453 VAL A N   1 
ATOM   3115 C CA  . VAL A 1 453 ? -13.921 -9.902  1.252   1.00 63.98  ? 453 VAL A CA  1 
ATOM   3116 C C   . VAL A 1 453 ? -12.943 -10.488 2.270   1.00 56.89  ? 453 VAL A C   1 
ATOM   3117 O O   . VAL A 1 453 ? -13.345 -11.240 3.154   1.00 54.71  ? 453 VAL A O   1 
ATOM   3118 C CB  . VAL A 1 453 ? -14.581 -8.620  1.802   1.00 62.68  ? 453 VAL A CB  1 
ATOM   3119 C CG1 . VAL A 1 453 ? -13.537 -7.606  2.256   1.00 63.08  ? 453 VAL A CG1 1 
ATOM   3120 C CG2 . VAL A 1 453 ? -15.524 -8.003  0.775   1.00 66.45  ? 453 VAL A CG2 1 
ATOM   3121 N N   . GLN A 1 454 ? -11.662 -10.113 2.121   1.00 64.85  ? 454 GLN A N   1 
ATOM   3122 C CA  . GLN A 1 454 ? -10.576 -10.497 3.014   1.00 55.20  ? 454 GLN A CA  1 
ATOM   3123 C C   . GLN A 1 454 ? -10.003 -9.246  3.675   1.00 58.11  ? 454 GLN A C   1 
ATOM   3124 O O   . GLN A 1 454 ? -9.329  -8.456  3.017   1.00 66.91  ? 454 GLN A O   1 
ATOM   3125 C CB  . GLN A 1 454 ? -9.461  -11.218 2.230   1.00 59.91  ? 454 GLN A CB  1 
ATOM   3126 C CG  . GLN A 1 454 ? -8.098  -11.330 2.956   1.00 57.20  ? 454 GLN A CG  1 
ATOM   3127 C CD  . GLN A 1 454 ? -8.039  -12.468 3.942   1.00 59.75  ? 454 GLN A CD  1 
ATOM   3128 O OE1 . GLN A 1 454 ? -7.966  -13.638 3.557   1.00 60.54  ? 454 GLN A OE1 1 
ATOM   3129 N NE2 . GLN A 1 454 ? -8.034  -12.161 5.235   1.00 54.07  ? 454 GLN A NE2 1 
ATOM   3130 N N   . LEU A 1 455 ? -10.249 -9.093  4.982   1.00 58.08  ? 455 LEU A N   1 
ATOM   3131 C CA  . LEU A 1 455 ? -9.832  -7.907  5.712   1.00 54.69  ? 455 LEU A CA  1 
ATOM   3132 C C   . LEU A 1 455 ? -8.375  -8.032  6.157   1.00 60.81  ? 455 LEU A C   1 
ATOM   3133 O O   . LEU A 1 455 ? -7.932  -9.101  6.579   1.00 50.84  ? 455 LEU A O   1 
ATOM   3134 C CB  . LEU A 1 455 ? -10.764 -7.689  6.916   1.00 63.30  ? 455 LEU A CB  1 
ATOM   3135 C CG  . LEU A 1 455 ? -10.975 -6.234  7.338   1.00 68.29  ? 455 LEU A CG  1 
ATOM   3136 C CD1 . LEU A 1 455 ? -12.141 -6.116  8.302   1.00 83.32  ? 455 LEU A CD1 1 
ATOM   3137 C CD2 . LEU A 1 455 ? -9.712  -5.633  7.961   1.00 63.57  ? 455 LEU A CD2 1 
ATOM   3138 N N   . ALA A 1 456 ? -7.635  -6.926  6.022   1.00 59.66  ? 456 ALA A N   1 
ATOM   3139 C CA  . ALA A 1 456 ? -6.261  -6.825  6.484   1.00 55.12  ? 456 ALA A CA  1 
ATOM   3140 C C   . ALA A 1 456 ? -6.148  -5.694  7.502   1.00 60.32  ? 456 ALA A C   1 
ATOM   3141 O O   . ALA A 1 456 ? -6.228  -4.521  7.137   1.00 52.37  ? 456 ALA A O   1 
ATOM   3142 C CB  . ALA A 1 456 ? -5.327  -6.570  5.314   1.00 50.22  ? 456 ALA A CB  1 
ATOM   3143 N N   . ASP A 1 457 ? -5.974  -6.056  8.780   1.00 59.52  ? 457 ASP A N   1 
ATOM   3144 C CA  . ASP A 1 457 ? -5.805  -5.063  9.828   1.00 58.57  ? 457 ASP A CA  1 
ATOM   3145 C C   . ASP A 1 457 ? -4.361  -4.564  9.824   1.00 56.88  ? 457 ASP A C   1 
ATOM   3146 O O   . ASP A 1 457 ? -3.436  -5.347  10.012  1.00 61.80  ? 457 ASP A O   1 
ATOM   3147 C CB  . ASP A 1 457 ? -6.199  -5.630  11.198  1.00 52.90  ? 457 ASP A CB  1 
ATOM   3148 C CG  . ASP A 1 457 ? -7.684  -5.886  11.345  1.00 69.04  ? 457 ASP A CG  1 
ATOM   3149 O OD1 . ASP A 1 457 ? -8.478  -4.981  10.996  1.00 74.25  ? 457 ASP A OD1 1 
ATOM   3150 O OD2 . ASP A 1 457 ? -8.057  -6.982  11.829  1.00 66.46  ? 457 ASP A OD2 1 
ATOM   3151 N N   . HIS A 1 458 ? -4.186  -3.257  9.597   1.00 55.10  ? 458 HIS A N   1 
ATOM   3152 C CA  . HIS A 1 458 ? -2.868  -2.646  9.565   1.00 58.14  ? 458 HIS A CA  1 
ATOM   3153 C C   . HIS A 1 458 ? -2.561  -1.974  10.898  1.00 52.01  ? 458 HIS A C   1 
ATOM   3154 O O   . HIS A 1 458 ? -3.424  -1.325  11.486  1.00 52.67  ? 458 HIS A O   1 
ATOM   3155 C CB  . HIS A 1 458 ? -2.738  -1.616  8.424   1.00 47.12  ? 458 HIS A CB  1 
ATOM   3156 C CG  . HIS A 1 458 ? -2.710  -2.214  7.049   1.00 49.72  ? 458 HIS A CG  1 
ATOM   3157 N ND1 . HIS A 1 458 ? -3.725  -3.029  6.596   1.00 50.73  ? 458 HIS A ND1 1 
ATOM   3158 C CD2 . HIS A 1 458 ? -1.785  -2.089  6.070   1.00 48.75  ? 458 HIS A CD2 1 
ATOM   3159 C CE1 . HIS A 1 458 ? -3.389  -3.382  5.361   1.00 58.52  ? 458 HIS A CE1 1 
ATOM   3160 N NE2 . HIS A 1 458 ? -2.224  -2.834  5.006   1.00 49.01  ? 458 HIS A NE2 1 
ATOM   3161 N N   . TYR A 1 459 ? -1.313  -2.150  11.347  1.00 49.58  ? 459 TYR A N   1 
ATOM   3162 C CA  . TYR A 1 459 ? -0.799  -1.516  12.546  1.00 51.54  ? 459 TYR A CA  1 
ATOM   3163 C C   . TYR A 1 459 ? 0.589   -0.981  12.205  1.00 53.14  ? 459 TYR A C   1 
ATOM   3164 O O   . TYR A 1 459 ? 1.450   -1.731  11.750  1.00 56.43  ? 459 TYR A O   1 
ATOM   3165 C CB  . TYR A 1 459 ? -0.779  -2.516  13.708  1.00 49.85  ? 459 TYR A CB  1 
ATOM   3166 C CG  . TYR A 1 459 ? -2.167  -2.975  14.097  1.00 51.62  ? 459 TYR A CG  1 
ATOM   3167 C CD1 . TYR A 1 459 ? -2.956  -2.221  14.954  1.00 48.85  ? 459 TYR A CD1 1 
ATOM   3168 C CD2 . TYR A 1 459 ? -2.713  -4.134  13.563  1.00 51.39  ? 459 TYR A CD2 1 
ATOM   3169 C CE1 . TYR A 1 459 ? -4.240  -2.629  15.299  1.00 47.44  ? 459 TYR A CE1 1 
ATOM   3170 C CE2 . TYR A 1 459 ? -3.995  -4.551  13.900  1.00 46.26  ? 459 TYR A CE2 1 
ATOM   3171 C CZ  . TYR A 1 459 ? -4.756  -3.796  14.768  1.00 46.13  ? 459 TYR A CZ  1 
ATOM   3172 O OH  . TYR A 1 459 ? -6.025  -4.210  15.088  1.00 50.45  ? 459 TYR A OH  1 
ATOM   3173 N N   . GLN A 1 460 ? 0.782   0.323   12.426  1.00 54.06  ? 460 GLN A N   1 
ATOM   3174 C CA  . GLN A 1 460 ? 1.905   1.054   11.867  1.00 57.78  ? 460 GLN A CA  1 
ATOM   3175 C C   . GLN A 1 460 ? 2.648   1.828   12.951  1.00 52.12  ? 460 GLN A C   1 
ATOM   3176 O O   . GLN A 1 460 ? 2.031   2.484   13.787  1.00 58.25  ? 460 GLN A O   1 
ATOM   3177 C CB  . GLN A 1 460 ? 1.379   2.013   10.784  1.00 57.33  ? 460 GLN A CB  1 
ATOM   3178 C CG  . GLN A 1 460 ? 2.449   2.695   9.943   1.00 53.04  ? 460 GLN A CG  1 
ATOM   3179 C CD  . GLN A 1 460 ? 1.831   3.669   8.959   1.00 64.45  ? 460 GLN A CD  1 
ATOM   3180 O OE1 . GLN A 1 460 ? 0.931   3.327   8.181   1.00 58.49  ? 460 GLN A OE1 1 
ATOM   3181 N NE2 . GLN A 1 460 ? 2.281   4.914   8.981   1.00 59.16  ? 460 GLN A NE2 1 
ATOM   3182 N N   . GLN A 1 461 ? 3.980   1.734   12.918  1.00 57.03  ? 461 GLN A N   1 
ATOM   3183 C CA  . GLN A 1 461 ? 4.851   2.509   13.785  1.00 64.87  ? 461 GLN A CA  1 
ATOM   3184 C C   . GLN A 1 461 ? 5.889   3.230   12.928  1.00 60.22  ? 461 GLN A C   1 
ATOM   3185 O O   . GLN A 1 461 ? 6.545   2.605   12.099  1.00 60.36  ? 461 GLN A O   1 
ATOM   3186 C CB  . GLN A 1 461 ? 5.514   1.580   14.804  1.00 53.81  ? 461 GLN A CB  1 
ATOM   3187 C CG  . GLN A 1 461 ? 6.654   2.206   15.584  1.00 60.34  ? 461 GLN A CG  1 
ATOM   3188 C CD  . GLN A 1 461 ? 7.208   1.224   16.578  1.00 72.05  ? 461 GLN A CD  1 
ATOM   3189 O OE1 . GLN A 1 461 ? 6.570   0.912   17.584  1.00 75.52  ? 461 GLN A OE1 1 
ATOM   3190 N NE2 . GLN A 1 461 ? 8.408   0.713   16.320  1.00 69.17  ? 461 GLN A NE2 1 
ATOM   3191 N N   . ASN A 1 462 ? 6.023   4.546   13.131  1.00 62.68  ? 462 ASN A N   1 
ATOM   3192 C CA  . ASN A 1 462 ? 7.008   5.347   12.419  1.00 73.09  ? 462 ASN A CA  1 
ATOM   3193 C C   . ASN A 1 462 ? 7.882   6.138   13.387  1.00 71.54  ? 462 ASN A C   1 
ATOM   3194 O O   . ASN A 1 462 ? 7.385   7.007   14.098  1.00 73.74  ? 462 ASN A O   1 
ATOM   3195 C CB  . ASN A 1 462 ? 6.341   6.308   11.437  1.00 65.65  ? 462 ASN A CB  1 
ATOM   3196 C CG  . ASN A 1 462 ? 5.693   5.603   10.286  1.00 64.92  ? 462 ASN A CG  1 
ATOM   3197 O OD1 . ASN A 1 462 ? 4.605   5.047   10.401  1.00 69.00  ? 462 ASN A OD1 1 
ATOM   3198 N ND2 . ASN A 1 462 ? 6.346   5.615   9.143   1.00 73.22  ? 462 ASN A ND2 1 
ATOM   3199 N N   . THR A 1 463 ? 9.184   5.826   13.398  1.00 69.61  ? 463 THR A N   1 
ATOM   3200 C CA  . THR A 1 463 ? 10.149  6.527   14.231  1.00 75.13  ? 463 THR A CA  1 
ATOM   3201 C C   . THR A 1 463 ? 11.292  7.042   13.356  1.00 81.04  ? 463 THR A C   1 
ATOM   3202 O O   . THR A 1 463 ? 11.568  6.462   12.308  1.00 78.37  ? 463 THR A O   1 
ATOM   3203 C CB  . THR A 1 463 ? 10.657  5.608   15.349  1.00 67.95  ? 463 THR A CB  1 
ATOM   3204 O OG1 . THR A 1 463 ? 11.513  4.616   14.784  1.00 70.36  ? 463 THR A OG1 1 
ATOM   3205 C CG2 . THR A 1 463 ? 9.526   4.927   16.112  1.00 69.16  ? 463 THR A CG2 1 
ATOM   3206 N N   . PRO A 1 464 ? 11.999  8.128   13.755  1.00 83.97  ? 464 PRO A N   1 
ATOM   3207 C CA  . PRO A 1 464 ? 13.112  8.653   12.970  1.00 84.44  ? 464 PRO A CA  1 
ATOM   3208 C C   . PRO A 1 464 ? 14.420  7.899   13.192  1.00 86.21  ? 464 PRO A C   1 
ATOM   3209 O O   . PRO A 1 464 ? 14.590  7.234   14.213  1.00 97.31  ? 464 PRO A O   1 
ATOM   3210 C CB  . PRO A 1 464 ? 13.228  10.113  13.436  1.00 88.16  ? 464 PRO A CB  1 
ATOM   3211 C CG  . PRO A 1 464 ? 12.353  10.238  14.682  1.00 89.09  ? 464 PRO A CG  1 
ATOM   3212 C CD  . PRO A 1 464 ? 11.774  8.887   14.995  1.00 87.69  ? 464 PRO A CD  1 
ATOM   3213 N N   . ILE A 1 465 ? 15.341  8.017   12.228  1.00 86.28  ? 465 ILE A N   1 
ATOM   3214 C CA  . ILE A 1 465 ? 16.653  7.396   12.331  1.00 96.11  ? 465 ILE A CA  1 
ATOM   3215 C C   . ILE A 1 465 ? 17.710  8.456   12.635  1.00 91.30  ? 465 ILE A C   1 
ATOM   3216 O O   . ILE A 1 465 ? 18.133  9.187   11.744  1.00 93.63  ? 465 ILE A O   1 
ATOM   3217 C CB  . ILE A 1 465 ? 16.994  6.597   11.052  1.00 94.29  ? 465 ILE A CB  1 
ATOM   3218 N N   . GLY A 1 466 ? 18.116  8.531   13.909  1.00 97.67  ? 466 GLY A N   1 
ATOM   3219 C CA  . GLY A 1 466 ? 19.134  9.469   14.357  1.00 104.98 ? 466 GLY A CA  1 
ATOM   3220 C C   . GLY A 1 466 ? 18.626  10.418  15.440  1.00 102.63 ? 466 GLY A C   1 
ATOM   3221 O O   . GLY A 1 466 ? 17.688  10.094  16.166  1.00 95.66  ? 466 GLY A O   1 
ATOM   3222 N N   . ASP A 1 467 ? 19.278  11.583  15.543  1.00 103.21 ? 467 ASP A N   1 
ATOM   3223 C CA  . ASP A 1 467 ? 18.833  12.661  16.413  1.00 105.28 ? 467 ASP A CA  1 
ATOM   3224 C C   . ASP A 1 467 ? 18.363  13.847  15.573  1.00 103.84 ? 467 ASP A C   1 
ATOM   3225 O O   . ASP A 1 467 ? 18.766  13.994  14.420  1.00 97.17  ? 467 ASP A O   1 
ATOM   3226 C CB  . ASP A 1 467 ? 19.959  13.089  17.367  1.00 101.24 ? 467 ASP A CB  1 
ATOM   3227 N N   . GLY A 1 468 ? 17.499  14.682  16.164  1.00 96.91  ? 468 GLY A N   1 
ATOM   3228 C CA  . GLY A 1 468 ? 16.991  15.874  15.507  1.00 90.34  ? 468 GLY A CA  1 
ATOM   3229 C C   . GLY A 1 468 ? 15.531  16.161  15.850  1.00 98.21  ? 468 GLY A C   1 
ATOM   3230 O O   . GLY A 1 468 ? 14.832  15.285  16.357  1.00 98.05  ? 468 GLY A O   1 
ATOM   3231 N N   . PRO A 1 469 ? 15.034  17.394  15.592  1.00 95.95  ? 469 PRO A N   1 
ATOM   3232 C CA  . PRO A 1 469 ? 13.643  17.738  15.868  1.00 95.26  ? 469 PRO A CA  1 
ATOM   3233 C C   . PRO A 1 469 ? 12.649  17.175  14.853  1.00 95.06  ? 469 PRO A C   1 
ATOM   3234 O O   . PRO A 1 469 ? 12.675  17.545  13.680  1.00 88.58  ? 469 PRO A O   1 
ATOM   3235 C CB  . PRO A 1 469 ? 13.659  19.269  15.840  1.00 97.47  ? 469 PRO A CB  1 
ATOM   3236 C CG  . PRO A 1 469 ? 14.779  19.615  14.898  1.00 100.68 ? 469 PRO A CG  1 
ATOM   3237 C CD  . PRO A 1 469 ? 15.811  18.526  15.059  1.00 93.88  ? 469 PRO A CD  1 
ATOM   3238 N N   . VAL A 1 470 ? 11.766  16.289  15.331  1.00 94.13  ? 470 VAL A N   1 
ATOM   3239 C CA  . VAL A 1 470 ? 10.647  15.796  14.543  1.00 89.19  ? 470 VAL A CA  1 
ATOM   3240 C C   . VAL A 1 470 ? 9.525   16.832  14.571  1.00 82.90  ? 470 VAL A C   1 
ATOM   3241 O O   . VAL A 1 470 ? 9.713   17.935  15.080  1.00 85.78  ? 470 VAL A O   1 
ATOM   3242 C CB  . VAL A 1 470 ? 10.175  14.415  15.064  1.00 80.11  ? 470 VAL A CB  1 
ATOM   3243 N N   . LEU A 1 471 ? 8.369   16.479  14.001  1.00 83.29  ? 471 LEU A N   1 
ATOM   3244 C CA  . LEU A 1 471 ? 7.169   17.291  14.117  1.00 87.18  ? 471 LEU A CA  1 
ATOM   3245 C C   . LEU A 1 471 ? 5.988   16.393  14.476  1.00 93.11  ? 471 LEU A C   1 
ATOM   3246 O O   . LEU A 1 471 ? 5.229   15.977  13.603  1.00 100.53 ? 471 LEU A O   1 
ATOM   3247 C CB  . LEU A 1 471 ? 6.903   18.043  12.807  1.00 88.73  ? 471 LEU A CB  1 
ATOM   3248 N N   . LEU A 1 472 ? 5.853   16.088  15.773  1.00 91.79  ? 472 LEU A N   1 
ATOM   3249 C CA  . LEU A 1 472 ? 4.803   15.202  16.248  1.00 86.56  ? 472 LEU A CA  1 
ATOM   3250 C C   . LEU A 1 472 ? 3.433   15.841  16.032  1.00 87.57  ? 472 LEU A C   1 
ATOM   3251 O O   . LEU A 1 472 ? 3.159   16.914  16.565  1.00 90.85  ? 472 LEU A O   1 
ATOM   3252 C CB  . LEU A 1 472 ? 5.009   14.863  17.736  1.00 79.70  ? 472 LEU A CB  1 
ATOM   3253 C CG  . LEU A 1 472 ? 6.288   14.088  18.092  1.00 85.50  ? 472 LEU A CG  1 
ATOM   3254 C CD1 . LEU A 1 472 ? 6.136   13.362  19.429  1.00 85.68  ? 472 LEU A CD1 1 
ATOM   3255 C CD2 . LEU A 1 472 ? 6.673   13.093  17.007  1.00 84.86  ? 472 LEU A CD2 1 
ATOM   3256 N N   . PRO A 1 473 ? 2.536   15.205  15.240  1.00 86.13  ? 473 PRO A N   1 
ATOM   3257 C CA  . PRO A 1 473 ? 1.234   15.787  14.924  1.00 90.48  ? 473 PRO A CA  1 
ATOM   3258 C C   . PRO A 1 473 ? 0.244   15.740  16.085  1.00 87.59  ? 473 PRO A C   1 
ATOM   3259 O O   . PRO A 1 473 ? 0.602   15.343  17.191  1.00 89.46  ? 473 PRO A O   1 
ATOM   3260 C CB  . PRO A 1 473 ? 0.756   14.935  13.744  1.00 92.15  ? 473 PRO A CB  1 
ATOM   3261 C CG  . PRO A 1 473 ? 1.422   13.608  13.941  1.00 92.97  ? 473 PRO A CG  1 
ATOM   3262 C CD  . PRO A 1 473 ? 2.744   13.891  14.610  1.00 83.10  ? 473 PRO A CD  1 
ATOM   3263 N N   . ASP A 1 474 ? -0.998  16.167  15.820  1.00 78.48  ? 474 ASP A N   1 
ATOM   3264 C CA  . ASP A 1 474 ? -2.062  16.116  16.809  1.00 85.11  ? 474 ASP A CA  1 
ATOM   3265 C C   . ASP A 1 474 ? -2.856  14.818  16.661  1.00 89.46  ? 474 ASP A C   1 
ATOM   3266 O O   . ASP A 1 474 ? -2.629  13.874  17.412  1.00 88.95  ? 474 ASP A O   1 
ATOM   3267 C CB  . ASP A 1 474 ? -2.964  17.360  16.704  1.00 90.45  ? 474 ASP A CB  1 
ATOM   3268 C CG  . ASP A 1 474 ? -2.233  18.664  16.953  1.00 94.19  ? 474 ASP A CG  1 
ATOM   3269 O OD1 . ASP A 1 474 ? -1.423  19.065  16.090  1.00 95.22  ? 474 ASP A OD1 1 
ATOM   3270 O OD2 . ASP A 1 474 ? -2.461  19.276  18.015  1.00 87.60  ? 474 ASP A OD2 1 
ATOM   3271 N N   . ASN A 1 475 ? -3.757  14.775  15.671  1.00 81.36  ? 475 ASN A N   1 
ATOM   3272 C CA  . ASN A 1 475 ? -4.646  13.645  15.444  1.00 86.39  ? 475 ASN A CA  1 
ATOM   3273 C C   . ASN A 1 475 ? -5.396  13.853  14.129  1.00 95.14  ? 475 ASN A C   1 
ATOM   3274 O O   . ASN A 1 475 ? -6.335  14.648  14.069  1.00 95.26  ? 475 ASN A O   1 
ATOM   3275 C CB  . ASN A 1 475 ? -5.641  13.463  16.613  1.00 87.02  ? 475 ASN A CB  1 
ATOM   3276 C CG  . ASN A 1 475 ? -5.321  12.326  17.562  1.00 83.57  ? 475 ASN A CG  1 
ATOM   3277 O OD1 . ASN A 1 475 ? -4.180  12.108  17.984  1.00 78.14  ? 475 ASN A OD1 1 
ATOM   3278 N ND2 . ASN A 1 475 ? -6.340  11.560  17.914  1.00 84.13  ? 475 ASN A ND2 1 
ATOM   3279 N N   . HIS A 1 476 ? -4.970  13.142  13.076  1.00 96.34  ? 476 HIS A N   1 
ATOM   3280 C CA  . HIS A 1 476 ? -5.531  13.330  11.747  1.00 90.54  ? 476 HIS A CA  1 
ATOM   3281 C C   . HIS A 1 476 ? -5.503  12.047  10.920  1.00 88.60  ? 476 HIS A C   1 
ATOM   3282 O O   . HIS A 1 476 ? -4.839  11.083  11.295  1.00 92.11  ? 476 HIS A O   1 
ATOM   3283 C CB  . HIS A 1 476 ? -4.771  14.447  11.018  1.00 81.04  ? 476 HIS A CB  1 
ATOM   3284 C CG  . HIS A 1 476 ? -3.345  14.121  10.688  1.00 85.64  ? 476 HIS A CG  1 
ATOM   3285 N ND1 . HIS A 1 476 ? -2.299  14.642  11.421  1.00 84.58  ? 476 HIS A ND1 1 
ATOM   3286 C CD2 . HIS A 1 476 ? -2.842  13.330  9.715   1.00 86.27  ? 476 HIS A CD2 1 
ATOM   3287 C CE1 . HIS A 1 476 ? -1.192  14.163  10.871  1.00 85.93  ? 476 HIS A CE1 1 
ATOM   3288 N NE2 . HIS A 1 476 ? -1.476  13.367  9.837   1.00 84.07  ? 476 HIS A NE2 1 
ATOM   3289 N N   . TYR A 1 477 ? -6.224  12.061  9.789   1.00 90.28  ? 477 TYR A N   1 
ATOM   3290 C CA  . TYR A 1 477 ? -6.300  10.911  8.901   1.00 90.87  ? 477 TYR A CA  1 
ATOM   3291 C C   . TYR A 1 477 ? -5.809  11.240  7.493   1.00 91.40  ? 477 TYR A C   1 
ATOM   3292 O O   . TYR A 1 477 ? -5.991  12.356  7.011   1.00 92.90  ? 477 TYR A O   1 
ATOM   3293 C CB  . TYR A 1 477 ? -7.740  10.335  8.858   1.00 85.66  ? 477 TYR A CB  1 
ATOM   3294 C CG  . TYR A 1 477 ? -8.790  11.192  8.179   1.00 86.41  ? 477 TYR A CG  1 
ATOM   3295 C CD1 . TYR A 1 477 ? -8.881  11.252  6.792   1.00 90.42  ? 477 TYR A CD1 1 
ATOM   3296 C CD2 . TYR A 1 477 ? -9.711  11.921  8.922   1.00 86.38  ? 477 TYR A CD2 1 
ATOM   3297 C CE1 . TYR A 1 477 ? -9.851  12.029  6.164   1.00 82.88  ? 477 TYR A CE1 1 
ATOM   3298 C CE2 . TYR A 1 477 ? -10.685 12.700  8.305   1.00 85.09  ? 477 TYR A CE2 1 
ATOM   3299 C CZ  . TYR A 1 477 ? -10.752 12.752  6.925   1.00 85.09  ? 477 TYR A CZ  1 
ATOM   3300 O OH  . TYR A 1 477 ? -11.712 13.521  6.318   1.00 72.44  ? 477 TYR A OH  1 
ATOM   3301 N N   . LEU A 1 478 ? -5.181  10.247  6.849   1.00 84.86  ? 478 LEU A N   1 
ATOM   3302 C CA  . LEU A 1 478 ? -4.759  10.349  5.462   1.00 79.61  ? 478 LEU A CA  1 
ATOM   3303 C C   . LEU A 1 478 ? -5.756  9.616   4.569   1.00 75.21  ? 478 LEU A C   1 
ATOM   3304 O O   . LEU A 1 478 ? -5.823  8.389   4.594   1.00 68.06  ? 478 LEU A O   1 
ATOM   3305 C CB  . LEU A 1 478 ? -3.347  9.758   5.281   1.00 79.65  ? 478 LEU A CB  1 
ATOM   3306 C CG  . LEU A 1 478 ? -2.175  10.725  5.457   1.00 76.01  ? 478 LEU A CG  1 
ATOM   3307 C CD1 . LEU A 1 478 ? -2.097  11.264  6.867   1.00 80.61  ? 478 LEU A CD1 1 
ATOM   3308 C CD2 . LEU A 1 478 ? -0.872  10.054  5.097   1.00 69.47  ? 478 LEU A CD2 1 
ATOM   3309 N N   . SER A 1 479 ? -6.528  10.385  3.789   1.00 77.93  ? 479 SER A N   1 
ATOM   3310 C CA  . SER A 1 479 ? -7.453  9.825   2.817   1.00 71.70  ? 479 SER A CA  1 
ATOM   3311 C C   . SER A 1 479 ? -6.678  9.324   1.600   1.00 70.20  ? 479 SER A C   1 
ATOM   3312 O O   . SER A 1 479 ? -6.516  10.042  0.615   1.00 77.61  ? 479 SER A O   1 
ATOM   3313 C CB  . SER A 1 479 ? -8.510  10.853  2.422   1.00 75.39  ? 479 SER A CB  1 
ATOM   3314 O OG  . SER A 1 479 ? -9.548  10.256  1.662   1.00 79.04  ? 479 SER A OG  1 
ATOM   3315 N N   . THR A 1 480 ? -6.175  8.088   1.702   1.00 74.67  ? 480 THR A N   1 
ATOM   3316 C CA  . THR A 1 480 ? -5.424  7.454   0.632   1.00 68.46  ? 480 THR A CA  1 
ATOM   3317 C C   . THR A 1 480 ? -6.393  6.844   -0.377  1.00 71.59  ? 480 THR A C   1 
ATOM   3318 O O   . THR A 1 480 ? -7.496  6.434   -0.020  1.00 69.12  ? 480 THR A O   1 
ATOM   3319 C CB  . THR A 1 480 ? -4.455  6.409   1.213   1.00 67.62  ? 480 THR A CB  1 
ATOM   3320 O OG1 . THR A 1 480 ? -3.662  7.018   2.241   1.00 71.59  ? 480 THR A OG1 1 
ATOM   3321 C CG2 . THR A 1 480 ? -3.543  5.806   0.154   1.00 61.37  ? 480 THR A CG2 1 
ATOM   3322 N N   . GLN A 1 481 ? -5.970  6.806   -1.643  1.00 71.09  ? 481 GLN A N   1 
ATOM   3323 C CA  . GLN A 1 481 ? -6.770  6.240   -2.715  1.00 70.81  ? 481 GLN A CA  1 
ATOM   3324 C C   . GLN A 1 481 ? -5.801  5.652   -3.738  1.00 73.25  ? 481 GLN A C   1 
ATOM   3325 O O   . GLN A 1 481 ? -4.773  6.255   -4.041  1.00 66.33  ? 481 GLN A O   1 
ATOM   3326 C CB  . GLN A 1 481 ? -7.682  7.321   -3.317  1.00 69.27  ? 481 GLN A CB  1 
ATOM   3327 C CG  . GLN A 1 481 ? -9.036  6.793   -3.792  1.00 80.21  ? 481 GLN A CG  1 
ATOM   3328 C CD  . GLN A 1 481 ? -10.016 7.901   -4.155  1.00 71.57  ? 481 GLN A CD  1 
ATOM   3329 O OE1 . GLN A 1 481 ? -11.188 7.657   -4.462  1.00 67.82  ? 481 GLN A OE1 1 
ATOM   3330 N NE2 . GLN A 1 481 ? -9.569  9.142   -4.123  1.00 74.63  ? 481 GLN A NE2 1 
ATOM   3331 N N   . SER A 1 482 ? -6.131  4.461   -4.246  1.00 71.34  ? 482 SER A N   1 
ATOM   3332 C CA  . SER A 1 482 ? -5.205  3.682   -5.048  1.00 69.71  ? 482 SER A CA  1 
ATOM   3333 C C   . SER A 1 482 ? -5.895  3.066   -6.259  1.00 63.73  ? 482 SER A C   1 
ATOM   3334 O O   . SER A 1 482 ? -6.992  2.531   -6.138  1.00 61.47  ? 482 SER A O   1 
ATOM   3335 C CB  . SER A 1 482 ? -4.574  2.576   -4.207  1.00 72.47  ? 482 SER A CB  1 
ATOM   3336 O OG  . SER A 1 482 ? -3.738  3.105   -3.190  1.00 71.50  ? 482 SER A OG  1 
ATOM   3337 N N   . LYS A 1 483 ? -5.244  3.166   -7.423  1.00 70.76  ? 483 LYS A N   1 
ATOM   3338 C CA  . LYS A 1 483 ? -5.704  2.487   -8.622  1.00 59.60  ? 483 LYS A CA  1 
ATOM   3339 C C   . LYS A 1 483 ? -4.585  1.558   -9.073  1.00 54.65  ? 483 LYS A C   1 
ATOM   3340 O O   . LYS A 1 483 ? -3.427  1.969   -9.122  1.00 57.55  ? 483 LYS A O   1 
ATOM   3341 C CB  . LYS A 1 483 ? -6.065  3.480   -9.729  1.00 69.87  ? 483 LYS A CB  1 
ATOM   3342 C CG  . LYS A 1 483 ? -6.980  2.894   -10.798 1.00 67.94  ? 483 LYS A CG  1 
ATOM   3343 C CD  . LYS A 1 483 ? -7.232  3.877   -11.931 1.00 71.42  ? 483 LYS A CD  1 
ATOM   3344 C CE  . LYS A 1 483 ? -8.232  3.372   -12.945 1.00 71.18  ? 483 LYS A CE  1 
ATOM   3345 N NZ  . LYS A 1 483 ? -7.807  2.084   -13.558 1.00 65.76  ? 483 LYS A NZ  1 
ATOM   3346 N N   . LEU A 1 484 ? -4.949  0.303   -9.364  1.00 50.59  ? 484 LEU A N   1 
ATOM   3347 C CA  . LEU A 1 484 ? -4.006  -0.714  -9.792  1.00 51.10  ? 484 LEU A CA  1 
ATOM   3348 C C   . LEU A 1 484 ? -4.293  -1.039  -11.250 1.00 58.10  ? 484 LEU A C   1 
ATOM   3349 O O   . LEU A 1 484 ? -5.370  -1.534  -11.578 1.00 59.06  ? 484 LEU A O   1 
ATOM   3350 C CB  . LEU A 1 484 ? -4.127  -1.983  -8.934  1.00 64.12  ? 484 LEU A CB  1 
ATOM   3351 C CG  . LEU A 1 484 ? -3.226  -2.067  -7.717  1.00 49.12  ? 484 LEU A CG  1 
ATOM   3352 C CD1 . LEU A 1 484 ? -3.504  -0.937  -6.755  1.00 47.04  ? 484 LEU A CD1 1 
ATOM   3353 C CD2 . LEU A 1 484 ? -3.391  -3.408  -7.026  1.00 51.88  ? 484 LEU A CD2 1 
ATOM   3354 N N   . SER A 1 485 ? -3.320  -0.731  -12.113 1.00 60.51  ? 485 SER A N   1 
ATOM   3355 C CA  . SER A 1 485 ? -3.428  -1.004  -13.536 1.00 63.38  ? 485 SER A CA  1 
ATOM   3356 C C   . SER A 1 485 ? -2.339  -2.007  -13.902 1.00 61.25  ? 485 SER A C   1 
ATOM   3357 O O   . SER A 1 485 ? -1.629  -2.498  -13.028 1.00 64.75  ? 485 SER A O   1 
ATOM   3358 C CB  . SER A 1 485 ? -3.356  0.291   -14.342 1.00 45.83  ? 485 SER A CB  1 
ATOM   3359 O OG  . SER A 1 485 ? -2.326  1.147   -13.880 1.00 59.10  ? 485 SER A OG  1 
ATOM   3360 N N   . LYS A 1 486 ? -2.233  -2.323  -15.193 1.00 60.09  ? 486 LYS A N   1 
ATOM   3361 C CA  . LYS A 1 486 ? -1.276  -3.304  -15.664 1.00 57.02  ? 486 LYS A CA  1 
ATOM   3362 C C   . LYS A 1 486 ? -0.609  -2.720  -16.904 1.00 59.42  ? 486 LYS A C   1 
ATOM   3363 O O   . LYS A 1 486 ? -1.272  -2.073  -17.710 1.00 69.57  ? 486 LYS A O   1 
ATOM   3364 C CB  . LYS A 1 486 ? -2.009  -4.625  -15.954 1.00 56.91  ? 486 LYS A CB  1 
ATOM   3365 C CG  . LYS A 1 486 ? -1.322  -5.883  -15.425 1.00 67.19  ? 486 LYS A CG  1 
ATOM   3366 C CD  . LYS A 1 486 ? -1.373  -6.043  -13.914 1.00 51.75  ? 486 LYS A CD  1 
ATOM   3367 C CE  . LYS A 1 486 ? -0.826  -7.388  -13.498 1.00 64.13  ? 486 LYS A CE  1 
ATOM   3368 N NZ  . LYS A 1 486 ? -0.758  -7.538  -12.015 1.00 63.92  ? 486 LYS A NZ  1 
ATOM   3369 N N   . ASP A 1 487 ? 0.710   -2.915  -17.027 1.00 59.83  ? 487 ASP A N   1 
ATOM   3370 C CA  . ASP A 1 487 ? 1.437   -2.492  -18.212 1.00 61.31  ? 487 ASP A CA  1 
ATOM   3371 C C   . ASP A 1 487 ? 1.385   -3.587  -19.276 1.00 62.76  ? 487 ASP A C   1 
ATOM   3372 O O   . ASP A 1 487 ? 1.951   -4.665  -19.084 1.00 58.93  ? 487 ASP A O   1 
ATOM   3373 C CB  . ASP A 1 487 ? 2.896   -2.138  -17.890 1.00 64.18  ? 487 ASP A CB  1 
ATOM   3374 C CG  . ASP A 1 487 ? 3.682   -1.754  -19.129 1.00 66.47  ? 487 ASP A CG  1 
ATOM   3375 O OD1 . ASP A 1 487 ? 3.188   -0.908  -19.904 1.00 73.54  ? 487 ASP A OD1 1 
ATOM   3376 O OD2 . ASP A 1 487 ? 4.782   -2.315  -19.334 1.00 67.63  ? 487 ASP A OD2 1 
ATOM   3377 N N   . PRO A 1 488 ? 0.730   -3.339  -20.437 1.00 66.91  ? 488 PRO A N   1 
ATOM   3378 C CA  . PRO A 1 488 ? 0.610   -4.352  -21.482 1.00 61.74  ? 488 PRO A CA  1 
ATOM   3379 C C   . PRO A 1 488 ? 1.936   -4.852  -22.057 1.00 58.04  ? 488 PRO A C   1 
ATOM   3380 O O   . PRO A 1 488 ? 1.966   -5.905  -22.684 1.00 57.75  ? 488 PRO A O   1 
ATOM   3381 C CB  . PRO A 1 488 ? -0.206  -3.644  -22.573 1.00 59.02  ? 488 PRO A CB  1 
ATOM   3382 C CG  . PRO A 1 488 ? -0.829  -2.466  -21.908 1.00 62.82  ? 488 PRO A CG  1 
ATOM   3383 C CD  . PRO A 1 488 ? 0.086   -2.068  -20.804 1.00 57.81  ? 488 PRO A CD  1 
ATOM   3384 N N   . ASN A 1 489 ? 3.025   -4.097  -21.861 1.00 61.34  ? 489 ASN A N   1 
ATOM   3385 C CA  . ASN A 1 489 ? 4.316   -4.454  -22.433 1.00 59.90  ? 489 ASN A CA  1 
ATOM   3386 C C   . ASN A 1 489 ? 5.308   -5.091  -21.458 1.00 67.47  ? 489 ASN A C   1 
ATOM   3387 O O   . ASN A 1 489 ? 6.289   -5.689  -21.892 1.00 70.27  ? 489 ASN A O   1 
ATOM   3388 C CB  . ASN A 1 489 ? 4.934   -3.215  -23.093 1.00 65.79  ? 489 ASN A CB  1 
ATOM   3389 C CG  . ASN A 1 489 ? 4.161   -2.781  -24.328 1.00 74.77  ? 489 ASN A CG  1 
ATOM   3390 O OD1 . ASN A 1 489 ? 4.072   -3.509  -25.328 1.00 61.88  ? 489 ASN A OD1 1 
ATOM   3391 N ND2 . ASN A 1 489 ? 3.578   -1.590  -24.286 1.00 66.40  ? 489 ASN A ND2 1 
ATOM   3392 N N   . GLU A 1 490 ? 5.050   -4.979  -20.149 1.00 61.63  ? 490 GLU A N   1 
ATOM   3393 C CA  . GLU A 1 490 ? 5.911   -5.585  -19.147 1.00 61.00  ? 490 GLU A CA  1 
ATOM   3394 C C   . GLU A 1 490 ? 5.797   -7.108  -19.171 1.00 60.07  ? 490 GLU A C   1 
ATOM   3395 O O   . GLU A 1 490 ? 4.700   -7.646  -19.070 1.00 66.20  ? 490 GLU A O   1 
ATOM   3396 C CB  . GLU A 1 490 ? 5.546   -5.063  -17.751 1.00 59.06  ? 490 GLU A CB  1 
ATOM   3397 C CG  . GLU A 1 490 ? 6.545   -5.439  -16.678 1.00 66.88  ? 490 GLU A CG  1 
ATOM   3398 C CD  . GLU A 1 490 ? 7.952   -4.978  -16.989 1.00 66.62  ? 490 GLU A CD  1 
ATOM   3399 O OE1 . GLU A 1 490 ? 8.164   -3.749  -17.104 1.00 62.94  ? 490 GLU A OE1 1 
ATOM   3400 O OE2 . GLU A 1 490 ? 8.839   -5.845  -17.144 1.00 69.79  ? 490 GLU A OE2 1 
ATOM   3401 N N   . LYS A 1 491 ? 6.940   -7.799  -19.264 1.00 58.46  ? 491 LYS A N   1 
ATOM   3402 C CA  . LYS A 1 491 ? 6.958   -9.243  -19.446 1.00 58.85  ? 491 LYS A CA  1 
ATOM   3403 C C   . LYS A 1 491 ? 7.054   -10.033 -18.142 1.00 62.95  ? 491 LYS A C   1 
ATOM   3404 O O   . LYS A 1 491 ? 6.871   -11.247 -18.136 1.00 67.72  ? 491 LYS A O   1 
ATOM   3405 C CB  . LYS A 1 491 ? 8.130   -9.637  -20.352 1.00 66.12  ? 491 LYS A CB  1 
ATOM   3406 C CG  . LYS A 1 491 ? 8.289   -8.717  -21.537 1.00 62.31  ? 491 LYS A CG  1 
ATOM   3407 C CD  . LYS A 1 491 ? 9.073   -9.319  -22.662 1.00 62.38  ? 491 LYS A CD  1 
ATOM   3408 C CE  . LYS A 1 491 ? 9.311   -8.285  -23.732 1.00 57.15  ? 491 LYS A CE  1 
ATOM   3409 N NZ  . LYS A 1 491 ? 9.478   -8.915  -25.046 1.00 56.89  ? 491 LYS A NZ  1 
ATOM   3410 N N   . ARG A 1 492 ? 7.333   -9.334  -17.041 1.00 48.14  ? 492 ARG A N   1 
ATOM   3411 C CA  . ARG A 1 492 ? 7.474   -9.966  -15.740 1.00 68.77  ? 492 ARG A CA  1 
ATOM   3412 C C   . ARG A 1 492 ? 6.286   -9.573  -14.868 1.00 64.17  ? 492 ARG A C   1 
ATOM   3413 O O   . ARG A 1 492 ? 5.703   -8.509  -15.058 1.00 56.69  ? 492 ARG A O   1 
ATOM   3414 C CB  . ARG A 1 492 ? 8.810   -9.567  -15.078 1.00 60.14  ? 492 ARG A CB  1 
ATOM   3415 C CG  . ARG A 1 492 ? 9.139   -8.086  -15.213 1.00 70.66  ? 492 ARG A CG  1 
ATOM   3416 C CD  . ARG A 1 492 ? 10.415  -7.676  -14.514 1.00 76.38  ? 492 ARG A CD  1 
ATOM   3417 N NE  . ARG A 1 492 ? 11.607  -8.053  -15.265 1.00 88.06  ? 492 ARG A NE  1 
ATOM   3418 C CZ  . ARG A 1 492 ? 12.432  -7.192  -15.849 1.00 78.40  ? 492 ARG A CZ  1 
ATOM   3419 N NH1 . ARG A 1 492 ? 12.059  -5.953  -16.122 1.00 67.98  ? 492 ARG A NH1 1 
ATOM   3420 N NH2 . ARG A 1 492 ? 13.655  -7.591  -16.185 1.00 92.72  ? 492 ARG A NH2 1 
ATOM   3421 N N   . ASP A 1 493 ? 5.934   -10.451 -13.923 1.00 54.84  ? 493 ASP A N   1 
ATOM   3422 C CA  . ASP A 1 493 ? 4.908   -10.156 -12.941 1.00 56.46  ? 493 ASP A CA  1 
ATOM   3423 C C   . ASP A 1 493 ? 5.145   -8.739  -12.427 1.00 57.99  ? 493 ASP A C   1 
ATOM   3424 O O   . ASP A 1 493 ? 6.227   -8.436  -11.931 1.00 58.22  ? 493 ASP A O   1 
ATOM   3425 C CB  . ASP A 1 493 ? 4.937   -11.177 -11.785 1.00 64.33  ? 493 ASP A CB  1 
ATOM   3426 C CG  . ASP A 1 493 ? 3.601   -11.364 -11.088 1.00 65.75  ? 493 ASP A CG  1 
ATOM   3427 O OD1 . ASP A 1 493 ? 2.643   -10.647 -11.443 1.00 61.54  ? 493 ASP A OD1 1 
ATOM   3428 O OD2 . ASP A 1 493 ? 3.510   -12.245 -10.201 1.00 66.51  ? 493 ASP A OD2 1 
ATOM   3429 N N   . HIS A 1 494 ? 4.138   -7.870  -12.578 1.00 62.17  ? 494 HIS A N   1 
ATOM   3430 C CA  . HIS A 1 494 ? 4.288   -6.462  -12.244 1.00 53.28  ? 494 HIS A CA  1 
ATOM   3431 C C   . HIS A 1 494 ? 3.002   -5.831  -11.716 1.00 55.53  ? 494 HIS A C   1 
ATOM   3432 O O   . HIS A 1 494 ? 1.945   -6.463  -11.712 1.00 55.80  ? 494 HIS A O   1 
ATOM   3433 C CB  . HIS A 1 494 ? 4.758   -5.700  -13.483 1.00 63.71  ? 494 HIS A CB  1 
ATOM   3434 C CG  . HIS A 1 494 ? 3.742   -5.666  -14.582 1.00 57.35  ? 494 HIS A CG  1 
ATOM   3435 N ND1 . HIS A 1 494 ? 3.290   -6.825  -15.182 1.00 58.55  ? 494 HIS A ND1 1 
ATOM   3436 C CD2 . HIS A 1 494 ? 3.119   -4.611  -15.143 1.00 54.59  ? 494 HIS A CD2 1 
ATOM   3437 C CE1 . HIS A 1 494 ? 2.413   -6.442  -16.098 1.00 59.62  ? 494 HIS A CE1 1 
ATOM   3438 N NE2 . HIS A 1 494 ? 2.277   -5.112  -16.104 1.00 61.46  ? 494 HIS A NE2 1 
ATOM   3439 N N   . MET A 1 495 ? 3.119   -4.574  -11.268 1.00 58.46  ? 495 MET A N   1 
ATOM   3440 C CA  . MET A 1 495 ? 1.976   -3.787  -10.837 1.00 57.23  ? 495 MET A CA  1 
ATOM   3441 C C   . MET A 1 495 ? 2.320   -2.309  -11.000 1.00 55.01  ? 495 MET A C   1 
ATOM   3442 O O   . MET A 1 495 ? 3.327   -1.853  -10.468 1.00 52.39  ? 495 MET A O   1 
ATOM   3443 C CB  . MET A 1 495 ? 1.609   -4.105  -9.364  1.00 56.11  ? 495 MET A CB  1 
ATOM   3444 C CG  . MET A 1 495 ? 0.622   -3.112  -8.734  1.00 53.98  ? 495 MET A CG  1 
ATOM   3445 S SD  . MET A 1 495 ? 0.224   -3.482  -7.006  1.00 50.52  ? 495 MET A SD  1 
ATOM   3446 C CE  . MET A 1 495 ? 1.021   -2.146  -6.210  1.00 54.37  ? 495 MET A CE  1 
ATOM   3447 N N   . VAL A 1 496 ? 1.474   -1.580  -11.742 1.00 58.75  ? 496 VAL A N   1 
ATOM   3448 C CA  . VAL A 1 496 ? 1.559   -0.129  -11.829 1.00 57.57  ? 496 VAL A CA  1 
ATOM   3449 C C   . VAL A 1 496 ? 0.499   0.440   -10.887 1.00 55.49  ? 496 VAL A C   1 
ATOM   3450 O O   . VAL A 1 496 ? -0.531  -0.187  -10.646 1.00 52.07  ? 496 VAL A O   1 
ATOM   3451 C CB  . VAL A 1 496 ? 1.453   0.410   -13.293 1.00 56.81  ? 496 VAL A CB  1 
ATOM   3452 C CG1 . VAL A 1 496 ? 0.389   -0.316  -14.087 1.00 60.84  ? 496 VAL A CG1 1 
ATOM   3453 C CG2 . VAL A 1 496 ? 1.218   1.921   -13.336 1.00 54.39  ? 496 VAL A CG2 1 
ATOM   3454 N N   . LEU A 1 497 ? 0.790   1.621   -10.336 1.00 55.43  ? 497 LEU A N   1 
ATOM   3455 C CA  . LEU A 1 497 ? 0.031   2.167   -9.227  1.00 61.02  ? 497 LEU A CA  1 
ATOM   3456 C C   . LEU A 1 497 ? -0.107  3.681   -9.352  1.00 57.94  ? 497 LEU A C   1 
ATOM   3457 O O   . LEU A 1 497 ? 0.894   4.384   -9.475  1.00 56.05  ? 497 LEU A O   1 
ATOM   3458 C CB  . LEU A 1 497 ? 0.758   1.806   -7.925  1.00 54.35  ? 497 LEU A CB  1 
ATOM   3459 C CG  . LEU A 1 497 ? 0.211   2.415   -6.638  1.00 63.48  ? 497 LEU A CG  1 
ATOM   3460 C CD1 . LEU A 1 497 ? -1.091  1.746   -6.220  1.00 51.78  ? 497 LEU A CD1 1 
ATOM   3461 C CD2 . LEU A 1 497 ? 1.241   2.328   -5.524  1.00 47.17  ? 497 LEU A CD2 1 
ATOM   3462 N N   . LEU A 1 498 ? -1.360  4.153   -9.320  1.00 54.32  ? 498 LEU A N   1 
ATOM   3463 C CA  . LEU A 1 498 ? -1.683  5.568   -9.227  1.00 56.10  ? 498 LEU A CA  1 
ATOM   3464 C C   . LEU A 1 498 ? -2.331  5.834   -7.869  1.00 60.63  ? 498 LEU A C   1 
ATOM   3465 O O   . LEU A 1 498 ? -3.388  5.280   -7.573  1.00 69.91  ? 498 LEU A O   1 
ATOM   3466 C CB  . LEU A 1 498 ? -2.627  5.938   -10.383 1.00 62.43  ? 498 LEU A CB  1 
ATOM   3467 C CG  . LEU A 1 498 ? -3.210  7.346   -10.379 1.00 61.44  ? 498 LEU A CG  1 
ATOM   3468 C CD1 . LEU A 1 498 ? -2.183  8.369   -10.788 1.00 52.34  ? 498 LEU A CD1 1 
ATOM   3469 C CD2 . LEU A 1 498 ? -4.416  7.428   -11.286 1.00 66.18  ? 498 LEU A CD2 1 
ATOM   3470 N N   . GLU A 1 499 ? -1.680  6.667   -7.045  1.00 56.12  ? 499 GLU A N   1 
ATOM   3471 C CA  . GLU A 1 499 ? -2.155  6.976   -5.704  1.00 63.84  ? 499 GLU A CA  1 
ATOM   3472 C C   . GLU A 1 499 ? -2.437  8.459   -5.489  1.00 62.62  ? 499 GLU A C   1 
ATOM   3473 O O   . GLU A 1 499 ? -1.725  9.309   -6.014  1.00 67.96  ? 499 GLU A O   1 
ATOM   3474 C CB  . GLU A 1 499 ? -1.135  6.535   -4.652  1.00 55.11  ? 499 GLU A CB  1 
ATOM   3475 C CG  . GLU A 1 499 ? -1.452  5.194   -4.029  1.00 69.83  ? 499 GLU A CG  1 
ATOM   3476 C CD  . GLU A 1 499 ? -0.645  4.892   -2.784  1.00 68.88  ? 499 GLU A CD  1 
ATOM   3477 O OE1 . GLU A 1 499 ? -0.628  5.740   -1.862  1.00 67.72  ? 499 GLU A OE1 1 
ATOM   3478 O OE2 . GLU A 1 499 ? -0.038  3.800   -2.724  1.00 77.08  ? 499 GLU A OE2 1 
ATOM   3479 N N   . PHE A 1 500 ? -3.468  8.742   -4.682  1.00 72.66  ? 500 PHE A N   1 
ATOM   3480 C CA  . PHE A 1 500 ? -3.847  10.098  -4.317  1.00 70.79  ? 500 PHE A CA  1 
ATOM   3481 C C   . PHE A 1 500 ? -3.987  10.209  -2.802  1.00 76.59  ? 500 PHE A C   1 
ATOM   3482 O O   . PHE A 1 500 ? -5.030  9.873   -2.243  1.00 74.34  ? 500 PHE A O   1 
ATOM   3483 C CB  . PHE A 1 500 ? -5.161  10.502  -5.004  1.00 71.48  ? 500 PHE A CB  1 
ATOM   3484 C CG  . PHE A 1 500 ? -5.057  11.039  -6.415  1.00 84.80  ? 500 PHE A CG  1 
ATOM   3485 C CD1 . PHE A 1 500 ? -3.822  11.255  -7.012  1.00 78.44  ? 500 PHE A CD1 1 
ATOM   3486 C CD2 . PHE A 1 500 ? -6.193  11.344  -7.140  1.00 88.38  ? 500 PHE A CD2 1 
ATOM   3487 C CE1 . PHE A 1 500 ? -3.734  11.758  -8.303  1.00 83.06  ? 500 PHE A CE1 1 
ATOM   3488 C CE2 . PHE A 1 500 ? -6.099  11.847  -8.433  1.00 99.12  ? 500 PHE A CE2 1 
ATOM   3489 C CZ  . PHE A 1 500 ? -4.869  12.049  -9.006  1.00 83.89  ? 500 PHE A CZ  1 
ATOM   3490 N N   . VAL A 1 501 ? -2.925  10.712  -2.162  1.00 69.53  ? 501 VAL A N   1 
ATOM   3491 C CA  . VAL A 1 501 ? -2.801  10.711  -0.714  1.00 74.69  ? 501 VAL A CA  1 
ATOM   3492 C C   . VAL A 1 501 ? -2.993  12.119  -0.157  1.00 77.23  ? 501 VAL A C   1 
ATOM   3493 O O   . VAL A 1 501 ? -2.057  12.916  -0.127  1.00 69.52  ? 501 VAL A O   1 
ATOM   3494 C CB  . VAL A 1 501 ? -1.453  10.097  -0.272  1.00 67.41  ? 501 VAL A CB  1 
ATOM   3495 C CG1 . VAL A 1 501 ? -1.532  8.580   -0.218  1.00 73.92  ? 501 VAL A CG1 1 
ATOM   3496 C CG2 . VAL A 1 501 ? -0.305  10.539  -1.167  1.00 77.53  ? 501 VAL A CG2 1 
ATOM   3497 N N   . THR A 1 502 ? -4.222  12.397  0.298   1.00 80.38  ? 502 THR A N   1 
ATOM   3498 C CA  . THR A 1 502 ? -4.598  13.704  0.812   1.00 83.77  ? 502 THR A CA  1 
ATOM   3499 C C   . THR A 1 502 ? -4.837  13.633  2.320   1.00 84.25  ? 502 THR A C   1 
ATOM   3500 O O   . THR A 1 502 ? -5.447  12.682  2.805   1.00 83.28  ? 502 THR A O   1 
ATOM   3501 C CB  . THR A 1 502 ? -5.846  14.205  0.071   1.00 83.18  ? 502 THR A CB  1 
ATOM   3502 O OG1 . THR A 1 502 ? -7.017  13.689  0.701   1.00 92.22  ? 502 THR A OG1 1 
ATOM   3503 C CG2 . THR A 1 502 ? -5.852  13.808  -1.397  1.00 89.59  ? 502 THR A CG2 1 
ATOM   3504 N N   . ALA A 1 503 ? -4.367  14.655  3.048   1.00 85.25  ? 503 ALA A N   1 
ATOM   3505 C CA  . ALA A 1 503 ? -4.525  14.725  4.493   1.00 86.87  ? 503 ALA A CA  1 
ATOM   3506 C C   . ALA A 1 503 ? -5.718  15.592  4.894   1.00 87.42  ? 503 ALA A C   1 
ATOM   3507 O O   . ALA A 1 503 ? -5.909  16.675  4.348   1.00 93.57  ? 503 ALA A O   1 
ATOM   3508 C CB  . ALA A 1 503 ? -3.256  15.266  5.123   1.00 83.17  ? 503 ALA A CB  1 
ATOM   3509 N N   . ALA A 1 504 ? -6.507  15.108  5.863   1.00 95.91  ? 504 ALA A N   1 
ATOM   3510 C CA  . ALA A 1 504 ? -7.694  15.808  6.331   1.00 92.57  ? 504 ALA A CA  1 
ATOM   3511 C C   . ALA A 1 504 ? -8.072  15.359  7.741   1.00 90.19  ? 504 ALA A C   1 
ATOM   3512 O O   . ALA A 1 504 ? -7.928  14.187  8.073   1.00 94.93  ? 504 ALA A O   1 
ATOM   3513 C CB  . ALA A 1 504 ? -8.854  15.563  5.378   1.00 88.98  ? 504 ALA A CB  1 
ATOM   3514 N N   . GLY A 1 505 ? -8.559  16.299  8.561   1.00 96.92  ? 505 GLY A N   1 
ATOM   3515 C CA  . GLY A 1 505 ? -8.963  15.997  9.926   1.00 92.46  ? 505 GLY A CA  1 
ATOM   3516 C C   . GLY A 1 505 ? -9.003  17.215  10.824  1.00 95.30  ? 505 GLY A C   1 
ATOM   3517 O O   . GLY A 1 505 ? -8.368  17.238  11.879  1.00 87.33  ? 505 GLY A O   1 
HETATM 3518 O O   . HOH B 2 .   ? -3.223  -17.887 2.667   1.00 60.49  ? 601 HOH A O   1 
HETATM 3519 O O   . HOH B 2 .   ? 1.108   -4.247  2.339   1.00 52.72  ? 602 HOH A O   1 
HETATM 3520 O O   . HOH B 2 .   ? 5.562   5.906   4.421   1.00 64.56  ? 603 HOH A O   1 
HETATM 3521 O O   . HOH B 2 .   ? 7.370   -22.289 1.462   1.00 78.62  ? 604 HOH A O   1 
HETATM 3522 O O   . HOH B 2 .   ? -19.873 42.628  -31.280 1.00 55.27  ? 605 HOH A O   1 
HETATM 3523 O O   . HOH B 2 .   ? 2.176   30.109  -25.410 1.00 63.74  ? 606 HOH A O   1 
HETATM 3524 O O   . HOH B 2 .   ? -4.413  35.411  -26.466 1.00 38.27  ? 607 HOH A O   1 
HETATM 3525 O O   . HOH B 2 .   ? 2.152   6.173   0.379   1.00 84.49  ? 608 HOH A O   1 
HETATM 3526 H H1  . HOH B 2 .   ? 2.310   6.173   -0.575  1.00 101.39 ? 608 HOH A H1  1 
HETATM 3527 H H2  . HOH B 2 .   ? 3.019   6.173   0.806   1.00 101.39 ? 608 HOH A H2  1 
HETATM 3528 O O   . HOH B 2 .   ? 0.923   18.759  -38.923 1.00 82.91  ? 609 HOH A O   1 
# 
