data_9JRY
# 
_entry.id   9JRY 
# 
_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   9JRY         pdb_00009jry 10.2210/pdb9jry/pdb 
WWPDB D_1300051977 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-01-22 ? 
2 'Structure model' 1 1 2025-03-19 ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Database references' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' citation        
2 2 'Structure model' citation_author 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 2 'Structure model' '_citation.journal_volume'          
2 2 'Structure model' '_citation.page_first'              
3 2 'Structure model' '_citation.page_last'               
4 2 'Structure model' '_citation_author.identifier_ORCID' 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9JRY 
_pdbx_database_status.recvd_initial_deposition_date   2024-09-29 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBJ 
_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_contact_author.id                 2 
_pdbx_contact_author.email              yipark@cnu.ac.kr 
_pdbx_contact_author.name_first         Youn-Il 
_pdbx_contact_author.name_last          Park 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-2912-2821 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Yang, H.W.'  1 0000-0003-0930-9963 
'Park, Y.-I.' 2 0000-0003-2912-2821 
'Song, J.-J.' 3 0000-0001-7120-6311 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Febs J.' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           1742-464X 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            292 
_citation.language                  ? 
_citation.page_first                1197 
_citation.page_last                 1216 
_citation.title                     'Dual-Cys bacteriophytochromes: intermediates in cyanobacterial phytochrome evolution?' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1111/febs.17395 
_citation.pdbx_database_id_PubMed   39801362 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Yang, H.W.'     1 ? 
primary 'Song, J.Y.'     2 ? 
primary 'Song, J.J.'     3 ? 
primary 'Kim, Y.W.'      4 ? 
primary 'Rockwell, N.C.' 5 ? 
primary 'Kim, W.'        6 ? 
primary 'Kim, H.'        7 ? 
primary 'Lagarias, J.C.' 8 ? 
primary 'Park, Y.I.'     9 ? 
# 
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 FiDCB 59569.668 2 ? ? ? ? 
2 non-polymer syn 
;3-[5-[(Z)-(4-ethenyl-3-methyl-5-oxidanylidene-pyrrol-2-ylidene)methyl]-2-[[5-[(Z)-(3-ethenyl-4-methyl-5-oxidanylidene-pyrrol-2-ylidene)methyl]-3-(3-hydroxy-3-oxopropyl)-4-methyl-1H-pyrrol-2-yl]methyl]-4-methyl-1H-pyrrol-3-yl]propanoic acid
;
584.662   2 ? ? ? ? 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;MNTNKNDTAFTVDLTNCDKEPIHIPGFVQPHGVLLAIKEPELTILQVSNNTYNCLGFHPEELLNQPLRKLLESEQIDFLN
DCLTQEDIQIVNPVEFTIKTFQEPIIFDGIIHRSNGVVILELEPAILEKNNNYFRFYHLVKLAIGKLQSTKTVTEISQII
VTEVRRITGFDRVMFYRFDRDWNGIVIAEDKQEHLPSYLDLHYPASDIPTPARKLYSQNWLRLIPDADYQAAAIVPTNNP
LTDEPLDLSGSVLRSVSPCHIEYLHNMGVKASMSISIIKNNKLWGLIACHHQTPKYVPYEIRHACEFLGQVTSLEIATKE
DNEDSESKIEIKSVLAKLVEYMSAEKSFIDGLINKQPNILNLVNAQGAAICFNKELYLLGNTPEKQDIQNLLLWIHNNID
EDIFYTDSLSQVYPEAEKFKDVASGLIALSISKTQNKYVLWFRPEEVQTVNWGGNPNQPVEVSENGGLHLSPRKSFELWK
EIVRLKSLPWKSYEVNAAAELRGAIITVVLRKIDEHHHHHH
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MNTNKNDTAFTVDLTNCDKEPIHIPGFVQPHGVLLAIKEPELTILQVSNNTYNCLGFHPEELLNQPLRKLLESEQIDFLN
DCLTQEDIQIVNPVEFTIKTFQEPIIFDGIIHRSNGVVILELEPAILEKNNNYFRFYHLVKLAIGKLQSTKTVTEISQII
VTEVRRITGFDRVMFYRFDRDWNGIVIAEDKQEHLPSYLDLHYPASDIPTPARKLYSQNWLRLIPDADYQAAAIVPTNNP
LTDEPLDLSGSVLRSVSPCHIEYLHNMGVKASMSISIIKNNKLWGLIACHHQTPKYVPYEIRHACEFLGQVTSLEIATKE
DNEDSESKIEIKSVLAKLVEYMSAEKSFIDGLINKQPNILNLVNAQGAAICFNKELYLLGNTPEKQDIQNLLLWIHNNID
EDIFYTDSLSQVYPEAEKFKDVASGLIALSISKTQNKYVLWFRPEEVQTVNWGGNPNQPVEVSENGGLHLSPRKSFELWK
EIVRLKSLPWKSYEVNAAAELRGAIITVVLRKIDEHHHHHH
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
_pdbx_entity_nonpoly.entity_id   2 
_pdbx_entity_nonpoly.name        
;3-[5-[(Z)-(4-ethenyl-3-methyl-5-oxidanylidene-pyrrol-2-ylidene)methyl]-2-[[5-[(Z)-(3-ethenyl-4-methyl-5-oxidanylidene-pyrrol-2-ylidene)methyl]-3-(3-hydroxy-3-oxopropyl)-4-methyl-1H-pyrrol-2-yl]methyl]-4-methyl-1H-pyrrol-3-yl]propanoic acid
;
_pdbx_entity_nonpoly.comp_id     BLR 
# 
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   ASN n 
1 3   THR n 
1 4   ASN n 
1 5   LYS n 
1 6   ASN n 
1 7   ASP n 
1 8   THR n 
1 9   ALA n 
1 10  PHE n 
1 11  THR n 
1 12  VAL n 
1 13  ASP n 
1 14  LEU n 
1 15  THR n 
1 16  ASN n 
1 17  CYS n 
1 18  ASP n 
1 19  LYS n 
1 20  GLU n 
1 21  PRO n 
1 22  ILE n 
1 23  HIS n 
1 24  ILE n 
1 25  PRO n 
1 26  GLY n 
1 27  PHE n 
1 28  VAL n 
1 29  GLN n 
1 30  PRO n 
1 31  HIS n 
1 32  GLY n 
1 33  VAL n 
1 34  LEU n 
1 35  LEU n 
1 36  ALA n 
1 37  ILE n 
1 38  LYS n 
1 39  GLU n 
1 40  PRO n 
1 41  GLU n 
1 42  LEU n 
1 43  THR n 
1 44  ILE n 
1 45  LEU n 
1 46  GLN n 
1 47  VAL n 
1 48  SER n 
1 49  ASN n 
1 50  ASN n 
1 51  THR n 
1 52  TYR n 
1 53  ASN n 
1 54  CYS n 
1 55  LEU n 
1 56  GLY n 
1 57  PHE n 
1 58  HIS n 
1 59  PRO n 
1 60  GLU n 
1 61  GLU n 
1 62  LEU n 
1 63  LEU n 
1 64  ASN n 
1 65  GLN n 
1 66  PRO n 
1 67  LEU n 
1 68  ARG n 
1 69  LYS n 
1 70  LEU n 
1 71  LEU n 
1 72  GLU n 
1 73  SER n 
1 74  GLU n 
1 75  GLN n 
1 76  ILE n 
1 77  ASP n 
1 78  PHE n 
1 79  LEU n 
1 80  ASN n 
1 81  ASP n 
1 82  CYS n 
1 83  LEU n 
1 84  THR n 
1 85  GLN n 
1 86  GLU n 
1 87  ASP n 
1 88  ILE n 
1 89  GLN n 
1 90  ILE n 
1 91  VAL n 
1 92  ASN n 
1 93  PRO n 
1 94  VAL n 
1 95  GLU n 
1 96  PHE n 
1 97  THR n 
1 98  ILE n 
1 99  LYS n 
1 100 THR n 
1 101 PHE n 
1 102 GLN n 
1 103 GLU n 
1 104 PRO n 
1 105 ILE n 
1 106 ILE n 
1 107 PHE n 
1 108 ASP n 
1 109 GLY n 
1 110 ILE n 
1 111 ILE n 
1 112 HIS n 
1 113 ARG n 
1 114 SER n 
1 115 ASN n 
1 116 GLY n 
1 117 VAL n 
1 118 VAL n 
1 119 ILE n 
1 120 LEU n 
1 121 GLU n 
1 122 LEU n 
1 123 GLU n 
1 124 PRO n 
1 125 ALA n 
1 126 ILE n 
1 127 LEU n 
1 128 GLU n 
1 129 LYS n 
1 130 ASN n 
1 131 ASN n 
1 132 ASN n 
1 133 TYR n 
1 134 PHE n 
1 135 ARG n 
1 136 PHE n 
1 137 TYR n 
1 138 HIS n 
1 139 LEU n 
1 140 VAL n 
1 141 LYS n 
1 142 LEU n 
1 143 ALA n 
1 144 ILE n 
1 145 GLY n 
1 146 LYS n 
1 147 LEU n 
1 148 GLN n 
1 149 SER n 
1 150 THR n 
1 151 LYS n 
1 152 THR n 
1 153 VAL n 
1 154 THR n 
1 155 GLU n 
1 156 ILE n 
1 157 SER n 
1 158 GLN n 
1 159 ILE n 
1 160 ILE n 
1 161 VAL n 
1 162 THR n 
1 163 GLU n 
1 164 VAL n 
1 165 ARG n 
1 166 ARG n 
1 167 ILE n 
1 168 THR n 
1 169 GLY n 
1 170 PHE n 
1 171 ASP n 
1 172 ARG n 
1 173 VAL n 
1 174 MET n 
1 175 PHE n 
1 176 TYR n 
1 177 ARG n 
1 178 PHE n 
1 179 ASP n 
1 180 ARG n 
1 181 ASP n 
1 182 TRP n 
1 183 ASN n 
1 184 GLY n 
1 185 ILE n 
1 186 VAL n 
1 187 ILE n 
1 188 ALA n 
1 189 GLU n 
1 190 ASP n 
1 191 LYS n 
1 192 GLN n 
1 193 GLU n 
1 194 HIS n 
1 195 LEU n 
1 196 PRO n 
1 197 SER n 
1 198 TYR n 
1 199 LEU n 
1 200 ASP n 
1 201 LEU n 
1 202 HIS n 
1 203 TYR n 
1 204 PRO n 
1 205 ALA n 
1 206 SER n 
1 207 ASP n 
1 208 ILE n 
1 209 PRO n 
1 210 THR n 
1 211 PRO n 
1 212 ALA n 
1 213 ARG n 
1 214 LYS n 
1 215 LEU n 
1 216 TYR n 
1 217 SER n 
1 218 GLN n 
1 219 ASN n 
1 220 TRP n 
1 221 LEU n 
1 222 ARG n 
1 223 LEU n 
1 224 ILE n 
1 225 PRO n 
1 226 ASP n 
1 227 ALA n 
1 228 ASP n 
1 229 TYR n 
1 230 GLN n 
1 231 ALA n 
1 232 ALA n 
1 233 ALA n 
1 234 ILE n 
1 235 VAL n 
1 236 PRO n 
1 237 THR n 
1 238 ASN n 
1 239 ASN n 
1 240 PRO n 
1 241 LEU n 
1 242 THR n 
1 243 ASP n 
1 244 GLU n 
1 245 PRO n 
1 246 LEU n 
1 247 ASP n 
1 248 LEU n 
1 249 SER n 
1 250 GLY n 
1 251 SER n 
1 252 VAL n 
1 253 LEU n 
1 254 ARG n 
1 255 SER n 
1 256 VAL n 
1 257 SER n 
1 258 PRO n 
1 259 CYS n 
1 260 HIS n 
1 261 ILE n 
1 262 GLU n 
1 263 TYR n 
1 264 LEU n 
1 265 HIS n 
1 266 ASN n 
1 267 MET n 
1 268 GLY n 
1 269 VAL n 
1 270 LYS n 
1 271 ALA n 
1 272 SER n 
1 273 MET n 
1 274 SER n 
1 275 ILE n 
1 276 SER n 
1 277 ILE n 
1 278 ILE n 
1 279 LYS n 
1 280 ASN n 
1 281 ASN n 
1 282 LYS n 
1 283 LEU n 
1 284 TRP n 
1 285 GLY n 
1 286 LEU n 
1 287 ILE n 
1 288 ALA n 
1 289 CYS n 
1 290 HIS n 
1 291 HIS n 
1 292 GLN n 
1 293 THR n 
1 294 PRO n 
1 295 LYS n 
1 296 TYR n 
1 297 VAL n 
1 298 PRO n 
1 299 TYR n 
1 300 GLU n 
1 301 ILE n 
1 302 ARG n 
1 303 HIS n 
1 304 ALA n 
1 305 CYS n 
1 306 GLU n 
1 307 PHE n 
1 308 LEU n 
1 309 GLY n 
1 310 GLN n 
1 311 VAL n 
1 312 THR n 
1 313 SER n 
1 314 LEU n 
1 315 GLU n 
1 316 ILE n 
1 317 ALA n 
1 318 THR n 
1 319 LYS n 
1 320 GLU n 
1 321 ASP n 
1 322 ASN n 
1 323 GLU n 
1 324 ASP n 
1 325 SER n 
1 326 GLU n 
1 327 SER n 
1 328 LYS n 
1 329 ILE n 
1 330 GLU n 
1 331 ILE n 
1 332 LYS n 
1 333 SER n 
1 334 VAL n 
1 335 LEU n 
1 336 ALA n 
1 337 LYS n 
1 338 LEU n 
1 339 VAL n 
1 340 GLU n 
1 341 TYR n 
1 342 MET n 
1 343 SER n 
1 344 ALA n 
1 345 GLU n 
1 346 LYS n 
1 347 SER n 
1 348 PHE n 
1 349 ILE n 
1 350 ASP n 
1 351 GLY n 
1 352 LEU n 
1 353 ILE n 
1 354 ASN n 
1 355 LYS n 
1 356 GLN n 
1 357 PRO n 
1 358 ASN n 
1 359 ILE n 
1 360 LEU n 
1 361 ASN n 
1 362 LEU n 
1 363 VAL n 
1 364 ASN n 
1 365 ALA n 
1 366 GLN n 
1 367 GLY n 
1 368 ALA n 
1 369 ALA n 
1 370 ILE n 
1 371 CYS n 
1 372 PHE n 
1 373 ASN n 
1 374 LYS n 
1 375 GLU n 
1 376 LEU n 
1 377 TYR n 
1 378 LEU n 
1 379 LEU n 
1 380 GLY n 
1 381 ASN n 
1 382 THR n 
1 383 PRO n 
1 384 GLU n 
1 385 LYS n 
1 386 GLN n 
1 387 ASP n 
1 388 ILE n 
1 389 GLN n 
1 390 ASN n 
1 391 LEU n 
1 392 LEU n 
1 393 LEU n 
1 394 TRP n 
1 395 ILE n 
1 396 HIS n 
1 397 ASN n 
1 398 ASN n 
1 399 ILE n 
1 400 ASP n 
1 401 GLU n 
1 402 ASP n 
1 403 ILE n 
1 404 PHE n 
1 405 TYR n 
1 406 THR n 
1 407 ASP n 
1 408 SER n 
1 409 LEU n 
1 410 SER n 
1 411 GLN n 
1 412 VAL n 
1 413 TYR n 
1 414 PRO n 
1 415 GLU n 
1 416 ALA n 
1 417 GLU n 
1 418 LYS n 
1 419 PHE n 
1 420 LYS n 
1 421 ASP n 
1 422 VAL n 
1 423 ALA n 
1 424 SER n 
1 425 GLY n 
1 426 LEU n 
1 427 ILE n 
1 428 ALA n 
1 429 LEU n 
1 430 SER n 
1 431 ILE n 
1 432 SER n 
1 433 LYS n 
1 434 THR n 
1 435 GLN n 
1 436 ASN n 
1 437 LYS n 
1 438 TYR n 
1 439 VAL n 
1 440 LEU n 
1 441 TRP n 
1 442 PHE n 
1 443 ARG n 
1 444 PRO n 
1 445 GLU n 
1 446 GLU n 
1 447 VAL n 
1 448 GLN n 
1 449 THR n 
1 450 VAL n 
1 451 ASN n 
1 452 TRP n 
1 453 GLY n 
1 454 GLY n 
1 455 ASN n 
1 456 PRO n 
1 457 ASN n 
1 458 GLN n 
1 459 PRO n 
1 460 VAL n 
1 461 GLU n 
1 462 VAL n 
1 463 SER n 
1 464 GLU n 
1 465 ASN n 
1 466 GLY n 
1 467 GLY n 
1 468 LEU n 
1 469 HIS n 
1 470 LEU n 
1 471 SER n 
1 472 PRO n 
1 473 ARG n 
1 474 LYS n 
1 475 SER n 
1 476 PHE n 
1 477 GLU n 
1 478 LEU n 
1 479 TRP n 
1 480 LYS n 
1 481 GLU n 
1 482 ILE n 
1 483 VAL n 
1 484 ARG n 
1 485 LEU n 
1 486 LYS n 
1 487 SER n 
1 488 LEU n 
1 489 PRO n 
1 490 TRP n 
1 491 LYS n 
1 492 SER n 
1 493 TYR n 
1 494 GLU n 
1 495 VAL n 
1 496 ASN n 
1 497 ALA n 
1 498 ALA n 
1 499 ALA n 
1 500 GLU n 
1 501 LEU n 
1 502 ARG n 
1 503 GLY n 
1 504 ALA n 
1 505 ILE n 
1 506 ILE n 
1 507 THR n 
1 508 VAL n 
1 509 VAL n 
1 510 LEU n 
1 511 ARG n 
1 512 LYS n 
1 513 ILE n 
1 514 ASP n 
1 515 GLU n 
1 516 HIS n 
1 517 HIS n 
1 518 HIS n 
1 519 HIS n 
1 520 HIS n 
1 521 HIS n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   521 
_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      'Fischerella sp. PCC 9605' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     1173024 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_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                   ? 
# 
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 
BLR non-polymer         . 
;3-[5-[(Z)-(4-ethenyl-3-methyl-5-oxidanylidene-pyrrol-2-ylidene)methyl]-2-[[5-[(Z)-(3-ethenyl-4-methyl-5-oxidanylidene-pyrrol-2-ylidene)methyl]-3-(3-hydroxy-3-oxopropyl)-4-methyl-1H-pyrrol-2-yl]methyl]-4-methyl-1H-pyrrol-3-yl]propanoic acid
;
'Bilirubin IX alpha' 'C33 H36 N4 O6'  584.662 
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 
ILE 'L-peptide linking' y ISOLEUCINE ?                    'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE ?                    'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE ?                    'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE ?                    'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking' y PHENYLALANINE ?                    'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE ?                    'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE ?                    'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE ?                    'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN ?                    'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE ?                    'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE ?                    'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   ?   ?   ?   A . n 
A 1 2   ASN 2   2   ?   ?   ?   A . n 
A 1 3   THR 3   3   ?   ?   ?   A . n 
A 1 4   ASN 4   4   ?   ?   ?   A . n 
A 1 5   LYS 5   5   ?   ?   ?   A . n 
A 1 6   ASN 6   6   ?   ?   ?   A . n 
A 1 7   ASP 7   7   ?   ?   ?   A . n 
A 1 8   THR 8   8   ?   ?   ?   A . n 
A 1 9   ALA 9   9   ?   ?   ?   A . n 
A 1 10  PHE 10  10  ?   ?   ?   A . n 
A 1 11  THR 11  11  ?   ?   ?   A . n 
A 1 12  VAL 12  12  ?   ?   ?   A . n 
A 1 13  ASP 13  13  ?   ?   ?   A . n 
A 1 14  LEU 14  14  ?   ?   ?   A . n 
A 1 15  THR 15  15  ?   ?   ?   A . n 
A 1 16  ASN 16  16  ?   ?   ?   A . n 
A 1 17  CYS 17  17  17  CYS CYS A . n 
A 1 18  ASP 18  18  18  ASP ASP A . n 
A 1 19  LYS 19  19  19  LYS LYS A . n 
A 1 20  GLU 20  20  20  GLU GLU A . n 
A 1 21  PRO 21  21  21  PRO PRO A . n 
A 1 22  ILE 22  22  22  ILE ILE A . n 
A 1 23  HIS 23  23  23  HIS HIS A . n 
A 1 24  ILE 24  24  24  ILE ILE A . n 
A 1 25  PRO 25  25  25  PRO PRO A . n 
A 1 26  GLY 26  26  26  GLY GLY A . n 
A 1 27  PHE 27  27  27  PHE PHE A . n 
A 1 28  VAL 28  28  28  VAL VAL A . n 
A 1 29  GLN 29  29  29  GLN GLN A . n 
A 1 30  PRO 30  30  30  PRO PRO A . n 
A 1 31  HIS 31  31  31  HIS HIS A . n 
A 1 32  GLY 32  32  32  GLY GLY A . n 
A 1 33  VAL 33  33  33  VAL VAL A . n 
A 1 34  LEU 34  34  34  LEU LEU A . n 
A 1 35  LEU 35  35  35  LEU LEU A . n 
A 1 36  ALA 36  36  36  ALA ALA A . n 
A 1 37  ILE 37  37  37  ILE ILE A . n 
A 1 38  LYS 38  38  38  LYS LYS A . n 
A 1 39  GLU 39  39  39  GLU GLU A . n 
A 1 40  PRO 40  40  40  PRO PRO A . n 
A 1 41  GLU 41  41  41  GLU GLU A . n 
A 1 42  LEU 42  42  42  LEU LEU A . n 
A 1 43  THR 43  43  43  THR THR A . n 
A 1 44  ILE 44  44  44  ILE ILE A . n 
A 1 45  LEU 45  45  45  LEU LEU A . n 
A 1 46  GLN 46  46  46  GLN GLN A . n 
A 1 47  VAL 47  47  47  VAL VAL A . n 
A 1 48  SER 48  48  48  SER SER A . n 
A 1 49  ASN 49  49  49  ASN ASN A . n 
A 1 50  ASN 50  50  50  ASN ASN A . n 
A 1 51  THR 51  51  51  THR THR A . n 
A 1 52  TYR 52  52  52  TYR TYR A . n 
A 1 53  ASN 53  53  53  ASN ASN A . n 
A 1 54  CYS 54  54  54  CYS CYS A . n 
A 1 55  LEU 55  55  55  LEU LEU A . n 
A 1 56  GLY 56  56  56  GLY GLY A . n 
A 1 57  PHE 57  57  57  PHE PHE A . n 
A 1 58  HIS 58  58  58  HIS HIS A . n 
A 1 59  PRO 59  59  59  PRO PRO A . n 
A 1 60  GLU 60  60  60  GLU GLU A . n 
A 1 61  GLU 61  61  61  GLU GLU A . n 
A 1 62  LEU 62  62  62  LEU LEU A . n 
A 1 63  LEU 63  63  63  LEU LEU A . n 
A 1 64  ASN 64  64  64  ASN ASN A . n 
A 1 65  GLN 65  65  65  GLN GLN A . n 
A 1 66  PRO 66  66  66  PRO PRO A . n 
A 1 67  LEU 67  67  67  LEU LEU A . n 
A 1 68  ARG 68  68  68  ARG ARG A . n 
A 1 69  LYS 69  69  69  LYS LYS A . n 
A 1 70  LEU 70  70  70  LEU LEU A . n 
A 1 71  LEU 71  71  71  LEU LEU A . n 
A 1 72  GLU 72  72  72  GLU GLU A . n 
A 1 73  SER 73  73  73  SER SER A . n 
A 1 74  GLU 74  74  74  GLU GLU A . n 
A 1 75  GLN 75  75  75  GLN GLN A . n 
A 1 76  ILE 76  76  76  ILE ILE A . n 
A 1 77  ASP 77  77  77  ASP ASP A . n 
A 1 78  PHE 78  78  78  PHE PHE A . n 
A 1 79  LEU 79  79  79  LEU LEU A . n 
A 1 80  ASN 80  80  80  ASN ASN A . n 
A 1 81  ASP 81  81  81  ASP ASP A . n 
A 1 82  CYS 82  82  82  CYS CYS A . n 
A 1 83  LEU 83  83  83  LEU LEU A . n 
A 1 84  THR 84  84  84  THR THR A . n 
A 1 85  GLN 85  85  85  GLN GLN A . n 
A 1 86  GLU 86  86  86  GLU GLU A . n 
A 1 87  ASP 87  87  87  ASP ASP A . n 
A 1 88  ILE 88  88  88  ILE ILE A . n 
A 1 89  GLN 89  89  89  GLN GLN A . n 
A 1 90  ILE 90  90  90  ILE ILE A . n 
A 1 91  VAL 91  91  91  VAL VAL A . n 
A 1 92  ASN 92  92  92  ASN ASN A . n 
A 1 93  PRO 93  93  93  PRO PRO A . n 
A 1 94  VAL 94  94  94  VAL VAL A . n 
A 1 95  GLU 95  95  95  GLU GLU A . n 
A 1 96  PHE 96  96  96  PHE PHE A . n 
A 1 97  THR 97  97  97  THR THR A . n 
A 1 98  ILE 98  98  98  ILE ILE A . n 
A 1 99  LYS 99  99  ?   ?   ?   A . n 
A 1 100 THR 100 100 ?   ?   ?   A . n 
A 1 101 PHE 101 101 ?   ?   ?   A . n 
A 1 102 GLN 102 102 ?   ?   ?   A . n 
A 1 103 GLU 103 103 103 GLU GLU A . n 
A 1 104 PRO 104 104 104 PRO PRO A . n 
A 1 105 ILE 105 105 105 ILE ILE A . n 
A 1 106 ILE 106 106 106 ILE ILE A . n 
A 1 107 PHE 107 107 107 PHE PHE A . n 
A 1 108 ASP 108 108 108 ASP ASP A . n 
A 1 109 GLY 109 109 109 GLY GLY A . n 
A 1 110 ILE 110 110 110 ILE ILE A . n 
A 1 111 ILE 111 111 111 ILE ILE A . n 
A 1 112 HIS 112 112 112 HIS HIS A . n 
A 1 113 ARG 113 113 113 ARG ARG A . n 
A 1 114 SER 114 114 114 SER SER A . n 
A 1 115 ASN 115 115 115 ASN ASN A . n 
A 1 116 GLY 116 116 116 GLY GLY A . n 
A 1 117 VAL 117 117 117 VAL VAL A . n 
A 1 118 VAL 118 118 118 VAL VAL A . n 
A 1 119 ILE 119 119 119 ILE ILE A . n 
A 1 120 LEU 120 120 120 LEU LEU A . n 
A 1 121 GLU 121 121 121 GLU GLU A . n 
A 1 122 LEU 122 122 122 LEU LEU A . n 
A 1 123 GLU 123 123 123 GLU GLU A . n 
A 1 124 PRO 124 124 124 PRO PRO A . n 
A 1 125 ALA 125 125 125 ALA ALA A . n 
A 1 126 ILE 126 126 126 ILE ILE A . n 
A 1 127 LEU 127 127 127 LEU LEU A . n 
A 1 128 GLU 128 128 ?   ?   ?   A . n 
A 1 129 LYS 129 129 ?   ?   ?   A . n 
A 1 130 ASN 130 130 ?   ?   ?   A . n 
A 1 131 ASN 131 131 ?   ?   ?   A . n 
A 1 132 ASN 132 132 ?   ?   ?   A . n 
A 1 133 TYR 133 133 ?   ?   ?   A . n 
A 1 134 PHE 134 134 ?   ?   ?   A . n 
A 1 135 ARG 135 135 ?   ?   ?   A . n 
A 1 136 PHE 136 136 136 PHE PHE A . n 
A 1 137 TYR 137 137 137 TYR TYR A . n 
A 1 138 HIS 138 138 138 HIS HIS A . n 
A 1 139 LEU 139 139 139 LEU LEU A . n 
A 1 140 VAL 140 140 140 VAL VAL A . n 
A 1 141 LYS 141 141 141 LYS LYS A . n 
A 1 142 LEU 142 142 142 LEU LEU A . n 
A 1 143 ALA 143 143 143 ALA ALA A . n 
A 1 144 ILE 144 144 144 ILE ILE A . n 
A 1 145 GLY 145 145 145 GLY GLY A . n 
A 1 146 LYS 146 146 146 LYS LYS A . n 
A 1 147 LEU 147 147 147 LEU LEU A . n 
A 1 148 GLN 148 148 148 GLN GLN A . n 
A 1 149 SER 149 149 149 SER SER A . n 
A 1 150 THR 150 150 150 THR THR A . n 
A 1 151 LYS 151 151 151 LYS LYS A . n 
A 1 152 THR 152 152 152 THR THR A . n 
A 1 153 VAL 153 153 153 VAL VAL A . n 
A 1 154 THR 154 154 154 THR THR A . n 
A 1 155 GLU 155 155 155 GLU GLU A . n 
A 1 156 ILE 156 156 156 ILE ILE A . n 
A 1 157 SER 157 157 157 SER SER A . n 
A 1 158 GLN 158 158 158 GLN GLN A . n 
A 1 159 ILE 159 159 159 ILE ILE A . n 
A 1 160 ILE 160 160 160 ILE ILE A . n 
A 1 161 VAL 161 161 161 VAL VAL 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 VAL 164 164 164 VAL VAL A . n 
A 1 165 ARG 165 165 165 ARG ARG A . n 
A 1 166 ARG 166 166 166 ARG ARG A . n 
A 1 167 ILE 167 167 167 ILE ILE A . n 
A 1 168 THR 168 168 168 THR THR A . n 
A 1 169 GLY 169 169 169 GLY GLY A . n 
A 1 170 PHE 170 170 170 PHE PHE A . n 
A 1 171 ASP 171 171 171 ASP ASP A . n 
A 1 172 ARG 172 172 172 ARG ARG A . n 
A 1 173 VAL 173 173 173 VAL VAL A . n 
A 1 174 MET 174 174 174 MET MET A . n 
A 1 175 PHE 175 175 175 PHE PHE A . n 
A 1 176 TYR 176 176 176 TYR TYR A . n 
A 1 177 ARG 177 177 177 ARG ARG A . n 
A 1 178 PHE 178 178 178 PHE PHE A . n 
A 1 179 ASP 179 179 179 ASP ASP A . n 
A 1 180 ARG 180 180 180 ARG ARG A . n 
A 1 181 ASP 181 181 181 ASP ASP A . n 
A 1 182 TRP 182 182 182 TRP TRP A . n 
A 1 183 ASN 183 183 183 ASN ASN A . n 
A 1 184 GLY 184 184 184 GLY GLY A . n 
A 1 185 ILE 185 185 185 ILE ILE A . n 
A 1 186 VAL 186 186 186 VAL VAL A . n 
A 1 187 ILE 187 187 187 ILE ILE A . n 
A 1 188 ALA 188 188 188 ALA ALA A . n 
A 1 189 GLU 189 189 189 GLU GLU A . n 
A 1 190 ASP 190 190 190 ASP ASP A . n 
A 1 191 LYS 191 191 191 LYS LYS A . n 
A 1 192 GLN 192 192 192 GLN GLN A . n 
A 1 193 GLU 193 193 193 GLU GLU A . n 
A 1 194 HIS 194 194 194 HIS HIS A . n 
A 1 195 LEU 195 195 195 LEU LEU A . n 
A 1 196 PRO 196 196 196 PRO PRO A . n 
A 1 197 SER 197 197 197 SER SER A . n 
A 1 198 TYR 198 198 198 TYR TYR A . n 
A 1 199 LEU 199 199 199 LEU LEU A . n 
A 1 200 ASP 200 200 200 ASP ASP A . n 
A 1 201 LEU 201 201 201 LEU LEU A . n 
A 1 202 HIS 202 202 202 HIS HIS A . n 
A 1 203 TYR 203 203 203 TYR TYR A . n 
A 1 204 PRO 204 204 204 PRO PRO A . n 
A 1 205 ALA 205 205 205 ALA ALA A . n 
A 1 206 SER 206 206 206 SER SER A . n 
A 1 207 ASP 207 207 207 ASP ASP A . n 
A 1 208 ILE 208 208 208 ILE ILE A . n 
A 1 209 PRO 209 209 209 PRO PRO A . n 
A 1 210 THR 210 210 210 THR THR A . n 
A 1 211 PRO 211 211 211 PRO PRO A . n 
A 1 212 ALA 212 212 212 ALA ALA A . n 
A 1 213 ARG 213 213 213 ARG ARG A . n 
A 1 214 LYS 214 214 214 LYS LYS A . n 
A 1 215 LEU 215 215 215 LEU LEU A . n 
A 1 216 TYR 216 216 216 TYR TYR A . n 
A 1 217 SER 217 217 217 SER SER A . n 
A 1 218 GLN 218 218 218 GLN GLN A . n 
A 1 219 ASN 219 219 219 ASN ASN A . n 
A 1 220 TRP 220 220 220 TRP TRP A . n 
A 1 221 LEU 221 221 221 LEU LEU A . n 
A 1 222 ARG 222 222 222 ARG ARG A . n 
A 1 223 LEU 223 223 223 LEU LEU A . n 
A 1 224 ILE 224 224 224 ILE ILE A . n 
A 1 225 PRO 225 225 225 PRO PRO A . n 
A 1 226 ASP 226 226 226 ASP ASP A . n 
A 1 227 ALA 227 227 227 ALA ALA A . n 
A 1 228 ASP 228 228 228 ASP ASP A . n 
A 1 229 TYR 229 229 229 TYR TYR A . n 
A 1 230 GLN 230 230 230 GLN GLN A . n 
A 1 231 ALA 231 231 231 ALA ALA A . n 
A 1 232 ALA 232 232 232 ALA ALA A . n 
A 1 233 ALA 233 233 233 ALA ALA A . n 
A 1 234 ILE 234 234 234 ILE ILE A . n 
A 1 235 VAL 235 235 235 VAL VAL A . n 
A 1 236 PRO 236 236 236 PRO PRO 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 PRO 240 240 240 PRO PRO A . n 
A 1 241 LEU 241 241 241 LEU LEU A . n 
A 1 242 THR 242 242 242 THR THR A . n 
A 1 243 ASP 243 243 243 ASP ASP A . n 
A 1 244 GLU 244 244 244 GLU GLU A . n 
A 1 245 PRO 245 245 245 PRO PRO A . n 
A 1 246 LEU 246 246 246 LEU LEU A . n 
A 1 247 ASP 247 247 247 ASP ASP A . n 
A 1 248 LEU 248 248 248 LEU LEU A . n 
A 1 249 SER 249 249 249 SER SER A . n 
A 1 250 GLY 250 250 250 GLY GLY A . n 
A 1 251 SER 251 251 251 SER SER A . n 
A 1 252 VAL 252 252 252 VAL VAL A . n 
A 1 253 LEU 253 253 253 LEU LEU A . n 
A 1 254 ARG 254 254 254 ARG ARG A . n 
A 1 255 SER 255 255 255 SER SER A . n 
A 1 256 VAL 256 256 256 VAL VAL A . n 
A 1 257 SER 257 257 257 SER SER A . n 
A 1 258 PRO 258 258 258 PRO PRO A . n 
A 1 259 CYS 259 259 259 CYS CYS A . n 
A 1 260 HIS 260 260 260 HIS HIS A . n 
A 1 261 ILE 261 261 261 ILE ILE A . n 
A 1 262 GLU 262 262 262 GLU GLU A . n 
A 1 263 TYR 263 263 263 TYR TYR A . n 
A 1 264 LEU 264 264 264 LEU LEU A . n 
A 1 265 HIS 265 265 265 HIS HIS A . n 
A 1 266 ASN 266 266 266 ASN ASN A . n 
A 1 267 MET 267 267 267 MET MET A . n 
A 1 268 GLY 268 268 268 GLY GLY A . n 
A 1 269 VAL 269 269 269 VAL VAL A . n 
A 1 270 LYS 270 270 270 LYS LYS A . n 
A 1 271 ALA 271 271 271 ALA ALA A . n 
A 1 272 SER 272 272 272 SER SER A . n 
A 1 273 MET 273 273 273 MET MET A . n 
A 1 274 SER 274 274 274 SER SER A . n 
A 1 275 ILE 275 275 275 ILE ILE A . n 
A 1 276 SER 276 276 276 SER SER A . n 
A 1 277 ILE 277 277 277 ILE ILE A . n 
A 1 278 ILE 278 278 278 ILE ILE A . n 
A 1 279 LYS 279 279 279 LYS LYS A . n 
A 1 280 ASN 280 280 280 ASN ASN A . n 
A 1 281 ASN 281 281 281 ASN ASN A . n 
A 1 282 LYS 282 282 282 LYS LYS A . n 
A 1 283 LEU 283 283 283 LEU LEU A . n 
A 1 284 TRP 284 284 284 TRP TRP A . n 
A 1 285 GLY 285 285 285 GLY GLY A . n 
A 1 286 LEU 286 286 286 LEU LEU A . n 
A 1 287 ILE 287 287 287 ILE ILE A . n 
A 1 288 ALA 288 288 288 ALA ALA A . n 
A 1 289 CYS 289 289 289 CYS CYS A . n 
A 1 290 HIS 290 290 290 HIS HIS A . n 
A 1 291 HIS 291 291 291 HIS HIS A . n 
A 1 292 GLN 292 292 292 GLN GLN A . n 
A 1 293 THR 293 293 293 THR THR A . n 
A 1 294 PRO 294 294 294 PRO PRO A . n 
A 1 295 LYS 295 295 295 LYS LYS A . n 
A 1 296 TYR 296 296 296 TYR TYR A . n 
A 1 297 VAL 297 297 297 VAL VAL A . n 
A 1 298 PRO 298 298 298 PRO PRO A . n 
A 1 299 TYR 299 299 299 TYR TYR A . n 
A 1 300 GLU 300 300 300 GLU GLU A . n 
A 1 301 ILE 301 301 301 ILE ILE A . n 
A 1 302 ARG 302 302 302 ARG ARG A . n 
A 1 303 HIS 303 303 303 HIS HIS A . n 
A 1 304 ALA 304 304 304 ALA ALA A . n 
A 1 305 CYS 305 305 305 CYS CYS A . n 
A 1 306 GLU 306 306 306 GLU GLU A . n 
A 1 307 PHE 307 307 307 PHE PHE A . n 
A 1 308 LEU 308 308 308 LEU LEU A . n 
A 1 309 GLY 309 309 309 GLY GLY A . n 
A 1 310 GLN 310 310 310 GLN GLN A . n 
A 1 311 VAL 311 311 311 VAL VAL A . n 
A 1 312 THR 312 312 312 THR THR A . n 
A 1 313 SER 313 313 313 SER SER A . n 
A 1 314 LEU 314 314 314 LEU LEU A . n 
A 1 315 GLU 315 315 315 GLU GLU A . n 
A 1 316 ILE 316 316 316 ILE ILE A . n 
A 1 317 ALA 317 317 317 ALA ALA A . n 
A 1 318 THR 318 318 318 THR THR A . n 
A 1 319 LYS 319 319 319 LYS LYS A . n 
A 1 320 GLU 320 320 320 GLU GLU A . n 
A 1 321 ASP 321 321 321 ASP ASP A . n 
A 1 322 ASN 322 322 322 ASN ASN A . n 
A 1 323 GLU 323 323 323 GLU GLU A . n 
A 1 324 ASP 324 324 324 ASP ASP A . n 
A 1 325 SER 325 325 325 SER SER A . n 
A 1 326 GLU 326 326 326 GLU GLU A . n 
A 1 327 SER 327 327 327 SER SER A . n 
A 1 328 LYS 328 328 328 LYS LYS A . n 
A 1 329 ILE 329 329 329 ILE ILE A . n 
A 1 330 GLU 330 330 330 GLU GLU A . n 
A 1 331 ILE 331 331 331 ILE ILE A . n 
A 1 332 LYS 332 332 332 LYS LYS A . n 
A 1 333 SER 333 333 333 SER SER A . n 
A 1 334 VAL 334 334 334 VAL VAL A . n 
A 1 335 LEU 335 335 335 LEU LEU A . n 
A 1 336 ALA 336 336 336 ALA ALA A . n 
A 1 337 LYS 337 337 337 LYS LYS A . n 
A 1 338 LEU 338 338 338 LEU LEU A . n 
A 1 339 VAL 339 339 339 VAL VAL A . n 
A 1 340 GLU 340 340 340 GLU GLU A . n 
A 1 341 TYR 341 341 341 TYR TYR A . n 
A 1 342 MET 342 342 342 MET MET A . n 
A 1 343 SER 343 343 ?   ?   ?   A . n 
A 1 344 ALA 344 344 ?   ?   ?   A . n 
A 1 345 GLU 345 345 ?   ?   ?   A . n 
A 1 346 LYS 346 346 ?   ?   ?   A . n 
A 1 347 SER 347 347 ?   ?   ?   A . n 
A 1 348 PHE 348 348 ?   ?   ?   A . n 
A 1 349 ILE 349 349 349 ILE ILE A . n 
A 1 350 ASP 350 350 350 ASP ASP A . n 
A 1 351 GLY 351 351 351 GLY GLY A . n 
A 1 352 LEU 352 352 352 LEU LEU A . n 
A 1 353 ILE 353 353 353 ILE ILE A . n 
A 1 354 ASN 354 354 354 ASN ASN A . n 
A 1 355 LYS 355 355 355 LYS LYS A . n 
A 1 356 GLN 356 356 356 GLN GLN A . n 
A 1 357 PRO 357 357 357 PRO PRO A . n 
A 1 358 ASN 358 358 358 ASN ASN A . n 
A 1 359 ILE 359 359 359 ILE ILE A . n 
A 1 360 LEU 360 360 360 LEU LEU A . n 
A 1 361 ASN 361 361 361 ASN ASN A . n 
A 1 362 LEU 362 362 362 LEU LEU A . n 
A 1 363 VAL 363 363 363 VAL VAL A . n 
A 1 364 ASN 364 364 364 ASN ASN A . n 
A 1 365 ALA 365 365 365 ALA ALA A . n 
A 1 366 GLN 366 366 366 GLN GLN A . n 
A 1 367 GLY 367 367 367 GLY GLY A . n 
A 1 368 ALA 368 368 368 ALA ALA A . n 
A 1 369 ALA 369 369 369 ALA ALA A . n 
A 1 370 ILE 370 370 370 ILE ILE A . n 
A 1 371 CYS 371 371 371 CYS CYS A . n 
A 1 372 PHE 372 372 372 PHE PHE A . n 
A 1 373 ASN 373 373 373 ASN ASN A . n 
A 1 374 LYS 374 374 374 LYS LYS A . n 
A 1 375 GLU 375 375 375 GLU GLU A . n 
A 1 376 LEU 376 376 376 LEU LEU A . n 
A 1 377 TYR 377 377 377 TYR TYR A . n 
A 1 378 LEU 378 378 378 LEU LEU A . n 
A 1 379 LEU 379 379 379 LEU LEU A . n 
A 1 380 GLY 380 380 380 GLY GLY A . n 
A 1 381 ASN 381 381 381 ASN ASN A . n 
A 1 382 THR 382 382 382 THR THR A . n 
A 1 383 PRO 383 383 383 PRO PRO A . n 
A 1 384 GLU 384 384 384 GLU GLU A . n 
A 1 385 LYS 385 385 385 LYS LYS A . n 
A 1 386 GLN 386 386 386 GLN GLN A . n 
A 1 387 ASP 387 387 387 ASP ASP A . n 
A 1 388 ILE 388 388 388 ILE ILE A . n 
A 1 389 GLN 389 389 389 GLN GLN A . n 
A 1 390 ASN 390 390 390 ASN ASN A . n 
A 1 391 LEU 391 391 391 LEU LEU A . n 
A 1 392 LEU 392 392 392 LEU LEU A . n 
A 1 393 LEU 393 393 393 LEU LEU A . n 
A 1 394 TRP 394 394 394 TRP TRP A . n 
A 1 395 ILE 395 395 395 ILE ILE A . n 
A 1 396 HIS 396 396 396 HIS HIS A . n 
A 1 397 ASN 397 397 397 ASN ASN A . n 
A 1 398 ASN 398 398 398 ASN ASN A . n 
A 1 399 ILE 399 399 399 ILE ILE A . n 
A 1 400 ASP 400 400 400 ASP ASP A . n 
A 1 401 GLU 401 401 401 GLU GLU A . n 
A 1 402 ASP 402 402 402 ASP ASP A . n 
A 1 403 ILE 403 403 403 ILE ILE A . n 
A 1 404 PHE 404 404 404 PHE PHE A . n 
A 1 405 TYR 405 405 405 TYR TYR A . n 
A 1 406 THR 406 406 406 THR THR A . n 
A 1 407 ASP 407 407 407 ASP ASP A . n 
A 1 408 SER 408 408 408 SER SER A . n 
A 1 409 LEU 409 409 409 LEU LEU A . n 
A 1 410 SER 410 410 410 SER SER A . n 
A 1 411 GLN 411 411 411 GLN GLN A . n 
A 1 412 VAL 412 412 412 VAL VAL A . n 
A 1 413 TYR 413 413 413 TYR TYR A . n 
A 1 414 PRO 414 414 414 PRO PRO A . n 
A 1 415 GLU 415 415 415 GLU GLU A . n 
A 1 416 ALA 416 416 416 ALA ALA A . n 
A 1 417 GLU 417 417 417 GLU GLU A . n 
A 1 418 LYS 418 418 418 LYS LYS A . n 
A 1 419 PHE 419 419 419 PHE PHE A . n 
A 1 420 LYS 420 420 420 LYS LYS A . n 
A 1 421 ASP 421 421 421 ASP ASP A . n 
A 1 422 VAL 422 422 422 VAL VAL A . n 
A 1 423 ALA 423 423 423 ALA ALA A . n 
A 1 424 SER 424 424 424 SER SER A . n 
A 1 425 GLY 425 425 425 GLY GLY A . n 
A 1 426 LEU 426 426 426 LEU LEU A . n 
A 1 427 ILE 427 427 427 ILE ILE A . n 
A 1 428 ALA 428 428 428 ALA ALA A . n 
A 1 429 LEU 429 429 429 LEU LEU A . n 
A 1 430 SER 430 430 430 SER SER A . n 
A 1 431 ILE 431 431 431 ILE ILE A . n 
A 1 432 SER 432 432 432 SER SER A . n 
A 1 433 LYS 433 433 433 LYS LYS A . n 
A 1 434 THR 434 434 434 THR THR A . n 
A 1 435 GLN 435 435 435 GLN GLN A . n 
A 1 436 ASN 436 436 436 ASN ASN A . n 
A 1 437 LYS 437 437 437 LYS LYS A . n 
A 1 438 TYR 438 438 438 TYR TYR A . n 
A 1 439 VAL 439 439 439 VAL VAL A . n 
A 1 440 LEU 440 440 440 LEU LEU A . n 
A 1 441 TRP 441 441 441 TRP TRP A . n 
A 1 442 PHE 442 442 442 PHE PHE A . n 
A 1 443 ARG 443 443 443 ARG ARG A . n 
A 1 444 PRO 444 444 444 PRO PRO A . n 
A 1 445 GLU 445 445 445 GLU GLU A . n 
A 1 446 GLU 446 446 446 GLU GLU A . n 
A 1 447 VAL 447 447 447 VAL VAL A . n 
A 1 448 GLN 448 448 448 GLN GLN A . n 
A 1 449 THR 449 449 449 THR THR A . n 
A 1 450 VAL 450 450 450 VAL VAL A . n 
A 1 451 ASN 451 451 451 ASN ASN A . n 
A 1 452 TRP 452 452 452 TRP TRP A . n 
A 1 453 GLY 453 453 453 GLY GLY A . n 
A 1 454 GLY 454 454 454 GLY GLY A . n 
A 1 455 ASN 455 455 455 ASN ASN A . n 
A 1 456 PRO 456 456 456 PRO PRO A . n 
A 1 457 ASN 457 457 ?   ?   ?   A . n 
A 1 458 GLN 458 458 ?   ?   ?   A . n 
A 1 459 PRO 459 459 ?   ?   ?   A . n 
A 1 460 VAL 460 460 ?   ?   ?   A . n 
A 1 461 GLU 461 461 ?   ?   ?   A . n 
A 1 462 VAL 462 462 ?   ?   ?   A . n 
A 1 463 SER 463 463 ?   ?   ?   A . n 
A 1 464 GLU 464 464 ?   ?   ?   A . n 
A 1 465 ASN 465 465 ?   ?   ?   A . n 
A 1 466 GLY 466 466 ?   ?   ?   A . n 
A 1 467 GLY 467 467 ?   ?   ?   A . n 
A 1 468 LEU 468 468 ?   ?   ?   A . n 
A 1 469 HIS 469 469 ?   ?   ?   A . n 
A 1 470 LEU 470 470 ?   ?   ?   A . n 
A 1 471 SER 471 471 ?   ?   ?   A . n 
A 1 472 PRO 472 472 ?   ?   ?   A . n 
A 1 473 ARG 473 473 ?   ?   ?   A . n 
A 1 474 LYS 474 474 ?   ?   ?   A . n 
A 1 475 SER 475 475 ?   ?   ?   A . n 
A 1 476 PHE 476 476 ?   ?   ?   A . n 
A 1 477 GLU 477 477 477 GLU GLU A . n 
A 1 478 LEU 478 478 478 LEU LEU A . n 
A 1 479 TRP 479 479 479 TRP TRP A . n 
A 1 480 LYS 480 480 480 LYS LYS A . n 
A 1 481 GLU 481 481 481 GLU GLU A . n 
A 1 482 ILE 482 482 482 ILE ILE A . n 
A 1 483 VAL 483 483 483 VAL VAL A . n 
A 1 484 ARG 484 484 484 ARG ARG A . n 
A 1 485 LEU 485 485 485 LEU LEU A . n 
A 1 486 LYS 486 486 486 LYS LYS A . n 
A 1 487 SER 487 487 487 SER SER A . n 
A 1 488 LEU 488 488 488 LEU LEU A . n 
A 1 489 PRO 489 489 489 PRO PRO A . n 
A 1 490 TRP 490 490 490 TRP TRP A . n 
A 1 491 LYS 491 491 491 LYS LYS A . n 
A 1 492 SER 492 492 492 SER SER A . n 
A 1 493 TYR 493 493 493 TYR TYR A . n 
A 1 494 GLU 494 494 494 GLU GLU A . n 
A 1 495 VAL 495 495 495 VAL VAL A . n 
A 1 496 ASN 496 496 496 ASN ASN A . n 
A 1 497 ALA 497 497 497 ALA ALA A . n 
A 1 498 ALA 498 498 498 ALA ALA A . n 
A 1 499 ALA 499 499 499 ALA ALA A . n 
A 1 500 GLU 500 500 500 GLU GLU A . n 
A 1 501 LEU 501 501 501 LEU LEU A . n 
A 1 502 ARG 502 502 502 ARG ARG A . n 
A 1 503 GLY 503 503 503 GLY GLY A . n 
A 1 504 ALA 504 504 504 ALA ALA A . n 
A 1 505 ILE 505 505 505 ILE ILE A . n 
A 1 506 ILE 506 506 506 ILE ILE A . n 
A 1 507 THR 507 507 507 THR THR A . n 
A 1 508 VAL 508 508 508 VAL VAL A . n 
A 1 509 VAL 509 509 509 VAL VAL A . n 
A 1 510 LEU 510 510 ?   ?   ?   A . n 
A 1 511 ARG 511 511 ?   ?   ?   A . n 
A 1 512 LYS 512 512 ?   ?   ?   A . n 
A 1 513 ILE 513 513 ?   ?   ?   A . n 
A 1 514 ASP 514 514 ?   ?   ?   A . n 
A 1 515 GLU 515 515 ?   ?   ?   A . n 
A 1 516 HIS 516 516 ?   ?   ?   A . n 
A 1 517 HIS 517 517 ?   ?   ?   A . n 
A 1 518 HIS 518 518 ?   ?   ?   A . n 
A 1 519 HIS 519 519 ?   ?   ?   A . n 
A 1 520 HIS 520 520 ?   ?   ?   A . n 
A 1 521 HIS 521 521 ?   ?   ?   A . n 
B 1 1   MET 1   1   ?   ?   ?   B . n 
B 1 2   ASN 2   2   ?   ?   ?   B . n 
B 1 3   THR 3   3   ?   ?   ?   B . n 
B 1 4   ASN 4   4   ?   ?   ?   B . n 
B 1 5   LYS 5   5   ?   ?   ?   B . n 
B 1 6   ASN 6   6   ?   ?   ?   B . n 
B 1 7   ASP 7   7   ?   ?   ?   B . n 
B 1 8   THR 8   8   ?   ?   ?   B . n 
B 1 9   ALA 9   9   ?   ?   ?   B . n 
B 1 10  PHE 10  10  ?   ?   ?   B . n 
B 1 11  THR 11  11  ?   ?   ?   B . n 
B 1 12  VAL 12  12  ?   ?   ?   B . n 
B 1 13  ASP 13  13  ?   ?   ?   B . n 
B 1 14  LEU 14  14  ?   ?   ?   B . n 
B 1 15  THR 15  15  ?   ?   ?   B . n 
B 1 16  ASN 16  16  16  ASN ASN B . n 
B 1 17  CYS 17  17  17  CYS CYS B . n 
B 1 18  ASP 18  18  18  ASP ASP B . n 
B 1 19  LYS 19  19  19  LYS LYS B . n 
B 1 20  GLU 20  20  20  GLU GLU B . n 
B 1 21  PRO 21  21  21  PRO PRO B . n 
B 1 22  ILE 22  22  22  ILE ILE B . n 
B 1 23  HIS 23  23  23  HIS HIS B . n 
B 1 24  ILE 24  24  24  ILE ILE B . n 
B 1 25  PRO 25  25  25  PRO PRO B . n 
B 1 26  GLY 26  26  26  GLY GLY B . n 
B 1 27  PHE 27  27  27  PHE PHE B . n 
B 1 28  VAL 28  28  28  VAL VAL B . n 
B 1 29  GLN 29  29  29  GLN GLN B . n 
B 1 30  PRO 30  30  30  PRO PRO B . n 
B 1 31  HIS 31  31  31  HIS HIS B . n 
B 1 32  GLY 32  32  32  GLY GLY B . n 
B 1 33  VAL 33  33  33  VAL VAL B . n 
B 1 34  LEU 34  34  34  LEU LEU B . n 
B 1 35  LEU 35  35  35  LEU LEU B . n 
B 1 36  ALA 36  36  36  ALA ALA B . n 
B 1 37  ILE 37  37  37  ILE ILE B . n 
B 1 38  LYS 38  38  38  LYS LYS B . n 
B 1 39  GLU 39  39  39  GLU GLU B . n 
B 1 40  PRO 40  40  40  PRO PRO B . n 
B 1 41  GLU 41  41  41  GLU GLU B . n 
B 1 42  LEU 42  42  42  LEU LEU B . n 
B 1 43  THR 43  43  43  THR THR B . n 
B 1 44  ILE 44  44  44  ILE ILE B . n 
B 1 45  LEU 45  45  45  LEU LEU B . n 
B 1 46  GLN 46  46  46  GLN GLN B . n 
B 1 47  VAL 47  47  47  VAL VAL B . n 
B 1 48  SER 48  48  48  SER SER B . n 
B 1 49  ASN 49  49  49  ASN ASN B . n 
B 1 50  ASN 50  50  50  ASN ASN B . n 
B 1 51  THR 51  51  51  THR THR B . n 
B 1 52  TYR 52  52  52  TYR TYR B . n 
B 1 53  ASN 53  53  53  ASN ASN B . n 
B 1 54  CYS 54  54  54  CYS CYS B . n 
B 1 55  LEU 55  55  55  LEU LEU B . n 
B 1 56  GLY 56  56  56  GLY GLY B . n 
B 1 57  PHE 57  57  57  PHE PHE B . n 
B 1 58  HIS 58  58  58  HIS HIS B . n 
B 1 59  PRO 59  59  59  PRO PRO B . n 
B 1 60  GLU 60  60  60  GLU GLU B . n 
B 1 61  GLU 61  61  61  GLU GLU B . n 
B 1 62  LEU 62  62  62  LEU LEU B . n 
B 1 63  LEU 63  63  63  LEU LEU B . n 
B 1 64  ASN 64  64  64  ASN ASN B . n 
B 1 65  GLN 65  65  65  GLN GLN B . n 
B 1 66  PRO 66  66  66  PRO PRO B . n 
B 1 67  LEU 67  67  67  LEU LEU B . n 
B 1 68  ARG 68  68  68  ARG ARG B . n 
B 1 69  LYS 69  69  69  LYS LYS B . n 
B 1 70  LEU 70  70  70  LEU LEU B . n 
B 1 71  LEU 71  71  71  LEU LEU B . n 
B 1 72  GLU 72  72  72  GLU GLU B . n 
B 1 73  SER 73  73  73  SER SER B . n 
B 1 74  GLU 74  74  74  GLU GLU B . n 
B 1 75  GLN 75  75  75  GLN GLN B . n 
B 1 76  ILE 76  76  76  ILE ILE B . n 
B 1 77  ASP 77  77  77  ASP ASP B . n 
B 1 78  PHE 78  78  78  PHE PHE B . n 
B 1 79  LEU 79  79  79  LEU LEU B . n 
B 1 80  ASN 80  80  80  ASN ASN B . n 
B 1 81  ASP 81  81  81  ASP ASP B . n 
B 1 82  CYS 82  82  82  CYS CYS B . n 
B 1 83  LEU 83  83  83  LEU LEU B . n 
B 1 84  THR 84  84  84  THR THR B . n 
B 1 85  GLN 85  85  85  GLN GLN B . n 
B 1 86  GLU 86  86  86  GLU GLU B . n 
B 1 87  ASP 87  87  87  ASP ASP B . n 
B 1 88  ILE 88  88  88  ILE ILE B . n 
B 1 89  GLN 89  89  89  GLN GLN B . n 
B 1 90  ILE 90  90  90  ILE ILE B . n 
B 1 91  VAL 91  91  91  VAL VAL B . n 
B 1 92  ASN 92  92  92  ASN ASN B . n 
B 1 93  PRO 93  93  93  PRO PRO B . n 
B 1 94  VAL 94  94  94  VAL VAL B . n 
B 1 95  GLU 95  95  95  GLU GLU B . n 
B 1 96  PHE 96  96  96  PHE PHE B . n 
B 1 97  THR 97  97  ?   ?   ?   B . n 
B 1 98  ILE 98  98  ?   ?   ?   B . n 
B 1 99  LYS 99  99  ?   ?   ?   B . n 
B 1 100 THR 100 100 ?   ?   ?   B . n 
B 1 101 PHE 101 101 ?   ?   ?   B . n 
B 1 102 GLN 102 102 ?   ?   ?   B . n 
B 1 103 GLU 103 103 ?   ?   ?   B . n 
B 1 104 PRO 104 104 ?   ?   ?   B . n 
B 1 105 ILE 105 105 ?   ?   ?   B . n 
B 1 106 ILE 106 106 106 ILE ILE B . n 
B 1 107 PHE 107 107 107 PHE PHE B . n 
B 1 108 ASP 108 108 108 ASP ASP B . n 
B 1 109 GLY 109 109 109 GLY GLY B . n 
B 1 110 ILE 110 110 110 ILE ILE B . n 
B 1 111 ILE 111 111 111 ILE ILE B . n 
B 1 112 HIS 112 112 112 HIS HIS B . n 
B 1 113 ARG 113 113 113 ARG ARG B . n 
B 1 114 SER 114 114 114 SER SER B . n 
B 1 115 ASN 115 115 115 ASN ASN B . n 
B 1 116 GLY 116 116 116 GLY GLY B . n 
B 1 117 VAL 117 117 117 VAL VAL B . n 
B 1 118 VAL 118 118 118 VAL VAL B . n 
B 1 119 ILE 119 119 119 ILE ILE B . n 
B 1 120 LEU 120 120 120 LEU LEU B . n 
B 1 121 GLU 121 121 121 GLU GLU B . n 
B 1 122 LEU 122 122 122 LEU LEU B . n 
B 1 123 GLU 123 123 123 GLU GLU B . n 
B 1 124 PRO 124 124 124 PRO PRO B . n 
B 1 125 ALA 125 125 125 ALA ALA B . n 
B 1 126 ILE 126 126 126 ILE ILE B . n 
B 1 127 LEU 127 127 ?   ?   ?   B . n 
B 1 128 GLU 128 128 ?   ?   ?   B . n 
B 1 129 LYS 129 129 ?   ?   ?   B . n 
B 1 130 ASN 130 130 ?   ?   ?   B . n 
B 1 131 ASN 131 131 ?   ?   ?   B . n 
B 1 132 ASN 132 132 132 ASN ASN B . n 
B 1 133 TYR 133 133 133 TYR TYR B . n 
B 1 134 PHE 134 134 134 PHE PHE B . n 
B 1 135 ARG 135 135 135 ARG ARG B . n 
B 1 136 PHE 136 136 136 PHE PHE B . n 
B 1 137 TYR 137 137 137 TYR TYR B . n 
B 1 138 HIS 138 138 138 HIS HIS B . n 
B 1 139 LEU 139 139 139 LEU LEU B . n 
B 1 140 VAL 140 140 140 VAL VAL B . n 
B 1 141 LYS 141 141 141 LYS LYS B . n 
B 1 142 LEU 142 142 142 LEU LEU B . n 
B 1 143 ALA 143 143 143 ALA ALA B . n 
B 1 144 ILE 144 144 144 ILE ILE B . n 
B 1 145 GLY 145 145 145 GLY GLY B . n 
B 1 146 LYS 146 146 146 LYS LYS B . n 
B 1 147 LEU 147 147 147 LEU LEU B . n 
B 1 148 GLN 148 148 148 GLN GLN B . n 
B 1 149 SER 149 149 149 SER SER B . n 
B 1 150 THR 150 150 150 THR THR B . n 
B 1 151 LYS 151 151 151 LYS LYS B . n 
B 1 152 THR 152 152 152 THR THR B . n 
B 1 153 VAL 153 153 153 VAL VAL B . n 
B 1 154 THR 154 154 154 THR THR B . n 
B 1 155 GLU 155 155 155 GLU GLU B . n 
B 1 156 ILE 156 156 156 ILE ILE B . n 
B 1 157 SER 157 157 157 SER SER B . n 
B 1 158 GLN 158 158 158 GLN GLN B . n 
B 1 159 ILE 159 159 159 ILE ILE B . n 
B 1 160 ILE 160 160 160 ILE ILE B . n 
B 1 161 VAL 161 161 161 VAL VAL B . n 
B 1 162 THR 162 162 162 THR THR B . n 
B 1 163 GLU 163 163 163 GLU GLU B . n 
B 1 164 VAL 164 164 164 VAL VAL B . n 
B 1 165 ARG 165 165 165 ARG ARG B . n 
B 1 166 ARG 166 166 166 ARG ARG B . n 
B 1 167 ILE 167 167 167 ILE ILE B . n 
B 1 168 THR 168 168 168 THR THR B . n 
B 1 169 GLY 169 169 169 GLY GLY B . n 
B 1 170 PHE 170 170 170 PHE PHE B . n 
B 1 171 ASP 171 171 171 ASP ASP B . n 
B 1 172 ARG 172 172 172 ARG ARG B . n 
B 1 173 VAL 173 173 173 VAL VAL B . n 
B 1 174 MET 174 174 174 MET MET B . n 
B 1 175 PHE 175 175 175 PHE PHE B . n 
B 1 176 TYR 176 176 176 TYR TYR B . n 
B 1 177 ARG 177 177 177 ARG ARG B . n 
B 1 178 PHE 178 178 178 PHE PHE B . n 
B 1 179 ASP 179 179 179 ASP ASP B . n 
B 1 180 ARG 180 180 180 ARG ARG B . n 
B 1 181 ASP 181 181 181 ASP ASP B . n 
B 1 182 TRP 182 182 182 TRP TRP B . n 
B 1 183 ASN 183 183 183 ASN ASN B . n 
B 1 184 GLY 184 184 184 GLY GLY B . n 
B 1 185 ILE 185 185 185 ILE ILE B . n 
B 1 186 VAL 186 186 186 VAL VAL B . n 
B 1 187 ILE 187 187 187 ILE ILE B . n 
B 1 188 ALA 188 188 188 ALA ALA B . n 
B 1 189 GLU 189 189 189 GLU GLU B . n 
B 1 190 ASP 190 190 190 ASP ASP B . n 
B 1 191 LYS 191 191 191 LYS LYS B . n 
B 1 192 GLN 192 192 192 GLN GLN B . n 
B 1 193 GLU 193 193 193 GLU GLU B . n 
B 1 194 HIS 194 194 194 HIS HIS B . n 
B 1 195 LEU 195 195 195 LEU LEU B . n 
B 1 196 PRO 196 196 196 PRO PRO B . n 
B 1 197 SER 197 197 197 SER SER B . n 
B 1 198 TYR 198 198 198 TYR TYR B . n 
B 1 199 LEU 199 199 199 LEU LEU B . n 
B 1 200 ASP 200 200 200 ASP ASP B . n 
B 1 201 LEU 201 201 201 LEU LEU B . n 
B 1 202 HIS 202 202 202 HIS HIS B . n 
B 1 203 TYR 203 203 203 TYR TYR B . n 
B 1 204 PRO 204 204 204 PRO PRO B . n 
B 1 205 ALA 205 205 205 ALA ALA B . n 
B 1 206 SER 206 206 206 SER SER B . n 
B 1 207 ASP 207 207 207 ASP ASP B . n 
B 1 208 ILE 208 208 208 ILE ILE B . n 
B 1 209 PRO 209 209 209 PRO PRO B . n 
B 1 210 THR 210 210 210 THR THR B . n 
B 1 211 PRO 211 211 211 PRO PRO B . n 
B 1 212 ALA 212 212 212 ALA ALA B . n 
B 1 213 ARG 213 213 213 ARG ARG B . n 
B 1 214 LYS 214 214 214 LYS LYS B . n 
B 1 215 LEU 215 215 215 LEU LEU B . n 
B 1 216 TYR 216 216 216 TYR TYR B . n 
B 1 217 SER 217 217 217 SER SER B . n 
B 1 218 GLN 218 218 218 GLN GLN B . n 
B 1 219 ASN 219 219 219 ASN ASN B . n 
B 1 220 TRP 220 220 220 TRP TRP B . n 
B 1 221 LEU 221 221 221 LEU LEU B . n 
B 1 222 ARG 222 222 222 ARG ARG B . n 
B 1 223 LEU 223 223 223 LEU LEU B . n 
B 1 224 ILE 224 224 224 ILE ILE B . n 
B 1 225 PRO 225 225 225 PRO PRO B . n 
B 1 226 ASP 226 226 226 ASP ASP B . n 
B 1 227 ALA 227 227 227 ALA ALA B . n 
B 1 228 ASP 228 228 228 ASP ASP B . n 
B 1 229 TYR 229 229 229 TYR TYR B . n 
B 1 230 GLN 230 230 230 GLN GLN B . n 
B 1 231 ALA 231 231 231 ALA ALA B . n 
B 1 232 ALA 232 232 232 ALA ALA B . n 
B 1 233 ALA 233 233 233 ALA ALA B . n 
B 1 234 ILE 234 234 234 ILE ILE B . n 
B 1 235 VAL 235 235 235 VAL VAL B . n 
B 1 236 PRO 236 236 236 PRO PRO B . n 
B 1 237 THR 237 237 237 THR THR B . n 
B 1 238 ASN 238 238 238 ASN ASN B . n 
B 1 239 ASN 239 239 239 ASN ASN B . n 
B 1 240 PRO 240 240 240 PRO PRO B . n 
B 1 241 LEU 241 241 241 LEU LEU B . n 
B 1 242 THR 242 242 242 THR THR B . n 
B 1 243 ASP 243 243 243 ASP ASP B . n 
B 1 244 GLU 244 244 244 GLU GLU B . n 
B 1 245 PRO 245 245 245 PRO PRO B . n 
B 1 246 LEU 246 246 246 LEU LEU B . n 
B 1 247 ASP 247 247 247 ASP ASP B . n 
B 1 248 LEU 248 248 248 LEU LEU B . n 
B 1 249 SER 249 249 249 SER SER B . n 
B 1 250 GLY 250 250 250 GLY GLY B . n 
B 1 251 SER 251 251 251 SER SER B . n 
B 1 252 VAL 252 252 252 VAL VAL B . n 
B 1 253 LEU 253 253 253 LEU LEU B . n 
B 1 254 ARG 254 254 254 ARG ARG B . n 
B 1 255 SER 255 255 255 SER SER B . n 
B 1 256 VAL 256 256 256 VAL VAL B . n 
B 1 257 SER 257 257 257 SER SER B . n 
B 1 258 PRO 258 258 258 PRO PRO B . n 
B 1 259 CYS 259 259 259 CYS CYS B . n 
B 1 260 HIS 260 260 260 HIS HIS B . n 
B 1 261 ILE 261 261 261 ILE ILE B . n 
B 1 262 GLU 262 262 262 GLU GLU B . n 
B 1 263 TYR 263 263 263 TYR TYR B . n 
B 1 264 LEU 264 264 264 LEU LEU B . n 
B 1 265 HIS 265 265 265 HIS HIS B . n 
B 1 266 ASN 266 266 266 ASN ASN B . n 
B 1 267 MET 267 267 267 MET MET B . n 
B 1 268 GLY 268 268 268 GLY GLY B . n 
B 1 269 VAL 269 269 269 VAL VAL B . n 
B 1 270 LYS 270 270 270 LYS LYS B . n 
B 1 271 ALA 271 271 271 ALA ALA B . n 
B 1 272 SER 272 272 272 SER SER B . n 
B 1 273 MET 273 273 273 MET MET B . n 
B 1 274 SER 274 274 274 SER SER B . n 
B 1 275 ILE 275 275 275 ILE ILE B . n 
B 1 276 SER 276 276 276 SER SER B . n 
B 1 277 ILE 277 277 277 ILE ILE B . n 
B 1 278 ILE 278 278 278 ILE ILE B . n 
B 1 279 LYS 279 279 279 LYS LYS B . n 
B 1 280 ASN 280 280 280 ASN ASN B . n 
B 1 281 ASN 281 281 281 ASN ASN B . n 
B 1 282 LYS 282 282 282 LYS LYS B . n 
B 1 283 LEU 283 283 283 LEU LEU B . n 
B 1 284 TRP 284 284 284 TRP TRP B . n 
B 1 285 GLY 285 285 285 GLY GLY B . n 
B 1 286 LEU 286 286 286 LEU LEU B . n 
B 1 287 ILE 287 287 287 ILE ILE B . n 
B 1 288 ALA 288 288 288 ALA ALA B . n 
B 1 289 CYS 289 289 289 CYS CYS B . n 
B 1 290 HIS 290 290 290 HIS HIS B . n 
B 1 291 HIS 291 291 291 HIS HIS B . n 
B 1 292 GLN 292 292 292 GLN GLN B . n 
B 1 293 THR 293 293 293 THR THR B . n 
B 1 294 PRO 294 294 294 PRO PRO B . n 
B 1 295 LYS 295 295 295 LYS LYS B . n 
B 1 296 TYR 296 296 296 TYR TYR B . n 
B 1 297 VAL 297 297 297 VAL VAL B . n 
B 1 298 PRO 298 298 298 PRO PRO B . n 
B 1 299 TYR 299 299 299 TYR TYR B . n 
B 1 300 GLU 300 300 300 GLU GLU B . n 
B 1 301 ILE 301 301 301 ILE ILE B . n 
B 1 302 ARG 302 302 302 ARG ARG B . n 
B 1 303 HIS 303 303 303 HIS HIS B . n 
B 1 304 ALA 304 304 304 ALA ALA B . n 
B 1 305 CYS 305 305 305 CYS CYS B . n 
B 1 306 GLU 306 306 306 GLU GLU B . n 
B 1 307 PHE 307 307 307 PHE PHE B . n 
B 1 308 LEU 308 308 308 LEU LEU B . n 
B 1 309 GLY 309 309 309 GLY GLY B . n 
B 1 310 GLN 310 310 310 GLN GLN B . n 
B 1 311 VAL 311 311 311 VAL VAL B . n 
B 1 312 THR 312 312 312 THR THR B . n 
B 1 313 SER 313 313 313 SER SER B . n 
B 1 314 LEU 314 314 314 LEU LEU B . n 
B 1 315 GLU 315 315 315 GLU GLU B . n 
B 1 316 ILE 316 316 316 ILE ILE B . n 
B 1 317 ALA 317 317 317 ALA ALA B . n 
B 1 318 THR 318 318 318 THR THR B . n 
B 1 319 LYS 319 319 319 LYS LYS B . n 
B 1 320 GLU 320 320 320 GLU GLU B . n 
B 1 321 ASP 321 321 321 ASP ASP B . n 
B 1 322 ASN 322 322 322 ASN ASN B . n 
B 1 323 GLU 323 323 323 GLU GLU B . n 
B 1 324 ASP 324 324 324 ASP ASP B . n 
B 1 325 SER 325 325 325 SER SER B . n 
B 1 326 GLU 326 326 326 GLU GLU B . n 
B 1 327 SER 327 327 327 SER SER B . n 
B 1 328 LYS 328 328 328 LYS LYS B . n 
B 1 329 ILE 329 329 329 ILE ILE B . n 
B 1 330 GLU 330 330 330 GLU GLU B . n 
B 1 331 ILE 331 331 331 ILE ILE B . n 
B 1 332 LYS 332 332 332 LYS LYS B . n 
B 1 333 SER 333 333 333 SER SER B . n 
B 1 334 VAL 334 334 334 VAL VAL B . n 
B 1 335 LEU 335 335 335 LEU LEU B . n 
B 1 336 ALA 336 336 336 ALA ALA B . n 
B 1 337 LYS 337 337 337 LYS LYS B . n 
B 1 338 LEU 338 338 338 LEU LEU B . n 
B 1 339 VAL 339 339 339 VAL VAL B . n 
B 1 340 GLU 340 340 340 GLU GLU B . n 
B 1 341 TYR 341 341 341 TYR TYR B . n 
B 1 342 MET 342 342 342 MET MET B . n 
B 1 343 SER 343 343 343 SER SER B . n 
B 1 344 ALA 344 344 344 ALA ALA B . n 
B 1 345 GLU 345 345 345 GLU GLU B . n 
B 1 346 LYS 346 346 346 LYS LYS B . n 
B 1 347 SER 347 347 347 SER SER B . n 
B 1 348 PHE 348 348 348 PHE PHE B . n 
B 1 349 ILE 349 349 349 ILE ILE B . n 
B 1 350 ASP 350 350 350 ASP ASP B . n 
B 1 351 GLY 351 351 351 GLY GLY B . n 
B 1 352 LEU 352 352 352 LEU LEU B . n 
B 1 353 ILE 353 353 353 ILE ILE B . n 
B 1 354 ASN 354 354 354 ASN ASN B . n 
B 1 355 LYS 355 355 355 LYS LYS B . n 
B 1 356 GLN 356 356 356 GLN GLN B . n 
B 1 357 PRO 357 357 357 PRO PRO B . n 
B 1 358 ASN 358 358 358 ASN ASN B . n 
B 1 359 ILE 359 359 359 ILE ILE B . n 
B 1 360 LEU 360 360 360 LEU LEU B . n 
B 1 361 ASN 361 361 361 ASN ASN B . n 
B 1 362 LEU 362 362 362 LEU LEU B . n 
B 1 363 VAL 363 363 363 VAL VAL B . n 
B 1 364 ASN 364 364 364 ASN ASN B . n 
B 1 365 ALA 365 365 365 ALA ALA B . n 
B 1 366 GLN 366 366 366 GLN GLN B . n 
B 1 367 GLY 367 367 367 GLY GLY B . n 
B 1 368 ALA 368 368 368 ALA ALA B . n 
B 1 369 ALA 369 369 369 ALA ALA B . n 
B 1 370 ILE 370 370 370 ILE ILE B . n 
B 1 371 CYS 371 371 371 CYS CYS B . n 
B 1 372 PHE 372 372 ?   ?   ?   B . n 
B 1 373 ASN 373 373 ?   ?   ?   B . n 
B 1 374 LYS 374 374 ?   ?   ?   B . n 
B 1 375 GLU 375 375 375 GLU GLU B . n 
B 1 376 LEU 376 376 376 LEU LEU B . n 
B 1 377 TYR 377 377 377 TYR TYR B . n 
B 1 378 LEU 378 378 378 LEU LEU B . n 
B 1 379 LEU 379 379 379 LEU LEU B . n 
B 1 380 GLY 380 380 380 GLY GLY B . n 
B 1 381 ASN 381 381 381 ASN ASN B . n 
B 1 382 THR 382 382 382 THR THR B . n 
B 1 383 PRO 383 383 383 PRO PRO B . n 
B 1 384 GLU 384 384 384 GLU GLU B . n 
B 1 385 LYS 385 385 385 LYS LYS B . n 
B 1 386 GLN 386 386 386 GLN GLN B . n 
B 1 387 ASP 387 387 387 ASP ASP B . n 
B 1 388 ILE 388 388 388 ILE ILE B . n 
B 1 389 GLN 389 389 389 GLN GLN B . n 
B 1 390 ASN 390 390 390 ASN ASN B . n 
B 1 391 LEU 391 391 391 LEU LEU B . n 
B 1 392 LEU 392 392 392 LEU LEU B . n 
B 1 393 LEU 393 393 393 LEU LEU B . n 
B 1 394 TRP 394 394 394 TRP TRP B . n 
B 1 395 ILE 395 395 395 ILE ILE B . n 
B 1 396 HIS 396 396 396 HIS HIS B . n 
B 1 397 ASN 397 397 397 ASN ASN B . n 
B 1 398 ASN 398 398 398 ASN ASN B . n 
B 1 399 ILE 399 399 399 ILE ILE B . n 
B 1 400 ASP 400 400 400 ASP ASP B . n 
B 1 401 GLU 401 401 401 GLU GLU B . n 
B 1 402 ASP 402 402 402 ASP ASP B . n 
B 1 403 ILE 403 403 403 ILE ILE B . n 
B 1 404 PHE 404 404 404 PHE PHE B . n 
B 1 405 TYR 405 405 405 TYR TYR B . n 
B 1 406 THR 406 406 406 THR THR B . n 
B 1 407 ASP 407 407 407 ASP ASP B . n 
B 1 408 SER 408 408 408 SER SER B . n 
B 1 409 LEU 409 409 409 LEU LEU B . n 
B 1 410 SER 410 410 410 SER SER B . n 
B 1 411 GLN 411 411 411 GLN GLN B . n 
B 1 412 VAL 412 412 412 VAL VAL B . n 
B 1 413 TYR 413 413 413 TYR TYR B . n 
B 1 414 PRO 414 414 414 PRO PRO B . n 
B 1 415 GLU 415 415 415 GLU GLU B . n 
B 1 416 ALA 416 416 416 ALA ALA B . n 
B 1 417 GLU 417 417 417 GLU GLU B . n 
B 1 418 LYS 418 418 418 LYS LYS B . n 
B 1 419 PHE 419 419 419 PHE PHE B . n 
B 1 420 LYS 420 420 420 LYS LYS B . n 
B 1 421 ASP 421 421 421 ASP ASP B . n 
B 1 422 VAL 422 422 422 VAL VAL B . n 
B 1 423 ALA 423 423 423 ALA ALA B . n 
B 1 424 SER 424 424 424 SER SER B . n 
B 1 425 GLY 425 425 425 GLY GLY B . n 
B 1 426 LEU 426 426 426 LEU LEU B . n 
B 1 427 ILE 427 427 427 ILE ILE B . n 
B 1 428 ALA 428 428 428 ALA ALA B . n 
B 1 429 LEU 429 429 429 LEU LEU B . n 
B 1 430 SER 430 430 430 SER SER B . n 
B 1 431 ILE 431 431 431 ILE ILE B . n 
B 1 432 SER 432 432 432 SER SER B . n 
B 1 433 LYS 433 433 433 LYS LYS B . n 
B 1 434 THR 434 434 434 THR THR B . n 
B 1 435 GLN 435 435 435 GLN GLN B . n 
B 1 436 ASN 436 436 436 ASN ASN B . n 
B 1 437 LYS 437 437 437 LYS LYS B . n 
B 1 438 TYR 438 438 438 TYR TYR B . n 
B 1 439 VAL 439 439 439 VAL VAL B . n 
B 1 440 LEU 440 440 440 LEU LEU B . n 
B 1 441 TRP 441 441 441 TRP TRP B . n 
B 1 442 PHE 442 442 442 PHE PHE B . n 
B 1 443 ARG 443 443 443 ARG ARG B . n 
B 1 444 PRO 444 444 444 PRO PRO B . n 
B 1 445 GLU 445 445 445 GLU GLU B . n 
B 1 446 GLU 446 446 446 GLU GLU B . n 
B 1 447 VAL 447 447 447 VAL VAL B . n 
B 1 448 GLN 448 448 448 GLN GLN B . n 
B 1 449 THR 449 449 449 THR THR B . n 
B 1 450 VAL 450 450 450 VAL VAL B . n 
B 1 451 ASN 451 451 451 ASN ASN B . n 
B 1 452 TRP 452 452 452 TRP TRP B . n 
B 1 453 GLY 453 453 453 GLY GLY B . n 
B 1 454 GLY 454 454 454 GLY GLY B . n 
B 1 455 ASN 455 455 455 ASN ASN B . n 
B 1 456 PRO 456 456 ?   ?   ?   B . n 
B 1 457 ASN 457 457 ?   ?   ?   B . n 
B 1 458 GLN 458 458 ?   ?   ?   B . n 
B 1 459 PRO 459 459 ?   ?   ?   B . n 
B 1 460 VAL 460 460 ?   ?   ?   B . n 
B 1 461 GLU 461 461 ?   ?   ?   B . n 
B 1 462 VAL 462 462 ?   ?   ?   B . n 
B 1 463 SER 463 463 ?   ?   ?   B . n 
B 1 464 GLU 464 464 ?   ?   ?   B . n 
B 1 465 ASN 465 465 ?   ?   ?   B . n 
B 1 466 GLY 466 466 ?   ?   ?   B . n 
B 1 467 GLY 467 467 ?   ?   ?   B . n 
B 1 468 LEU 468 468 ?   ?   ?   B . n 
B 1 469 HIS 469 469 ?   ?   ?   B . n 
B 1 470 LEU 470 470 ?   ?   ?   B . n 
B 1 471 SER 471 471 ?   ?   ?   B . n 
B 1 472 PRO 472 472 ?   ?   ?   B . n 
B 1 473 ARG 473 473 ?   ?   ?   B . n 
B 1 474 LYS 474 474 ?   ?   ?   B . n 
B 1 475 SER 475 475 ?   ?   ?   B . n 
B 1 476 PHE 476 476 ?   ?   ?   B . n 
B 1 477 GLU 477 477 477 GLU GLU B . n 
B 1 478 LEU 478 478 478 LEU LEU B . n 
B 1 479 TRP 479 479 479 TRP TRP B . n 
B 1 480 LYS 480 480 480 LYS LYS B . n 
B 1 481 GLU 481 481 481 GLU GLU B . n 
B 1 482 ILE 482 482 482 ILE ILE B . n 
B 1 483 VAL 483 483 483 VAL VAL B . n 
B 1 484 ARG 484 484 484 ARG ARG B . n 
B 1 485 LEU 485 485 485 LEU LEU B . n 
B 1 486 LYS 486 486 486 LYS LYS B . n 
B 1 487 SER 487 487 487 SER SER B . n 
B 1 488 LEU 488 488 488 LEU LEU B . n 
B 1 489 PRO 489 489 489 PRO PRO B . n 
B 1 490 TRP 490 490 490 TRP TRP B . n 
B 1 491 LYS 491 491 491 LYS LYS B . n 
B 1 492 SER 492 492 492 SER SER B . n 
B 1 493 TYR 493 493 493 TYR TYR B . n 
B 1 494 GLU 494 494 494 GLU GLU B . n 
B 1 495 VAL 495 495 495 VAL VAL B . n 
B 1 496 ASN 496 496 496 ASN ASN B . n 
B 1 497 ALA 497 497 497 ALA ALA B . n 
B 1 498 ALA 498 498 498 ALA ALA B . n 
B 1 499 ALA 499 499 499 ALA ALA B . n 
B 1 500 GLU 500 500 500 GLU GLU B . n 
B 1 501 LEU 501 501 501 LEU LEU B . n 
B 1 502 ARG 502 502 502 ARG ARG B . n 
B 1 503 GLY 503 503 503 GLY GLY B . n 
B 1 504 ALA 504 504 504 ALA ALA B . n 
B 1 505 ILE 505 505 505 ILE ILE B . n 
B 1 506 ILE 506 506 506 ILE ILE B . n 
B 1 507 THR 507 507 507 THR THR B . n 
B 1 508 VAL 508 508 508 VAL VAL B . n 
B 1 509 VAL 509 509 509 VAL VAL B . n 
B 1 510 LEU 510 510 510 LEU LEU B . n 
B 1 511 ARG 511 511 511 ARG ARG B . n 
B 1 512 LYS 512 512 512 LYS LYS B . n 
B 1 513 ILE 513 513 ?   ?   ?   B . n 
B 1 514 ASP 514 514 ?   ?   ?   B . n 
B 1 515 GLU 515 515 ?   ?   ?   B . n 
B 1 516 HIS 516 516 ?   ?   ?   B . n 
B 1 517 HIS 517 517 ?   ?   ?   B . n 
B 1 518 HIS 518 518 ?   ?   ?   B . n 
B 1 519 HIS 519 519 ?   ?   ?   B . n 
B 1 520 HIS 520 520 ?   ?   ?   B . n 
B 1 521 HIS 521 521 ?   ?   ?   B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        BLR 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   BLR 
_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 
C 2 BLR 1 601 902 BLR BLR A . 
D 2 BLR 1 601 902 BLR BLR B . 
# 
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 N 0 A BLR 601 ? NB  ? C BLR ? NB  
2  1 N 0 A BLR 601 ? C1B ? C BLR ? C1B 
3  1 N 0 A BLR 601 ? C2B ? C BLR ? C2B 
4  1 N 0 A BLR 601 ? C3B ? C BLR ? C3B 
5  1 N 0 A BLR 601 ? C4B ? C BLR ? C4B 
6  1 N 0 A BLR 601 ? CMB ? C BLR ? CMB 
7  1 N 0 A BLR 601 ? OB  ? C BLR ? OB  
8  1 N 0 A BLR 601 ? CAB ? C BLR ? CAB 
9  1 N 0 A BLR 601 ? CBB ? C BLR ? CBB 
10 1 N 0 B BLR 601 ? NB  ? D BLR ? NB  
11 1 N 0 B BLR 601 ? C1B ? D BLR ? C1B 
12 1 N 0 B BLR 601 ? C2B ? D BLR ? C2B 
13 1 N 0 B BLR 601 ? C3B ? D BLR ? C3B 
14 1 N 0 B BLR 601 ? C4B ? D BLR ? C4B 
15 1 N 0 B BLR 601 ? CMB ? D BLR ? CMB 
16 1 N 0 B BLR 601 ? OB  ? D BLR ? OB  
17 1 N 0 B BLR 601 ? CAB ? D BLR ? CAB 
18 1 N 0 B BLR 601 ? CBB ? D BLR ? CBB 
# 
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   ? ? ? 1.21.1_5286 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? HKL-3000 ? ? ? .           2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? HKL-3000 ? ? ? .           3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? .           4 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   99.145 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9JRY 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     104.551 
_cell.length_a_esd                 ? 
_cell.length_b                     147.131 
_cell.length_b_esd                 ? 
_cell.length_c                     88.076 
_cell.length_c_esd                 ? 
_cell.volume                       1337625.022 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9JRY 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                5 
_symmetry.space_group_name_Hall            'C 2y' 
_symmetry.space_group_name_H-M             'C 1 2 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                   9JRY 
_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             2.81 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          56.18 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.1 M BICINE (pH 8.0), 181.8 mM NaCl, 9% 2-propanol, 23~34.5% PEG1500' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293.15 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     110 
_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 PILATUS 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2024-03-22 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1 
_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                        'PAL/PLS BEAMLINE 11C' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   11C 
_diffrn_source.pdbx_synchrotron_site       PAL/PLS 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9JRY 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              3.349 
_reflns.d_resolution_low                               37.43 
_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                                     17035 
_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                           89.86 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                4.5 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          34.28 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   1 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    3.35 
_reflns_shell.d_res_low                                     3.45 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             867 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  1 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_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                               32.75 
_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                                 9JRY 
_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                            3.35 
_refine.ls_d_res_low                             37.43 
_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                     17035 
_refine.ls_number_reflns_R_free                  1704 
_refine.ls_number_reflns_R_work                  15331 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    89.86 
_refine.ls_percent_reflns_R_free                 10.00 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2816 
_refine.ls_R_factor_R_free                       0.2968 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2799 
_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                          0.10 
_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                      6BAP 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_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             1.1000 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 31.1142 
_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                            0.5170 
_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                       3.35 
_refine_hist.d_res_low                        37.43 
_refine_hist.number_atoms_solvent             0 
_refine_hist.number_atoms_total               7430 
_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        7344 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         86 
_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' ? 0.0026  ? 7596  ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.6361  ? 10339 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0449  ? 1171  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0045  ? 1317  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 14.0264 ? 2814  ? f_dihedral_angle_d ? ? 
# 
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' 3.35 3.45  . . 87  780  55.61 . . . . 0.3947 . . . . . . . . . . . 0.4480 
'X-RAY DIFFRACTION' 3.45 3.56  . . 126 1137 80.29 . . . . 0.3724 . . . . . . . . . . . 0.3796 
'X-RAY DIFFRACTION' 3.56 3.69  . . 137 1229 86.40 . . . . 0.3424 . . . . . . . . . . . 0.3445 
'X-RAY DIFFRACTION' 3.69 3.83  . . 138 1244 88.19 . . . . 0.3262 . . . . . . . . . . . 0.3174 
'X-RAY DIFFRACTION' 3.83 4.01  . . 136 1231 86.41 . . . . 0.3060 . . . . . . . . . . . 0.3334 
'X-RAY DIFFRACTION' 4.01 4.22  . . 145 1296 91.55 . . . . 0.2807 . . . . . . . . . . . 0.3221 
'X-RAY DIFFRACTION' 4.22 4.48  . . 153 1385 97.90 . . . . 0.2560 . . . . . . . . . . . 0.2913 
'X-RAY DIFFRACTION' 4.48 4.83  . . 153 1373 96.95 . . . . 0.2388 . . . . . . . . . . . 0.2549 
'X-RAY DIFFRACTION' 4.83 5.31  . . 156 1405 98.30 . . . . 0.2650 . . . . . . . . . . . 0.2743 
'X-RAY DIFFRACTION' 5.31 6.08  . . 153 1376 96.83 . . . . 0.2660 . . . . . . . . . . . 0.3002 
'X-RAY DIFFRACTION' 6.08 7.65  . . 158 1426 99.56 . . . . 0.2689 . . . . . . . . . . . 0.2709 
'X-RAY DIFFRACTION' 7.65 37.43 . . 162 1449 99.63 . . . . 0.2006 . . . . . . . . . . . 0.2058 
# 
_struct.entry_id                     9JRY 
_struct.title                        
'Crystal structure of FiDCB, a dual-cysteine cyanobacterial phytochrome of Fischerella sp. PCC 9605' 
_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        9JRY 
_struct_keywords.text            'Cyanobacteria, Dual-Cysteine Bacteriophytochrome, SIGNALING PROTEIN' 
_struct_keywords.pdbx_keywords   'SIGNALING 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 1 ? 
C N N 2 ? 
D N N 2 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    PDB 
_struct_ref.db_code                    9JRY 
_struct_ref.pdbx_db_accession          9JRY 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   ? 
_struct_ref.pdbx_align_begin           1 
# 
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 9JRY A 1 ? 521 ? 9JRY 1 ? 521 ? 1 521 
2 1 9JRY B 1 ? 521 ? 9JRY 1 ? 521 ? 1 521 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 2520  ? 
1 MORE         -13   ? 
1 'SSA (A^2)'  41660 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_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 ASN A 50  ? GLY A 56  ? ASN A 50  GLY A 56  1 ? 7  
HELX_P HELX_P2  AA2 HIS A 58  ? LEU A 63  ? HIS A 58  LEU A 63  1 ? 6  
HELX_P HELX_P3  AA3 PRO A 66  ? LEU A 70  ? PRO A 66  LEU A 70  5 ? 5  
HELX_P HELX_P4  AA4 GLU A 72  ? GLN A 85  ? GLU A 72  GLN A 85  1 ? 14 
HELX_P HELX_P5  AA5 ASP A 87  ? ASN A 92  ? ASP A 87  ASN A 92  5 ? 6  
HELX_P HELX_P6  AA6 TYR A 137 ? SER A 149 ? TYR A 137 SER A 149 1 ? 13 
HELX_P HELX_P7  AA7 THR A 152 ? GLY A 169 ? THR A 152 GLY A 169 1 ? 18 
HELX_P HELX_P8  AA8 PRO A 204 ? ILE A 208 ? PRO A 204 ILE A 208 5 ? 5  
HELX_P HELX_P9  AA9 PRO A 209 ? ASN A 219 ? PRO A 209 ASN A 219 1 ? 11 
HELX_P HELX_P10 AB1 SER A 257 ? GLY A 268 ? SER A 257 GLY A 268 1 ? 12 
HELX_P HELX_P11 AB2 PRO A 298 ? MET A 342 ? PRO A 298 MET A 342 1 ? 45 
HELX_P HELX_P12 AB3 ASP A 350 ? ASN A 354 ? ASP A 350 ASN A 354 1 ? 5  
HELX_P HELX_P13 AB4 ASN A 358 ? VAL A 363 ? ASN A 358 VAL A 363 1 ? 6  
HELX_P HELX_P14 AB5 GLU A 384 ? ASN A 398 ? GLU A 384 ASN A 398 1 ? 15 
HELX_P HELX_P15 AB6 SER A 408 ? VAL A 412 ? SER A 408 VAL A 412 5 ? 5  
HELX_P HELX_P16 AB7 TYR A 413 ? LYS A 418 ? TYR A 413 LYS A 418 5 ? 6  
HELX_P HELX_P17 AB8 PHE A 419 ? SER A 424 ? PHE A 419 SER A 424 1 ? 6  
HELX_P HELX_P18 AB9 LYS A 491 ? VAL A 508 ? LYS A 491 VAL A 508 1 ? 18 
HELX_P HELX_P19 AC1 ASN B 16  ? GLU B 20  ? ASN B 16  GLU B 20  5 ? 5  
HELX_P HELX_P20 AC2 ASN B 50  ? GLY B 56  ? ASN B 50  GLY B 56  1 ? 7  
HELX_P HELX_P21 AC3 HIS B 58  ? LEU B 63  ? HIS B 58  LEU B 63  5 ? 6  
HELX_P HELX_P22 AC4 ARG B 68  ? LEU B 70  ? ARG B 68  LEU B 70  5 ? 3  
HELX_P HELX_P23 AC5 GLU B 72  ? THR B 84  ? GLU B 72  THR B 84  1 ? 13 
HELX_P HELX_P24 AC6 ASP B 87  ? ASN B 92  ? ASP B 87  ASN B 92  5 ? 6  
HELX_P HELX_P25 AC7 TYR B 133 ? SER B 149 ? TYR B 133 SER B 149 1 ? 17 
HELX_P HELX_P26 AC8 THR B 152 ? GLY B 169 ? THR B 152 GLY B 169 1 ? 18 
HELX_P HELX_P27 AC9 PRO B 204 ? ILE B 208 ? PRO B 204 ILE B 208 5 ? 5  
HELX_P HELX_P28 AD1 PRO B 209 ? ASN B 219 ? PRO B 209 ASN B 219 1 ? 11 
HELX_P HELX_P29 AD2 ASP B 247 ? SER B 251 ? ASP B 247 SER B 251 5 ? 5  
HELX_P HELX_P30 AD3 SER B 257 ? GLY B 268 ? SER B 257 GLY B 268 1 ? 12 
HELX_P HELX_P31 AD4 PRO B 298 ? SER B 343 ? PRO B 298 SER B 343 1 ? 46 
HELX_P HELX_P32 AD5 SER B 347 ? ASN B 354 ? SER B 347 ASN B 354 1 ? 8  
HELX_P HELX_P33 AD6 ILE B 359 ? ASN B 364 ? ILE B 359 ASN B 364 1 ? 6  
HELX_P HELX_P34 AD7 GLN B 386 ? ILE B 399 ? GLN B 386 ILE B 399 1 ? 14 
HELX_P HELX_P35 AD8 SER B 408 ? VAL B 412 ? SER B 408 VAL B 412 5 ? 5  
HELX_P HELX_P36 AD9 TYR B 413 ? LYS B 420 ? TYR B 413 LYS B 420 5 ? 8  
HELX_P HELX_P37 AE1 LYS B 491 ? LYS B 512 ? LYS B 491 LYS B 512 1 ? 22 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 GLU 39  A . ? GLU 39  A PRO 40  A ? PRO 40  A 1 7.93  
2 VAL 235 A . ? VAL 235 A PRO 236 A ? PRO 236 A 1 -5.87 
3 GLU 39  B . ? GLU 39  B PRO 40  B ? PRO 40  B 1 -5.54 
4 ASN 92  B . ? ASN 92  B PRO 93  B ? PRO 93  B 1 -1.54 
5 VAL 235 B . ? VAL 235 B PRO 236 B ? PRO 236 B 1 -9.97 
6 GLN 356 B . ? GLN 356 B PRO 357 B ? PRO 357 B 1 -0.33 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2 ? 
AA2 ? 5 ? 
AA3 ? 8 ? 
AA4 ? 5 ? 
AA5 ? 4 ? 
AA6 ? 7 ? 
AA7 ? 6 ? 
AA8 ? 5 ? 
AA9 ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? 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 
AA3 6 7 ? parallel      
AA3 7 8 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA4 4 5 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA5 2 3 ? anti-parallel 
AA5 3 4 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA6 2 3 ? anti-parallel 
AA6 3 4 ? anti-parallel 
AA6 4 5 ? anti-parallel 
AA6 5 6 ? anti-parallel 
AA6 6 7 ? anti-parallel 
AA7 1 2 ? anti-parallel 
AA7 2 3 ? anti-parallel 
AA7 3 4 ? anti-parallel 
AA7 4 5 ? anti-parallel 
AA7 5 6 ? anti-parallel 
AA8 1 2 ? anti-parallel 
AA8 2 3 ? anti-parallel 
AA8 3 4 ? anti-parallel 
AA8 4 5 ? anti-parallel 
AA9 1 2 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 PHE A 27  ? VAL A 28  ? PHE A 27  VAL A 28  
AA1 2 ALA A 232 ? ALA A 233 ? ALA A 232 ALA A 233 
AA2 1 ILE A 44  ? VAL A 47  ? ILE A 44  VAL A 47  
AA2 2 VAL A 33  ? ILE A 37  ? VAL A 33  ILE A 37  
AA2 3 VAL A 118 ? PRO A 124 ? VAL A 118 PRO A 124 
AA2 4 ILE A 105 ? ARG A 113 ? ILE A 105 ARG A 113 
AA2 5 VAL A 94  ? ILE A 98  ? VAL A 94  ILE A 98  
AA3 1 LEU A 221 ? ILE A 224 ? LEU A 221 ILE A 224 
AA3 2 ALA A 271 ? LYS A 279 ? ALA A 271 LYS A 279 
AA3 3 LYS A 282 ? HIS A 291 ? LYS A 282 HIS A 291 
AA3 4 ARG A 172 ? ARG A 177 ? ARG A 172 ARG A 177 
AA3 5 GLY A 184 ? LYS A 191 ? GLY A 184 LYS A 191 
AA3 6 LEU A 201 ? TYR A 203 ? LEU A 201 TYR A 203 
AA3 7 GLN A 448 ? TRP A 452 ? GLN A 448 TRP A 452 
AA3 8 TRP A 479 ? VAL A 483 ? TRP A 479 VAL A 483 
AA4 1 GLU A 375 ? GLY A 380 ? GLU A 375 GLY A 380 
AA4 2 GLY A 367 ? PHE A 372 ? GLY A 367 PHE A 372 
AA4 3 LYS A 437 ? ARG A 443 ? LYS A 437 ARG A 443 
AA4 4 GLY A 425 ? SER A 432 ? GLY A 425 SER A 432 
AA4 5 ILE A 403 ? THR A 406 ? ILE A 403 THR A 406 
AA5 1 PHE B 27  ? VAL B 28  ? PHE B 27  VAL B 28  
AA5 2 ALA B 232 ? VAL B 235 ? ALA B 232 VAL B 235 
AA5 3 THR B 43  ? SER B 48  ? THR B 43  SER B 48  
AA5 4 GLN B 65  ? PRO B 66  ? GLN B 65  PRO B 66  
AA6 1 PHE B 27  ? VAL B 28  ? PHE B 27  VAL B 28  
AA6 2 ALA B 232 ? VAL B 235 ? ALA B 232 VAL B 235 
AA6 3 THR B 43  ? SER B 48  ? THR B 43  SER B 48  
AA6 4 VAL B 33  ? LYS B 38  ? VAL B 33  LYS B 38  
AA6 5 VAL B 118 ? PRO B 124 ? VAL B 118 PRO B 124 
AA6 6 PHE B 107 ? ARG B 113 ? PHE B 107 ARG B 113 
AA6 7 VAL B 94  ? GLU B 95  ? VAL B 94  GLU B 95  
AA7 1 HIS B 202 ? TYR B 203 ? HIS B 202 TYR B 203 
AA7 2 GLY B 184 ? LYS B 191 ? GLY B 184 LYS B 191 
AA7 3 ARG B 172 ? PHE B 178 ? ARG B 172 PHE B 178 
AA7 4 LYS B 282 ? HIS B 291 ? LYS B 282 HIS B 291 
AA7 5 ALA B 271 ? LYS B 279 ? ALA B 271 LYS B 279 
AA7 6 LEU B 221 ? ILE B 224 ? LEU B 221 ILE B 224 
AA8 1 LEU B 378 ? GLY B 380 ? LEU B 378 GLY B 380 
AA8 2 GLY B 367 ? CYS B 371 ? GLY B 367 CYS B 371 
AA8 3 LYS B 437 ? ARG B 443 ? LYS B 437 ARG B 443 
AA8 4 GLY B 425 ? SER B 432 ? GLY B 425 SER B 432 
AA8 5 ILE B 403 ? THR B 406 ? ILE B 403 THR B 406 
AA9 1 GLN B 448 ? TRP B 452 ? GLN B 448 TRP B 452 
AA9 2 TRP B 479 ? VAL B 483 ? TRP B 479 VAL B 483 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N VAL A 28  ? N VAL A 28  O ALA A 232 ? O ALA A 232 
AA2 1 2 O GLN A 46  ? O GLN A 46  N ALA A 36  ? N ALA A 36  
AA2 2 3 N ILE A 37  ? N ILE A 37  O VAL A 118 ? O VAL A 118 
AA2 3 4 O ILE A 119 ? O ILE A 119 N HIS A 112 ? N HIS A 112 
AA2 4 5 O PHE A 107 ? O PHE A 107 N PHE A 96  ? N PHE A 96  
AA3 1 2 N ILE A 224 ? N ILE A 224 O SER A 272 ? O SER A 272 
AA3 2 3 N LYS A 279 ? N LYS A 279 O LYS A 282 ? O LYS A 282 
AA3 3 4 O LEU A 286 ? O LEU A 286 N TYR A 176 ? N TYR A 176 
AA3 4 5 N PHE A 175 ? N PHE A 175 O ALA A 188 ? O ALA A 188 
AA3 5 6 N GLY A 184 ? N GLY A 184 O TYR A 203 ? O TYR A 203 
AA3 6 7 N HIS A 202 ? N HIS A 202 O ASN A 451 ? O ASN A 451 
AA3 7 8 N TRP A 452 ? N TRP A 452 O TRP A 479 ? O TRP A 479 
AA4 1 2 O GLU A 375 ? O GLU A 375 N PHE A 372 ? N PHE A 372 
AA4 2 3 N GLY A 367 ? N GLY A 367 O PHE A 442 ? O PHE A 442 
AA4 3 4 O VAL A 439 ? O VAL A 439 N LEU A 429 ? N LEU A 429 
AA4 4 5 O LEU A 426 ? O LEU A 426 N THR A 406 ? N THR A 406 
AA5 1 2 N VAL B 28  ? N VAL B 28  O ALA B 232 ? O ALA B 232 
AA5 2 3 O VAL B 235 ? O VAL B 235 N VAL B 47  ? N VAL B 47  
AA5 3 4 N ILE B 44  ? N ILE B 44  O GLN B 65  ? O GLN B 65  
AA6 1 2 N VAL B 28  ? N VAL B 28  O ALA B 232 ? O ALA B 232 
AA6 2 3 O VAL B 235 ? O VAL B 235 N VAL B 47  ? N VAL B 47  
AA6 3 4 O THR B 43  ? O THR B 43  N LYS B 38  ? N LYS B 38  
AA6 4 5 N VAL B 33  ? N VAL B 33  O LEU B 122 ? O LEU B 122 
AA6 5 6 O GLU B 121 ? O GLU B 121 N ILE B 110 ? N ILE B 110 
AA6 6 7 O GLY B 109 ? O GLY B 109 N VAL B 94  ? N VAL B 94  
AA7 1 2 O TYR B 203 ? O TYR B 203 N GLY B 184 ? N GLY B 184 
AA7 2 3 O ASP B 190 ? O ASP B 190 N VAL B 173 ? N VAL B 173 
AA7 3 4 N ARG B 172 ? N ARG B 172 O HIS B 290 ? O HIS B 290 
AA7 4 5 O CYS B 289 ? O CYS B 289 N MET B 273 ? N MET B 273 
AA7 5 6 O SER B 272 ? O SER B 272 N ILE B 224 ? N ILE B 224 
AA8 1 2 O LEU B 379 ? O LEU B 379 N ALA B 368 ? N ALA B 368 
AA8 2 3 N ALA B 369 ? N ALA B 369 O LEU B 440 ? O LEU B 440 
AA8 3 4 O VAL B 439 ? O VAL B 439 N LEU B 429 ? N LEU B 429 
AA8 4 5 O LEU B 426 ? O LEU B 426 N THR B 406 ? N THR B 406 
AA9 1 2 N GLN B 448 ? N GLN B 448 O VAL B 483 ? O VAL B 483 
# 
_pdbx_entry_details.entry_id                   9JRY 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1  1 OD2 A ASP 207 ? ? CMB A BLR 601 ? ? 1.37 
2  1 OH  A TYR 263 ? ? C4B A BLR 601 ? ? 1.38 
3  1 OH  B TYR 263 ? ? CMB B BLR 601 ? ? 1.38 
4  1 OH  A TYR 263 ? ? OB  A BLR 601 ? ? 1.53 
5  1 OH  A TYR 263 ? ? NB  A BLR 601 ? ? 1.67 
6  1 SG  B CYS 17  ? ? CBC B BLR 601 ? ? 1.77 
7  1 SD  B MET 267 ? ? CBB B BLR 601 ? ? 1.77 
8  1 SG  A CYS 17  ? ? CBC A BLR 601 ? ? 1.77 
9  1 SG  A CYS 259 ? ? CAC A BLR 601 ? ? 1.77 
10 1 SG  B CYS 17  ? ? CAC B BLR 601 ? ? 1.89 
11 1 SG  A CYS 259 ? ? C3C A BLR 601 ? ? 2.03 
12 1 OG  A SER 272 ? ? O1A A BLR 601 ? ? 2.19 
# 
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 SER A 48  ? ? -75.90  -164.61 
2  1 TYR A 52  ? ? -70.25  -71.57  
3  1 ASN A 64  ? ? 64.38   -4.43   
4  1 PRO A 93  ? ? -67.43  66.29   
5  1 ASP A 179 ? ? -103.79 -169.19 
6  1 ASP A 243 ? ? 64.96   -2.60   
7  1 ASN A 373 ? ? 53.16   -122.43 
8  1 ASN A 398 ? ? -96.81  -60.29  
9  1 ALA A 423 ? ? -145.39 55.52   
10 1 GLN B 218 ? ? -90.32  -67.73  
11 1 ILE B 353 ? ? -96.82  -61.29  
12 1 ASN B 358 ? ? -105.08 -168.77 
13 1 GLN B 386 ? ? 81.89   -34.21  
14 1 ASN B 398 ? ? -122.60 -54.72  
15 1 ASP B 400 ? ? -141.26 46.88   
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z           
2 -x,y,-z         
3 x+1/2,y+1/2,z   
4 -x+1/2,y+1/2,-z 
# 
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 ASN 2   ? A ASN 2   
3   1 Y 1 A THR 3   ? A THR 3   
4   1 Y 1 A ASN 4   ? A ASN 4   
5   1 Y 1 A LYS 5   ? A LYS 5   
6   1 Y 1 A ASN 6   ? A ASN 6   
7   1 Y 1 A ASP 7   ? A ASP 7   
8   1 Y 1 A THR 8   ? A THR 8   
9   1 Y 1 A ALA 9   ? A ALA 9   
10  1 Y 1 A PHE 10  ? A PHE 10  
11  1 Y 1 A THR 11  ? A THR 11  
12  1 Y 1 A VAL 12  ? A VAL 12  
13  1 Y 1 A ASP 13  ? A ASP 13  
14  1 Y 1 A LEU 14  ? A LEU 14  
15  1 Y 1 A THR 15  ? A THR 15  
16  1 Y 1 A ASN 16  ? A ASN 16  
17  1 Y 1 A LYS 99  ? A LYS 99  
18  1 Y 1 A THR 100 ? A THR 100 
19  1 Y 1 A PHE 101 ? A PHE 101 
20  1 Y 1 A GLN 102 ? A GLN 102 
21  1 Y 1 A GLU 128 ? A GLU 128 
22  1 Y 1 A LYS 129 ? A LYS 129 
23  1 Y 1 A ASN 130 ? A ASN 130 
24  1 Y 1 A ASN 131 ? A ASN 131 
25  1 Y 1 A ASN 132 ? A ASN 132 
26  1 Y 1 A TYR 133 ? A TYR 133 
27  1 Y 1 A PHE 134 ? A PHE 134 
28  1 Y 1 A ARG 135 ? A ARG 135 
29  1 Y 1 A SER 343 ? A SER 343 
30  1 Y 1 A ALA 344 ? A ALA 344 
31  1 Y 1 A GLU 345 ? A GLU 345 
32  1 Y 1 A LYS 346 ? A LYS 346 
33  1 Y 1 A SER 347 ? A SER 347 
34  1 Y 1 A PHE 348 ? A PHE 348 
35  1 Y 1 A ASN 457 ? A ASN 457 
36  1 Y 1 A GLN 458 ? A GLN 458 
37  1 Y 1 A PRO 459 ? A PRO 459 
38  1 Y 1 A VAL 460 ? A VAL 460 
39  1 Y 1 A GLU 461 ? A GLU 461 
40  1 Y 1 A VAL 462 ? A VAL 462 
41  1 Y 1 A SER 463 ? A SER 463 
42  1 Y 1 A GLU 464 ? A GLU 464 
43  1 Y 1 A ASN 465 ? A ASN 465 
44  1 Y 1 A GLY 466 ? A GLY 466 
45  1 Y 1 A GLY 467 ? A GLY 467 
46  1 Y 1 A LEU 468 ? A LEU 468 
47  1 Y 1 A HIS 469 ? A HIS 469 
48  1 Y 1 A LEU 470 ? A LEU 470 
49  1 Y 1 A SER 471 ? A SER 471 
50  1 Y 1 A PRO 472 ? A PRO 472 
51  1 Y 1 A ARG 473 ? A ARG 473 
52  1 Y 1 A LYS 474 ? A LYS 474 
53  1 Y 1 A SER 475 ? A SER 475 
54  1 Y 1 A PHE 476 ? A PHE 476 
55  1 Y 1 A LEU 510 ? A LEU 510 
56  1 Y 1 A ARG 511 ? A ARG 511 
57  1 Y 1 A LYS 512 ? A LYS 512 
58  1 Y 1 A ILE 513 ? A ILE 513 
59  1 Y 1 A ASP 514 ? A ASP 514 
60  1 Y 1 A GLU 515 ? A GLU 515 
61  1 Y 1 A HIS 516 ? A HIS 516 
62  1 Y 1 A HIS 517 ? A HIS 517 
63  1 Y 1 A HIS 518 ? A HIS 518 
64  1 Y 1 A HIS 519 ? A HIS 519 
65  1 Y 1 A HIS 520 ? A HIS 520 
66  1 Y 1 A HIS 521 ? A HIS 521 
67  1 Y 1 B MET 1   ? B MET 1   
68  1 Y 1 B ASN 2   ? B ASN 2   
69  1 Y 1 B THR 3   ? B THR 3   
70  1 Y 1 B ASN 4   ? B ASN 4   
71  1 Y 1 B LYS 5   ? B LYS 5   
72  1 Y 1 B ASN 6   ? B ASN 6   
73  1 Y 1 B ASP 7   ? B ASP 7   
74  1 Y 1 B THR 8   ? B THR 8   
75  1 Y 1 B ALA 9   ? B ALA 9   
76  1 Y 1 B PHE 10  ? B PHE 10  
77  1 Y 1 B THR 11  ? B THR 11  
78  1 Y 1 B VAL 12  ? B VAL 12  
79  1 Y 1 B ASP 13  ? B ASP 13  
80  1 Y 1 B LEU 14  ? B LEU 14  
81  1 Y 1 B THR 15  ? B THR 15  
82  1 Y 1 B THR 97  ? B THR 97  
83  1 Y 1 B ILE 98  ? B ILE 98  
84  1 Y 1 B LYS 99  ? B LYS 99  
85  1 Y 1 B THR 100 ? B THR 100 
86  1 Y 1 B PHE 101 ? B PHE 101 
87  1 Y 1 B GLN 102 ? B GLN 102 
88  1 Y 1 B GLU 103 ? B GLU 103 
89  1 Y 1 B PRO 104 ? B PRO 104 
90  1 Y 1 B ILE 105 ? B ILE 105 
91  1 Y 1 B LEU 127 ? B LEU 127 
92  1 Y 1 B GLU 128 ? B GLU 128 
93  1 Y 1 B LYS 129 ? B LYS 129 
94  1 Y 1 B ASN 130 ? B ASN 130 
95  1 Y 1 B ASN 131 ? B ASN 131 
96  1 Y 1 B PHE 372 ? B PHE 372 
97  1 Y 1 B ASN 373 ? B ASN 373 
98  1 Y 1 B LYS 374 ? B LYS 374 
99  1 Y 1 B PRO 456 ? B PRO 456 
100 1 Y 1 B ASN 457 ? B ASN 457 
101 1 Y 1 B GLN 458 ? B GLN 458 
102 1 Y 1 B PRO 459 ? B PRO 459 
103 1 Y 1 B VAL 460 ? B VAL 460 
104 1 Y 1 B GLU 461 ? B GLU 461 
105 1 Y 1 B VAL 462 ? B VAL 462 
106 1 Y 1 B SER 463 ? B SER 463 
107 1 Y 1 B GLU 464 ? B GLU 464 
108 1 Y 1 B ASN 465 ? B ASN 465 
109 1 Y 1 B GLY 466 ? B GLY 466 
110 1 Y 1 B GLY 467 ? B GLY 467 
111 1 Y 1 B LEU 468 ? B LEU 468 
112 1 Y 1 B HIS 469 ? B HIS 469 
113 1 Y 1 B LEU 470 ? B LEU 470 
114 1 Y 1 B SER 471 ? B SER 471 
115 1 Y 1 B PRO 472 ? B PRO 472 
116 1 Y 1 B ARG 473 ? B ARG 473 
117 1 Y 1 B LYS 474 ? B LYS 474 
118 1 Y 1 B SER 475 ? B SER 475 
119 1 Y 1 B PHE 476 ? B PHE 476 
120 1 Y 1 B ILE 513 ? B ILE 513 
121 1 Y 1 B ASP 514 ? B ASP 514 
122 1 Y 1 B GLU 515 ? B GLU 515 
123 1 Y 1 B HIS 516 ? B HIS 516 
124 1 Y 1 B HIS 517 ? B HIS 517 
125 1 Y 1 B HIS 518 ? B HIS 518 
126 1 Y 1 B HIS 519 ? B HIS 519 
127 1 Y 1 B HIS 520 ? B HIS 520 
128 1 Y 1 B HIS 521 ? B HIS 521 
# 
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  
BLR CHA  C N N 74  
BLR NA   N Y N 75  
BLR C1A  C Y N 76  
BLR C2A  C Y N 77  
BLR C3A  C Y N 78  
BLR C4A  C Y N 79  
BLR CMA  C N N 80  
BLR CAA  C N N 81  
BLR CBA  C N N 82  
BLR CGA  C N N 83  
BLR O1A  O N N 84  
BLR O2A  O N N 85  
BLR CHB  C N N 86  
BLR NB   N N N 87  
BLR C1B  C N N 88  
BLR C2B  C N N 89  
BLR C3B  C N N 90  
BLR C4B  C N N 91  
BLR CMB  C N N 92  
BLR OB   O N N 93  
BLR CAB  C N N 94  
BLR CBB  C N N 95  
BLR NC   N N N 96  
BLR C1C  C N N 97  
BLR C2C  C N N 98  
BLR C3C  C N N 99  
BLR C4C  C N N 100 
BLR CMC  C N N 101 
BLR OC   O N N 102 
BLR CAC  C N N 103 
BLR CBC  C N N 104 
BLR CHD  C N N 105 
BLR ND   N Y N 106 
BLR C1D  C Y N 107 
BLR C2D  C Y N 108 
BLR C3D  C Y N 109 
BLR C4D  C Y N 110 
BLR CMD  C N N 111 
BLR CAD  C N N 112 
BLR CBD  C N N 113 
BLR CGD  C N N 114 
BLR O1D  O N N 115 
BLR O2D  O N N 116 
BLR H1   H N N 117 
BLR H2   H N N 118 
BLR H3   H N N 119 
BLR H4   H N N 120 
BLR H5   H N N 121 
BLR H6   H N N 122 
BLR H7   H N N 123 
BLR H8   H N N 124 
BLR H9   H N N 125 
BLR H10  H N N 126 
BLR H11  H N N 127 
BLR H12  H N N 128 
BLR H13  H N N 129 
BLR H14  H N N 130 
BLR H15  H N N 131 
BLR H16  H N N 132 
BLR H17  H N N 133 
BLR H18  H N N 134 
BLR H19  H N N 135 
BLR H20  H N N 136 
BLR H21  H N N 137 
BLR H22  H N N 138 
BLR H23  H N N 139 
BLR H24  H N N 140 
BLR H25  H N N 141 
BLR H26  H N N 142 
BLR H27  H N N 143 
BLR H28  H N N 144 
BLR H29  H N N 145 
BLR H30  H N N 146 
BLR H31  H N N 147 
BLR H32  H N N 148 
BLR H33  H N N 149 
BLR H34  H N N 150 
BLR H35  H N N 151 
BLR H36  H N N 152 
CYS N    N N N 153 
CYS CA   C N R 154 
CYS C    C N N 155 
CYS O    O N N 156 
CYS CB   C N N 157 
CYS SG   S N N 158 
CYS OXT  O N N 159 
CYS H    H N N 160 
CYS H2   H N N 161 
CYS HA   H N N 162 
CYS HB2  H N N 163 
CYS HB3  H N N 164 
CYS HG   H N N 165 
CYS HXT  H N N 166 
GLN N    N N N 167 
GLN CA   C N S 168 
GLN C    C N N 169 
GLN O    O N N 170 
GLN CB   C N N 171 
GLN CG   C N N 172 
GLN CD   C N N 173 
GLN OE1  O N N 174 
GLN NE2  N N N 175 
GLN OXT  O N N 176 
GLN H    H N N 177 
GLN H2   H N N 178 
GLN HA   H N N 179 
GLN HB2  H N N 180 
GLN HB3  H N N 181 
GLN HG2  H N N 182 
GLN HG3  H N N 183 
GLN HE21 H N N 184 
GLN HE22 H N N 185 
GLN HXT  H N N 186 
GLU N    N N N 187 
GLU CA   C N S 188 
GLU C    C N N 189 
GLU O    O N N 190 
GLU CB   C N N 191 
GLU CG   C N N 192 
GLU CD   C N N 193 
GLU OE1  O N N 194 
GLU OE2  O N N 195 
GLU OXT  O N N 196 
GLU H    H N N 197 
GLU H2   H N N 198 
GLU HA   H N N 199 
GLU HB2  H N N 200 
GLU HB3  H N N 201 
GLU HG2  H N N 202 
GLU HG3  H N N 203 
GLU HE2  H N N 204 
GLU HXT  H N N 205 
GLY N    N N N 206 
GLY CA   C N N 207 
GLY C    C N N 208 
GLY O    O N N 209 
GLY OXT  O N N 210 
GLY H    H N N 211 
GLY H2   H N N 212 
GLY HA2  H N N 213 
GLY HA3  H N N 214 
GLY HXT  H N N 215 
HIS N    N N N 216 
HIS CA   C N S 217 
HIS C    C N N 218 
HIS O    O N N 219 
HIS CB   C N N 220 
HIS CG   C Y N 221 
HIS ND1  N Y N 222 
HIS CD2  C Y N 223 
HIS CE1  C Y N 224 
HIS NE2  N Y N 225 
HIS OXT  O N N 226 
HIS H    H N N 227 
HIS H2   H N N 228 
HIS HA   H N N 229 
HIS HB2  H N N 230 
HIS HB3  H N N 231 
HIS HD1  H N N 232 
HIS HD2  H N N 233 
HIS HE1  H N N 234 
HIS HE2  H N N 235 
HIS HXT  H N N 236 
ILE N    N N N 237 
ILE CA   C N S 238 
ILE C    C N N 239 
ILE O    O N N 240 
ILE CB   C N S 241 
ILE CG1  C N N 242 
ILE CG2  C N N 243 
ILE CD1  C N N 244 
ILE OXT  O N N 245 
ILE H    H N N 246 
ILE H2   H N N 247 
ILE HA   H N N 248 
ILE HB   H N N 249 
ILE HG12 H N N 250 
ILE HG13 H N N 251 
ILE HG21 H N N 252 
ILE HG22 H N N 253 
ILE HG23 H N N 254 
ILE HD11 H N N 255 
ILE HD12 H N N 256 
ILE HD13 H N N 257 
ILE HXT  H N N 258 
LEU N    N N N 259 
LEU CA   C N S 260 
LEU C    C N N 261 
LEU O    O N N 262 
LEU CB   C N N 263 
LEU CG   C N N 264 
LEU CD1  C N N 265 
LEU CD2  C N N 266 
LEU OXT  O N N 267 
LEU H    H N N 268 
LEU H2   H N N 269 
LEU HA   H N N 270 
LEU HB2  H N N 271 
LEU HB3  H N N 272 
LEU HG   H N N 273 
LEU HD11 H N N 274 
LEU HD12 H N N 275 
LEU HD13 H N N 276 
LEU HD21 H N N 277 
LEU HD22 H N N 278 
LEU HD23 H N N 279 
LEU HXT  H N N 280 
LYS N    N N N 281 
LYS CA   C N S 282 
LYS C    C N N 283 
LYS O    O N N 284 
LYS CB   C N N 285 
LYS CG   C N N 286 
LYS CD   C N N 287 
LYS CE   C N N 288 
LYS NZ   N N N 289 
LYS OXT  O N N 290 
LYS H    H N N 291 
LYS H2   H N N 292 
LYS HA   H N N 293 
LYS HB2  H N N 294 
LYS HB3  H N N 295 
LYS HG2  H N N 296 
LYS HG3  H N N 297 
LYS HD2  H N N 298 
LYS HD3  H N N 299 
LYS HE2  H N N 300 
LYS HE3  H N N 301 
LYS HZ1  H N N 302 
LYS HZ2  H N N 303 
LYS HZ3  H N N 304 
LYS HXT  H N N 305 
MET N    N N N 306 
MET CA   C N S 307 
MET C    C N N 308 
MET O    O N N 309 
MET CB   C N N 310 
MET CG   C N N 311 
MET SD   S N N 312 
MET CE   C N N 313 
MET OXT  O N N 314 
MET H    H N N 315 
MET H2   H N N 316 
MET HA   H N N 317 
MET HB2  H N N 318 
MET HB3  H N N 319 
MET HG2  H N N 320 
MET HG3  H N N 321 
MET HE1  H N N 322 
MET HE2  H N N 323 
MET HE3  H N N 324 
MET HXT  H N N 325 
PHE N    N N N 326 
PHE CA   C N S 327 
PHE C    C N N 328 
PHE O    O N N 329 
PHE CB   C N N 330 
PHE CG   C Y N 331 
PHE CD1  C Y N 332 
PHE CD2  C Y N 333 
PHE CE1  C Y N 334 
PHE CE2  C Y N 335 
PHE CZ   C Y N 336 
PHE OXT  O N N 337 
PHE H    H N N 338 
PHE H2   H N N 339 
PHE HA   H N N 340 
PHE HB2  H N N 341 
PHE HB3  H N N 342 
PHE HD1  H N N 343 
PHE HD2  H N N 344 
PHE HE1  H N N 345 
PHE HE2  H N N 346 
PHE HZ   H N N 347 
PHE HXT  H N N 348 
PRO N    N N N 349 
PRO CA   C N S 350 
PRO C    C N N 351 
PRO O    O N N 352 
PRO CB   C N N 353 
PRO CG   C N N 354 
PRO CD   C N N 355 
PRO OXT  O N N 356 
PRO H    H N N 357 
PRO HA   H N N 358 
PRO HB2  H N N 359 
PRO HB3  H N N 360 
PRO HG2  H N N 361 
PRO HG3  H N N 362 
PRO HD2  H N N 363 
PRO HD3  H N N 364 
PRO HXT  H N N 365 
SER N    N N N 366 
SER CA   C N S 367 
SER C    C N N 368 
SER O    O N N 369 
SER CB   C N N 370 
SER OG   O N N 371 
SER OXT  O N N 372 
SER H    H N N 373 
SER H2   H N N 374 
SER HA   H N N 375 
SER HB2  H N N 376 
SER HB3  H N N 377 
SER HG   H N N 378 
SER HXT  H N N 379 
THR N    N N N 380 
THR CA   C N S 381 
THR C    C N N 382 
THR O    O N N 383 
THR CB   C N R 384 
THR OG1  O N N 385 
THR CG2  C N N 386 
THR OXT  O N N 387 
THR H    H N N 388 
THR H2   H N N 389 
THR HA   H N N 390 
THR HB   H N N 391 
THR HG1  H N N 392 
THR HG21 H N N 393 
THR HG22 H N N 394 
THR HG23 H N N 395 
THR HXT  H N N 396 
TRP N    N N N 397 
TRP CA   C N S 398 
TRP C    C N N 399 
TRP O    O N N 400 
TRP CB   C N N 401 
TRP CG   C Y N 402 
TRP CD1  C Y N 403 
TRP CD2  C Y N 404 
TRP NE1  N Y N 405 
TRP CE2  C Y N 406 
TRP CE3  C Y N 407 
TRP CZ2  C Y N 408 
TRP CZ3  C Y N 409 
TRP CH2  C Y N 410 
TRP OXT  O N N 411 
TRP H    H N N 412 
TRP H2   H N N 413 
TRP HA   H N N 414 
TRP HB2  H N N 415 
TRP HB3  H N N 416 
TRP HD1  H N N 417 
TRP HE1  H N N 418 
TRP HE3  H N N 419 
TRP HZ2  H N N 420 
TRP HZ3  H N N 421 
TRP HH2  H N N 422 
TRP HXT  H N N 423 
TYR N    N N N 424 
TYR CA   C N S 425 
TYR C    C N N 426 
TYR O    O N N 427 
TYR CB   C N N 428 
TYR CG   C Y N 429 
TYR CD1  C Y N 430 
TYR CD2  C Y N 431 
TYR CE1  C Y N 432 
TYR CE2  C Y N 433 
TYR CZ   C Y N 434 
TYR OH   O N N 435 
TYR OXT  O N N 436 
TYR H    H N N 437 
TYR H2   H N N 438 
TYR HA   H N N 439 
TYR HB2  H N N 440 
TYR HB3  H N N 441 
TYR HD1  H N N 442 
TYR HD2  H N N 443 
TYR HE1  H N N 444 
TYR HE2  H N N 445 
TYR HH   H N N 446 
TYR HXT  H N N 447 
VAL N    N N N 448 
VAL CA   C N S 449 
VAL C    C N N 450 
VAL O    O N N 451 
VAL CB   C N N 452 
VAL CG1  C N N 453 
VAL CG2  C N N 454 
VAL OXT  O N N 455 
VAL H    H N N 456 
VAL H2   H N N 457 
VAL HA   H N N 458 
VAL HB   H N N 459 
VAL HG11 H N N 460 
VAL HG12 H N N 461 
VAL HG13 H N N 462 
VAL HG21 H N N 463 
VAL HG22 H N N 464 
VAL HG23 H N N 465 
VAL HXT  H N N 466 
# 
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  
BLR CMB C2B  sing N N 70  
BLR CAB CBB  doub N N 71  
BLR CAB C3B  sing N N 72  
BLR C2B C3B  doub N N 73  
BLR C2B C1B  sing N N 74  
BLR C3B C4B  sing N N 75  
BLR CMA C3A  sing N N 76  
BLR CHB C1B  doub N Z 77  
BLR CHB C4A  sing N N 78  
BLR C1B NB   sing N N 79  
BLR C4B NB   sing N N 80  
BLR C4B OB   doub N N 81  
BLR C3A C4A  doub Y N 82  
BLR C3A C2A  sing Y N 83  
BLR C4A NA   sing Y N 84  
BLR C2A CAA  sing N N 85  
BLR C2A C1A  doub Y N 86  
BLR CAA CBA  sing N N 87  
BLR O2A CGA  doub N N 88  
BLR NA  C1A  sing Y N 89  
BLR CBA CGA  sing N N 90  
BLR CGA O1A  sing N N 91  
BLR C1A CHA  sing N N 92  
BLR CHA C4D  sing N N 93  
BLR O2D CGD  doub N N 94  
BLR CAD C3D  sing N N 95  
BLR CAD CBD  sing N N 96  
BLR C4D C3D  doub Y N 97  
BLR C4D ND   sing Y N 98  
BLR C3D C2D  sing Y N 99  
BLR CGD CBD  sing N N 100 
BLR CGD O1D  sing N N 101 
BLR ND  C1D  sing Y N 102 
BLR C2D CMD  sing N N 103 
BLR C2D C1D  doub Y N 104 
BLR C1D CHD  sing N N 105 
BLR CHD C4C  doub N Z 106 
BLR C4C NC   sing N N 107 
BLR C4C C3C  sing N N 108 
BLR NC  C1C  sing N N 109 
BLR CAC C3C  sing N N 110 
BLR CAC CBC  doub N N 111 
BLR C3C C2C  doub N N 112 
BLR C1C C2C  sing N N 113 
BLR C1C OC   doub N N 114 
BLR C2C CMC  sing N N 115 
BLR CHA H1   sing N N 116 
BLR CHA H2   sing N N 117 
BLR NA  H3   sing N N 118 
BLR CMA H4   sing N N 119 
BLR CMA H5   sing N N 120 
BLR CMA H6   sing N N 121 
BLR CAA H7   sing N N 122 
BLR CAA H8   sing N N 123 
BLR CBA H9   sing N N 124 
BLR CBA H10  sing N N 125 
BLR O1A H11  sing N N 126 
BLR CHB H12  sing N N 127 
BLR NB  H13  sing N N 128 
BLR CMB H14  sing N N 129 
BLR CMB H15  sing N N 130 
BLR CMB H16  sing N N 131 
BLR CAB H17  sing N N 132 
BLR CBB H18  sing N N 133 
BLR CBB H19  sing N N 134 
BLR NC  H20  sing N N 135 
BLR CMC H21  sing N N 136 
BLR CMC H22  sing N N 137 
BLR CMC H23  sing N N 138 
BLR CAC H24  sing N N 139 
BLR CBC H25  sing N N 140 
BLR CBC H26  sing N N 141 
BLR CHD H27  sing N N 142 
BLR ND  H28  sing N N 143 
BLR CMD H29  sing N N 144 
BLR CMD H30  sing N N 145 
BLR CMD H31  sing N N 146 
BLR CAD H32  sing N N 147 
BLR CAD H33  sing N N 148 
BLR CBD H34  sing N N 149 
BLR CBD H35  sing N N 150 
BLR O1D H36  sing N N 151 
CYS N   CA   sing N N 152 
CYS N   H    sing N N 153 
CYS N   H2   sing N N 154 
CYS CA  C    sing N N 155 
CYS CA  CB   sing N N 156 
CYS CA  HA   sing N N 157 
CYS C   O    doub N N 158 
CYS C   OXT  sing N N 159 
CYS CB  SG   sing N N 160 
CYS CB  HB2  sing N N 161 
CYS CB  HB3  sing N N 162 
CYS SG  HG   sing N N 163 
CYS OXT HXT  sing N N 164 
GLN N   CA   sing N N 165 
GLN N   H    sing N N 166 
GLN N   H2   sing N N 167 
GLN CA  C    sing N N 168 
GLN CA  CB   sing N N 169 
GLN CA  HA   sing N N 170 
GLN C   O    doub N N 171 
GLN C   OXT  sing N N 172 
GLN CB  CG   sing N N 173 
GLN CB  HB2  sing N N 174 
GLN CB  HB3  sing N N 175 
GLN CG  CD   sing N N 176 
GLN CG  HG2  sing N N 177 
GLN CG  HG3  sing N N 178 
GLN CD  OE1  doub N N 179 
GLN CD  NE2  sing N N 180 
GLN NE2 HE21 sing N N 181 
GLN NE2 HE22 sing N N 182 
GLN OXT HXT  sing N N 183 
GLU N   CA   sing N N 184 
GLU N   H    sing N N 185 
GLU N   H2   sing N N 186 
GLU CA  C    sing N N 187 
GLU CA  CB   sing N N 188 
GLU CA  HA   sing N N 189 
GLU C   O    doub N N 190 
GLU C   OXT  sing N N 191 
GLU CB  CG   sing N N 192 
GLU CB  HB2  sing N N 193 
GLU CB  HB3  sing N N 194 
GLU CG  CD   sing N N 195 
GLU CG  HG2  sing N N 196 
GLU CG  HG3  sing N N 197 
GLU CD  OE1  doub N N 198 
GLU CD  OE2  sing N N 199 
GLU OE2 HE2  sing N N 200 
GLU OXT HXT  sing N N 201 
GLY N   CA   sing N N 202 
GLY N   H    sing N N 203 
GLY N   H2   sing N N 204 
GLY CA  C    sing N N 205 
GLY CA  HA2  sing N N 206 
GLY CA  HA3  sing N N 207 
GLY C   O    doub N N 208 
GLY C   OXT  sing N N 209 
GLY OXT HXT  sing N N 210 
HIS N   CA   sing N N 211 
HIS N   H    sing N N 212 
HIS N   H2   sing N N 213 
HIS CA  C    sing N N 214 
HIS CA  CB   sing N N 215 
HIS CA  HA   sing N N 216 
HIS C   O    doub N N 217 
HIS C   OXT  sing N N 218 
HIS CB  CG   sing N N 219 
HIS CB  HB2  sing N N 220 
HIS CB  HB3  sing N N 221 
HIS CG  ND1  sing Y N 222 
HIS CG  CD2  doub Y N 223 
HIS ND1 CE1  doub Y N 224 
HIS ND1 HD1  sing N N 225 
HIS CD2 NE2  sing Y N 226 
HIS CD2 HD2  sing N N 227 
HIS CE1 NE2  sing Y N 228 
HIS CE1 HE1  sing N N 229 
HIS NE2 HE2  sing N N 230 
HIS OXT HXT  sing N N 231 
ILE N   CA   sing N N 232 
ILE N   H    sing N N 233 
ILE N   H2   sing N N 234 
ILE CA  C    sing N N 235 
ILE CA  CB   sing N N 236 
ILE CA  HA   sing N N 237 
ILE C   O    doub N N 238 
ILE C   OXT  sing N N 239 
ILE CB  CG1  sing N N 240 
ILE CB  CG2  sing N N 241 
ILE CB  HB   sing N N 242 
ILE CG1 CD1  sing N N 243 
ILE CG1 HG12 sing N N 244 
ILE CG1 HG13 sing N N 245 
ILE CG2 HG21 sing N N 246 
ILE CG2 HG22 sing N N 247 
ILE CG2 HG23 sing N N 248 
ILE CD1 HD11 sing N N 249 
ILE CD1 HD12 sing N N 250 
ILE CD1 HD13 sing N N 251 
ILE OXT HXT  sing N N 252 
LEU N   CA   sing N N 253 
LEU N   H    sing N N 254 
LEU N   H2   sing N N 255 
LEU CA  C    sing N N 256 
LEU CA  CB   sing N N 257 
LEU CA  HA   sing N N 258 
LEU C   O    doub N N 259 
LEU C   OXT  sing N N 260 
LEU CB  CG   sing N N 261 
LEU CB  HB2  sing N N 262 
LEU CB  HB3  sing N N 263 
LEU CG  CD1  sing N N 264 
LEU CG  CD2  sing N N 265 
LEU CG  HG   sing N N 266 
LEU CD1 HD11 sing N N 267 
LEU CD1 HD12 sing N N 268 
LEU CD1 HD13 sing N N 269 
LEU CD2 HD21 sing N N 270 
LEU CD2 HD22 sing N N 271 
LEU CD2 HD23 sing N N 272 
LEU OXT HXT  sing N N 273 
LYS N   CA   sing N N 274 
LYS N   H    sing N N 275 
LYS N   H2   sing N N 276 
LYS CA  C    sing N N 277 
LYS CA  CB   sing N N 278 
LYS CA  HA   sing N N 279 
LYS C   O    doub N N 280 
LYS C   OXT  sing N N 281 
LYS CB  CG   sing N N 282 
LYS CB  HB2  sing N N 283 
LYS CB  HB3  sing N N 284 
LYS CG  CD   sing N N 285 
LYS CG  HG2  sing N N 286 
LYS CG  HG3  sing N N 287 
LYS CD  CE   sing N N 288 
LYS CD  HD2  sing N N 289 
LYS CD  HD3  sing N N 290 
LYS CE  NZ   sing N N 291 
LYS CE  HE2  sing N N 292 
LYS CE  HE3  sing N N 293 
LYS NZ  HZ1  sing N N 294 
LYS NZ  HZ2  sing N N 295 
LYS NZ  HZ3  sing N N 296 
LYS OXT HXT  sing N N 297 
MET N   CA   sing N N 298 
MET N   H    sing N N 299 
MET N   H2   sing N N 300 
MET CA  C    sing N N 301 
MET CA  CB   sing N N 302 
MET CA  HA   sing N N 303 
MET C   O    doub N N 304 
MET C   OXT  sing N N 305 
MET CB  CG   sing N N 306 
MET CB  HB2  sing N N 307 
MET CB  HB3  sing N N 308 
MET CG  SD   sing N N 309 
MET CG  HG2  sing N N 310 
MET CG  HG3  sing N N 311 
MET SD  CE   sing N N 312 
MET CE  HE1  sing N N 313 
MET CE  HE2  sing N N 314 
MET CE  HE3  sing N N 315 
MET OXT HXT  sing N N 316 
PHE N   CA   sing N N 317 
PHE N   H    sing N N 318 
PHE N   H2   sing N N 319 
PHE CA  C    sing N N 320 
PHE CA  CB   sing N N 321 
PHE CA  HA   sing N N 322 
PHE C   O    doub N N 323 
PHE C   OXT  sing N N 324 
PHE CB  CG   sing N N 325 
PHE CB  HB2  sing N N 326 
PHE CB  HB3  sing N N 327 
PHE CG  CD1  doub Y N 328 
PHE CG  CD2  sing Y N 329 
PHE CD1 CE1  sing Y N 330 
PHE CD1 HD1  sing N N 331 
PHE CD2 CE2  doub Y N 332 
PHE CD2 HD2  sing N N 333 
PHE CE1 CZ   doub Y N 334 
PHE CE1 HE1  sing N N 335 
PHE CE2 CZ   sing Y N 336 
PHE CE2 HE2  sing N N 337 
PHE CZ  HZ   sing N N 338 
PHE OXT HXT  sing N N 339 
PRO N   CA   sing N N 340 
PRO N   CD   sing N N 341 
PRO N   H    sing N N 342 
PRO CA  C    sing N N 343 
PRO CA  CB   sing N N 344 
PRO CA  HA   sing N N 345 
PRO C   O    doub N N 346 
PRO C   OXT  sing N N 347 
PRO CB  CG   sing N N 348 
PRO CB  HB2  sing N N 349 
PRO CB  HB3  sing N N 350 
PRO CG  CD   sing N N 351 
PRO CG  HG2  sing N N 352 
PRO CG  HG3  sing N N 353 
PRO CD  HD2  sing N N 354 
PRO CD  HD3  sing N N 355 
PRO OXT HXT  sing N N 356 
SER N   CA   sing N N 357 
SER N   H    sing N N 358 
SER N   H2   sing N N 359 
SER CA  C    sing N N 360 
SER CA  CB   sing N N 361 
SER CA  HA   sing N N 362 
SER C   O    doub N N 363 
SER C   OXT  sing N N 364 
SER CB  OG   sing N N 365 
SER CB  HB2  sing N N 366 
SER CB  HB3  sing N N 367 
SER OG  HG   sing N N 368 
SER OXT HXT  sing N N 369 
THR N   CA   sing N N 370 
THR N   H    sing N N 371 
THR N   H2   sing N N 372 
THR CA  C    sing N N 373 
THR CA  CB   sing N N 374 
THR CA  HA   sing N N 375 
THR C   O    doub N N 376 
THR C   OXT  sing N N 377 
THR CB  OG1  sing N N 378 
THR CB  CG2  sing N N 379 
THR CB  HB   sing N N 380 
THR OG1 HG1  sing N N 381 
THR CG2 HG21 sing N N 382 
THR CG2 HG22 sing N N 383 
THR CG2 HG23 sing N N 384 
THR OXT HXT  sing N N 385 
TRP N   CA   sing N N 386 
TRP N   H    sing N N 387 
TRP N   H2   sing N N 388 
TRP CA  C    sing N N 389 
TRP CA  CB   sing N N 390 
TRP CA  HA   sing N N 391 
TRP C   O    doub N N 392 
TRP C   OXT  sing N N 393 
TRP CB  CG   sing N N 394 
TRP CB  HB2  sing N N 395 
TRP CB  HB3  sing N N 396 
TRP CG  CD1  doub Y N 397 
TRP CG  CD2  sing Y N 398 
TRP CD1 NE1  sing Y N 399 
TRP CD1 HD1  sing N N 400 
TRP CD2 CE2  doub Y N 401 
TRP CD2 CE3  sing Y N 402 
TRP NE1 CE2  sing Y N 403 
TRP NE1 HE1  sing N N 404 
TRP CE2 CZ2  sing Y N 405 
TRP CE3 CZ3  doub Y N 406 
TRP CE3 HE3  sing N N 407 
TRP CZ2 CH2  doub Y N 408 
TRP CZ2 HZ2  sing N N 409 
TRP CZ3 CH2  sing Y N 410 
TRP CZ3 HZ3  sing N N 411 
TRP CH2 HH2  sing N N 412 
TRP OXT HXT  sing N N 413 
TYR N   CA   sing N N 414 
TYR N   H    sing N N 415 
TYR N   H2   sing N N 416 
TYR CA  C    sing N N 417 
TYR CA  CB   sing N N 418 
TYR CA  HA   sing N N 419 
TYR C   O    doub N N 420 
TYR C   OXT  sing N N 421 
TYR CB  CG   sing N N 422 
TYR CB  HB2  sing N N 423 
TYR CB  HB3  sing N N 424 
TYR CG  CD1  doub Y N 425 
TYR CG  CD2  sing Y N 426 
TYR CD1 CE1  sing Y N 427 
TYR CD1 HD1  sing N N 428 
TYR CD2 CE2  doub Y N 429 
TYR CD2 HD2  sing N N 430 
TYR CE1 CZ   doub Y N 431 
TYR CE1 HE1  sing N N 432 
TYR CE2 CZ   sing Y N 433 
TYR CE2 HE2  sing N N 434 
TYR CZ  OH   sing N N 435 
TYR OH  HH   sing N N 436 
TYR OXT HXT  sing N N 437 
VAL N   CA   sing N N 438 
VAL N   H    sing N N 439 
VAL N   H2   sing N N 440 
VAL CA  C    sing N N 441 
VAL CA  CB   sing N N 442 
VAL CA  HA   sing N N 443 
VAL C   O    doub N N 444 
VAL C   OXT  sing N N 445 
VAL CB  CG1  sing N N 446 
VAL CB  CG2  sing N N 447 
VAL CB  HB   sing N N 448 
VAL CG1 HG11 sing N N 449 
VAL CG1 HG12 sing N N 450 
VAL CG1 HG13 sing N N 451 
VAL CG2 HG21 sing N N 452 
VAL CG2 HG22 sing N N 453 
VAL CG2 HG23 sing N N 454 
VAL OXT HXT  sing N N 455 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'Other government'                          ?                    KGM1002311         1 
'National Research Foundation (NRF, Korea)' 'Korea, Republic Of' 2020M3A9G710393422 2 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   6BAP 
_pdbx_initial_refinement_model.details          ? 
# 
_space_group.name_H-M_alt     'C 1 2 1' 
_space_group.name_Hall        'C 2y' 
_space_group.IT_number        5 
_space_group.crystal_system   monoclinic 
_space_group.id               1 
# 
_atom_sites.entry_id                    9JRY 
_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]   0.009565 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.001540 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.006797 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   0.000000 
_atom_sites.fract_transf_matrix[3][3]   0.011500 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C ? ? 5.96793  ? ? ? 14.89577 ? ? ? 0.0 
;1-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N ? ? 6.96715  ? ? ? 11.43723 ? ? ? 0.0 
;1-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O ? ? 7.96527  ? ? ? 9.05267  ? ? ? 0.0 
;1-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S ? ? 15.91112 ? ? ? 10.84690 ? ? ? 0.0 
;1-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
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   . CYS A 1 17  ? 33.37000  -14.15800 28.54100 1.000 43.61000 ? 17  CYS A N   1 
ATOM   2    C CA  . CYS A 1 17  ? 32.08000  -13.48900 28.42500 1.000 43.61000 ? 17  CYS A CA  1 
ATOM   3    C C   . CYS A 1 17  ? 32.27000  -11.97800 28.43000 1.000 43.61000 ? 17  CYS A C   1 
ATOM   4    O O   . CYS A 1 17  ? 31.83000  -11.28500 27.51100 1.000 43.61000 ? 17  CYS A O   1 
ATOM   5    C CB  . CYS A 1 17  ? 31.14600  -13.91400 29.55900 1.000 43.61000 ? 17  CYS A CB  1 
ATOM   6    S SG  . CYS A 1 17  ? 29.39000  -13.59300 29.25500 1.000 43.61000 ? 17  CYS A SG  1 
ATOM   7    N N   . ASP A 1 18  ? 32.91800  -11.46300 29.47600 1.000 47.86000 ? 18  ASP A N   1 
ATOM   8    C CA  . ASP A 1 18  ? 33.29500  -10.05600 29.46900 1.000 47.86000 ? 18  ASP A CA  1 
ATOM   9    C C   . ASP A 1 18  ? 34.47600  -9.79200  28.54500 1.000 47.86000 ? 18  ASP A C   1 
ATOM   10   O O   . ASP A 1 18  ? 34.72600  -8.63600  28.18500 1.000 47.86000 ? 18  ASP A O   1 
ATOM   11   C CB  . ASP A 1 18  ? 33.61500  -9.58400  30.88900 1.000 47.86000 ? 18  ASP A CB  1 
ATOM   12   C CG  . ASP A 1 18  ? 34.78000  -10.33400 31.50600 1.000 47.86000 ? 18  ASP A CG  1 
ATOM   13   O OD1 . ASP A 1 18  ? 35.05300  -11.47600 31.07600 1.000 47.86000 ? 18  ASP A OD1 1 
ATOM   14   O OD2 . ASP A 1 18  ? 35.41700  -9.78200  32.42900 1.000 47.86000 ? 18  ASP A OD2 1 
ATOM   15   N N   . LYS A 1 19  ? 35.21300  -10.83600 28.16900 1.000 48.47000 ? 19  LYS A N   1 
ATOM   16   C CA  . LYS A 1 19  ? 36.27200  -10.71900 27.17600 1.000 48.47000 ? 19  LYS A CA  1 
ATOM   17   C C   . LYS A 1 19  ? 35.73900  -10.65200 25.75000 1.000 48.47000 ? 19  LYS A C   1 
ATOM   18   O O   . LYS A 1 19  ? 36.44800  -10.16900 24.85900 1.000 48.47000 ? 19  LYS A O   1 
ATOM   19   C CB  . LYS A 1 19  ? 37.23100  -11.90100 27.31800 1.000 48.47000 ? 19  LYS A CB  1 
ATOM   20   C CG  . LYS A 1 19  ? 36.51100  -13.23100 27.47400 1.000 48.47000 ? 19  LYS A CG  1 
ATOM   21   C CD  . LYS A 1 19  ? 37.47900  -14.38900 27.62400 1.000 48.47000 ? 19  LYS A CD  1 
ATOM   22   C CE  . LYS A 1 19  ? 36.73400  -15.67100 27.95400 1.000 48.47000 ? 19  LYS A CE  1 
ATOM   23   N NZ  . LYS A 1 19  ? 35.63300  -15.93400 26.98400 1.000 48.47000 ? 19  LYS A NZ  1 
ATOM   24   N N   . GLU A 1 20  ? 34.51400  -11.11300 25.52100 1.000 43.35000 ? 20  GLU A N   1 
ATOM   25   C CA  . GLU A 1 20  ? 33.96800  -11.17200 24.16900 1.000 43.35000 ? 20  GLU A CA  1 
ATOM   26   C C   . GLU A 1 20  ? 33.66800  -9.76800  23.65400 1.000 43.35000 ? 20  GLU A C   1 
ATOM   27   O O   . GLU A 1 20  ? 32.96300  -9.00400  24.32400 1.000 43.35000 ? 20  GLU A O   1 
ATOM   28   C CB  . GLU A 1 20  ? 32.70100  -12.02400 24.15500 1.000 43.35000 ? 20  GLU A CB  1 
ATOM   29   C CG  . GLU A 1 20  ? 31.82300  -11.82800 22.93200 1.000 43.35000 ? 20  GLU A CG  1 
ATOM   30   C CD  . GLU A 1 20  ? 30.52500  -12.60900 23.02200 1.000 43.35000 ? 20  GLU A CD  1 
ATOM   31   O OE1 . GLU A 1 20  ? 30.49600  -13.63700 23.73100 1.000 43.35000 ? 20  GLU A OE1 1 
ATOM   32   O OE2 . GLU A 1 20  ? 29.53300  -12.19100 22.38900 1.000 43.35000 ? 20  GLU A OE2 1 
ATOM   33   N N   . PRO A 1 21  ? 34.17500  -9.39300  22.47700 1.000 39.55000 ? 21  PRO A N   1 
ATOM   34   C CA  . PRO A 1 21  ? 33.87300  -8.06300  21.93300 1.000 39.55000 ? 21  PRO A CA  1 
ATOM   35   C C   . PRO A 1 21  ? 32.54000  -8.01500  21.20100 1.000 39.55000 ? 21  PRO A C   1 
ATOM   36   O O   . PRO A 1 21  ? 32.48600  -8.17700  19.97800 1.000 39.55000 ? 21  PRO A O   1 
ATOM   37   C CB  . PRO A 1 21  ? 35.04800  -7.80600  20.98200 1.000 39.55000 ? 21  PRO A CB  1 
ATOM   38   C CG  . PRO A 1 21  ? 35.44300  -9.17100  20.51900 1.000 39.55000 ? 21  PRO A CG  1 
ATOM   39   C CD  . PRO A 1 21  ? 35.16000  -10.12100 21.65800 1.000 39.55000 ? 21  PRO A CD  1 
ATOM   40   N N   . ILE A 1 22  ? 31.45300  -7.78800  21.94300 1.000 33.34000 ? 22  ILE A N   1 
ATOM   41   C CA  . ILE A 1 22  ? 30.14200  -7.66700  21.31900 1.000 33.34000 ? 22  ILE A CA  1 
ATOM   42   C C   . ILE A 1 22  ? 30.04400  -6.41900  20.45200 1.000 33.34000 ? 22  ILE A C   1 
ATOM   43   O O   . ILE A 1 22  ? 29.17800  -6.34800  19.57300 1.000 33.34000 ? 22  ILE A O   1 
ATOM   44   C CB  . ILE A 1 22  ? 29.03100  -7.67600  22.38400 1.000 33.34000 ? 22  ILE A CB  1 
ATOM   45   C CG1 . ILE A 1 22  ? 29.26200  -6.56800  23.41200 1.000 33.34000 ? 22  ILE A CG1 1 
ATOM   46   C CG2 . ILE A 1 22  ? 28.95700  -9.03000  23.07000 1.000 33.34000 ? 22  ILE A CG2 1 
ATOM   47   C CD1 . ILE A 1 22  ? 28.22900  -6.54600  24.51200 1.000 33.34000 ? 22  ILE A CD1 1 
ATOM   48   N N   . HIS A 1 23  ? 30.90500  -5.42400  20.68100 1.000 29.53000 ? 23  HIS A N   1 
ATOM   49   C CA  . HIS A 1 23  ? 30.82600  -4.17800  19.92700 1.000 29.53000 ? 23  HIS A CA  1 
ATOM   50   C C   . HIS A 1 23  ? 31.30300  -4.32700  18.48700 1.000 29.53000 ? 23  HIS A C   1 
ATOM   51   O O   . HIS A 1 23  ? 31.02800  -3.44500  17.66700 1.000 29.53000 ? 23  HIS A O   1 
ATOM   52   C CB  . HIS A 1 23  ? 31.62900  -3.08400  20.63100 1.000 29.53000 ? 23  HIS A CB  1 
ATOM   53   C CG  . HIS A 1 23  ? 33.09600  -3.36900  20.71600 1.000 29.53000 ? 23  HIS A CG  1 
ATOM   54   N ND1 . HIS A 1 23  ? 33.99200  -2.95400  19.75400 1.000 29.53000 ? 23  HIS A ND1 1 
ATOM   55   C CD2 . HIS A 1 23  ? 33.82300  -4.03000  21.64700 1.000 29.53000 ? 23  HIS A CD2 1 
ATOM   56   C CE1 . HIS A 1 23  ? 35.20800  -3.34500  20.09100 1.000 29.53000 ? 23  HIS A CE1 1 
ATOM   57   N NE2 . HIS A 1 23  ? 35.13300  -4.00000  21.23500 1.000 29.53000 ? 23  HIS A NE2 1 
ATOM   58   N N   . ILE A 1 24  ? 31.99800  -5.41100  18.15400 1.000 27.65000 ? 24  ILE A N   1 
ATOM   59   C CA  . ILE A 1 24  ? 32.42300  -5.64700  16.77400 1.000 27.65000 ? 24  ILE A CA  1 
ATOM   60   C C   . ILE A 1 24  ? 32.05400  -7.07200  16.37200 1.000 27.65000 ? 24  ILE A C   1 
ATOM   61   O O   . ILE A 1 24  ? 32.94400  -7.90800  16.15700 1.000 27.65000 ? 24  ILE A O   1 
ATOM   62   C CB  . ILE A 1 24  ? 33.93100  -5.39100  16.60800 1.000 27.65000 ? 24  ILE A CB  1 
ATOM   63   C CG1 . ILE A 1 24  ? 34.72000  -6.00800  17.76600 1.000 27.65000 ? 24  ILE A CG1 1 
ATOM   64   C CG2 . ILE A 1 24  ? 34.22100  -3.90400  16.53700 1.000 27.65000 ? 24  ILE A CG2 1 
ATOM   65   C CD1 . ILE A 1 24  ? 36.22200  -5.84100  17.63600 1.000 27.65000 ? 24  ILE A CD1 1 
ATOM   66   N N   . PRO A 1 25  ? 30.76000  -7.39100  16.24100 1.000 27.95000 ? 25  PRO A N   1 
ATOM   67   C CA  . PRO A 1 25  ? 30.37600  -8.75900  15.86200 1.000 27.95000 ? 25  PRO A CA  1 
ATOM   68   C C   . PRO A 1 25  ? 30.63900  -9.11400  14.40800 1.000 27.95000 ? 25  PRO A C   1 
ATOM   69   O O   . PRO A 1 25  ? 30.69600  -10.30900 14.08700 1.000 27.95000 ? 25  PRO A O   1 
ATOM   70   C CB  . PRO A 1 25  ? 28.87200  -8.79400  16.16500 1.000 27.95000 ? 25  PRO A CB  1 
ATOM   71   C CG  . PRO A 1 25  ? 28.43400  -7.38800  15.97100 1.000 27.95000 ? 25  PRO A CG  1 
ATOM   72   C CD  . PRO A 1 25  ? 29.58600  -6.51800  16.41300 1.000 27.95000 ? 25  PRO A CD  1 
ATOM   73   N N   . GLY A 1 26  ? 30.78200  -8.13400  13.51900 1.000 25.44000 ? 26  GLY A N   1 
ATOM   74   C CA  . GLY A 1 26  ? 30.88400  -8.43100  12.10500 1.000 25.44000 ? 26  GLY A CA  1 
ATOM   75   C C   . GLY A 1 26  ? 29.57300  -8.77400  11.43500 1.000 25.44000 ? 26  GLY A C   1 
ATOM   76   O O   . GLY A 1 26  ? 29.58600  -9.27300  10.30400 1.000 25.44000 ? 26  GLY A O   1 
ATOM   77   N N   . PHE A 1 27  ? 28.44200  -8.52400  12.09400 1.000 25.16000 ? 27  PHE A N   1 
ATOM   78   C CA  . PHE A 1 27  ? 27.12700  -8.88200  11.58100 1.000 25.16000 ? 27  PHE A CA  1 
ATOM   79   C C   . PHE A 1 27  ? 26.13700  -7.77900  11.92500 1.000 25.16000 ? 27  PHE A C   1 
ATOM   80   O O   . PHE A 1 27  ? 26.39300  -6.93800  12.78900 1.000 25.16000 ? 27  PHE A O   1 
ATOM   81   C CB  . PHE A 1 27  ? 26.62500  -10.21200 12.16300 1.000 25.16000 ? 27  PHE A CB  1 
ATOM   82   C CG  . PHE A 1 27  ? 27.31300  -11.42400 11.61000 1.000 25.16000 ? 27  PHE A CG  1 
ATOM   83   C CD1 . PHE A 1 27  ? 28.53900  -11.83100 12.10700 1.000 25.16000 ? 27  PHE A CD1 1 
ATOM   84   C CD2 . PHE A 1 27  ? 26.71900  -12.17300 10.60800 1.000 25.16000 ? 27  PHE A CD2 1 
ATOM   85   C CE1 . PHE A 1 27  ? 29.17000  -12.95200 11.60400 1.000 25.16000 ? 27  PHE A CE1 1 
ATOM   86   C CE2 . PHE A 1 27  ? 27.34300  -13.29600 10.10100 1.000 25.16000 ? 27  PHE A CE2 1 
ATOM   87   C CZ  . PHE A 1 27  ? 28.57100  -13.68600 10.59900 1.000 25.16000 ? 27  PHE A CZ  1 
ATOM   88   N N   . VAL A 1 28  ? 24.99400  -7.78900  11.23500 1.000 22.75000 ? 28  VAL A N   1 
ATOM   89   C CA  . VAL A 1 28  ? 23.91200  -6.84800  11.49700 1.000 22.75000 ? 28  VAL A CA  1 
ATOM   90   C C   . VAL A 1 28  ? 22.58800  -7.59400  11.43900 1.000 22.75000 ? 28  VAL A C   1 
ATOM   91   O O   . VAL A 1 28  ? 22.49000  -8.69600  10.89600 1.000 22.75000 ? 28  VAL A O   1 
ATOM   92   C CB  . VAL A 1 28  ? 23.87700  -5.66100  10.50700 1.000 22.75000 ? 28  VAL A CB  1 
ATOM   93   C CG1 . VAL A 1 28  ? 25.19900  -4.91100  10.50400 1.000 22.75000 ? 28  VAL A CG1 1 
ATOM   94   C CG2 . VAL A 1 28  ? 23.50900  -6.14300  9.11400  1.000 22.75000 ? 28  VAL A CG2 1 
ATOM   95   N N   . GLN A 1 29  ? 21.56400  -6.98500  12.02200 1.000 23.99000 ? 29  GLN A N   1 
ATOM   96   C CA  . GLN A 1 29  ? 20.24200  -7.58400  11.98900 1.000 23.99000 ? 29  GLN A CA  1 
ATOM   97   C C   . GLN A 1 29  ? 19.62100  -7.40600  10.60300 1.000 23.99000 ? 29  GLN A C   1 
ATOM   98   O O   . GLN A 1 29  ? 19.79300  -6.35600  9.97500  1.000 23.99000 ? 29  GLN A O   1 
ATOM   99   C CB  . GLN A 1 29  ? 19.35500  -6.96800  13.07300 1.000 23.99000 ? 29  GLN A CB  1 
ATOM   100  C CG  . GLN A 1 29  ? 20.02800  -6.93500  14.44500 1.000 23.99000 ? 29  GLN A CG  1 
ATOM   101  C CD  . GLN A 1 29  ? 19.06800  -6.57800  15.56300 1.000 23.99000 ? 29  GLN A CD  1 
ATOM   102  O OE1 . GLN A 1 29  ? 17.98200  -7.14600  15.66600 1.000 23.99000 ? 29  GLN A OE1 1 
ATOM   103  N NE2 . GLN A 1 29  ? 19.46300  -5.62700  16.40300 1.000 23.99000 ? 29  GLN A NE2 1 
ATOM   104  N N   . PRO A 1 30  ? 18.91600  -8.42200  10.09000 1.000 26.14000 ? 30  PRO A N   1 
ATOM   105  C CA  . PRO A 1 30  ? 18.46100  -8.37700  8.68900  1.000 26.14000 ? 30  PRO A CA  1 
ATOM   106  C C   . PRO A 1 30  ? 17.56000  -7.20400  8.34200  1.000 26.14000 ? 30  PRO A C   1 
ATOM   107  O O   . PRO A 1 30  ? 17.60900  -6.73000  7.19900  1.000 26.14000 ? 30  PRO A O   1 
ATOM   108  C CB  . PRO A 1 30  ? 17.71700  -9.71000  8.52800  1.000 26.14000 ? 30  PRO A CB  1 
ATOM   109  C CG  . PRO A 1 30  ? 17.27800  -10.05900 9.90500  1.000 26.14000 ? 30  PRO A CG  1 
ATOM   110  C CD  . PRO A 1 30  ? 18.40000  -9.60500  10.79300 1.000 26.14000 ? 30  PRO A CD  1 
ATOM   111  N N   . HIS A 1 31  ? 16.73300  -6.72000  9.27700  1.000 26.09000 ? 31  HIS A N   1 
ATOM   112  C CA  . HIS A 1 31  ? 15.66000  -5.79700  8.90500  1.000 26.09000 ? 31  HIS A CA  1 
ATOM   113  C C   . HIS A 1 31  ? 16.19500  -4.49400  8.32600  1.000 26.09000 ? 31  HIS A C   1 
ATOM   114  O O   . HIS A 1 31  ? 15.50200  -3.83900  7.54000  1.000 26.09000 ? 31  HIS A O   1 
ATOM   115  C CB  . HIS A 1 31  ? 14.76200  -5.52300  10.11000 1.000 26.09000 ? 31  HIS A CB  1 
ATOM   116  C CG  . HIS A 1 31  ? 15.44200  -4.78400  11.22000 1.000 26.09000 ? 31  HIS A CG  1 
ATOM   117  N ND1 . HIS A 1 31  ? 16.39900  -5.36500  12.02300 1.000 26.09000 ? 31  HIS A ND1 1 
ATOM   118  C CD2 . HIS A 1 31  ? 15.30000  -3.51300  11.66400 1.000 26.09000 ? 31  HIS A CD2 1 
ATOM   119  C CE1 . HIS A 1 31  ? 16.82100  -4.48400  12.91200 1.000 26.09000 ? 31  HIS A CE1 1 
ATOM   120  N NE2 . HIS A 1 31  ? 16.17000  -3.35100  12.71600 1.000 26.09000 ? 31  HIS A NE2 1 
ATOM   121  N N   . GLY A 1 32  ? 17.41200  -4.09500  8.70000  1.000 25.45000 ? 32  GLY A N   1 
ATOM   122  C CA  . GLY A 1 32  ? 18.05100  -2.92600  8.14200  1.000 25.45000 ? 32  GLY A CA  1 
ATOM   123  C C   . GLY A 1 32  ? 19.24900  -3.28200  7.27100  1.000 25.45000 ? 32  GLY A C   1 
ATOM   124  O O   . GLY A 1 32  ? 19.67500  -4.43200  7.17800  1.000 25.45000 ? 32  GLY A O   1 
ATOM   125  N N   . VAL A 1 33  ? 19.78900  -2.25300  6.62400  1.000 23.85000 ? 33  VAL A N   1 
ATOM   126  C CA  . VAL A 1 33  ? 20.99300  -2.36000  5.81100  1.000 23.85000 ? 33  VAL A CA  1 
ATOM   127  C C   . VAL A 1 33  ? 22.05900  -1.46900  6.42600  1.000 23.85000 ? 33  VAL A C   1 
ATOM   128  O O   . VAL A 1 33  ? 21.75500  -0.38000  6.92500  1.000 23.85000 ? 33  VAL A O   1 
ATOM   129  C CB  . VAL A 1 33  ? 20.73500  -1.95800  4.34400  1.000 23.85000 ? 33  VAL A CB  1 
ATOM   130  C CG1 . VAL A 1 33  ? 21.90700  -2.36800  3.46500  1.000 23.85000 ? 33  VAL A CG1 1 
ATOM   131  C CG2 . VAL A 1 33  ? 19.44400  -2.57000  3.84500  1.000 23.85000 ? 33  VAL A CG2 1 
ATOM   132  N N   . LEU A 1 34  ? 23.30600  -1.92700  6.38700  1.000 22.06000 ? 34  LEU A N   1 
ATOM   133  C CA  . LEU A 1 34  ? 24.43200  -1.15600  6.88900  1.000 22.06000 ? 34  LEU A CA  1 
ATOM   134  C C   . LEU A 1 34  ? 25.39100  -0.85200  5.74800  1.000 22.06000 ? 34  LEU A C   1 
ATOM   135  O O   . LEU A 1 34  ? 25.63800  -1.70300  4.88800  1.000 22.06000 ? 34  LEU A O   1 
ATOM   136  C CB  . LEU A 1 34  ? 25.15600  -1.90700  8.00900  1.000 22.06000 ? 34  LEU A CB  1 
ATOM   137  C CG  . LEU A 1 34  ? 26.22500  -1.12200  8.76800  1.000 22.06000 ? 34  LEU A CG  1 
ATOM   138  C CD1 . LEU A 1 34  ? 26.09300  -1.36200  10.26000 1.000 22.06000 ? 34  LEU A CD1 1 
ATOM   139  C CD2 . LEU A 1 34  ? 27.61200  -1.50900  8.28400  1.000 22.06000 ? 34  LEU A CD2 1 
ATOM   140  N N   . LEU A 1 35  ? 25.93000  0.36600   5.74500  1.000 21.42000 ? 35  LEU A N   1 
ATOM   141  C CA  . LEU A 1 35  ? 26.90500  0.79000   4.74400  1.000 21.42000 ? 35  LEU A CA  1 
ATOM   142  C C   . LEU A 1 35  ? 27.97800  1.60500   5.44900  1.000 21.42000 ? 35  LEU A C   1 
ATOM   143  O O   . LEU A 1 35  ? 27.71800  2.73000   5.88900  1.000 21.42000 ? 35  LEU A O   1 
ATOM   144  C CB  . LEU A 1 35  ? 26.25100  1.61000   3.63000  1.000 21.42000 ? 35  LEU A CB  1 
ATOM   145  C CG  . LEU A 1 35  ? 25.10100  0.99100   2.83400  1.000 21.42000 ? 35  LEU A CG  1 
ATOM   146  C CD1 . LEU A 1 35  ? 23.76100  1.49300   3.35000  1.000 21.42000 ? 35  LEU A CD1 1 
ATOM   147  C CD2 . LEU A 1 35  ? 25.25800  1.28800   1.35000  1.000 21.42000 ? 35  LEU A CD2 1 
ATOM   148  N N   . ALA A 1 36  ? 29.17000  1.03400   5.58100  1.000 21.55000 ? 36  ALA A N   1 
ATOM   149  C CA  . ALA A 1 36  ? 30.33200  1.80100   6.00400  1.000 21.55000 ? 36  ALA A CA  1 
ATOM   150  C C   . ALA A 1 36  ? 30.89400  2.51900   4.78500  1.000 21.55000 ? 36  ALA A C   1 
ATOM   151  O O   . ALA A 1 36  ? 31.30400  1.86900   3.81400  1.000 21.55000 ? 36  ALA A O   1 
ATOM   152  C CB  . ALA A 1 36  ? 31.38000  0.89200   6.63800  1.000 21.55000 ? 36  ALA A CB  1 
ATOM   153  N N   . ILE A 1 37  ? 30.92800  3.84900   4.84500  1.000 22.19000 ? 37  ILE A N   1 
ATOM   154  C CA  . ILE A 1 37  ? 31.20500  4.70400   3.70000  1.000 22.19000 ? 37  ILE A CA  1 
ATOM   155  C C   . ILE A 1 37  ? 32.32900  5.65300   4.08900  1.000 22.19000 ? 37  ILE A C   1 
ATOM   156  O O   . ILE A 1 37  ? 32.14900  6.50200   4.97100  1.000 22.19000 ? 37  ILE A O   1 
ATOM   157  C CB  . ILE A 1 37  ? 29.96300  5.49400   3.26800  1.000 22.19000 ? 37  ILE A CB  1 
ATOM   158  C CG1 . ILE A 1 37  ? 28.82900  4.54600   2.87900  1.000 22.19000 ? 37  ILE A CG1 1 
ATOM   159  C CG2 . ILE A 1 37  ? 30.29400  6.43100   2.13100  1.000 22.19000 ? 37  ILE A CG2 1 
ATOM   160  C CD1 . ILE A 1 37  ? 27.50300  5.24600   2.68100  1.000 22.19000 ? 37  ILE A CD1 1 
ATOM   161  N N   . LYS A 1 38  ? 33.48100  5.51700   3.44000  1.000 24.88000 ? 38  LYS A N   1 
ATOM   162  C CA  . LYS A 1 38  ? 34.57000  6.45200   3.67200  1.000 24.88000 ? 38  LYS A CA  1 
ATOM   163  C C   . LYS A 1 38  ? 34.26200  7.79900   3.02400  1.000 24.88000 ? 38  LYS A C   1 
ATOM   164  O O   . LYS A 1 38  ? 33.48200  7.90100   2.07500  1.000 24.88000 ? 38  LYS A O   1 
ATOM   165  C CB  . LYS A 1 38  ? 35.89100  5.90500   3.13400  1.000 24.88000 ? 38  LYS A CB  1 
ATOM   166  C CG  . LYS A 1 38  ? 36.04500  6.00800   1.62700  1.000 24.88000 ? 38  LYS A CG  1 
ATOM   167  C CD  . LYS A 1 38  ? 37.47000  5.69600   1.20500  1.000 24.88000 ? 38  LYS A CD  1 
ATOM   168  C CE  . LYS A 1 38  ? 38.43900  6.76900   1.68000  1.000 24.88000 ? 38  LYS A CE  1 
ATOM   169  N NZ  . LYS A 1 38  ? 38.36700  8.00100   0.85200  1.000 24.88000 ? 38  LYS A NZ  1 
ATOM   170  N N   . GLU A 1 39  ? 34.87800  8.83900   3.56100  1.000 26.48000 ? 39  GLU A N   1 
ATOM   171  C CA  . GLU A 1 39  ? 34.74300  10.20600  3.08700  1.000 26.48000 ? 39  GLU A CA  1 
ATOM   172  C C   . GLU A 1 39  ? 36.13300  10.76800  2.83900  1.000 26.48000 ? 39  GLU A C   1 
ATOM   173  O O   . GLU A 1 39  ? 37.11300  10.28100  3.41300  1.000 26.48000 ? 39  GLU A O   1 
ATOM   174  C CB  . GLU A 1 39  ? 33.98300  11.07000  4.10500  1.000 26.48000 ? 39  GLU A CB  1 
ATOM   175  C CG  . GLU A 1 39  ? 34.45800  10.91700  5.53500  1.000 26.48000 ? 39  GLU A CG  1 
ATOM   176  C CD  . GLU A 1 39  ? 33.64600  11.75000  6.50600  1.000 26.48000 ? 39  GLU A CD  1 
ATOM   177  O OE1 . GLU A 1 39  ? 32.83800  12.58500  6.04500  1.000 26.48000 ? 39  GLU A OE1 1 
ATOM   178  O OE2 . GLU A 1 39  ? 33.81300  11.56900  7.73000  1.000 26.48000 ? 39  GLU A OE2 1 
ATOM   179  N N   . PRO A 1 40  ? 36.26400  11.79800  1.98100  1.000 27.87000 ? 40  PRO A N   1 
ATOM   180  C CA  . PRO A 1 40  ? 35.23500  12.61900  1.31400  1.000 27.87000 ? 40  PRO A CA  1 
ATOM   181  C C   . PRO A 1 40  ? 34.60600  12.03300  0.04900  1.000 27.87000 ? 40  PRO A C   1 
ATOM   182  O O   . PRO A 1 40  ? 33.59100  12.54700  -0.41300 1.000 27.87000 ? 40  PRO A O   1 
ATOM   183  C CB  . PRO A 1 40  ? 36.00900  13.89900  0.98300  1.000 27.87000 ? 40  PRO A CB  1 
ATOM   184  C CG  . PRO A 1 40  ? 37.38200  13.39500  0.66000  1.000 27.87000 ? 40  PRO A CG  1 
ATOM   185  C CD  . PRO A 1 40  ? 37.62000  12.25100  1.62000  1.000 27.87000 ? 40  PRO A CD  1 
ATOM   186  N N   . GLU A 1 41  ? 35.16500  10.97600  -0.54100 1.000 27.27000 ? 41  GLU A N   1 
ATOM   187  C CA  . GLU A 1 41  ? 34.65600  10.48500  -1.81600 1.000 27.27000 ? 41  GLU A CA  1 
ATOM   188  C C   . GLU A 1 41  ? 33.29600  9.81400   -1.69400 1.000 27.27000 ? 41  GLU A C   1 
ATOM   189  O O   . GLU A 1 41  ? 32.63400  9.61000   -2.71700 1.000 27.27000 ? 41  GLU A O   1 
ATOM   190  C CB  . GLU A 1 41  ? 35.64800  9.50400   -2.44700 1.000 27.27000 ? 41  GLU A CB  1 
ATOM   191  C CG  . GLU A 1 41  ? 37.02500  10.08800  -2.72900 1.000 27.27000 ? 41  GLU A CG  1 
ATOM   192  C CD  . GLU A 1 41  ? 37.91500  10.10100  -1.50300 1.000 27.27000 ? 41  GLU A CD  1 
ATOM   193  O OE1 . GLU A 1 41  ? 37.46500  9.62500   -0.44000 1.000 27.27000 ? 41  GLU A OE1 1 
ATOM   194  O OE2 . GLU A 1 41  ? 39.06200  10.58600  -1.60100 1.000 27.27000 ? 41  GLU A OE2 1 
ATOM   195  N N   . LEU A 1 42  ? 32.87000  9.47000   -0.47900 1.000 25.88000 ? 42  LEU A N   1 
ATOM   196  C CA  . LEU A 1 42  ? 31.63600  8.72200   -0.24100 1.000 25.88000 ? 42  LEU A CA  1 
ATOM   197  C C   . LEU A 1 42  ? 31.64700  7.37100   -0.94900 1.000 25.88000 ? 42  LEU A C   1 
ATOM   198  O O   . LEU A 1 42  ? 30.59600  6.85300   -1.34100 1.000 25.88000 ? 42  LEU A O   1 
ATOM   199  C CB  . LEU A 1 42  ? 30.39600  9.53000   -0.63600 1.000 25.88000 ? 42  LEU A CB  1 
ATOM   200  C CG  . LEU A 1 42  ? 30.14300  10.82300  0.14300  1.000 25.88000 ? 42  LEU A CG  1 
ATOM   201  C CD1 . LEU A 1 42  ? 28.69500  11.26900  -0.00700 1.000 25.88000 ? 42  LEU A CD1 1 
ATOM   202  C CD2 . LEU A 1 42  ? 30.50900  10.66100  1.61000  1.000 25.88000 ? 42  LEU A CD2 1 
ATOM   203  N N   . THR A 1 43  ? 32.83500  6.79700   -1.12100 1.000 24.67000 ? 43  THR A N   1 
ATOM   204  C CA  . THR A 1 43  ? 32.95200  5.42500   -1.59500 1.000 24.67000 ? 43  THR A CA  1 
ATOM   205  C C   . THR A 1 43  ? 32.45200  4.44200   -0.54300 1.000 24.67000 ? 43  THR A C   1 
ATOM   206  O O   . THR A 1 43  ? 32.75000  4.57700   0.64800  1.000 24.67000 ? 43  THR A O   1 
ATOM   207  C CB  . THR A 1 43  ? 34.40500  5.12600   -1.95300 1.000 24.67000 ? 43  THR A CB  1 
ATOM   208  O OG1 . THR A 1 43  ? 34.79500  5.96700   -3.04500 1.000 24.67000 ? 43  THR A OG1 1 
ATOM   209  C CG2 . THR A 1 43  ? 34.57200  3.67500   -2.35600 1.000 24.67000 ? 43  THR A CG2 1 
ATOM   210  N N   . ILE A 1 44  ? 31.70200  3.43900   -0.99200 1.000 22.23000 ? 44  ILE A N   1 
ATOM   211  C CA  . ILE A 1 44  ? 31.14000  2.42300   -0.10600 1.000 22.23000 ? 44  ILE A CA  1 
ATOM   212  C C   . ILE A 1 44  ? 32.23000  1.40300   0.20500  1.000 22.23000 ? 44  ILE A C   1 
ATOM   213  O O   . ILE A 1 44  ? 32.58700  0.58100   -0.64100 1.000 22.23000 ? 44  ILE A O   1 
ATOM   214  C CB  . ILE A 1 44  ? 29.91600  1.74300   -0.72800 1.000 22.23000 ? 44  ILE A CB  1 
ATOM   215  C CG1 . ILE A 1 44  ? 28.76900  2.73800   -0.89900 1.000 22.23000 ? 44  ILE A CG1 1 
ATOM   216  C CG2 . ILE A 1 44  ? 29.47100  0.58000   0.12800  1.000 22.23000 ? 44  ILE A CG2 1 
ATOM   217  C CD1 . ILE A 1 44  ? 27.53600  2.12800   -1.53900 1.000 22.23000 ? 44  ILE A CD1 1 
ATOM   218  N N   . LEU A 1 45  ? 32.76300  1.45300   1.42300  1.000 23.65000 ? 45  LEU A N   1 
ATOM   219  C CA  . LEU A 1 45  ? 33.82800  0.52600   1.78300  1.000 23.65000 ? 45  LEU A CA  1 
ATOM   220  C C   . LEU A 1 45  ? 33.28100  -0.82100  2.23600  1.000 23.65000 ? 45  LEU A C   1 
ATOM   221  O O   . LEU A 1 45  ? 33.86700  -1.86400  1.92300  1.000 23.65000 ? 45  LEU A O   1 
ATOM   222  C CB  . LEU A 1 45  ? 34.71800  1.13800   2.86400  1.000 23.65000 ? 45  LEU A CB  1 
ATOM   223  C CG  . LEU A 1 45  ? 35.65800  2.25100   2.39400  1.000 23.65000 ? 45  LEU A CG  1 
ATOM   224  C CD1 . LEU A 1 45  ? 36.79300  2.42800   3.38600  1.000 23.65000 ? 45  LEU A CD1 1 
ATOM   225  C CD2 . LEU A 1 45  ? 36.19800  1.95300   1.00500  1.000 23.65000 ? 45  LEU A CD2 1 
ATOM   226  N N   . GLN A 1 46  ? 32.16000  -0.83000  2.95700  1.000 24.91000 ? 46  GLN A N   1 
ATOM   227  C CA  . GLN A 1 46  ? 31.63100  -2.06900  3.51400  1.000 24.91000 ? 46  GLN A CA  1 
ATOM   228  C C   . GLN A 1 46  ? 30.11100  -2.06300  3.45400  1.000 24.91000 ? 46  GLN A C   1 
ATOM   229  O O   . GLN A 1 46  ? 29.47500  -1.01800  3.59900  1.000 24.91000 ? 46  GLN A O   1 
ATOM   230  C CB  . GLN A 1 46  ? 32.08500  -2.27300  4.96700  1.000 24.91000 ? 46  GLN A CB  1 
ATOM   231  C CG  . GLN A 1 46  ? 33.57400  -2.52500  5.13000  1.000 24.91000 ? 46  GLN A CG  1 
ATOM   232  C CD  . GLN A 1 46  ? 34.00600  -2.52800  6.58200  1.000 24.91000 ? 46  GLN A CD  1 
ATOM   233  O OE1 . GLN A 1 46  ? 34.04300  -1.48400  7.23400  1.000 24.91000 ? 46  GLN A OE1 1 
ATOM   234  N NE2 . GLN A 1 46  ? 34.33400  -3.70500  7.09800  1.000 24.91000 ? 46  GLN A NE2 1 
ATOM   235  N N   . VAL A 1 47  ? 29.53300  -3.25200  3.27200  1.000 24.53000 ? 47  VAL A N   1 
ATOM   236  C CA  . VAL A 1 47  ? 28.08800  -3.42600  3.20500  1.000 24.53000 ? 47  VAL A CA  1 
ATOM   237  C C   . VAL A 1 47  ? 27.69900  -4.64000  4.03400  1.000 24.53000 ? 47  VAL A C   1 
ATOM   238  O O   . VAL A 1 47  ? 28.52800  -5.49000  4.36200  1.000 24.53000 ? 47  VAL A O   1 
ATOM   239  C CB  . VAL A 1 47  ? 27.57400  -3.60900  1.75800  1.000 24.53000 ? 47  VAL A CB  1 
ATOM   240  C CG1 . VAL A 1 47  ? 27.67400  -2.31300  0.98200  1.000 24.53000 ? 47  VAL A CG1 1 
ATOM   241  C CG2 . VAL A 1 47  ? 28.34200  -4.72200  1.06100  1.000 24.53000 ? 47  VAL A CG2 1 
ATOM   242  N N   . SER A 1 48  ? 26.41100  -4.71700  4.36500  1.000 27.35000 ? 48  SER A N   1 
ATOM   243  C CA  . SER A 1 48  ? 25.87400  -5.90900  5.00900  1.000 27.35000 ? 48  SER A CA  1 
ATOM   244  C C   . SER A 1 48  ? 25.71300  -7.02100  3.98100  1.000 27.35000 ? 48  SER A C   1 
ATOM   245  O O   . SER A 1 48  ? 26.30300  -6.96000  2.89700  1.000 27.35000 ? 48  SER A O   1 
ATOM   246  C CB  . SER A 1 48  ? 24.53600  -5.60700  5.68200  1.000 27.35000 ? 48  SER A CB  1 
ATOM   247  O OG  . SER A 1 48  ? 23.51900  -5.43000  4.71400  1.000 27.35000 ? 48  SER A OG  1 
ATOM   248  N N   . ASN A 1 49  ? 24.95200  -8.06200  4.32100  1.000 30.32000 ? 49  ASN A N   1 
ATOM   249  C CA  . ASN A 1 49  ? 24.60600  -9.09000  3.34400  1.000 30.32000 ? 49  ASN A CA  1 
ATOM   250  C C   . ASN A 1 49  ? 23.20300  -8.94000  2.77200  1.000 30.32000 ? 49  ASN A C   1 
ATOM   251  O O   . ASN A 1 49  ? 22.97800  -9.30900  1.61500  1.000 30.32000 ? 49  ASN A O   1 
ATOM   252  C CB  . ASN A 1 49  ? 24.75400  -10.48900 3.95300  1.000 30.32000 ? 49  ASN A CB  1 
ATOM   253  C CG  . ASN A 1 49  ? 24.32400  -11.58200 2.99600  1.000 30.32000 ? 49  ASN A CG  1 
ATOM   254  O OD1 . ASN A 1 49  ? 23.26500  -12.18600 3.16100  1.000 30.32000 ? 49  ASN A OD1 1 
ATOM   255  N ND2 . ASN A 1 49  ? 25.13300  -11.82300 1.96900  1.000 30.32000 ? 49  ASN A ND2 1 
ATOM   256  N N   . ASN A 1 50  ? 22.26300  -8.37700  3.53200  1.000 30.46000 ? 50  ASN A N   1 
ATOM   257  C CA  . ASN A 1 50  ? 20.90700  -8.14800  3.04300  1.000 30.46000 ? 50  ASN A CA  1 
ATOM   258  C C   . ASN A 1 50  ? 20.81100  -6.89600  2.17200  1.000 30.46000 ? 50  ASN A C   1 
ATOM   259  O O   . ASN A 1 50  ? 19.71800  -6.33000  2.04900  1.000 30.46000 ? 50  ASN A O   1 
ATOM   260  C CB  . ASN A 1 50  ? 19.92000  -8.06300  4.21700  1.000 30.46000 ? 50  ASN A CB  1 
ATOM   261  C CG  . ASN A 1 50  ? 20.26000  -6.95000  5.19000  1.000 30.46000 ? 50  ASN A CG  1 
ATOM   262  O OD1 . ASN A 1 50  ? 21.27500  -7.01100  5.88200  1.000 30.46000 ? 50  ASN A OD1 1 
ATOM   263  N ND2 . ASN A 1 50  ? 19.41500  -5.92300  5.24800  1.000 30.46000 ? 50  ASN A ND2 1 
ATOM   264  N N   . THR A 1 51  ? 21.93100  -6.43900  1.59600  1.000 32.27000 ? 51  THR A N   1 
ATOM   265  C CA  . THR A 1 51  ? 21.89900  -5.31200  0.67000  1.000 32.27000 ? 51  THR A CA  1 
ATOM   266  C C   . THR A 1 51  ? 21.08100  -5.62400  -0.57500 1.000 32.27000 ? 51  THR A C   1 
ATOM   267  O O   . THR A 1 51  ? 20.50500  -4.71500  -1.18000 1.000 32.27000 ? 51  THR A O   1 
ATOM   268  C CB  . THR A 1 51  ? 23.32400  -4.93800  0.26500  1.000 32.27000 ? 51  THR A CB  1 
ATOM   269  O OG1 . THR A 1 51  ? 23.77700  -5.82800  -0.75900 1.000 32.27000 ? 51  THR A OG1 1 
ATOM   270  C CG2 . THR A 1 51  ? 24.25100  -5.04500  1.45100  1.000 32.27000 ? 51  THR A CG2 1 
ATOM   271  N N   . TYR A 1 52  ? 21.03000  -6.89000  -0.98700 1.000 36.66000 ? 52  TYR A N   1 
ATOM   272  C CA  . TYR A 1 52  ? 20.22400  -7.24500  -2.14600 1.000 36.66000 ? 52  TYR A CA  1 
ATOM   273  C C   . TYR A 1 52  ? 18.74800  -7.12700  -1.80200 1.000 36.66000 ? 52  TYR A C   1 
ATOM   274  O O   . TYR A 1 52  ? 18.08800  -6.16200  -2.20800 1.000 36.66000 ? 52  TYR A O   1 
ATOM   275  C CB  . TYR A 1 52  ? 20.54900  -8.65900  -2.63700 1.000 36.66000 ? 52  TYR A CB  1 
ATOM   276  C CG  . TYR A 1 52  ? 19.72000  -9.08200  -3.83400 1.000 36.66000 ? 52  TYR A CG  1 
ATOM   277  C CD1 . TYR A 1 52  ? 19.95400  -8.53900  -5.09100 1.000 36.66000 ? 52  TYR A CD1 1 
ATOM   278  C CD2 . TYR A 1 52  ? 18.70100  -10.01800 -3.70600 1.000 36.66000 ? 52  TYR A CD2 1 
ATOM   279  C CE1 . TYR A 1 52  ? 19.19600  -8.91400  -6.18900 1.000 36.66000 ? 52  TYR A CE1 1 
ATOM   280  C CE2 . TYR A 1 52  ? 17.93900  -10.40200 -4.80000 1.000 36.66000 ? 52  TYR A CE2 1 
ATOM   281  C CZ  . TYR A 1 52  ? 18.19200  -9.84600  -6.03800 1.000 36.66000 ? 52  TYR A CZ  1 
ATOM   282  O OH  . TYR A 1 52  ? 17.44000  -10.22100 -7.13000 1.000 36.66000 ? 52  TYR A OH  1 
ATOM   283  N N   . ASN A 1 53  ? 18.25000  -8.05500  -0.97900 1.000 38.30000 ? 53  ASN A N   1 
ATOM   284  C CA  . ASN A 1 53  ? 16.80800  -8.19700  -0.80600 1.000 38.30000 ? 53  ASN A CA  1 
ATOM   285  C C   . ASN A 1 53  ? 16.17300  -6.89500  -0.33900 1.000 38.30000 ? 53  ASN A C   1 
ATOM   286  O O   . ASN A 1 53  ? 15.02800  -6.59300  -0.69400 1.000 38.30000 ? 53  ASN A O   1 
ATOM   287  C CB  . ASN A 1 53  ? 16.50300  -9.31700  0.19100  1.000 38.30000 ? 53  ASN A CB  1 
ATOM   288  C CG  . ASN A 1 53  ? 17.23900  -10.59800 -0.12800 1.000 38.30000 ? 53  ASN A CG  1 
ATOM   289  O OD1 . ASN A 1 53  ? 18.40900  -10.75500 0.21700  1.000 38.30000 ? 53  ASN A OD1 1 
ATOM   290  N ND2 . ASN A 1 53  ? 16.55400  -11.52800 -0.78500 1.000 38.30000 ? 53  ASN A ND2 1 
ATOM   291  N N   . CYS A 1 54  ? 16.90300  -6.10300  0.44500  1.000 37.12000 ? 54  CYS A N   1 
ATOM   292  C CA  . CYS A 1 54  ? 16.33300  -4.84600  0.91200  1.000 37.12000 ? 54  CYS A CA  1 
ATOM   293  C C   . CYS A 1 54  ? 16.54500  -3.71800  -0.08900 1.000 37.12000 ? 54  CYS A C   1 
ATOM   294  O O   . CYS A 1 54  ? 15.62700  -2.92800  -0.33600 1.000 37.12000 ? 54  CYS A O   1 
ATOM   295  C CB  . CYS A 1 54  ? 16.92800  -4.47500  2.27200  1.000 37.12000 ? 54  CYS A CB  1 
ATOM   296  S SG  . CYS A 1 54  ? 16.59300  -5.67100  3.58400  1.000 37.12000 ? 54  CYS A SG  1 
ATOM   297  N N   . LEU A 1 55  ? 17.73600  -3.62600  -0.68100 1.000 36.04000 ? 55  LEU A N   1 
ATOM   298  C CA  . LEU A 1 55  ? 18.08400  -2.47800  -1.50800 1.000 36.04000 ? 55  LEU A CA  1 
ATOM   299  C C   . LEU A 1 55  ? 18.12500  -2.79300  -2.99600 1.000 36.04000 ? 55  LEU A C   1 
ATOM   300  O O   . LEU A 1 55  ? 18.36000  -1.88500  -3.79900 1.000 36.04000 ? 55  LEU A O   1 
ATOM   301  C CB  . LEU A 1 55  ? 19.43400  -1.89100  -1.07400 1.000 36.04000 ? 55  LEU A CB  1 
ATOM   302  C CG  . LEU A 1 55  ? 19.54300  -1.24400  0.30700  1.000 36.04000 ? 55  LEU A CG  1 
ATOM   303  C CD1 . LEU A 1 55  ? 20.88000  -0.52900  0.45200  1.000 36.04000 ? 55  LEU A CD1 1 
ATOM   304  C CD2 . LEU A 1 55  ? 18.39500  -0.28300  0.53900  1.000 36.04000 ? 55  LEU A CD2 1 
ATOM   305  N N   . GLY A 1 56  ? 17.90000  -4.03900  -3.38600 1.000 35.52000 ? 56  GLY A N   1 
ATOM   306  C CA  . GLY A 1 56  ? 17.96000  -4.38400  -4.80300 1.000 35.52000 ? 56  GLY A CA  1 
ATOM   307  C C   . GLY A 1 56  ? 19.34200  -4.66300  -5.34800 1.000 35.52000 ? 56  GLY A C   1 
ATOM   308  O O   . GLY A 1 56  ? 19.55000  -5.68100  -6.01100 1.000 35.52000 ? 56  GLY A O   1 
ATOM   309  N N   . PHE A 1 57  ? 20.29400  -3.76500  -5.10400 1.000 35.60000 ? 57  PHE A N   1 
ATOM   310  C CA  . PHE A 1 57  ? 21.66300  -3.98600  -5.55100 1.000 35.60000 ? 57  PHE A CA  1 
ATOM   311  C C   . PHE A 1 57  ? 22.29500  -5.15300  -4.79900 1.000 35.60000 ? 57  PHE A C   1 
ATOM   312  O O   . PHE A 1 57  ? 22.15800  -5.27100  -3.57900 1.000 35.60000 ? 57  PHE A O   1 
ATOM   313  C CB  . PHE A 1 57  ? 22.49700  -2.72100  -5.34400 1.000 35.60000 ? 57  PHE A CB  1 
ATOM   314  C CG  . PHE A 1 57  ? 22.15600  -1.59300  -6.28300 1.000 35.60000 ? 57  PHE A CG  1 
ATOM   315  C CD1 . PHE A 1 57  ? 20.92500  -0.95800  -6.21700 1.000 35.60000 ? 57  PHE A CD1 1 
ATOM   316  C CD2 . PHE A 1 57  ? 23.08300  -1.14700  -7.21400 1.000 35.60000 ? 57  PHE A CD2 1 
ATOM   317  C CE1 . PHE A 1 57  ? 20.61700  0.08300   -7.07400 1.000 35.60000 ? 57  PHE A CE1 1 
ATOM   318  C CE2 . PHE A 1 57  ? 22.78100  -0.10500  -8.07200 1.000 35.60000 ? 57  PHE A CE2 1 
ATOM   319  C CZ  . PHE A 1 57  ? 21.54600  0.51100   -8.00200 1.000 35.60000 ? 57  PHE A CZ  1 
ATOM   320  N N   . HIS A 1 58  ? 23.01100  -6.00600  -5.52900 1.000 33.73000 ? 58  HIS A N   1 
ATOM   321  C CA  . HIS A 1 58  ? 23.72800  -7.10500  -4.90300 1.000 33.73000 ? 58  HIS A CA  1 
ATOM   322  C C   . HIS A 1 58  ? 24.93600  -6.57600  -4.13000 1.000 33.73000 ? 58  HIS A C   1 
ATOM   323  O O   . HIS A 1 58  ? 25.47400  -5.51500  -4.46000 1.000 33.73000 ? 58  HIS A O   1 
ATOM   324  C CB  . HIS A 1 58  ? 24.17700  -8.12300  -5.94700 1.000 33.73000 ? 58  HIS A CB  1 
ATOM   325  C CG  . HIS A 1 58  ? 23.21500  -9.25200  -6.13800 1.000 33.73000 ? 58  HIS A CG  1 
ATOM   326  N ND1 . HIS A 1 58  ? 22.99500  -10.21200 -5.17400 1.000 33.73000 ? 58  HIS A ND1 1 
ATOM   327  C CD2 . HIS A 1 58  ? 22.41700  -9.57800  -7.18200 1.000 33.73000 ? 58  HIS A CD2 1 
ATOM   328  C CE1 . HIS A 1 58  ? 22.10200  -11.08000 -5.61400 1.000 33.73000 ? 58  HIS A CE1 1 
ATOM   329  N NE2 . HIS A 1 58  ? 21.73500  -10.71800 -6.83100 1.000 33.73000 ? 58  HIS A NE2 1 
ATOM   330  N N   . PRO A 1 59  ? 25.36500  -7.28200  -3.07500 1.000 29.87000 ? 59  PRO A N   1 
ATOM   331  C CA  . PRO A 1 59  ? 26.47900  -6.76200  -2.26100 1.000 29.87000 ? 59  PRO A CA  1 
ATOM   332  C C   . PRO A 1 59  ? 27.76100  -6.52800  -3.04500 1.000 29.87000 ? 59  PRO A C   1 
ATOM   333  O O   . PRO A 1 59  ? 28.49300  -5.57700  -2.74400 1.000 29.87000 ? 59  PRO A O   1 
ATOM   334  C CB  . PRO A 1 59  ? 26.66900  -7.85300  -1.19600 1.000 29.87000 ? 59  PRO A CB  1 
ATOM   335  C CG  . PRO A 1 59  ? 25.35700  -8.56300  -1.13700 1.000 29.87000 ? 59  PRO A CG  1 
ATOM   336  C CD  . PRO A 1 59  ? 24.81400  -8.53600  -2.53000 1.000 29.87000 ? 59  PRO A CD  1 
ATOM   337  N N   . GLU A 1 60  ? 28.05700  -7.36600  -4.04100 1.000 30.11000 ? 60  GLU A N   1 
ATOM   338  C CA  . GLU A 1 60  ? 29.21500  -7.11100  -4.89100 1.000 30.11000 ? 60  GLU A CA  1 
ATOM   339  C C   . GLU A 1 60  ? 28.99000  -5.91400  -5.80400 1.000 30.11000 ? 60  GLU A C   1 
ATOM   340  O O   . GLU A 1 60  ? 29.95400  -5.25200  -6.20600 1.000 30.11000 ? 60  GLU A O   1 
ATOM   341  C CB  . GLU A 1 60  ? 29.55300  -8.35600  -5.71200 1.000 30.11000 ? 60  GLU A CB  1 
ATOM   342  C CG  . GLU A 1 60  ? 30.15500  -9.50100  -4.90100 1.000 30.11000 ? 60  GLU A CG  1 
ATOM   343  C CD  . GLU A 1 60  ? 29.13600  -10.22200 -4.03400 1.000 30.11000 ? 60  GLU A CD  1 
ATOM   344  O OE1 . GLU A 1 60  ? 27.92300  -9.96500  -4.19300 1.000 30.11000 ? 60  GLU A OE1 1 
ATOM   345  O OE2 . GLU A 1 60  ? 29.55100  -11.05000 -3.19400 1.000 30.11000 ? 60  GLU A OE2 1 
ATOM   346  N N   . GLU A 1 61  ? 27.73100  -5.62200  -6.14000 1.000 30.70000 ? 61  GLU A N   1 
ATOM   347  C CA  . GLU A 1 61  ? 27.42500  -4.48200  -6.99500 1.000 30.70000 ? 61  GLU A CA  1 
ATOM   348  C C   . GLU A 1 61  ? 27.59500  -3.15300  -6.27100 1.000 30.70000 ? 61  GLU A C   1 
ATOM   349  O O   . GLU A 1 61  ? 27.71000  -2.11400  -6.93000 1.000 30.70000 ? 61  GLU A O   1 
ATOM   350  C CB  . GLU A 1 61  ? 25.99800  -4.59700  -7.53800 1.000 30.70000 ? 61  GLU A CB  1 
ATOM   351  C CG  . GLU A 1 61  ? 25.73200  -5.86400  -8.33600 1.000 30.70000 ? 61  GLU A CG  1 
ATOM   352  C CD  . GLU A 1 61  ? 24.27600  -6.00600  -8.74100 1.000 30.70000 ? 61  GLU A CD  1 
ATOM   353  O OE1 . GLU A 1 61  ? 23.51000  -5.03400  -8.57000 1.000 30.70000 ? 61  GLU A OE1 1 
ATOM   354  O OE2 . GLU A 1 61  ? 23.89400  -7.09200  -9.22500 1.000 30.70000 ? 61  GLU A OE2 1 
ATOM   355  N N   . LEU A 1 62  ? 27.60100  -3.15900  -4.93800 1.000 27.22000 ? 62  LEU A N   1 
ATOM   356  C CA  . LEU A 1 62  ? 27.70700  -1.93600  -4.15200 1.000 27.22000 ? 62  LEU A CA  1 
ATOM   357  C C   . LEU A 1 62  ? 29.11000  -1.64900  -3.64300 1.000 27.22000 ? 62  LEU A C   1 
ATOM   358  O O   . LEU A 1 62  ? 29.44600  -0.48000  -3.42500 1.000 27.22000 ? 62  LEU A O   1 
ATOM   359  C CB  . LEU A 1 62  ? 26.75600  -1.99400  -2.95400 1.000 27.22000 ? 62  LEU A CB  1 
ATOM   360  C CG  . LEU A 1 62  ? 25.27900  -1.83900  -3.29400 1.000 27.22000 ? 62  LEU A CG  1 
ATOM   361  C CD1 . LEU A 1 62  ? 24.43700  -1.87500  -2.03100 1.000 27.22000 ? 62  LEU A CD1 1 
ATOM   362  C CD2 . LEU A 1 62  ? 25.06500  -0.54300  -4.05800 1.000 27.22000 ? 62  LEU A CD2 1 
ATOM   363  N N   . LEU A 1 63  ? 29.92900  -2.67600  -3.43300 1.000 23.11000 ? 63  LEU A N   1 
ATOM   364  C CA  . LEU A 1 63  ? 31.23100  -2.46500  -2.81700 1.000 23.11000 ? 63  LEU A CA  1 
ATOM   365  C C   . LEU A 1 63  ? 32.11600  -1.58200  -3.68700 1.000 23.11000 ? 63  LEU A C   1 
ATOM   366  O O   . LEU A 1 63  ? 32.17900  -1.74600  -4.90900 1.000 23.11000 ? 63  LEU A O   1 
ATOM   367  C CB  . LEU A 1 63  ? 31.91400  -3.80400  -2.55700 1.000 23.11000 ? 63  LEU A CB  1 
ATOM   368  C CG  . LEU A 1 63  ? 31.46100  -4.51900  -1.28700 1.000 23.11000 ? 63  LEU A CG  1 
ATOM   369  C CD1 . LEU A 1 63  ? 32.02200  -5.92300  -1.26600 1.000 23.11000 ? 63  LEU A CD1 1 
ATOM   370  C CD2 . LEU A 1 63  ? 31.91700  -3.73800  -0.06400 1.000 23.11000 ? 63  LEU A CD2 1 
ATOM   371  N N   . ASN A 1 64  ? 32.79600  -0.63300  -3.03400 1.000 23.15000 ? 64  ASN A N   1 
ATOM   372  C CA  . ASN A 1 64  ? 33.73600  0.31700   -3.62700 1.000 23.15000 ? 64  ASN A CA  1 
ATOM   373  C C   . ASN A 1 64  ? 33.07500  1.27500   -4.61300 1.000 23.15000 ? 64  ASN A C   1 
ATOM   374  O O   . ASN A 1 64  ? 33.73700  2.17500   -5.13700 1.000 23.15000 ? 64  ASN A O   1 
ATOM   375  C CB  . ASN A 1 64  ? 34.89800  -0.41000  -4.30800 1.000 23.15000 ? 64  ASN A CB  1 
ATOM   376  C CG  . ASN A 1 64  ? 35.71800  -1.23200  -3.33700 1.000 23.15000 ? 64  ASN A CG  1 
ATOM   377  O OD1 . ASN A 1 64  ? 35.47500  -2.42500  -3.16500 1.000 23.15000 ? 64  ASN A OD1 1 
ATOM   378  N ND2 . ASN A 1 64  ? 36.69000  -0.59600  -2.68700 1.000 23.15000 ? 64  ASN A ND2 1 
ATOM   379  N N   . GLN A 1 65  ? 31.78800  1.08900   -4.88500 1.000 23.82000 ? 65  GLN A N   1 
ATOM   380  C CA  . GLN A 1 65  ? 31.05500  2.07700   -5.66100 1.000 23.82000 ? 65  GLN A CA  1 
ATOM   381  C C   . GLN A 1 65  ? 30.77500  3.30400   -4.79600 1.000 23.82000 ? 65  GLN A C   1 
ATOM   382  O O   . GLN A 1 65  ? 30.46200  3.16700   -3.61100 1.000 23.82000 ? 65  GLN A O   1 
ATOM   383  C CB  . GLN A 1 65  ? 29.74200  1.49400   -6.17700 1.000 23.82000 ? 65  GLN A CB  1 
ATOM   384  C CG  . GLN A 1 65  ? 29.89800  0.20200   -6.94900 1.000 23.82000 ? 65  GLN A CG  1 
ATOM   385  C CD  . GLN A 1 65  ? 30.55800  0.40200   -8.29800 1.000 23.82000 ? 65  GLN A CD  1 
ATOM   386  O OE1 . GLN A 1 65  ? 30.65100  1.52300   -8.80000 1.000 23.82000 ? 65  GLN A OE1 1 
ATOM   387  N NE2 . GLN A 1 65  ? 31.01800  -0.68900  -8.89700 1.000 23.82000 ? 65  GLN A NE2 1 
ATOM   388  N N   . PRO A 1 66  ? 30.87000  4.50500   -5.35500 1.000 28.72000 ? 66  PRO A N   1 
ATOM   389  C CA  . PRO A 1 66  ? 30.52600  5.70400   -4.58700 1.000 28.72000 ? 66  PRO A CA  1 
ATOM   390  C C   . PRO A 1 66  ? 29.05000  5.72400   -4.22500 1.000 28.72000 ? 66  PRO A C   1 
ATOM   391  O O   . PRO A 1 66  ? 28.21100  5.14400   -4.91800 1.000 28.72000 ? 66  PRO A O   1 
ATOM   392  C CB  . PRO A 1 66  ? 30.88600  6.85500   -5.53600 1.000 28.72000 ? 66  PRO A CB  1 
ATOM   393  C CG  . PRO A 1 66  ? 30.84000  6.24600   -6.89600 1.000 28.72000 ? 66  PRO A CG  1 
ATOM   394  C CD  . PRO A 1 66  ? 31.29100  4.82800   -6.72900 1.000 28.72000 ? 66  PRO A CD  1 
ATOM   395  N N   . LEU A 1 67  ? 28.74100  6.40400   -3.11600 1.000 31.62000 ? 67  LEU A N   1 
ATOM   396  C CA  . LEU A 1 67  ? 27.38600  6.40300   -2.57300 1.000 31.62000 ? 67  LEU A CA  1 
ATOM   397  C C   . LEU A 1 67  ? 26.36100  6.90700   -3.58400 1.000 31.62000 ? 67  LEU A C   1 
ATOM   398  O O   . LEU A 1 67  ? 25.16500  6.63000   -3.43300 1.000 31.62000 ? 67  LEU A O   1 
ATOM   399  C CB  . LEU A 1 67  ? 27.33500  7.24800   -1.29600 1.000 31.62000 ? 67  LEU A CB  1 
ATOM   400  C CG  . LEU A 1 67  ? 26.00600  7.36000   -0.54100 1.000 31.62000 ? 67  LEU A CG  1 
ATOM   401  C CD1 . LEU A 1 67  ? 25.44800  5.98500   -0.20200 1.000 31.62000 ? 67  LEU A CD1 1 
ATOM   402  C CD2 . LEU A 1 67  ? 26.16800  8.20100   0.71600  1.000 31.62000 ? 67  LEU A CD2 1 
ATOM   403  N N   . ARG A 1 68  ? 26.80500  7.61700   -4.62100 1.000 36.32000 ? 68  ARG A N   1 
ATOM   404  C CA  . ARG A 1 68  ? 25.92700  8.00600   -5.71700 1.000 36.32000 ? 68  ARG A CA  1 
ATOM   405  C C   . ARG A 1 68  ? 25.39800  6.80600   -6.49100 1.000 36.32000 ? 68  ARG A C   1 
ATOM   406  O O   . ARG A 1 68  ? 24.48100  6.96900   -7.30300 1.000 36.32000 ? 68  ARG A O   1 
ATOM   407  C CB  . ARG A 1 68  ? 26.67000  8.96500   -6.65000 1.000 36.32000 ? 68  ARG A CB  1 
ATOM   408  C CG  . ARG A 1 68  ? 25.79500  10.03900  -7.27700 1.000 36.32000 ? 68  ARG A CG  1 
ATOM   409  C CD  . ARG A 1 68  ? 26.62700  11.23100  -7.74500 1.000 36.32000 ? 68  ARG A CD  1 
ATOM   410  N NE  . ARG A 1 68  ? 27.08000  12.06900  -6.63900 1.000 36.32000 ? 68  ARG A NE  1 
ATOM   411  C CZ  . ARG A 1 68  ? 28.27300  11.98100  -6.06400 1.000 36.32000 ? 68  ARG A CZ  1 
ATOM   412  N NH1 . ARG A 1 68  ? 29.16700  11.08900  -6.45800 1.000 36.32000 ? 68  ARG A NH1 1 
ATOM   413  N NH2 . ARG A 1 68  ? 28.57600  12.81000  -5.06900 1.000 36.32000 ? 68  ARG A NH2 1 
ATOM   414  N N   . LYS A 1 69  ? 25.96000  5.61300   -6.26600 1.000 31.64000 ? 69  LYS A N   1 
ATOM   415  C CA  . LYS A 1 69  ? 25.47100  4.41100   -6.93300 1.000 31.64000 ? 69  LYS A CA  1 
ATOM   416  C C   . LYS A 1 69  ? 24.01100  4.12800   -6.59500 1.000 31.64000 ? 69  LYS A C   1 
ATOM   417  O O   . LYS A 1 69  ? 23.28900  3.54700   -7.41300 1.000 31.64000 ? 69  LYS A O   1 
ATOM   418  C CB  . LYS A 1 69  ? 26.34600  3.21500   -6.54500 1.000 31.64000 ? 69  LYS A CB  1 
ATOM   419  C CG  . LYS A 1 69  ? 26.01700  1.91300   -7.25700 1.000 31.64000 ? 69  LYS A CG  1 
ATOM   420  C CD  . LYS A 1 69  ? 26.50600  1.92400   -8.69400 1.000 31.64000 ? 69  LYS A CD  1 
ATOM   421  C CE  . LYS A 1 69  ? 26.27500  0.57800   -9.36100 1.000 31.64000 ? 69  LYS A CE  1 
ATOM   422  N NZ  . LYS A 1 69  ? 26.99300  -0.51900  -8.65300 1.000 31.64000 ? 69  LYS A NZ  1 
ATOM   423  N N   . LEU A 1 70  ? 23.55200  4.53500   -5.40800 1.000 34.61000 ? 70  LEU A N   1 
ATOM   424  C CA  . LEU A 1 70  ? 22.17700  4.27900   -5.00300 1.000 34.61000 ? 70  LEU A CA  1 
ATOM   425  C C   . LEU A 1 70  ? 21.45400  5.49900   -4.44700 1.000 34.61000 ? 70  LEU A C   1 
ATOM   426  O O   . LEU A 1 70  ? 20.26900  5.38900   -4.11300 1.000 34.61000 ? 70  LEU A O   1 
ATOM   427  C CB  . LEU A 1 70  ? 22.12800  3.14500   -3.96500 1.000 34.61000 ? 70  LEU A CB  1 
ATOM   428  C CG  . LEU A 1 70  ? 22.83500  3.35800   -2.62300 1.000 34.61000 ? 70  LEU A CG  1 
ATOM   429  C CD1 . LEU A 1 70  ? 21.87200  3.88000   -1.56700 1.000 34.61000 ? 70  LEU A CD1 1 
ATOM   430  C CD2 . LEU A 1 70  ? 23.49400  2.07400   -2.15300 1.000 34.61000 ? 70  LEU A CD2 1 
ATOM   431  N N   . LEU A 1 71  ? 22.11600  6.64700   -4.33500 1.000 38.39000 ? 71  LEU A N   1 
ATOM   432  C CA  . LEU A 1 71  ? 21.49700  7.84900   -3.79800 1.000 38.39000 ? 71  LEU A CA  1 
ATOM   433  C C   . LEU A 1 71  ? 21.51100  8.96500   -4.83300 1.000 38.39000 ? 71  LEU A C   1 
ATOM   434  O O   . LEU A 1 71  ? 22.41500  9.05300   -5.66900 1.000 38.39000 ? 71  LEU A O   1 
ATOM   435  C CB  . LEU A 1 71  ? 22.20200  8.32200   -2.52000 1.000 38.39000 ? 71  LEU A CB  1 
ATOM   436  C CG  . LEU A 1 71  ? 21.89200  7.54000   -1.24100 1.000 38.39000 ? 71  LEU A CG  1 
ATOM   437  C CD1 . LEU A 1 71  ? 22.46700  8.24800   -0.02500 1.000 38.39000 ? 71  LEU A CD1 1 
ATOM   438  C CD2 . LEU A 1 71  ? 20.39200  7.33200   -1.08500 1.000 38.39000 ? 71  LEU A CD2 1 
ATOM   439  N N   . GLU A 1 72  ? 20.49000  9.81500   -4.76700 1.000 47.41000 ? 72  GLU A N   1 
ATOM   440  C CA  . GLU A 1 72  ? 20.39500  10.95600  -5.66400 1.000 47.41000 ? 72  GLU A CA  1 
ATOM   441  C C   . GLU A 1 72  ? 21.38700  12.04200  -5.26100 1.000 47.41000 ? 72  GLU A C   1 
ATOM   442  O O   . GLU A 1 72  ? 21.75100  12.18000  -4.09100 1.000 47.41000 ? 72  GLU A O   1 
ATOM   443  C CB  . GLU A 1 72  ? 18.97300  11.51400  -5.66500 1.000 47.41000 ? 72  GLU A CB  1 
ATOM   444  C CG  . GLU A 1 72  ? 17.92400  10.48800  -6.05300 1.000 47.41000 ? 72  GLU A CG  1 
ATOM   445  C CD  . GLU A 1 72  ? 18.32500  9.68200   -7.27300 1.000 47.41000 ? 72  GLU A CD  1 
ATOM   446  O OE1 . GLU A 1 72  ? 18.64100  10.29000  -8.31800 1.000 47.41000 ? 72  GLU A OE1 1 
ATOM   447  O OE2 . GLU A 1 72  ? 18.33600  8.43600   -7.18400 1.000 47.41000 ? 72  GLU A OE2 1 
ATOM   448  N N   . SER A 1 73  ? 21.82400  12.81900  -6.25700 1.000 48.81000 ? 73  SER A N   1 
ATOM   449  C CA  . SER A 1 73  ? 22.80900  13.86600  -6.00300 1.000 48.81000 ? 73  SER A CA  1 
ATOM   450  C C   . SER A 1 73  ? 22.27500  14.92900  -5.05300 1.000 48.81000 ? 73  SER A C   1 
ATOM   451  O O   . SER A 1 73  ? 23.05400  15.56100  -4.33200 1.000 48.81000 ? 73  SER A O   1 
ATOM   452  C CB  . SER A 1 73  ? 23.25000  14.50100  -7.32100 1.000 48.81000 ? 73  SER A CB  1 
ATOM   453  O OG  . SER A 1 73  ? 23.86000  13.54200  -8.16800 1.000 48.81000 ? 73  SER A OG  1 
ATOM   454  N N   . GLU A 1 74  ? 20.95900  15.14900  -5.03700 1.000 51.42000 ? 74  GLU A N   1 
ATOM   455  C CA  . GLU A 1 74  ? 20.38500  16.07400  -4.06400 1.000 51.42000 ? 74  GLU A CA  1 
ATOM   456  C C   . GLU A 1 74  ? 20.42000  15.48600  -2.65700 1.000 51.42000 ? 74  GLU A C   1 
ATOM   457  O O   . GLU A 1 74  ? 20.77700  16.17800  -1.69300 1.000 51.42000 ? 74  GLU A O   1 
ATOM   458  C CB  . GLU A 1 74  ? 18.95800  16.43600  -4.47200 1.000 51.42000 ? 74  GLU A CB  1 
ATOM   459  C CG  . GLU A 1 74  ? 18.87000  17.13800  -5.82000 1.000 51.42000 ? 74  GLU A CG  1 
ATOM   460  C CD  . GLU A 1 74  ? 17.45800  17.18700  -6.36700 1.000 51.42000 ? 74  GLU A CD  1 
ATOM   461  O OE1 . GLU A 1 74  ? 16.51500  16.87000  -5.61100 1.000 51.42000 ? 74  GLU A OE1 1 
ATOM   462  O OE2 . GLU A 1 74  ? 17.29100  17.53700  -7.55500 1.000 51.42000 ? 74  GLU A OE2 1 
ATOM   463  N N   . GLN A 1 75  ? 20.07300  14.20300  -2.51800 1.000 42.58000 ? 75  GLN A N   1 
ATOM   464  C CA  . GLN A 1 75  ? 20.21400  13.54700  -1.22300 1.000 42.58000 ? 75  GLN A CA  1 
ATOM   465  C C   . GLN A 1 75  ? 21.67300  13.47700  -0.80000 1.000 42.58000 ? 75  GLN A C   1 
ATOM   466  O O   . GLN A 1 75  ? 21.98100  13.55400  0.39500  1.000 42.58000 ? 75  GLN A O   1 
ATOM   467  C CB  . GLN A 1 75  ? 19.61100  12.14200  -1.27400 1.000 42.58000 ? 75  GLN A CB  1 
ATOM   468  C CG  . GLN A 1 75  ? 18.18100  12.09400  -1.78800 1.000 42.58000 ? 75  GLN A CG  1 
ATOM   469  C CD  . GLN A 1 75  ? 17.58100  10.70200  -1.72300 1.000 42.58000 ? 75  GLN A CD  1 
ATOM   470  O OE1 . GLN A 1 75  ? 16.96300  10.32700  -0.72700 1.000 42.58000 ? 75  GLN A OE1 1 
ATOM   471  N NE2 . GLN A 1 75  ? 17.75900  9.92800   -2.78800 1.000 42.58000 ? 75  GLN A NE2 1 
ATOM   472  N N   . ILE A 1 76  ? 22.58500  13.34000  -1.76300 1.000 39.83000 ? 76  ILE A N   1 
ATOM   473  C CA  . ILE A 1 76  ? 24.00700  13.33800  -1.44200 1.000 39.83000 ? 76  ILE A CA  1 
ATOM   474  C C   . ILE A 1 76  ? 24.46800  14.72400  -1.00500 1.000 39.83000 ? 76  ILE A C   1 
ATOM   475  O O   . ILE A 1 76  ? 25.32000  14.85500  -0.12100 1.000 39.83000 ? 76  ILE A O   1 
ATOM   476  C CB  . ILE A 1 76  ? 24.81100  12.80900  -2.64100 1.000 39.83000 ? 76  ILE A CB  1 
ATOM   477  C CG1 . ILE A 1 76  ? 24.58400  11.30600  -2.78000 1.000 39.83000 ? 76  ILE A CG1 1 
ATOM   478  C CG2 . ILE A 1 76  ? 26.28900  13.11900  -2.49300 1.000 39.83000 ? 76  ILE A CG2 1 
ATOM   479  C CD1 . ILE A 1 76  ? 25.68000  10.61100  -3.50700 1.000 39.83000 ? 76  ILE A CD1 1 
ATOM   480  N N   . ASP A 1 77  ? 23.90700  15.77900  -1.60100 1.000 44.47000 ? 77  ASP A N   1 
ATOM   481  C CA  . ASP A 1 77  ? 24.20700  17.12800  -1.13100 1.000 44.47000 ? 77  ASP A CA  1 
ATOM   482  C C   . ASP A 1 77  ? 23.69600  17.32100  0.29000  1.000 44.47000 ? 77  ASP A C   1 
ATOM   483  O O   . ASP A 1 77  ? 24.36500  17.94200  1.12700  1.000 44.47000 ? 77  ASP A O   1 
ATOM   484  C CB  . ASP A 1 77  ? 23.58400  18.15600  -2.08100 1.000 44.47000 ? 77  ASP A CB  1 
ATOM   485  C CG  . ASP A 1 77  ? 24.16800  19.55200  -1.91800 1.000 44.47000 ? 77  ASP A CG  1 
ATOM   486  O OD1 . ASP A 1 77  ? 24.55700  19.92700  -0.79200 1.000 44.47000 ? 77  ASP A OD1 1 
ATOM   487  O OD2 . ASP A 1 77  ? 24.23000  20.28400  -2.92800 1.000 44.47000 ? 77  ASP A OD2 1 
ATOM   488  N N   . PHE A 1 78  ? 22.53600  16.73400  0.59300  1.000 40.85000 ? 78  PHE A N   1 
ATOM   489  C CA  . PHE A 1 78  ? 22.00500  16.78600  1.95000  1.000 40.85000 ? 78  PHE A CA  1 
ATOM   490  C C   . PHE A 1 78  ? 22.94100  16.07800  2.92200  1.000 40.85000 ? 78  PHE A C   1 
ATOM   491  O O   . PHE A 1 78  ? 23.28900  16.61900  3.97800  1.000 40.85000 ? 78  PHE A O   1 
ATOM   492  C CB  . PHE A 1 78  ? 20.60900  16.15600  1.97500  1.000 40.85000 ? 78  PHE A CB  1 
ATOM   493  C CG  . PHE A 1 78  ? 19.92800  16.21400  3.31400  1.000 40.85000 ? 78  PHE A CG  1 
ATOM   494  C CD1 . PHE A 1 78  ? 19.14400  17.30300  3.65800  1.000 40.85000 ? 78  PHE A CD1 1 
ATOM   495  C CD2 . PHE A 1 78  ? 20.04900  15.16900  4.21700  1.000 40.85000 ? 78  PHE A CD2 1 
ATOM   496  C CE1 . PHE A 1 78  ? 18.50800  17.35800  4.88300  1.000 40.85000 ? 78  PHE A CE1 1 
ATOM   497  C CE2 . PHE A 1 78  ? 19.41500  15.21800  5.44400  1.000 40.85000 ? 78  PHE A CE2 1 
ATOM   498  C CZ  . PHE A 1 78  ? 18.64300  16.31400  5.77700  1.000 40.85000 ? 78  PHE A CZ  1 
ATOM   499  N N   . LEU A 1 79  ? 23.38100  14.87000  2.56400  1.000 35.67000 ? 79  LEU A N   1 
ATOM   500  C CA  . LEU A 1 79  ? 24.27700  14.11600  3.43400  1.000 35.67000 ? 79  LEU A CA  1 
ATOM   501  C C   . LEU A 1 79  ? 25.62500  14.81100  3.59700  1.000 35.67000 ? 79  LEU A C   1 
ATOM   502  O O   . LEU A 1 79  ? 26.22300  14.75400  4.67700  1.000 35.67000 ? 79  LEU A O   1 
ATOM   503  C CB  . LEU A 1 79  ? 24.46000  12.69900  2.88400  1.000 35.67000 ? 79  LEU A CB  1 
ATOM   504  C CG  . LEU A 1 79  ? 25.16400  11.64200  3.74100  1.000 35.67000 ? 79  LEU A CG  1 
ATOM   505  C CD1 . LEU A 1 79  ? 24.62500  10.26400  3.40500  1.000 35.67000 ? 79  LEU A CD1 1 
ATOM   506  C CD2 . LEU A 1 79  ? 26.67500  11.67100  3.54600  1.000 35.67000 ? 79  LEU A CD2 1 
ATOM   507  N N   . ASN A 1 80  ? 26.11700  15.47400  2.54900  1.000 37.50000 ? 80  ASN A N   1 
ATOM   508  C CA  . ASN A 1 80  ? 27.38500  16.18500  2.66700  1.000 37.50000 ? 80  ASN A CA  1 
ATOM   509  C C   . ASN A 1 80  ? 27.25000  17.41400  3.55100  1.000 37.50000 ? 80  ASN A C   1 
ATOM   510  O O   . ASN A 1 80  ? 28.17500  17.74800  4.30000  1.000 37.50000 ? 80  ASN A O   1 
ATOM   511  C CB  . ASN A 1 80  ? 27.91000  16.57000  1.28500  1.000 37.50000 ? 80  ASN A CB  1 
ATOM   512  C CG  . ASN A 1 80  ? 28.61400  15.42300  0.59500  1.000 37.50000 ? 80  ASN A CG  1 
ATOM   513  O OD1 . ASN A 1 80  ? 29.80700  15.19200  0.80200  1.000 37.50000 ? 80  ASN A OD1 1 
ATOM   514  N ND2 . ASN A 1 80  ? 27.87800  14.69300  -0.22800 1.000 37.50000 ? 80  ASN A ND2 1 
ATOM   515  N N   . ASP A 1 81  ? 26.10700  18.10300  3.48300  1.000 41.59000 ? 81  ASP A N   1 
ATOM   516  C CA  . ASP A 1 81  ? 25.86600  19.18600  4.42900  1.000 41.59000 ? 81  ASP A CA  1 
ATOM   517  C C   . ASP A 1 81  ? 25.75800  18.65600  5.85100  1.000 41.59000 ? 81  ASP A C   1 
ATOM   518  O O   . ASP A 1 81  ? 26.15200  19.33900  6.80300  1.000 41.59000 ? 81  ASP A O   1 
ATOM   519  C CB  . ASP A 1 81  ? 24.60400  19.95700  4.04600  1.000 41.59000 ? 81  ASP A CB  1 
ATOM   520  C CG  . ASP A 1 81  ? 24.82200  20.88100  2.86500  1.000 41.59000 ? 81  ASP A CG  1 
ATOM   521  O OD1 . ASP A 1 81  ? 25.92600  20.85100  2.28200  1.000 41.59000 ? 81  ASP A OD1 1 
ATOM   522  O OD2 . ASP A 1 81  ? 23.89200  21.64300  2.52400  1.000 41.59000 ? 81  ASP A OD2 1 
ATOM   523  N N   . CYS A 1 82  ? 25.22700  17.44300  6.01300  1.000 35.49000 ? 82  CYS A N   1 
ATOM   524  C CA  . CYS A 1 82  ? 25.23300  16.81100  7.32800  1.000 35.49000 ? 82  CYS A CA  1 
ATOM   525  C C   . CYS A 1 82  ? 26.64900  16.48500  7.78800  1.000 35.49000 ? 82  CYS A C   1 
ATOM   526  O O   . CYS A 1 82  ? 26.93600  16.53000  8.99000  1.000 35.49000 ? 82  CYS A O   1 
ATOM   527  C CB  . CYS A 1 82  ? 24.38300  15.54300  7.30000  1.000 35.49000 ? 82  CYS A CB  1 
ATOM   528  S SG  . CYS A 1 82  ? 22.67300  15.81600  6.78800  1.000 35.49000 ? 82  CYS A SG  1 
ATOM   529  N N   . LEU A 1 83  ? 27.54100  16.15300  6.85200  1.000 36.57000 ? 83  LEU A N   1 
ATOM   530  C CA  . LEU A 1 83  ? 28.92500  15.86000  7.21300  1.000 36.57000 ? 83  LEU A CA  1 
ATOM   531  C C   . LEU A 1 83  ? 29.66200  17.09900  7.70900  1.000 36.57000 ? 83  LEU A C   1 
ATOM   532  O O   . LEU A 1 83  ? 30.58700  16.97900  8.52200  1.000 36.57000 ? 83  LEU A O   1 
ATOM   533  C CB  . LEU A 1 83  ? 29.65900  15.25000  6.01900  1.000 36.57000 ? 83  LEU A CB  1 
ATOM   534  C CG  . LEU A 1 83  ? 29.24200  13.83700  5.61300  1.000 36.57000 ? 83  LEU A CG  1 
ATOM   535  C CD1 . LEU A 1 83  ? 29.96500  13.42700  4.34400  1.000 36.57000 ? 83  LEU A CD1 1 
ATOM   536  C CD2 . LEU A 1 83  ? 29.53000  12.85700  6.73500  1.000 36.57000 ? 83  LEU A CD2 1 
ATOM   537  N N   . THR A 1 84  ? 29.27200  18.28800  7.23700  1.000 43.12000 ? 84  THR A N   1 
ATOM   538  C CA  . THR A 1 84  ? 29.93300  19.52300  7.64800  1.000 43.12000 ? 84  THR A CA  1 
ATOM   539  C C   . THR A 1 84  ? 29.73400  19.83700  9.12500  1.000 43.12000 ? 84  THR A C   1 
ATOM   540  O O   . THR A 1 84  ? 30.56500  20.53900  9.71000  1.000 43.12000 ? 84  THR A O   1 
ATOM   541  C CB  . THR A 1 84  ? 29.42900  20.70500  6.81400  1.000 43.12000 ? 84  THR A CB  1 
ATOM   542  O OG1 . THR A 1 84  ? 28.04600  20.94700  7.10900  1.000 43.12000 ? 84  THR A OG1 1 
ATOM   543  C CG2 . THR A 1 84  ? 29.58300  20.42700  5.32300  1.000 43.12000 ? 84  THR A CG2 1 
ATOM   544  N N   . GLN A 1 85  ? 28.65700  19.34700  9.73500  1.000 46.69000 ? 85  GLN A N   1 
ATOM   545  C CA  . GLN A 1 85  ? 28.36300  19.65800  11.12700 1.000 46.69000 ? 85  GLN A CA  1 
ATOM   546  C C   . GLN A 1 85  ? 29.40000  19.04400  12.06000 1.000 46.69000 ? 85  GLN A C   1 
ATOM   547  O O   . GLN A 1 85  ? 30.03500  18.03500  11.74200 1.000 46.69000 ? 85  GLN A O   1 
ATOM   548  C CB  . GLN A 1 85  ? 26.96700  19.16200  11.50200 1.000 46.69000 ? 85  GLN A CB  1 
ATOM   549  C CG  . GLN A 1 85  ? 25.85500  19.93500  10.83300 1.000 46.69000 ? 85  GLN A CG  1 
ATOM   550  C CD  . GLN A 1 85  ? 25.92600  21.41400  11.14400 1.000 46.69000 ? 85  GLN A CD  1 
ATOM   551  O OE1 . GLN A 1 85  ? 26.08600  21.80800  12.29800 1.000 46.69000 ? 85  GLN A OE1 1 
ATOM   552  N NE2 . GLN A 1 85  ? 25.82400  22.24200  10.11100 1.000 46.69000 ? 85  GLN A NE2 1 
ATOM   553  N N   . GLU A 1 86  ? 29.58000  19.68000  13.22300 1.000 54.25000 ? 86  GLU A N   1 
ATOM   554  C CA  . GLU A 1 86  ? 30.55600  19.19200  14.19500 1.000 54.25000 ? 86  GLU A CA  1 
ATOM   555  C C   . GLU A 1 86  ? 30.23300  17.77000  14.63500 1.000 54.25000 ? 86  GLU A C   1 
ATOM   556  O O   . GLU A 1 86  ? 31.13400  16.93700  14.79100 1.000 54.25000 ? 86  GLU A O   1 
ATOM   557  C CB  . GLU A 1 86  ? 30.58600  20.11900  15.40900 1.000 54.25000 ? 86  GLU A CB  1 
ATOM   558  C CG  . GLU A 1 86  ? 30.42700  21.59400  15.07700 1.000 54.25000 ? 86  GLU A CG  1 
ATOM   559  C CD  . GLU A 1 86  ? 31.71500  22.22300  14.59300 1.000 54.25000 ? 86  GLU A CD  1 
ATOM   560  O OE1 . GLU A 1 86  ? 32.79300  21.65300  14.86400 1.000 54.25000 ? 86  GLU A OE1 1 
ATOM   561  O OE2 . GLU A 1 86  ? 31.65000  23.28800  13.94400 1.000 54.25000 ? 86  GLU A OE2 1 
ATOM   562  N N   . ASP A 1 87  ? 28.95100  17.46800  14.80600 1.000 47.79000 ? 87  ASP A N   1 
ATOM   563  C CA  . ASP A 1 87  ? 28.47200  16.12000  15.06800 1.000 47.79000 ? 87  ASP A CA  1 
ATOM   564  C C   . ASP A 1 87  ? 27.36800  15.82600  14.06600 1.000 47.79000 ? 87  ASP A C   1 
ATOM   565  O O   . ASP A 1 87  ? 26.40500  16.59100  13.95900 1.000 47.79000 ? 87  ASP A O   1 
ATOM   566  C CB  . ASP A 1 87  ? 27.95600  15.97700  16.50400 1.000 47.79000 ? 87  ASP A CB  1 
ATOM   567  C CG  . ASP A 1 87  ? 27.55000  14.55100  16.84300 1.000 47.79000 ? 87  ASP A CG  1 
ATOM   568  O OD1 . ASP A 1 87  ? 27.75300  13.64900  16.00100 1.000 47.79000 ? 87  ASP A OD1 1 
ATOM   569  O OD2 . ASP A 1 87  ? 27.02600  14.33000  17.95600 1.000 47.79000 ? 87  ASP A OD2 1 
ATOM   570  N N   . ILE A 1 88  ? 27.52100  14.73200  13.31700 1.000 38.64000 ? 88  ILE A N   1 
ATOM   571  C CA  . ILE A 1 88  ? 26.52400  14.40600  12.30300 1.000 38.64000 ? 88  ILE A CA  1 
ATOM   572  C C   . ILE A 1 88  ? 25.19400  14.03900  12.94800 1.000 38.64000 ? 88  ILE A C   1 
ATOM   573  O O   . ILE A 1 88  ? 24.12800  14.24800  12.35400 1.000 38.64000 ? 88  ILE A O   1 
ATOM   574  C CB  . ILE A 1 88  ? 27.03000  13.27800  11.39000 1.000 38.64000 ? 88  ILE A CB  1 
ATOM   575  C CG1 . ILE A 1 88  ? 28.54800  13.34200  11.24900 1.000 38.64000 ? 88  ILE A CG1 1 
ATOM   576  C CG2 . ILE A 1 88  ? 26.38900  13.39300  10.02000 1.000 38.64000 ? 88  ILE A CG2 1 
ATOM   577  C CD1 . ILE A 1 88  ? 29.09600  12.28700  10.32400 1.000 38.64000 ? 88  ILE A CD1 1 
ATOM   578  N N   . GLN A 1 89  ? 25.22400  13.53500  14.18200 1.000 38.79000 ? 89  GLN A N   1 
ATOM   579  C CA  . GLN A 1 89  ? 24.02200  13.02700  14.83100 1.000 38.79000 ? 89  GLN A CA  1 
ATOM   580  C C   . GLN A 1 89  ? 23.00500  14.12200  15.12200 1.000 38.79000 ? 89  GLN A C   1 
ATOM   581  O O   . GLN A 1 89  ? 21.87800  13.80600  15.51800 1.000 38.79000 ? 89  GLN A O   1 
ATOM   582  C CB  . GLN A 1 89  ? 24.39900  12.29400  16.11800 1.000 38.79000 ? 89  GLN A CB  1 
ATOM   583  C CG  . GLN A 1 89  ? 25.18400  11.01600  15.87200 1.000 38.79000 ? 89  GLN A CG  1 
ATOM   584  C CD  . GLN A 1 89  ? 25.54500  10.29500  17.15300 1.000 38.79000 ? 89  GLN A CD  1 
ATOM   585  O OE1 . GLN A 1 89  ? 26.13500  10.87900  18.06200 1.000 38.79000 ? 89  GLN A OE1 1 
ATOM   586  N NE2 . GLN A 1 89  ? 25.18700  9.01900   17.23500 1.000 38.79000 ? 89  GLN A NE2 1 
ATOM   587  N N   . ILE A 1 90  ? 23.37800  15.39100  14.94400 1.000 36.65000 ? 90  ILE A N   1 
ATOM   588  C CA  . ILE A 1 90  ? 22.41000  16.47800  15.03300 1.000 36.65000 ? 90  ILE A CA  1 
ATOM   589  C C   . ILE A 1 90  ? 21.30000  16.29000  14.00700 1.000 36.65000 ? 90  ILE A C   1 
ATOM   590  O O   . ILE A 1 90  ? 20.15200  16.69300  14.23500 1.000 36.65000 ? 90  ILE A O   1 
ATOM   591  C CB  . ILE A 1 90  ? 23.13600  17.82700  14.84600 1.000 36.65000 ? 90  ILE A CB  1 
ATOM   592  C CG1 . ILE A 1 90  ? 24.26200  17.97300  15.87300 1.000 36.65000 ? 90  ILE A CG1 1 
ATOM   593  C CG2 . ILE A 1 90  ? 22.16700  18.99000  14.94300 1.000 36.65000 ? 90  ILE A CG2 1 
ATOM   594  C CD1 . ILE A 1 90  ? 25.13900  19.18800  15.65200 1.000 36.65000 ? 90  ILE A CD1 1 
ATOM   595  N N   . VAL A 1 91  ? 21.61100  15.65700  12.87500 1.000 34.12000 ? 91  VAL A N   1 
ATOM   596  C CA  . VAL A 1 91  ? 20.64200  15.43900  11.80700 1.000 34.12000 ? 91  VAL A CA  1 
ATOM   597  C C   . VAL A 1 91  ? 20.12500  14.00300  11.79400 1.000 34.12000 ? 91  VAL A C   1 
ATOM   598  O O   . VAL A 1 91  ? 19.39200  13.61900  10.87700 1.000 34.12000 ? 91  VAL A O   1 
ATOM   599  C CB  . VAL A 1 91  ? 21.25400  15.81300  10.44800 1.000 34.12000 ? 91  VAL A CB  1 
ATOM   600  C CG1 . VAL A 1 91  ? 22.15000  14.68600  9.95000  1.000 34.12000 ? 91  VAL A CG1 1 
ATOM   601  C CG2 . VAL A 1 91  ? 20.17200  16.16900  9.43200  1.000 34.12000 ? 91  VAL A CG2 1 
ATOM   602  N N   . ASN A 1 92  ? 20.43600  13.22300  12.82900 1.000 33.37000 ? 92  ASN A N   1 
ATOM   603  C CA  . ASN A 1 92  ? 20.50600  11.76600  12.70700 1.000 33.37000 ? 92  ASN A CA  1 
ATOM   604  C C   . ASN A 1 92  ? 19.26500  11.10600  12.11400 1.000 33.37000 ? 92  ASN A C   1 
ATOM   605  O O   . ASN A 1 92  ? 19.42400  10.25500  11.22600 1.000 33.37000 ? 92  ASN A O   1 
ATOM   606  C CB  . ASN A 1 92  ? 20.85100  11.16100  14.07200 1.000 33.37000 ? 92  ASN A CB  1 
ATOM   607  C CG  . ASN A 1 92  ? 21.68800  9.90800   13.94900 1.000 33.37000 ? 92  ASN A CG  1 
ATOM   608  O OD1 . ASN A 1 92  ? 22.14400  9.56300   12.85800 1.000 33.37000 ? 92  ASN A OD1 1 
ATOM   609  N ND2 . ASN A 1 92  ? 21.90400  9.22300   15.06500 1.000 33.37000 ? 92  ASN A ND2 1 
ATOM   610  N N   . PRO A 1 93  ? 18.02200  11.41800  12.53700 1.000 30.95000 ? 93  PRO A N   1 
ATOM   611  C CA  . PRO A 1 93  ? 16.87000  10.73000  11.92900 1.000 30.95000 ? 93  PRO A CA  1 
ATOM   612  C C   . PRO A 1 93  ? 16.66300  11.09600  10.46400 1.000 30.95000 ? 93  PRO A C   1 
ATOM   613  O O   . PRO A 1 93  ? 15.65400  11.71200  10.10600 1.000 30.95000 ? 93  PRO A O   1 
ATOM   614  C CB  . PRO A 1 93  ? 15.68600  11.19000  12.79200 1.000 30.95000 ? 93  PRO A CB  1 
ATOM   615  C CG  . PRO A 1 93  ? 16.29800  11.69500  14.05700 1.000 30.95000 ? 93  PRO A CG  1 
ATOM   616  C CD  . PRO A 1 93  ? 17.60200  12.29200  13.64600 1.000 30.95000 ? 93  PRO A CD  1 
ATOM   617  N N   . VAL A 1 94  ? 17.61400  10.70600  9.60700  1.000 31.40000 ? 94  VAL A N   1 
ATOM   618  C CA  . VAL A 1 94  ? 17.56400  11.07800  8.19100  1.000 31.40000 ? 94  VAL A CA  1 
ATOM   619  C C   . VAL A 1 94  ? 16.47800  10.27800  7.47600  1.000 31.40000 ? 94  VAL A C   1 
ATOM   620  O O   . VAL A 1 94  ? 16.07700  9.19600   7.90800  1.000 31.40000 ? 94  VAL A O   1 
ATOM   621  C CB  . VAL A 1 94  ? 18.94100  10.86700  7.53700  1.000 31.40000 ? 94  VAL A CB  1 
ATOM   622  C CG1 . VAL A 1 94  ? 18.97700  11.43600  6.12500  1.000 31.40000 ? 94  VAL A CG1 1 
ATOM   623  C CG2 . VAL A 1 94  ? 20.02900  11.50100  8.38400  1.000 31.40000 ? 94  VAL A CG2 1 
ATOM   624  N N   . GLU A 1 95  ? 15.97000  10.83600  6.37800  1.000 35.32000 ? 95  GLU A N   1 
ATOM   625  C CA  . GLU A 1 95  ? 15.06600  10.11600  5.48500  1.000 35.32000 ? 95  GLU A CA  1 
ATOM   626  C C   . GLU A 1 95  ? 15.63800  10.15000  4.07300  1.000 35.32000 ? 95  GLU A C   1 
ATOM   627  O O   . GLU A 1 95  ? 15.74500  11.22200  3.46700  1.000 35.32000 ? 95  GLU A O   1 
ATOM   628  C CB  . GLU A 1 95  ? 13.65800  10.70600  5.51700  1.000 35.32000 ? 95  GLU A CB  1 
ATOM   629  C CG  . GLU A 1 95  ? 12.75200  10.15700  4.42700  1.000 35.32000 ? 95  GLU A CG  1 
ATOM   630  C CD  . GLU A 1 95  ? 11.28800  10.46200  4.66700  1.000 35.32000 ? 95  GLU A CD  1 
ATOM   631  O OE1 . GLU A 1 95  ? 10.77700  10.12000  5.75500  1.000 35.32000 ? 95  GLU A OE1 1 
ATOM   632  O OE2 . GLU A 1 95  ? 10.64700  11.04300  3.76600  1.000 35.32000 ? 95  GLU A OE2 1 
ATOM   633  N N   . PHE A 1 96  ? 16.01500  8.98200   3.56000  1.000 35.88000 ? 96  PHE A N   1 
ATOM   634  C CA  . PHE A 1 96  ? 16.42800  8.81000   2.17600  1.000 35.88000 ? 96  PHE A CA  1 
ATOM   635  C C   . PHE A 1 96  ? 15.35700  8.04700   1.40800  1.000 35.88000 ? 96  PHE A C   1 
ATOM   636  O O   . PHE A 1 96  ? 14.47600  7.41100   1.99100  1.000 35.88000 ? 96  PHE A O   1 
ATOM   637  C CB  . PHE A 1 96  ? 17.76500  8.06900   2.08000  1.000 35.88000 ? 96  PHE A CB  1 
ATOM   638  C CG  . PHE A 1 96  ? 18.93900  8.86900   2.56100  1.000 35.88000 ? 96  PHE A CG  1 
ATOM   639  C CD1 . PHE A 1 96  ? 19.23800  10.09300  1.99000  1.000 35.88000 ? 96  PHE A CD1 1 
ATOM   640  C CD2 . PHE A 1 96  ? 19.75100  8.39300   3.57500  1.000 35.88000 ? 96  PHE A CD2 1 
ATOM   641  C CE1 . PHE A 1 96  ? 20.32100  10.83300  2.42900  1.000 35.88000 ? 96  PHE A CE1 1 
ATOM   642  C CE2 . PHE A 1 96  ? 20.83600  9.12800   4.01700  1.000 35.88000 ? 96  PHE A CE2 1 
ATOM   643  C CZ  . PHE A 1 96  ? 21.12000  10.34800  3.44300  1.000 35.88000 ? 96  PHE A CZ  1 
ATOM   644  N N   . THR A 1 97  ? 15.43600  8.12600   0.08200  1.000 40.21000 ? 97  THR A N   1 
ATOM   645  C CA  . THR A 1 97  ? 14.56600  7.34900   -0.78700 1.000 40.21000 ? 97  THR A CA  1 
ATOM   646  C C   . THR A 1 97  ? 15.39700  6.73800   -1.90400 1.000 40.21000 ? 97  THR A C   1 
ATOM   647  O O   . THR A 1 97  ? 16.28200  7.39300   -2.46100 1.000 40.21000 ? 97  THR A O   1 
ATOM   648  C CB  . THR A 1 97  ? 13.43500  8.20400   -1.37800 1.000 40.21000 ? 97  THR A CB  1 
ATOM   649  O OG1 . THR A 1 97  ? 13.95600  9.47300   -1.79600 1.000 40.21000 ? 97  THR A OG1 1 
ATOM   650  C CG2 . THR A 1 97  ? 12.33300  8.41800   -0.35000 1.000 40.21000 ? 97  THR A CG2 1 
ATOM   651  N N   . ILE A 1 98  ? 15.10500  5.48000   -2.22400 1.000 42.68000 ? 98  ILE A N   1 
ATOM   652  C CA  . ILE A 1 98  ? 15.85500  4.74900   -3.23700 1.000 42.68000 ? 98  ILE A CA  1 
ATOM   653  C C   . ILE A 1 98  ? 14.90000  4.15400   -4.26500 1.000 42.68000 ? 98  ILE A C   1 
ATOM   654  O O   . ILE A 1 98  ? 14.01800  3.36800   -3.92200 1.000 42.68000 ? 98  ILE A O   1 
ATOM   655  C CB  . ILE A 1 98  ? 16.72600  3.64700   -2.60600 1.000 42.68000 ? 98  ILE A CB  1 
ATOM   656  C CG1 . ILE A 1 98  ? 17.55200  4.20900   -1.44800 1.000 42.68000 ? 98  ILE A CG1 1 
ATOM   657  C CG2 . ILE A 1 98  ? 17.64200  3.03400   -3.65100 1.000 42.68000 ? 98  ILE A CG2 1 
ATOM   658  C CD1 . ILE A 1 98  ? 18.37200  3.16700   -0.72300 1.000 42.68000 ? 98  ILE A CD1 1 
ATOM   659  N N   . GLU A 1 103 ? 9.99600   1.79500   -8.09000 1.000 59.21000 ? 103 GLU A N   1 
ATOM   660  C CA  . GLU A 1 103 ? 9.98900   1.45800   -6.67100 1.000 59.21000 ? 103 GLU A CA  1 
ATOM   661  C C   . GLU A 1 103 ? 10.59500  2.57300   -5.81800 1.000 59.21000 ? 103 GLU A C   1 
ATOM   662  O O   . GLU A 1 103 ? 11.77600  2.52900   -5.47400 1.000 59.21000 ? 103 GLU A O   1 
ATOM   663  C CB  . GLU A 1 103 ? 10.74100  0.14500   -6.43300 1.000 59.21000 ? 103 GLU A CB  1 
ATOM   664  C CG  . GLU A 1 103 ? 12.04100  0.01800   -7.21500 1.000 59.21000 ? 103 GLU A CG  1 
ATOM   665  C CD  . GLU A 1 103 ? 12.99400  -0.98900  -6.60400 1.000 59.21000 ? 103 GLU A CD  1 
ATOM   666  O OE1 . GLU A 1 103 ? 12.56700  -1.74600  -5.70600 1.000 59.21000 ? 103 GLU A OE1 1 
ATOM   667  O OE2 . GLU A 1 103 ? 14.17300  -1.01800  -7.01500 1.000 59.21000 ? 103 GLU A OE2 1 
ATOM   668  N N   . PRO A 1 104 ? 9.78800   3.58000   -5.48100 1.000 55.52000 ? 104 PRO A N   1 
ATOM   669  C CA  . PRO A 1 104 ? 10.27300  4.65800   -4.58900 1.000 55.52000 ? 104 PRO A CA  1 
ATOM   670  C C   . PRO A 1 104 ? 10.30100  4.22300   -3.12700 1.000 55.52000 ? 104 PRO A C   1 
ATOM   671  O O   . PRO A 1 104 ? 9.51900   4.67600   -2.28300 1.000 55.52000 ? 104 PRO A O   1 
ATOM   672  C CB  . PRO A 1 104 ? 9.26400   5.78600   -4.85000 1.000 55.52000 ? 104 PRO A CB  1 
ATOM   673  C CG  . PRO A 1 104 ? 8.50100   5.38600   -6.08800 1.000 55.52000 ? 104 PRO A CG  1 
ATOM   674  C CD  . PRO A 1 104 ? 8.47800   3.90000   -6.06400 1.000 55.52000 ? 104 PRO A CD  1 
ATOM   675  N N   . ILE A 1 105 ? 11.21700  3.30500   -2.80900 1.000 47.13000 ? 105 ILE A N   1 
ATOM   676  C CA  . ILE A 1 105 ? 11.34600  2.82100   -1.44000 1.000 47.13000 ? 105 ILE A CA  1 
ATOM   677  C C   . ILE A 1 105 ? 11.83800  3.94900   -0.54300 1.000 47.13000 ? 105 ILE A C   1 
ATOM   678  O O   . ILE A 1 105 ? 12.73600  4.71700   -0.91300 1.000 47.13000 ? 105 ILE A O   1 
ATOM   679  C CB  . ILE A 1 105 ? 12.29500  1.61200   -1.38100 1.000 47.13000 ? 105 ILE A CB  1 
ATOM   680  C CG1 . ILE A 1 105 ? 12.12600  0.73400   -2.62300 1.000 47.13000 ? 105 ILE A CG1 1 
ATOM   681  C CG2 . ILE A 1 105 ? 12.02900  0.79500   -0.12700 1.000 47.13000 ? 105 ILE A CG2 1 
ATOM   682  C CD1 . ILE A 1 105 ? 13.05900  -0.45900  -2.65700 1.000 47.13000 ? 105 ILE A CD1 1 
ATOM   683  N N   . ILE A 1 106 ? 11.25300  4.04900   0.64800  1.000 39.02000 ? 106 ILE A N   1 
ATOM   684  C CA  . ILE A 1 106 ? 11.59800  5.07900   1.62100  1.000 39.02000 ? 106 ILE A CA  1 
ATOM   685  C C   . ILE A 1 106 ? 12.32400  4.41900   2.78400  1.000 39.02000 ? 106 ILE A C   1 
ATOM   686  O O   . ILE A 1 106 ? 11.95900  3.31800   3.21400  1.000 39.02000 ? 106 ILE A O   1 
ATOM   687  C CB  . ILE A 1 106 ? 10.35100  5.84300   2.11100  1.000 39.02000 ? 106 ILE A CB  1 
ATOM   688  C CG1 . ILE A 1 106 ? 9.46200   6.24200   0.93000  1.000 39.02000 ? 106 ILE A CG1 1 
ATOM   689  C CG2 . ILE A 1 106 ? 10.75500  7.08100   2.89500  1.000 39.02000 ? 106 ILE A CG2 1 
ATOM   690  C CD1 . ILE A 1 106 ? 8.29100   5.30500   0.69200  1.000 39.02000 ? 106 ILE A CD1 1 
ATOM   691  N N   . PHE A 1 107 ? 13.34800  5.09900   3.30000  1.000 34.29000 ? 107 PHE A N   1 
ATOM   692  C CA  . PHE A 1 107 ? 14.16500  4.57000   4.38300  1.000 34.29000 ? 107 PHE A CA  1 
ATOM   693  C C   . PHE A 1 107 ? 14.44900  5.65900   5.40300  1.000 34.29000 ? 107 PHE A C   1 
ATOM   694  O O   . PHE A 1 107 ? 14.91900  6.74400   5.04800  1.000 34.29000 ? 107 PHE A O   1 
ATOM   695  C CB  . PHE A 1 107 ? 15.49700  4.01500   3.86000  1.000 34.29000 ? 107 PHE A CB  1 
ATOM   696  C CG  . PHE A 1 107 ? 15.35900  2.77500   3.03100  1.000 34.29000 ? 107 PHE A CG  1 
ATOM   697  C CD1 . PHE A 1 107 ? 15.19700  1.53900   3.63300  1.000 34.29000 ? 107 PHE A CD1 1 
ATOM   698  C CD2 . PHE A 1 107 ? 15.41100  2.84100   1.65000  1.000 34.29000 ? 107 PHE A CD2 1 
ATOM   699  C CE1 . PHE A 1 107 ? 15.07700  0.39200   2.87300  1.000 34.29000 ? 107 PHE A CE1 1 
ATOM   700  C CE2 . PHE A 1 107 ? 15.29200  1.69900   0.88400  1.000 34.29000 ? 107 PHE A CE2 1 
ATOM   701  C CZ  . PHE A 1 107 ? 15.12400  0.47200   1.49800  1.000 34.29000 ? 107 PHE A CZ  1 
ATOM   702  N N   . ASP A 1 108 ? 14.15200  5.37200   6.66700  1.000 29.37000 ? 108 ASP A N   1 
ATOM   703  C CA  . ASP A 1 108 ? 14.78000  6.10100   7.75300  1.000 29.37000 ? 108 ASP A CA  1 
ATOM   704  C C   . ASP A 1 108 ? 16.23400  5.66300   7.86300  1.000 29.37000 ? 108 ASP A C   1 
ATOM   705  O O   . ASP A 1 108 ? 16.58500  4.52200   7.55600  1.000 29.37000 ? 108 ASP A O   1 
ATOM   706  C CB  . ASP A 1 108 ? 14.04300  5.84800   9.06600  1.000 29.37000 ? 108 ASP A CB  1 
ATOM   707  C CG  . ASP A 1 108 ? 12.59000  6.26400   9.00500  1.000 29.37000 ? 108 ASP A CG  1 
ATOM   708  O OD1 . ASP A 1 108 ? 12.31300  7.37900   8.51500  1.000 29.37000 ? 108 ASP A OD1 1 
ATOM   709  O OD2 . ASP A 1 108 ? 11.72600  5.47300   9.43700  1.000 29.37000 ? 108 ASP A OD2 1 
ATOM   710  N N   . GLY A 1 109 ? 17.08400  6.57800   8.29400  1.000 29.97000 ? 109 GLY A N   1 
ATOM   711  C CA  . GLY A 1 109 ? 18.51300  6.34200   8.26700  1.000 29.97000 ? 109 GLY A CA  1 
ATOM   712  C C   . GLY A 1 109 ? 19.20000  6.96700   9.45900  1.000 29.97000 ? 109 GLY A C   1 
ATOM   713  O O   . GLY A 1 109 ? 18.80200  8.02300   9.95800  1.000 29.97000 ? 109 GLY A O   1 
ATOM   714  N N   . ILE A 1 110 ? 20.25200  6.28900   9.90500  1.000 26.19000 ? 110 ILE A N   1 
ATOM   715  C CA  . ILE A 1 110 ? 21.08900  6.72200   11.01500 1.000 26.19000 ? 110 ILE A CA  1 
ATOM   716  C C   . ILE A 1 110 ? 22.51200  6.89500   10.50600 1.000 26.19000 ? 110 ILE A C   1 
ATOM   717  O O   . ILE A 1 110 ? 23.02400  6.04500   9.76800  1.000 26.19000 ? 110 ILE A O   1 
ATOM   718  C CB  . ILE A 1 110 ? 21.03700  5.71600   12.18200 1.000 26.19000 ? 110 ILE A CB  1 
ATOM   719  C CG1 . ILE A 1 110 ? 19.69200  5.81900   12.90200 1.000 26.19000 ? 110 ILE A CG1 1 
ATOM   720  C CG2 . ILE A 1 110 ? 22.19700  5.93000   13.14500 1.000 26.19000 ? 110 ILE A CG2 1 
ATOM   721  C CD1 . ILE A 1 110 ? 19.37200  7.21300   13.39500 1.000 26.19000 ? 110 ILE A CD1 1 
ATOM   722  N N   . ILE A 1 111 ? 23.15000  7.99300   10.90700 1.000 26.65000 ? 111 ILE A N   1 
ATOM   723  C CA  . ILE A 1 111 ? 24.48800  8.35600   10.45500 1.000 26.65000 ? 111 ILE A CA  1 
ATOM   724  C C   . ILE A 1 111 ? 25.37300  8.53800   11.67900 1.000 26.65000 ? 111 ILE A C   1 
ATOM   725  O O   . ILE A 1 111 ? 24.99900  9.25700   12.61300 1.000 26.65000 ? 111 ILE A O   1 
ATOM   726  C CB  . ILE A 1 111 ? 24.46200  9.65000   9.62000  1.000 26.65000 ? 111 ILE A CB  1 
ATOM   727  C CG1 . ILE A 1 111 ? 23.51300  9.51300   8.42900  1.000 26.65000 ? 111 ILE A CG1 1 
ATOM   728  C CG2 . ILE A 1 111 ? 25.85400  10.00500  9.15000  1.000 26.65000 ? 111 ILE A CG2 1 
ATOM   729  C CD1 . ILE A 1 111 ? 24.11100  8.77100   7.25900  1.000 26.65000 ? 111 ILE A CD1 1 
ATOM   730  N N   . HIS A 1 112 ? 26.54600  7.90200   11.67600 1.000 24.17000 ? 112 HIS A N   1 
ATOM   731  C CA  . HIS A 1 112 ? 27.49700  8.18000   12.74900 1.000 24.17000 ? 112 HIS A CA  1 
ATOM   732  C C   . HIS A 1 112 ? 28.90200  7.76200   12.34000 1.000 24.17000 ? 112 HIS A C   1 
ATOM   733  O O   . HIS A 1 112 ? 29.08000  6.74500   11.67200 1.000 24.17000 ? 112 HIS A O   1 
ATOM   734  C CB  . HIS A 1 112 ? 27.09500  7.47200   14.05000 1.000 24.17000 ? 112 HIS A CB  1 
ATOM   735  C CG  . HIS A 1 112 ? 26.96200  5.98700   13.91900 1.000 24.17000 ? 112 HIS A CG  1 
ATOM   736  N ND1 . HIS A 1 112 ? 28.00700  5.12200   14.16200 1.000 24.17000 ? 112 HIS A ND1 1 
ATOM   737  C CD2 . HIS A 1 112 ? 25.90500  5.21400   13.57600 1.000 24.17000 ? 112 HIS A CD2 1 
ATOM   738  C CE1 . HIS A 1 112 ? 27.59900  3.87900   13.97300 1.000 24.17000 ? 112 HIS A CE1 1 
ATOM   739  N NE2 . HIS A 1 112 ? 26.32700  3.90800   13.61700 1.000 24.17000 ? 112 HIS A NE2 1 
ATOM   740  N N   . ARG A 1 113 ? 29.89500  8.54400   12.75400 1.000 25.77000 ? 113 ARG A N   1 
ATOM   741  C CA  . ARG A 1 113 ? 31.27800  8.17900   12.48600 1.000 25.77000 ? 113 ARG A CA  1 
ATOM   742  C C   . ARG A 1 113 ? 31.71700  7.02800   13.38700 1.000 25.77000 ? 113 ARG A C   1 
ATOM   743  O O   . ARG A 1 113 ? 31.27800  6.90400   14.53400 1.000 25.77000 ? 113 ARG A O   1 
ATOM   744  C CB  . ARG A 1 113 ? 32.20600  9.37800   12.68900 1.000 25.77000 ? 113 ARG A CB  1 
ATOM   745  C CG  . ARG A 1 113 ? 31.81600  10.62100  11.90800 1.000 25.77000 ? 113 ARG A CG  1 
ATOM   746  C CD  . ARG A 1 113 ? 33.00200  11.56100  11.74100 1.000 25.77000 ? 113 ARG A CD  1 
ATOM   747  N NE  . ARG A 1 113 ? 32.59400  12.93500  11.47100 1.000 25.77000 ? 113 ARG A NE  1 
ATOM   748  C CZ  . ARG A 1 113 ? 32.30700  13.41400  10.26800 1.000 25.77000 ? 113 ARG A CZ  1 
ATOM   749  N NH1 . ARG A 1 113 ? 32.34400  12.64600  9.19100  1.000 25.77000 ? 113 ARG A NH1 1 
ATOM   750  N NH2 . ARG A 1 113 ? 31.96700  14.69300  10.14300 1.000 25.77000 ? 113 ARG A NH2 1 
ATOM   751  N N   . SER A 1 114 ? 32.59600  6.18200   12.85200 1.000 25.31000 ? 114 SER A N   1 
ATOM   752  C CA  . SER A 1 114 ? 33.26900  5.15100   13.64200 1.000 25.31000 ? 114 SER A CA  1 
ATOM   753  C C   . SER A 1 114 ? 34.47000  4.67300   12.84300 1.000 25.31000 ? 114 SER A C   1 
ATOM   754  O O   . SER A 1 114 ? 34.30400  4.18700   11.72000 1.000 25.31000 ? 114 SER A O   1 
ATOM   755  C CB  . SER A 1 114 ? 32.33400  3.98500   13.96600 1.000 25.31000 ? 114 SER A CB  1 
ATOM   756  O OG  . SER A 1 114 ? 32.26500  3.07000   12.88700 1.000 25.31000 ? 114 SER A OG  1 
ATOM   757  N N   . ASN A 1 115 ? 35.66700  4.80000   13.42000 1.000 26.64000 ? 115 ASN A N   1 
ATOM   758  C CA  . ASN A 1 115 ? 36.92000  4.54400   12.70600 1.000 26.64000 ? 115 ASN A CA  1 
ATOM   759  C C   . ASN A 1 115 ? 37.03400  5.40100   11.45100 1.000 26.64000 ? 115 ASN A C   1 
ATOM   760  O O   . ASN A 1 115 ? 37.58300  4.96400   10.43900 1.000 26.64000 ? 115 ASN A O   1 
ATOM   761  C CB  . ASN A 1 115 ? 37.07300  3.06200   12.33900 1.000 26.64000 ? 115 ASN A CB  1 
ATOM   762  C CG  . ASN A 1 115 ? 36.76000  2.13900   13.48800 1.000 26.64000 ? 115 ASN A CG  1 
ATOM   763  O OD1 . ASN A 1 115 ? 35.62500  1.69100   13.64300 1.000 26.64000 ? 115 ASN A OD1 1 
ATOM   764  N ND2 . ASN A 1 115 ? 37.76600  1.84600   14.30300 1.000 26.64000 ? 115 ASN A ND2 1 
ATOM   765  N N   . GLY A 1 116 ? 36.50300  6.61300   11.50100 1.000 27.75000 ? 116 GLY A N   1 
ATOM   766  C CA  . GLY A 1 116 ? 36.49900  7.47200   10.32000 1.000 27.75000 ? 116 GLY A CA  1 
ATOM   767  C C   . GLY A 1 116 ? 35.45500  7.15700   9.26700  1.000 27.75000 ? 116 GLY A C   1 
ATOM   768  O O   . GLY A 1 116 ? 34.79600  8.06700   8.75500  1.000 27.75000 ? 116 GLY A O   1 
ATOM   769  N N   . VAL A 1 117 ? 35.30000  5.88200   8.91500  1.000 24.60000 ? 117 VAL A N   1 
ATOM   770  C CA  . VAL A 1 117 ? 34.28100  5.49400   7.94600  1.000 24.60000 ? 117 VAL A CA  1 
ATOM   771  C C   . VAL A 1 117 ? 32.90700  5.75500   8.54700  1.000 24.60000 ? 117 VAL A C   1 
ATOM   772  O O   . VAL A 1 117 ? 32.55400  5.20700   9.59800  1.000 24.60000 ? 117 VAL A O   1 
ATOM   773  C CB  . VAL A 1 117 ? 34.44200  4.02500   7.53400  1.000 24.60000 ? 117 VAL A CB  1 
ATOM   774  C CG1 . VAL A 1 117 ? 35.53400  3.90200   6.49400  1.000 24.60000 ? 117 VAL A CG1 1 
ATOM   775  C CG2 . VAL A 1 117 ? 34.77800  3.16900   8.74400  1.000 24.60000 ? 117 VAL A CG2 1 
ATOM   776  N N   . VAL A 1 118 ? 32.11900  6.59000   7.87500  1.000 22.28000 ? 118 VAL A N   1 
ATOM   777  C CA  . VAL A 1 118 ? 30.79700  6.93600   8.37800  1.000 22.28000 ? 118 VAL A CA  1 
ATOM   778  C C   . VAL A 1 118 ? 29.87000  5.74800   8.16700  1.000 22.28000 ? 118 VAL A C   1 
ATOM   779  O O   . VAL A 1 118 ? 29.70100  5.26500   7.04200  1.000 22.28000 ? 118 VAL A O   1 
ATOM   780  C CB  . VAL A 1 118 ? 30.26300  8.19200   7.67900  1.000 22.28000 ? 118 VAL A CB  1 
ATOM   781  C CG1 . VAL A 1 118 ? 28.93700  8.60200   8.27300  1.000 22.28000 ? 118 VAL A CG1 1 
ATOM   782  C CG2 . VAL A 1 118 ? 31.27700  9.32500   7.77600  1.000 22.28000 ? 118 VAL A CG2 1 
ATOM   783  N N   . ILE A 1 119 ? 29.27900  5.25500   9.24800  1.000 22.77000 ? 119 ILE A N   1 
ATOM   784  C CA  . ILE A 1 119 ? 28.28000  4.20300   9.14100  1.000 22.77000 ? 119 ILE A CA  1 
ATOM   785  C C   . ILE A 1 119 ? 26.93000  4.84300   8.86200  1.000 22.77000 ? 119 ILE A C   1 
ATOM   786  O O   . ILE A 1 119 ? 26.49200  5.74800   9.59000  1.000 22.77000 ? 119 ILE A O   1 
ATOM   787  C CB  . ILE A 1 119 ? 28.23900  3.35300   10.42000 1.000 22.77000 ? 119 ILE A CB  1 
ATOM   788  C CG1 . ILE A 1 119 ? 29.57200  2.63400   10.62400 1.000 22.77000 ? 119 ILE A CG1 1 
ATOM   789  C CG2 . ILE A 1 119 ? 27.09300  2.35500   10.35700 1.000 22.77000 ? 119 ILE A CG2 1 
ATOM   790  C CD1 . ILE A 1 119 ? 29.56900  1.68500   11.79500 1.000 22.77000 ? 119 ILE A CD1 1 
ATOM   791  N N   . LEU A 1 120 ? 26.28000  4.38400   7.79600  1.000 23.37000 ? 120 LEU A N   1 
ATOM   792  C CA  . LEU A 1 120 ? 24.89600  4.70500   7.49200  1.000 23.37000 ? 120 LEU A CA  1 
ATOM   793  C C   . LEU A 1 120 ? 24.06200  3.44200   7.64300  1.000 23.37000 ? 120 LEU A C   1 
ATOM   794  O O   . LEU A 1 120 ? 24.48600  2.35400   7.24500  1.000 23.37000 ? 120 LEU A O   1 
ATOM   795  C CB  . LEU A 1 120 ? 24.76000  5.27400   6.07400  1.000 23.37000 ? 120 LEU A CB  1 
ATOM   796  C CG  . LEU A 1 120 ? 23.40700  5.19600   5.35600  1.000 23.37000 ? 120 LEU A CG  1 
ATOM   797  C CD1 . LEU A 1 120 ? 22.31500  5.96700   6.08700  1.000 23.37000 ? 120 LEU A CD1 1 
ATOM   798  C CD2 . LEU A 1 120 ? 23.54000  5.69000   3.92300  1.000 23.37000 ? 120 LEU A CD2 1 
ATOM   799  N N   . GLU A 1 121 ? 22.88300  3.58500   8.23400  1.000 25.20000 ? 121 GLU A N   1 
ATOM   800  C CA  . GLU A 1 121 ? 21.99400  2.45600   8.46200  1.000 25.20000 ? 121 GLU A CA  1 
ATOM   801  C C   . GLU A 1 121 ? 20.60700  2.81400   7.96200  1.000 25.20000 ? 121 GLU A C   1 
ATOM   802  O O   . GLU A 1 121 ? 20.09500  3.89400   8.27200  1.000 25.20000 ? 121 GLU A O   1 
ATOM   803  C CB  . GLU A 1 121 ? 21.95600  2.08200   9.94200  1.000 25.20000 ? 121 GLU A CB  1 
ATOM   804  C CG  . GLU A 1 121 ? 23.27300  1.53600   10.45500 1.000 25.20000 ? 121 GLU A CG  1 
ATOM   805  C CD  . GLU A 1 121 ? 23.53500  1.91800   11.89300 1.000 25.20000 ? 121 GLU A CD  1 
ATOM   806  O OE1 . GLU A 1 121 ? 23.76200  3.11800   12.16000 1.000 25.20000 ? 121 GLU A OE1 1 
ATOM   807  O OE2 . GLU A 1 121 ? 23.50100  1.01800   12.75500 1.000 25.20000 ? 121 GLU A OE2 1 
ATOM   808  N N   . LEU A 1 122 ? 20.00600  1.90600   7.19800  1.000 25.95000 ? 122 LEU A N   1 
ATOM   809  C CA  . LEU A 1 122 ? 18.71900  2.13700   6.55200  1.000 25.95000 ? 122 LEU A CA  1 
ATOM   810  C C   . LEU A 1 122 ? 17.70200  1.13400   7.07500  1.000 25.95000 ? 122 LEU A C   1 
ATOM   811  O O   . LEU A 1 122 ? 17.90700  -0.07900  6.96800  1.000 25.95000 ? 122 LEU A O   1 
ATOM   812  C CB  . LEU A 1 122 ? 18.84200  2.02200   5.03100  1.000 25.95000 ? 122 LEU A CB  1 
ATOM   813  C CG  . LEU A 1 122 ? 19.75000  3.03300   4.33000  1.000 25.95000 ? 122 LEU A CG  1 
ATOM   814  C CD1 . LEU A 1 122 ? 19.74600  2.79200   2.83100  1.000 25.95000 ? 122 LEU A CD1 1 
ATOM   815  C CD2 . LEU A 1 122 ? 19.31600  4.45500   4.64800  1.000 25.95000 ? 122 LEU A CD2 1 
ATOM   816  N N   . GLU A 1 123 ? 16.60400  1.64300   7.62600  1.000 28.87000 ? 123 GLU A N   1 
ATOM   817  C CA  . GLU A 1 123 ? 15.46400  0.84100   8.01800  1.000 28.87000 ? 123 GLU A CA  1 
ATOM   818  C C   . GLU A 1 123 ? 14.23300  1.36500   7.29100  1.000 28.87000 ? 123 GLU A C   1 
ATOM   819  O O   . GLU A 1 123 ? 14.00300  2.58200   7.28500  1.000 28.87000 ? 123 GLU A O   1 
ATOM   820  C CB  . GLU A 1 123 ? 15.24000  0.90000   9.53800  1.000 28.87000 ? 123 GLU A CB  1 
ATOM   821  C CG  . GLU A 1 123 ? 16.49200  0.66100   10.36700 1.000 28.87000 ? 123 GLU A CG  1 
ATOM   822  C CD  . GLU A 1 123 ? 16.22300  0.73700   11.85700 1.000 28.87000 ? 123 GLU A CD  1 
ATOM   823  O OE1 . GLU A 1 123 ? 15.04400  0.63200   12.25300 1.000 28.87000 ? 123 GLU A OE1 1 
ATOM   824  O OE2 . GLU A 1 123 ? 17.18900  0.90600   12.63100 1.000 28.87000 ? 123 GLU A OE2 1 
ATOM   825  N N   . PRO A 1 124 ? 13.42000  0.50400   6.67900  1.000 30.26000 ? 124 PRO A N   1 
ATOM   826  C CA  . PRO A 1 124 ? 12.31300  1.00800   5.85600  1.000 30.26000 ? 124 PRO A CA  1 
ATOM   827  C C   . PRO A 1 124 ? 11.33100  1.83900   6.67000  1.000 30.26000 ? 124 PRO A C   1 
ATOM   828  O O   . PRO A 1 124 ? 11.03900  1.53700   7.82800  1.000 30.26000 ? 124 PRO A O   1 
ATOM   829  C CB  . PRO A 1 124 ? 11.66300  -0.27300  5.32400  1.000 30.26000 ? 124 PRO A CB  1 
ATOM   830  C CG  . PRO A 1 124 ? 12.76900  -1.28500  5.34700  1.000 30.26000 ? 124 PRO A CG  1 
ATOM   831  C CD  . PRO A 1 124 ? 13.58500  -0.95300  6.56100  1.000 30.26000 ? 124 PRO A CD  1 
ATOM   832  N N   . ALA A 1 125 ? 10.81800  2.89300   6.04000  1.000 35.95000 ? 125 ALA A N   1 
ATOM   833  C CA  . ALA A 1 125 ? 9.95400   3.85900   6.70100  1.000 35.95000 ? 125 ALA A CA  1 
ATOM   834  C C   . ALA A 1 125 ? 8.54000   3.31300   6.87700  1.000 35.95000 ? 125 ALA A C   1 
ATOM   835  O O   . ALA A 1 125 ? 8.09100   2.42200   6.15100  1.000 35.95000 ? 125 ALA A O   1 
ATOM   836  C CB  . ALA A 1 125 ? 9.90800   5.16700   5.91300  1.000 35.95000 ? 125 ALA A CB  1 
ATOM   837  N N   . ILE A 1 126 ? 7.84100   3.85600   7.87400  1.000 42.42000 ? 126 ILE A N   1 
ATOM   838  C CA  . ILE A 1 126 ? 6.44100   3.52400   8.11200  1.000 42.42000 ? 126 ILE A CA  1 
ATOM   839  C C   . ILE A 1 126 ? 5.55400   4.66700   7.63000  1.000 42.42000 ? 126 ILE A C   1 
ATOM   840  O O   . ILE A 1 126 ? 5.28400   5.61400   8.37800  1.000 42.42000 ? 126 ILE A O   1 
ATOM   841  C CB  . ILE A 1 126 ? 6.18900   3.21500   9.59900  1.000 42.42000 ? 126 ILE A CB  1 
ATOM   842  C CG1 . ILE A 1 126 ? 7.12500   2.09900   10.06900 1.000 42.42000 ? 126 ILE A CG1 1 
ATOM   843  C CG2 . ILE A 1 126 ? 4.73500   2.82800   9.82700  1.000 42.42000 ? 126 ILE A CG2 1 
ATOM   844  C CD1 . ILE A 1 126 ? 6.89200   1.66200   11.49300 1.000 42.42000 ? 126 ILE A CD1 1 
ATOM   845  N N   . LEU A 1 127 ? 5.09700   4.57800   6.38200  1.000 48.00000 ? 127 LEU A N   1 
ATOM   846  C CA  . LEU A 1 127 ? 4.22600   5.58300   5.76500  1.000 48.00000 ? 127 LEU A CA  1 
ATOM   847  C C   . LEU A 1 127 ? 4.76200   7.00500   5.92000  1.000 48.00000 ? 127 LEU A C   1 
ATOM   848  O O   . LEU A 1 127 ? 4.18100   7.82300   6.63500  1.000 48.00000 ? 127 LEU A O   1 
ATOM   849  C CB  . LEU A 1 127 ? 2.81100   5.49800   6.34700  1.000 48.00000 ? 127 LEU A CB  1 
ATOM   850  C CG  . LEU A 1 127 ? 2.07400   4.17000   6.16200  1.000 48.00000 ? 127 LEU A CG  1 
ATOM   851  C CD1 . LEU A 1 127 ? 0.59800   4.32000   6.50300  1.000 48.00000 ? 127 LEU A CD1 1 
ATOM   852  C CD2 . LEU A 1 127 ? 2.25200   3.64100   4.74700  1.000 48.00000 ? 127 LEU A CD2 1 
ATOM   853  N N   . PHE A 1 136 ? 6.31800   14.55300  17.75700 1.000 30.54000 ? 136 PHE A N   1 
ATOM   854  C CA  . PHE A 1 136 ? 6.26800   13.43700  18.69500 1.000 30.54000 ? 136 PHE A CA  1 
ATOM   855  C C   . PHE A 1 136 ? 6.19900   13.94800  20.12800 1.000 30.54000 ? 136 PHE A C   1 
ATOM   856  O O   . PHE A 1 136 ? 5.97300   13.17800  21.06200 1.000 30.54000 ? 136 PHE A O   1 
ATOM   857  C CB  . PHE A 1 136 ? 7.48900   12.52800  18.52500 1.000 30.54000 ? 136 PHE A CB  1 
ATOM   858  C CG  . PHE A 1 136 ? 8.74100   13.06500  19.16600 1.000 30.54000 ? 136 PHE A CG  1 
ATOM   859  C CD1 . PHE A 1 136 ? 9.53100   13.99300  18.50800 1.000 30.54000 ? 136 PHE A CD1 1 
ATOM   860  C CD2 . PHE A 1 136 ? 9.13000   12.63900  20.42600 1.000 30.54000 ? 136 PHE A CD2 1 
ATOM   861  C CE1 . PHE A 1 136 ? 10.68200  14.48700  19.09700 1.000 30.54000 ? 136 PHE A CE1 1 
ATOM   862  C CE2 . PHE A 1 136 ? 10.27800  13.13100  21.01800 1.000 30.54000 ? 136 PHE A CE2 1 
ATOM   863  C CZ  . PHE A 1 136 ? 11.05400  14.05500  20.35200 1.000 30.54000 ? 136 PHE A CZ  1 
ATOM   864  N N   . TYR A 1 137 ? 6.40000   15.25900  20.28700 1.000 34.06000 ? 137 TYR A N   1 
ATOM   865  C CA  . TYR A 1 137 ? 6.48000   15.85900  21.61400 1.000 34.06000 ? 137 TYR A CA  1 
ATOM   866  C C   . TYR A 1 137 ? 5.17900   15.71400  22.39400 1.000 34.06000 ? 137 TYR A C   1 
ATOM   867  O O   . TYR A 1 137 ? 5.20800   15.73400  23.62900 1.000 34.06000 ? 137 TYR A O   1 
ATOM   868  C CB  . TYR A 1 137 ? 6.87800   17.33400  21.48700 1.000 34.06000 ? 137 TYR A CB  1 
ATOM   869  C CG  . TYR A 1 137 ? 6.89000   18.12000  22.78400 1.000 34.06000 ? 137 TYR A CG  1 
ATOM   870  C CD1 . TYR A 1 137 ? 7.56300   17.65200  23.90500 1.000 34.06000 ? 137 TYR A CD1 1 
ATOM   871  C CD2 . TYR A 1 137 ? 6.24600   19.34800  22.87400 1.000 34.06000 ? 137 TYR A CD2 1 
ATOM   872  C CE1 . TYR A 1 137 ? 7.57800   18.37700  25.08600 1.000 34.06000 ? 137 TYR A CE1 1 
ATOM   873  C CE2 . TYR A 1 137 ? 6.25600   20.08000  24.04700 1.000 34.06000 ? 137 TYR A CE2 1 
ATOM   874  C CZ  . TYR A 1 137 ? 6.92300   19.59200  25.14900 1.000 34.06000 ? 137 TYR A CZ  1 
ATOM   875  O OH  . TYR A 1 137 ? 6.93200   20.32100  26.31700 1.000 34.06000 ? 137 TYR A OH  1 
ATOM   876  N N   . HIS A 1 138 ? 4.04200   15.56900  21.70800 1.000 40.63000 ? 138 HIS A N   1 
ATOM   877  C CA  . HIS A 1 138 ? 2.78500   15.36100  22.42000 1.000 40.63000 ? 138 HIS A CA  1 
ATOM   878  C C   . HIS A 1 138 ? 2.79600   14.06300  23.21900 1.000 40.63000 ? 138 HIS A C   1 
ATOM   879  O O   . HIS A 1 138 ? 2.20100   13.99800  24.30100 1.000 40.63000 ? 138 HIS A O   1 
ATOM   880  C CB  . HIS A 1 138 ? 1.61400   15.35500  21.43700 1.000 40.63000 ? 138 HIS A CB  1 
ATOM   881  C CG  . HIS A 1 138 ? 1.43700   16.64300  20.69600 1.000 40.63000 ? 138 HIS A CG  1 
ATOM   882  N ND1 . HIS A 1 138 ? 2.02000   16.88400  19.47000 1.000 40.63000 ? 138 HIS A ND1 1 
ATOM   883  C CD2 . HIS A 1 138 ? 0.73700   17.76000  21.00500 1.000 40.63000 ? 138 HIS A CD2 1 
ATOM   884  C CE1 . HIS A 1 138 ? 1.68700   18.09400  19.05600 1.000 40.63000 ? 138 HIS A CE1 1 
ATOM   885  N NE2 . HIS A 1 138 ? 0.91000   18.64700  19.97000 1.000 40.63000 ? 138 HIS A NE2 1 
ATOM   886  N N   . LEU A 1 139 ? 3.45600   13.02200  22.70500 1.000 33.85000 ? 139 LEU A N   1 
ATOM   887  C CA  . LEU A 1 139 ? 3.50300   11.75200  23.42400 1.000 33.85000 ? 139 LEU A CA  1 
ATOM   888  C C   . LEU A 1 139 ? 4.30900   11.86700  24.71100 1.000 33.85000 ? 139 LEU A C   1 
ATOM   889  O O   . LEU A 1 139 ? 3.95500   11.26200  25.72900 1.000 33.85000 ? 139 LEU A O   1 
ATOM   890  C CB  . LEU A 1 139 ? 4.09200   10.66200  22.52800 1.000 33.85000 ? 139 LEU A CB  1 
ATOM   891  C CG  . LEU A 1 139 ? 3.44500   10.45800  21.15700 1.000 33.85000 ? 139 LEU A CG  1 
ATOM   892  C CD1 . LEU A 1 139 ? 4.15500   9.35300   20.38700 1.000 33.85000 ? 139 LEU A CD1 1 
ATOM   893  C CD2 . LEU A 1 139 ? 1.96400   10.15100  21.30100 1.000 33.85000 ? 139 LEU A CD2 1 
ATOM   894  N N   . VAL A 1 140 ? 5.38900   12.64400  24.69100 1.000 30.83000 ? 140 VAL A N   1 
ATOM   895  C CA  . VAL A 1 140 ? 6.25400   12.72400  25.86000 1.000 30.83000 ? 140 VAL A CA  1 
ATOM   896  C C   . VAL A 1 140 ? 5.81300   13.81500  26.82900 1.000 30.83000 ? 140 VAL A C   1 
ATOM   897  O O   . VAL A 1 140 ? 5.95900   13.64800  28.04300 1.000 30.83000 ? 140 VAL A O   1 
ATOM   898  C CB  . VAL A 1 140 ? 7.72000   12.92600  25.43600 1.000 30.83000 ? 140 VAL A CB  1 
ATOM   899  C CG1 . VAL A 1 140 ? 8.19500   11.74800  24.61000 1.000 30.83000 ? 140 VAL A CG1 1 
ATOM   900  C CG2 . VAL A 1 140 ? 7.89200   14.22200  24.65800 1.000 30.83000 ? 140 VAL A CG2 1 
ATOM   901  N N   . LYS A 1 141 ? 5.23100   14.90800  26.32300 1.000 31.88000 ? 141 LYS A N   1 
ATOM   902  C CA  . LYS A 1 141 ? 4.98000   16.07500  27.16300 1.000 31.88000 ? 141 LYS A CA  1 
ATOM   903  C C   . LYS A 1 141 ? 4.07900   15.73600  28.33800 1.000 31.88000 ? 141 LYS A C   1 
ATOM   904  O O   . LYS A 1 141 ? 4.19600   16.34400  29.40900 1.000 31.88000 ? 141 LYS A O   1 
ATOM   905  C CB  . LYS A 1 141 ? 4.36400   17.19600  26.32700 1.000 31.88000 ? 141 LYS A CB  1 
ATOM   906  C CG  . LYS A 1 141 ? 4.19400   18.51200  27.06500 1.000 31.88000 ? 141 LYS A CG  1 
ATOM   907  C CD  . LYS A 1 141 ? 3.48000   19.53400  26.19900 1.000 31.88000 ? 141 LYS A CD  1 
ATOM   908  C CE  . LYS A 1 141 ? 3.38900   20.87900  26.89700 1.000 31.88000 ? 141 LYS A CE  1 
ATOM   909  N NZ  . LYS A 1 141 ? 4.73000   21.49100  27.11500 1.000 31.88000 ? 141 LYS A NZ  1 
ATOM   910  N N   . LEU A 1 142 ? 3.18300   14.76500  28.16300 1.000 28.78000 ? 142 LEU A N   1 
ATOM   911  C CA  . LEU A 1 142 ? 2.44200   14.22800  29.29600 1.000 28.78000 ? 142 LEU A CA  1 
ATOM   912  C C   . LEU A 1 142 ? 3.39200   13.58100  30.29500 1.000 28.78000 ? 142 LEU A C   1 
ATOM   913  O O   . LEU A 1 142 ? 3.33900   13.86100  31.50000 1.000 28.78000 ? 142 LEU A O   1 
ATOM   914  C CB  . LEU A 1 142 ? 1.40800   13.22000  28.78500 1.000 28.78000 ? 142 LEU A CB  1 
ATOM   915  C CG  . LEU A 1 142 ? 0.36400   12.52500  29.66000 1.000 28.78000 ? 142 LEU A CG  1 
ATOM   916  C CD1 . LEU A 1 142 ? -0.62800  11.85000  28.74100 1.000 28.78000 ? 142 LEU A CD1 1 
ATOM   917  C CD2 . LEU A 1 142 ? 0.96800   11.49000  30.59300 1.000 28.78000 ? 142 LEU A CD2 1 
ATOM   918  N N   . ALA A 1 143 ? 4.27800   12.71300  29.80300 1.000 27.53000 ? 143 ALA A N   1 
ATOM   919  C CA  . ALA A 1 143 ? 5.19600   12.00500  30.68500 1.000 27.53000 ? 143 ALA A CA  1 
ATOM   920  C C   . ALA A 1 143 ? 6.20200   12.94200  31.33900 1.000 27.53000 ? 143 ALA A C   1 
ATOM   921  O O   . ALA A 1 143 ? 6.61700   12.69300  32.47400 1.000 27.53000 ? 143 ALA A O   1 
ATOM   922  C CB  . ALA A 1 143 ? 5.91900   10.90300  29.91200 1.000 27.53000 ? 143 ALA A CB  1 
ATOM   923  N N   . ILE A 1 144 ? 6.59100   14.02900  30.66700 1.000 25.91000 ? 144 ILE A N   1 
ATOM   924  C CA  . ILE A 1 144 ? 7.59500   14.92000  31.24600 1.000 25.91000 ? 144 ILE A CA  1 
ATOM   925  C C   . ILE A 1 144 ? 7.05000   15.57300  32.50900 1.000 25.91000 ? 144 ILE A C   1 
ATOM   926  O O   . ILE A 1 144 ? 7.68800   15.55700  33.57000 1.000 25.91000 ? 144 ILE A O   1 
ATOM   927  C CB  . ILE A 1 144 ? 8.04600   15.98300  30.22700 1.000 25.91000 ? 144 ILE A CB  1 
ATOM   928  C CG1 . ILE A 1 144 ? 8.25700   15.38200  28.83500 1.000 25.91000 ? 144 ILE A CG1 1 
ATOM   929  C CG2 . ILE A 1 144 ? 9.32000   16.66100  30.70900 1.000 25.91000 ? 144 ILE A CG2 1 
ATOM   930  C CD1 . ILE A 1 144 ? 9.21400   14.21900  28.78500 1.000 25.91000 ? 144 ILE A CD1 1 
ATOM   931  N N   . GLY A 1 145 ? 5.84100   16.13000  32.42200 1.000 25.13000 ? 145 GLY A N   1 
ATOM   932  C CA  . GLY A 1 145 ? 5.23900   16.74300  33.59000 1.000 25.13000 ? 145 GLY A CA  1 
ATOM   933  C C   . GLY A 1 145 ? 4.76600   15.72800  34.60700 1.000 25.13000 ? 145 GLY A C   1 
ATOM   934  O O   . GLY A 1 145 ? 4.74100   16.01600  35.80800 1.000 25.13000 ? 145 GLY A O   1 
ATOM   935  N N   . LYS A 1 146 ? 4.38800   14.53100  34.15200 1.000 24.29000 ? 146 LYS A N   1 
ATOM   936  C CA  . LYS A 1 146 ? 4.05600   13.47500  35.09900 1.000 24.29000 ? 146 LYS A CA  1 
ATOM   937  C C   . LYS A 1 146 ? 5.27300   13.05400  35.91400 1.000 24.29000 ? 146 LYS A C   1 
ATOM   938  O O   . LYS A 1 146 ? 5.13600   12.71200  37.09400 1.000 24.29000 ? 146 LYS A O   1 
ATOM   939  C CB  . LYS A 1 146 ? 3.45300   12.28400  34.35200 1.000 24.29000 ? 146 LYS A CB  1 
ATOM   940  C CG  . LYS A 1 146 ? 2.70900   11.30200  35.23600 1.000 24.29000 ? 146 LYS A CG  1 
ATOM   941  C CD  . LYS A 1 146 ? 1.93600   10.28300  34.41200 1.000 24.29000 ? 146 LYS A CD  1 
ATOM   942  C CE  . LYS A 1 146 ? 0.55200   10.79700  34.04900 1.000 24.29000 ? 146 LYS A CE  1 
ATOM   943  N NZ  . LYS A 1 146 ? -0.21900  9.81000   33.23800 1.000 24.29000 ? 146 LYS A NZ  1 
ATOM   944  N N   . LEU A 1 147 ? 6.46300   13.08000  35.31000 1.000 23.23000 ? 147 LEU A N   1 
ATOM   945  C CA  . LEU A 1 147 ? 7.68800   12.84000  36.06300 1.000 23.23000 ? 147 LEU A CA  1 
ATOM   946  C C   . LEU A 1 147 ? 8.06800   14.03700  36.92200 1.000 23.23000 ? 147 LEU A C   1 
ATOM   947  O O   . LEU A 1 147 ? 8.67400   13.86500  37.98400 1.000 23.23000 ? 147 LEU A O   1 
ATOM   948  C CB  . LEU A 1 147 ? 8.83500   12.48900  35.11400 1.000 23.23000 ? 147 LEU A CB  1 
ATOM   949  C CG  . LEU A 1 147 ? 8.71500   11.17600  34.33600 1.000 23.23000 ? 147 LEU A CG  1 
ATOM   950  C CD1 . LEU A 1 147 ? 9.93100   10.95700  33.44800 1.000 23.23000 ? 147 LEU A CD1 1 
ATOM   951  C CD2 . LEU A 1 147 ? 8.51400   9.99900   35.27900 1.000 23.23000 ? 147 LEU A CD2 1 
ATOM   952  N N   . GLN A 1 148 ? 7.72800   15.25300  36.48400 1.000 24.24000 ? 148 GLN A N   1 
ATOM   953  C CA  . GLN A 1 148 ? 8.07600   16.43400  37.26700 1.000 24.24000 ? 148 GLN A CA  1 
ATOM   954  C C   . GLN A 1 148 ? 7.31800   16.48800  38.59000 1.000 24.24000 ? 148 GLN A C   1 
ATOM   955  O O   . GLN A 1 148 ? 7.80300   17.09000  39.55500 1.000 24.24000 ? 148 GLN A O   1 
ATOM   956  C CB  . GLN A 1 148 ? 7.82000   17.70200  36.45200 1.000 24.24000 ? 148 GLN A CB  1 
ATOM   957  C CG  . GLN A 1 148 ? 8.83100   17.93600  35.34200 1.000 24.24000 ? 148 GLN A CG  1 
ATOM   958  C CD  . GLN A 1 148 ? 8.70200   19.31000  34.71500 1.000 24.24000 ? 148 GLN A CD  1 
ATOM   959  O OE1 . GLN A 1 148 ? 8.05500   20.20000  35.26800 1.000 24.24000 ? 148 GLN A OE1 1 
ATOM   960  N NE2 . GLN A 1 148 ? 9.31900   19.49000  33.55300 1.000 24.24000 ? 148 GLN A NE2 1 
ATOM   961  N N   . SER A 1 149 ? 6.14200   15.86800  38.65800 1.000 23.27000 ? 149 SER A N   1 
ATOM   962  C CA  . SER A 1 149 ? 5.33000   15.87000  39.87100 1.000 23.27000 ? 149 SER A CA  1 
ATOM   963  C C   . SER A 1 149 ? 5.71800   14.77400  40.85800 1.000 23.27000 ? 149 SER A C   1 
ATOM   964  O O   . SER A 1 149 ? 5.14900   14.72300  41.95400 1.000 23.27000 ? 149 SER A O   1 
ATOM   965  C CB  . SER A 1 149 ? 3.84800   15.73900  39.50700 1.000 23.27000 ? 149 SER A CB  1 
ATOM   966  O OG  . SER A 1 149 ? 3.63500   14.68000  38.58900 1.000 23.27000 ? 149 SER A OG  1 
ATOM   967  N N   . THR A 1 150 ? 6.66000   13.90300  40.50100 1.000 22.74000 ? 150 THR A N   1 
ATOM   968  C CA  . THR A 1 150 ? 7.04200   12.78300  41.34900 1.000 22.74000 ? 150 THR A CA  1 
ATOM   969  C C   . THR A 1 150 ? 7.80800   13.25400  42.58400 1.000 22.74000 ? 150 THR A C   1 
ATOM   970  O O   . THR A 1 150 ? 8.42500   14.32200  42.60300 1.000 22.74000 ? 150 THR A O   1 
ATOM   971  C CB  . THR A 1 150 ? 7.90200   11.78900  40.57200 1.000 22.74000 ? 150 THR A CB  1 
ATOM   972  O OG1 . THR A 1 150 ? 9.12400   12.42300  40.17500 1.000 22.74000 ? 150 THR A OG1 1 
ATOM   973  C CG2 . THR A 1 150 ? 7.16200   11.30200  39.34000 1.000 22.74000 ? 150 THR A CG2 1 
ATOM   974  N N   . LYS A 1 151 ? 7.74500   12.43600  43.63500 1.000 23.86000 ? 151 LYS A N   1 
ATOM   975  C CA  . LYS A 1 151 ? 8.47000   12.67100  44.87900 1.000 23.86000 ? 151 LYS A CA  1 
ATOM   976  C C   . LYS A 1 151 ? 9.57600   11.65900  45.13700 1.000 23.86000 ? 151 LYS A C   1 
ATOM   977  O O   . LYS A 1 151 ? 10.67400  12.04500  45.54700 1.000 23.86000 ? 151 LYS A O   1 
ATOM   978  C CB  . LYS A 1 151 ? 7.49900   12.65700  46.06600 1.000 23.86000 ? 151 LYS A CB  1 
ATOM   979  C CG  . LYS A 1 151 ? 6.21400   13.44300  45.84300 1.000 23.86000 ? 151 LYS A CG  1 
ATOM   980  C CD  . LYS A 1 151 ? 6.47200   14.93800  45.72800 1.000 23.86000 ? 151 LYS A CD  1 
ATOM   981  C CE  . LYS A 1 151 ? 5.16900   15.70600  45.54800 1.000 23.86000 ? 151 LYS A CE  1 
ATOM   982  N NZ  . LYS A 1 151 ? 5.38300   17.17900  45.47600 1.000 23.86000 ? 151 LYS A NZ  1 
ATOM   983  N N   . THR A 1 152 ? 9.31800   10.37200  44.91200 1.000 21.94000 ? 152 THR A N   1 
ATOM   984  C CA  . THR A 1 152 ? 10.27100  9.30900   45.19100 1.000 21.94000 ? 152 THR A CA  1 
ATOM   985  C C   . THR A 1 152 ? 10.66100  8.59300   43.90300 1.000 21.94000 ? 152 THR A C   1 
ATOM   986  O O   . THR A 1 152 ? 9.96800   8.67400   42.88500 1.000 21.94000 ? 152 THR A O   1 
ATOM   987  C CB  . THR A 1 152 ? 9.70200   8.29500   46.19300 1.000 21.94000 ? 152 THR A CB  1 
ATOM   988  O OG1 . THR A 1 152 ? 8.55300   7.65500   45.62600 1.000 21.94000 ? 152 THR A OG1 1 
ATOM   989  C CG2 . THR A 1 152 ? 9.30200   8.99300   47.48300 1.000 21.94000 ? 152 THR A CG2 1 
ATOM   990  N N   . VAL A 1 153 ? 11.79600  7.88900   43.96200 1.000 18.40000 ? 153 VAL A N   1 
ATOM   991  C CA  . VAL A 1 153 ? 12.30800  7.19200   42.78500 1.000 18.40000 ? 153 VAL A CA  1 
ATOM   992  C C   . VAL A 1 153 ? 11.34300  6.10800   42.32100 1.000 18.40000 ? 153 VAL A C   1 
ATOM   993  O O   . VAL A 1 153 ? 11.20600  5.86300   41.11600 1.000 18.40000 ? 153 VAL A O   1 
ATOM   994  C CB  . VAL A 1 153 ? 13.70800  6.61500   43.08400 1.000 18.40000 ? 153 VAL A CB  1 
ATOM   995  C CG1 . VAL A 1 153 ? 14.24000  5.83300   41.89100 1.000 18.40000 ? 153 VAL A CG1 1 
ATOM   996  C CG2 . VAL A 1 153 ? 14.67200  7.73000   43.46700 1.000 18.40000 ? 153 VAL A CG2 1 
ATOM   997  N N   . THR A 1 154 ? 10.65600  5.44400   43.25500 1.000 17.87000 ? 154 THR A N   1 
ATOM   998  C CA  . THR A 1 154 ? 9.71500   4.39800   42.86300 1.000 17.87000 ? 154 THR A CA  1 
ATOM   999  C C   . THR A 1 154 ? 8.52700   4.96800   42.09600 1.000 17.87000 ? 154 THR A C   1 
ATOM   1000 O O   . THR A 1 154 ? 7.99200   4.30400   41.19600 1.000 17.87000 ? 154 THR A O   1 
ATOM   1001 C CB  . THR A 1 154 ? 9.24000   3.62900   44.09600 1.000 17.87000 ? 154 THR A CB  1 
ATOM   1002 O OG1 . THR A 1 154 ? 10.37600  3.14900   44.82600 1.000 17.87000 ? 154 THR A OG1 1 
ATOM   1003 C CG2 . THR A 1 154 ? 8.37700   2.44400   43.69000 1.000 17.87000 ? 154 THR A CG2 1 
ATOM   1004 N N   . GLU A 1 155 ? 8.10700   6.19200   42.42800 1.000 20.53000 ? 155 GLU A N   1 
ATOM   1005 C CA  . GLU A 1 155 ? 7.07500   6.85000   41.63500 1.000 20.53000 ? 155 GLU A CA  1 
ATOM   1006 C C   . GLU A 1 155 ? 7.55600   7.08900   40.21300 1.000 20.53000 ? 155 GLU A C   1 
ATOM   1007 O O   . GLU A 1 155 ? 6.81200   6.86300   39.25000 1.000 20.53000 ? 155 GLU A O   1 
ATOM   1008 C CB  . GLU A 1 155 ? 6.67100   8.17300   42.28400 1.000 20.53000 ? 155 GLU A CB  1 
ATOM   1009 C CG  . GLU A 1 155 ? 5.99500   8.03800   43.63400 1.000 20.53000 ? 155 GLU A CG  1 
ATOM   1010 C CD  . GLU A 1 155 ? 5.54800   9.37700   44.18800 1.000 20.53000 ? 155 GLU A CD  1 
ATOM   1011 O OE1 . GLU A 1 155 ? 6.04600   10.41700  43.70600 1.000 20.53000 ? 155 GLU A OE1 1 
ATOM   1012 O OE2 . GLU A 1 155 ? 4.69500   9.39000   45.09900 1.000 20.53000 ? 155 GLU A OE2 1 
ATOM   1013 N N   . ILE A 1 156 ? 8.81500   7.51100   40.06300 1.000 18.15000 ? 156 ILE A N   1 
ATOM   1014 C CA  . ILE A 1 156 ? 9.37600   7.70000   38.73100 1.000 18.15000 ? 156 ILE A CA  1 
ATOM   1015 C C   . ILE A 1 156 ? 9.40400   6.37700   37.98700 1.000 18.15000 ? 156 ILE A C   1 
ATOM   1016 O O   . ILE A 1 156 ? 9.09300   6.31300   36.79300 1.000 18.15000 ? 156 ILE A O   1 
ATOM   1017 C CB  . ILE A 1 156 ? 10.78500  8.31400   38.82700 1.000 18.15000 ? 156 ILE A CB  1 
ATOM   1018 C CG1 . ILE A 1 156 ? 10.76400  9.58900   39.66700 1.000 18.15000 ? 156 ILE A CG1 1 
ATOM   1019 C CG2 . ILE A 1 156 ? 11.34700  8.58700   37.44100 1.000 18.15000 ? 156 ILE A CG2 1 
ATOM   1020 C CD1 . ILE A 1 156 ? 12.14000  10.15600  39.92800 1.000 18.15000 ? 156 ILE A CD1 1 
ATOM   1021 N N   . SER A 1 157 ? 9.70800   5.29200   38.70100 1.000 16.84000 ? 157 SER A N   1 
ATOM   1022 C CA  . SER A 1 157 ? 9.82400   3.98500   38.06500 1.000 16.84000 ? 157 SER A CA  1 
ATOM   1023 C C   . SER A 1 157 ? 8.47500   3.50200   37.55300 1.000 16.84000 ? 157 SER A C   1 
ATOM   1024 O O   . SER A 1 157 ? 8.34800   3.08800   36.39200 1.000 16.84000 ? 157 SER A O   1 
ATOM   1025 C CB  . SER A 1 157 ? 10.41500  2.97900   39.05200 1.000 16.84000 ? 157 SER A CB  1 
ATOM   1026 O OG  . SER A 1 157 ? 11.52400  3.53000   39.73800 1.000 16.84000 ? 157 SER A OG  1 
ATOM   1027 N N   . GLN A 1 158 ? 7.44800   3.56500   38.40400 1.000 18.36000 ? 158 GLN A N   1 
ATOM   1028 C CA  . GLN A 1 158 ? 6.12700   3.11600   37.98000 1.000 18.36000 ? 158 GLN A CA  1 
ATOM   1029 C C   . GLN A 1 158 ? 5.56800   4.00600   36.87500 1.000 18.36000 ? 158 GLN A C   1 
ATOM   1030 O O   . GLN A 1 158 ? 5.01700   3.50500   35.88100 1.000 18.36000 ? 158 GLN A O   1 
ATOM   1031 C CB  . GLN A 1 158 ? 5.17600   3.07700   39.17500 1.000 18.36000 ? 158 GLN A CB  1 
ATOM   1032 C CG  . GLN A 1 158 ? 3.74600   2.71300   38.81000 1.000 18.36000 ? 158 GLN A CG  1 
ATOM   1033 C CD  . GLN A 1 158 ? 3.65800   1.42500   38.01500 1.000 18.36000 ? 158 GLN A CD  1 
ATOM   1034 O OE1 . GLN A 1 158 ? 3.12200   1.40200   36.90700 1.000 18.36000 ? 158 GLN A OE1 1 
ATOM   1035 N NE2 . GLN A 1 158 ? 4.18200   0.34300   38.57900 1.000 18.36000 ? 158 GLN A NE2 1 
ATOM   1036 N N   . ILE A 1 159 ? 5.72800   5.32500   37.00800 1.000 18.65000 ? 159 ILE A N   1 
ATOM   1037 C CA  . ILE A 1 159 ? 5.19200   6.22300   35.99400 1.000 18.65000 ? 159 ILE A CA  1 
ATOM   1038 C C   . ILE A 1 159 ? 5.89100   6.00600   34.65900 1.000 18.65000 ? 159 ILE A C   1 
ATOM   1039 O O   . ILE A 1 159 ? 5.24500   5.99300   33.60400 1.000 18.65000 ? 159 ILE A O   1 
ATOM   1040 C CB  . ILE A 1 159 ? 5.30400   7.68300   36.47100 1.000 18.65000 ? 159 ILE A CB  1 
ATOM   1041 C CG1 . ILE A 1 159 ? 4.29900   7.94800   37.59400 1.000 18.65000 ? 159 ILE A CG1 1 
ATOM   1042 C CG2 . ILE A 1 159 ? 5.09700   8.64200   35.31200 1.000 18.65000 ? 159 ILE A CG2 1 
ATOM   1043 C CD1 . ILE A 1 159 ? 4.27300   9.38000   38.07200 1.000 18.65000 ? 159 ILE A CD1 1 
ATOM   1044 N N   . ILE A 1 160 ? 7.20700   5.77300   34.67700 1.000 17.74000 ? 160 ILE A N   1 
ATOM   1045 C CA  . ILE A 1 160 ? 7.91600   5.64600   33.41200 1.000 17.74000 ? 160 ILE A CA  1 
ATOM   1046 C C   . ILE A 1 160 ? 7.62900   4.30000   32.76500 1.000 17.74000 ? 160 ILE A C   1 
ATOM   1047 O O   . ILE A 1 160 ? 7.53000   4.21100   31.53900 1.000 17.74000 ? 160 ILE A O   1 
ATOM   1048 C CB  . ILE A 1 160 ? 9.42700   5.88600   33.58900 1.000 17.74000 ? 160 ILE A CB  1 
ATOM   1049 C CG1 . ILE A 1 160 ? 10.08100  6.08100   32.22100 1.000 17.74000 ? 160 ILE A CG1 1 
ATOM   1050 C CG2 . ILE A 1 160 ? 10.09200  4.72500   34.28600 1.000 17.74000 ? 160 ILE A CG2 1 
ATOM   1051 C CD1 . ILE A 1 160 ? 9.44700   7.17800   31.39400 1.000 17.74000 ? 160 ILE A CD1 1 
ATOM   1052 N N   . VAL A 1 161 ? 7.47400   3.23000   33.55600 1.000 18.45000 ? 161 VAL A N   1 
ATOM   1053 C CA  . VAL A 1 161 ? 7.14700   1.95700   32.91900 1.000 18.45000 ? 161 VAL A CA  1 
ATOM   1054 C C   . VAL A 1 161 ? 5.75000   2.01300   32.31500 1.000 18.45000 ? 161 VAL A C   1 
ATOM   1055 O O   . VAL A 1 161 ? 5.53000   1.53800   31.19200 1.000 18.45000 ? 161 VAL A O   1 
ATOM   1056 C CB  . VAL A 1 161 ? 7.31000   0.77200   33.89100 1.000 18.45000 ? 161 VAL A CB  1 
ATOM   1057 C CG1 . VAL A 1 161 ? 8.75700   0.64600   34.32700 1.000 18.45000 ? 161 VAL A CG1 1 
ATOM   1058 C CG2 . VAL A 1 161 ? 6.38900   0.89400   35.08900 1.000 18.45000 ? 161 VAL A CG2 1 
ATOM   1059 N N   . THR A 1 162 ? 4.80200   2.66000   33.00500 1.000 19.47000 ? 162 THR A N   1 
ATOM   1060 C CA  . THR A 1 162 ? 3.46000   2.76300   32.43800 1.000 19.47000 ? 162 THR A CA  1 
ATOM   1061 C C   . THR A 1 162 ? 3.45500   3.62600   31.18200 1.000 19.47000 ? 162 THR A C   1 
ATOM   1062 O O   . THR A 1 162 ? 2.80800   3.27900   30.18600 1.000 19.47000 ? 162 THR A O   1 
ATOM   1063 C CB  . THR A 1 162 ? 2.48800   3.32400   33.47600 1.000 19.47000 ? 162 THR A CB  1 
ATOM   1064 O OG1 . THR A 1 162 ? 2.55000   2.53300   34.66800 1.000 19.47000 ? 162 THR A OG1 1 
ATOM   1065 C CG2 . THR A 1 162 ? 1.06500   3.30000   32.93600 1.000 19.47000 ? 162 THR A CG2 1 
ATOM   1066 N N   . GLU A 1 163 ? 4.20500   4.73100   31.19100 1.000 22.97000 ? 163 GLU A N   1 
ATOM   1067 C CA  . GLU A 1 163 ? 4.20900   5.61600   30.03200 1.000 22.97000 ? 163 GLU A CA  1 
ATOM   1068 C C   . GLU A 1 163 ? 4.93900   4.99300   28.85000 1.000 22.97000 ? 163 GLU A C   1 
ATOM   1069 O O   . GLU A 1 163 ? 4.50400   5.14000   27.70200 1.000 22.97000 ? 163 GLU A O   1 
ATOM   1070 C CB  . GLU A 1 163 ? 4.82900   6.96200   30.40500 1.000 22.97000 ? 163 GLU A CB  1 
ATOM   1071 C CG  . GLU A 1 163 ? 3.86900   7.88200   31.13400 1.000 22.97000 ? 163 GLU A CG  1 
ATOM   1072 C CD  . GLU A 1 163 ? 2.67500   8.25800   30.27800 1.000 22.97000 ? 163 GLU A CD  1 
ATOM   1073 O OE1 . GLU A 1 163 ? 2.88600   8.74400   29.14600 1.000 22.97000 ? 163 GLU A OE1 1 
ATOM   1074 O OE2 . GLU A 1 163 ? 1.52900   8.05700   30.73100 1.000 22.97000 ? 163 GLU A OE2 1 
ATOM   1075 N N   . VAL A 1 164 ? 6.05100   4.30000   29.10100 1.000 20.19000 ? 164 VAL A N   1 
ATOM   1076 C CA  . VAL A 1 164 ? 6.76300   3.64100   28.01300 1.000 20.19000 ? 164 VAL A CA  1 
ATOM   1077 C C   . VAL A 1 164 ? 5.92300   2.51300   27.43600 1.000 20.19000 ? 164 VAL A C   1 
ATOM   1078 O O   . VAL A 1 164 ? 5.94400   2.26500   26.22500 1.000 20.19000 ? 164 VAL A O   1 
ATOM   1079 C CB  . VAL A 1 164 ? 8.13700   3.14200   28.49700 1.000 20.19000 ? 164 VAL A CB  1 
ATOM   1080 C CG1 . VAL A 1 164 ? 8.78300   2.24500   27.44800 1.000 20.19000 ? 164 VAL A CG1 1 
ATOM   1081 C CG2 . VAL A 1 164 ? 9.04400   4.31600   28.80000 1.000 20.19000 ? 164 VAL A CG2 1 
ATOM   1082 N N   . ARG A 1 165 ? 5.14800   1.82400   28.28100 1.000 23.13000 ? 165 ARG A N   1 
ATOM   1083 C CA  . ARG A 1 165 ? 4.26100   0.79700   27.75100 1.000 23.13000 ? 165 ARG A CA  1 
ATOM   1084 C C   . ARG A 1 165 ? 3.13400   1.40900   26.92500 1.000 23.13000 ? 165 ARG A C   1 
ATOM   1085 O O   . ARG A 1 165 ? 2.75400   0.86100   25.88400 1.000 23.13000 ? 165 ARG A O   1 
ATOM   1086 C CB  . ARG A 1 165 ? 3.69900   -0.05500  28.89000 1.000 23.13000 ? 165 ARG A CB  1 
ATOM   1087 C CG  . ARG A 1 165 ? 2.70700   -1.10000  28.41800 1.000 23.13000 ? 165 ARG A CG  1 
ATOM   1088 C CD  . ARG A 1 165 ? 2.98300   -2.46500  29.02100 1.000 23.13000 ? 165 ARG A CD  1 
ATOM   1089 N NE  . ARG A 1 165 ? 2.19900   -3.50500  28.36500 1.000 23.13000 ? 165 ARG A NE  1 
ATOM   1090 C CZ  . ARG A 1 165 ? 0.97200   -3.85700  28.72200 1.000 23.13000 ? 165 ARG A CZ  1 
ATOM   1091 N NH1 . ARG A 1 165 ? 0.35200   -3.27300  29.73400 1.000 23.13000 ? 165 ARG A NH1 1 
ATOM   1092 N NH2 . ARG A 1 165 ? 0.35000   -4.82000  28.04600 1.000 23.13000 ? 165 ARG A NH2 1 
ATOM   1093 N N   . ARG A 1 166 ? 2.59100   2.54700   27.36600 1.000 26.14000 ? 166 ARG A N   1 
ATOM   1094 C CA  . ARG A 1 166 ? 1.51400   3.17900   26.61000 1.000 26.14000 ? 166 ARG A CA  1 
ATOM   1095 C C   . ARG A 1 166 ? 2.01500   3.74200   25.28400 1.000 26.14000 ? 166 ARG A C   1 
ATOM   1096 O O   . ARG A 1 166 ? 1.29500   3.71500   24.28000 1.000 26.14000 ? 166 ARG A O   1 
ATOM   1097 C CB  . ARG A 1 166 ? 0.85900   4.27600   27.44500 1.000 26.14000 ? 166 ARG A CB  1 
ATOM   1098 C CG  . ARG A 1 166 ? -0.51200  4.69800   26.94700 1.000 26.14000 ? 166 ARG A CG  1 
ATOM   1099 C CD  . ARG A 1 166 ? -0.95200  5.97400   27.63200 1.000 26.14000 ? 166 ARG A CD  1 
ATOM   1100 N NE  . ARG A 1 166 ? -0.09600  7.09300   27.25800 1.000 26.14000 ? 166 ARG A NE  1 
ATOM   1101 C CZ  . ARG A 1 166 ? -0.03900  8.24500   27.91100 1.000 26.14000 ? 166 ARG A CZ  1 
ATOM   1102 N NH1 . ARG A 1 166 ? -0.76000  8.45800   29.00000 1.000 26.14000 ? 166 ARG A NH1 1 
ATOM   1103 N NH2 . ARG A 1 166 ? 0.76500   9.20400   27.46300 1.000 26.14000 ? 166 ARG A NH2 1 
ATOM   1104 N N   . ILE A 1 167 ? 3.24900   4.24800   25.25800 1.000 23.16000 ? 167 ILE A N   1 
ATOM   1105 C CA  . ILE A 1 167 ? 3.80400   4.79600   24.02600 1.000 23.16000 ? 167 ILE A CA  1 
ATOM   1106 C C   . ILE A 1 167 ? 4.21100   3.68000   23.07400 1.000 23.16000 ? 167 ILE A C   1 
ATOM   1107 O O   . ILE A 1 167 ? 3.95600   3.75200   21.86800 1.000 23.16000 ? 167 ILE A O   1 
ATOM   1108 C CB  . ILE A 1 167 ? 4.99000   5.72500   24.34900 1.000 23.16000 ? 167 ILE A CB  1 
ATOM   1109 C CG1 . ILE A 1 167 ? 4.48900   7.05800   24.91100 1.000 23.16000 ? 167 ILE A CG1 1 
ATOM   1110 C CG2 . ILE A 1 167 ? 5.86300   5.94300   23.11900 1.000 23.16000 ? 167 ILE A CG2 1 
ATOM   1111 C CD1 . ILE A 1 167 ? 5.59000   8.06700   25.17600 1.000 23.16000 ? 167 ILE A CD1 1 
ATOM   1112 N N   . THR A 1 168 ? 4.83700   2.62800   23.59600 1.000 21.93000 ? 168 THR A N   1 
ATOM   1113 C CA  . THR A 1 168 ? 5.35400   1.57100   22.73900 1.000 21.93000 ? 168 THR A CA  1 
ATOM   1114 C C   . THR A 1 168 ? 4.30100   0.51400   22.44000 1.000 21.93000 ? 168 THR A C   1 
ATOM   1115 O O   . THR A 1 168 ? 4.18200   0.06100   21.29600 1.000 21.93000 ? 168 THR A O   1 
ATOM   1116 C CB  . THR A 1 168 ? 6.57000   0.92200   23.39400 1.000 21.93000 ? 168 THR A CB  1 
ATOM   1117 O OG1 . THR A 1 168 ? 6.22900   0.52100   24.72600 1.000 21.93000 ? 168 THR A OG1 1 
ATOM   1118 C CG2 . THR A 1 168 ? 7.72900   1.88700   23.43900 1.000 21.93000 ? 168 THR A CG2 1 
ATOM   1119 N N   . GLY A 1 169 ? 3.51900   0.12500   23.44200 1.000 22.84000 ? 169 GLY A N   1 
ATOM   1120 C CA  . GLY A 1 169 ? 2.64000   -1.01400  23.29400 1.000 22.84000 ? 169 GLY A CA  1 
ATOM   1121 C C   . GLY A 1 169 ? 3.28700   -2.36200  23.52200 1.000 22.84000 ? 169 GLY A C   1 
ATOM   1122 O O   . GLY A 1 169 ? 2.68700   -3.38400  23.17100 1.000 22.84000 ? 169 GLY A O   1 
ATOM   1123 N N   . PHE A 1 170 ? 4.49300   -2.40100  24.08900 1.000 23.05000 ? 170 PHE A N   1 
ATOM   1124 C CA  . PHE A 1 170 ? 5.15400   -3.66900  24.37200 1.000 23.05000 ? 170 PHE A CA  1 
ATOM   1125 C C   . PHE A 1 170 ? 4.35400   -4.48600  25.38100 1.000 23.05000 ? 170 PHE A C   1 
ATOM   1126 O O   . PHE A 1 170 ? 3.64700   -3.94400  26.23500 1.000 23.05000 ? 170 PHE A O   1 
ATOM   1127 C CB  . PHE A 1 170 ? 6.56600   -3.43300  24.91400 1.000 23.05000 ? 170 PHE A CB  1 
ATOM   1128 C CG  . PHE A 1 170 ? 7.62200   -3.35600  23.85200 1.000 23.05000 ? 170 PHE A CG  1 
ATOM   1129 C CD1 . PHE A 1 170 ? 7.91200   -2.15600  23.23200 1.000 23.05000 ? 170 PHE A CD1 1 
ATOM   1130 C CD2 . PHE A 1 170 ? 8.33700   -4.48100  23.48500 1.000 23.05000 ? 170 PHE A CD2 1 
ATOM   1131 C CE1 . PHE A 1 170 ? 8.88700   -2.07700  22.25700 1.000 23.05000 ? 170 PHE A CE1 1 
ATOM   1132 C CE2 . PHE A 1 170 ? 9.31400   -4.41200  22.51100 1.000 23.05000 ? 170 PHE A CE2 1 
ATOM   1133 C CZ  . PHE A 1 170 ? 9.58900   -3.20800  21.89600 1.000 23.05000 ? 170 PHE A CZ  1 
ATOM   1134 N N   . ASP A 1 171 ? 4.46300   -5.81300  25.26600 1.000 25.93000 ? 171 ASP A N   1 
ATOM   1135 C CA  . ASP A 1 171 ? 3.77000   -6.70500  26.19100 1.000 25.93000 ? 171 ASP A CA  1 
ATOM   1136 C C   . ASP A 1 171 ? 4.28700   -6.56900  27.61800 1.000 25.93000 ? 171 ASP A C   1 
ATOM   1137 O O   . ASP A 1 171 ? 3.54600   -6.83800  28.57000 1.000 25.93000 ? 171 ASP A O   1 
ATOM   1138 C CB  . ASP A 1 171 ? 3.90400   -8.15600  25.72600 1.000 25.93000 ? 171 ASP A CB  1 
ATOM   1139 C CG  . ASP A 1 171 ? 3.15900   -8.42800  24.43600 1.000 25.93000 ? 171 ASP A CG  1 
ATOM   1140 O OD1 . ASP A 1 171 ? 2.06100   -7.86100  24.25400 1.000 25.93000 ? 171 ASP A OD1 1 
ATOM   1141 O OD2 . ASP A 1 171 ? 3.67200   -9.20700  23.60500 1.000 25.93000 ? 171 ASP A OD2 1 
ATOM   1142 N N   . ARG A 1 172 ? 5.54400   -6.16600  27.79200 1.000 22.07000 ? 172 ARG A N   1 
ATOM   1143 C CA  . ARG A 1 172 ? 6.14100   -6.08400  29.11700 1.000 22.07000 ? 172 ARG A CA  1 
ATOM   1144 C C   . ARG A 1 172 ? 7.17600   -4.96900  29.14200 1.000 22.07000 ? 172 ARG A C   1 
ATOM   1145 O O   . ARG A 1 172 ? 7.98100   -4.84800  28.21700 1.000 22.07000 ? 172 ARG A O   1 
ATOM   1146 C CB  . ARG A 1 172 ? 6.78900   -7.42000  29.50200 1.000 22.07000 ? 172 ARG A CB  1 
ATOM   1147 C CG  . ARG A 1 172 ? 7.75000   -7.34300  30.67300 1.000 22.07000 ? 172 ARG A CG  1 
ATOM   1148 C CD  . ARG A 1 172 ? 8.46500   -8.66700  30.88400 1.000 22.07000 ? 172 ARG A CD  1 
ATOM   1149 N NE  . ARG A 1 172 ? 7.53000   -9.75800  31.13200 1.000 22.07000 ? 172 ARG A NE  1 
ATOM   1150 C CZ  . ARG A 1 172 ? 7.01500   -10.04500 32.32000 1.000 22.07000 ? 172 ARG A CZ  1 
ATOM   1151 N NH1 . ARG A 1 172 ? 7.31700   -9.33500  33.39300 1.000 22.07000 ? 172 ARG A NH1 1 
ATOM   1152 N NH2 . ARG A 1 172 ? 6.17600   -11.07100 32.43200 1.000 22.07000 ? 172 ARG A NH2 1 
ATOM   1153 N N   . VAL A 1 173 ? 7.16800   -4.18000  30.21900 1.000 19.11000 ? 173 VAL A N   1 
ATOM   1154 C CA  . VAL A 1 173 ? 8.10900   -3.08200  30.42200 1.000 19.11000 ? 173 VAL A CA  1 
ATOM   1155 C C   . VAL A 1 173 ? 8.52100   -3.10000  31.88800 1.000 19.11000 ? 173 VAL A C   1 
ATOM   1156 O O   . VAL A 1 173 ? 7.68800   -2.87600  32.77200 1.000 19.11000 ? 173 VAL A O   1 
ATOM   1157 C CB  . VAL A 1 173 ? 7.50800   -1.71100  30.05700 1.000 19.11000 ? 173 VAL A CB  1 
ATOM   1158 C CG1 . VAL A 1 173 ? 8.49700   -0.59800  30.36800 1.000 19.11000 ? 173 VAL A CG1 1 
ATOM   1159 C CG2 . VAL A 1 173 ? 7.09700   -1.66700  28.59100 1.000 19.11000 ? 173 VAL A CG2 1 
ATOM   1160 N N   . MET A 1 174 ? 9.79800   -3.35600  32.14600 1.000 15.97000 ? 174 MET A N   1 
ATOM   1161 C CA  . MET A 1 174 ? 10.31800  -3.48900  33.49900 1.000 15.97000 ? 174 MET A CA  1 
ATOM   1162 C C   . MET A 1 174 ? 11.41300  -2.46300  33.73400 1.000 15.97000 ? 174 MET A C   1 
ATOM   1163 O O   . MET A 1 174 ? 12.36900  -2.38000  32.95500 1.000 15.97000 ? 174 MET A O   1 
ATOM   1164 C CB  . MET A 1 174 ? 10.87400  -4.89400  33.74100 1.000 15.97000 ? 174 MET A CB  1 
ATOM   1165 C CG  . MET A 1 174 ? 10.04000  -6.02300  33.15700 1.000 15.97000 ? 174 MET A CG  1 
ATOM   1166 S SD  . MET A 1 174 ? 10.76300  -7.65100  33.45800 1.000 15.97000 ? 174 MET A SD  1 
ATOM   1167 C CE  . MET A 1 174 ? 12.44400  -7.39800  32.89100 1.000 15.97000 ? 174 MET A CE  1 
ATOM   1168 N N   . PHE A 1 175 ? 11.27100  -1.68700  34.80400 1.000 15.40000 ? 175 PHE A N   1 
ATOM   1169 C CA  . PHE A 1 175 ? 12.36400  -0.86600  35.29900 1.000 15.40000 ? 175 PHE A CA  1 
ATOM   1170 C C   . PHE A 1 175 ? 13.22200  -1.71300  36.22500 1.000 15.40000 ? 175 PHE A C   1 
ATOM   1171 O O   . PHE A 1 175 ? 12.70900  -2.32000  37.17700 1.000 15.40000 ? 175 PHE A O   1 
ATOM   1172 C CB  . PHE A 1 175 ? 11.83700  0.36400   36.03400 1.000 15.40000 ? 175 PHE A CB  1 
ATOM   1173 C CG  . PHE A 1 175 ? 12.78500  1.52800   36.03100 1.000 15.40000 ? 175 PHE A CG  1 
ATOM   1174 C CD1 . PHE A 1 175 ? 14.15700  1.33400   36.03600 1.000 15.40000 ? 175 PHE A CD1 1 
ATOM   1175 C CD2 . PHE A 1 175 ? 12.30200  2.81500   36.01300 1.000 15.40000 ? 175 PHE A CD2 1 
ATOM   1176 C CE1 . PHE A 1 175 ? 15.02100  2.40400   36.03200 1.000 15.40000 ? 175 PHE A CE1 1 
ATOM   1177 C CE2 . PHE A 1 175 ? 13.15700  3.89100   36.00900 1.000 15.40000 ? 175 PHE A CE2 1 
ATOM   1178 C CZ  . PHE A 1 175 ? 14.52000  3.68400   36.01700 1.000 15.40000 ? 175 PHE A CZ  1 
ATOM   1179 N N   . TYR A 1 176 ? 14.53600  -1.67700  35.98100 1.000 17.86000 ? 176 TYR A N   1 
ATOM   1180 C CA  . TYR A 1 176 ? 15.50400  -2.69600  36.38000 1.000 17.86000 ? 176 TYR A CA  1 
ATOM   1181 C C   . TYR A 1 176 ? 16.73300  -1.95000  36.90300 1.000 17.86000 ? 176 TYR A C   1 
ATOM   1182 O O   . TYR A 1 176 ? 17.59600  -1.53700  36.12400 1.000 17.86000 ? 176 TYR A O   1 
ATOM   1183 C CB  . TYR A 1 176 ? 15.80500  -3.56400  35.16100 1.000 17.86000 ? 176 TYR A CB  1 
ATOM   1184 C CG  . TYR A 1 176 ? 16.86900  -4.62800  35.27400 1.000 17.86000 ? 176 TYR A CG  1 
ATOM   1185 C CD1 . TYR A 1 176 ? 18.21000  -4.32700  35.06300 1.000 17.86000 ? 176 TYR A CD1 1 
ATOM   1186 C CD2 . TYR A 1 176 ? 16.52600  -5.95100  35.51400 1.000 17.86000 ? 176 TYR A CD2 1 
ATOM   1187 C CE1 . TYR A 1 176 ? 19.18300  -5.30600  35.13700 1.000 17.86000 ? 176 TYR A CE1 1 
ATOM   1188 C CE2 . TYR A 1 176 ? 17.48900  -6.93400  35.58800 1.000 17.86000 ? 176 TYR A CE2 1 
ATOM   1189 C CZ  . TYR A 1 176 ? 18.81500  -6.61100  35.39400 1.000 17.86000 ? 176 TYR A CZ  1 
ATOM   1190 O OH  . TYR A 1 176 ? 19.77500  -7.59600  35.47300 1.000 17.86000 ? 176 TYR A OH  1 
ATOM   1191 N N   . ARG A 1 177 ? 16.78100  -1.73100  38.21700 1.000 16.32000 ? 177 ARG A N   1 
ATOM   1192 C CA  . ARG A 1 177 ? 17.85700  -0.96000  38.83100 1.000 16.32000 ? 177 ARG A CA  1 
ATOM   1193 C C   . ARG A 1 177 ? 19.06800  -1.83900  39.12000 1.000 16.32000 ? 177 ARG A C   1 
ATOM   1194 O O   . ARG A 1 177 ? 18.92900  -2.99300  39.53400 1.000 16.32000 ? 177 ARG A O   1 
ATOM   1195 C CB  . ARG A 1 177 ? 17.37400  -0.29500  40.12500 1.000 16.32000 ? 177 ARG A CB  1 
ATOM   1196 C CG  . ARG A 1 177 ? 18.49900  0.14800   41.04900 1.000 16.32000 ? 177 ARG A CG  1 
ATOM   1197 C CD  . ARG A 1 177 ? 18.13900  1.36800   41.88300 1.000 16.32000 ? 177 ARG A CD  1 
ATOM   1198 N NE  . ARG A 1 177 ? 17.40900  1.04100   43.10200 1.000 16.32000 ? 177 ARG A NE  1 
ATOM   1199 C CZ  . ARG A 1 177 ? 17.17800  1.90100   44.08600 1.000 16.32000 ? 177 ARG A CZ  1 
ATOM   1200 N NH1 . ARG A 1 177 ? 17.61600  3.14800   44.03200 1.000 16.32000 ? 177 ARG A NH1 1 
ATOM   1201 N NH2 . ARG A 1 177 ? 16.49200  1.49800   45.15200 1.000 16.32000 ? 177 ARG A NH2 1 
ATOM   1202 N N   . PHE A 1 178 ? 20.25800  -1.28400  38.89800 1.000 17.82000 ? 178 PHE A N   1 
ATOM   1203 C CA  . PHE A 1 178 ? 21.50500  -1.93600  39.27500 1.000 17.82000 ? 178 PHE A CA  1 
ATOM   1204 C C   . PHE A 1 178 ? 21.87800  -1.55300  40.70200 1.000 17.82000 ? 178 PHE A C   1 
ATOM   1205 O O   . PHE A 1 178 ? 21.64100  -0.42100  41.13300 1.000 17.82000 ? 178 PHE A O   1 
ATOM   1206 C CB  . PHE A 1 178 ? 22.63400  -1.54900  38.31600 1.000 17.82000 ? 178 PHE A CB  1 
ATOM   1207 C CG  . PHE A 1 178 ? 22.47800  -2.11600  36.93000 1.000 17.82000 ? 178 PHE A CG  1 
ATOM   1208 C CD1 . PHE A 1 178 ? 21.45900  -1.68600  36.10000 1.000 17.82000 ? 178 PHE A CD1 1 
ATOM   1209 C CD2 . PHE A 1 178 ? 23.35900  -3.07100  36.45500 1.000 17.82000 ? 178 PHE A CD2 1 
ATOM   1210 C CE1 . PHE A 1 178 ? 21.31200  -2.20200  34.83000 1.000 17.82000 ? 178 PHE A CE1 1 
ATOM   1211 C CE2 . PHE A 1 178 ? 23.21900  -3.59000  35.18200 1.000 17.82000 ? 178 PHE A CE2 1 
ATOM   1212 C CZ  . PHE A 1 178 ? 22.19300  -3.15400  34.36900 1.000 17.82000 ? 178 PHE A CZ  1 
ATOM   1213 N N   . ASP A 1 179 ? 22.47700  -2.49400  41.42600 1.000 22.00000 ? 179 ASP A N   1 
ATOM   1214 C CA  . ASP A 1 179 ? 22.85600  -2.27600  42.81200 1.000 22.00000 ? 179 ASP A CA  1 
ATOM   1215 C C   . ASP A 1 179 ? 24.36400  -2.04200  42.91200 1.000 22.00000 ? 179 ASP A C   1 
ATOM   1216 O O   . ASP A 1 179 ? 25.05700  -1.85100  41.90600 1.000 22.00000 ? 179 ASP A O   1 
ATOM   1217 C CB  . ASP A 1 179 ? 22.39700  -3.45500  43.67800 1.000 22.00000 ? 179 ASP A CB  1 
ATOM   1218 C CG  . ASP A 1 179 ? 23.27200  -4.68300  43.51100 1.000 22.00000 ? 179 ASP A CG  1 
ATOM   1219 O OD1 . ASP A 1 179 ? 23.80200  -4.89700  42.40300 1.000 22.00000 ? 179 ASP A OD1 1 
ATOM   1220 O OD2 . ASP A 1 179 ? 23.42900  -5.43700  44.49400 1.000 22.00000 ? 179 ASP A OD2 1 
ATOM   1221 N N   . ARG A 1 180 ? 24.88400  -2.05000  44.14300 1.000 26.03000 ? 180 ARG A N   1 
ATOM   1222 C CA  . ARG A 1 180 ? 26.30800  -1.80600  44.35000 1.000 26.03000 ? 180 ARG A CA  1 
ATOM   1223 C C   . ARG A 1 180 ? 27.16500  -2.90300  43.73400 1.000 26.03000 ? 180 ARG A C   1 
ATOM   1224 O O   . ARG A 1 180 ? 28.31200  -2.65100  43.34800 1.000 26.03000 ? 180 ARG A O   1 
ATOM   1225 C CB  . ARG A 1 180 ? 26.60500  -1.67200  45.84400 1.000 26.03000 ? 180 ARG A CB  1 
ATOM   1226 C CG  . ARG A 1 180 ? 25.94400  -0.47000  46.49700 1.000 26.03000 ? 180 ARG A CG  1 
ATOM   1227 C CD  . ARG A 1 180 ? 26.27800  -0.39100  47.97800 1.000 26.03000 ? 180 ARG A CD  1 
ATOM   1228 N NE  . ARG A 1 180 ? 27.71600  -0.41100  48.21100 1.000 26.03000 ? 180 ARG A NE  1 
ATOM   1229 C CZ  . ARG A 1 180 ? 28.48700  0.66800   48.23800 1.000 26.03000 ? 180 ARG A CZ  1 
ATOM   1230 N NH1 . ARG A 1 180 ? 27.98800  1.87900   48.05100 1.000 26.03000 ? 180 ARG A NH1 1 
ATOM   1231 N NH2 . ARG A 1 180 ? 29.79100  0.52900   48.45800 1.000 26.03000 ? 180 ARG A NH2 1 
ATOM   1232 N N   . ASP A 1 181 ? 26.63600  -4.12100  43.63800 1.000 25.04000 ? 181 ASP A N   1 
ATOM   1233 C CA  . ASP A 1 181 ? 27.32300  -5.22700  42.98700 1.000 25.04000 ? 181 ASP A CA  1 
ATOM   1234 C C   . ASP A 1 181 ? 26.89000  -5.40500  41.53800 1.000 25.04000 ? 181 ASP A C   1 
ATOM   1235 O O   . ASP A 1 181 ? 27.17700  -6.44700  40.93800 1.000 25.04000 ? 181 ASP A O   1 
ATOM   1236 C CB  . ASP A 1 181 ? 27.10100  -6.52200  43.76900 1.000 25.04000 ? 181 ASP A CB  1 
ATOM   1237 C CG  . ASP A 1 181 ? 27.73500  -6.48800  45.14200 1.000 25.04000 ? 181 ASP A CG  1 
ATOM   1238 O OD1 . ASP A 1 181 ? 28.76300  -5.79600  45.30700 1.000 25.04000 ? 181 ASP A OD1 1 
ATOM   1239 O OD2 . ASP A 1 181 ? 27.20600  -7.15300  46.05700 1.000 25.04000 ? 181 ASP A OD2 1 
ATOM   1240 N N   . TRP A 1 182 ? 26.19600  -4.41700  40.97300 1.000 23.04000 ? 182 TRP A N   1 
ATOM   1241 C CA  . TRP A 1 182 ? 25.69600  -4.43400  39.59900 1.000 23.04000 ? 182 TRP A CA  1 
ATOM   1242 C C   . TRP A 1 182 ? 24.74400  -5.59600  39.33100 1.000 23.04000 ? 182 TRP A C   1 
ATOM   1243 O O   . TRP A 1 182 ? 24.57900  -6.01400  38.18000 1.000 23.04000 ? 182 TRP A O   1 
ATOM   1244 C CB  . TRP A 1 182 ? 26.85000  -4.44800  38.58800 1.000 23.04000 ? 182 TRP A CB  1 
ATOM   1245 C CG  . TRP A 1 182 ? 27.64800  -3.18000  38.58300 1.000 23.04000 ? 182 TRP A CG  1 
ATOM   1246 C CD1 . TRP A 1 182 ? 28.74300  -2.89700  39.34600 1.000 23.04000 ? 182 TRP A CD1 1 
ATOM   1247 C CD2 . TRP A 1 182 ? 27.40800  -2.02000  37.77900 1.000 23.04000 ? 182 TRP A CD2 1 
ATOM   1248 N NE1 . TRP A 1 182 ? 29.20100  -1.63200  39.06500 1.000 23.04000 ? 182 TRP A NE1 1 
ATOM   1249 C CE2 . TRP A 1 182 ? 28.39800  -1.07300  38.10600 1.000 23.04000 ? 182 TRP A CE2 1 
ATOM   1250 C CE3 . TRP A 1 182 ? 26.45100  -1.68900  36.81500 1.000 23.04000 ? 182 TRP A CE3 1 
ATOM   1251 C CZ2 . TRP A 1 182 ? 28.45900  0.18100   37.50100 1.000 23.04000 ? 182 TRP A CZ2 1 
ATOM   1252 C CZ3 . TRP A 1 182 ? 26.51400  -0.44600  36.21400 1.000 23.04000 ? 182 TRP A CZ3 1 
ATOM   1253 C CH2 . TRP A 1 182 ? 27.51000  0.47400   36.56000 1.000 23.04000 ? 182 TRP A CH2 1 
ATOM   1254 N N   . ASN A 1 183 ? 24.11400  -6.13200  40.37300 1.000 20.09000 ? 183 ASN A N   1 
ATOM   1255 C CA  . ASN A 1 183 ? 22.98900  -7.03400  40.18000 1.000 20.09000 ? 183 ASN A CA  1 
ATOM   1256 C C   . ASN A 1 183 ? 21.76000  -6.25200  39.73400 1.000 20.09000 ? 183 ASN A C   1 
ATOM   1257 O O   . ASN A 1 183 ? 21.54800  -5.10400  40.13300 1.000 20.09000 ? 183 ASN A O   1 
ATOM   1258 C CB  . ASN A 1 183 ? 22.67400  -7.79200  41.46900 1.000 20.09000 ? 183 ASN A CB  1 
ATOM   1259 C CG  . ASN A 1 183 ? 23.75600  -8.77900  41.84500 1.000 20.09000 ? 183 ASN A CG  1 
ATOM   1260 O OD1 . ASN A 1 183 ? 23.67900  -9.95900  41.50800 1.000 20.09000 ? 183 ASN A OD1 1 
ATOM   1261 N ND2 . ASN A 1 183 ? 24.77200  -8.30300  42.55100 1.000 20.09000 ? 183 ASN A ND2 1 
ATOM   1262 N N   . GLY A 1 184 ? 20.95000  -6.87900  38.89600 1.000 17.36000 ? 184 GLY A N   1 
ATOM   1263 C CA  . GLY A 1 184 ? 19.68400  -6.29300  38.52900 1.000 17.36000 ? 184 GLY A CA  1 
ATOM   1264 C C   . GLY A 1 184 ? 18.58400  -6.58700  39.53200 1.000 17.36000 ? 184 GLY A C   1 
ATOM   1265 O O   . GLY A 1 184 ? 18.70600  -7.47100  40.37700 1.000 17.36000 ? 184 GLY A O   1 
ATOM   1266 N N   . ILE A 1 185 ? 17.49700  -5.82500  39.42000 1.000 15.79000 ? 185 ILE A N   1 
ATOM   1267 C CA  . ILE A 1 185 ? 16.28400  -6.06900  40.19400 1.000 15.79000 ? 185 ILE A CA  1 
ATOM   1268 C C   . ILE A 1 185 ? 15.13700  -5.30500  39.54600 1.000 15.79000 ? 185 ILE A C   1 
ATOM   1269 O O   . ILE A 1 185 ? 15.26300  -4.11400  39.24000 1.000 15.79000 ? 185 ILE A O   1 
ATOM   1270 C CB  . ILE A 1 185 ? 16.46000  -5.67500  41.67400 1.000 15.79000 ? 185 ILE A CB  1 
ATOM   1271 C CG1 . ILE A 1 185 ? 15.11900  -5.72600  42.41000 1.000 15.79000 ? 185 ILE A CG1 1 
ATOM   1272 C CG2 . ILE A 1 185 ? 17.08900  -4.29900  41.80100 1.000 15.79000 ? 185 ILE A CG2 1 
ATOM   1273 C CD1 . ILE A 1 185 ? 15.20600  -5.30100  43.85900 1.000 15.79000 ? 185 ILE A CD1 1 
ATOM   1274 N N   . VAL A 1 186 ? 14.00700  -5.97800  39.34000 1.000 15.01000 ? 186 VAL A N   1 
ATOM   1275 C CA  . VAL A 1 186 ? 12.87100  -5.36200  38.66500 1.000 15.01000 ? 186 VAL A CA  1 
ATOM   1276 C C   . VAL A 1 186 ? 12.14800  -4.46100  39.65500 1.000 15.01000 ? 186 VAL A C   1 
ATOM   1277 O O   . VAL A 1 186 ? 11.19300  -4.88200  40.31800 1.000 15.01000 ? 186 VAL A O   1 
ATOM   1278 C CB  . VAL A 1 186 ? 11.92700  -6.42600  38.07600 1.000 15.01000 ? 186 VAL A CB  1 
ATOM   1279 C CG1 . VAL A 1 186 ? 10.75800  -5.76900  37.36100 1.000 15.01000 ? 186 VAL A CG1 1 
ATOM   1280 C CG2 . VAL A 1 186 ? 12.68900  -7.33200  37.12500 1.000 15.01000 ? 186 VAL A CG2 1 
ATOM   1281 N N   . ILE A 1 187 ? 12.61600  -3.21600  39.78000 1.000 15.13000 ? 187 ILE A N   1 
ATOM   1282 C CA  . ILE A 1 187 ? 11.99100  -2.28200  40.70500 1.000 15.13000 ? 187 ILE A CA  1 
ATOM   1283 C C   . ILE A 1 187 ? 10.60100  -1.87000  40.24600 1.000 15.13000 ? 187 ILE A C   1 
ATOM   1284 O O   . ILE A 1 187 ? 9.78200   -1.45500  41.07400 1.000 15.13000 ? 187 ILE A O   1 
ATOM   1285 C CB  . ILE A 1 187 ? 12.87300  -1.04000  40.91600 1.000 15.13000 ? 187 ILE A CB  1 
ATOM   1286 C CG1 . ILE A 1 187 ? 12.96700  -0.21400  39.63300 1.000 15.13000 ? 187 ILE A CG1 1 
ATOM   1287 C CG2 . ILE A 1 187 ? 14.25100  -1.45400  41.38500 1.000 15.13000 ? 187 ILE A CG2 1 
ATOM   1288 C CD1 . ILE A 1 187 ? 13.77800  1.04700   39.79100 1.000 15.13000 ? 187 ILE A CD1 1 
ATOM   1289 N N   . ALA A 1 188 ? 10.29700  -1.97300  38.95300 1.000 14.65000 ? 188 ALA A N   1 
ATOM   1290 C CA  . ALA A 1 188 ? 8.96100   -1.60100  38.50600 1.000 14.65000 ? 188 ALA A CA  1 
ATOM   1291 C C   . ALA A 1 188 ? 8.57600   -2.44800  37.30600 1.000 14.65000 ? 188 ALA A C   1 
ATOM   1292 O O   . ALA A 1 188 ? 9.43500   -2.95300  36.58400 1.000 14.65000 ? 188 ALA A O   1 
ATOM   1293 C CB  . ALA A 1 188 ? 8.87300   -0.11100  38.16200 1.000 14.65000 ? 188 ALA A CB  1 
ATOM   1294 N N   . GLU A 1 189 ? 7.26900   -2.57600  37.08100 1.000 18.84000 ? 189 GLU A N   1 
ATOM   1295 C CA  . GLU A 1 189 ? 6.78400   -3.43400  36.01100 1.000 18.84000 ? 189 GLU A CA  1 
ATOM   1296 C C   . GLU A 1 189 ? 5.41500   -2.97400  35.53200 1.000 18.84000 ? 189 GLU A C   1 
ATOM   1297 O O   . GLU A 1 189 ? 4.57700   -2.54600  36.33000 1.000 18.84000 ? 189 GLU A O   1 
ATOM   1298 C CB  . GLU A 1 189 ? 6.70500   -4.89100  36.47500 1.000 18.84000 ? 189 GLU A CB  1 
ATOM   1299 C CG  . GLU A 1 189 ? 6.47800   -5.90300  35.36500 1.000 18.84000 ? 189 GLU A CG  1 
ATOM   1300 C CD  . GLU A 1 189 ? 6.22400   -7.29500  35.90700 1.000 18.84000 ? 189 GLU A CD  1 
ATOM   1301 O OE1 . GLU A 1 189 ? 5.56000   -7.40800  36.95800 1.000 18.84000 ? 189 GLU A OE1 1 
ATOM   1302 O OE2 . GLU A 1 189 ? 6.69600   -8.27300  35.29400 1.000 18.84000 ? 189 GLU A OE2 1 
ATOM   1303 N N   . ASP A 1 190 ? 5.20200   -3.08600  34.22300 1.000 21.04000 ? 190 ASP A N   1 
ATOM   1304 C CA  . ASP A 1 190 ? 3.90100   -2.89100  33.59300 1.000 21.04000 ? 190 ASP A CA  1 
ATOM   1305 C C   . ASP A 1 190 ? 3.82100   -3.88000  32.44100 1.000 21.04000 ? 190 ASP A C   1 
ATOM   1306 O O   . ASP A 1 190 ? 4.64500   -3.82900  31.52400 1.000 21.04000 ? 190 ASP A O   1 
ATOM   1307 C CB  . ASP A 1 190 ? 3.72400   -1.45000  33.09900 1.000 21.04000 ? 190 ASP A CB  1 
ATOM   1308 C CG  . ASP A 1 190 ? 2.30100   -1.14700  32.65800 1.000 21.04000 ? 190 ASP A CG  1 
ATOM   1309 O OD1 . ASP A 1 190 ? 1.61900   -2.05600  32.13800 1.000 21.04000 ? 190 ASP A OD1 1 
ATOM   1310 O OD2 . ASP A 1 190 ? 1.86200   0.00900   32.83100 1.000 21.04000 ? 190 ASP A OD2 1 
ATOM   1311 N N   . LYS A 1 191 ? 2.82700   -4.76300  32.47300 1.000 23.56000 ? 191 LYS A N   1 
ATOM   1312 C CA  . LYS A 1 191 ? 2.84600   -5.95200  31.63400 1.000 23.56000 ? 191 LYS A CA  1 
ATOM   1313 C C   . LYS A 1 191 ? 1.42900   -6.32300  31.22500 1.000 23.56000 ? 191 LYS A C   1 
ATOM   1314 O O   . LYS A 1 191 ? 0.44600   -5.75300  31.70500 1.000 23.56000 ? 191 LYS A O   1 
ATOM   1315 C CB  . LYS A 1 191 ? 3.49000   -7.13100  32.36600 1.000 23.56000 ? 191 LYS A CB  1 
ATOM   1316 C CG  . LYS A 1 191 ? 2.69200   -7.54700  33.58800 1.000 23.56000 ? 191 LYS A CG  1 
ATOM   1317 C CD  . LYS A 1 191 ? 3.28300   -8.74800  34.28800 1.000 23.56000 ? 191 LYS A CD  1 
ATOM   1318 C CE  . LYS A 1 191 ? 2.35400   -9.21200  35.39500 1.000 23.56000 ? 191 LYS A CE  1 
ATOM   1319 N NZ  . LYS A 1 191 ? 1.05700   -9.69200  34.84700 1.000 23.56000 ? 191 LYS A NZ  1 
ATOM   1320 N N   . GLN A 1 192 ? 1.34100   -7.29500  30.31900 1.000 26.92000 ? 192 GLN A N   1 
ATOM   1321 C CA  . GLN A 1 192 ? 0.06500   -7.93100  30.03300 1.000 26.92000 ? 192 GLN A CA  1 
ATOM   1322 C C   . GLN A 1 192 ? -0.46600  -8.59300  31.29600 1.000 26.92000 ? 192 GLN A C   1 
ATOM   1323 O O   . GLN A 1 192 ? 0.29700   -9.15000  32.09000 1.000 26.92000 ? 192 GLN A O   1 
ATOM   1324 C CB  . GLN A 1 192 ? 0.22600   -8.97100  28.92400 1.000 26.92000 ? 192 GLN A CB  1 
ATOM   1325 C CG  . GLN A 1 192 ? 0.72900   -8.41900  27.60200 1.000 26.92000 ? 192 GLN A CG  1 
ATOM   1326 C CD  . GLN A 1 192 ? -0.39000  -7.89100  26.72700 1.000 26.92000 ? 192 GLN A CD  1 
ATOM   1327 O OE1 . GLN A 1 192 ? -1.22700  -7.10700  27.17200 1.000 26.92000 ? 192 GLN A OE1 1 
ATOM   1328 N NE2 . GLN A 1 192 ? -0.41500  -8.33000  25.47300 1.000 26.92000 ? 192 GLN A NE2 1 
ATOM   1329 N N   . GLU A 1 193 ? -1.78400  -8.51500  31.49200 1.000 32.66000 ? 193 GLU A N   1 
ATOM   1330 C CA  . GLU A 1 193 ? -2.37200  -9.05200  32.71500 1.000 32.66000 ? 193 GLU A CA  1 
ATOM   1331 C C   . GLU A 1 193 ? -2.21000  -10.56500 32.80600 1.000 32.66000 ? 193 GLU A C   1 
ATOM   1332 O O   . GLU A 1 193 ? -2.11400  -11.11100 33.91200 1.000 32.66000 ? 193 GLU A O   1 
ATOM   1333 C CB  . GLU A 1 193 ? -3.84700  -8.66100  32.80600 1.000 32.66000 ? 193 GLU A CB  1 
ATOM   1334 C CG  . GLU A 1 193 ? -4.07800  -7.16700  32.98500 1.000 32.66000 ? 193 GLU A CG  1 
ATOM   1335 C CD  . GLU A 1 193 ? -5.51900  -6.83200  33.32200 1.000 32.66000 ? 193 GLU A CD  1 
ATOM   1336 O OE1 . GLU A 1 193 ? -6.39000  -7.71400  33.16500 1.000 32.66000 ? 193 GLU A OE1 1 
ATOM   1337 O OE2 . GLU A 1 193 ? -5.78000  -5.68800  33.75000 1.000 32.66000 ? 193 GLU A OE2 1 
ATOM   1338 N N   . HIS A 1 194 ? -2.16900  -11.25800 31.66700 1.000 27.29000 ? 194 HIS A N   1 
ATOM   1339 C CA  . HIS A 1 194 ? -1.99700  -12.70500 31.68300 1.000 27.29000 ? 194 HIS A CA  1 
ATOM   1340 C C   . HIS A 1 194 ? -0.54600  -13.13600 31.86000 1.000 27.29000 ? 194 HIS A C   1 
ATOM   1341 O O   . HIS A 1 194 ? -0.30000  -14.31700 32.12800 1.000 27.29000 ? 194 HIS A O   1 
ATOM   1342 C CB  . HIS A 1 194 ? -2.56900  -13.32100 30.39900 1.000 27.29000 ? 194 HIS A CB  1 
ATOM   1343 C CG  . HIS A 1 194 ? -1.80400  -12.97000 29.15900 1.000 27.29000 ? 194 HIS A CG  1 
ATOM   1344 N ND1 . HIS A 1 194 ? -0.66800  -13.64600 28.76800 1.000 27.29000 ? 194 HIS A ND1 1 
ATOM   1345 C CD2 . HIS A 1 194 ? -2.02100  -12.02200 28.21600 1.000 27.29000 ? 194 HIS A CD2 1 
ATOM   1346 C CE1 . HIS A 1 194 ? -0.21400  -13.12600 27.64200 1.000 27.29000 ? 194 HIS A CE1 1 
ATOM   1347 N NE2 . HIS A 1 194 ? -1.01700  -12.13900 27.28600 1.000 27.29000 ? 194 HIS A NE2 1 
ATOM   1348 N N   . LEU A 1 195 ? 0.41300   -12.22100 31.71500 1.000 24.76000 ? 195 LEU A N   1 
ATOM   1349 C CA  . LEU A 1 195 ? 1.82100   -12.55400 31.87800 1.000 24.76000 ? 195 LEU A CA  1 
ATOM   1350 C C   . LEU A 1 195 ? 2.19000   -12.68300 33.35600 1.000 24.76000 ? 195 LEU A C   1 
ATOM   1351 O O   . LEU A 1 195 ? 1.60500   -12.01300 34.21100 1.000 24.76000 ? 195 LEU A O   1 
ATOM   1352 C CB  . LEU A 1 195 ? 2.70000   -11.49600 31.21800 1.000 24.76000 ? 195 LEU A CB  1 
ATOM   1353 C CG  . LEU A 1 195 ? 2.73500   -11.48800 29.68900 1.000 24.76000 ? 195 LEU A CG  1 
ATOM   1354 C CD1 . LEU A 1 195 ? 3.70300   -10.42800 29.17900 1.000 24.76000 ? 195 LEU A CD1 1 
ATOM   1355 C CD2 . LEU A 1 195 ? 3.10600   -12.86100 29.15200 1.000 24.76000 ? 195 LEU A CD2 1 
ATOM   1356 N N   . PRO A 1 196 ? 3.14500   -13.55600 33.68000 1.000 22.75000 ? 196 PRO A N   1 
ATOM   1357 C CA  . PRO A 1 196 ? 3.67100   -13.59200 35.04900 1.000 22.75000 ? 196 PRO A CA  1 
ATOM   1358 C C   . PRO A 1 196 ? 4.39800   -12.30200 35.39700 1.000 22.75000 ? 196 PRO A C   1 
ATOM   1359 O O   . PRO A 1 196 ? 5.02400   -11.66500 34.54700 1.000 22.75000 ? 196 PRO A O   1 
ATOM   1360 C CB  . PRO A 1 196 ? 4.63300   -14.78600 35.02700 1.000 22.75000 ? 196 PRO A CB  1 
ATOM   1361 C CG  . PRO A 1 196 ? 5.05700   -14.88800 33.59800 1.000 22.75000 ? 196 PRO A CG  1 
ATOM   1362 C CD  . PRO A 1 196 ? 3.84400   -14.50300 32.79300 1.000 22.75000 ? 196 PRO A CD  1 
ATOM   1363 N N   . SER A 1 197 ? 4.31300   -11.91800 36.66800 1.000 20.02000 ? 197 SER A N   1 
ATOM   1364 C CA  . SER A 1 197 ? 5.01400   -10.73900 37.16000 1.000 20.02000 ? 197 SER A CA  1 
ATOM   1365 C C   . SER A 1 197 ? 6.41700   -11.12100 37.60900 1.000 20.02000 ? 197 SER A C   1 
ATOM   1366 O O   . SER A 1 197 ? 6.60300   -12.12200 38.30700 1.000 20.02000 ? 197 SER A O   1 
ATOM   1367 C CB  . SER A 1 197 ? 4.25000   -10.09000 38.31500 1.000 20.02000 ? 197 SER A CB  1 
ATOM   1368 O OG  . SER A 1 197 ? 4.87900   -8.88600  38.72300 1.000 20.02000 ? 197 SER A OG  1 
ATOM   1369 N N   . TYR A 1 198 ? 7.40100   -10.31400 37.21400 1.000 18.98000 ? 198 TYR A N   1 
ATOM   1370 C CA  . TYR A 1 198 ? 8.78100   -10.48400 37.64400 1.000 18.98000 ? 198 TYR A CA  1 
ATOM   1371 C C   . TYR A 1 198 ? 9.17800   -9.45400  38.69200 1.000 18.98000 ? 198 TYR A C   1 
ATOM   1372 O O   . TYR A 1 198 ? 10.36700  -9.15900  38.84600 1.000 18.98000 ? 198 TYR A O   1 
ATOM   1373 C CB  . TYR A 1 198 ? 9.72900   -10.40800 36.44600 1.000 18.98000 ? 198 TYR A CB  1 
ATOM   1374 C CG  . TYR A 1 198 ? 9.42700   -11.40000 35.34500 1.000 18.98000 ? 198 TYR A CG  1 
ATOM   1375 C CD1 . TYR A 1 198 ? 8.71600   -12.56500 35.60500 1.000 18.98000 ? 198 TYR A CD1 1 
ATOM   1376 C CD2 . TYR A 1 198 ? 9.85600   -11.17200 34.04500 1.000 18.98000 ? 198 TYR A CD2 1 
ATOM   1377 C CE1 . TYR A 1 198 ? 8.43800   -13.46900 34.60300 1.000 18.98000 ? 198 TYR A CE1 1 
ATOM   1378 C CE2 . TYR A 1 198 ? 9.58400   -12.07200 33.03400 1.000 18.98000 ? 198 TYR A CE2 1 
ATOM   1379 C CZ  . TYR A 1 198 ? 8.87400   -13.22000 33.31800 1.000 18.98000 ? 198 TYR A CZ  1 
ATOM   1380 O OH  . TYR A 1 198 ? 8.59800   -14.12300 32.31700 1.000 18.98000 ? 198 TYR A OH  1 
ATOM   1381 N N   . LEU A 1 199 ? 8.20000   -8.89500  39.40100 1.000 16.73000 ? 199 LEU A N   1 
ATOM   1382 C CA  . LEU A 1 199 ? 8.44500   -7.74600  40.26100 1.000 16.73000 ? 199 LEU A CA  1 
ATOM   1383 C C   . LEU A 1 199 ? 9.40000   -8.09200  41.39700 1.000 16.73000 ? 199 LEU A C   1 
ATOM   1384 O O   . LEU A 1 199 ? 9.27200   -9.13100  42.04900 1.000 16.73000 ? 199 LEU A O   1 
ATOM   1385 C CB  . LEU A 1 199 ? 7.11600   -7.23500  40.82100 1.000 16.73000 ? 199 LEU A CB  1 
ATOM   1386 C CG  . LEU A 1 199 ? 7.05700   -5.78200  41.28200 1.000 16.73000 ? 199 LEU A CG  1 
ATOM   1387 C CD1 . LEU A 1 199 ? 7.65600   -4.88200  40.21900 1.000 16.73000 ? 199 LEU A CD1 1 
ATOM   1388 C CD2 . LEU A 1 199 ? 5.61800   -5.37900  41.57100 1.000 16.73000 ? 199 LEU A CD2 1 
ATOM   1389 N N   . ASP A 1 200 ? 10.35700  -7.19200  41.63600 1.000 17.31000 ? 200 ASP A N   1 
ATOM   1390 C CA  . ASP A 1 200 ? 11.32200  -7.30900  42.73400 1.000 17.31000 ? 200 ASP A CA  1 
ATOM   1391 C C   . ASP A 1 200 ? 12.09400  -8.62800  42.68800 1.000 17.31000 ? 200 ASP A C   1 
ATOM   1392 O O   . ASP A 1 200 ? 12.52800  -9.14700  43.72000 1.000 17.31000 ? 200 ASP A O   1 
ATOM   1393 C CB  . ASP A 1 200 ? 10.63400  -7.12700  44.09000 1.000 17.31000 ? 200 ASP A CB  1 
ATOM   1394 C CG  . ASP A 1 200 ? 10.57200  -5.66900  44.51900 1.000 17.31000 ? 200 ASP A CG  1 
ATOM   1395 O OD1 . ASP A 1 200 ? 11.64700  -5.06400  44.72000 1.000 17.31000 ? 200 ASP A OD1 1 
ATOM   1396 O OD2 . ASP A 1 200 ? 9.45200   -5.12400  44.63700 1.000 17.31000 ? 200 ASP A OD2 1 
ATOM   1397 N N   . LEU A 1 201 ? 12.28600  -9.17300  41.48900 1.000 15.92000 ? 201 LEU A N   1 
ATOM   1398 C CA  . LEU A 1 201 ? 13.16500  -10.31900 41.30000 1.000 15.92000 ? 201 LEU A CA  1 
ATOM   1399 C C   . LEU A 1 201 ? 14.58000  -9.82400  41.03200 1.000 15.92000 ? 201 LEU A C   1 
ATOM   1400 O O   . LEU A 1 201 ? 14.79600  -9.00800  40.13100 1.000 15.92000 ? 201 LEU A O   1 
ATOM   1401 C CB  . LEU A 1 201 ? 12.68800  -11.19900 40.14400 1.000 15.92000 ? 201 LEU A CB  1 
ATOM   1402 C CG  . LEU A 1 201 ? 11.32600  -11.89000 40.24800 1.000 15.92000 ? 201 LEU A CG  1 
ATOM   1403 C CD1 . LEU A 1 201 ? 11.14900  -12.86500 39.09400 1.000 15.92000 ? 201 LEU A CD1 1 
ATOM   1404 C CD2 . LEU A 1 201 ? 11.15700  -12.60200 41.57900 1.000 15.92000 ? 201 LEU A CD2 1 
ATOM   1405 N N   . HIS A 1 202 ? 15.53300  -10.29600 41.83000 1.000 14.81000 ? 202 HIS A N   1 
ATOM   1406 C CA  . HIS A 1 202 ? 16.93200  -9.97300  41.59700 1.000 14.81000 ? 202 HIS A CA  1 
ATOM   1407 C C   . HIS A 1 202 ? 17.51500  -10.87000 40.51400 1.000 14.81000 ? 202 HIS A C   1 
ATOM   1408 O O   . HIS A 1 202 ? 17.17300  -12.05100 40.40500 1.000 14.81000 ? 202 HIS A O   1 
ATOM   1409 C CB  . HIS A 1 202 ? 17.74500  -10.12400 42.88200 1.000 14.81000 ? 202 HIS A CB  1 
ATOM   1410 C CG  . HIS A 1 202 ? 17.32700  -9.19200  43.97400 1.000 14.81000 ? 202 HIS A CG  1 
ATOM   1411 N ND1 . HIS A 1 202 ? 16.05600  -9.19500  44.50700 1.000 14.81000 ? 202 HIS A ND1 1 
ATOM   1412 C CD2 . HIS A 1 202 ? 18.01200  -8.23400  44.64100 1.000 14.81000 ? 202 HIS A CD2 1 
ATOM   1413 C CE1 . HIS A 1 202 ? 15.97500  -8.27600  45.45200 1.000 14.81000 ? 202 HIS A CE1 1 
ATOM   1414 N NE2 . HIS A 1 202 ? 17.14800  -7.67700  45.55200 1.000 14.81000 ? 202 HIS A NE2 1 
ATOM   1415 N N   . TYR A 1 203 ? 18.43000  -10.30500 39.73200 1.000 21.33000 ? 203 TYR A N   1 
ATOM   1416 C CA  . TYR A 1 203 ? 19.18200  -11.04900 38.73900 1.000 21.33000 ? 203 TYR A CA  1 
ATOM   1417 C C   . TYR A 1 203 ? 20.66900  -10.82400 38.96600 1.000 21.33000 ? 203 TYR A C   1 
ATOM   1418 O O   . TYR A 1 203 ? 21.08500  -9.73300  39.36600 1.000 21.33000 ? 203 TYR A O   1 
ATOM   1419 C CB  . TYR A 1 203 ? 18.81000  -10.62400 37.30800 1.000 21.33000 ? 203 TYR A CB  1 
ATOM   1420 C CG  . TYR A 1 203 ? 17.36700  -10.89300 36.92200 1.000 21.33000 ? 203 TYR A CG  1 
ATOM   1421 C CD1 . TYR A 1 203 ? 16.65800  -11.94900 37.47800 1.000 21.33000 ? 203 TYR A CD1 1 
ATOM   1422 C CD2 . TYR A 1 203 ? 16.71500  -10.08800 35.99600 1.000 21.33000 ? 203 TYR A CD2 1 
ATOM   1423 C CE1 . TYR A 1 203 ? 15.34100  -12.19100 37.13300 1.000 21.33000 ? 203 TYR A CE1 1 
ATOM   1424 C CE2 . TYR A 1 203 ? 15.40000  -10.32200 35.64200 1.000 21.33000 ? 203 TYR A CE2 1 
ATOM   1425 C CZ  . TYR A 1 203 ? 14.71700  -11.37500 36.21200 1.000 21.33000 ? 203 TYR A CZ  1 
ATOM   1426 O OH  . TYR A 1 203 ? 13.40700  -11.61400 35.86300 1.000 21.33000 ? 203 TYR A OH  1 
ATOM   1427 N N   . PRO A 1 204 ? 21.48700  -11.84100 38.72000 1.000 22.18000 ? 204 PRO A N   1 
ATOM   1428 C CA  . PRO A 1 204 ? 22.92900  -11.70800 38.95400 1.000 22.18000 ? 204 PRO A CA  1 
ATOM   1429 C C   . PRO A 1 204 ? 23.57600  -10.71300 38.00400 1.000 22.18000 ? 204 PRO A C   1 
ATOM   1430 O O   . PRO A 1 204 ? 23.11000  -10.49100 36.88300 1.000 22.18000 ? 204 PRO A O   1 
ATOM   1431 C CB  . PRO A 1 204 ? 23.46200  -13.12600 38.72200 1.000 22.18000 ? 204 PRO A CB  1 
ATOM   1432 C CG  . PRO A 1 204 ? 22.43000  -13.77800 37.85800 1.000 22.18000 ? 204 PRO A CG  1 
ATOM   1433 C CD  . PRO A 1 204 ? 21.11800  -13.19500 38.26800 1.000 22.18000 ? 204 PRO A CD  1 
ATOM   1434 N N   . ALA A 1 205 ? 24.66500  -10.10300 38.47700 1.000 23.05000 ? 205 ALA A N   1 
ATOM   1435 C CA  . ALA A 1 205 ? 25.44000  -9.20100  37.63300 1.000 23.05000 ? 205 ALA A CA  1 
ATOM   1436 C C   . ALA A 1 205 ? 26.01200  -9.91100  36.41300 1.000 23.05000 ? 205 ALA A C   1 
ATOM   1437 O O   . ALA A 1 205 ? 26.32400  -9.25200  35.41600 1.000 23.05000 ? 205 ALA A O   1 
ATOM   1438 C CB  . ALA A 1 205 ? 26.56900  -8.56300  38.44300 1.000 23.05000 ? 205 ALA A CB  1 
ATOM   1439 N N   . SER A 1 206 ? 26.17000  -11.23500 36.47800 1.000 25.03000 ? 206 SER A N   1 
ATOM   1440 C CA  . SER A 1 206 ? 26.66600  -11.98900 35.33100 1.000 25.03000 ? 206 SER A CA  1 
ATOM   1441 C C   . SER A 1 206 ? 25.72000  -11.90300 34.14100 1.000 25.03000 ? 206 SER A C   1 
ATOM   1442 O O   . SER A 1 206 ? 26.15600  -12.03900 32.99200 1.000 25.03000 ? 206 SER A O   1 
ATOM   1443 C CB  . SER A 1 206 ? 26.88100  -13.45200 35.72200 1.000 25.03000 ? 206 SER A CB  1 
ATOM   1444 O OG  . SER A 1 206 ? 25.66600  -14.04700 36.15000 1.000 25.03000 ? 206 SER A OG  1 
ATOM   1445 N N   . ASP A 1 207 ? 24.42600  -11.69100 34.39400 1.000 26.75000 ? 207 ASP A N   1 
ATOM   1446 C CA  . ASP A 1 207 ? 23.44600  -11.68400 33.31200 1.000 26.75000 ? 207 ASP A CA  1 
ATOM   1447 C C   . ASP A 1 207 ? 23.68800  -10.55000 32.32300 1.000 26.75000 ? 207 ASP A C   1 
ATOM   1448 O O   . ASP A 1 207 ? 23.35800  -10.68000 31.13900 1.000 26.75000 ? 207 ASP A O   1 
ATOM   1449 C CB  . ASP A 1 207 ? 22.03700  -11.58900 33.89200 1.000 26.75000 ? 207 ASP A CB  1 
ATOM   1450 C CG  . ASP A 1 207 ? 21.55300  -12.90600 34.45600 1.000 26.75000 ? 207 ASP A CG  1 
ATOM   1451 O OD1 . ASP A 1 207 ? 22.36800  -13.85000 34.54000 1.000 26.75000 ? 207 ASP A OD1 1 
ATOM   1452 O OD2 . ASP A 1 207 ? 20.35900  -13.00200 34.80600 1.000 26.75000 ? 207 ASP A OD2 1 
ATOM   1453 N N   . ILE A 1 208 ? 24.25900  -9.44400  32.77900 1.000 25.99000 ? 208 ILE A N   1 
ATOM   1454 C CA  . ILE A 1 208 ? 24.61000  -8.31900  31.92400 1.000 25.99000 ? 208 ILE A CA  1 
ATOM   1455 C C   . ILE A 1 208 ? 26.10600  -8.06700  32.06700 1.000 25.99000 ? 208 ILE A C   1 
ATOM   1456 O O   . ILE A 1 208 ? 26.54700  -7.38200  32.99100 1.000 25.99000 ? 208 ILE A O   1 
ATOM   1457 C CB  . ILE A 1 208 ? 23.79300  -7.06200  32.27600 1.000 25.99000 ? 208 ILE A CB  1 
ATOM   1458 C CG1 . ILE A 1 208 ? 22.29500  -7.36500  32.20400 1.000 25.99000 ? 208 ILE A CG1 1 
ATOM   1459 C CG2 . ILE A 1 208 ? 24.13700  -5.92800  31.32900 1.000 25.99000 ? 208 ILE A CG2 1 
ATOM   1460 C CD1 . ILE A 1 208 ? 21.41100  -6.15900  32.43800 1.000 25.99000 ? 208 ILE A CD1 1 
ATOM   1461 N N   . PRO A 1 209 ? 26.91800  -8.60800  31.16400 1.000 28.09000 ? 209 PRO A N   1 
ATOM   1462 C CA  . PRO A 1 209 ? 28.37600  -8.51000  31.30400 1.000 28.09000 ? 209 PRO A CA  1 
ATOM   1463 C C   . PRO A 1 209 ? 28.87800  -7.09500  31.05600 1.000 28.09000 ? 209 PRO A C   1 
ATOM   1464 O O   . PRO A 1 209 ? 28.15500  -6.21000  30.59500 1.000 28.09000 ? 209 PRO A O   1 
ATOM   1465 C CB  . PRO A 1 209 ? 28.89800  -9.48500  30.24700 1.000 28.09000 ? 209 PRO A CB  1 
ATOM   1466 C CG  . PRO A 1 209 ? 27.82200  -9.51700  29.21600 1.000 28.09000 ? 209 PRO A CG  1 
ATOM   1467 C CD  . PRO A 1 209 ? 26.52500  -9.35800  29.95900 1.000 28.09000 ? 209 PRO A CD  1 
ATOM   1468 N N   . THR A 1 210 ? 30.15300  -6.89500  31.40100 1.000 28.98000 ? 210 THR A N   1 
ATOM   1469 C CA  . THR A 1 210 ? 30.76000  -5.56700  31.31300 1.000 28.98000 ? 210 THR A CA  1 
ATOM   1470 C C   . THR A 1 210 ? 30.64500  -4.93100  29.93000 1.000 28.98000 ? 210 THR A C   1 
ATOM   1471 O O   . THR A 1 210 ? 30.26100  -3.75000  29.85700 1.000 28.98000 ? 210 THR A O   1 
ATOM   1472 C CB  . THR A 1 210 ? 32.22600  -5.65100  31.76600 1.000 28.98000 ? 210 THR A CB  1 
ATOM   1473 O OG1 . THR A 1 210 ? 32.28300  -6.11000  33.12100 1.000 28.98000 ? 210 THR A OG1 1 
ATOM   1474 C CG2 . THR A 1 210 ? 32.90000  -4.29000  31.66300 1.000 28.98000 ? 210 THR A CG2 1 
ATOM   1475 N N   . PRO A 1 211 ? 30.97500  -5.60500  28.81700 1.000 30.70000 ? 211 PRO A N   1 
ATOM   1476 C CA  . PRO A 1 211 ? 30.80600  -4.94300  27.51300 1.000 30.70000 ? 211 PRO A CA  1 
ATOM   1477 C C   . PRO A 1 211 ? 29.37600  -4.51200  27.24000 1.000 30.70000 ? 211 PRO A C   1 
ATOM   1478 O O   . PRO A 1 211 ? 29.15500  -3.45100  26.63600 1.000 30.70000 ? 211 PRO A O   1 
ATOM   1479 C CB  . PRO A 1 211 ? 31.27500  -6.01000  26.51000 1.000 30.70000 ? 211 PRO A CB  1 
ATOM   1480 C CG  . PRO A 1 211 ? 32.10200  -6.95000  27.30000 1.000 30.70000 ? 211 PRO A CG  1 
ATOM   1481 C CD  . PRO A 1 211 ? 31.48100  -6.98000  28.65700 1.000 30.70000 ? 211 PRO A CD  1 
ATOM   1482 N N   . ALA A 1 212 ? 28.39500  -5.29100  27.69800 1.000 27.16000 ? 212 ALA A N   1 
ATOM   1483 C CA  . ALA A 1 212 ? 27.00700  -4.89400  27.50700 1.000 27.16000 ? 212 ALA A CA  1 
ATOM   1484 C C   . ALA A 1 212 ? 26.68200  -3.64700  28.31300 1.000 27.16000 ? 212 ALA A C   1 
ATOM   1485 O O   . ALA A 1 212 ? 25.98000  -2.75400  27.82600 1.000 27.16000 ? 212 ALA A O   1 
ATOM   1486 C CB  . ALA A 1 212 ? 26.07200  -6.04100  27.88900 1.000 27.16000 ? 212 ALA A CB  1 
ATOM   1487 N N   . ARG A 1 213 ? 27.20300  -3.55400  29.53900 1.000 26.70000 ? 213 ARG A N   1 
ATOM   1488 C CA  . ARG A 1 213 ? 26.97200  -2.35600  30.33500 1.000 26.70000 ? 213 ARG A CA  1 
ATOM   1489 C C   . ARG A 1 213 ? 27.66100  -1.13800  29.73600 1.000 26.70000 ? 213 ARG A C   1 
ATOM   1490 O O   . ARG A 1 213 ? 27.11800  -0.03000  29.80100 1.000 26.70000 ? 213 ARG A O   1 
ATOM   1491 C CB  . ARG A 1 213 ? 27.42700  -2.58600  31.77500 1.000 26.70000 ? 213 ARG A CB  1 
ATOM   1492 C CG  . ARG A 1 213 ? 26.63200  -3.67400  32.47500 1.000 26.70000 ? 213 ARG A CG  1 
ATOM   1493 C CD  . ARG A 1 213 ? 26.69100  -3.54500  33.98300 1.000 26.70000 ? 213 ARG A CD  1 
ATOM   1494 N NE  . ARG A 1 213 ? 27.93300  -4.06700  34.54100 1.000 26.70000 ? 213 ARG A NE  1 
ATOM   1495 C CZ  . ARG A 1 213 ? 28.08400  -5.30300  34.99700 1.000 26.70000 ? 213 ARG A CZ  1 
ATOM   1496 N NH1 . ARG A 1 213 ? 27.09000  -6.17500  34.97100 1.000 26.70000 ? 213 ARG A NH1 1 
ATOM   1497 N NH2 . ARG A 1 213 ? 29.26100  -5.67100  35.49300 1.000 26.70000 ? 213 ARG A NH2 1 
ATOM   1498 N N   . LYS A 1 214 ? 28.82900  -1.31700  29.11400 1.000 26.19000 ? 214 LYS A N   1 
ATOM   1499 C CA  . LYS A 1 214 ? 29.47500  -0.17500  28.47400 1.000 26.19000 ? 214 LYS A CA  1 
ATOM   1500 C C   . LYS A 1 214 ? 28.69400  0.28300   27.24900 1.000 26.19000 ? 214 LYS A C   1 
ATOM   1501 O O   . LYS A 1 214 ? 28.50500  1.48900   27.03900 1.000 26.19000 ? 214 LYS A O   1 
ATOM   1502 C CB  . LYS A 1 214 ? 30.91700  -0.51400  28.09400 1.000 26.19000 ? 214 LYS A CB  1 
ATOM   1503 C CG  . LYS A 1 214 ? 31.69500  0.69000   27.58100 1.000 26.19000 ? 214 LYS A CG  1 
ATOM   1504 C CD  . LYS A 1 214 ? 33.07600  0.31400   27.07500 1.000 26.19000 ? 214 LYS A CD  1 
ATOM   1505 C CE  . LYS A 1 214 ? 33.81900  1.54300   26.56800 1.000 26.19000 ? 214 LYS A CE  1 
ATOM   1506 N NZ  . LYS A 1 214 ? 35.13800  1.20000   25.96800 1.000 26.19000 ? 214 LYS A NZ  1 
ATOM   1507 N N   . LEU A 1 215 ? 28.22000  -0.66500  26.43400 1.000 25.78000 ? 215 LEU A N   1 
ATOM   1508 C CA  . LEU A 1 215 ? 27.41200  -0.28600  25.28000 1.000 25.78000 ? 215 LEU A CA  1 
ATOM   1509 C C   . LEU A 1 215 ? 26.09400  0.35300   25.70000 1.000 25.78000 ? 215 LEU A C   1 
ATOM   1510 O O   . LEU A 1 215 ? 25.59400  1.24500   25.00800 1.000 25.78000 ? 215 LEU A O   1 
ATOM   1511 C CB  . LEU A 1 215 ? 27.15600  -1.49700  24.38300 1.000 25.78000 ? 215 LEU A CB  1 
ATOM   1512 C CG  . LEU A 1 215 ? 28.37800  -2.04200  23.63800 1.000 25.78000 ? 215 LEU A CG  1 
ATOM   1513 C CD1 . LEU A 1 215 ? 27.96100  -2.95900  22.49500 1.000 25.78000 ? 215 LEU A CD1 1 
ATOM   1514 C CD2 . LEU A 1 215 ? 29.25200  -0.90400  23.13200 1.000 25.78000 ? 215 LEU A CD2 1 
ATOM   1515 N N   . TYR A 1 216 ? 25.51500  -0.08700  26.82200 1.000 23.85000 ? 216 TYR A N   1 
ATOM   1516 C CA  . TYR A 1 216 ? 24.33900  0.59500   27.35100 1.000 23.85000 ? 216 TYR A CA  1 
ATOM   1517 C C   . TYR A 1 216 ? 24.67900  1.99100   27.85700 1.000 23.85000 ? 216 TYR A C   1 
ATOM   1518 O O   . TYR A 1 216 ? 23.85700  2.90600   27.74600 1.000 23.85000 ? 216 TYR A O   1 
ATOM   1519 C CB  . TYR A 1 216 ? 23.70500  -0.23500  28.46700 1.000 23.85000 ? 216 TYR A CB  1 
ATOM   1520 C CG  . TYR A 1 216 ? 23.03400  -1.50800  27.99600 1.000 23.85000 ? 216 TYR A CG  1 
ATOM   1521 C CD1 . TYR A 1 216 ? 22.35500  -1.55200  26.78500 1.000 23.85000 ? 216 TYR A CD1 1 
ATOM   1522 C CD2 . TYR A 1 216 ? 23.07900  -2.66500  28.76400 1.000 23.85000 ? 216 TYR A CD2 1 
ATOM   1523 C CE1 . TYR A 1 216 ? 21.74000  -2.71400  26.35200 1.000 23.85000 ? 216 TYR A CE1 1 
ATOM   1524 C CE2 . TYR A 1 216 ? 22.46900  -3.83200  28.33900 1.000 23.85000 ? 216 TYR A CE2 1 
ATOM   1525 C CZ  . TYR A 1 216 ? 21.80100  -3.85200  27.13400 1.000 23.85000 ? 216 TYR A CZ  1 
ATOM   1526 O OH  . TYR A 1 216 ? 21.19300  -5.01300  26.71300 1.000 23.85000 ? 216 TYR A OH  1 
ATOM   1527 N N   . SER A 1 217 ? 25.87800  2.17500   28.41500 1.000 22.68000 ? 217 SER A N   1 
ATOM   1528 C CA  . SER A 1 217 ? 26.29500  3.50600   28.84000 1.000 22.68000 ? 217 SER A CA  1 
ATOM   1529 C C   . SER A 1 217 ? 26.48800  4.44100   27.65500 1.000 22.68000 ? 217 SER A C   1 
ATOM   1530 O O   . SER A 1 217 ? 26.26300  5.65100   27.77800 1.000 22.68000 ? 217 SER A O   1 
ATOM   1531 C CB  . SER A 1 217 ? 27.58200  3.41300   29.65800 1.000 22.68000 ? 217 SER A CB  1 
ATOM   1532 O OG  . SER A 1 217 ? 27.36800  2.71000   30.86900 1.000 22.68000 ? 217 SER A OG  1 
ATOM   1533 N N   . GLN A 1 218 ? 26.91100  3.90800   26.50900 1.000 24.93000 ? 218 GLN A N   1 
ATOM   1534 C CA  . GLN A 1 218 ? 27.13000  4.72700   25.32400 1.000 24.93000 ? 218 GLN A CA  1 
ATOM   1535 C C   . GLN A 1 218 ? 25.91500  4.82500   24.40700 1.000 24.93000 ? 218 GLN A C   1 
ATOM   1536 O O   . GLN A 1 218 ? 25.92400  5.65000   23.48700 1.000 24.93000 ? 218 GLN A O   1 
ATOM   1537 C CB  . GLN A 1 218 ? 28.32300  4.19000   24.53000 1.000 24.93000 ? 218 GLN A CB  1 
ATOM   1538 C CG  . GLN A 1 218 ? 29.65400  4.39400   25.22700 1.000 24.93000 ? 218 GLN A CG  1 
ATOM   1539 C CD  . GLN A 1 218 ? 30.76200  3.56900   24.61100 1.000 24.93000 ? 218 GLN A CD  1 
ATOM   1540 O OE1 . GLN A 1 218 ? 30.50500  2.61700   23.87400 1.000 24.93000 ? 218 GLN A OE1 1 
ATOM   1541 N NE2 . GLN A 1 218 ? 32.00500  3.92900   24.91000 1.000 24.93000 ? 218 GLN A NE2 1 
ATOM   1542 N N   . ASN A 1 219 ? 24.87600  4.02100   24.62800 1.000 22.58000 ? 219 ASN A N   1 
ATOM   1543 C CA  . ASN A 1 219 ? 23.69900  4.00300   23.76600 1.000 22.58000 ? 219 ASN A CA  1 
ATOM   1544 C C   . ASN A 1 219 ? 22.45600  4.24900   24.60700 1.000 22.58000 ? 219 ASN A C   1 
ATOM   1545 O O   . ASN A 1 219 ? 22.18400  3.50100   25.55100 1.000 22.58000 ? 219 ASN A O   1 
ATOM   1546 C CB  . ASN A 1 219 ? 23.57600  2.67200   23.02000 1.000 22.58000 ? 219 ASN A CB  1 
ATOM   1547 C CG  . ASN A 1 219 ? 24.58000  2.53800   21.89500 1.000 22.58000 ? 219 ASN A CG  1 
ATOM   1548 O OD1 . ASN A 1 219 ? 24.25600  2.76100   20.72800 1.000 22.58000 ? 219 ASN A OD1 1 
ATOM   1549 N ND2 . ASN A 1 219 ? 25.80900  2.17500   22.23900 1.000 22.58000 ? 219 ASN A ND2 1 
ATOM   1550 N N   . TRP A 1 220 ? 21.70000  5.29100   24.25400 1.000 21.15000 ? 220 TRP A N   1 
ATOM   1551 C CA  . TRP A 1 220 ? 20.44400  5.56000   24.94500 1.000 21.15000 ? 220 TRP A CA  1 
ATOM   1552 C C   . TRP A 1 220 ? 19.43100  4.44500   24.72900 1.000 21.15000 ? 220 TRP A C   1 
ATOM   1553 O O   . TRP A 1 220 ? 18.59800  4.18300   25.60500 1.000 21.15000 ? 220 TRP A O   1 
ATOM   1554 C CB  . TRP A 1 220 ? 19.85400  6.88600   24.47000 1.000 21.15000 ? 220 TRP A CB  1 
ATOM   1555 C CG  . TRP A 1 220 ? 20.33200  8.08900   25.21400 1.000 21.15000 ? 220 TRP A CG  1 
ATOM   1556 C CD1 . TRP A 1 220 ? 21.16700  9.06300   24.75100 1.000 21.15000 ? 220 TRP A CD1 1 
ATOM   1557 C CD2 . TRP A 1 220 ? 19.99100  8.45600   26.55500 1.000 21.15000 ? 220 TRP A CD2 1 
ATOM   1558 N NE1 . TRP A 1 220 ? 21.37200  10.01200  25.72300 1.000 21.15000 ? 220 TRP A NE1 1 
ATOM   1559 C CE2 . TRP A 1 220 ? 20.66100  9.66200   26.84100 1.000 21.15000 ? 220 TRP A CE2 1 
ATOM   1560 C CE3 . TRP A 1 220 ? 19.18800  7.87900   27.54400 1.000 21.15000 ? 220 TRP A CE3 1 
ATOM   1561 C CZ2 . TRP A 1 220 ? 20.55100  10.30200  28.07400 1.000 21.15000 ? 220 TRP A CZ2 1 
ATOM   1562 C CZ3 . TRP A 1 220 ? 19.08200  8.51500   28.76600 1.000 21.15000 ? 220 TRP A CZ3 1 
ATOM   1563 C CH2 . TRP A 1 220 ? 19.76000  9.71300   29.02100 1.000 21.15000 ? 220 TRP A CH2 1 
ATOM   1564 N N   . LEU A 1 221 ? 19.49200  3.76900   23.58600 1.000 18.94000 ? 221 LEU A N   1 
ATOM   1565 C CA  . LEU A 1 221 ? 18.46300  2.81600   23.20500 1.000 18.94000 ? 221 LEU A CA  1 
ATOM   1566 C C   . LEU A 1 221 ? 19.10800  1.63700   22.49400 1.000 18.94000 ? 221 LEU A C   1 
ATOM   1567 O O   . LEU A 1 221 ? 20.06700  1.80600   21.73500 1.000 18.94000 ? 221 LEU A O   1 
ATOM   1568 C CB  . LEU A 1 221 ? 17.41700  3.48900   22.30400 1.000 18.94000 ? 221 LEU A CB  1 
ATOM   1569 C CG  . LEU A 1 221 ? 15.96500  3.01200   22.32300 1.000 18.94000 ? 221 LEU A CG  1 
ATOM   1570 C CD1 . LEU A 1 221 ? 15.07000  4.06600   21.69300 1.000 18.94000 ? 221 LEU A CD1 1 
ATOM   1571 C CD2 . LEU A 1 221 ? 15.81900  1.70000   21.58600 1.000 18.94000 ? 221 LEU A CD2 1 
ATOM   1572 N N   . ARG A 1 222 ? 18.57200  0.44600   22.74700 1.000 21.92000 ? 222 ARG A N   1 
ATOM   1573 C CA  . ARG A 1 222 ? 19.03200  -0.78500  22.11800 1.000 21.92000 ? 222 ARG A CA  1 
ATOM   1574 C C   . ARG A 1 222 ? 17.81400  -1.56900  21.65300 1.000 21.92000 ? 222 ARG A C   1 
ATOM   1575 O O   . ARG A 1 222 ? 16.81900  -1.65900  22.37600 1.000 21.92000 ? 222 ARG A O   1 
ATOM   1576 C CB  . ARG A 1 222 ? 19.87800  -1.61600  23.09400 1.000 21.92000 ? 222 ARG A CB  1 
ATOM   1577 C CG  . ARG A 1 222 ? 20.15600  -3.03800  22.65300 1.000 21.92000 ? 222 ARG A CG  1 
ATOM   1578 C CD  . ARG A 1 222 ? 20.92000  -3.08000  21.34500 1.000 21.92000 ? 222 ARG A CD  1 
ATOM   1579 N NE  . ARG A 1 222 ? 21.30600  -4.44200  20.99600 1.000 21.92000 ? 222 ARG A NE  1 
ATOM   1580 C CZ  . ARG A 1 222 ? 21.79000  -4.80300  19.81600 1.000 21.92000 ? 222 ARG A CZ  1 
ATOM   1581 N NH1 . ARG A 1 222 ? 21.94300  -3.92800  18.83500 1.000 21.92000 ? 222 ARG A NH1 1 
ATOM   1582 N NH2 . ARG A 1 222 ? 22.12800  -6.07300  19.61500 1.000 21.92000 ? 222 ARG A NH2 1 
ATOM   1583 N N   . LEU A 1 223 ? 17.89400  -2.14100  20.45200 1.000 23.49000 ? 223 LEU A N   1 
ATOM   1584 C CA  . LEU A 1 223 ? 16.71300  -2.70700  19.81200 1.000 23.49000 ? 223 LEU A CA  1 
ATOM   1585 C C   . LEU A 1 223 ? 17.01700  -4.05100  19.17100 1.000 23.49000 ? 223 LEU A C   1 
ATOM   1586 O O   . LEU A 1 223 ? 18.02800  -4.20600  18.47900 1.000 23.49000 ? 223 LEU A O   1 
ATOM   1587 C CB  . LEU A 1 223 ? 16.15800  -1.74300  18.75900 1.000 23.49000 ? 223 LEU A CB  1 
ATOM   1588 C CG  . LEU A 1 223 ? 14.96900  -0.92700  19.25700 1.000 23.49000 ? 223 LEU A CG  1 
ATOM   1589 C CD1 . LEU A 1 223 ? 14.63100  0.18000   18.28500 1.000 23.49000 ? 223 LEU A CD1 1 
ATOM   1590 C CD2 . LEU A 1 223 ? 13.78300  -1.84700  19.46300 1.000 23.49000 ? 223 LEU A CD2 1 
ATOM   1591 N N   . ILE A 1 224 ? 16.12600  -5.01100  19.40200 1.000 24.23000 ? 224 ILE A N   1 
ATOM   1592 C CA  . ILE A 1 224 ? 16.15000  -6.34200  18.80300 1.000 24.23000 ? 224 ILE A CA  1 
ATOM   1593 C C   . ILE A 1 224 ? 14.74600  -6.60300  18.26600 1.000 24.23000 ? 224 ILE A C   1 
ATOM   1594 O O   . ILE A 1 224 ? 13.91300  -7.17400  18.98600 1.000 24.23000 ? 224 ILE A O   1 
ATOM   1595 C CB  . ILE A 1 224 ? 16.58000  -7.41500  19.81600 1.000 24.23000 ? 224 ILE A CB  1 
ATOM   1596 C CG1 . ILE A 1 224 ? 17.87200  -7.00200  20.52000 1.000 24.23000 ? 224 ILE A CG1 1 
ATOM   1597 C CG2 . ILE A 1 224 ? 16.77100  -8.75300  19.12500 1.000 24.23000 ? 224 ILE A CG2 1 
ATOM   1598 C CD1 . ILE A 1 224 ? 18.27900  -7.93900  21.62900 1.000 24.23000 ? 224 ILE A CD1 1 
ATOM   1599 N N   . PRO A 1 225 ? 14.41600  -6.12500  17.06100 1.000 25.35000 ? 225 PRO A N   1 
ATOM   1600 C CA  . PRO A 1 225 ? 13.03000  -6.23900  16.57400 1.000 25.35000 ? 225 PRO A CA  1 
ATOM   1601 C C   . PRO A 1 225 ? 12.51000  -7.66300  16.48900 1.000 25.35000 ? 225 PRO A C   1 
ATOM   1602 O O   . PRO A 1 225 ? 11.30900  -7.88300  16.68400 1.000 25.35000 ? 225 PRO A O   1 
ATOM   1603 C CB  . PRO A 1 225 ? 13.09400  -5.58300  15.18500 1.000 25.35000 ? 225 PRO A CB  1 
ATOM   1604 C CG  . PRO A 1 225 ? 14.29300  -4.69600  15.24000 1.000 25.35000 ? 225 PRO A CG  1 
ATOM   1605 C CD  . PRO A 1 225 ? 15.28100  -5.41900  16.10200 1.000 25.35000 ? 225 PRO A CD  1 
ATOM   1606 N N   . ASP A 1 226 ? 13.36600  -8.63600  16.17900 1.000 28.53000 ? 226 ASP A N   1 
ATOM   1607 C CA  . ASP A 1 226 ? 12.94600  -10.02900 16.07200 1.000 28.53000 ? 226 ASP A CA  1 
ATOM   1608 C C   . ASP A 1 226 ? 14.05700  -10.91500 16.61100 1.000 28.53000 ? 226 ASP A C   1 
ATOM   1609 O O   . ASP A 1 226 ? 15.17000  -10.90800 16.07800 1.000 28.53000 ? 226 ASP A O   1 
ATOM   1610 C CB  . ASP A 1 226 ? 12.61200  -10.39900 14.62500 1.000 28.53000 ? 226 ASP A CB  1 
ATOM   1611 C CG  . ASP A 1 226 ? 11.86900  -11.71700 14.51600 1.000 28.53000 ? 226 ASP A CG  1 
ATOM   1612 O OD1 . ASP A 1 226 ? 11.52100  -12.29500 15.56900 1.000 28.53000 ? 226 ASP A OD1 1 
ATOM   1613 O OD2 . ASP A 1 226 ? 11.62900  -12.17700 13.38000 1.000 28.53000 ? 226 ASP A OD2 1 
ATOM   1614 N N   . ALA A 1 227 ? 13.74900  -11.68000 17.66200 1.000 31.91000 ? 227 ALA A N   1 
ATOM   1615 C CA  . ALA A 1 227 ? 14.74100  -12.55400 18.27700 1.000 31.91000 ? 227 ALA A CA  1 
ATOM   1616 C C   . ALA A 1 227 ? 15.19800  -13.66600 17.34300 1.000 31.91000 ? 227 ALA A C   1 
ATOM   1617 O O   . ALA A 1 227 ? 16.29600  -14.20200 17.52700 1.000 31.91000 ? 227 ALA A O   1 
ATOM   1618 C CB  . ALA A 1 227 ? 14.18200  -13.15600 19.56500 1.000 31.91000 ? 227 ALA A CB  1 
ATOM   1619 N N   . ASP A 1 228 ? 14.38900  -14.01800 16.34800 1.000 32.08000 ? 228 ASP A N   1 
ATOM   1620 C CA  . ASP A 1 228 ? 14.71700  -15.06200 15.38700 1.000 32.08000 ? 228 ASP A CA  1 
ATOM   1621 C C   . ASP A 1 228 ? 15.57400  -14.55200 14.23700 1.000 32.08000 ? 228 ASP A C   1 
ATOM   1622 O O   . ASP A 1 228 ? 15.70300  -15.24900 13.22400 1.000 32.08000 ? 228 ASP A O   1 
ATOM   1623 C CB  . ASP A 1 228 ? 13.43300  -15.68900 14.83700 1.000 32.08000 ? 228 ASP A CB  1 
ATOM   1624 C CG  . ASP A 1 228 ? 12.43500  -16.02500 15.92700 1.000 32.08000 ? 228 ASP A CG  1 
ATOM   1625 O OD1 . ASP A 1 228 ? 12.86700  -16.47400 17.00900 1.000 32.08000 ? 228 ASP A OD1 1 
ATOM   1626 O OD2 . ASP A 1 228 ? 11.22100  -15.83200 15.70300 1.000 32.08000 ? 228 ASP A OD2 1 
ATOM   1627 N N   . TYR A 1 229 ? 16.14300  -13.35500 14.36700 1.000 28.49000 ? 229 TYR A N   1 
ATOM   1628 C CA  . TYR A 1 229 ? 16.82200  -12.71700 13.24800 1.000 28.49000 ? 229 TYR A CA  1 
ATOM   1629 C C   . TYR A 1 229 ? 18.00600  -13.55100 12.76900 1.000 28.49000 ? 229 TYR A C   1 
ATOM   1630 O O   . TYR A 1 229 ? 18.77900  -14.08900 13.56600 1.000 28.49000 ? 229 TYR A O   1 
ATOM   1631 C CB  . TYR A 1 229 ? 17.28300  -11.31100 13.65000 1.000 28.49000 ? 229 TYR A CB  1 
ATOM   1632 C CG  . TYR A 1 229 ? 18.63600  -11.23500 14.33500 1.000 28.49000 ? 229 TYR A CG  1 
ATOM   1633 C CD1 . TYR A 1 229 ? 18.77100  -11.49700 15.69200 1.000 28.49000 ? 229 TYR A CD1 1 
ATOM   1634 C CD2 . TYR A 1 229 ? 19.77500  -10.87900 13.62400 1.000 28.49000 ? 229 TYR A CD2 1 
ATOM   1635 C CE1 . TYR A 1 229 ? 20.00700  -11.41900 16.31500 1.000 28.49000 ? 229 TYR A CE1 1 
ATOM   1636 C CE2 . TYR A 1 229 ? 21.01000  -10.79800 14.23800 1.000 28.49000 ? 229 TYR A CE2 1 
ATOM   1637 C CZ  . TYR A 1 229 ? 21.12100  -11.06900 15.58100 1.000 28.49000 ? 229 TYR A CZ  1 
ATOM   1638 O OH  . TYR A 1 229 ? 22.35300  -10.98700 16.18700 1.000 28.49000 ? 229 TYR A OH  1 
ATOM   1639 N N   . GLN A 1 230 ? 18.12900  -13.66400 11.44800 1.000 31.74000 ? 230 GLN A N   1 
ATOM   1640 C CA  . GLN A 1 230 ? 19.27500  -14.30300 10.80800 1.000 31.74000 ? 230 GLN A CA  1 
ATOM   1641 C C   . GLN A 1 230 ? 20.28100  -13.21300 10.46000 1.000 31.74000 ? 230 GLN A C   1 
ATOM   1642 O O   . GLN A 1 230 ? 20.04500  -12.40900 9.55200  1.000 31.74000 ? 230 GLN A O   1 
ATOM   1643 C CB  . GLN A 1 230 ? 18.83800  -15.07700 9.56700  1.000 31.74000 ? 230 GLN A CB  1 
ATOM   1644 C CG  . GLN A 1 230 ? 19.98200  -15.59700 8.70400  1.000 31.74000 ? 230 GLN A CG  1 
ATOM   1645 C CD  . GLN A 1 230 ? 20.71900  -16.76600 9.33500  1.000 31.74000 ? 230 GLN A CD  1 
ATOM   1646 O OE1 . GLN A 1 230 ? 20.26500  -17.34200 10.32400 1.000 31.74000 ? 230 GLN A OE1 1 
ATOM   1647 N NE2 . GLN A 1 230 ? 21.86300  -17.12200 8.76100  1.000 31.74000 ? 230 GLN A NE2 1 
ATOM   1648 N N   . ALA A 1 231 ? 21.39600  -13.18000 11.18600 1.000 28.20000 ? 231 ALA A N   1 
ATOM   1649 C CA  . ALA A 1 231 ? 22.35100  -12.09100 11.03600 1.000 28.20000 ? 231 ALA A CA  1 
ATOM   1650 C C   . ALA A 1 231 ? 22.94100  -12.06200 9.63200  1.000 28.20000 ? 231 ALA A C   1 
ATOM   1651 O O   . ALA A 1 231 ? 23.31700  -13.09700 9.07300  1.000 28.20000 ? 231 ALA A O   1 
ATOM   1652 C CB  . ALA A 1 231 ? 23.46900  -12.22500 12.07100 1.000 28.20000 ? 231 ALA A CB  1 
ATOM   1653 N N   . ALA A 1 232 ? 23.02200  -10.86100 9.06500  1.000 27.44000 ? 232 ALA A N   1 
ATOM   1654 C CA  . ALA A 1 232 ? 23.67200  -10.62900 7.78300  1.000 27.44000 ? 232 ALA A CA  1 
ATOM   1655 C C   . ALA A 1 232 ? 25.08000  -10.10200 8.02700  1.000 27.44000 ? 232 ALA A C   1 
ATOM   1656 O O   . ALA A 1 232 ? 25.26100  -9.11400  8.74700  1.000 27.44000 ? 232 ALA A O   1 
ATOM   1657 C CB  . ALA A 1 232 ? 22.87200  -9.63900  6.93600  1.000 27.44000 ? 232 ALA A CB  1 
ATOM   1658 N N   . ALA A 1 233 ? 26.06800  -10.75800 7.42700  1.000 26.00000 ? 233 ALA A N   1 
ATOM   1659 C CA  . ALA A 1 233 ? 27.45700  -10.40200 7.67300  1.000 26.00000 ? 233 ALA A CA  1 
ATOM   1660 C C   . ALA A 1 233 ? 27.82200  -9.08800  6.99200  1.000 26.00000 ? 233 ALA A C   1 
ATOM   1661 O O   . ALA A 1 233 ? 27.27900  -8.73100  5.94300  1.000 26.00000 ? 233 ALA A O   1 
ATOM   1662 C CB  . ALA A 1 233 ? 28.38600  -11.51300 7.18900  1.000 26.00000 ? 233 ALA A CB  1 
ATOM   1663 N N   . ILE A 1 234 ? 28.75400  -8.36500  7.60600  1.000 25.26000 ? 234 ILE A N   1 
ATOM   1664 C CA  . ILE A 1 234 ? 29.34600  -7.17500  7.00400  1.000 25.26000 ? 234 ILE A CA  1 
ATOM   1665 C C   . ILE A 1 234 ? 30.52500  -7.63300  6.15300  1.000 25.26000 ? 234 ILE A C   1 
ATOM   1666 O O   . ILE A 1 234 ? 31.53800  -8.09900  6.68000  1.000 25.26000 ? 234 ILE A O   1 
ATOM   1667 C CB  . ILE A 1 234 ? 29.78600  -6.16100  8.06500  1.000 25.26000 ? 234 ILE A CB  1 
ATOM   1668 C CG1 . ILE A 1 234 ? 28.58200  -5.69700  8.88700  1.000 25.26000 ? 234 ILE A CG1 1 
ATOM   1669 C CG2 . ILE A 1 234 ? 30.48700  -4.97800  7.41000  1.000 25.26000 ? 234 ILE A CG2 1 
ATOM   1670 C CD1 . ILE A 1 234 ? 28.92900  -4.69300  9.96200  1.000 25.26000 ? 234 ILE A CD1 1 
ATOM   1671 N N   . VAL A 1 235 ? 30.38700  -7.51500  4.84100  1.000 24.63000 ? 235 VAL A N   1 
ATOM   1672 C CA  . VAL A 1 235 ? 31.39100  -7.96200  3.88000  1.000 24.63000 ? 235 VAL A CA  1 
ATOM   1673 C C   . VAL A 1 235 ? 32.01300  -6.72900  3.23100  1.000 24.63000 ? 235 VAL A C   1 
ATOM   1674 O O   . VAL A 1 235 ? 31.28200  -5.89000  2.68600  1.000 24.63000 ? 235 VAL A O   1 
ATOM   1675 C CB  . VAL A 1 235 ? 30.78900  -8.90400  2.82400  1.000 24.63000 ? 235 VAL A CB  1 
ATOM   1676 C CG1 . VAL A 1 235 ? 29.49400  -8.33100  2.25400  1.000 24.63000 ? 235 VAL A CG1 1 
ATOM   1677 C CG2 . VAL A 1 235 ? 31.79900  -9.17100  1.71800  1.000 24.63000 ? 235 VAL A CG2 1 
ATOM   1678 N N   . PRO A 1 236 ? 33.34200  -6.55400  3.28500  1.000 25.80000 ? 236 PRO A N   1 
ATOM   1679 C CA  . PRO A 1 236 ? 34.35300  -7.34700  4.00500  1.000 25.80000 ? 236 PRO A CA  1 
ATOM   1680 C C   . PRO A 1 236 ? 34.24600  -7.20300  5.51800  1.000 25.80000 ? 236 PRO A C   1 
ATOM   1681 O O   . PRO A 1 236 ? 33.77200  -6.18500  6.01300  1.000 25.80000 ? 236 PRO A O   1 
ATOM   1682 C CB  . PRO A 1 236 ? 35.67600  -6.78500  3.46600  1.000 25.80000 ? 236 PRO A CB  1 
ATOM   1683 C CG  . PRO A 1 236 ? 35.35600  -5.37000  3.11800  1.000 25.80000 ? 236 PRO A CG  1 
ATOM   1684 C CD  . PRO A 1 236 ? 33.95600  -5.42300  2.56700  1.000 25.80000 ? 236 PRO A CD  1 
ATOM   1685 N N   . THR A 1 237 ? 34.67800  -8.21600  6.27500  1.000 26.26000 ? 237 THR A N   1 
ATOM   1686 C CA  . THR A 1 237 ? 34.60500  -8.13600  7.73000  1.000 26.26000 ? 237 THR A CA  1 
ATOM   1687 C C   . THR A 1 237 ? 35.46000  -6.99900  8.27700  1.000 26.26000 ? 237 THR A C   1 
ATOM   1688 O O   . THR A 1 237 ? 35.10200  -6.38500  9.28900  1.000 26.26000 ? 237 THR A O   1 
ATOM   1689 C CB  . THR A 1 237 ? 35.03900  -9.46700  8.34600  1.000 26.26000 ? 237 THR A CB  1 
ATOM   1690 O OG1 . THR A 1 237 ? 34.21400  -10.52100 7.83400  1.000 26.26000 ? 237 THR A OG1 1 
ATOM   1691 C CG2 . THR A 1 237 ? 34.91400  -9.42700  9.86100  1.000 26.26000 ? 237 THR A CG2 1 
ATOM   1692 N N   . ASN A 1 238 ? 36.57200  -6.69200  7.62000  1.000 29.30000 ? 238 ASN A N   1 
ATOM   1693 C CA  . ASN A 1 238 ? 37.45700  -5.61500  8.03100  1.000 29.30000 ? 238 ASN A CA  1 
ATOM   1694 C C   . ASN A 1 238 ? 37.40700  -4.47500  7.02200  1.000 29.30000 ? 238 ASN A C   1 
ATOM   1695 O O   . ASN A 1 238 ? 37.06700  -4.66500  5.85200  1.000 29.30000 ? 238 ASN A O   1 
ATOM   1696 C CB  . ASN A 1 238 ? 38.89400  -6.12000  8.18800  1.000 29.30000 ? 238 ASN A CB  1 
ATOM   1697 C CG  . ASN A 1 238 ? 39.03500  -7.12000  9.31500  1.000 29.30000 ? 238 ASN A CG  1 
ATOM   1698 O OD1 . ASN A 1 238 ? 38.76200  -8.30800  9.14300  1.000 29.30000 ? 238 ASN A OD1 1 
ATOM   1699 N ND2 . ASN A 1 238 ? 39.45600  -6.64200  10.48000 1.000 29.30000 ? 238 ASN A ND2 1 
ATOM   1700 N N   . ASN A 1 239 ? 37.74800  -3.28100  7.49500  1.000 32.35000 ? 239 ASN A N   1 
ATOM   1701 C CA  . ASN A 1 239 ? 37.75300  -2.11000  6.62300  1.000 32.35000 ? 239 ASN A CA  1 
ATOM   1702 C C   . ASN A 1 239 ? 38.82200  -2.27700  5.54800  1.000 32.35000 ? 239 ASN A C   1 
ATOM   1703 O O   . ASN A 1 239 ? 39.96900  -2.60300  5.86700  1.000 32.35000 ? 239 ASN A O   1 
ATOM   1704 C CB  . ASN A 1 239 ? 38.00400  -0.84200  7.43400  1.000 32.35000 ? 239 ASN A CB  1 
ATOM   1705 C CG  . ASN A 1 239 ? 37.87700  0.41700   6.59800  1.000 32.35000 ? 239 ASN A CG  1 
ATOM   1706 O OD1 . ASN A 1 239 ? 38.87500  1.01900   6.20000  1.000 32.35000 ? 239 ASN A OD1 1 
ATOM   1707 N ND2 . ASN A 1 239 ? 36.64300  0.81800   6.32200  1.000 32.35000 ? 239 ASN A ND2 1 
ATOM   1708 N N   . PRO A 1 240 ? 38.48400  -2.08000  4.27000  1.000 31.48000 ? 240 PRO A N   1 
ATOM   1709 C CA  . PRO A 1 240 ? 39.47400  -2.32200  3.20600  1.000 31.48000 ? 240 PRO A CA  1 
ATOM   1710 C C   . PRO A 1 240 ? 40.73600  -1.48700  3.32900  1.000 31.48000 ? 240 PRO A C   1 
ATOM   1711 O O   . PRO A 1 240 ? 41.81700  -1.96500  2.96500  1.000 31.48000 ? 240 PRO A O   1 
ATOM   1712 C CB  . PRO A 1 240 ? 38.69800  -1.98000  1.92700  1.000 31.48000 ? 240 PRO A CB  1 
ATOM   1713 C CG  . PRO A 1 240 ? 37.26000  -2.14400  2.29700  1.000 31.48000 ? 240 PRO A CG  1 
ATOM   1714 C CD  . PRO A 1 240 ? 37.16600  -1.71100  3.72800  1.000 31.48000 ? 240 PRO A CD  1 
ATOM   1715 N N   . LEU A 1 241 ? 40.64000  -0.25800  3.84000  1.000 35.22000 ? 241 LEU A N   1 
ATOM   1716 C CA  . LEU A 1 241 ? 41.81400  0.60100   3.93900  1.000 35.22000 ? 241 LEU A CA  1 
ATOM   1717 C C   . LEU A 1 241 ? 42.61200  0.35800   5.21700  1.000 35.22000 ? 241 LEU A C   1 
ATOM   1718 O O   . LEU A 1 241 ? 43.84100  0.24600   5.17100  1.000 35.22000 ? 241 LEU A O   1 
ATOM   1719 C CB  . LEU A 1 241 ? 41.39800  2.07400   3.86300  1.000 35.22000 ? 241 LEU A CB  1 
ATOM   1720 C CG  . LEU A 1 241 ? 40.58200  2.52400   2.65100  1.000 35.22000 ? 241 LEU A CG  1 
ATOM   1721 C CD1 . LEU A 1 241 ? 40.49500  4.03900   2.62000  1.000 35.22000 ? 241 LEU A CD1 1 
ATOM   1722 C CD2 . LEU A 1 241 ? 41.17200  1.98800   1.35500  1.000 35.22000 ? 241 LEU A CD2 1 
ATOM   1723 N N   . THR A 1 242 ? 41.93100  0.26900   6.36000  1.000 34.35000 ? 242 THR A N   1 
ATOM   1724 C CA  . THR A 1 242 ? 42.60000  0.21400   7.65300  1.000 34.35000 ? 242 THR A CA  1 
ATOM   1725 C C   . THR A 1 242 ? 42.76800  -1.19800  8.19700  1.000 34.35000 ? 242 THR A C   1 
ATOM   1726 O O   . THR A 1 242 ? 43.52200  -1.38100  9.16100  1.000 34.35000 ? 242 THR A O   1 
ATOM   1727 C CB  . THR A 1 242 ? 41.83600  1.05700   8.68300  1.000 34.35000 ? 242 THR A CB  1 
ATOM   1728 O OG1 . THR A 1 242 ? 40.58300  0.43100   8.98600  1.000 34.35000 ? 242 THR A OG1 1 
ATOM   1729 C CG2 . THR A 1 242 ? 41.57700  2.45500   8.14100  1.000 34.35000 ? 242 THR A CG2 1 
ATOM   1730 N N   . ASP A 1 243 ? 42.08300  -2.18900  7.62300  1.000 34.38000 ? 243 ASP A N   1 
ATOM   1731 C CA  . ASP A 1 243 ? 42.05300  -3.57900  8.07400  1.000 34.38000 ? 243 ASP A CA  1 
ATOM   1732 C C   . ASP A 1 243 ? 41.40400  -3.73100  9.44900  1.000 34.38000 ? 243 ASP A C   1 
ATOM   1733 O O   . ASP A 1 243 ? 41.25400  -4.86100  9.92800  1.000 34.38000 ? 243 ASP A O   1 
ATOM   1734 C CB  . ASP A 1 243 ? 43.45500  -4.21300  8.09100  1.000 34.38000 ? 243 ASP A CB  1 
ATOM   1735 C CG  . ASP A 1 243 ? 43.42100  -5.71900  8.27800  1.000 34.38000 ? 243 ASP A CG  1 
ATOM   1736 O OD1 . ASP A 1 243 ? 42.62100  -6.39000  7.59100  1.000 34.38000 ? 243 ASP A OD1 1 
ATOM   1737 O OD2 . ASP A 1 243 ? 44.20600  -6.23200  9.10300  1.000 34.38000 ? 243 ASP A OD2 1 
ATOM   1738 N N   . GLU A 1 244 ? 41.00100  -2.64000  10.09200 1.000 33.31000 ? 244 GLU A N   1 
ATOM   1739 C CA  . GLU A 1 244 ? 40.36000  -2.74100  11.39300 1.000 33.31000 ? 244 GLU A CA  1 
ATOM   1740 C C   . GLU A 1 244 ? 38.93900  -3.28600  11.24700 1.000 33.31000 ? 244 GLU A C   1 
ATOM   1741 O O   . GLU A 1 244 ? 38.26400  -3.00900  10.25100 1.000 33.31000 ? 244 GLU A O   1 
ATOM   1742 C CB  . GLU A 1 244 ? 40.31800  -1.37600  12.08000 1.000 33.31000 ? 244 GLU A CB  1 
ATOM   1743 C CG  . GLU A 1 244 ? 41.67700  -0.79400  12.42600 1.000 33.31000 ? 244 GLU A CG  1 
ATOM   1744 C CD  . GLU A 1 244 ? 41.57600  0.62800   12.94900 1.000 33.31000 ? 244 GLU A CD  1 
ATOM   1745 O OE1 . GLU A 1 244 ? 40.65200  1.35400   12.52300 1.000 33.31000 ? 244 GLU A OE1 1 
ATOM   1746 O OE2 . GLU A 1 244 ? 42.41400  1.01900   13.79000 1.000 33.31000 ? 244 GLU A OE2 1 
ATOM   1747 N N   . PRO A 1 245 ? 38.46600  -4.08400  12.20300 1.000 28.42000 ? 245 PRO A N   1 
ATOM   1748 C CA  . PRO A 1 245 ? 37.04200  -4.43100  12.22300 1.000 28.42000 ? 245 PRO A CA  1 
ATOM   1749 C C   . PRO A 1 245 ? 36.18900  -3.18800  12.42800 1.000 28.42000 ? 245 PRO A C   1 
ATOM   1750 O O   . PRO A 1 245 ? 36.58200  -2.24600  13.12300 1.000 28.42000 ? 245 PRO A O   1 
ATOM   1751 C CB  . PRO A 1 245 ? 36.92200  -5.40100  13.40300 1.000 28.42000 ? 245 PRO A CB  1 
ATOM   1752 C CG  . PRO A 1 245 ? 38.30900  -5.90900  13.63300 1.000 28.42000 ? 245 PRO A CG  1 
ATOM   1753 C CD  . PRO A 1 245 ? 39.21700  -4.77000  13.26600 1.000 28.42000 ? 245 PRO A CD  1 
ATOM   1754 N N   . LEU A 1 246 ? 35.01100  -3.18900  11.81100 1.000 25.12000 ? 246 LEU A N   1 
ATOM   1755 C CA  . LEU A 1 246 ? 34.10800  -2.04900  11.91800 1.000 25.12000 ? 246 LEU A CA  1 
ATOM   1756 C C   . LEU A 1 246 ? 33.54900  -1.95900  13.33300 1.000 25.12000 ? 246 LEU A C   1 
ATOM   1757 O O   . LEU A 1 246 ? 32.92100  -2.90600  13.82000 1.000 25.12000 ? 246 LEU A O   1 
ATOM   1758 C CB  . LEU A 1 246 ? 32.97600  -2.17800  10.90300 1.000 25.12000 ? 246 LEU A CB  1 
ATOM   1759 C CG  . LEU A 1 246 ? 32.00500  -1.00300  10.78200 1.000 25.12000 ? 246 LEU A CG  1 
ATOM   1760 C CD1 . LEU A 1 246 ? 32.71100  0.21700   10.21100 1.000 25.12000 ? 246 LEU A CD1 1 
ATOM   1761 C CD2 . LEU A 1 246 ? 30.81900  -1.39200  9.92100  1.000 25.12000 ? 246 LEU A CD2 1 
ATOM   1762 N N   . ASP A 1 247 ? 33.75600  -0.81500  13.98400 1.000 25.08000 ? 247 ASP A N   1 
ATOM   1763 C CA  . ASP A 1 247 ? 33.23700  -0.60200  15.32900 1.000 25.08000 ? 247 ASP A CA  1 
ATOM   1764 C C   . ASP A 1 247 ? 31.74800  -0.29700  15.24300 1.000 25.08000 ? 247 ASP A C   1 
ATOM   1765 O O   . ASP A 1 247 ? 31.34200  0.67400   14.59600 1.000 25.08000 ? 247 ASP A O   1 
ATOM   1766 C CB  . ASP A 1 247 ? 33.98700  0.53300   16.02300 1.000 25.08000 ? 247 ASP A CB  1 
ATOM   1767 C CG  . ASP A 1 247 ? 33.61100  0.67700   17.48300 1.000 25.08000 ? 247 ASP A CG  1 
ATOM   1768 O OD1 . ASP A 1 247 ? 32.85300  -0.17500  17.99500 1.000 25.08000 ? 247 ASP A OD1 1 
ATOM   1769 O OD2 . ASP A 1 247 ? 34.07500  1.64400   18.12100 1.000 25.08000 ? 247 ASP A OD2 1 
ATOM   1770 N N   . LEU A 1 248 ? 30.93800  -1.11600  15.91100 1.000 24.22000 ? 248 LEU A N   1 
ATOM   1771 C CA  . LEU A 1 248 ? 29.48700  -1.05200  15.80200 1.000 24.22000 ? 248 LEU A CA  1 
ATOM   1772 C C   . LEU A 1 248 ? 28.82700  -0.67600  17.12300 1.000 24.22000 ? 248 LEU A C   1 
ATOM   1773 O O   . LEU A 1 248 ? 27.65500  -0.99600  17.34200 1.000 24.22000 ? 248 LEU A O   1 
ATOM   1774 C CB  . LEU A 1 248 ? 28.95000  -2.38700  15.28200 1.000 24.22000 ? 248 LEU A CB  1 
ATOM   1775 C CG  . LEU A 1 248 ? 29.45800  -2.75700  13.88500 1.000 24.22000 ? 248 LEU A CG  1 
ATOM   1776 C CD1 . LEU A 1 248 ? 29.44500  -4.25900  13.67100 1.000 24.22000 ? 248 LEU A CD1 1 
ATOM   1777 C CD2 . LEU A 1 248 ? 28.63000  -2.06200  12.81700 1.000 24.22000 ? 248 LEU A CD2 1 
ATOM   1778 N N   . SER A 1 249 ? 29.56300  0.00000   18.00700 1.000 24.34000 ? 249 SER A N   1 
ATOM   1779 C CA  . SER A 1 249 ? 29.01700  0.35900   19.31100 1.000 24.34000 ? 249 SER A CA  1 
ATOM   1780 C C   . SER A 1 249 ? 27.80600  1.27200   19.16600 1.000 24.34000 ? 249 SER A C   1 
ATOM   1781 O O   . SER A 1 249 ? 26.76900  1.05500   19.80400 1.000 24.34000 ? 249 SER A O   1 
ATOM   1782 C CB  . SER A 1 249 ? 30.09800  1.03400   20.15500 1.000 24.34000 ? 249 SER A CB  1 
ATOM   1783 O OG  . SER A 1 249 ? 31.30300  0.29000   20.12700 1.000 24.34000 ? 249 SER A OG  1 
ATOM   1784 N N   . GLY A 1 250 ? 27.91200  2.28200   18.30800 1.000 24.72000 ? 250 GLY A N   1 
ATOM   1785 C CA  . GLY A 1 250 ? 26.82100  3.18600   18.02400 1.000 24.72000 ? 250 GLY A CA  1 
ATOM   1786 C C   . GLY A 1 250 ? 25.86500  2.70100   16.96500 1.000 24.72000 ? 250 GLY A C   1 
ATOM   1787 O O   . GLY A 1 250 ? 24.87800  3.38300   16.66900 1.000 24.72000 ? 250 GLY A O   1 
ATOM   1788 N N   . SER A 1 251 ? 26.12700  1.53600   16.37700 1.000 24.03000 ? 251 SER A N   1 
ATOM   1789 C CA  . SER A 1 251 ? 25.26900  1.01200   15.32400 1.000 24.03000 ? 251 SER A CA  1 
ATOM   1790 C C   . SER A 1 251 ? 23.95600  0.51400   15.91400 1.000 24.03000 ? 251 SER A C   1 
ATOM   1791 O O   . SER A 1 251 ? 23.95200  -0.32700  16.82000 1.000 24.03000 ? 251 SER A O   1 
ATOM   1792 C CB  . SER A 1 251 ? 25.98100  -0.11300  14.57700 1.000 24.03000 ? 251 SER A CB  1 
ATOM   1793 O OG  . SER A 1 251 ? 25.13600  -0.67300  13.58800 1.000 24.03000 ? 251 SER A OG  1 
ATOM   1794 N N   . VAL A 1 252 ? 22.83800  1.02500   15.39300 1.000 22.70000 ? 252 VAL A N   1 
ATOM   1795 C CA  . VAL A 1 252 ? 21.53300  0.58400   15.86600 1.000 22.70000 ? 252 VAL A CA  1 
ATOM   1796 C C   . VAL A 1 252 ? 21.17900  -0.79800  15.33700 1.000 22.70000 ? 252 VAL A C   1 
ATOM   1797 O O   . VAL A 1 252 ? 20.27400  -1.44800  15.87200 1.000 22.70000 ? 252 VAL A O   1 
ATOM   1798 C CB  . VAL A 1 252 ? 20.44800  1.60600   15.48200 1.000 22.70000 ? 252 VAL A CB  1 
ATOM   1799 C CG1 . VAL A 1 252 ? 20.84900  2.99800   15.94300 1.000 22.70000 ? 252 VAL A CG1 1 
ATOM   1800 C CG2 . VAL A 1 252 ? 20.20700  1.58200   13.98400 1.000 22.70000 ? 252 VAL A CG2 1 
ATOM   1801 N N   . LEU A 1 253 ? 21.86700  -1.26200  14.29500 1.000 23.00000 ? 253 LEU A N   1 
ATOM   1802 C CA  . LEU A 1 253 ? 21.62300  -2.56400  13.69000 1.000 23.00000 ? 253 LEU A CA  1 
ATOM   1803 C C   . LEU A 1 253 ? 22.60600  -3.62600  14.16500 1.000 23.00000 ? 253 LEU A C   1 
ATOM   1804 O O   . LEU A 1 253 ? 22.67900  -4.69900  13.55800 1.000 23.00000 ? 253 LEU A O   1 
ATOM   1805 C CB  . LEU A 1 253 ? 21.67500  -2.45300  12.16600 1.000 23.00000 ? 253 LEU A CB  1 
ATOM   1806 C CG  . LEU A 1 253 ? 20.54600  -1.66800  11.49800 1.000 23.00000 ? 253 LEU A CG  1 
ATOM   1807 C CD1 . LEU A 1 253 ? 20.85800  -1.43500  10.03200 1.000 23.00000 ? 253 LEU A CD1 1 
ATOM   1808 C CD2 . LEU A 1 253 ? 19.23000  -2.40700  11.65100 1.000 23.00000 ? 253 LEU A CD2 1 
ATOM   1809 N N   . ARG A 1 254 ? 23.35700  -3.35000  15.22900 1.000 24.38000 ? 254 ARG A N   1 
ATOM   1810 C CA  . ARG A 1 254 ? 24.43400  -4.23600  15.65100 1.000 24.38000 ? 254 ARG A CA  1 
ATOM   1811 C C   . ARG A 1 254 ? 23.89400  -5.61500  16.00900 1.000 24.38000 ? 254 ARG A C   1 
ATOM   1812 O O   . ARG A 1 254 ? 22.81100  -5.74800  16.58600 1.000 24.38000 ? 254 ARG A O   1 
ATOM   1813 C CB  . ARG A 1 254 ? 25.17000  -3.62900  16.84700 1.000 24.38000 ? 254 ARG A CB  1 
ATOM   1814 C CG  . ARG A 1 254 ? 26.23700  -4.52300  17.45200 1.000 24.38000 ? 254 ARG A CG  1 
ATOM   1815 C CD  . ARG A 1 254 ? 26.86600  -3.87700  18.67400 1.000 24.38000 ? 254 ARG A CD  1 
ATOM   1816 N NE  . ARG A 1 254 ? 25.85800  -3.38100  19.60200 1.000 24.38000 ? 254 ARG A NE  1 
ATOM   1817 C CZ  . ARG A 1 254 ? 25.25800  -4.12100  20.52400 1.000 24.38000 ? 254 ARG A CZ  1 
ATOM   1818 N NH1 . ARG A 1 254 ? 25.54100  -5.40500  20.67300 1.000 24.38000 ? 254 ARG A NH1 1 
ATOM   1819 N NH2 . ARG A 1 254 ? 24.34800  -3.56000  21.31600 1.000 24.38000 ? 254 ARG A NH2 1 
ATOM   1820 N N   . SER A 1 255 ? 24.65100  -6.64800  15.64400 1.000 27.15000 ? 255 SER A N   1 
ATOM   1821 C CA  . SER A 1 255 ? 24.22700  -8.01600  15.91100 1.000 27.15000 ? 255 SER A CA  1 
ATOM   1822 C C   . SER A 1 255 ? 24.16500  -8.28300  17.40900 1.000 27.15000 ? 255 SER A C   1 
ATOM   1823 O O   . SER A 1 255 ? 25.03100  -7.84900  18.17300 1.000 27.15000 ? 255 SER A O   1 
ATOM   1824 C CB  . SER A 1 255 ? 25.18300  -9.00400  15.24200 1.000 27.15000 ? 255 SER A CB  1 
ATOM   1825 O OG  . SER A 1 255 ? 24.84500  -10.33800 15.57500 1.000 27.15000 ? 255 SER A OG  1 
ATOM   1826 N N   . VAL A 1 256 ? 23.12100  -8.99900  17.82700 1.000 29.72000 ? 256 VAL A N   1 
ATOM   1827 C CA  . VAL A 1 256 ? 22.99200  -9.39000  19.22300 1.000 29.72000 ? 256 VAL A CA  1 
ATOM   1828 C C   . VAL A 1 256 ? 23.96400  -10.52500 19.52800 1.000 29.72000 ? 256 VAL A C   1 
ATOM   1829 O O   . VAL A 1 256 ? 24.30100  -11.33800 18.65800 1.000 29.72000 ? 256 VAL A O   1 
ATOM   1830 C CB  . VAL A 1 256 ? 21.54400  -9.80600  19.53900 1.000 29.72000 ? 256 VAL A CB  1 
ATOM   1831 C CG1 . VAL A 1 256 ? 21.31500  -9.85000  21.04200 1.000 29.72000 ? 256 VAL A CG1 1 
ATOM   1832 C CG2 . VAL A 1 256 ? 20.55300  -8.87200  18.86000 1.000 29.72000 ? 256 VAL A CG2 1 
ATOM   1833 N N   . SER A 1 257 ? 24.41700  -10.58500 20.77200 1.000 32.61000 ? 257 SER A N   1 
ATOM   1834 C CA  . SER A 1 257 ? 25.21200  -11.72400 21.21000 1.000 32.61000 ? 257 SER A CA  1 
ATOM   1835 C C   . SER A 1 257 ? 24.34100  -12.97600 21.22300 1.000 32.61000 ? 257 SER A C   1 
ATOM   1836 O O   . SER A 1 257 ? 23.21500  -12.93300 21.73300 1.000 32.61000 ? 257 SER A O   1 
ATOM   1837 C CB  . SER A 1 257 ? 25.79500  -11.47100 22.59800 1.000 32.61000 ? 257 SER A CB  1 
ATOM   1838 O OG  . SER A 1 257 ? 26.50400  -12.60200 23.07400 1.000 32.61000 ? 257 SER A OG  1 
ATOM   1839 N N   . PRO A 1 258 ? 24.80400  -14.09200 20.65600 1.000 32.52000 ? 258 PRO A N   1 
ATOM   1840 C CA  . PRO A 1 258 ? 24.02100  -15.33700 20.75100 1.000 32.52000 ? 258 PRO A CA  1 
ATOM   1841 C C   . PRO A 1 258 ? 23.76600  -15.76500 22.18500 1.000 32.52000 ? 258 PRO A C   1 
ATOM   1842 O O   . PRO A 1 258 ? 22.69600  -16.30900 22.49400 1.000 32.52000 ? 258 PRO A O   1 
ATOM   1843 C CB  . PRO A 1 258 ? 24.88900  -16.34300 19.99500 1.000 32.52000 ? 258 PRO A CB  1 
ATOM   1844 C CG  . PRO A 1 258 ? 26.27900  -15.84000 20.19700 1.000 32.52000 ? 258 PRO A CG  1 
ATOM   1845 C CD  . PRO A 1 258 ? 26.14800  -14.34000 20.10400 1.000 32.52000 ? 258 PRO A CD  1 
ATOM   1846 N N   . CYS A 1 259 ? 24.71000  -15.46400 23.08500 1.000 35.19000 ? 259 CYS A N   1 
ATOM   1847 C CA  . CYS A 1 259 ? 24.55400  -15.73100 24.51100 1.000 35.19000 ? 259 CYS A CA  1 
ATOM   1848 C C   . CYS A 1 259 ? 23.30400  -15.06300 25.07500 1.000 35.19000 ? 259 CYS A C   1 
ATOM   1849 O O   . CYS A 1 259 ? 22.76200  -15.53400 26.07800 1.000 35.19000 ? 259 CYS A O   1 
ATOM   1850 C CB  . CYS A 1 259 ? 25.81500  -15.25300 25.24300 1.000 35.19000 ? 259 CYS A CB  1 
ATOM   1851 S SG  . CYS A 1 259 ? 25.80800  -15.24100 27.06200 1.000 35.19000 ? 259 CYS A SG  1 
ATOM   1852 N N   . HIS A 1 260 ? 22.84000  -13.96900 24.46400 1.000 33.85000 ? 260 HIS A N   1 
ATOM   1853 C CA  . HIS A 1 260 ? 21.59800  -13.31300 24.86900 1.000 33.85000 ? 260 HIS A CA  1 
ATOM   1854 C C   . HIS A 1 260 ? 20.40500  -13.66700 23.99100 1.000 33.85000 ? 260 HIS A C   1 
ATOM   1855 O O   . HIS A 1 260 ? 19.26500  -13.64400 24.47200 1.000 33.85000 ? 260 HIS A O   1 
ATOM   1856 C CB  . HIS A 1 260 ? 21.78600  -11.79000 24.87200 1.000 33.85000 ? 260 HIS A CB  1 
ATOM   1857 C CG  . HIS A 1 260 ? 20.51500  -11.01000 25.03100 1.000 33.85000 ? 260 HIS A CG  1 
ATOM   1858 N ND1 . HIS A 1 260 ? 19.62700  -11.22400 26.06300 1.000 33.85000 ? 260 HIS A ND1 1 
ATOM   1859 C CD2 . HIS A 1 260 ? 19.99600  -10.00000 24.29300 1.000 33.85000 ? 260 HIS A CD2 1 
ATOM   1860 C CE1 . HIS A 1 260 ? 18.61500  -10.38200 25.95200 1.000 33.85000 ? 260 HIS A CE1 1 
ATOM   1861 N NE2 . HIS A 1 260 ? 18.81300  -9.63000  24.88500 1.000 33.85000 ? 260 HIS A NE2 1 
ATOM   1862 N N   . ILE A 1 261 ? 20.63000  -13.97700 22.71300 1.000 35.08000 ? 261 ILE A N   1 
ATOM   1863 C CA  . ILE A 1 261 ? 19.51900  -14.37500 21.85400 1.000 35.08000 ? 261 ILE A CA  1 
ATOM   1864 C C   . ILE A 1 261 ? 18.92300  -15.68700 22.34100 1.000 35.08000 ? 261 ILE A C   1 
ATOM   1865 O O   . ILE A 1 261 ? 17.69900  -15.87700 22.32400 1.000 35.08000 ? 261 ILE A O   1 
ATOM   1866 C CB  . ILE A 1 261 ? 19.98500  -14.46600 20.38900 1.000 35.08000 ? 261 ILE A CB  1 
ATOM   1867 C CG1 . ILE A 1 261 ? 20.13100  -13.06700 19.79300 1.000 35.08000 ? 261 ILE A CG1 1 
ATOM   1868 C CG2 . ILE A 1 261 ? 19.01700  -15.29000 19.56100 1.000 35.08000 ? 261 ILE A CG2 1 
ATOM   1869 C CD1 . ILE A 1 261 ? 18.81500  -12.33100 19.64100 1.000 35.08000 ? 261 ILE A CD1 1 
ATOM   1870 N N   . GLU A 1 262 ? 19.77200  -16.59600 22.82500 1.000 36.41000 ? 262 GLU A N   1 
ATOM   1871 C CA  . GLU A 1 262 ? 19.25100  -17.83700 23.38700 1.000 36.41000 ? 262 GLU A CA  1 
ATOM   1872 C C   . GLU A 1 262 ? 18.42700  -17.56700 24.63900 1.000 36.41000 ? 262 GLU A C   1 
ATOM   1873 O O   . GLU A 1 262 ? 17.40500  -18.22300 24.87400 1.000 36.41000 ? 262 GLU A O   1 
ATOM   1874 C CB  . GLU A 1 262 ? 20.40000  -18.79500 23.69000 1.000 36.41000 ? 262 GLU A CB  1 
ATOM   1875 C CG  . GLU A 1 262 ? 19.95900  -20.18600 24.11100 1.000 36.41000 ? 262 GLU A CG  1 
ATOM   1876 C CD  . GLU A 1 262 ? 21.12000  -21.15400 24.19700 1.000 36.41000 ? 262 GLU A CD  1 
ATOM   1877 O OE1 . GLU A 1 262 ? 22.25800  -20.69700 24.43900 1.000 36.41000 ? 262 GLU A OE1 1 
ATOM   1878 O OE2 . GLU A 1 262 ? 20.89700  -22.36800 24.01200 1.000 36.41000 ? 262 GLU A OE2 1 
ATOM   1879 N N   . TYR A 1 263 ? 18.83900  -16.57600 25.43400 1.000 35.24000 ? 263 TYR A N   1 
ATOM   1880 C CA  . TYR A 1 263 ? 18.07900  -16.22300 26.62700 1.000 35.24000 ? 263 TYR A CA  1 
ATOM   1881 C C   . TYR A 1 263 ? 16.72200  -15.63700 26.26300 1.000 35.24000 ? 263 TYR A C   1 
ATOM   1882 O O   . TYR A 1 263 ? 15.71500  -15.93000 26.91900 1.000 35.24000 ? 263 TYR A O   1 
ATOM   1883 C CB  . TYR A 1 263 ? 18.87400  -15.23500 27.47800 1.000 35.24000 ? 263 TYR A CB  1 
ATOM   1884 C CG  . TYR A 1 263 ? 18.02900  -14.50300 28.49200 1.000 35.24000 ? 263 TYR A CG  1 
ATOM   1885 C CD1 . TYR A 1 263 ? 17.65900  -15.11500 29.67800 1.000 35.24000 ? 263 TYR A CD1 1 
ATOM   1886 C CD2 . TYR A 1 263 ? 17.59900  -13.20100 28.26100 1.000 35.24000 ? 263 TYR A CD2 1 
ATOM   1887 C CE1 . TYR A 1 263 ? 16.88700  -14.45900 30.60800 1.000 35.24000 ? 263 TYR A CE1 1 
ATOM   1888 C CE2 . TYR A 1 263 ? 16.82100  -12.53400 29.18700 1.000 35.24000 ? 263 TYR A CE2 1 
ATOM   1889 C CZ  . TYR A 1 263 ? 16.46400  -13.17300 30.36100 1.000 35.24000 ? 263 TYR A CZ  1 
ATOM   1890 O OH  . TYR A 1 263 ? 15.69800  -12.52800 31.31400 1.000 35.24000 ? 263 TYR A OH  1 
ATOM   1891 N N   . LEU A 1 264 ? 16.67800  -14.80100 25.22400 1.000 34.67000 ? 264 LEU A N   1 
ATOM   1892 C CA  . LEU A 1 264 ? 15.39300  -14.28000 24.76800 1.000 34.67000 ? 264 LEU A CA  1 
ATOM   1893 C C   . LEU A 1 264 ? 14.50800  -15.39500 24.22600 1.000 34.67000 ? 264 LEU A C   1 
ATOM   1894 O O   . LEU A 1 264 ? 13.28400  -15.36300 24.39600 1.000 34.67000 ? 264 LEU A O   1 
ATOM   1895 C CB  . LEU A 1 264 ? 15.59900  -13.20400 23.70300 1.000 34.67000 ? 264 LEU A CB  1 
ATOM   1896 C CG  . LEU A 1 264 ? 16.18800  -11.87200 24.16700 1.000 34.67000 ? 264 LEU A CG  1 
ATOM   1897 C CD1 . LEU A 1 264 ? 16.30700  -10.90100 23.00300 1.000 34.67000 ? 264 LEU A CD1 1 
ATOM   1898 C CD2 . LEU A 1 264 ? 15.34700  -11.27600 25.28400 1.000 34.67000 ? 264 LEU A CD2 1 
ATOM   1899 N N   . HIS A 1 265 ? 15.11100  -16.39100 23.57100 1.000 38.10000 ? 265 HIS A N   1 
ATOM   1900 C CA  . HIS A 1 265 ? 14.33200  -17.53000 23.09700 1.000 38.10000 ? 265 HIS A CA  1 
ATOM   1901 C C   . HIS A 1 265 ? 13.78700  -18.36300 24.24900 1.000 38.10000 ? 265 HIS A C   1 
ATOM   1902 O O   . HIS A 1 265 ? 12.69500  -18.93100 24.13500 1.000 38.10000 ? 265 HIS A O   1 
ATOM   1903 C CB  . HIS A 1 265 ? 15.17700  -18.39700 22.16500 1.000 38.10000 ? 265 HIS A CB  1 
ATOM   1904 C CG  . HIS A 1 265 ? 15.27900  -17.85900 20.77200 1.000 38.10000 ? 265 HIS A CG  1 
ATOM   1905 N ND1 . HIS A 1 265 ? 15.92800  -18.53000 19.75800 1.000 38.10000 ? 265 HIS A ND1 1 
ATOM   1906 C CD2 . HIS A 1 265 ? 14.80900  -16.71400 20.22300 1.000 38.10000 ? 265 HIS A CD2 1 
ATOM   1907 C CE1 . HIS A 1 265 ? 15.85500  -17.82100 18.64600 1.000 38.10000 ? 265 HIS A CE1 1 
ATOM   1908 N NE2 . HIS A 1 265 ? 15.18100  -16.71400 18.90100 1.000 38.10000 ? 265 HIS A NE2 1 
ATOM   1909 N N   . ASN A 1 266 ? 14.52600  -18.45600 25.35900 1.000 39.12000 ? 266 ASN A N   1 
ATOM   1910 C CA  . ASN A 1 266 ? 14.01400  -19.19400 26.50900 1.000 39.12000 ? 266 ASN A CA  1 
ATOM   1911 C C   . ASN A 1 266 ? 12.77700  -18.53200 27.10300 1.000 39.12000 ? 266 ASN A C   1 
ATOM   1912 O O   . ASN A 1 266 ? 11.87400  -19.22900 27.58000 1.000 39.12000 ? 266 ASN A O   1 
ATOM   1913 C CB  . ASN A 1 266 ? 15.09300  -19.32600 27.58200 1.000 39.12000 ? 266 ASN A CB  1 
ATOM   1914 C CG  . ASN A 1 266 ? 16.32300  -20.05700 27.08800 1.000 39.12000 ? 266 ASN A CG  1 
ATOM   1915 O OD1 . ASN A 1 266 ? 16.26900  -20.79000 26.10000 1.000 39.12000 ? 266 ASN A OD1 1 
ATOM   1916 N ND2 . ASN A 1 266 ? 17.44000  -19.86700 27.77800 1.000 39.12000 ? 266 ASN A ND2 1 
ATOM   1917 N N   . MET A 1 267 ? 12.71400  -17.20400 27.07800 1.000 39.01000 ? 267 MET A N   1 
ATOM   1918 C CA  . MET A 1 267 ? 11.61500  -16.46300 27.68000 1.000 39.01000 ? 267 MET A CA  1 
ATOM   1919 C C   . MET A 1 267 ? 10.46400  -16.20200 26.71800 1.000 39.01000 ? 267 MET A C   1 
ATOM   1920 O O   . MET A 1 267 ? 9.44800   -15.63600 27.13400 1.000 39.01000 ? 267 MET A O   1 
ATOM   1921 C CB  . MET A 1 267 ? 12.12800  -15.13300 28.24300 1.000 39.01000 ? 267 MET A CB  1 
ATOM   1922 C CG  . MET A 1 267 ? 13.22400  -15.29400 29.28400 1.000 39.01000 ? 267 MET A CG  1 
ATOM   1923 S SD  . MET A 1 267 ? 12.71700  -16.39300 30.62200 1.000 39.01000 ? 267 MET A SD  1 
ATOM   1924 C CE  . MET A 1 267 ? 14.19600  -16.43500 31.63000 1.000 39.01000 ? 267 MET A CE  1 
ATOM   1925 N N   . GLY A 1 268 ? 10.59300  -16.59000 25.45100 1.000 36.39000 ? 268 GLY A N   1 
ATOM   1926 C CA  . GLY A 1 268 ? 9.55900   -16.28700 24.48500 1.000 36.39000 ? 268 GLY A CA  1 
ATOM   1927 C C   . GLY A 1 268 ? 9.56200   -14.85800 23.99900 1.000 36.39000 ? 268 GLY A C   1 
ATOM   1928 O O   . GLY A 1 268 ? 8.57900   -14.41400 23.39700 1.000 36.39000 ? 268 GLY A O   1 
ATOM   1929 N N   . VAL A 1 269 ? 10.64500  -14.12100 24.24000 1.000 32.57000 ? 269 VAL A N   1 
ATOM   1930 C CA  . VAL A 1 269 ? 10.72800  -12.69500 23.92700 1.000 32.57000 ? 269 VAL A CA  1 
ATOM   1931 C C   . VAL A 1 269 ? 11.14300  -12.56400 22.46400 1.000 32.57000 ? 269 VAL A C   1 
ATOM   1932 O O   . VAL A 1 269 ? 12.32500  -12.65900 22.13400 1.000 32.57000 ? 269 VAL A O   1 
ATOM   1933 C CB  . VAL A 1 269 ? 11.70300  -11.96800 24.85600 1.000 32.57000 ? 269 VAL A CB  1 
ATOM   1934 C CG1 . VAL A 1 269 ? 11.85200  -10.51700 24.44200 1.000 32.57000 ? 269 VAL A CG1 1 
ATOM   1935 C CG2 . VAL A 1 269 ? 11.23800  -12.07100 26.29800 1.000 32.57000 ? 269 VAL A CG2 1 
ATOM   1936 N N   . LYS A 1 270 ? 10.16800  -12.35700 21.58000 1.000 31.20000 ? 270 LYS A N   1 
ATOM   1937 C CA  . LYS A 1 270 ? 10.44900  -12.15900 20.16400 1.000 31.20000 ? 270 LYS A CA  1 
ATOM   1938 C C   . LYS A 1 270 ? 10.77000  -10.71400 19.80400 1.000 31.20000 ? 270 LYS A C   1 
ATOM   1939 O O   . LYS A 1 270 ? 11.13600  -10.45400 18.65400 1.000 31.20000 ? 270 LYS A O   1 
ATOM   1940 C CB  . LYS A 1 270 ? 9.27500   -12.64800 19.31000 1.000 31.20000 ? 270 LYS A CB  1 
ATOM   1941 C CG  . LYS A 1 270 ? 9.01300   -14.14300 19.41800 1.000 31.20000 ? 270 LYS A CG  1 
ATOM   1942 C CD  . LYS A 1 270 ? 10.27800  -14.95200 19.18600 1.000 31.20000 ? 270 LYS A CD  1 
ATOM   1943 C CE  . LYS A 1 270 ? 10.02600  -16.43800 19.39100 1.000 31.20000 ? 270 LYS A CE  1 
ATOM   1944 N NZ  . LYS A 1 270 ? 11.27300  -17.23600 19.24400 1.000 31.20000 ? 270 LYS A NZ  1 
ATOM   1945 N N   . ALA A 1 271 ? 10.63700  -9.77000  20.73600 1.000 26.65000 ? 271 ALA A N   1 
ATOM   1946 C CA  . ALA A 1 271 ? 11.05100  -8.39800  20.46900 1.000 26.65000 ? 271 ALA A CA  1 
ATOM   1947 C C   . ALA A 1 271 ? 11.58000  -7.77500  21.75100 1.000 26.65000 ? 271 ALA A C   1 
ATOM   1948 O O   . ALA A 1 271 ? 10.99900  -7.96800  22.82100 1.000 26.65000 ? 271 ALA A O   1 
ATOM   1949 C CB  . ALA A 1 271 ? 9.89500   -7.56100  19.91200 1.000 26.65000 ? 271 ALA A CB  1 
ATOM   1950 N N   . SER A 1 272 ? 12.65800  -7.00100  21.63300 1.000 24.63000 ? 272 SER A N   1 
ATOM   1951 C CA  . SER A 1 272 ? 13.31100  -6.43600  22.80600 1.000 24.63000 ? 272 SER A CA  1 
ATOM   1952 C C   . SER A 1 272 ? 13.70600  -4.98700  22.55700 1.000 24.63000 ? 272 SER A C   1 
ATOM   1953 O O   . SER A 1 272 ? 14.14700  -4.63300  21.46000 1.000 24.63000 ? 272 SER A O   1 
ATOM   1954 C CB  . SER A 1 272 ? 14.55000  -7.25500  23.18600 1.000 24.63000 ? 272 SER A CB  1 
ATOM   1955 O OG  . SER A 1 272 ? 15.27400  -6.62900  24.22800 1.000 24.63000 ? 272 SER A OG  1 
ATOM   1956 N N   . MET A 1 273 ? 13.55300  -4.15500  23.58500 1.000 20.07000 ? 273 MET A N   1 
ATOM   1957 C CA  . MET A 1 273 ? 13.98200  -2.76000  23.50900 1.000 20.07000 ? 273 MET A CA  1 
ATOM   1958 C C   . MET A 1 273 ? 14.42100  -2.29100  24.88800 1.000 20.07000 ? 273 MET A C   1 
ATOM   1959 O O   . MET A 1 273 ? 13.62200  -2.29700  25.82600 1.000 20.07000 ? 273 MET A O   1 
ATOM   1960 C CB  . MET A 1 273 ? 12.86300  -1.86500  22.97300 1.000 20.07000 ? 273 MET A CB  1 
ATOM   1961 C CG  . MET A 1 273 ? 13.24200  -0.39300  22.91900 1.000 20.07000 ? 273 MET A CG  1 
ATOM   1962 S SD  . MET A 1 273 ? 12.02700  0.65500   22.09700 1.000 20.07000 ? 273 MET A SD  1 
ATOM   1963 C CE  . MET A 1 273 ? 11.55900  1.74000   23.44300 1.000 20.07000 ? 273 MET A CE  1 
ATOM   1964 N N   . SER A 1 274 ? 15.67800  -1.87600  25.01200 1.000 19.41000 ? 274 SER A N   1 
ATOM   1965 C CA  . SER A 1 274 ? 16.22100  -1.39600  26.27700 1.000 19.41000 ? 274 SER A CA  1 
ATOM   1966 C C   . SER A 1 274 ? 16.46100  0.10700   26.21500 1.000 19.41000 ? 274 SER A C   1 
ATOM   1967 O O   . SER A 1 274 ? 17.02400  0.61400   25.23700 1.000 19.41000 ? 274 SER A O   1 
ATOM   1968 C CB  . SER A 1 274 ? 17.52400  -2.11900  26.62800 1.000 19.41000 ? 274 SER A CB  1 
ATOM   1969 O OG  . SER A 1 274 ? 18.63800  -1.48200  26.03000 1.000 19.41000 ? 274 SER A OG  1 
ATOM   1970 N N   . ILE A 1 275 ? 16.03600  0.80600   27.26600 1.000 16.72000 ? 275 ILE A N   1 
ATOM   1971 C CA  . ILE A 1 275 ? 16.32800  2.22300   27.47000 1.000 16.72000 ? 275 ILE A CA  1 
ATOM   1972 C C   . ILE A 1 275 ? 17.29800  2.32800   28.63800 1.000 16.72000 ? 275 ILE A C   1 
ATOM   1973 O O   . ILE A 1 275 ? 17.00400  1.84900   29.73900 1.000 16.72000 ? 275 ILE A O   1 
ATOM   1974 C CB  . ILE A 1 275 ? 15.05400  3.03400   27.74400 1.000 16.72000 ? 275 ILE A CB  1 
ATOM   1975 C CG1 . ILE A 1 275 ? 14.02300  2.79700   26.64100 1.000 16.72000 ? 275 ILE A CG1 1 
ATOM   1976 C CG2 . ILE A 1 275 ? 15.38400  4.51500   27.88300 1.000 16.72000 ? 275 ILE A CG2 1 
ATOM   1977 C CD1 . ILE A 1 275 ? 12.68100  3.42600   26.92600 1.000 16.72000 ? 275 ILE A CD1 1 
ATOM   1978 N N   . SER A 1 276 ? 18.44100  2.96500   28.41100 1.000 16.46000 ? 276 SER A N   1 
ATOM   1979 C CA  . SER A 1 276 ? 19.52200  2.98700   29.39200 1.000 16.46000 ? 276 SER A CA  1 
ATOM   1980 C C   . SER A 1 276 ? 19.33800  4.17400   30.33200 1.000 16.46000 ? 276 SER A C   1 
ATOM   1981 O O   . SER A 1 276 ? 19.55200  5.32500   29.94000 1.000 16.46000 ? 276 SER A O   1 
ATOM   1982 C CB  . SER A 1 276 ? 20.87400  3.04600   28.68800 1.000 16.46000 ? 276 SER A CB  1 
ATOM   1983 O OG  . SER A 1 276 ? 21.02900  1.95300   27.80000 1.000 16.46000 ? 276 SER A OG  1 
ATOM   1984 N N   . ILE A 1 277 ? 18.94700  3.89500   31.57300 1.000 14.53000 ? 277 ILE A N   1 
ATOM   1985 C CA  . ILE A 1 277 ? 18.83300  4.93700   32.58800 1.000 14.53000 ? 277 ILE A CA  1 
ATOM   1986 C C   . ILE A 1 277 ? 20.23300  5.19800   33.13200 1.000 14.53000 ? 277 ILE A C   1 
ATOM   1987 O O   . ILE A 1 277 ? 20.82500  4.33300   33.78000 1.000 14.53000 ? 277 ILE A O   1 
ATOM   1988 C CB  . ILE A 1 277 ? 17.86700  4.53400   33.70600 1.000 14.53000 ? 277 ILE A CB  1 
ATOM   1989 C CG1 . ILE A 1 277 ? 16.48900  4.20600   33.12700 1.000 14.53000 ? 277 ILE A CG1 1 
ATOM   1990 C CG2 . ILE A 1 277 ? 17.75800  5.63900   34.74100 1.000 14.53000 ? 277 ILE A CG2 1 
ATOM   1991 C CD1 . ILE A 1 277 ? 15.79900  5.38600   32.47700 1.000 14.53000 ? 277 ILE A CD1 1 
ATOM   1992 N N   . ILE A 1 278 ? 20.75900  6.39400   32.87800 1.000 16.04000 ? 278 ILE A N   1 
ATOM   1993 C CA  . ILE A 1 278 ? 22.14300  6.72900   33.18700 1.000 16.04000 ? 278 ILE A CA  1 
ATOM   1994 C C   . ILE A 1 278 ? 22.17500  7.81400   34.25300 1.000 16.04000 ? 278 ILE A C   1 
ATOM   1995 O O   . ILE A 1 278 ? 21.38500  8.76300   34.21500 1.000 16.04000 ? 278 ILE A O   1 
ATOM   1996 C CB  . ILE A 1 278 ? 22.90300  7.17500   31.92000 1.000 16.04000 ? 278 ILE A CB  1 
ATOM   1997 C CG1 . ILE A 1 278 ? 22.92100  6.04100   30.89400 1.000 16.04000 ? 278 ILE A CG1 1 
ATOM   1998 C CG2 . ILE A 1 278 ? 24.32000  7.61300   32.25900 1.000 16.04000 ? 278 ILE A CG2 1 
ATOM   1999 C CD1 . ILE A 1 278 ? 23.65300  6.37900   29.61500 1.000 16.04000 ? 278 ILE A CD1 1 
ATOM   2000 N N   . LYS A 1 279 ? 23.09900  7.67200   35.20200 1.000 18.33000 ? 279 LYS A N   1 
ATOM   2001 C CA  . LYS A 1 279 ? 23.34900  8.67500   36.22500 1.000 18.33000 ? 279 LYS A CA  1 
ATOM   2002 C C   . LYS A 1 279 ? 24.84300  8.72200   36.50000 1.000 18.33000 ? 279 LYS A C   1 
ATOM   2003 O O   . LYS A 1 279 ? 25.50000  7.67900   36.56000 1.000 18.33000 ? 279 LYS A O   1 
ATOM   2004 C CB  . LYS A 1 279 ? 22.58400  8.37100   37.52100 1.000 18.33000 ? 279 LYS A CB  1 
ATOM   2005 C CG  . LYS A 1 279 ? 22.99600  9.24100   38.69700 1.000 18.33000 ? 279 LYS A CG  1 
ATOM   2006 C CD  . LYS A 1 279 ? 22.34700  8.78100   39.98800 1.000 18.33000 ? 279 LYS A CD  1 
ATOM   2007 C CE  . LYS A 1 279 ? 22.95700  9.48100   41.19500 1.000 18.33000 ? 279 LYS A CE  1 
ATOM   2008 N NZ  . LYS A 1 279 ? 22.81700  10.96200  41.12500 1.000 18.33000 ? 279 LYS A NZ  1 
ATOM   2009 N N   . ASN A 1 280 ? 25.37100  9.93700   36.67200 1.000 22.82000 ? 280 ASN A N   1 
ATOM   2010 C CA  . ASN A 1 280 ? 26.80600  10.15600  36.86200 1.000 22.82000 ? 280 ASN A CA  1 
ATOM   2011 C C   . ASN A 1 280 ? 27.61100  9.53600   35.72200 1.000 22.82000 ? 280 ASN A C   1 
ATOM   2012 O O   . ASN A 1 280 ? 28.69400  8.98500   35.93400 1.000 22.82000 ? 280 ASN A O   1 
ATOM   2013 C CB  . ASN A 1 280 ? 27.27900  9.62000   38.21600 1.000 22.82000 ? 280 ASN A CB  1 
ATOM   2014 C CG  . ASN A 1 280 ? 26.40800  10.08400  39.36600 1.000 22.82000 ? 280 ASN A CG  1 
ATOM   2015 O OD1 . ASN A 1 280 ? 26.08800  9.30900   40.26600 1.000 22.82000 ? 280 ASN A OD1 1 
ATOM   2016 N ND2 . ASN A 1 280 ? 26.02100  11.35400  39.34200 1.000 22.82000 ? 280 ASN A ND2 1 
ATOM   2017 N N   . ASN A 1 281 ? 27.06800  9.62400   34.50400 1.000 21.52000 ? 281 ASN A N   1 
ATOM   2018 C CA  . ASN A 1 281 ? 27.68000  9.04300   33.30700 1.000 21.52000 ? 281 ASN A CA  1 
ATOM   2019 C C   . ASN A 1 281 ? 27.95500  7.55000   33.48400 1.000 21.52000 ? 281 ASN A C   1 
ATOM   2020 O O   . ASN A 1 281 ? 29.00200  7.04100   33.08000 1.000 21.52000 ? 281 ASN A O   1 
ATOM   2021 C CB  . ASN A 1 281 ? 28.95600  9.79000   32.91300 1.000 21.52000 ? 281 ASN A CB  1 
ATOM   2022 C CG  . ASN A 1 281 ? 28.67800  11.19700  32.41700 1.000 21.52000 ? 281 ASN A CG  1 
ATOM   2023 O OD1 . ASN A 1 281 ? 28.39100  11.40800  31.23700 1.000 21.52000 ? 281 ASN A OD1 1 
ATOM   2024 N ND2 . ASN A 1 281 ? 28.76500  12.16800  33.31700 1.000 21.52000 ? 281 ASN A ND2 1 
ATOM   2025 N N   . LYS A 1 282 ? 27.00300  6.84100   34.09000 1.000 19.47000 ? 282 LYS A N   1 
ATOM   2026 C CA  . LYS A 1 282 ? 27.12600  5.40400   34.29100 1.000 19.47000 ? 282 LYS A CA  1 
ATOM   2027 C C   . LYS A 1 282 ? 25.73100  4.80300   34.41300 1.000 19.47000 ? 282 LYS A C   1 
ATOM   2028 O O   . LYS A 1 282 ? 24.76700  5.48700   34.76600 1.000 19.47000 ? 282 LYS A O   1 
ATOM   2029 C CB  . LYS A 1 282 ? 27.98700  5.08600   35.52100 1.000 19.47000 ? 282 LYS A CB  1 
ATOM   2030 C CG  . LYS A 1 282 ? 28.44400  3.63500   35.61400 1.000 19.47000 ? 282 LYS A CG  1 
ATOM   2031 C CD  . LYS A 1 282 ? 28.89200  3.08200   34.26000 1.000 19.47000 ? 282 LYS A CD  1 
ATOM   2032 C CE  . LYS A 1 282 ? 30.20900  3.68800   33.79300 1.000 19.47000 ? 282 LYS A CE  1 
ATOM   2033 N NZ  . LYS A 1 282 ? 30.61600  3.16600   32.45700 1.000 19.47000 ? 282 LYS A NZ  1 
ATOM   2034 N N   . LEU A 1 283 ? 25.64200  3.50300   34.12900 1.000 16.17000 ? 283 LEU A N   1 
ATOM   2035 C CA  . LEU A 1 283 ? 24.36400  2.82700   33.94100 1.000 16.17000 ? 283 LEU A CA  1 
ATOM   2036 C C   . LEU A 1 283 ? 23.63000  2.63300   35.26100 1.000 16.17000 ? 283 LEU A C   1 
ATOM   2037 O O   . LEU A 1 283 ? 23.78800  1.60300   35.92400 1.000 16.17000 ? 283 LEU A O   1 
ATOM   2038 C CB  . LEU A 1 283 ? 24.58400  1.48100   33.25100 1.000 16.17000 ? 283 LEU A CB  1 
ATOM   2039 C CG  . LEU A 1 283 ? 23.36000  0.76200   32.69100 1.000 16.17000 ? 283 LEU A CG  1 
ATOM   2040 C CD1 . LEU A 1 283 ? 22.67500  1.62500   31.64700 1.000 16.17000 ? 283 LEU A CD1 1 
ATOM   2041 C CD2 . LEU A 1 283 ? 23.76800  -0.57600  32.10000 1.000 16.17000 ? 283 LEU A CD2 1 
ATOM   2042 N N   . TRP A 1 284 ? 22.82400  3.62500   35.64800 1.000 14.42000 ? 284 TRP A N   1 
ATOM   2043 C CA  . TRP A 1 284 ? 22.04800  3.51000   36.87900 1.000 14.42000 ? 284 TRP A CA  1 
ATOM   2044 C C   . TRP A 1 284 ? 21.01000  2.39800   36.78600 1.000 14.42000 ? 284 TRP A C   1 
ATOM   2045 O O   . TRP A 1 284 ? 20.59300  1.84700   37.81300 1.000 14.42000 ? 284 TRP A O   1 
ATOM   2046 C CB  . TRP A 1 284 ? 21.38100  4.85100   37.19600 1.000 14.42000 ? 284 TRP A CB  1 
ATOM   2047 C CG  . TRP A 1 284 ? 20.65100  4.90400   38.50700 1.000 14.42000 ? 284 TRP A CG  1 
ATOM   2048 C CD1 . TRP A 1 284 ? 21.13700  5.35800   39.69900 1.000 14.42000 ? 284 TRP A CD1 1 
ATOM   2049 C CD2 . TRP A 1 284 ? 19.29000  4.52900   38.74800 1.000 14.42000 ? 284 TRP A CD2 1 
ATOM   2050 N NE1 . TRP A 1 284 ? 20.16700  5.27700   40.66900 1.000 14.42000 ? 284 TRP A NE1 1 
ATOM   2051 C CE2 . TRP A 1 284 ? 19.02400  4.77100   40.11000 1.000 14.42000 ? 284 TRP A CE2 1 
ATOM   2052 C CE3 . TRP A 1 284 ? 18.27200  4.00600   37.94400 1.000 14.42000 ? 284 TRP A CE3 1 
ATOM   2053 C CZ2 . TRP A 1 284 ? 17.78300  4.51000   40.68400 1.000 14.42000 ? 284 TRP A CZ2 1 
ATOM   2054 C CZ3 . TRP A 1 284 ? 17.04300  3.74400   38.51800 1.000 14.42000 ? 284 TRP A CZ3 1 
ATOM   2055 C CH2 . TRP A 1 284 ? 16.80900  3.99500   39.87400 1.000 14.42000 ? 284 TRP A CH2 1 
ATOM   2056 N N   . GLY A 1 285 ? 20.57600  2.06300   35.57900 1.000 14.77000 ? 285 GLY A N   1 
ATOM   2057 C CA  . GLY A 1 285 ? 19.53200  1.07200   35.43300 1.000 14.77000 ? 285 GLY A CA  1 
ATOM   2058 C C   . GLY A 1 285 ? 19.13700  0.91200   33.98200 1.000 14.77000 ? 285 GLY A C   1 
ATOM   2059 O O   . GLY A 1 285 ? 19.72100  1.52400   33.08500 1.000 14.77000 ? 285 GLY A O   1 
ATOM   2060 N N   . LEU A 1 286 ? 18.12500  0.07700   33.76900 1.000 16.20000 ? 286 LEU A N   1 
ATOM   2061 C CA  . LEU A 1 286 ? 17.61400  -0.19400  32.43700 1.000 16.20000 ? 286 LEU A CA  1 
ATOM   2062 C C   . LEU A 1 286 ? 16.09600  -0.25200  32.48100 1.000 16.20000 ? 286 LEU A C   1 
ATOM   2063 O O   . LEU A 1 286 ? 15.48300  -0.46300  33.53100 1.000 16.20000 ? 286 LEU A O   1 
ATOM   2064 C CB  . LEU A 1 286 ? 18.17100  -1.50600  31.87100 1.000 16.20000 ? 286 LEU A CB  1 
ATOM   2065 C CG  . LEU A 1 286 ? 19.62900  -1.53800  31.41100 1.000 16.20000 ? 286 LEU A CG  1 
ATOM   2066 C CD1 . LEU A 1 286 ? 19.99100  -2.92200  30.89700 1.000 16.20000 ? 286 LEU A CD1 1 
ATOM   2067 C CD2 . LEU A 1 286 ? 19.87800  -0.49500  30.33900 1.000 16.20000 ? 286 LEU A CD2 1 
ATOM   2068 N N   . ILE A 1 287 ? 15.49600  -0.03000  31.31900 1.000 16.41000 ? 287 ILE A N   1 
ATOM   2069 C CA  . ILE A 1 287 ? 14.07000  -0.22000  31.10700 1.000 16.41000 ? 287 ILE A CA  1 
ATOM   2070 C C   . ILE A 1 287 ? 13.94300  -1.21800  29.96900 1.000 16.41000 ? 287 ILE A C   1 
ATOM   2071 O O   . ILE A 1 287 ? 14.20000  -0.87400  28.80800 1.000 16.41000 ? 287 ILE A O   1 
ATOM   2072 C CB  . ILE A 1 287 ? 13.34800  1.09200   30.77400 1.000 16.41000 ? 287 ILE A CB  1 
ATOM   2073 C CG1 . ILE A 1 287 ? 13.45300  2.07800   31.93900 1.000 16.41000 ? 287 ILE A CG1 1 
ATOM   2074 C CG2 . ILE A 1 287 ? 11.89100  0.82000   30.43700 1.000 16.41000 ? 287 ILE A CG2 1 
ATOM   2075 C CD1 . ILE A 1 287 ? 12.73600  3.38900   31.69500 1.000 16.41000 ? 287 ILE A CD1 1 
ATOM   2076 N N   . ALA A 1 288 ? 13.58000  -2.45300  30.30100 1.000 18.62000 ? 288 ALA A N   1 
ATOM   2077 C CA  . ALA A 1 288 ? 13.49700  -3.53200  29.32600 1.000 18.62000 ? 288 ALA A CA  1 
ATOM   2078 C C   . ALA A 1 288 ? 12.06200  -3.68600  28.84500 1.000 18.62000 ? 288 ALA A C   1 
ATOM   2079 O O   . ALA A 1 288 ? 11.13500  -3.74200  29.65600 1.000 18.62000 ? 288 ALA A O   1 
ATOM   2080 C CB  . ALA A 1 288 ? 13.99800  -4.84800  29.92100 1.000 18.62000 ? 288 ALA A CB  1 
ATOM   2081 N N   . CYS A 1 289 ? 11.88600  -3.77300  27.53000 1.000 21.23000 ? 289 CYS A N   1 
ATOM   2082 C CA  . CYS A 1 289 ? 10.58000  -3.94300  26.90700 1.000 21.23000 ? 289 CYS A CA  1 
ATOM   2083 C C   . CYS A 1 289 ? 10.62500  -5.23100  26.10200 1.000 21.23000 ? 289 CYS A C   1 
ATOM   2084 O O   . CYS A 1 289 ? 11.33100  -5.31100  25.09100 1.000 21.23000 ? 289 CYS A O   1 
ATOM   2085 C CB  . CYS A 1 289 ? 10.23300  -2.75000  26.01700 1.000 21.23000 ? 289 CYS A CB  1 
ATOM   2086 S SG  . CYS A 1 289 ? 10.34900  -1.14600  26.83400 1.000 21.23000 ? 289 CYS A SG  1 
ATOM   2087 N N   . HIS A 1 290 ? 9.89100   -6.23400  26.56700 1.000 24.78000 ? 290 HIS A N   1 
ATOM   2088 C CA  . HIS A 1 290 ? 9.80000   -7.52900  25.91300 1.000 24.78000 ? 290 HIS A CA  1 
ATOM   2089 C C   . HIS A 1 290 ? 8.42200   -7.69500  25.28700 1.000 24.78000 ? 290 HIS A C   1 
ATOM   2090 O O   . HIS A 1 290 ? 7.40300   -7.37900  25.91100 1.000 24.78000 ? 290 HIS A O   1 
ATOM   2091 C CB  . HIS A 1 290 ? 10.07500  -8.65900  26.90900 1.000 24.78000 ? 290 HIS A CB  1 
ATOM   2092 C CG  . HIS A 1 290 ? 11.47700  -8.66900  27.43500 1.000 24.78000 ? 290 HIS A CG  1 
ATOM   2093 N ND1 . HIS A 1 290 ? 11.90900  -9.56800  28.38700 1.000 24.78000 ? 290 HIS A ND1 1 
ATOM   2094 C CD2 . HIS A 1 290 ? 12.54500  -7.89100  27.14000 1.000 24.78000 ? 290 HIS A CD2 1 
ATOM   2095 C CE1 . HIS A 1 290 ? 13.18300  -9.34300  28.65500 1.000 24.78000 ? 290 HIS A CE1 1 
ATOM   2096 N NE2 . HIS A 1 290 ? 13.59300  -8.33100  27.91300 1.000 24.78000 ? 290 HIS A NE2 1 
ATOM   2097 N N   . HIS A 1 291 ? 8.39700   -8.19500  24.05400 1.000 28.71000 ? 291 HIS A N   1 
ATOM   2098 C CA  . HIS A 1 291 ? 7.16500   -8.37500  23.29900 1.000 28.71000 ? 291 HIS A CA  1 
ATOM   2099 C C   . HIS A 1 291 ? 7.11700   -9.79900  22.77000 1.000 28.71000 ? 291 HIS A C   1 
ATOM   2100 O O   . HIS A 1 291 ? 8.08300   -10.26900 22.15500 1.000 28.71000 ? 291 HIS A O   1 
ATOM   2101 C CB  . HIS A 1 291 ? 7.07200   -7.37100  22.14500 1.000 28.71000 ? 291 HIS A CB  1 
ATOM   2102 C CG  . HIS A 1 291 ? 5.67100   -7.08200  21.70100 1.000 28.71000 ? 291 HIS A CG  1 
ATOM   2103 N ND1 . HIS A 1 291 ? 5.17500   -7.49500  20.48300 1.000 28.71000 ? 291 HIS A ND1 1 
ATOM   2104 C CD2 . HIS A 1 291 ? 4.66500   -6.41200  22.30900 1.000 28.71000 ? 291 HIS A CD2 1 
ATOM   2105 C CE1 . HIS A 1 291 ? 3.92200   -7.09300  20.36200 1.000 28.71000 ? 291 HIS A CE1 1 
ATOM   2106 N NE2 . HIS A 1 291 ? 3.58800   -6.43500  21.45700 1.000 28.71000 ? 291 HIS A NE2 1 
ATOM   2107 N N   . GLN A 1 292 ? 5.99200   -10.47800 23.01500 1.000 31.04000 ? 292 GLN A N   1 
ATOM   2108 C CA  . GLN A 1 292 ? 5.85700   -11.87400 22.61300 1.000 31.04000 ? 292 GLN A CA  1 
ATOM   2109 C C   . GLN A 1 292 ? 5.80500   -12.01800 21.09700 1.000 31.04000 ? 292 GLN A C   1 
ATOM   2110 O O   . GLN A 1 292 ? 6.39300   -12.95100 20.53900 1.000 31.04000 ? 292 GLN A O   1 
ATOM   2111 C CB  . GLN A 1 292 ? 4.61000   -12.48100 23.25600 1.000 31.04000 ? 292 GLN A CB  1 
ATOM   2112 C CG  . GLN A 1 292 ? 4.56000   -12.32800 24.77100 1.000 31.04000 ? 292 GLN A CG  1 
ATOM   2113 C CD  . GLN A 1 292 ? 3.33900   -12.98500 25.38900 1.000 31.04000 ? 292 GLN A CD  1 
ATOM   2114 O OE1 . GLN A 1 292 ? 2.26200   -12.39000 25.45200 1.000 31.04000 ? 292 GLN A OE1 1 
ATOM   2115 N NE2 . GLN A 1 292 ? 3.50300   -14.21900 25.85000 1.000 31.04000 ? 292 GLN A NE2 1 
ATOM   2116 N N   . THR A 1 293 ? 5.08200   -11.12500 20.41100 1.000 29.75000 ? 293 THR A N   1 
ATOM   2117 C CA  . THR A 1 293 ? 5.26300   -11.14500 18.96800 1.000 29.75000 ? 293 THR A CA  1 
ATOM   2118 C C   . THR A 1 293 ? 6.43300   -10.24800 18.57600 1.000 29.75000 ? 293 THR A C   1 
ATOM   2119 O O   . THR A 1 293 ? 6.72300   -9.26400  19.26600 1.000 29.75000 ? 293 THR A O   1 
ATOM   2120 C CB  . THR A 1 293 ? 3.99600   -10.67600 18.25600 1.000 29.75000 ? 293 THR A CB  1 
ATOM   2121 O OG1 . THR A 1 293 ? 3.88000   -9.25300  18.36300 1.000 29.75000 ? 293 THR A OG1 1 
ATOM   2122 C CG2 . THR A 1 293 ? 2.76800   -11.32700 18.87400 1.000 29.75000 ? 293 THR A CG2 1 
ATOM   2123 N N   . PRO A 1 294 ? 7.13800   -10.55500 17.48700 1.000 28.03000 ? 294 PRO A N   1 
ATOM   2124 C CA  . PRO A 1 294 ? 8.19700   -9.64900  17.02900 1.000 28.03000 ? 294 PRO A CA  1 
ATOM   2125 C C   . PRO A 1 294 ? 7.61700   -8.28900  16.67100 1.000 28.03000 ? 294 PRO A C   1 
ATOM   2126 O O   . PRO A 1 294 ? 6.51000   -8.18600  16.13900 1.000 28.03000 ? 294 PRO A O   1 
ATOM   2127 C CB  . PRO A 1 294 ? 8.77600   -10.36500 15.80400 1.000 28.03000 ? 294 PRO A CB  1 
ATOM   2128 C CG  . PRO A 1 294 ? 7.69300   -11.29200 15.35600 1.000 28.03000 ? 294 PRO A CG  1 
ATOM   2129 C CD  . PRO A 1 294 ? 6.99500   -11.72800 16.60700 1.000 28.03000 ? 294 PRO A CD  1 
ATOM   2130 N N   . LYS A 1 295 ? 8.37700   -7.23700  16.96600 1.000 23.73000 ? 295 LYS A N   1 
ATOM   2131 C CA  . LYS A 1 295 ? 7.84800   -5.88400  16.88400 1.000 23.73000 ? 295 LYS A CA  1 
ATOM   2132 C C   . LYS A 1 295 ? 8.92400   -4.92000  16.41400 1.000 23.73000 ? 295 LYS A C   1 
ATOM   2133 O O   . LYS A 1 295 ? 10.03000  -4.90000  16.96200 1.000 23.73000 ? 295 LYS A O   1 
ATOM   2134 C CB  . LYS A 1 295 ? 7.30200   -5.43900  18.24300 1.000 23.73000 ? 295 LYS A CB  1 
ATOM   2135 C CG  . LYS A 1 295 ? 6.68700   -4.06000  18.24200 1.000 23.73000 ? 295 LYS A CG  1 
ATOM   2136 C CD  . LYS A 1 295 ? 6.17500   -3.71500  19.62000 1.000 23.73000 ? 295 LYS A CD  1 
ATOM   2137 C CE  . LYS A 1 295 ? 5.47700   -2.37600  19.62400 1.000 23.73000 ? 295 LYS A CE  1 
ATOM   2138 N NZ  . LYS A 1 295 ? 5.00100   -2.05800  20.99000 1.000 23.73000 ? 295 LYS A NZ  1 
ATOM   2139 N N   . TYR A 1 296 ? 8.58800   -4.12200  15.40300 1.000 28.02000 ? 296 TYR A N   1 
ATOM   2140 C CA  . TYR A 1 296 ? 9.44600   -3.05100  14.91500 1.000 28.02000 ? 296 TYR A CA  1 
ATOM   2141 C C   . TYR A 1 296 ? 8.98600   -1.73200  15.52200 1.000 28.02000 ? 296 TYR A C   1 
ATOM   2142 O O   . TYR A 1 296 ? 7.79200   -1.41700  15.49900 1.000 28.02000 ? 296 TYR A O   1 
ATOM   2143 C CB  . TYR A 1 296 ? 9.40700   -2.98400  13.38700 1.000 28.02000 ? 296 TYR A CB  1 
ATOM   2144 C CG  . TYR A 1 296 ? 10.20800  -1.85000  12.78800 1.000 28.02000 ? 296 TYR A CG  1 
ATOM   2145 C CD1 . TYR A 1 296 ? 11.59200  -1.92300  12.70000 1.000 28.02000 ? 296 TYR A CD1 1 
ATOM   2146 C CD2 . TYR A 1 296 ? 9.57800   -0.71300  12.29500 1.000 28.02000 ? 296 TYR A CD2 1 
ATOM   2147 C CE1 . TYR A 1 296 ? 12.32800  -0.89200  12.14800 1.000 28.02000 ? 296 TYR A CE1 1 
ATOM   2148 C CE2 . TYR A 1 296 ? 10.30600  0.32400   11.74100 1.000 28.02000 ? 296 TYR A CE2 1 
ATOM   2149 C CZ  . TYR A 1 296 ? 11.68100  0.22900   11.67000 1.000 28.02000 ? 296 TYR A CZ  1 
ATOM   2150 O OH  . TYR A 1 296 ? 12.41000  1.25800   11.11900 1.000 28.02000 ? 296 TYR A OH  1 
ATOM   2151 N N   . VAL A 1 297 ? 9.92800   -0.96800  16.06000 1.000 25.90000 ? 297 VAL A N   1 
ATOM   2152 C CA  . VAL A 1 297 ? 9.63200   0.26900   16.77600 1.000 25.90000 ? 297 VAL A CA  1 
ATOM   2153 C C   . VAL A 1 297 ? 9.81200   1.43700   15.81100 1.000 25.90000 ? 297 VAL A C   1 
ATOM   2154 O O   . VAL A 1 297 ? 10.92400  1.63000   15.29400 1.000 25.90000 ? 297 VAL A O   1 
ATOM   2155 C CB  . VAL A 1 297 ? 10.51800  0.43100   18.01900 1.000 25.90000 ? 297 VAL A CB  1 
ATOM   2156 C CG1 . VAL A 1 297 ? 10.12500  1.68100   18.78800 1.000 25.90000 ? 297 VAL A CG1 1 
ATOM   2157 C CG2 . VAL A 1 297 ? 10.39400  -0.79600  18.90800 1.000 25.90000 ? 297 VAL A CG2 1 
ATOM   2158 N N   . PRO A 1 298 ? 8.77000   2.22200   15.53700 1.000 26.65000 ? 298 PRO A N   1 
ATOM   2159 C CA  . PRO A 1 298 ? 8.91800   3.38000   14.64600 1.000 26.65000 ? 298 PRO A CA  1 
ATOM   2160 C C   . PRO A 1 298 ? 9.88200   4.41200   15.21100 1.000 26.65000 ? 298 PRO A C   1 
ATOM   2161 O O   . PRO A 1 298 ? 9.99400   4.59000   16.42700 1.000 26.65000 ? 298 PRO A O   1 
ATOM   2162 C CB  . PRO A 1 298 ? 7.49400   3.94100   14.55200 1.000 26.65000 ? 298 PRO A CB  1 
ATOM   2163 C CG  . PRO A 1 298 ? 6.60200   2.81100   14.96600 1.000 26.65000 ? 298 PRO A CG  1 
ATOM   2164 C CD  . PRO A 1 298 ? 7.37800   2.03400   15.97900 1.000 26.65000 ? 298 PRO A CD  1 
ATOM   2165 N N   . TYR A 1 299 ? 10.59200  5.09400   14.30400 1.000 27.49000 ? 299 TYR A N   1 
ATOM   2166 C CA  . TYR A 1 299 ? 11.57700  6.08900   14.72000 1.000 27.49000 ? 299 TYR A CA  1 
ATOM   2167 C C   . TYR A 1 299 ? 10.95100  7.20700   15.54100 1.000 27.49000 ? 299 TYR A C   1 
ATOM   2168 O O   . TYR A 1 299 ? 11.59500  7.74200   16.45100 1.000 27.49000 ? 299 TYR A O   1 
ATOM   2169 C CB  . TYR A 1 299 ? 12.27100  6.68400   13.49500 1.000 27.49000 ? 299 TYR A CB  1 
ATOM   2170 C CG  . TYR A 1 299 ? 13.56100  6.00500   13.11400 1.000 27.49000 ? 299 TYR A CG  1 
ATOM   2171 C CD1 . TYR A 1 299 ? 13.55700  4.77700   12.46800 1.000 27.49000 ? 299 TYR A CD1 1 
ATOM   2172 C CD2 . TYR A 1 299 ? 14.78500  6.60100   13.38500 1.000 27.49000 ? 299 TYR A CD2 1 
ATOM   2173 C CE1 . TYR A 1 299 ? 14.73800  4.15600   12.11200 1.000 27.49000 ? 299 TYR A CE1 1 
ATOM   2174 C CE2 . TYR A 1 299 ? 15.97000  5.99000   13.03200 1.000 27.49000 ? 299 TYR A CE2 1 
ATOM   2175 C CZ  . TYR A 1 299 ? 15.94100  4.76700   12.39500 1.000 27.49000 ? 299 TYR A CZ  1 
ATOM   2176 O OH  . TYR A 1 299 ? 17.11800  4.15100   12.04000 1.000 27.49000 ? 299 TYR A OH  1 
ATOM   2177 N N   . GLU A 1 300 ? 9.70300   7.57400   15.24300 1.000 29.22000 ? 300 GLU A N   1 
ATOM   2178 C CA  . GLU A 1 300 ? 9.02600   8.57700   16.05600 1.000 29.22000 ? 300 GLU A CA  1 
ATOM   2179 C C   . GLU A 1 300 ? 8.75300   8.06500   17.46300 1.000 29.22000 ? 300 GLU A C   1 
ATOM   2180 O O   . GLU A 1 300 ? 8.64200   8.86400   18.39900 1.000 29.22000 ? 300 GLU A O   1 
ATOM   2181 C CB  . GLU A 1 300 ? 7.72400   9.01800   15.38100 1.000 29.22000 ? 300 GLU A CB  1 
ATOM   2182 C CG  . GLU A 1 300 ? 7.86100   10.28800  14.55000 1.000 29.22000 ? 300 GLU A CG  1 
ATOM   2183 C CD  . GLU A 1 300 ? 8.98600   10.21300  13.53400 1.000 29.22000 ? 300 GLU A CD  1 
ATOM   2184 O OE1 . GLU A 1 300 ? 9.12400   9.16400   12.86800 1.000 29.22000 ? 300 GLU A OE1 1 
ATOM   2185 O OE2 . GLU A 1 300 ? 9.73700   11.20300  13.40600 1.000 29.22000 ? 300 GLU A OE2 1 
ATOM   2186 N N   . ILE A 1 301 ? 8.63500   6.74500   17.63400 1.000 25.21000 ? 301 ILE A N   1 
ATOM   2187 C CA  . ILE A 1 301 ? 8.50100   6.18400   18.97300 1.000 25.21000 ? 301 ILE A CA  1 
ATOM   2188 C C   . ILE A 1 301 ? 9.86600   6.04900   19.63800 1.000 25.21000 ? 301 ILE A C   1 
ATOM   2189 O O   . ILE A 1 301 ? 10.00700  6.30000   20.84100 1.000 25.21000 ? 301 ILE A O   1 
ATOM   2190 C CB  . ILE A 1 301 ? 7.75400   4.83800   18.91700 1.000 25.21000 ? 301 ILE A CB  1 
ATOM   2191 C CG1 . ILE A 1 301 ? 6.30900   5.05400   18.46800 1.000 25.21000 ? 301 ILE A CG1 1 
ATOM   2192 C CG2 . ILE A 1 301 ? 7.78300   4.14800   20.27400 1.000 25.21000 ? 301 ILE A CG2 1 
ATOM   2193 C CD1 . ILE A 1 301 ? 5.50900   5.94700   19.39700 1.000 25.21000 ? 301 ILE A CD1 1 
ATOM   2194 N N   . ARG A 1 302 ? 10.89400  5.66900   18.87200 1.000 24.99000 ? 302 ARG A N   1 
ATOM   2195 C CA  . ARG A 1 302 ? 12.23900  5.61100   19.43500 1.000 24.99000 ? 302 ARG A CA  1 
ATOM   2196 C C   . ARG A 1 302 ? 12.69500  6.98800   19.88600 1.000 24.99000 ? 302 ARG A C   1 
ATOM   2197 O O   . ARG A 1 302 ? 13.40000  7.12100   20.89200 1.000 24.99000 ? 302 ARG A O   1 
ATOM   2198 C CB  . ARG A 1 302 ? 13.22700  5.05800   18.40800 1.000 24.99000 ? 302 ARG A CB  1 
ATOM   2199 C CG  . ARG A 1 302 ? 12.84000  3.74700   17.76700 1.000 24.99000 ? 302 ARG A CG  1 
ATOM   2200 C CD  . ARG A 1 302 ? 13.81100  3.41800   16.65000 1.000 24.99000 ? 302 ARG A CD  1 
ATOM   2201 N NE  . ARG A 1 302 ? 13.51200  2.14600   16.00700 1.000 24.99000 ? 302 ARG A NE  1 
ATOM   2202 C CZ  . ARG A 1 302 ? 14.27300  1.58300   15.08000 1.000 24.99000 ? 302 ARG A CZ  1 
ATOM   2203 N NH1 . ARG A 1 302 ? 15.38300  2.16300   14.65200 1.000 24.99000 ? 302 ARG A NH1 1 
ATOM   2204 N NH2 . ARG A 1 302 ? 13.91600  0.40700   14.57300 1.000 24.99000 ? 302 ARG A NH2 1 
ATOM   2205 N N   . HIS A 1 303 ? 12.29300  8.02800   19.15400 1.000 27.90000 ? 303 HIS A N   1 
ATOM   2206 C CA  . HIS A 1 303 ? 12.60600  9.38900   19.56900 1.000 27.90000 ? 303 HIS A CA  1 
ATOM   2207 C C   . HIS A 1 303 ? 11.87000  9.74900   20.85300 1.000 27.90000 ? 303 HIS A C   1 
ATOM   2208 O O   . HIS A 1 303 ? 12.42300  10.43100  21.72300 1.000 27.90000 ? 303 HIS A O   1 
ATOM   2209 C CB  . HIS A 1 303 ? 12.24600  10.36100  18.44400 1.000 27.90000 ? 303 HIS A CB  1 
ATOM   2210 C CG  . HIS A 1 303 ? 13.13500  11.56300  18.36600 1.000 27.90000 ? 303 HIS A CG  1 
ATOM   2211 N ND1 . HIS A 1 303 ? 13.19700  12.36800  17.24900 1.000 27.90000 ? 303 HIS A ND1 1 
ATOM   2212 C CD2 . HIS A 1 303 ? 13.99600  12.09900  19.26400 1.000 27.90000 ? 303 HIS A CD2 1 
ATOM   2213 C CE1 . HIS A 1 303 ? 14.05800  13.34800  17.46200 1.000 27.90000 ? 303 HIS A CE1 1 
ATOM   2214 N NE2 . HIS A 1 303 ? 14.55700  13.20700  18.67700 1.000 27.90000 ? 303 HIS A NE2 1 
ATOM   2215 N N   . ALA A 1 304 ? 10.62400  9.28900   20.99300 1.000 24.88000 ? 304 ALA A N   1 
ATOM   2216 C CA  . ALA A 1 304 ? 9.85800   9.58800   22.19800 1.000 24.88000 ? 304 ALA A CA  1 
ATOM   2217 C C   . ALA A 1 304 ? 10.40600  8.84300   23.40800 1.000 24.88000 ? 304 ALA A C   1 
ATOM   2218 O O   . ALA A 1 304 ? 10.40700  9.37500   24.52300 1.000 24.88000 ? 304 ALA A O   1 
ATOM   2219 C CB  . ALA A 1 304 ? 8.38400   9.24700   21.98100 1.000 24.88000 ? 304 ALA A CB  1 
ATOM   2220 N N   . CYS A 1 305 ? 10.88400  7.61400   23.20800 1.000 22.96000 ? 305 CYS A N   1 
ATOM   2221 C CA  . CYS A 1 305 ? 11.36900  6.82300   24.33400 1.000 22.96000 ? 305 CYS A CA  1 
ATOM   2222 C C   . CYS A 1 305 ? 12.79500  7.19600   24.70600 1.000 22.96000 ? 305 CYS A C   1 
ATOM   2223 O O   . CYS A 1 305 ? 13.13300  7.26200   25.89200 1.000 22.96000 ? 305 CYS A O   1 
ATOM   2224 C CB  . CYS A 1 305 ? 11.27600  5.33500   24.00500 1.000 22.96000 ? 305 CYS A CB  1 
ATOM   2225 S SG  . CYS A 1 305 ? 9.60100   4.78400   23.63600 1.000 22.96000 ? 305 CYS A SG  1 
ATOM   2226 N N   . GLU A 1 306 ? 13.64400  7.43400   23.70600 1.000 22.67000 ? 306 GLU A N   1 
ATOM   2227 C CA  . GLU A 1 306 ? 15.01100  7.85200   23.99100 1.000 22.67000 ? 306 GLU A CA  1 
ATOM   2228 C C   . GLU A 1 306 ? 15.03500  9.20400   24.69100 1.000 22.67000 ? 306 GLU A C   1 
ATOM   2229 O O   . GLU A 1 306 ? 15.88200  9.45000   25.55800 1.000 22.67000 ? 306 GLU A O   1 
ATOM   2230 C CB  . GLU A 1 306 ? 15.81400  7.89500   22.69300 1.000 22.67000 ? 306 GLU A CB  1 
ATOM   2231 C CG  . GLU A 1 306 ? 17.22000  8.43300   22.82200 1.000 22.67000 ? 306 GLU A CG  1 
ATOM   2232 C CD  . GLU A 1 306 ? 18.09900  8.01700   21.66000 1.000 22.67000 ? 306 GLU A CD  1 
ATOM   2233 O OE1 . GLU A 1 306 ? 17.64600  7.19200   20.83500 1.000 22.67000 ? 306 GLU A OE1 1 
ATOM   2234 O OE2 . GLU A 1 306 ? 19.24300  8.50900   21.57400 1.000 22.67000 ? 306 GLU A OE2 1 
ATOM   2235 N N   . PHE A 1 307 ? 14.10500  10.09400  24.33600 1.000 22.58000 ? 307 PHE A N   1 
ATOM   2236 C CA  . PHE A 1 307 ? 13.97300  11.34600  25.07200 1.000 22.58000 ? 307 PHE A CA  1 
ATOM   2237 C C   . PHE A 1 307 ? 13.43800  11.11600  26.48000 1.000 22.58000 ? 307 PHE A C   1 
ATOM   2238 O O   . PHE A 1 307 ? 13.80700  11.84500  27.40900 1.000 22.58000 ? 307 PHE A O   1 
ATOM   2239 C CB  . PHE A 1 307 ? 13.06800  12.31400  24.31100 1.000 22.58000 ? 307 PHE A CB  1 
ATOM   2240 C CG  . PHE A 1 307 ? 13.04100  13.69300  24.89400 1.000 22.58000 ? 307 PHE A CG  1 
ATOM   2241 C CD1 . PHE A 1 307 ? 14.04400  14.60000  24.59700 1.000 22.58000 ? 307 PHE A CD1 1 
ATOM   2242 C CD2 . PHE A 1 307 ? 12.01800  14.08300  25.74100 1.000 22.58000 ? 307 PHE A CD2 1 
ATOM   2243 C CE1 . PHE A 1 307 ? 14.02700  15.87300  25.13300 1.000 22.58000 ? 307 PHE A CE1 1 
ATOM   2244 C CE2 . PHE A 1 307 ? 11.99300  15.35500  26.28100 1.000 22.58000 ? 307 PHE A CE2 1 
ATOM   2245 C CZ  . PHE A 1 307 ? 12.99900  16.25200  25.97600 1.000 22.58000 ? 307 PHE A CZ  1 
ATOM   2246 N N   . LEU A 1 308 ? 12.57200  10.11400  26.65900 1.000 20.31000 ? 308 LEU A N   1 
ATOM   2247 C CA  . LEU A 1 308 ? 12.06000  9.81800   27.99300 1.000 20.31000 ? 308 LEU A CA  1 
ATOM   2248 C C   . LEU A 1 308 ? 13.15500  9.29800   28.90800 1.000 20.31000 ? 308 LEU A C   1 
ATOM   2249 O O   . LEU A 1 308 ? 13.05300  9.43200   30.13200 1.000 20.31000 ? 308 LEU A O   1 
ATOM   2250 C CB  . LEU A 1 308 ? 10.91100  8.81200   27.91900 1.000 20.31000 ? 308 LEU A CB  1 
ATOM   2251 C CG  . LEU A 1 308 ? 9.52100   9.42100   27.73500 1.000 20.31000 ? 308 LEU A CG  1 
ATOM   2252 C CD1 . LEU A 1 308 ? 8.44000   8.36400   27.90700 1.000 20.31000 ? 308 LEU A CD1 1 
ATOM   2253 C CD2 . LEU A 1 308 ? 9.32000   10.56600  28.71100 1.000 20.31000 ? 308 LEU A CD2 1 
ATOM   2254 N N   . GLY A 1 309 ? 14.20500  8.70500   28.34100 1.000 19.85000 ? 309 GLY A N   1 
ATOM   2255 C CA  . GLY A 1 309 ? 15.31300  8.26300   29.16700 1.000 19.85000 ? 309 GLY A CA  1 
ATOM   2256 C C   . GLY A 1 309 ? 16.08900  9.42200   29.76100 1.000 19.85000 ? 309 GLY A C   1 
ATOM   2257 O O   . GLY A 1 309 ? 16.53800  9.35300   30.90700 1.000 19.85000 ? 309 GLY A O   1 
ATOM   2258 N N   . GLN A 1 310 ? 16.24900  10.50800  28.99700 1.000 18.64000 ? 310 GLN A N   1 
ATOM   2259 C CA  . GLN A 1 310 ? 16.92600  11.68100  29.53800 1.000 18.64000 ? 310 GLN A CA  1 
ATOM   2260 C C   . GLN A 1 310 ? 16.11800  12.33100  30.65200 1.000 18.64000 ? 310 GLN A C   1 
ATOM   2261 O O   . GLN A 1 310 ? 16.69500  12.87700  31.60100 1.000 18.64000 ? 310 GLN A O   1 
ATOM   2262 C CB  . GLN A 1 310 ? 17.20400  12.69500  28.42900 1.000 18.64000 ? 310 GLN A CB  1 
ATOM   2263 C CG  . GLN A 1 310 ? 18.08000  13.85400  28.87900 1.000 18.64000 ? 310 GLN A CG  1 
ATOM   2264 C CD  . GLN A 1 310 ? 17.65300  15.18200  28.28400 1.000 18.64000 ? 310 GLN A CD  1 
ATOM   2265 O OE1 . GLN A 1 310 ? 16.63700  15.26700  27.59400 1.000 18.64000 ? 310 GLN A OE1 1 
ATOM   2266 N NE2 . GLN A 1 310 ? 18.42700  16.22900  28.55400 1.000 18.64000 ? 310 GLN A NE2 1 
ATOM   2267 N N   . VAL A 1 311 ? 14.79000  12.27700  30.56300 1.000 18.23000 ? 311 VAL A N   1 
ATOM   2268 C CA  . VAL A 1 311 ? 13.96500  12.85800  31.61400 1.000 18.23000 ? 311 VAL A CA  1 
ATOM   2269 C C   . VAL A 1 311 ? 13.97800  11.96900  32.84600 1.000 18.23000 ? 311 VAL A C   1 
ATOM   2270 O O   . VAL A 1 311 ? 14.11000  12.45000  33.97800 1.000 18.23000 ? 311 VAL A O   1 
ATOM   2271 C CB  . VAL A 1 311 ? 12.53500  13.09400  31.09900 1.000 18.23000 ? 311 VAL A CB  1 
ATOM   2272 C CG1 . VAL A 1 311 ? 11.74600  13.93400  32.08900 1.000 18.23000 ? 311 VAL A CG1 1 
ATOM   2273 C CG2 . VAL A 1 311 ? 12.57400  13.75500  29.73600 1.000 18.23000 ? 311 VAL A CG2 1 
ATOM   2274 N N   . THR A 1 312 ? 13.84500  10.65700  32.64900 1.000 17.99000 ? 312 THR A N   1 
ATOM   2275 C CA  . THR A 1 312 ? 13.89700  9.73700   33.77800 1.000 17.99000 ? 312 THR A CA  1 
ATOM   2276 C C   . THR A 1 312 ? 15.28200  9.71700   34.41300 1.000 17.99000 ? 312 THR A C   1 
ATOM   2277 O O   . THR A 1 312 ? 15.40500  9.63800   35.64000 1.000 17.99000 ? 312 THR A O   1 
ATOM   2278 C CB  . THR A 1 312 ? 13.48900  8.33600   33.32200 1.000 17.99000 ? 312 THR A CB  1 
ATOM   2279 O OG1 . THR A 1 312 ? 12.24900  8.41600   32.60800 1.000 17.99000 ? 312 THR A OG1 1 
ATOM   2280 C CG2 . THR A 1 312 ? 13.31200  7.41000   34.51300 1.000 17.99000 ? 312 THR A CG2 1 
ATOM   2281 N N   . SER A 1 313 ? 16.33800  9.81300   33.60000 1.000 17.26000 ? 313 SER A N   1 
ATOM   2282 C CA  . SER A 1 313 ? 17.68400  9.84200   34.16200 1.000 17.26000 ? 313 SER A CA  1 
ATOM   2283 C C   . SER A 1 313 ? 17.92500  11.09600  34.99100 1.000 17.26000 ? 313 SER A C   1 
ATOM   2284 O O   . SER A 1 313 ? 18.66800  11.05100  35.97700 1.000 17.26000 ? 313 SER A O   1 
ATOM   2285 C CB  . SER A 1 313 ? 18.72500  9.74000   33.04700 1.000 17.26000 ? 313 SER A CB  1 
ATOM   2286 O OG  . SER A 1 313 ? 18.64300  8.49200   32.38200 1.000 17.26000 ? 313 SER A OG  1 
ATOM   2287 N N   . LEU A 1 314 ? 17.31400  12.22000  34.61200 1.000 19.12000 ? 314 LEU A N   1 
ATOM   2288 C CA  . LEU A 1 314 ? 17.49600  13.44100  35.38600 1.000 19.12000 ? 314 LEU A CA  1 
ATOM   2289 C C   . LEU A 1 314 ? 16.61200  13.45800  36.62400 1.000 19.12000 ? 314 LEU A C   1 
ATOM   2290 O O   . LEU A 1 314 ? 17.07100  13.83400  37.70800 1.000 19.12000 ? 314 LEU A O   1 
ATOM   2291 C CB  . LEU A 1 314 ? 17.21300  14.66600  34.51700 1.000 19.12000 ? 314 LEU A CB  1 
ATOM   2292 C CG  . LEU A 1 314 ? 18.37800  15.18200  33.67300 1.000 19.12000 ? 314 LEU A CG  1 
ATOM   2293 C CD1 . LEU A 1 314 ? 17.97400  16.45000  32.93800 1.000 19.12000 ? 314 LEU A CD1 1 
ATOM   2294 C CD2 . LEU A 1 314 ? 19.60600  15.42500  34.54100 1.000 19.12000 ? 314 LEU A CD2 1 
ATOM   2295 N N   . GLU A 1 315 ? 15.34700  13.05500  36.48400 1.000 20.16000 ? 315 GLU A N   1 
ATOM   2296 C CA  . GLU A 1 315 ? 14.45100  13.05400  37.63400 1.000 20.16000 ? 315 GLU A CA  1 
ATOM   2297 C C   . GLU A 1 315 ? 14.91400  12.06900  38.69600 1.000 20.16000 ? 315 GLU A C   1 
ATOM   2298 O O   . GLU A 1 315 ? 14.74300  12.32100  39.89300 1.000 20.16000 ? 315 GLU A O   1 
ATOM   2299 C CB  . GLU A 1 315 ? 13.02100  12.72900  37.19500 1.000 20.16000 ? 315 GLU A CB  1 
ATOM   2300 C CG  . GLU A 1 315 ? 12.38100  13.75700  36.26300 1.000 20.16000 ? 315 GLU A CG  1 
ATOM   2301 C CD  . GLU A 1 315 ? 11.87200  14.99400  36.98700 1.000 20.16000 ? 315 GLU A CD  1 
ATOM   2302 O OE1 . GLU A 1 315 ? 12.18800  15.17100  38.18200 1.000 20.16000 ? 315 GLU A OE1 1 
ATOM   2303 O OE2 . GLU A 1 315 ? 11.14600  15.79100  36.35500 1.000 20.16000 ? 315 GLU A OE2 1 
ATOM   2304 N N   . ILE A 1 316 ? 15.52100  10.95700  38.28400 1.000 18.41000 ? 316 ILE A N   1 
ATOM   2305 C CA  . ILE A 1 316 ? 16.01800  9.98500   39.25200 1.000 18.41000 ? 316 ILE A CA  1 
ATOM   2306 C C   . ILE A 1 316 ? 17.25000  10.52600  39.96500 1.000 18.41000 ? 316 ILE A C   1 
ATOM   2307 O O   . ILE A 1 316 ? 17.35300  10.46200  41.19600 1.000 18.41000 ? 316 ILE A O   1 
ATOM   2308 C CB  . ILE A 1 316 ? 16.30400  8.64200   38.56000 1.000 18.41000 ? 316 ILE A CB  1 
ATOM   2309 C CG1 . ILE A 1 316 ? 14.99800  7.88300   38.33100 1.000 18.41000 ? 316 ILE A CG1 1 
ATOM   2310 C CG2 . ILE A 1 316 ? 17.29500  7.81300   39.36600 1.000 18.41000 ? 316 ILE A CG2 1 
ATOM   2311 C CD1 . ILE A 1 316 ? 15.17900  6.59400   37.59200 1.000 18.41000 ? 316 ILE A CD1 1 
ATOM   2312 N N   . ALA A 1 317 ? 18.19700  11.08100  39.20600 1.000 18.59000 ? 317 ALA A N   1 
ATOM   2313 C CA  . ALA A 1 317 ? 19.39800  11.62900  39.82300 1.000 18.59000 ? 317 ALA A CA  1 
ATOM   2314 C C   . ALA A 1 317 ? 19.07800  12.82100  40.71400 1.000 18.59000 ? 317 ALA A C   1 
ATOM   2315 O O   . ALA A 1 317 ? 19.77000  13.05100  41.71200 1.000 18.59000 ? 317 ALA A O   1 
ATOM   2316 C CB  . ALA A 1 317 ? 20.40800  12.02400  38.74600 1.000 18.59000 ? 317 ALA A CB  1 
ATOM   2317 N N   . THR A 1 318 ? 18.03800  13.58500  40.37600 1.000 21.62000 ? 318 THR A N   1 
ATOM   2318 C CA  . THR A 1 318 ? 17.66400  14.72800  41.20100 1.000 21.62000 ? 318 THR A CA  1 
ATOM   2319 C C   . THR A 1 318 ? 16.92500  14.28900  42.46100 1.000 21.62000 ? 318 THR A C   1 
ATOM   2320 O O   . THR A 1 318 ? 17.22000  14.77300  43.55900 1.000 21.62000 ? 318 THR A O   1 
ATOM   2321 C CB  . THR A 1 318 ? 16.81300  15.70900  40.38900 1.000 21.62000 ? 318 THR A CB  1 
ATOM   2322 O OG1 . THR A 1 318 ? 17.62500  16.32500  39.38100 1.000 21.62000 ? 318 THR A OG1 1 
ATOM   2323 C CG2 . THR A 1 318 ? 16.22500  16.78900  41.28700 1.000 21.62000 ? 318 THR A CG2 1 
ATOM   2324 N N   . LYS A 1 319 ? 15.96400  13.36900  42.32500 1.000 22.52000 ? 319 LYS A N   1 
ATOM   2325 C CA  . LYS A 1 319 ? 15.24700  12.88700  43.50200 1.000 22.52000 ? 319 LYS A CA  1 
ATOM   2326 C C   . LYS A 1 319 ? 16.16000  12.11400  44.44200 1.000 22.52000 ? 319 LYS A C   1 
ATOM   2327 O O   . LYS A 1 319 ? 15.94300  12.12200  45.65900 1.000 22.52000 ? 319 LYS A O   1 
ATOM   2328 C CB  . LYS A 1 319 ? 14.06200  12.00900  43.09600 1.000 22.52000 ? 319 LYS A CB  1 
ATOM   2329 C CG  . LYS A 1 319 ? 12.95700  12.73400  42.34700 1.000 22.52000 ? 319 LYS A CG  1 
ATOM   2330 C CD  . LYS A 1 319 ? 12.66000  14.09300  42.95000 1.000 22.52000 ? 319 LYS A CD  1 
ATOM   2331 C CE  . LYS A 1 319 ? 11.50800  14.76300  42.22300 1.000 22.52000 ? 319 LYS A CE  1 
ATOM   2332 N NZ  . LYS A 1 319 ? 11.66100  14.69900  40.74300 1.000 22.52000 ? 319 LYS A NZ  1 
ATOM   2333 N N   . GLU A 1 320 ? 17.17600  11.43600  43.90400 1.000 20.95000 ? 320 GLU A N   1 
ATOM   2334 C CA  . GLU A 1 320 ? 18.04500  10.62400  44.75100 1.000 20.95000 ? 320 GLU A CA  1 
ATOM   2335 C C   . GLU A 1 320 ? 18.92700  11.49100  45.64000 1.000 20.95000 ? 320 GLU A C   1 
ATOM   2336 O O   . GLU A 1 320 ? 19.12500  11.18000  46.82100 1.000 20.95000 ? 320 GLU A O   1 
ATOM   2337 C CB  . GLU A 1 320 ? 18.90100  9.70100   43.88500 1.000 20.95000 ? 320 GLU A CB  1 
ATOM   2338 C CG  . GLU A 1 320 ? 18.99700  8.27800   44.40100 1.000 20.95000 ? 320 GLU A CG  1 
ATOM   2339 C CD  . GLU A 1 320 ? 19.79500  7.38600   43.47400 1.000 20.95000 ? 320 GLU A CD  1 
ATOM   2340 O OE1 . GLU A 1 320 ? 20.63000  7.92000   42.71600 1.000 20.95000 ? 320 GLU A OE1 1 
ATOM   2341 O OE2 . GLU A 1 320 ? 19.58200  6.15500   43.49700 1.000 20.95000 ? 320 GLU A OE2 1 
ATOM   2342 N N   . ASP A 1 321 ? 19.47000  12.58100  45.09200 1.000 23.96000 ? 321 ASP A N   1 
ATOM   2343 C CA  . ASP A 1 321 ? 20.28200  13.48400  45.89900 1.000 23.96000 ? 321 ASP A CA  1 
ATOM   2344 C C   . ASP A 1 321 ? 19.44300  14.23200  46.92800 1.000 23.96000 ? 321 ASP A C   1 
ATOM   2345 O O   . ASP A 1 321 ? 19.95800  14.61400  47.98400 1.000 23.96000 ? 321 ASP A O   1 
ATOM   2346 C CB  . ASP A 1 321 ? 21.02500  14.46400  44.99200 1.000 23.96000 ? 321 ASP A CB  1 
ATOM   2347 C CG  . ASP A 1 321 ? 21.99800  13.76700  44.06200 1.000 23.96000 ? 321 ASP A CG  1 
ATOM   2348 O OD1 . ASP A 1 321 ? 22.58300  12.74400  44.47800 1.000 23.96000 ? 321 ASP A OD1 1 
ATOM   2349 O OD2 . ASP A 1 321 ? 22.17400  14.23600  42.91700 1.000 23.96000 ? 321 ASP A OD2 1 
ATOM   2350 N N   . ASN A 1 322 ? 18.15800  14.46000  46.64000 1.000 26.95000 ? 322 ASN A N   1 
ATOM   2351 C CA  . ASN A 1 322 ? 17.29500  15.10600  47.62400 1.000 26.95000 ? 322 ASN A CA  1 
ATOM   2352 C C   . ASN A 1 322 ? 17.05500  14.20100  48.82400 1.000 26.95000 ? 322 ASN A C   1 
ATOM   2353 O O   . ASN A 1 322 ? 17.09900  14.65800  49.97100 1.000 26.95000 ? 322 ASN A O   1 
ATOM   2354 C CB  . ASN A 1 322 ? 15.96600  15.50200  46.98300 1.000 26.95000 ? 322 ASN A CB  1 
ATOM   2355 C CG  . ASN A 1 322 ? 16.12800  16.56900  45.92100 1.000 26.95000 ? 322 ASN A CG  1 
ATOM   2356 O OD1 . ASN A 1 322 ? 17.05300  17.37800  45.97600 1.000 26.95000 ? 322 ASN A OD1 1 
ATOM   2357 N ND2 . ASN A 1 322 ? 15.22400  16.57800  44.94800 1.000 26.95000 ? 322 ASN A ND2 1 
ATOM   2358 N N   . GLU A 1 323 ? 16.80800  12.91200  48.58300 1.000 28.08000 ? 323 GLU A N   1 
ATOM   2359 C CA  . GLU A 1 323 ? 16.64400  11.97800  49.68900 1.000 28.08000 ? 323 GLU A CA  1 
ATOM   2360 C C   . GLU A 1 323 ? 17.94400  11.78700  50.45800 1.000 28.08000 ? 323 GLU A C   1 
ATOM   2361 O O   . GLU A 1 323 ? 17.91700  11.49600  51.65700 1.000 28.08000 ? 323 GLU A O   1 
ATOM   2362 C CB  . GLU A 1 323 ? 16.13500  10.63300  49.17200 1.000 28.08000 ? 323 GLU A CB  1 
ATOM   2363 C CG  . GLU A 1 323 ? 14.83800  10.71900  48.37500 1.000 28.08000 ? 323 GLU A CG  1 
ATOM   2364 C CD  . GLU A 1 323 ? 14.40100  9.37800   47.80900 1.000 28.08000 ? 323 GLU A CD  1 
ATOM   2365 O OE1 . GLU A 1 323 ? 14.87400  8.33600   48.31100 1.000 28.08000 ? 323 GLU A OE1 1 
ATOM   2366 O OE2 . GLU A 1 323 ? 13.58700  9.36600   46.86000 1.000 28.08000 ? 323 GLU A OE2 1 
ATOM   2367 N N   . ASP A 1 324 ? 19.08800  11.93400  49.78900 1.000 28.63000 ? 324 ASP A N   1 
ATOM   2368 C CA  . ASP A 1 324 ? 20.36100  11.68600  50.45500 1.000 28.63000 ? 324 ASP A CA  1 
ATOM   2369 C C   . ASP A 1 324 ? 20.85200  12.91900  51.20700 1.000 28.63000 ? 324 ASP A C   1 
ATOM   2370 O O   . ASP A 1 324 ? 21.25800  12.82200  52.37000 1.000 28.63000 ? 324 ASP A O   1 
ATOM   2371 C CB  . ASP A 1 324 ? 21.40200  11.22500  49.43300 1.000 28.63000 ? 324 ASP A CB  1 
ATOM   2372 C CG  . ASP A 1 324 ? 22.63200  10.62700  50.08400 1.000 28.63000 ? 324 ASP A CG  1 
ATOM   2373 O OD1 . ASP A 1 324 ? 22.54400  9.49300   50.60300 1.000 28.63000 ? 324 ASP A OD1 1 
ATOM   2374 O OD2 . ASP A 1 324 ? 23.68900  11.29000  50.07200 1.000 28.63000 ? 324 ASP A OD2 1 
ATOM   2375 N N   . SER A 1 325 ? 20.82400  14.08800  50.55800 1.000 28.54000 ? 325 SER A N   1 
ATOM   2376 C CA  . SER A 1 325 ? 21.28600  15.30200  51.22500 1.000 28.54000 ? 325 SER A CA  1 
ATOM   2377 C C   . SER A 1 325 ? 20.36900  15.68000  52.37900 1.000 28.54000 ? 325 SER A C   1 
ATOM   2378 O O   . SER A 1 325 ? 20.83900  16.12400  53.43400 1.000 28.54000 ? 325 SER A O   1 
ATOM   2379 C CB  . SER A 1 325 ? 21.38500  16.45200  50.22200 1.000 28.54000 ? 325 SER A CB  1 
ATOM   2380 O OG  . SER A 1 325 ? 22.42700  16.22000  49.29100 1.000 28.54000 ? 325 SER A OG  1 
ATOM   2381 N N   . GLU A 1 326 ? 19.05900  15.49800  52.20600 1.000 29.66000 ? 326 GLU A N   1 
ATOM   2382 C CA  . GLU A 1 326 ? 18.13800  15.72600  53.31200 1.000 29.66000 ? 326 GLU A CA  1 
ATOM   2383 C C   . GLU A 1 326 ? 18.37300  14.73500  54.44200 1.000 29.66000 ? 326 GLU A C   1 
ATOM   2384 O O   . GLU A 1 326 ? 18.23800  15.09300  55.61700 1.000 29.66000 ? 326 GLU A O   1 
ATOM   2385 C CB  . GLU A 1 326 ? 16.69700  15.65400  52.80300 1.000 29.66000 ? 326 GLU A CB  1 
ATOM   2386 C CG  . GLU A 1 326 ? 15.66000  15.21900  53.81600 1.000 29.66000 ? 326 GLU A CG  1 
ATOM   2387 C CD  . GLU A 1 326 ? 14.33400  14.88100  53.16300 1.000 29.66000 ? 326 GLU A CD  1 
ATOM   2388 O OE1 . GLU A 1 326 ? 14.20700  15.08200  51.93500 1.000 29.66000 ? 326 GLU A OE1 1 
ATOM   2389 O OE2 . GLU A 1 326 ? 13.42200  14.41100  53.87300 1.000 29.66000 ? 326 GLU A OE2 1 
ATOM   2390 N N   . SER A 1 327 ? 18.73900  13.49300  54.11300 1.000 28.55000 ? 327 SER A N   1 
ATOM   2391 C CA  . SER A 1 327 ? 19.13800  12.55000  55.15100 1.000 28.55000 ? 327 SER A CA  1 
ATOM   2392 C C   . SER A 1 327 ? 20.46500  12.95200  55.78100 1.000 28.55000 ? 327 SER A C   1 
ATOM   2393 O O   . SER A 1 327 ? 20.67000  12.76300  56.98500 1.000 28.55000 ? 327 SER A O   1 
ATOM   2394 C CB  . SER A 1 327 ? 19.23000  11.14000  54.57000 1.000 28.55000 ? 327 SER A CB  1 
ATOM   2395 O OG  . SER A 1 327 ? 18.01500  10.76400  53.94600 1.000 28.55000 ? 327 SER A OG  1 
ATOM   2396 N N   . LYS A 1 328 ? 21.37300  13.51900  54.98500 1.000 27.23000 ? 328 LYS A N   1 
ATOM   2397 C CA  . LYS A 1 328 ? 22.68500  13.88300  55.50700 1.000 27.23000 ? 328 LYS A CA  1 
ATOM   2398 C C   . LYS A 1 328 ? 22.60500  15.13200  56.37300 1.000 27.23000 ? 328 LYS A C   1 
ATOM   2399 O O   . LYS A 1 328 ? 23.24000  15.20300  57.43200 1.000 27.23000 ? 328 LYS A O   1 
ATOM   2400 C CB  . LYS A 1 328 ? 23.66500  14.07900  54.35000 1.000 27.23000 ? 328 LYS A CB  1 
ATOM   2401 C CG  . LYS A 1 328 ? 25.12200  13.84800  54.70900 1.000 27.23000 ? 328 LYS A CG  1 
ATOM   2402 C CD  . LYS A 1 328 ? 25.93200  13.51700  53.46500 1.000 27.23000 ? 328 LYS A CD  1 
ATOM   2403 C CE  . LYS A 1 328 ? 25.35900  12.29900  52.75100 1.000 27.23000 ? 328 LYS A CE  1 
ATOM   2404 N NZ  . LYS A 1 328 ? 26.05300  12.01700  51.46400 1.000 27.23000 ? 328 LYS A NZ  1 
ATOM   2405 N N   . ILE A 1 329 ? 21.83000  16.12900  55.93900 1.000 26.09000 ? 329 ILE A N   1 
ATOM   2406 C CA  . ILE A 1 329 ? 21.63300  17.32000  56.75700 1.000 26.09000 ? 329 ILE A CA  1 
ATOM   2407 C C   . ILE A 1 329 ? 20.85000  16.98500  58.02200 1.000 26.09000 ? 329 ILE A C   1 
ATOM   2408 O O   . ILE A 1 329 ? 21.08200  17.58200  59.08000 1.000 26.09000 ? 329 ILE A O   1 
ATOM   2409 C CB  . ILE A 1 329 ? 20.94300  18.41800  55.92500 1.000 26.09000 ? 329 ILE A CB  1 
ATOM   2410 C CG1 . ILE A 1 329 ? 21.80400  18.78600  54.71500 1.000 26.09000 ? 329 ILE A CG1 1 
ATOM   2411 C CG2 . ILE A 1 329 ? 20.67900  19.65700  56.76600 1.000 26.09000 ? 329 ILE A CG2 1 
ATOM   2412 C CD1 . ILE A 1 329 ? 21.08000  19.62100  53.68500 1.000 26.09000 ? 329 ILE A CD1 1 
ATOM   2413 N N   . GLU A 1 330 ? 19.93000  16.01800  57.94800 1.000 26.65000 ? 330 GLU A N   1 
ATOM   2414 C CA  . GLU A 1 330 ? 19.15200  15.65700  59.13000 1.000 26.65000 ? 330 GLU A CA  1 
ATOM   2415 C C   . GLU A 1 330 ? 20.01900  14.97500  60.18000 1.000 26.65000 ? 330 GLU A C   1 
ATOM   2416 O O   . GLU A 1 330 ? 19.89900  15.26500  61.37600 1.000 26.65000 ? 330 GLU A O   1 
ATOM   2417 C CB  . GLU A 1 330 ? 17.98100  14.75600  58.73700 1.000 26.65000 ? 330 GLU A CB  1 
ATOM   2418 C CG  . GLU A 1 330 ? 17.29100  14.07200  59.91100 1.000 26.65000 ? 330 GLU A CG  1 
ATOM   2419 C CD  . GLU A 1 330 ? 16.65300  15.05400  60.87700 1.000 26.65000 ? 330 GLU A CD  1 
ATOM   2420 O OE1 . GLU A 1 330 ? 16.28400  16.16700  60.44400 1.000 26.65000 ? 330 GLU A OE1 1 
ATOM   2421 O OE2 . GLU A 1 330 ? 16.52000  14.71200  62.07100 1.000 26.65000 ? 330 GLU A OE2 1 
ATOM   2422 N N   . ILE A 1 331 ? 20.89900  14.06400  59.75500 1.000 23.74000 ? 331 ILE A N   1 
ATOM   2423 C CA  . ILE A 1 331 ? 21.83100  13.44400  60.69300 1.000 23.74000 ? 331 ILE A CA  1 
ATOM   2424 C C   . ILE A 1 331 ? 22.79400  14.48400  61.24800 1.000 23.74000 ? 331 ILE A C   1 
ATOM   2425 O O   . ILE A 1 331 ? 23.19600  14.41300  62.41700 1.000 23.74000 ? 331 ILE A O   1 
ATOM   2426 C CB  . ILE A 1 331 ? 22.57700  12.27900  60.00800 1.000 23.74000 ? 331 ILE A CB  1 
ATOM   2427 C CG1 . ILE A 1 331 ? 21.59300  11.18300  59.59100 1.000 23.74000 ? 331 ILE A CG1 1 
ATOM   2428 C CG2 . ILE A 1 331 ? 23.64300  11.69800  60.92000 1.000 23.74000 ? 331 ILE A CG2 1 
ATOM   2429 C CD1 . ILE A 1 331 ? 20.82700  10.57400  60.74400 1.000 23.74000 ? 331 ILE A CD1 1 
ATOM   2430 N N   . LYS A 1 332 ? 23.16900  15.47300  60.43100 1.000 23.56000 ? 332 LYS A N   1 
ATOM   2431 C CA  . LYS A 1 332 ? 24.02400  16.55100  60.91700 1.000 23.56000 ? 332 LYS A CA  1 
ATOM   2432 C C   . LYS A 1 332 ? 23.31700  17.42300  61.94800 1.000 23.56000 ? 332 LYS A C   1 
ATOM   2433 O O   . LYS A 1 332 ? 23.97000  17.95800  62.85200 1.000 23.56000 ? 332 LYS A O   1 
ATOM   2434 C CB  . LYS A 1 332 ? 24.50700  17.40100  59.74100 1.000 23.56000 ? 332 LYS A CB  1 
ATOM   2435 C CG  . LYS A 1 332 ? 25.87400  17.00400  59.21200 1.000 23.56000 ? 332 LYS A CG  1 
ATOM   2436 C CD  . LYS A 1 332 ? 26.96000  17.32300  60.23000 1.000 23.56000 ? 332 LYS A CD  1 
ATOM   2437 C CE  . LYS A 1 332 ? 28.33200  16.87700  59.75200 1.000 23.56000 ? 332 LYS A CE  1 
ATOM   2438 N NZ  . LYS A 1 332 ? 28.43800  15.39500  59.66500 1.000 23.56000 ? 332 LYS A NZ  1 
ATOM   2439 N N   . SER A 1 333 ? 21.99600  17.57300  61.83900 1.000 23.78000 ? 333 SER A N   1 
ATOM   2440 C CA  . SER A 1 333 ? 21.28700  18.44400  62.76800 1.000 23.78000 ? 333 SER A CA  1 
ATOM   2441 C C   . SER A 1 333 ? 21.10500  17.78600  64.13000 1.000 23.78000 ? 333 SER A C   1 
ATOM   2442 O O   . SER A 1 333 ? 21.28000  18.44200  65.16200 1.000 23.78000 ? 333 SER A O   1 
ATOM   2443 C CB  . SER A 1 333 ? 19.92800  18.84800  62.19200 1.000 23.78000 ? 333 SER A CB  1 
ATOM   2444 O OG  . SER A 1 333 ? 19.00000  17.78100  62.27900 1.000 23.78000 ? 333 SER A OG  1 
ATOM   2445 N N   . VAL A 1 334 ? 20.75600  16.49700  64.15500 1.000 24.60000 ? 334 VAL A N   1 
ATOM   2446 C CA  . VAL A 1 334 ? 20.53700  15.82700  65.43400 1.000 24.60000 ? 334 VAL A CA  1 
ATOM   2447 C C   . VAL A 1 334 ? 21.82800  15.73900  66.23300 1.000 24.60000 ? 334 VAL A C   1 
ATOM   2448 O O   . VAL A 1 334 ? 21.79800  15.73800  67.47000 1.000 24.60000 ? 334 VAL A O   1 
ATOM   2449 C CB  . VAL A 1 334 ? 19.91000  14.43700  65.22200 1.000 24.60000 ? 334 VAL A CB  1 
ATOM   2450 C CG1 . VAL A 1 334 ? 18.51400  14.57200  64.63700 1.000 24.60000 ? 334 VAL A CG1 1 
ATOM   2451 C CG2 . VAL A 1 334 ? 20.78900  13.58200  64.32600 1.000 24.60000 ? 334 VAL A CG2 1 
ATOM   2452 N N   . LEU A 1 335 ? 22.97900  15.65300  65.56000 1.000 23.42000 ? 335 LEU A N   1 
ATOM   2453 C CA  . LEU A 1 335 ? 24.24000  15.72900  66.28700 1.000 23.42000 ? 335 LEU A CA  1 
ATOM   2454 C C   . LEU A 1 335 ? 24.42100  17.10000  66.92400 1.000 23.42000 ? 335 LEU A C   1 
ATOM   2455 O O   . LEU A 1 335 ? 24.97800  17.21000  68.02100 1.000 23.42000 ? 335 LEU A O   1 
ATOM   2456 C CB  . LEU A 1 335 ? 25.41200  15.40800  65.35900 1.000 23.42000 ? 335 LEU A CB  1 
ATOM   2457 C CG  . LEU A 1 335 ? 26.79100  15.24200  66.01100 1.000 23.42000 ? 335 LEU A CG  1 
ATOM   2458 C CD1 . LEU A 1 335 ? 27.57900  14.14400  65.31800 1.000 23.42000 ? 335 LEU A CD1 1 
ATOM   2459 C CD2 . LEU A 1 335 ? 27.57900  16.54600  65.99100 1.000 23.42000 ? 335 LEU A CD2 1 
ATOM   2460 N N   . ALA A 1 336 ? 23.95100  18.15600  66.25500 1.000 25.28000 ? 336 ALA A N   1 
ATOM   2461 C CA  . ALA A 1 336 ? 24.09100  19.49500  66.81900 1.000 25.28000 ? 336 ALA A CA  1 
ATOM   2462 C C   . ALA A 1 336 ? 23.22800  19.66700  68.06100 1.000 25.28000 ? 336 ALA A C   1 
ATOM   2463 O O   . ALA A 1 336 ? 23.65700  20.29100  69.03900 1.000 25.28000 ? 336 ALA A O   1 
ATOM   2464 C CB  . ALA A 1 336 ? 23.74100  20.54700  65.76800 1.000 25.28000 ? 336 ALA A CB  1 
ATOM   2465 N N   . LYS A 1 337 ? 22.00700  19.12100  68.04600 1.000 26.43000 ? 337 LYS A N   1 
ATOM   2466 C CA  . LYS A 1 337 ? 21.17400  19.17400  69.24200 1.000 26.43000 ? 337 LYS A CA  1 
ATOM   2467 C C   . LYS A 1 337 ? 21.78500  18.36100  70.37300 1.000 26.43000 ? 337 LYS A C   1 
ATOM   2468 O O   . LYS A 1 337 ? 21.63600  18.72200  71.54600 1.000 26.43000 ? 337 LYS A O   1 
ATOM   2469 C CB  . LYS A 1 337 ? 19.76200  18.66800  68.93800 1.000 26.43000 ? 337 LYS A CB  1 
ATOM   2470 C CG  . LYS A 1 337 ? 19.28800  18.89400  67.50900 1.000 26.43000 ? 337 LYS A CG  1 
ATOM   2471 C CD  . LYS A 1 337 ? 19.13900  20.36900  67.16700 1.000 26.43000 ? 337 LYS A CD  1 
ATOM   2472 C CE  . LYS A 1 337 ? 18.69700  20.54800  65.72000 1.000 26.43000 ? 337 LYS A CE  1 
ATOM   2473 N NZ  . LYS A 1 337 ? 18.53300  21.98100  65.34300 1.000 26.43000 ? 337 LYS A NZ  1 
ATOM   2474 N N   . LEU A 1 338 ? 22.47300  17.26600  70.04400 1.000 25.61000 ? 338 LEU A N   1 
ATOM   2475 C CA  . LEU A 1 338 ? 23.16000  16.49100  71.07100 1.000 25.61000 ? 338 LEU A CA  1 
ATOM   2476 C C   . LEU A 1 338 ? 24.32500  17.27000  71.66700 1.000 25.61000 ? 338 LEU A C   1 
ATOM   2477 O O   . LEU A 1 338 ? 24.56300  17.20900  72.87800 1.000 25.61000 ? 338 LEU A O   1 
ATOM   2478 C CB  . LEU A 1 338 ? 23.64800  15.16500  70.48700 1.000 25.61000 ? 338 LEU A CB  1 
ATOM   2479 C CG  . LEU A 1 338 ? 22.63000  14.02800  70.40300 1.000 25.61000 ? 338 LEU A CG  1 
ATOM   2480 C CD1 . LEU A 1 338 ? 23.19000  12.86200  69.60400 1.000 25.61000 ? 338 LEU A CD1 1 
ATOM   2481 C CD2 . LEU A 1 338 ? 22.24300  13.57800  71.80000 1.000 25.61000 ? 338 LEU A CD2 1 
ATOM   2482 N N   . VAL A 1 339 ? 25.06000  18.00900  70.83300 1.000 26.23000 ? 339 VAL A N   1 
ATOM   2483 C CA  . VAL A 1 339 ? 26.21300  18.75000  71.32900 1.000 26.23000 ? 339 VAL A CA  1 
ATOM   2484 C C   . VAL A 1 339 ? 25.77300  19.86800  72.26700 1.000 26.23000 ? 339 VAL A C   1 
ATOM   2485 O O   . VAL A 1 339 ? 26.42200  20.13000  73.28800 1.000 26.23000 ? 339 VAL A O   1 
ATOM   2486 C CB  . VAL A 1 339 ? 27.04900  19.28200  70.15000 1.000 26.23000 ? 339 VAL A CB  1 
ATOM   2487 C CG1 . VAL A 1 339 ? 28.09600  20.27500  70.63100 1.000 26.23000 ? 339 VAL A CG1 1 
ATOM   2488 C CG2 . VAL A 1 339 ? 27.71600  18.12800  69.41700 1.000 26.23000 ? 339 VAL A CG2 1 
ATOM   2489 N N   . GLU A 1 340 ? 24.66100  20.53800  71.94800 1.000 30.14000 ? 340 GLU A N   1 
ATOM   2490 C CA  . GLU A 1 340 ? 24.17300  21.58900  72.83500 1.000 30.14000 ? 340 GLU A CA  1 
ATOM   2491 C C   . GLU A 1 340 ? 23.60300  21.01500  74.12700 1.000 30.14000 ? 340 GLU A C   1 
ATOM   2492 O O   . GLU A 1 340 ? 23.61600  21.69200  75.16100 1.000 30.14000 ? 340 GLU A O   1 
ATOM   2493 C CB  . GLU A 1 340 ? 23.12800  22.45200  72.12100 1.000 30.14000 ? 340 GLU A CB  1 
ATOM   2494 C CG  . GLU A 1 340 ? 21.75000  21.82200  71.99800 1.000 30.14000 ? 340 GLU A CG  1 
ATOM   2495 C CD  . GLU A 1 340 ? 20.72800  22.76000  71.38300 1.000 30.14000 ? 340 GLU A CD  1 
ATOM   2496 O OE1 . GLU A 1 340 ? 21.08700  23.91800  71.08300 1.000 30.14000 ? 340 GLU A OE1 1 
ATOM   2497 O OE2 . GLU A 1 340 ? 19.56600  22.33800  71.20200 1.000 30.14000 ? 340 GLU A OE2 1 
ATOM   2498 N N   . TYR A 1 341 ? 23.11000  19.77400  74.09200 1.000 29.36000 ? 341 TYR A N   1 
ATOM   2499 C CA  . TYR A 1 341 ? 22.59300  19.15600  75.30800 1.000 29.36000 ? 341 TYR A CA  1 
ATOM   2500 C C   . TYR A 1 341 ? 23.70300  18.90200  76.31800 1.000 29.36000 ? 341 TYR A C   1 
ATOM   2501 O O   . TYR A 1 341 ? 23.48400  19.00800  77.53000 1.000 29.36000 ? 341 TYR A O   1 
ATOM   2502 C CB  . TYR A 1 341 ? 21.87500  17.85100  74.97100 1.000 29.36000 ? 341 TYR A CB  1 
ATOM   2503 C CG  . TYR A 1 341 ? 20.56200  18.04500  74.25500 1.000 29.36000 ? 341 TYR A CG  1 
ATOM   2504 C CD1 . TYR A 1 341 ? 19.88300  19.25300  74.33200 1.000 29.36000 ? 341 TYR A CD1 1 
ATOM   2505 C CD2 . TYR A 1 341 ? 20.00200  17.02300  73.50100 1.000 29.36000 ? 341 TYR A CD2 1 
ATOM   2506 C CE1 . TYR A 1 341 ? 18.68400  19.43900  73.68000 1.000 29.36000 ? 341 TYR A CE1 1 
ATOM   2507 C CE2 . TYR A 1 341 ? 18.80400  17.20000  72.84300 1.000 29.36000 ? 341 TYR A CE2 1 
ATOM   2508 C CZ  . TYR A 1 341 ? 18.14700  18.41000  72.93800 1.000 29.36000 ? 341 TYR A CZ  1 
ATOM   2509 O OH  . TYR A 1 341 ? 16.95000  18.59800  72.28900 1.000 29.36000 ? 341 TYR A OH  1 
ATOM   2510 N N   . MET A 1 342 ? 24.90500  18.59800  75.84000 1.000 31.73000 ? 342 MET A N   1 
ATOM   2511 C CA  . MET A 1 342 ? 26.01700  18.29600  76.72900 1.000 31.73000 ? 342 MET A CA  1 
ATOM   2512 C C   . MET A 1 342 ? 27.06000  19.40500  76.68300 1.000 31.73000 ? 342 MET A C   1 
ATOM   2513 O O   . MET A 1 342 ? 26.74500  20.57200  76.92000 1.000 31.73000 ? 342 MET A O   1 
ATOM   2514 C CB  . MET A 1 342 ? 26.64800  16.94900  76.36400 1.000 31.73000 ? 342 MET A CB  1 
ATOM   2515 C CG  . MET A 1 342 ? 27.03400  16.81000  74.90000 1.000 31.73000 ? 342 MET A CG  1 
ATOM   2516 S SD  . MET A 1 342 ? 27.96500  15.30000  74.57800 1.000 31.73000 ? 342 MET A SD  1 
ATOM   2517 C CE  . MET A 1 342 ? 29.31500  15.50200  75.73700 1.000 31.73000 ? 342 MET A CE  1 
ATOM   2518 N N   . ILE A 1 349 ? 26.49100  12.68500  79.47300 1.000 28.24000 ? 349 ILE A N   1 
ATOM   2519 C CA  . ILE A 1 349 ? 25.58300  11.54800  79.58200 1.000 28.24000 ? 349 ILE A CA  1 
ATOM   2520 C C   . ILE A 1 349 ? 24.14500  12.04200  79.67200 1.000 28.24000 ? 349 ILE A C   1 
ATOM   2521 O O   . ILE A 1 349 ? 23.20300  11.31800  79.34400 1.000 28.24000 ? 349 ILE A O   1 
ATOM   2522 C CB  . ILE A 1 349 ? 25.92800  10.66700  80.79800 1.000 28.24000 ? 349 ILE A CB  1 
ATOM   2523 C CG1 . ILE A 1 349 ? 27.42400  10.35700  80.83400 1.000 28.24000 ? 349 ILE A CG1 1 
ATOM   2524 C CG2 . ILE A 1 349 ? 25.12300  9.37200   80.77400 1.000 28.24000 ? 349 ILE A CG2 1 
ATOM   2525 C CD1 . ILE A 1 349 ? 27.83400  9.51600   82.02300 1.000 28.24000 ? 349 ILE A CD1 1 
ATOM   2526 N N   . ASP A 1 350 ? 23.98400  13.28900  80.11400 1.000 32.04000 ? 350 ASP A N   1 
ATOM   2527 C CA  . ASP A 1 350 ? 22.66400  13.83400  80.39600 1.000 32.04000 ? 350 ASP A CA  1 
ATOM   2528 C C   . ASP A 1 350 ? 21.79300  13.87300  79.14500 1.000 32.04000 ? 350 ASP A C   1 
ATOM   2529 O O   . ASP A 1 350 ? 20.78300  13.16700  79.06800 1.000 32.04000 ? 350 ASP A O   1 
ATOM   2530 C CB  . ASP A 1 350 ? 22.78500  15.23700  81.00200 1.000 32.04000 ? 350 ASP A CB  1 
ATOM   2531 C CG  . ASP A 1 350 ? 21.62600  15.57700  81.92600 1.000 32.04000 ? 350 ASP A CG  1 
ATOM   2532 O OD1 . ASP A 1 350 ? 20.80100  14.68000  82.19800 1.000 32.04000 ? 350 ASP A OD1 1 
ATOM   2533 O OD2 . ASP A 1 350 ? 21.54600  16.74000  82.38100 1.000 32.04000 ? 350 ASP A OD2 1 
ATOM   2534 N N   . GLY A 1 351 ? 22.17900  14.67900  78.15500 1.000 28.54000 ? 351 GLY A N   1 
ATOM   2535 C CA  . GLY A 1 351 ? 21.34400  14.85400  76.98000 1.000 28.54000 ? 351 GLY A CA  1 
ATOM   2536 C C   . GLY A 1 351 ? 21.44400  13.76900  75.92900 1.000 28.54000 ? 351 GLY A C   1 
ATOM   2537 O O   . GLY A 1 351 ? 20.62300  13.74900  75.00600 1.000 28.54000 ? 351 GLY A O   1 
ATOM   2538 N N   . LEU A 1 352 ? 22.42800  12.87200  76.03700 1.000 25.71000 ? 352 LEU A N   1 
ATOM   2539 C CA  . LEU A 1 352 ? 22.58200  11.82400  75.03200 1.000 25.71000 ? 352 LEU A CA  1 
ATOM   2540 C C   . LEU A 1 352 ? 21.42600  10.83100  75.06800 1.000 25.71000 ? 352 LEU A C   1 
ATOM   2541 O O   . LEU A 1 352 ? 20.94200  10.40000  74.01600 1.000 25.71000 ? 352 LEU A O   1 
ATOM   2542 C CB  . LEU A 1 352 ? 23.90800  11.09200  75.23400 1.000 25.71000 ? 352 LEU A CB  1 
ATOM   2543 C CG  . LEU A 1 352 ? 25.18500  11.80700  74.79700 1.000 25.71000 ? 352 LEU A CG  1 
ATOM   2544 C CD1 . LEU A 1 352 ? 26.40800  11.05500  75.29100 1.000 25.71000 ? 352 LEU A CD1 1 
ATOM   2545 C CD2 . LEU A 1 352 ? 25.22300  11.94900  73.28500 1.000 25.71000 ? 352 LEU A CD2 1 
ATOM   2546 N N   . ILE A 1 353 ? 20.96100  10.46700  76.26100 1.000 26.28000 ? 353 ILE A N   1 
ATOM   2547 C CA  . ILE A 1 353 ? 19.97400  9.40400   76.41900 1.000 26.28000 ? 353 ILE A CA  1 
ATOM   2548 C C   . ILE A 1 353 ? 18.62100  9.91900   76.87200 1.000 26.28000 ? 353 ILE A C   1 
ATOM   2549 O O   . ILE A 1 353 ? 17.69500  9.11300   77.04800 1.000 26.28000 ? 353 ILE A O   1 
ATOM   2550 C CB  . ILE A 1 353 ? 20.47800  8.31900   77.38900 1.000 26.28000 ? 353 ILE A CB  1 
ATOM   2551 C CG1 . ILE A 1 353 ? 20.91600  8.95700   78.70900 1.000 26.28000 ? 353 ILE A CG1 1 
ATOM   2552 C CG2 . ILE A 1 353 ? 21.61800  7.53300   76.76500 1.000 26.28000 ? 353 ILE A CG2 1 
ATOM   2553 C CD1 . ILE A 1 353 ? 21.44100  7.96700   79.72300 1.000 26.28000 ? 353 ILE A CD1 1 
ATOM   2554 N N   . ASN A 1 354 ? 18.46300  11.22800  77.05900 1.000 32.12000 ? 354 ASN A N   1 
ATOM   2555 C CA  . ASN A 1 354 ? 17.27100  11.76200  77.71100 1.000 32.12000 ? 354 ASN A CA  1 
ATOM   2556 C C   . ASN A 1 354 ? 16.43900  12.64500  76.79100 1.000 32.12000 ? 354 ASN A C   1 
ATOM   2557 O O   . ASN A 1 354 ? 15.27300  12.32800  76.53500 1.000 32.12000 ? 354 ASN A O   1 
ATOM   2558 C CB  . ASN A 1 354 ? 17.67900  12.52500  78.97700 1.000 32.12000 ? 354 ASN A CB  1 
ATOM   2559 C CG  . ASN A 1 354 ? 18.32700  11.62600  80.01600 1.000 32.12000 ? 354 ASN A CG  1 
ATOM   2560 O OD1 . ASN A 1 354 ? 17.90400  10.48700  80.21800 1.000 32.12000 ? 354 ASN A OD1 1 
ATOM   2561 N ND2 . ASN A 1 354 ? 19.36300  12.13200  80.67500 1.000 32.12000 ? 354 ASN A ND2 1 
ATOM   2562 N N   . LYS A 1 355 ? 16.99300  13.74600  76.29000 1.000 33.43000 ? 355 LYS A N   1 
ATOM   2563 C CA  . LYS A 1 355 ? 16.21300  14.70800  75.52700 1.000 33.43000 ? 355 LYS A CA  1 
ATOM   2564 C C   . LYS A 1 355 ? 15.91400  14.18200  74.12100 1.000 33.43000 ? 355 LYS A C   1 
ATOM   2565 O O   . LYS A 1 355 ? 16.50900  13.20900  73.64900 1.000 33.43000 ? 355 LYS A O   1 
ATOM   2566 C CB  . LYS A 1 355 ? 16.92400  16.05800  75.48600 1.000 33.43000 ? 355 LYS A CB  1 
ATOM   2567 C CG  . LYS A 1 355 ? 16.68600  16.88100  76.74800 1.000 33.43000 ? 355 LYS A CG  1 
ATOM   2568 C CD  . LYS A 1 355 ? 17.33500  18.25200  76.68300 1.000 33.43000 ? 355 LYS A CD  1 
ATOM   2569 C CE  . LYS A 1 355 ? 16.74000  19.19000  77.72800 1.000 33.43000 ? 355 LYS A CE  1 
ATOM   2570 N NZ  . LYS A 1 355 ? 16.73600  18.59800  79.09700 1.000 33.43000 ? 355 LYS A NZ  1 
ATOM   2571 N N   . GLN A 1 356 ? 14.96600  14.84900  73.45600 1.000 38.83000 ? 356 GLN A N   1 
ATOM   2572 C CA  . GLN A 1 356 ? 14.27100  14.27900  72.30000 1.000 38.83000 ? 356 GLN A CA  1 
ATOM   2573 C C   . GLN A 1 356 ? 15.19300  13.79200  71.18700 1.000 38.83000 ? 356 GLN A C   1 
ATOM   2574 O O   . GLN A 1 356 ? 15.00600  12.65500  70.72500 1.000 38.83000 ? 356 GLN A O   1 
ATOM   2575 C CB  . GLN A 1 356 ? 13.25600  15.30700  71.77400 1.000 38.83000 ? 356 GLN A CB  1 
ATOM   2576 C CG  . GLN A 1 356 ? 11.87900  15.21700  72.40400 1.000 38.83000 ? 356 GLN A CG  1 
ATOM   2577 C CD  . GLN A 1 356 ? 11.03700  14.12000  71.78800 1.000 38.83000 ? 356 GLN A CD  1 
ATOM   2578 O OE1 . GLN A 1 356 ? 11.21000  12.94100  72.09500 1.000 38.83000 ? 356 GLN A OE1 1 
ATOM   2579 N NE2 . GLN A 1 356 ? 10.12400  14.50400  70.90400 1.000 38.83000 ? 356 GLN A NE2 1 
ATOM   2580 N N   . PRO A 1 357 ? 16.18600  14.55900  70.70700 1.000 30.56000 ? 357 PRO A N   1 
ATOM   2581 C CA  . PRO A 1 357 ? 17.17200  13.95100  69.80400 1.000 30.56000 ? 357 PRO A CA  1 
ATOM   2582 C C   . PRO A 1 357 ? 18.21900  13.18000  70.58900 1.000 30.56000 ? 357 PRO A C   1 
ATOM   2583 O O   . PRO A 1 357 ? 19.24200  13.74500  70.98800 1.000 30.56000 ? 357 PRO A O   1 
ATOM   2584 C CB  . PRO A 1 357 ? 17.77800  15.15600  69.06800 1.000 30.56000 ? 357 PRO A CB  1 
ATOM   2585 C CG  . PRO A 1 357 ? 16.85300  16.30100  69.35100 1.000 30.56000 ? 357 PRO A CG  1 
ATOM   2586 C CD  . PRO A 1 357 ? 16.31900  16.02400  70.71500 1.000 30.56000 ? 357 PRO A CD  1 
ATOM   2587 N N   . ASN A 1 358 ? 17.96300  11.89600  70.83300 1.000 24.17000 ? 358 ASN A N   1 
ATOM   2588 C CA  . ASN A 1 358 ? 18.83500  11.07100  71.65500 1.000 24.17000 ? 358 ASN A CA  1 
ATOM   2589 C C   . ASN A 1 358 ? 19.92800  10.42100  70.80600 1.000 24.17000 ? 358 ASN A C   1 
ATOM   2590 O O   . ASN A 1 358 ? 19.95700  10.53400  69.57800 1.000 24.17000 ? 358 ASN A O   1 
ATOM   2591 C CB  . ASN A 1 358 ? 18.02200  10.02200  72.41100 1.000 24.17000 ? 358 ASN A CB  1 
ATOM   2592 C CG  . ASN A 1 358 ? 17.20200  9.16000   71.49500 1.000 24.17000 ? 358 ASN A CG  1 
ATOM   2593 O OD1 . ASN A 1 358 ? 17.74300  8.43700   70.66600 1.000 24.17000 ? 358 ASN A OD1 1 
ATOM   2594 N ND2 . ASN A 1 358 ? 15.88500  9.22900   71.63600 1.000 24.17000 ? 358 ASN A ND2 1 
ATOM   2595 N N   . ILE A 1 359 ? 20.84500  9.72700   71.48500 1.000 21.45000 ? 359 ILE A N   1 
ATOM   2596 C CA  . ILE A 1 359 ? 22.05600  9.22300   70.84200 1.000 21.45000 ? 359 ILE A CA  1 
ATOM   2597 C C   . ILE A 1 359 ? 21.74400  8.20500   69.75000 1.000 21.45000 ? 359 ILE A C   1 
ATOM   2598 O O   . ILE A 1 359 ? 22.46900  8.12200   68.75100 1.000 21.45000 ? 359 ILE A O   1 
ATOM   2599 C CB  . ILE A 1 359 ? 23.00400  8.64000   71.91300 1.000 21.45000 ? 359 ILE A CB  1 
ATOM   2600 C CG1 . ILE A 1 359 ? 24.36600  8.29800   71.31000 1.000 21.45000 ? 359 ILE A CG1 1 
ATOM   2601 C CG2 . ILE A 1 359 ? 22.39000  7.41200   72.58300 1.000 21.45000 ? 359 ILE A CG2 1 
ATOM   2602 C CD1 . ILE A 1 359 ? 25.38300  7.86600   72.34000 1.000 21.45000 ? 359 ILE A CD1 1 
ATOM   2603 N N   . LEU A 1 360 ? 20.67800  7.41400   69.90500 1.000 19.13000 ? 360 LEU A N   1 
ATOM   2604 C CA  . LEU A 1 360 ? 20.37500  6.43000   68.87100 1.000 19.13000 ? 360 LEU A CA  1 
ATOM   2605 C C   . LEU A 1 360 ? 19.67200  7.04300   67.66600 1.000 19.13000 ? 360 LEU A C   1 
ATOM   2606 O O   . LEU A 1 360 ? 19.61800  6.40600   66.60800 1.000 19.13000 ? 360 LEU A O   1 
ATOM   2607 C CB  . LEU A 1 360 ? 19.55300  5.26800   69.44700 1.000 19.13000 ? 360 LEU A CB  1 
ATOM   2608 C CG  . LEU A 1 360 ? 18.20400  5.42000   70.15600 1.000 19.13000 ? 360 LEU A CG  1 
ATOM   2609 C CD1 . LEU A 1 360 ? 17.06600  5.68000   69.17700 1.000 19.13000 ? 360 LEU A CD1 1 
ATOM   2610 C CD2 . LEU A 1 360 ? 17.91900  4.17500   70.97700 1.000 19.13000 ? 360 LEU A CD2 1 
ATOM   2611 N N   . ASN A 1 361 ? 19.13500  8.25700   67.79700 1.000 19.50000 ? 361 ASN A N   1 
ATOM   2612 C CA  . ASN A 1 361 ? 18.64800  8.97600   66.62500 1.000 19.50000 ? 361 ASN A CA  1 
ATOM   2613 C C   . ASN A 1 361 ? 19.78600  9.43400   65.72400 1.000 19.50000 ? 361 ASN A C   1 
ATOM   2614 O O   . ASN A 1 361 ? 19.56200  9.67000   64.53200 1.000 19.50000 ? 361 ASN A O   1 
ATOM   2615 C CB  . ASN A 1 361 ? 17.80700  10.18100  67.04800 1.000 19.50000 ? 361 ASN A CB  1 
ATOM   2616 C CG  . ASN A 1 361 ? 16.39800  9.79600   67.44900 1.000 19.50000 ? 361 ASN A CG  1 
ATOM   2617 O OD1 . ASN A 1 361 ? 16.12200  9.53300   68.61900 1.000 19.50000 ? 361 ASN A OD1 1 
ATOM   2618 N ND2 . ASN A 1 361 ? 15.49500  9.76400   66.47600 1.000 19.50000 ? 361 ASN A ND2 1 
ATOM   2619 N N   . LEU A 1 362 ? 20.99400  9.57600   66.27200 1.000 18.71000 ? 362 LEU A N   1 
ATOM   2620 C CA  . LEU A 1 362 ? 22.11400  10.09000  65.49200 1.000 18.71000 ? 362 LEU A CA  1 
ATOM   2621 C C   . LEU A 1 362 ? 22.49400  9.14800   64.35600 1.000 18.71000 ? 362 LEU A C   1 
ATOM   2622 O O   . LEU A 1 362 ? 22.88300  9.60100   63.27400 1.000 18.71000 ? 362 LEU A O   1 
ATOM   2623 C CB  . LEU A 1 362 ? 23.31200  10.32500  66.41000 1.000 18.71000 ? 362 LEU A CB  1 
ATOM   2624 C CG  . LEU A 1 362 ? 24.65100  10.61300  65.73600 1.000 18.71000 ? 362 LEU A CG  1 
ATOM   2625 C CD1 . LEU A 1 362 ? 24.59700  11.95300  65.03300 1.000 18.71000 ? 362 LEU A CD1 1 
ATOM   2626 C CD2 . LEU A 1 362 ? 25.78100  10.57400  66.74700 1.000 18.71000 ? 362 LEU A CD2 1 
ATOM   2627 N N   . VAL A 1 363 ? 22.37800  7.83900   64.57400 1.000 16.51000 ? 363 VAL A N   1 
ATOM   2628 C CA  . VAL A 1 363 ? 22.77600  6.85000   63.58300 1.000 16.51000 ? 363 VAL A CA  1 
ATOM   2629 C C   . VAL A 1 363 ? 21.62700  5.92400   63.20500 1.000 16.51000 ? 363 VAL A C   1 
ATOM   2630 O O   . VAL A 1 363 ? 21.84700  4.91700   62.53200 1.000 16.51000 ? 363 VAL A O   1 
ATOM   2631 C CB  . VAL A 1 363 ? 23.99500  6.03700   64.06100 1.000 16.51000 ? 363 VAL A CB  1 
ATOM   2632 C CG1 . VAL A 1 363 ? 25.13400  6.96500   64.46000 1.000 16.51000 ? 363 VAL A CG1 1 
ATOM   2633 C CG2 . VAL A 1 363 ? 23.60700  5.13500   65.21300 1.000 16.51000 ? 363 VAL A CG2 1 
ATOM   2634 N N   . ASN A 1 364 ? 20.40200  6.25000   63.62200 1.000 16.80000 ? 364 ASN A N   1 
ATOM   2635 C CA  . ASN A 1 364 ? 19.21700  5.44400   63.32400 1.000 16.80000 ? 364 ASN A CA  1 
ATOM   2636 C C   . ASN A 1 364 ? 19.37400  4.00700   63.82100 1.000 16.80000 ? 364 ASN A C   1 
ATOM   2637 O O   . ASN A 1 364 ? 19.10300  3.04200   63.10400 1.000 16.80000 ? 364 ASN A O   1 
ATOM   2638 C CB  . ASN A 1 364 ? 18.89300  5.47500   61.82900 1.000 16.80000 ? 364 ASN A CB  1 
ATOM   2639 C CG  . ASN A 1 364 ? 18.30400  6.79400   61.39500 1.000 16.80000 ? 364 ASN A CG  1 
ATOM   2640 O OD1 . ASN A 1 364 ? 18.90600  7.53000   60.61500 1.000 16.80000 ? 364 ASN A OD1 1 
ATOM   2641 N ND2 . ASN A 1 364 ? 17.11800  7.10600   61.90500 1.000 16.80000 ? 364 ASN A ND2 1 
ATOM   2642 N N   . ALA A 1 365 ? 19.84400  3.87400   65.05700 1.000 17.17000 ? 365 ALA A N   1 
ATOM   2643 C CA  . ALA A 1 365 ? 19.89600  2.59600   65.75000 1.000 17.17000 ? 365 ALA A CA  1 
ATOM   2644 C C   . ALA A 1 365 ? 18.56000  2.29000   66.42600 1.000 17.17000 ? 365 ALA A C   1 
ATOM   2645 O O   . ALA A 1 365 ? 17.72100  3.16900   66.63100 1.000 17.17000 ? 365 ALA A O   1 
ATOM   2646 C CB  . ALA A 1 365 ? 21.02100  2.59000   66.78900 1.000 17.17000 ? 365 ALA A CB  1 
ATOM   2647 N N   . GLN A 1 366 ? 18.36000  1.01000   66.74400 1.000 19.62000 ? 366 GLN A N   1 
ATOM   2648 C CA  . GLN A 1 366 ? 17.24600  0.60100   67.59200 1.000 19.62000 ? 366 GLN A CA  1 
ATOM   2649 C C   . GLN A 1 366 ? 17.57300  0.70300   69.07900 1.000 19.62000 ? 366 GLN A C   1 
ATOM   2650 O O   . GLN A 1 366 ? 16.72900  1.14100   69.86900 1.000 19.62000 ? 366 GLN A O   1 
ATOM   2651 C CB  . GLN A 1 366 ? 16.82900  -0.83200  67.26500 1.000 19.62000 ? 366 GLN A CB  1 
ATOM   2652 C CG  . GLN A 1 366 ? 15.73200  -1.38900  68.15900 1.000 19.62000 ? 366 GLN A CG  1 
ATOM   2653 C CD  . GLN A 1 366 ? 15.80500  -2.90000  68.29300 1.000 19.62000 ? 366 GLN A CD  1 
ATOM   2654 O OE1 . GLN A 1 366 ? 16.88900  -3.46700  68.43900 1.000 19.62000 ? 366 GLN A OE1 1 
ATOM   2655 N NE2 . GLN A 1 366 ? 14.65300  -3.55900  68.23700 1.000 19.62000 ? 366 GLN A NE2 1 
ATOM   2656 N N   . GLY A 1 367 ? 18.78100  0.29700   69.48500 1.000 18.67000 ? 367 GLY A N   1 
ATOM   2657 C CA  . GLY A 1 367 ? 19.18900  0.39100   70.86800 1.000 18.67000 ? 367 GLY A CA  1 
ATOM   2658 C C   . GLY A 1 367 ? 20.55200  1.05100   70.98400 1.000 18.67000 ? 367 GLY A C   1 
ATOM   2659 O O   . GLY A 1 367 ? 21.24700  1.26600   69.99400 1.000 18.67000 ? 367 GLY A O   1 
ATOM   2660 N N   . ALA A 1 368 ? 20.93000  1.34800   72.22300 1.000 19.32000 ? 368 ALA A N   1 
ATOM   2661 C CA  . ALA A 1 368 ? 22.20800  1.99700   72.47100 1.000 19.32000 ? 368 ALA A CA  1 
ATOM   2662 C C   . ALA A 1 368 ? 22.63200  1.73300   73.90600 1.000 19.32000 ? 368 ALA A C   1 
ATOM   2663 O O   . ALA A 1 368 ? 21.79600  1.50600   74.78500 1.000 19.32000 ? 368 ALA A O   1 
ATOM   2664 C CB  . ALA A 1 368 ? 22.13500  3.50400   72.20100 1.000 19.32000 ? 368 ALA A CB  1 
ATOM   2665 N N   . ALA A 1 369 ? 23.94200  1.76400   74.12800 1.000 21.92000 ? 369 ALA A N   1 
ATOM   2666 C CA  . ALA A 1 369 ? 24.51100  1.54100   75.45000 1.000 21.92000 ? 369 ALA A CA  1 
ATOM   2667 C C   . ALA A 1 369 ? 25.72900  2.43300   75.61300 1.000 21.92000 ? 369 ALA A C   1 
ATOM   2668 O O   . ALA A 1 369 ? 26.68800  2.32400   74.84100 1.000 21.92000 ? 369 ALA A O   1 
ATOM   2669 C CB  . ALA A 1 369 ? 24.88800  0.07100   75.65100 1.000 21.92000 ? 369 ALA A CB  1 
ATOM   2670 N N   . ILE A 1 370 ? 25.68300  3.32000   76.59900 1.000 26.97000 ? 370 ILE A N   1 
ATOM   2671 C CA  . ILE A 1 370 ? 26.83400  4.12200   76.99700 1.000 26.97000 ? 370 ILE A CA  1 
ATOM   2672 C C   . ILE A 1 370 ? 27.50100  3.39400   78.15500 1.000 26.97000 ? 370 ILE A C   1 
ATOM   2673 O O   . ILE A 1 370 ? 26.94500  3.32500   79.25600 1.000 26.97000 ? 370 ILE A O   1 
ATOM   2674 C CB  . ILE A 1 370 ? 26.42800  5.54900   77.39000 1.000 26.97000 ? 370 ILE A CB  1 
ATOM   2675 C CG1 . ILE A 1 370 ? 25.74200  6.25400   76.21800 1.000 26.97000 ? 370 ILE A CG1 1 
ATOM   2676 C CG2 . ILE A 1 370 ? 27.64400  6.33600   77.85300 1.000 26.97000 ? 370 ILE A CG2 1 
ATOM   2677 C CD1 . ILE A 1 370 ? 25.32300  7.67700   76.52200 1.000 26.97000 ? 370 ILE A CD1 1 
ATOM   2678 N N   . CYS A 1 371 ? 28.67800  2.82500   77.91200 1.000 33.80000 ? 371 CYS A N   1 
ATOM   2679 C CA  . CYS A 1 371 ? 29.37300  1.99900   78.89400 1.000 33.80000 ? 371 CYS A CA  1 
ATOM   2680 C C   . CYS A 1 371 ? 30.61300  2.75800   79.35600 1.000 33.80000 ? 371 CYS A C   1 
ATOM   2681 O O   . CYS A 1 371 ? 31.68100  2.65700   78.75200 1.000 33.80000 ? 371 CYS A O   1 
ATOM   2682 C CB  . CYS A 1 371 ? 29.73500  0.65000   78.29400 1.000 33.80000 ? 371 CYS A CB  1 
ATOM   2683 S SG  . CYS A 1 371 ? 28.47100  -0.02000  77.18700 1.000 33.80000 ? 371 CYS A SG  1 
ATOM   2684 N N   . PHE A 1 372 ? 30.45900  3.53500   80.42300 1.000 38.25000 ? 372 PHE A N   1 
ATOM   2685 C CA  . PHE A 1 372 ? 31.56600  4.26500   81.03000 1.000 38.25000 ? 372 PHE A CA  1 
ATOM   2686 C C   . PHE A 1 372 ? 32.01400  3.50700   82.27300 1.000 38.25000 ? 372 PHE A C   1 
ATOM   2687 O O   . PHE A 1 372 ? 31.30000  3.48300   83.28200 1.000 38.25000 ? 372 PHE A O   1 
ATOM   2688 C CB  . PHE A 1 372 ? 31.15700  5.69600   81.37000 1.000 38.25000 ? 372 PHE A CB  1 
ATOM   2689 C CG  . PHE A 1 372 ? 31.00100  6.58400   80.16900 1.000 38.25000 ? 372 PHE A CG  1 
ATOM   2690 C CD1 . PHE A 1 372 ? 31.54100  6.22300   78.94500 1.000 38.25000 ? 372 PHE A CD1 1 
ATOM   2691 C CD2 . PHE A 1 372 ? 30.32000  7.78500   80.26600 1.000 38.25000 ? 372 PHE A CD2 1 
ATOM   2692 C CE1 . PHE A 1 372 ? 31.40000  7.04200   77.84000 1.000 38.25000 ? 372 PHE A CE1 1 
ATOM   2693 C CE2 . PHE A 1 372 ? 30.17500  8.60900   79.16600 1.000 38.25000 ? 372 PHE A CE2 1 
ATOM   2694 C CZ  . PHE A 1 372 ? 30.71600  8.23700   77.95200 1.000 38.25000 ? 372 PHE A CZ  1 
ATOM   2695 N N   . ASN A 1 373 ? 33.19700  2.89400   82.19700 1.000 39.37000 ? 373 ASN A N   1 
ATOM   2696 C CA  . ASN A 1 373 ? 33.74600  2.09000   83.28400 1.000 39.37000 ? 373 ASN A CA  1 
ATOM   2697 C C   . ASN A 1 373 ? 32.74300  1.03000   83.72400 1.000 39.37000 ? 373 ASN A C   1 
ATOM   2698 O O   . ASN A 1 373 ? 32.30800  0.20600   82.91200 1.000 39.37000 ? 373 ASN A O   1 
ATOM   2699 C CB  . ASN A 1 373 ? 34.14600  2.98200   84.46400 1.000 39.37000 ? 373 ASN A CB  1 
ATOM   2700 C CG  . ASN A 1 373 ? 35.19000  2.33800   85.36000 1.000 39.37000 ? 373 ASN A CG  1 
ATOM   2701 O OD1 . ASN A 1 373 ? 35.44700  1.13800   85.27200 1.000 39.37000 ? 373 ASN A OD1 1 
ATOM   2702 N ND2 . ASN A 1 373 ? 35.79300  3.13800   86.23300 1.000 39.37000 ? 373 ASN A ND2 1 
ATOM   2703 N N   . LYS A 1 374 ? 32.37300  1.04100   85.00500 1.000 36.89000 ? 374 LYS A N   1 
ATOM   2704 C CA  . LYS A 1 374 ? 31.38600  0.10000   85.51800 1.000 36.89000 ? 374 LYS A CA  1 
ATOM   2705 C C   . LYS A 1 374 ? 29.94900  0.55400   85.29000 1.000 36.89000 ? 374 LYS A C   1 
ATOM   2706 O O   . LYS A 1 374 ? 29.02600  -0.23300  85.53000 1.000 36.89000 ? 374 LYS A O   1 
ATOM   2707 C CB  . LYS A 1 374 ? 31.61500  -0.13500  87.01400 1.000 36.89000 ? 374 LYS A CB  1 
ATOM   2708 C CG  . LYS A 1 374 ? 33.01500  -0.62000  87.35900 1.000 36.89000 ? 374 LYS A CG  1 
ATOM   2709 C CD  . LYS A 1 374 ? 33.10700  -1.05300  88.81500 1.000 36.89000 ? 374 LYS A CD  1 
ATOM   2710 C CE  . LYS A 1 374 ? 32.68200  0.06300   89.75600 1.000 36.89000 ? 374 LYS A CE  1 
ATOM   2711 N NZ  . LYS A 1 374 ? 32.70500  -0.37200  91.18000 1.000 36.89000 ? 374 LYS A NZ  1 
ATOM   2712 N N   . GLU A 1 375 ? 29.73600  1.78900   84.84400 1.000 33.73000 ? 375 GLU A N   1 
ATOM   2713 C CA  . GLU A 1 375 ? 28.39500  2.30800   84.61700 1.000 33.73000 ? 375 GLU A CA  1 
ATOM   2714 C C   . GLU A 1 375 ? 27.90300  1.93200   83.22500 1.000 33.73000 ? 375 GLU A C   1 
ATOM   2715 O O   . GLU A 1 375 ? 28.66000  1.97400   82.25200 1.000 33.73000 ? 375 GLU A O   1 
ATOM   2716 C CB  . GLU A 1 375 ? 28.37800  3.82700   84.79000 1.000 33.73000 ? 375 GLU A CB  1 
ATOM   2717 C CG  . GLU A 1 375 ? 29.09700  4.30000   86.04300 1.000 33.73000 ? 375 GLU A CG  1 
ATOM   2718 C CD  . GLU A 1 375 ? 29.03600  5.80100   86.22500 1.000 33.73000 ? 375 GLU A CD  1 
ATOM   2719 O OE1 . GLU A 1 375 ? 28.06100  6.42100   85.74900 1.000 33.73000 ? 375 GLU A OE1 1 
ATOM   2720 O OE2 . GLU A 1 375 ? 29.96500  6.36200   86.84200 1.000 33.73000 ? 375 GLU A OE2 1 
ATOM   2721 N N   . LEU A 1 376 ? 26.62000  1.58400   83.13400 1.000 27.11000 ? 376 LEU A N   1 
ATOM   2722 C CA  . LEU A 1 376 ? 25.99400  1.20400   81.87300 1.000 27.11000 ? 376 LEU A CA  1 
ATOM   2723 C C   . LEU A 1 376 ? 24.66100  1.92200   81.75200 1.000 27.11000 ? 376 LEU A C   1 
ATOM   2724 O O   . LEU A 1 376 ? 23.78400  1.75400   82.60600 1.000 27.11000 ? 376 LEU A O   1 
ATOM   2725 C CB  . LEU A 1 376 ? 25.79200  -0.31100  81.78200 1.000 27.11000 ? 376 LEU A CB  1 
ATOM   2726 C CG  . LEU A 1 376 ? 24.95000  -0.76800  80.58900 1.000 27.11000 ? 376 LEU A CG  1 
ATOM   2727 C CD1 . LEU A 1 376 ? 25.64800  -0.42800  79.28600 1.000 27.11000 ? 376 LEU A CD1 1 
ATOM   2728 C CD2 . LEU A 1 376 ? 24.64400  -2.25300  80.65900 1.000 27.11000 ? 376 LEU A CD2 1 
ATOM   2729 N N   . TYR A 1 377 ? 24.50800  2.71600   80.69700 1.000 26.39000 ? 377 TYR A N   1 
ATOM   2730 C CA  . TYR A 1 377 ? 23.27400  3.44100   80.41700 1.000 26.39000 ? 377 TYR A CA  1 
ATOM   2731 C C   . TYR A 1 377 ? 22.65800  2.85300   79.15500 1.000 26.39000 ? 377 TYR A C   1 
ATOM   2732 O O   . TYR A 1 377 ? 23.15800  3.08400   78.04900 1.000 26.39000 ? 377 TYR A O   1 
ATOM   2733 C CB  . TYR A 1 377 ? 23.54400  4.93400   80.25500 1.000 26.39000 ? 377 TYR A CB  1 
ATOM   2734 C CG  . TYR A 1 377 ? 24.24500  5.56400   81.43600 1.000 26.39000 ? 377 TYR A CG  1 
ATOM   2735 C CD1 . TYR A 1 377 ? 25.63000  5.56000   81.52900 1.000 26.39000 ? 377 TYR A CD1 1 
ATOM   2736 C CD2 . TYR A 1 377 ? 23.52200  6.16600   82.45400 1.000 26.39000 ? 377 TYR A CD2 1 
ATOM   2737 C CE1 . TYR A 1 377 ? 26.27500  6.13500   82.60600 1.000 26.39000 ? 377 TYR A CE1 1 
ATOM   2738 C CE2 . TYR A 1 377 ? 24.15700  6.74400   83.53500 1.000 26.39000 ? 377 TYR A CE2 1 
ATOM   2739 C CZ  . TYR A 1 377 ? 25.53400  6.72600   83.60600 1.000 26.39000 ? 377 TYR A CZ  1 
ATOM   2740 O OH  . TYR A 1 377 ? 26.17000  7.30200   84.68100 1.000 26.39000 ? 377 TYR A OH  1 
ATOM   2741 N N   . LEU A 1 378 ? 21.60300  2.06400   79.32800 1.000 22.28000 ? 378 LEU A N   1 
ATOM   2742 C CA  . LEU A 1 378 ? 20.87900  1.46600   78.21600 1.000 22.28000 ? 378 LEU A CA  1 
ATOM   2743 C C   . LEU A 1 378 ? 19.83100  2.42500   77.66700 1.000 22.28000 ? 378 LEU A C   1 
ATOM   2744 O O   . LEU A 1 378 ? 19.32600  3.29900   78.37600 1.000 22.28000 ? 378 LEU A O   1 
ATOM   2745 C CB  . LEU A 1 378 ? 20.21700  0.15900   78.65000 1.000 22.28000 ? 378 LEU A CB  1 
ATOM   2746 C CG  . LEU A 1 378 ? 21.21100  -0.91500  79.08600 1.000 22.28000 ? 378 LEU A CG  1 
ATOM   2747 C CD1 . LEU A 1 378 ? 20.51400  -2.23400  79.38700 1.000 22.28000 ? 378 LEU A CD1 1 
ATOM   2748 C CD2 . LEU A 1 378 ? 22.26300  -1.09000  78.01400 1.000 22.28000 ? 378 LEU A CD2 1 
ATOM   2749 N N   . LEU A 1 379 ? 19.50900  2.25100   76.38700 1.000 20.34000 ? 379 LEU A N   1 
ATOM   2750 C CA  . LEU A 1 379 ? 18.46100  3.02300   75.73700 1.000 20.34000 ? 379 LEU A CA  1 
ATOM   2751 C C   . LEU A 1 379 ? 17.88100  2.17300   74.61800 1.000 20.34000 ? 379 LEU A C   1 
ATOM   2752 O O   . LEU A 1 379 ? 18.62000  1.47300   73.92400 1.000 20.34000 ? 379 LEU A O   1 
ATOM   2753 C CB  . LEU A 1 379 ? 19.00500  4.34900   75.19000 1.000 20.34000 ? 379 LEU A CB  1 
ATOM   2754 C CG  . LEU A 1 379 ? 18.03200  5.28900   74.47700 1.000 20.34000 ? 379 LEU A CG  1 
ATOM   2755 C CD1 . LEU A 1 379 ? 16.88300  5.66800   75.39400 1.000 20.34000 ? 379 LEU A CD1 1 
ATOM   2756 C CD2 . LEU A 1 379 ? 18.76300  6.53000   73.99100 1.000 20.34000 ? 379 LEU A CD2 1 
ATOM   2757 N N   . GLY A 1 380 ? 16.56300  2.24100   74.44000 1.000 21.37000 ? 380 GLY A N   1 
ATOM   2758 C CA  . GLY A 1 380 ? 15.95700  1.40000   73.42700 1.000 21.37000 ? 380 GLY A CA  1 
ATOM   2759 C C   . GLY A 1 380 ? 16.03500  -0.07500  73.79000 1.000 21.37000 ? 380 GLY A C   1 
ATOM   2760 O O   . GLY A 1 380 ? 15.99900  -0.46400  74.96200 1.000 21.37000 ? 380 GLY A O   1 
ATOM   2761 N N   . ASN A 1 381 ? 16.12900  -0.91000  72.75600 1.000 22.12000 ? 381 ASN A N   1 
ATOM   2762 C CA  . ASN A 1 381 ? 16.21800  -2.35600  72.90600 1.000 22.12000 ? 381 ASN A CA  1 
ATOM   2763 C C   . ASN A 1 381 ? 17.67800  -2.77800  72.80400 1.000 22.12000 ? 381 ASN A C   1 
ATOM   2764 O O   . ASN A 1 381 ? 18.30800  -2.60200  71.75500 1.000 22.12000 ? 381 ASN A O   1 
ATOM   2765 C CB  . ASN A 1 381 ? 15.37500  -3.06000  71.84500 1.000 22.12000 ? 381 ASN A CB  1 
ATOM   2766 C CG  . ASN A 1 381 ? 13.96700  -2.51200  71.76700 1.000 22.12000 ? 381 ASN A CG  1 
ATOM   2767 O OD1 . ASN A 1 381 ? 13.71400  -1.51000  71.09600 1.000 22.12000 ? 381 ASN A OD1 1 
ATOM   2768 N ND2 . ASN A 1 381 ? 13.04100  -3.16100  72.46100 1.000 22.12000 ? 381 ASN A ND2 1 
ATOM   2769 N N   . THR A 1 382 ? 18.20800  -3.33000  73.88500 1.000 24.00000 ? 382 THR A N   1 
ATOM   2770 C CA  . THR A 1 382 ? 19.61400  -3.67500  74.01800 1.000 24.00000 ? 382 THR A CA  1 
ATOM   2771 C C   . THR A 1 382 ? 19.75200  -5.09300  74.54500 1.000 24.00000 ? 382 THR A C   1 
ATOM   2772 O O   . THR A 1 382 ? 18.83000  -5.62800  75.16900 1.000 24.00000 ? 382 THR A O   1 
ATOM   2773 C CB  . THR A 1 382 ? 20.34800  -2.71500  74.96600 1.000 24.00000 ? 382 THR A CB  1 
ATOM   2774 O OG1 . THR A 1 382 ? 19.86700  -2.90400  76.30200 1.000 24.00000 ? 382 THR A OG1 1 
ATOM   2775 C CG2 . THR A 1 382 ? 20.13300  -1.27100  74.55100 1.000 24.00000 ? 382 THR A CG2 1 
ATOM   2776 N N   . PRO A 1 383 ? 20.89200  -5.73400  74.29500 1.000 27.14000 ? 383 PRO A N   1 
ATOM   2777 C CA  . PRO A 1 383 ? 21.18900  -7.00100  74.97000 1.000 27.14000 ? 383 PRO A CA  1 
ATOM   2778 C C   . PRO A 1 383 ? 21.30400  -6.80100  76.47300 1.000 27.14000 ? 383 PRO A C   1 
ATOM   2779 O O   . PRO A 1 383 ? 21.62100  -5.71200  76.95600 1.000 27.14000 ? 383 PRO A O   1 
ATOM   2780 C CB  . PRO A 1 383 ? 22.52800  -7.42700  74.35800 1.000 27.14000 ? 383 PRO A CB  1 
ATOM   2781 C CG  . PRO A 1 383 ? 22.59800  -6.70800  73.05900 1.000 27.14000 ? 383 PRO A CG  1 
ATOM   2782 C CD  . PRO A 1 383 ? 21.90800  -5.40000  73.28300 1.000 27.14000 ? 383 PRO A CD  1 
ATOM   2783 N N   . GLU A 1 384 ? 21.00700  -7.86300  77.21600 1.000 32.90000 ? 384 GLU A N   1 
ATOM   2784 C CA  . GLU A 1 384 ? 21.04200  -7.80300  78.66900 1.000 32.90000 ? 384 GLU A CA  1 
ATOM   2785 C C   . GLU A 1 384 ? 22.44700  -7.45800  79.16000 1.000 32.90000 ? 384 GLU A C   1 
ATOM   2786 O O   . GLU A 1 384 ? 23.44500  -7.66200  78.46400 1.000 32.90000 ? 384 GLU A O   1 
ATOM   2787 C CB  . GLU A 1 384 ? 20.58100  -9.13100  79.27000 1.000 32.90000 ? 384 GLU A CB  1 
ATOM   2788 C CG  . GLU A 1 384 ? 19.18700  -9.55400  78.83600 1.000 32.90000 ? 384 GLU A CG  1 
ATOM   2789 C CD  . GLU A 1 384 ? 18.70000  -10.79200 79.56300 1.000 32.90000 ? 384 GLU A CD  1 
ATOM   2790 O OE1 . GLU A 1 384 ? 19.21300  -11.07600 80.66500 1.000 32.90000 ? 384 GLU A OE1 1 
ATOM   2791 O OE2 . GLU A 1 384 ? 17.80500  -11.48100 79.03100 1.000 32.90000 ? 384 GLU A OE2 1 
ATOM   2792 N N   . LYS A 1 385 ? 22.50800  -6.91500  80.38000 1.000 33.14000 ? 385 LYS A N   1 
ATOM   2793 C CA  . LYS A 1 385 ? 23.72700  -6.27700  80.87100 1.000 33.14000 ? 385 LYS A CA  1 
ATOM   2794 C C   . LYS A 1 385 ? 24.92200  -7.22600  80.86000 1.000 33.14000 ? 385 LYS A C   1 
ATOM   2795 O O   . LYS A 1 385 ? 26.04800  -6.80100  80.57000 1.000 33.14000 ? 385 LYS A O   1 
ATOM   2796 C CB  . LYS A 1 385 ? 23.47500  -5.74600  82.28500 1.000 33.14000 ? 385 LYS A CB  1 
ATOM   2797 C CG  . LYS A 1 385 ? 24.61600  -4.97300  82.91800 1.000 33.14000 ? 385 LYS A CG  1 
ATOM   2798 C CD  . LYS A 1 385 ? 24.15700  -4.33500  84.22300 1.000 33.14000 ? 385 LYS A CD  1 
ATOM   2799 C CE  . LYS A 1 385 ? 25.14200  -3.29300  84.72900 1.000 33.14000 ? 385 LYS A CE  1 
ATOM   2800 N NZ  . LYS A 1 385 ? 26.45000  -3.88900  85.10700 1.000 33.14000 ? 385 LYS A NZ  1 
ATOM   2801 N N   . GLN A 1 386 ? 24.69600  -8.51400  81.12800 1.000 37.15000 ? 386 GLN A N   1 
ATOM   2802 C CA  . GLN A 1 386 ? 25.79200  -9.47300  81.04700 1.000 37.15000 ? 386 GLN A CA  1 
ATOM   2803 C C   . GLN A 1 386 ? 26.25600  -9.65800  79.60900 1.000 37.15000 ? 386 GLN A C   1 
ATOM   2804 O O   . GLN A 1 386 ? 27.46300  -9.73600  79.34400 1.000 37.15000 ? 386 GLN A O   1 
ATOM   2805 C CB  . GLN A 1 386 ? 25.36500  -10.81100 81.65100 1.000 37.15000 ? 386 GLN A CB  1 
ATOM   2806 C CG  . GLN A 1 386 ? 26.47600  -11.85200 81.70900 1.000 37.15000 ? 386 GLN A CG  1 
ATOM   2807 C CD  . GLN A 1 386 ? 27.64500  -11.40300 82.56100 1.000 37.15000 ? 386 GLN A CD  1 
ATOM   2808 O OE1 . GLN A 1 386 ? 28.77100  -11.28400 82.07800 1.000 37.15000 ? 386 GLN A OE1 1 
ATOM   2809 N NE2 . GLN A 1 386 ? 27.38200  -11.14600 83.83800 1.000 37.15000 ? 386 GLN A NE2 1 
ATOM   2810 N N   . ASP A 1 387 ? 25.31300  -9.71700  78.66400 1.000 33.25000 ? 387 ASP A N   1 
ATOM   2811 C CA  . ASP A 1 387 ? 25.69100  -9.85700  77.26200 1.000 33.25000 ? 387 ASP A CA  1 
ATOM   2812 C C   . ASP A 1 387 ? 26.44900  -8.63100  76.77400 1.000 33.25000 ? 387 ASP A C   1 
ATOM   2813 O O   . ASP A 1 387 ? 27.40600  -8.75200  75.99800 1.000 33.25000 ? 387 ASP A O   1 
ATOM   2814 C CB  . ASP A 1 387 ? 24.44900  -10.08800 76.40200 1.000 33.25000 ? 387 ASP A CB  1 
ATOM   2815 C CG  . ASP A 1 387 ? 23.69600  -11.34300 76.78900 1.000 33.25000 ? 387 ASP A CG  1 
ATOM   2816 O OD1 . ASP A 1 387 ? 24.33300  -12.27700 77.32200 1.000 33.25000 ? 387 ASP A OD1 1 
ATOM   2817 O OD2 . ASP A 1 387 ? 22.46900  -11.39700 76.55700 1.000 33.25000 ? 387 ASP A OD2 1 
ATOM   2818 N N   . ILE A 1 388 ? 26.05200  -7.44400  77.23400 1.000 31.41000 ? 388 ILE A N   1 
ATOM   2819 C CA  . ILE A 1 388 ? 26.76000  -6.23700  76.82700 1.000 31.41000 ? 388 ILE A CA  1 
ATOM   2820 C C   . ILE A 1 388 ? 28.15200  -6.20100  77.44000 1.000 31.41000 ? 388 ILE A C   1 
ATOM   2821 O O   . ILE A 1 388 ? 29.11000  -5.76300  76.79700 1.000 31.41000 ? 388 ILE A O   1 
ATOM   2822 C CB  . ILE A 1 388 ? 25.94100  -4.98300  77.17900 1.000 31.41000 ? 388 ILE A CB  1 
ATOM   2823 C CG1 . ILE A 1 388 ? 24.63400  -4.98800  76.38600 1.000 31.41000 ? 388 ILE A CG1 1 
ATOM   2824 C CG2 . ILE A 1 388 ? 26.74300  -3.71700  76.89100 1.000 31.41000 ? 388 ILE A CG2 1 
ATOM   2825 C CD1 . ILE A 1 388 ? 23.96500  -3.64300  76.28800 1.000 31.41000 ? 388 ILE A CD1 1 
ATOM   2826 N N   . GLN A 1 389 ? 28.30100  -6.67900  78.67900 1.000 35.98000 ? 389 GLN A N   1 
ATOM   2827 C CA  . GLN A 1 389 ? 29.63800  -6.73100  79.26400 1.000 35.98000 ? 389 GLN A CA  1 
ATOM   2828 C C   . GLN A 1 389 ? 30.52400  -7.73500  78.53200 1.000 35.98000 ? 389 GLN A C   1 
ATOM   2829 O O   . GLN A 1 389 ? 31.72300  -7.49100  78.33600 1.000 35.98000 ? 389 GLN A O   1 
ATOM   2830 C CB  . GLN A 1 389 ? 29.54600  -7.05600  80.75400 1.000 35.98000 ? 389 GLN A CB  1 
ATOM   2831 C CG  . GLN A 1 389 ? 29.27500  -5.83100  81.62200 1.000 35.98000 ? 389 GLN A CG  1 
ATOM   2832 C CD  . GLN A 1 389 ? 28.60400  -6.17100  82.93900 1.000 35.98000 ? 389 GLN A CD  1 
ATOM   2833 O OE1 . GLN A 1 389 ? 27.90100  -7.17500  83.05000 1.000 35.98000 ? 389 GLN A OE1 1 
ATOM   2834 N NE2 . GLN A 1 389 ? 28.81600  -5.32900  83.94500 1.000 35.98000 ? 389 GLN A NE2 1 
ATOM   2835 N N   . ASN A 1 390 ? 29.94400  -8.84900  78.07800 1.000 37.46000 ? 390 ASN A N   1 
ATOM   2836 C CA  . ASN A 1 390 ? 30.72600  -9.80600  77.30000 1.000 37.46000 ? 390 ASN A CA  1 
ATOM   2837 C C   . ASN A 1 390 ? 31.13800  -9.21500  75.95700 1.000 37.46000 ? 390 ASN A C   1 
ATOM   2838 O O   . ASN A 1 390 ? 32.29200  -9.36200  75.53100 1.000 37.46000 ? 390 ASN A O   1 
ATOM   2839 C CB  . ASN A 1 390 ? 29.93000  -11.09500 77.09900 1.000 37.46000 ? 390 ASN A CB  1 
ATOM   2840 C CG  . ASN A 1 390 ? 29.59000  -11.78100 78.40800 1.000 37.46000 ? 390 ASN A CG  1 
ATOM   2841 O OD1 . ASN A 1 390 ? 30.35800  -11.72600 79.36800 1.000 37.46000 ? 390 ASN A OD1 1 
ATOM   2842 N ND2 . ASN A 1 390 ? 28.43100  -12.42900 78.45300 1.000 37.46000 ? 390 ASN A ND2 1 
ATOM   2843 N N   . LEU A 1 391 ? 30.21500  -8.51800  75.28800 1.000 32.99000 ? 391 LEU A N   1 
ATOM   2844 C CA  . LEU A 1 391 ? 30.56300  -7.86500  74.03300 1.000 32.99000 ? 391 LEU A CA  1 
ATOM   2845 C C   . LEU A 1 391 ? 31.60400  -6.77600  74.24400 1.000 32.99000 ? 391 LEU A C   1 
ATOM   2846 O O   . LEU A 1 391 ? 32.45200  -6.55300  73.37700 1.000 32.99000 ? 391 LEU A O   1 
ATOM   2847 C CB  . LEU A 1 391 ? 29.31200  -7.28100  73.37600 1.000 32.99000 ? 391 LEU A CB  1 
ATOM   2848 C CG  . LEU A 1 391 ? 29.53100  -6.47000  72.09600 1.000 32.99000 ? 391 LEU A CG  1 
ATOM   2849 C CD1 . LEU A 1 391 ? 29.98600  -7.36400  70.95200 1.000 32.99000 ? 391 LEU A CD1 1 
ATOM   2850 C CD2 . LEU A 1 391 ? 28.27700  -5.70000  71.72000 1.000 32.99000 ? 391 LEU A CD2 1 
ATOM   2851 N N   . LEU A 1 392 ? 31.56900  -6.10200  75.39500 1.000 36.08000 ? 392 LEU A N   1 
ATOM   2852 C CA  . LEU A 1 392 ? 32.56900  -5.08100  75.68200 1.000 36.08000 ? 392 LEU A CA  1 
ATOM   2853 C C   . LEU A 1 392 ? 33.94400  -5.69700  75.89100 1.000 36.08000 ? 392 LEU A C   1 
ATOM   2854 O O   . LEU A 1 392 ? 34.95000  -5.15000  75.42500 1.000 36.08000 ? 392 LEU A O   1 
ATOM   2855 C CB  . LEU A 1 392 ? 32.15500  -4.27300  76.90800 1.000 36.08000 ? 392 LEU A CB  1 
ATOM   2856 C CG  . LEU A 1 392 ? 31.02100  -3.27800  76.69000 1.000 36.08000 ? 392 LEU A CG  1 
ATOM   2857 C CD1 . LEU A 1 392 ? 30.48200  -2.82100  78.02900 1.000 36.08000 ? 392 LEU A CD1 1 
ATOM   2858 C CD2 . LEU A 1 392 ? 31.50700  -2.09900  75.86400 1.000 36.08000 ? 392 LEU A CD2 1 
ATOM   2859 N N   . LEU A 1 393 ? 34.00900  -6.83600  76.58400 1.000 40.70000 ? 393 LEU A N   1 
ATOM   2860 C CA  . LEU A 1 393 ? 35.29100  -7.52300  76.71400 1.000 40.70000 ? 393 LEU A CA  1 
ATOM   2861 C C   . LEU A 1 393 ? 35.79700  -7.98900  75.35400 1.000 40.70000 ? 393 LEU A C   1 
ATOM   2862 O O   . LEU A 1 393 ? 36.99900  -7.90900  75.06300 1.000 40.70000 ? 393 LEU A O   1 
ATOM   2863 C CB  . LEU A 1 393 ? 35.16200  -8.70400  77.67500 1.000 40.70000 ? 393 LEU A CB  1 
ATOM   2864 C CG  . LEU A 1 393 ? 34.71000  -8.39000  79.10300 1.000 40.70000 ? 393 LEU A CG  1 
ATOM   2865 C CD1 . LEU A 1 393 ? 34.63800  -9.66000  79.93900 1.000 40.70000 ? 393 LEU A CD1 1 
ATOM   2866 C CD2 . LEU A 1 393 ? 35.62500  -7.36200  79.75600 1.000 40.70000 ? 393 LEU A CD2 1 
ATOM   2867 N N   . TRP A 1 394 ? 34.88300  -8.43100  74.48700 1.000 36.82000 ? 394 TRP A N   1 
ATOM   2868 C CA  . TRP A 1 394 ? 35.28500  -8.84100  73.14700 1.000 36.82000 ? 394 TRP A CA  1 
ATOM   2869 C C   . TRP A 1 394 ? 35.82400  -7.66100  72.34600 1.000 36.82000 ? 394 TRP A C   1 
ATOM   2870 O O   . TRP A 1 394 ? 36.84400  -7.78200  71.65900 1.000 36.82000 ? 394 TRP A O   1 
ATOM   2871 C CB  . TRP A 1 394 ? 34.09900  -9.48600  72.42700 1.000 36.82000 ? 394 TRP A CB  1 
ATOM   2872 C CG  . TRP A 1 394 ? 34.40300  -9.97700  71.04000 1.000 36.82000 ? 394 TRP A CG  1 
ATOM   2873 C CD1 . TRP A 1 394 ? 34.74800  -11.24700 70.67600 1.000 36.82000 ? 394 TRP A CD1 1 
ATOM   2874 C CD2 . TRP A 1 394 ? 34.37700  -9.20700  69.83100 1.000 36.82000 ? 394 TRP A CD2 1 
ATOM   2875 N NE1 . TRP A 1 394 ? 34.94200  -11.31400 69.31700 1.000 36.82000 ? 394 TRP A NE1 1 
ATOM   2876 C CE2 . TRP A 1 394 ? 34.72200  -10.07500 68.77600 1.000 36.82000 ? 394 TRP A CE2 1 
ATOM   2877 C CE3 . TRP A 1 394 ? 34.10000  -7.86800  69.53900 1.000 36.82000 ? 394 TRP A CE3 1 
ATOM   2878 C CZ2 . TRP A 1 394 ? 34.79700  -9.64600  67.45200 1.000 36.82000 ? 394 TRP A CZ2 1 
ATOM   2879 C CZ3 . TRP A 1 394 ? 34.17600  -7.44500  68.22600 1.000 36.82000 ? 394 TRP A CZ3 1 
ATOM   2880 C CH2 . TRP A 1 394 ? 34.52200  -8.33100  67.19900 1.000 36.82000 ? 394 TRP A CH2 1 
ATOM   2881 N N   . ILE A 1 395 ? 35.14700  -6.51300  72.41800 1.000 37.36000 ? 395 ILE A N   1 
ATOM   2882 C CA  . ILE A 1 395 ? 35.58500  -5.33700  71.67100 1.000 37.36000 ? 395 ILE A CA  1 
ATOM   2883 C C   . ILE A 1 395 ? 36.91100  -4.82100  72.21300 1.000 37.36000 ? 395 ILE A C   1 
ATOM   2884 O O   . ILE A 1 395 ? 37.76700  -4.34600  71.45600 1.000 37.36000 ? 395 ILE A O   1 
ATOM   2885 C CB  . ILE A 1 395 ? 34.48900  -4.25400  71.70300 1.000 37.36000 ? 395 ILE A CB  1 
ATOM   2886 C CG1 . ILE A 1 395 ? 33.26000  -4.73300  70.92900 1.000 37.36000 ? 395 ILE A CG1 1 
ATOM   2887 C CG2 . ILE A 1 395 ? 35.00000  -2.94200  71.12600 1.000 37.36000 ? 395 ILE A CG2 1 
ATOM   2888 C CD1 . ILE A 1 395 ? 32.05400  -3.84000  71.08200 1.000 37.36000 ? 395 ILE A CD1 1 
ATOM   2889 N N   . HIS A 1 396 ? 37.11300  -4.92400  73.52700 1.000 44.29000 ? 396 HIS A N   1 
ATOM   2890 C CA  . HIS A 1 396 ? 38.39400  -4.54600  74.10800 1.000 44.29000 ? 396 HIS A CA  1 
ATOM   2891 C C   . HIS A 1 396 ? 39.50900  -5.48100  73.66100 1.000 44.29000 ? 396 HIS A C   1 
ATOM   2892 O O   . HIS A 1 396 ? 40.65700  -5.04700  73.50900 1.000 44.29000 ? 396 HIS A O   1 
ATOM   2893 C CB  . HIS A 1 396 ? 38.29200  -4.53100  75.63100 1.000 44.29000 ? 396 HIS A CB  1 
ATOM   2894 C CG  . HIS A 1 396 ? 39.57300  -4.17200  76.31400 1.000 44.29000 ? 396 HIS A CG  1 
ATOM   2895 N ND1 . HIS A 1 396 ? 40.05200  -2.88100  76.36300 1.000 44.29000 ? 396 HIS A ND1 1 
ATOM   2896 C CD2 . HIS A 1 396 ? 40.48100  -4.93600  76.96700 1.000 44.29000 ? 396 HIS A CD2 1 
ATOM   2897 C CE1 . HIS A 1 396 ? 41.19700  -2.86300  77.02200 1.000 44.29000 ? 396 HIS A CE1 1 
ATOM   2898 N NE2 . HIS A 1 396 ? 41.48000  -4.09700  77.39900 1.000 44.29000 ? 396 HIS A NE2 1 
ATOM   2899 N N   . ASN A 1 397 ? 39.19600  -6.76000  73.44000 1.000 44.41000 ? 397 ASN A N   1 
ATOM   2900 C CA  . ASN A 1 397 ? 40.22900  -7.69000  72.99100 1.000 44.41000 ? 397 ASN A CA  1 
ATOM   2901 C C   . ASN A 1 397 ? 40.51300  -7.55600  71.49800 1.000 44.41000 ? 397 ASN A C   1 
ATOM   2902 O O   . ASN A 1 397 ? 41.67700  -7.57900  71.08200 1.000 44.41000 ? 397 ASN A O   1 
ATOM   2903 C CB  . ASN A 1 397 ? 39.82600  -9.12800  73.32000 1.000 44.41000 ? 397 ASN A CB  1 
ATOM   2904 C CG  . ASN A 1 397 ? 39.99100  -9.45900  74.78800 1.000 44.41000 ? 397 ASN A CG  1 
ATOM   2905 O OD1 . ASN A 1 397 ? 40.93000  -9.00000  75.43900 1.000 44.41000 ? 397 ASN A OD1 1 
ATOM   2906 N ND2 . ASN A 1 397 ? 39.07700  -10.26400 75.31900 1.000 44.41000 ? 397 ASN A ND2 1 
ATOM   2907 N N   . ASN A 1 398 ? 39.46900  -7.40200  70.68200 1.000 41.12000 ? 398 ASN A N   1 
ATOM   2908 C CA  . ASN A 1 398 ? 39.59800  -7.47600  69.23000 1.000 41.12000 ? 398 ASN A CA  1 
ATOM   2909 C C   . ASN A 1 398 ? 39.72700  -6.10100  68.58400 1.000 41.12000 ? 398 ASN A C   1 
ATOM   2910 O O   . ASN A 1 398 ? 40.73000  -5.81800  67.92000 1.000 41.12000 ? 398 ASN A O   1 
ATOM   2911 C CB  . ASN A 1 398 ? 38.39600  -8.22900  68.64500 1.000 41.12000 ? 398 ASN A CB  1 
ATOM   2912 C CG  . ASN A 1 398 ? 38.34500  -9.67400  69.09400 1.000 41.12000 ? 398 ASN A CG  1 
ATOM   2913 O OD1 . ASN A 1 398 ? 38.10400  -9.96300  70.26600 1.000 41.12000 ? 398 ASN A OD1 1 
ATOM   2914 N ND2 . ASN A 1 398 ? 38.56900  -10.59200 68.16200 1.000 41.12000 ? 398 ASN A ND2 1 
ATOM   2915 N N   . ILE A 1 399 ? 38.72000  -5.24200  68.75900 1.000 41.19000 ? 399 ILE A N   1 
ATOM   2916 C CA  . ILE A 1 399 ? 38.72000  -3.95400  68.07900 1.000 41.19000 ? 399 ILE A CA  1 
ATOM   2917 C C   . ILE A 1 399 ? 39.87400  -3.10300  68.58300 1.000 41.19000 ? 399 ILE A C   1 
ATOM   2918 O O   . ILE A 1 399 ? 40.13000  -3.01100  69.79100 1.000 41.19000 ? 399 ILE A O   1 
ATOM   2919 C CB  . ILE A 1 399 ? 37.37300  -3.24300  68.28100 1.000 41.19000 ? 399 ILE A CB  1 
ATOM   2920 C CG1 . ILE A 1 399 ? 36.22500  -4.16400  67.86600 1.000 41.19000 ? 399 ILE A CG1 1 
ATOM   2921 C CG2 . ILE A 1 399 ? 37.33100  -1.94400  67.49400 1.000 41.19000 ? 399 ILE A CG2 1 
ATOM   2922 C CD1 . ILE A 1 399 ? 36.38000  -4.74300  66.47300 1.000 41.19000 ? 399 ILE A CD1 1 
ATOM   2923 N N   . ASP A 1 400 ? 40.57900  -2.46900  67.64600 1.000 47.27000 ? 400 ASP A N   1 
ATOM   2924 C CA  . ASP A 1 400 ? 41.71700  -1.61400  67.96000 1.000 47.27000 ? 400 ASP A CA  1 
ATOM   2925 C C   . ASP A 1 400 ? 41.58000  -0.26200  67.26800 1.000 47.27000 ? 400 ASP A C   1 
ATOM   2926 O O   . ASP A 1 400 ? 42.58000  0.36000   66.89800 1.000 47.27000 ? 400 ASP A O   1 
ATOM   2927 C CB  . ASP A 1 400 ? 43.03000  -2.29300  67.57300 1.000 47.27000 ? 400 ASP A CB  1 
ATOM   2928 C CG  . ASP A 1 400 ? 44.16600  -1.94000  68.50900 1.000 47.27000 ? 400 ASP A CG  1 
ATOM   2929 O OD1 . ASP A 1 400 ? 43.94700  -1.12400  69.42900 1.000 47.27000 ? 400 ASP A OD1 1 
ATOM   2930 O OD2 . ASP A 1 400 ? 45.27600  -2.48300  68.33000 1.000 47.27000 ? 400 ASP A OD2 1 
ATOM   2931 N N   . GLU A 1 401 ? 40.34400  0.19700   67.08200 1.000 44.39000 ? 401 GLU A N   1 
ATOM   2932 C CA  . GLU A 1 401 ? 40.06300  1.45800   66.41300 1.000 44.39000 ? 401 GLU A CA  1 
ATOM   2933 C C   . GLU A 1 401 ? 38.99100  2.19900   67.19800 1.000 44.39000 ? 401 GLU A C   1 
ATOM   2934 O O   . GLU A 1 401 ? 38.21400  1.59800   67.94400 1.000 44.39000 ? 401 GLU A O   1 
ATOM   2935 C CB  . GLU A 1 401 ? 39.60300  1.25100   64.95900 1.000 44.39000 ? 401 GLU A CB  1 
ATOM   2936 C CG  . GLU A 1 401 ? 40.40400  0.22100   64.16600 1.000 44.39000 ? 401 GLU A CG  1 
ATOM   2937 C CD  . GLU A 1 401 ? 39.93600  -1.20400  64.41200 1.000 44.39000 ? 401 GLU A CD  1 
ATOM   2938 O OE1 . GLU A 1 401 ? 38.70900  -1.42400  64.49300 1.000 44.39000 ? 401 GLU A OE1 1 
ATOM   2939 O OE2 . GLU A 1 401 ? 40.79600  -2.10200  64.53200 1.000 44.39000 ? 401 GLU A OE2 1 
ATOM   2940 N N   . ASP A 1 402 ? 38.96400  3.52400   67.03000 1.000 36.65000 ? 402 ASP A N   1 
ATOM   2941 C CA  . ASP A 1 402 ? 37.97900  4.33600   67.73800 1.000 36.65000 ? 402 ASP A CA  1 
ATOM   2942 C C   . ASP A 1 402 ? 36.55600  4.03000   67.29100 1.000 36.65000 ? 402 ASP A C   1 
ATOM   2943 O O   . ASP A 1 402 ? 35.61200  4.22800   68.06400 1.000 36.65000 ? 402 ASP A O   1 
ATOM   2944 C CB  . ASP A 1 402 ? 38.28100  5.82200   67.54500 1.000 36.65000 ? 402 ASP A CB  1 
ATOM   2945 C CG  . ASP A 1 402 ? 39.54900  6.25300   68.25000 1.000 36.65000 ? 402 ASP A CG  1 
ATOM   2946 O OD1 . ASP A 1 402 ? 40.27800  5.37200   68.75200 1.000 36.65000 ? 402 ASP A OD1 1 
ATOM   2947 O OD2 . ASP A 1 402 ? 39.81400  7.47300   68.30800 1.000 36.65000 ? 402 ASP A OD2 1 
ATOM   2948 N N   . ILE A 1 403 ? 36.37700  3.55200   66.06200 1.000 32.53000 ? 403 ILE A N   1 
ATOM   2949 C CA  . ILE A 1 403 ? 35.05300  3.29400   65.50900 1.000 32.53000 ? 403 ILE A CA  1 
ATOM   2950 C C   . ILE A 1 403 ? 35.08800  1.96700   64.76200 1.000 32.53000 ? 403 ILE A C   1 
ATOM   2951 O O   . ILE A 1 403 ? 36.03100  1.69400   64.01100 1.000 32.53000 ? 403 ILE A O   1 
ATOM   2952 C CB  . ILE A 1 403 ? 34.59500  4.44200   64.58300 1.000 32.53000 ? 403 ILE A CB  1 
ATOM   2953 C CG1 . ILE A 1 403 ? 33.22200  4.14700   63.97700 1.000 32.53000 ? 403 ILE A CG1 1 
ATOM   2954 C CG2 . ILE A 1 403 ? 35.63600  4.73100   63.50300 1.000 32.53000 ? 403 ILE A CG2 1 
ATOM   2955 C CD1 . ILE A 1 403 ? 32.08000  4.41400   64.92400 1.000 32.53000 ? 403 ILE A CD1 1 
ATOM   2956 N N   . PHE A 1 404 ? 34.06400  1.14300   64.96900 1.000 27.49000 ? 404 PHE A N   1 
ATOM   2957 C CA  . PHE A 1 404 ? 33.95500  -0.13800  64.28500 1.000 27.49000 ? 404 PHE A CA  1 
ATOM   2958 C C   . PHE A 1 404 ? 32.48000  -0.43600  64.07500 1.000 27.49000 ? 404 PHE A C   1 
ATOM   2959 O O   . PHE A 1 404 ? 31.66000  -0.16100  64.95000 1.000 27.49000 ? 404 PHE A O   1 
ATOM   2960 C CB  . PHE A 1 404 ? 34.63300  -1.25500  65.08800 1.000 27.49000 ? 404 PHE A CB  1 
ATOM   2961 C CG  . PHE A 1 404 ? 34.14300  -2.63600  64.75500 1.000 27.49000 ? 404 PHE A CG  1 
ATOM   2962 C CD1 . PHE A 1 404 ? 34.56900  -3.28400  63.60700 1.000 27.49000 ? 404 PHE A CD1 1 
ATOM   2963 C CD2 . PHE A 1 404 ? 33.26800  -3.29600  65.60400 1.000 27.49000 ? 404 PHE A CD2 1 
ATOM   2964 C CE1 . PHE A 1 404 ? 34.12100  -4.56000  63.30700 1.000 27.49000 ? 404 PHE A CE1 1 
ATOM   2965 C CE2 . PHE A 1 404 ? 32.81900  -4.56900  65.31100 1.000 27.49000 ? 404 PHE A CE2 1 
ATOM   2966 C CZ  . PHE A 1 404 ? 33.24500  -5.20200  64.16100 1.000 27.49000 ? 404 PHE A CZ  1 
ATOM   2967 N N   . TYR A 1 405 ? 32.14200  -0.99700  62.91900 1.000 22.72000 ? 405 TYR A N   1 
ATOM   2968 C CA  . TYR A 1 405 ? 30.73600  -1.15800  62.58500 1.000 22.72000 ? 405 TYR A CA  1 
ATOM   2969 C C   . TYR A 1 405 ? 30.54800  -2.41200  61.75000 1.000 22.72000 ? 405 TYR A C   1 
ATOM   2970 O O   . TYR A 1 405 ? 31.42500  -2.80100  60.97400 1.000 22.72000 ? 405 TYR A O   1 
ATOM   2971 C CB  . TYR A 1 405 ? 30.19400  0.06400   61.83300 1.000 22.72000 ? 405 TYR A CB  1 
ATOM   2972 C CG  . TYR A 1 405 ? 30.73200  0.21400   60.42700 1.000 22.72000 ? 405 TYR A CG  1 
ATOM   2973 C CD1 . TYR A 1 405 ? 32.05800  0.56600   60.19900 1.000 22.72000 ? 405 TYR A CD1 1 
ATOM   2974 C CD2 . TYR A 1 405 ? 29.91000  0.01300   59.32600 1.000 22.72000 ? 405 TYR A CD2 1 
ATOM   2975 C CE1 . TYR A 1 405 ? 32.55200  0.70400   58.91300 1.000 22.72000 ? 405 TYR A CE1 1 
ATOM   2976 C CE2 . TYR A 1 405 ? 30.39400  0.15000   58.03700 1.000 22.72000 ? 405 TYR A CE2 1 
ATOM   2977 C CZ  . TYR A 1 405 ? 31.71600  0.49600   57.83600 1.000 22.72000 ? 405 TYR A CZ  1 
ATOM   2978 O OH  . TYR A 1 405 ? 32.20100  0.63400   56.55500 1.000 22.72000 ? 405 TYR A OH  1 
ATOM   2979 N N   . THR A 1 406 ? 29.38900  -3.04100  61.92300 1.000 19.92000 ? 406 THR A N   1 
ATOM   2980 C CA  . THR A 1 406 ? 29.02700  -4.19300  61.11100 1.000 19.92000 ? 406 THR A CA  1 
ATOM   2981 C C   . THR A 1 406 ? 27.51300  -4.34000  61.10100 1.000 19.92000 ? 406 THR A C   1 
ATOM   2982 O O   . THR A 1 406 ? 26.83800  -4.02700  62.08500 1.000 19.92000 ? 406 THR A O   1 
ATOM   2983 C CB  . THR A 1 406 ? 29.68200  -5.48000  61.62600 1.000 19.92000 ? 406 THR A CB  1 
ATOM   2984 O OG1 . THR A 1 406 ? 29.14900  -6.60500  60.91500 1.000 19.92000 ? 406 THR A OG1 1 
ATOM   2985 C CG2 . THR A 1 406 ? 29.42600  -5.65600  63.11400 1.000 19.92000 ? 406 THR A CG2 1 
ATOM   2986 N N   . ASP A 1 407 ? 26.98900  -4.80000  59.96900 1.000 19.44000 ? 407 ASP A N   1 
ATOM   2987 C CA  . ASP A 1 407 ? 25.57100  -5.10900  59.84500 1.000 19.44000 ? 407 ASP A CA  1 
ATOM   2988 C C   . ASP A 1 407 ? 25.24300  -6.53800  60.25300 1.000 19.44000 ? 407 ASP A C   1 
ATOM   2989 O O   . ASP A 1 407 ? 24.07300  -6.92900  60.19300 1.000 19.44000 ? 407 ASP A O   1 
ATOM   2990 C CB  . ASP A 1 407 ? 25.08800  -4.84700  58.41300 1.000 19.44000 ? 407 ASP A CB  1 
ATOM   2991 C CG  . ASP A 1 407 ? 26.02600  -5.40700  57.36500 1.000 19.44000 ? 407 ASP A CG  1 
ATOM   2992 O OD1 . ASP A 1 407 ? 26.10300  -6.64600  57.23600 1.000 19.44000 ? 407 ASP A OD1 1 
ATOM   2993 O OD2 . ASP A 1 407 ? 26.68300  -4.60700  56.66700 1.000 19.44000 ? 407 ASP A OD2 1 
ATOM   2994 N N   . SER A 1 408 ? 26.24600  -7.32800  60.64500 1.000 21.89000 ? 408 SER A N   1 
ATOM   2995 C CA  . SER A 1 408 ? 26.02400  -8.69500  61.12400 1.000 21.89000 ? 408 SER A CA  1 
ATOM   2996 C C   . SER A 1 408 ? 27.12000  -9.00600  62.14700 1.000 21.89000 ? 408 SER A C   1 
ATOM   2997 O O   . SER A 1 408 ? 28.18900  -9.51400  61.80000 1.000 21.89000 ? 408 SER A O   1 
ATOM   2998 C CB  . SER A 1 408 ? 26.02100  -9.69800  59.98000 1.000 21.89000 ? 408 SER A CB  1 
ATOM   2999 O OG  . SER A 1 408 ? 25.76100  -11.00800 60.45400 1.000 21.89000 ? 408 SER A OG  1 
ATOM   3000 N N   . LEU A 1 409 ? 26.83700  -8.68200  63.41100 1.000 25.88000 ? 409 LEU A N   1 
ATOM   3001 C CA  . LEU A 1 409 ? 27.77100  -8.96300  64.49500 1.000 25.88000 ? 409 LEU A CA  1 
ATOM   3002 C C   . LEU A 1 409 ? 27.96500  -10.45700 64.72200 1.000 25.88000 ? 409 LEU A C   1 
ATOM   3003 O O   . LEU A 1 409 ? 29.00900  -10.86300 65.24500 1.000 25.88000 ? 409 LEU A O   1 
ATOM   3004 C CB  . LEU A 1 409 ? 27.28500  -8.28900  65.78400 1.000 25.88000 ? 409 LEU A CB  1 
ATOM   3005 C CG  . LEU A 1 409 ? 28.14100  -8.45400  67.04100 1.000 25.88000 ? 409 LEU A CG  1 
ATOM   3006 C CD1 . LEU A 1 409 ? 29.54200  -7.89800  66.82600 1.000 25.88000 ? 409 LEU A CD1 1 
ATOM   3007 C CD2 . LEU A 1 409 ? 27.46900  -7.79300  68.23200 1.000 25.88000 ? 409 LEU A CD2 1 
ATOM   3008 N N   . SER A 1 410 ? 26.99300  -11.28200 64.32300 1.000 28.18000 ? 410 SER A N   1 
ATOM   3009 C CA  . SER A 1 410 ? 27.05600  -12.71800 64.57300 1.000 28.18000 ? 410 SER A CA  1 
ATOM   3010 C C   . SER A 1 410 ? 28.24400  -13.38400 63.88900 1.000 28.18000 ? 410 SER A C   1 
ATOM   3011 O O   . SER A 1 410 ? 28.69900  -14.43200 64.35700 1.000 28.18000 ? 410 SER A O   1 
ATOM   3012 C CB  . SER A 1 410 ? 25.75900  -13.38500 64.10600 1.000 28.18000 ? 410 SER A CB  1 
ATOM   3013 O OG  . SER A 1 410 ? 24.61900  -12.71700 64.62300 1.000 28.18000 ? 410 SER A OG  1 
ATOM   3014 N N   . GLN A 1 411 ? 28.74900  -12.81400 62.79200 1.000 30.11000 ? 411 GLN A N   1 
ATOM   3015 C CA  . GLN A 1 411 ? 29.83100  -13.43300 62.03500 1.000 30.11000 ? 411 GLN A CA  1 
ATOM   3016 C C   . GLN A 1 411 ? 31.21700  -13.14600 62.59700 1.000 30.11000 ? 411 GLN A C   1 
ATOM   3017 O O   . GLN A 1 411 ? 32.19000  -13.72400 62.10400 1.000 30.11000 ? 411 GLN A O   1 
ATOM   3018 C CB  . GLN A 1 411 ? 29.77000  -12.97900 60.57500 1.000 30.11000 ? 411 GLN A CB  1 
ATOM   3019 C CG  . GLN A 1 411 ? 28.52800  -13.45300 59.84300 1.000 30.11000 ? 411 GLN A CG  1 
ATOM   3020 C CD  . GLN A 1 411 ? 28.47700  -12.98200 58.40400 1.000 30.11000 ? 411 GLN A CD  1 
ATOM   3021 O OE1 . GLN A 1 411 ? 27.96700  -11.90000 58.11200 1.000 30.11000 ? 411 GLN A OE1 1 
ATOM   3022 N NE2 . GLN A 1 411 ? 28.99700  -13.79800 57.49400 1.000 30.11000 ? 411 GLN A NE2 1 
ATOM   3023 N N   . VAL A 1 412 ? 31.34400  -12.27200 63.59500 1.000 30.10000 ? 412 VAL A N   1 
ATOM   3024 C CA  . VAL A 1 412 ? 32.65500  -11.95600 64.15700 1.000 30.10000 ? 412 VAL A CA  1 
ATOM   3025 C C   . VAL A 1 412 ? 32.65400  -12.21900 65.65700 1.000 30.10000 ? 412 VAL A C   1 
ATOM   3026 O O   . VAL A 1 412 ? 33.70400  -12.47600 66.25700 1.000 30.10000 ? 412 VAL A O   1 
ATOM   3027 C CB  . VAL A 1 412 ? 33.05700  -10.50200 63.85000 1.000 30.10000 ? 412 VAL A CB  1 
ATOM   3028 C CG1 . VAL A 1 412 ? 33.36000  -10.33900 62.37000 1.000 30.10000 ? 412 VAL A CG1 1 
ATOM   3029 C CG2 . VAL A 1 412 ? 31.95500  -9.54500  64.28100 1.000 30.10000 ? 412 VAL A CG2 1 
ATOM   3030 N N   . TYR A 1 413 ? 31.47700  -12.14900 66.26900 1.000 33.88000 ? 413 TYR A N   1 
ATOM   3031 C CA  . TYR A 1 413 ? 31.28200  -12.44500 67.68800 1.000 33.88000 ? 413 TYR A CA  1 
ATOM   3032 C C   . TYR A 1 413 ? 30.13200  -13.43700 67.76000 1.000 33.88000 ? 413 TYR A C   1 
ATOM   3033 O O   . TYR A 1 413 ? 28.97400  -13.04900 67.96300 1.000 33.88000 ? 413 TYR A O   1 
ATOM   3034 C CB  . TYR A 1 413 ? 31.00900  -11.17800 68.50100 1.000 33.88000 ? 413 TYR A CB  1 
ATOM   3035 C CG  . TYR A 1 413 ? 30.62900  -11.42700 69.94800 1.000 33.88000 ? 413 TYR A CG  1 
ATOM   3036 C CD1 . TYR A 1 413 ? 31.51000  -12.04500 70.82600 1.000 33.88000 ? 413 TYR A CD1 1 
ATOM   3037 C CD2 . TYR A 1 413 ? 29.39300  -11.02500 70.43700 1.000 33.88000 ? 413 TYR A CD2 1 
ATOM   3038 C CE1 . TYR A 1 413 ? 31.16400  -12.26700 72.15000 1.000 33.88000 ? 413 TYR A CE1 1 
ATOM   3039 C CE2 . TYR A 1 413 ? 29.03900  -11.24100 71.75700 1.000 33.88000 ? 413 TYR A CE2 1 
ATOM   3040 C CZ  . TYR A 1 413 ? 29.92600  -11.86100 72.60900 1.000 33.88000 ? 413 TYR A CZ  1 
ATOM   3041 O OH  . TYR A 1 413 ? 29.56700  -12.07300 73.92200 1.000 33.88000 ? 413 TYR A OH  1 
ATOM   3042 N N   . PRO A 1 414 ? 30.41800  -14.73100 67.59000 1.000 34.94000 ? 414 PRO A N   1 
ATOM   3043 C CA  . PRO A 1 414 ? 29.33500  -15.70600 67.36900 1.000 34.94000 ? 414 PRO A CA  1 
ATOM   3044 C C   . PRO A 1 414 ? 28.28800  -15.72400 68.46800 1.000 34.94000 ? 414 PRO A C   1 
ATOM   3045 O O   . PRO A 1 414 ? 27.11200  -15.99200 68.18000 1.000 34.94000 ? 414 PRO A O   1 
ATOM   3046 C CB  . PRO A 1 414 ? 30.08700  -17.04000 67.27400 1.000 34.94000 ? 414 PRO A CB  1 
ATOM   3047 C CG  . PRO A 1 414 ? 31.45500  -16.65900 66.80200 1.000 34.94000 ? 414 PRO A CG  1 
ATOM   3048 C CD  . PRO A 1 414 ? 31.75100  -15.34500 67.46700 1.000 34.94000 ? 414 PRO A CD  1 
ATOM   3049 N N   . GLU A 1 415 ? 28.66900  -15.42200 69.71300 1.000 36.30000 ? 415 GLU A N   1 
ATOM   3050 C CA  . GLU A 1 415 ? 27.68900  -15.35700 70.79200 1.000 36.30000 ? 415 GLU A CA  1 
ATOM   3051 C C   . GLU A 1 415 ? 26.57000  -14.37500 70.47900 1.000 36.30000 ? 415 GLU A C   1 
ATOM   3052 O O   . GLU A 1 415 ? 25.45800  -14.53000 70.99700 1.000 36.30000 ? 415 GLU A O   1 
ATOM   3053 C CB  . GLU A 1 415 ? 28.36000  -14.95500 72.10600 1.000 36.30000 ? 415 GLU A CB  1 
ATOM   3054 C CG  . GLU A 1 415 ? 29.47500  -15.87600 72.56600 1.000 36.30000 ? 415 GLU A CG  1 
ATOM   3055 C CD  . GLU A 1 415 ? 30.07400  -15.43700 73.88800 1.000 36.30000 ? 415 GLU A CD  1 
ATOM   3056 O OE1 . GLU A 1 415 ? 29.54000  -14.48400 74.49500 1.000 36.30000 ? 415 GLU A OE1 1 
ATOM   3057 O OE2 . GLU A 1 415 ? 31.07900  -16.04100 74.31900 1.000 36.30000 ? 415 GLU A OE2 1 
ATOM   3058 N N   . ALA A 1 416 ? 26.82400  -13.40200 69.60000 1.000 30.81000 ? 416 ALA A N   1 
ATOM   3059 C CA  . ALA A 1 416 ? 25.80200  -12.43100 69.23400 1.000 30.81000 ? 416 ALA A CA  1 
ATOM   3060 C C   . ALA A 1 416 ? 24.56800  -13.08900 68.63800 1.000 30.81000 ? 416 ALA A C   1 
ATOM   3061 O O   . ALA A 1 416 ? 23.50700  -12.45600 68.59700 1.000 30.81000 ? 416 ALA A O   1 
ATOM   3062 C CB  . ALA A 1 416 ? 26.36800  -11.40600 68.25000 1.000 30.81000 ? 416 ALA A CB  1 
ATOM   3063 N N   . GLU A 1 417 ? 24.67400  -14.34100 68.18000 1.000 29.33000 ? 417 GLU A N   1 
ATOM   3064 C CA  . GLU A 1 417 ? 23.48800  -15.02000 67.66900 1.000 29.33000 ? 417 GLU A CA  1 
ATOM   3065 C C   . GLU A 1 417 ? 22.38700  -15.09100 68.71900 1.000 29.33000 ? 417 GLU A C   1 
ATOM   3066 O O   . GLU A 1 417 ? 21.20200  -15.11300 68.36800 1.000 29.33000 ? 417 GLU A O   1 
ATOM   3067 C CB  . GLU A 1 417 ? 23.83500  -16.43300 67.19600 1.000 29.33000 ? 417 GLU A CB  1 
ATOM   3068 C CG  . GLU A 1 417 ? 24.73900  -16.49900 65.98200 1.000 29.33000 ? 417 GLU A CG  1 
ATOM   3069 C CD  . GLU A 1 417 ? 24.68100  -17.85000 65.29600 1.000 29.33000 ? 417 GLU A CD  1 
ATOM   3070 O OE1 . GLU A 1 417 ? 23.56100  -18.31600 64.99200 1.000 29.33000 ? 417 GLU A OE1 1 
ATOM   3071 O OE2 . GLU A 1 417 ? 25.75400  -18.44700 65.06600 1.000 29.33000 ? 417 GLU A OE2 1 
ATOM   3072 N N   . LYS A 1 418 ? 22.74900  -15.13400 70.00600 1.000 29.93000 ? 418 LYS A N   1 
ATOM   3073 C CA  . LYS A 1 418 ? 21.71400  -15.16800 71.03600 1.000 29.93000 ? 418 LYS A CA  1 
ATOM   3074 C C   . LYS A 1 418 ? 20.95100  -13.85000 71.12100 1.000 29.93000 ? 418 LYS A C   1 
ATOM   3075 O O   . LYS A 1 418 ? 19.77200  -13.84700 71.49500 1.000 29.93000 ? 418 LYS A O   1 
ATOM   3076 C CB  . LYS A 1 418 ? 22.31300  -15.53800 72.39300 1.000 29.93000 ? 418 LYS A CB  1 
ATOM   3077 C CG  . LYS A 1 418 ? 23.19200  -14.48300 73.02600 1.000 29.93000 ? 418 LYS A CG  1 
ATOM   3078 C CD  . LYS A 1 418 ? 23.73200  -14.96500 74.36000 1.000 29.93000 ? 418 LYS A CD  1 
ATOM   3079 C CE  . LYS A 1 418 ? 24.90700  -14.12000 74.81600 1.000 29.93000 ? 418 LYS A CE  1 
ATOM   3080 N NZ  . LYS A 1 418 ? 25.34100  -14.46800 76.19700 1.000 29.93000 ? 418 LYS A NZ  1 
ATOM   3081 N N   . PHE A 1 419 ? 21.58500  -12.72800 70.77700 1.000 26.31000 ? 419 PHE A N   1 
ATOM   3082 C CA  . PHE A 1 419 ? 20.90900  -11.43400 70.76000 1.000 26.31000 ? 419 PHE A CA  1 
ATOM   3083 C C   . PHE A 1 419 ? 20.91300  -10.83200 69.36000 1.000 26.31000 ? 419 PHE A C   1 
ATOM   3084 O O   . PHE A 1 419 ? 21.07300  -9.62300  69.17800 1.000 26.31000 ? 419 PHE A O   1 
ATOM   3085 C CB  . PHE A 1 419 ? 21.50900  -10.46600 71.78200 1.000 26.31000 ? 419 PHE A CB  1 
ATOM   3086 C CG  . PHE A 1 419 ? 23.01000  -10.34000 71.72600 1.000 26.31000 ? 419 PHE A CG  1 
ATOM   3087 C CD1 . PHE A 1 419 ? 23.61800  -9.45400  70.85300 1.000 26.31000 ? 419 PHE A CD1 1 
ATOM   3088 C CD2 . PHE A 1 419 ? 23.81000  -11.07300 72.58700 1.000 26.31000 ? 419 PHE A CD2 1 
ATOM   3089 C CE1 . PHE A 1 419 ? 24.99600  -9.32500  70.81700 1.000 26.31000 ? 419 PHE A CE1 1 
ATOM   3090 C CE2 . PHE A 1 419 ? 25.18800  -10.94900 72.55600 1.000 26.31000 ? 419 PHE A CE2 1 
ATOM   3091 C CZ  . PHE A 1 419 ? 25.78000  -10.07100 71.67300 1.000 26.31000 ? 419 PHE A CZ  1 
ATOM   3092 N N   . LYS A 1 420 ? 20.72000  -11.68500 68.34900 1.000 22.53000 ? 420 LYS A N   1 
ATOM   3093 C CA  . LYS A 1 420 ? 20.60000  -11.20200 66.97900 1.000 22.53000 ? 420 LYS A CA  1 
ATOM   3094 C C   . LYS A 1 420 ? 19.35800  -10.34300 66.79100 1.000 22.53000 ? 420 LYS A C   1 
ATOM   3095 O O   . LYS A 1 420 ? 19.33300  -9.47000  65.91700 1.000 22.53000 ? 420 LYS A O   1 
ATOM   3096 C CB  . LYS A 1 420 ? 20.56200  -12.37900 66.00600 1.000 22.53000 ? 420 LYS A CB  1 
ATOM   3097 C CG  . LYS A 1 420 ? 19.34300  -13.27600 66.19200 1.000 22.53000 ? 420 LYS A CG  1 
ATOM   3098 C CD  . LYS A 1 420 ? 19.05100  -14.09100 64.94600 1.000 22.53000 ? 420 LYS A CD  1 
ATOM   3099 C CE  . LYS A 1 420 ? 17.83500  -14.99000 65.12000 1.000 22.53000 ? 420 LYS A CE  1 
ATOM   3100 N NZ  . LYS A 1 420 ? 16.55500  -14.23000 65.10600 1.000 22.53000 ? 420 LYS A NZ  1 
ATOM   3101 N N   . ASP A 1 421 ? 18.32000  -10.57400 67.59200 1.000 22.23000 ? 421 ASP A N   1 
ATOM   3102 C CA  . ASP A 1 421 ? 17.04600  -9.89900  67.39700 1.000 22.23000 ? 421 ASP A CA  1 
ATOM   3103 C C   . ASP A 1 421 ? 17.00900  -8.50100  67.99600 1.000 22.23000 ? 421 ASP A C   1 
ATOM   3104 O O   . ASP A 1 421 ? 16.02900  -7.77900  67.77700 1.000 22.23000 ? 421 ASP A O   1 
ATOM   3105 C CB  . ASP A 1 421 ? 15.92000  -10.75100 67.98300 1.000 22.23000 ? 421 ASP A CB  1 
ATOM   3106 C CG  . ASP A 1 421 ? 15.86100  -12.13100 67.36200 1.000 22.23000 ? 421 ASP A CG  1 
ATOM   3107 O OD1 . ASP A 1 421 ? 16.10600  -12.23900 66.14100 1.000 22.23000 ? 421 ASP A OD1 1 
ATOM   3108 O OD2 . ASP A 1 421 ? 15.58500  -13.10600 68.09200 1.000 22.23000 ? 421 ASP A OD2 1 
ATOM   3109 N N   . VAL A 1 422 ? 18.03500  -8.10400  68.74700 1.000 22.12000 ? 422 VAL A N   1 
ATOM   3110 C CA  . VAL A 1 422 ? 18.09500  -6.75800  69.30400 1.000 22.12000 ? 422 VAL A CA  1 
ATOM   3111 C C   . VAL A 1 422 ? 19.37200  -6.06800  68.84300 1.000 22.12000 ? 422 VAL A C   1 
ATOM   3112 O O   . VAL A 1 422 ? 19.42400  -4.83600  68.75200 1.000 22.12000 ? 422 VAL A O   1 
ATOM   3113 C CB  . VAL A 1 422 ? 18.00400  -6.78000  70.84100 1.000 22.12000 ? 422 VAL A CB  1 
ATOM   3114 C CG1 . VAL A 1 422 ? 16.62300  -7.24100  71.28400 1.000 22.12000 ? 422 VAL A CG1 1 
ATOM   3115 C CG2 . VAL A 1 422 ? 19.08500  -7.67400  71.43000 1.000 22.12000 ? 422 VAL A CG2 1 
ATOM   3116 N N   . ALA A 1 423 ? 20.40800  -6.85100  68.53900 1.000 19.57000 ? 423 ALA A N   1 
ATOM   3117 C CA  . ALA A 1 423 ? 21.70700  -6.30100  68.17500 1.000 19.57000 ? 423 ALA A CA  1 
ATOM   3118 C C   . ALA A 1 423 ? 22.39500  -7.17700  67.12400 1.000 19.57000 ? 423 ALA A C   1 
ATOM   3119 O O   . ALA A 1 423 ? 23.51000  -7.65700  67.30500 1.000 19.57000 ? 423 ALA A O   1 
ATOM   3120 C CB  . ALA A 1 423 ? 22.58700  -6.13900  69.41300 1.000 19.57000 ? 423 ALA A CB  1 
ATOM   3121 N N   . SER A 1 424 ? 21.71100  -7.41400  66.00000 1.000 19.73000 ? 424 SER A N   1 
ATOM   3122 C CA  . SER A 1 424 ? 22.38600  -8.02600  64.85800 1.000 19.73000 ? 424 SER A CA  1 
ATOM   3123 C C   . SER A 1 424 ? 23.43800  -7.09200  64.27600 1.000 19.73000 ? 424 SER A C   1 
ATOM   3124 O O   . SER A 1 424 ? 24.49900  -7.54100  63.83000 1.000 19.73000 ? 424 SER A O   1 
ATOM   3125 C CB  . SER A 1 424 ? 21.37600  -8.41200  63.78000 1.000 19.73000 ? 424 SER A CB  1 
ATOM   3126 O OG  . SER A 1 424 ? 20.69000  -9.59900  64.12600 1.000 19.73000 ? 424 SER A OG  1 
ATOM   3127 N N   . GLY A 1 425 ? 23.16800  -5.79000  64.28800 1.000 17.83000 ? 425 GLY A N   1 
ATOM   3128 C CA  . GLY A 1 425 ? 24.09200  -4.79400  63.78700 1.000 17.83000 ? 425 GLY A CA  1 
ATOM   3129 C C   . GLY A 1 425 ? 24.66400  -3.99700  64.94100 1.000 17.83000 ? 425 GLY A C   1 
ATOM   3130 O O   . GLY A 1 425 ? 23.98400  -3.75200  65.94000 1.000 17.83000 ? 425 GLY A O   1 
ATOM   3131 N N   . LEU A 1 426 ? 25.91800  -3.58200  64.79700 1.000 18.80000 ? 426 LEU A N   1 
ATOM   3132 C CA  . LEU A 1 426 ? 26.62300  -2.92700  65.88500 1.000 18.80000 ? 426 LEU A CA  1 
ATOM   3133 C C   . LEU A 1 426 ? 27.48000  -1.79000  65.35300 1.000 18.80000 ? 426 LEU A C   1 
ATOM   3134 O O   . LEU A 1 426 ? 28.05200  -1.88300  64.26200 1.000 18.80000 ? 426 LEU A O   1 
ATOM   3135 C CB  . LEU A 1 426 ? 27.50300  -3.92600  66.65200 1.000 18.80000 ? 426 LEU A CB  1 
ATOM   3136 C CG  . LEU A 1 426 ? 28.50800  -3.36200  67.66000 1.000 18.80000 ? 426 LEU A CG  1 
ATOM   3137 C CD1 . LEU A 1 426 ? 27.79500  -2.67200  68.81100 1.000 18.80000 ? 426 LEU A CD1 1 
ATOM   3138 C CD2 . LEU A 1 426 ? 29.43200  -4.45200  68.17500 1.000 18.80000 ? 426 LEU A CD2 1 
ATOM   3139 N N   . ILE A 1 427 ? 27.54600  -0.71400  66.13300 1.000 19.19000 ? 427 ILE A N   1 
ATOM   3140 C CA  . ILE A 1 427 ? 28.53400  0.34300   65.96800 1.000 19.19000 ? 427 ILE A CA  1 
ATOM   3141 C C   . ILE A 1 427 ? 29.16800  0.56100   67.33300 1.000 19.19000 ? 427 ILE A C   1 
ATOM   3142 O O   . ILE A 1 427 ? 28.53100  1.12000   68.23500 1.000 19.19000 ? 427 ILE A O   1 
ATOM   3143 C CB  . ILE A 1 427 ? 27.93000  1.65000   65.43900 1.000 19.19000 ? 427 ILE A CB  1 
ATOM   3144 C CG1 . ILE A 1 427 ? 27.40600  1.47600   64.01700 1.000 19.19000 ? 427 ILE A CG1 1 
ATOM   3145 C CG2 . ILE A 1 427 ? 28.97100  2.75000   65.45800 1.000 19.19000 ? 427 ILE A CG2 1 
ATOM   3146 C CD1 . ILE A 1 427 ? 27.05300  2.78600   63.35200 1.000 19.19000 ? 427 ILE A CD1 1 
ATOM   3147 N N   . ALA A 1 428 ? 30.40400  0.10500   67.49700 1.000 24.01000 ? 428 ALA A N   1 
ATOM   3148 C CA  . ALA A 1 428 ? 31.17000  0.37200   68.70400 1.000 24.01000 ? 428 ALA A CA  1 
ATOM   3149 C C   . ALA A 1 428 ? 32.00700  1.62800   68.50600 1.000 24.01000 ? 428 ALA A C   1 
ATOM   3150 O O   . ALA A 1 428 ? 32.71400  1.76200   67.50000 1.000 24.01000 ? 428 ALA A O   1 
ATOM   3151 C CB  . ALA A 1 428 ? 32.06700  -0.81600  69.05300 1.000 24.01000 ? 428 ALA A CB  1 
ATOM   3152 N N   . LEU A 1 429 ? 31.91800  2.54400   69.46500 1.000 28.56000 ? 429 LEU A N   1 
ATOM   3153 C CA  . LEU A 1 429 ? 32.69800  3.77800   69.47400 1.000 28.56000 ? 429 LEU A CA  1 
ATOM   3154 C C   . LEU A 1 429 ? 33.52100  3.78000   70.75600 1.000 28.56000 ? 429 LEU A C   1 
ATOM   3155 O O   . LEU A 1 429 ? 32.99800  4.06600   71.83800 1.000 28.56000 ? 429 LEU A O   1 
ATOM   3156 C CB  . LEU A 1 429 ? 31.79800  5.00600   69.38600 1.000 28.56000 ? 429 LEU A CB  1 
ATOM   3157 C CG  . LEU A 1 429 ? 32.52800  6.34800   69.33600 1.000 28.56000 ? 429 LEU A CG  1 
ATOM   3158 C CD1 . LEU A 1 429 ? 33.21000  6.53300   67.98900 1.000 28.56000 ? 429 LEU A CD1 1 
ATOM   3159 C CD2 . LEU A 1 429 ? 31.57100  7.49100   69.63000 1.000 28.56000 ? 429 LEU A CD2 1 
ATOM   3160 N N   . SER A 1 430 ? 34.80800  3.46500   70.63300 1.000 34.17000 ? 430 SER A N   1 
ATOM   3161 C CA  . SER A 1 430 ? 35.69800  3.35500   71.78700 1.000 34.17000 ? 430 SER A CA  1 
ATOM   3162 C C   . SER A 1 430 ? 36.16200  4.75400   72.16700 1.000 34.17000 ? 430 SER A C   1 
ATOM   3163 O O   . SER A 1 430 ? 37.16100  5.26400   71.65700 1.000 34.17000 ? 430 SER A O   1 
ATOM   3164 C CB  . SER A 1 430 ? 36.87500  2.44000   71.47200 1.000 34.17000 ? 430 SER A CB  1 
ATOM   3165 O OG  . SER A 1 430 ? 37.72400  2.29700   72.59600 1.000 34.17000 ? 430 SER A OG  1 
ATOM   3166 N N   . ILE A 1 431 ? 35.40700  5.39200   73.06500 1.000 35.18000 ? 431 ILE A N   1 
ATOM   3167 C CA  . ILE A 1 431 ? 35.77800  6.72500   73.53200 1.000 35.18000 ? 431 ILE A CA  1 
ATOM   3168 C C   . ILE A 1 431 ? 37.11200  6.69000   74.26300 1.000 35.18000 ? 431 ILE A C   1 
ATOM   3169 O O   . ILE A 1 431 ? 37.90200  7.63900   74.17700 1.000 35.18000 ? 431 ILE A O   1 
ATOM   3170 C CB  . ILE A 1 431 ? 34.66200  7.30400   74.42400 1.000 35.18000 ? 431 ILE A CB  1 
ATOM   3171 C CG1 . ILE A 1 431 ? 33.36700  7.46000   73.62800 1.000 35.18000 ? 431 ILE A CG1 1 
ATOM   3172 C CG2 . ILE A 1 431 ? 35.07600  8.64200   75.01300 1.000 35.18000 ? 431 ILE A CG2 1 
ATOM   3173 C CD1 . ILE A 1 431 ? 32.26100  8.11100   74.41900 1.000 35.18000 ? 431 ILE A CD1 1 
ATOM   3174 N N   . SER A 1 432 ? 37.40200  5.59700   74.96500 1.000 41.54000 ? 432 SER A N   1 
ATOM   3175 C CA  . SER A 1 432 ? 38.66400  5.48800   75.69500 1.000 41.54000 ? 432 SER A CA  1 
ATOM   3176 C C   . SER A 1 432 ? 38.96300  4.02300   75.95800 1.000 41.54000 ? 432 SER A C   1 
ATOM   3177 O O   . SER A 1 432 ? 38.17000  3.33400   76.61300 1.000 41.54000 ? 432 SER A O   1 
ATOM   3178 C CB  . SER A 1 432 ? 38.61100  6.27000   77.00500 1.000 41.54000 ? 432 SER A CB  1 
ATOM   3179 O OG  . SER A 1 432 ? 39.87400  6.24700   77.64700 1.000 41.54000 ? 432 SER A OG  1 
ATOM   3180 N N   . LYS A 1 433 ? 40.10700  3.55200   75.45400 1.000 47.33000 ? 433 LYS A N   1 
ATOM   3181 C CA  . LYS A 1 433 ? 40.51900  2.17300   75.69100 1.000 47.33000 ? 433 LYS A CA  1 
ATOM   3182 C C   . LYS A 1 433 ? 40.97000  1.96600   77.13200 1.000 47.33000 ? 433 LYS A C   1 
ATOM   3183 O O   . LYS A 1 433 ? 40.61800  0.96000   77.76000 1.000 47.33000 ? 433 LYS A O   1 
ATOM   3184 C CB  . LYS A 1 433 ? 41.63800  1.79800   74.71800 1.000 47.33000 ? 433 LYS A CB  1 
ATOM   3185 C CG  . LYS A 1 433 ? 42.09600  0.35100   74.79400 1.000 47.33000 ? 433 LYS A CG  1 
ATOM   3186 C CD  . LYS A 1 433 ? 41.07700  -0.58700  74.17100 1.000 47.33000 ? 433 LYS A CD  1 
ATOM   3187 C CE  . LYS A 1 433 ? 41.73400  -1.51600  73.16400 1.000 47.33000 ? 433 LYS A CE  1 
ATOM   3188 N NZ  . LYS A 1 433 ? 42.87200  -2.26700  73.76200 1.000 47.33000 ? 433 LYS A NZ  1 
ATOM   3189 N N   . THR A 1 434 ? 41.75200  2.90500   77.67400 1.000 49.00000 ? 434 THR A N   1 
ATOM   3190 C CA  . THR A 1 434 ? 42.27500  2.75200   79.02900 1.000 49.00000 ? 434 THR A CA  1 
ATOM   3191 C C   . THR A 1 434 ? 41.20700  3.01100   80.08700 1.000 49.00000 ? 434 THR A C   1 
ATOM   3192 O O   . THR A 1 434 ? 41.19900  2.35400   81.13500 1.000 49.00000 ? 434 THR A O   1 
ATOM   3193 C CB  . THR A 1 434 ? 43.47200  3.68400   79.24000 1.000 49.00000 ? 434 THR A CB  1 
ATOM   3194 O OG1 . THR A 1 434 ? 43.80400  3.73500   80.63400 1.000 49.00000 ? 434 THR A OG1 1 
ATOM   3195 C CG2 . THR A 1 434 ? 43.16100  5.09000   78.73900 1.000 49.00000 ? 434 THR A CG2 1 
ATOM   3196 N N   . GLN A 1 435 ? 40.30000  3.95300   79.83300 1.000 45.23000 ? 435 GLN A N   1 
ATOM   3197 C CA  . GLN A 1 435 ? 39.24100  4.27700   80.78000 1.000 45.23000 ? 435 GLN A CA  1 
ATOM   3198 C C   . GLN A 1 435 ? 38.04600  3.34100   80.68100 1.000 45.23000 ? 435 GLN A C   1 
ATOM   3199 O O   . GLN A 1 435 ? 37.12500  3.46000   81.49600 1.000 45.23000 ? 435 GLN A O   1 
ATOM   3200 C CB  . GLN A 1 435 ? 38.77200  5.72100   80.58400 1.000 45.23000 ? 435 GLN A CB  1 
ATOM   3201 C CG  . GLN A 1 435 ? 39.83800  6.77500   80.83700 1.000 45.23000 ? 435 GLN A CG  1 
ATOM   3202 C CD  . GLN A 1 435 ? 39.29000  8.18900   80.75100 1.000 45.23000 ? 435 GLN A CD  1 
ATOM   3203 O OE1 . GLN A 1 435 ? 38.35600  8.55000   81.46900 1.000 45.23000 ? 435 GLN A OE1 1 
ATOM   3204 N NE2 . GLN A 1 435 ? 39.86500  8.99600   79.86600 1.000 45.23000 ? 435 GLN A NE2 1 
ATOM   3205 N N   . ASN A 1 436 ? 38.03800  2.42500   79.70800 1.000 43.31000 ? 436 ASN A N   1 
ATOM   3206 C CA  . ASN A 1 436 ? 36.90200  1.53700   79.46000 1.000 43.31000 ? 436 ASN A CA  1 
ATOM   3207 C C   . ASN A 1 436 ? 35.63400  2.34600   79.18600 1.000 43.31000 ? 436 ASN A C   1 
ATOM   3208 O O   . ASN A 1 436 ? 34.59200  2.14800   79.81500 1.000 43.31000 ? 436 ASN A O   1 
ATOM   3209 C CB  . ASN A 1 436 ? 36.69800  0.56000   80.62300 1.000 43.31000 ? 436 ASN A CB  1 
ATOM   3210 C CG  . ASN A 1 436 ? 35.83800  -0.63600  80.24500 1.000 43.31000 ? 436 ASN A CG  1 
ATOM   3211 O OD1 . ASN A 1 436 ? 34.99200  -0.55700  79.35400 1.000 43.31000 ? 436 ASN A OD1 1 
ATOM   3212 N ND2 . ASN A 1 436 ? 36.05400  -1.75300  80.92700 1.000 43.31000 ? 436 ASN A ND2 1 
ATOM   3213 N N   . LYS A 1 437 ? 35.73800  3.28900   78.25300 1.000 39.83000 ? 437 LYS A N   1 
ATOM   3214 C CA  . LYS A 1 437 ? 34.61600  4.13400   77.85900 1.000 39.83000 ? 437 LYS A CA  1 
ATOM   3215 C C   . LYS A 1 437 ? 34.22900  3.78200   76.42700 1.000 39.83000 ? 437 LYS A C   1 
ATOM   3216 O O   . LYS A 1 437 ? 35.01200  4.00300   75.49600 1.000 39.83000 ? 437 LYS A O   1 
ATOM   3217 C CB  . LYS A 1 437 ? 34.97400  5.61400   77.99600 1.000 39.83000 ? 437 LYS A CB  1 
ATOM   3218 C CG  . LYS A 1 437 ? 35.14800  6.08100   79.43500 1.000 39.83000 ? 437 LYS A CG  1 
ATOM   3219 C CD  . LYS A 1 437 ? 35.83400  7.44000   79.50400 1.000 39.83000 ? 437 LYS A CD  1 
ATOM   3220 C CE  . LYS A 1 437 ? 35.08300  8.49300   78.70700 1.000 39.83000 ? 437 LYS A CE  1 
ATOM   3221 N NZ  . LYS A 1 437 ? 35.81000  9.79400   78.69800 1.000 39.83000 ? 437 LYS A NZ  1 
ATOM   3222 N N   . TYR A 1 438 ? 33.01400  3.25900   76.25400 1.000 34.89000 ? 438 TYR A N   1 
ATOM   3223 C CA  . TYR A 1 438 ? 32.51500  2.81100   74.96300 1.000 34.89000 ? 438 TYR A CA  1 
ATOM   3224 C C   . TYR A 1 438 ? 31.09800  3.32100   74.73800 1.000 34.89000 ? 438 TYR A C   1 
ATOM   3225 O O   . TYR A 1 438 ? 30.36200  3.62900   75.68100 1.000 34.89000 ? 438 TYR A O   1 
ATOM   3226 C CB  . TYR A 1 438 ? 32.50400  1.27700   74.84700 1.000 34.89000 ? 438 TYR A CB  1 
ATOM   3227 C CG  . TYR A 1 438 ? 33.86100  0.60900   74.84600 1.000 34.89000 ? 438 TYR A CG  1 
ATOM   3228 C CD1 . TYR A 1 438 ? 34.61800  0.53200   73.68400 1.000 34.89000 ? 438 TYR A CD1 1 
ATOM   3229 C CD2 . TYR A 1 438 ? 34.37200  0.02900   76.00000 1.000 34.89000 ? 438 TYR A CD2 1 
ATOM   3230 C CE1 . TYR A 1 438 ? 35.85400  -0.08700  73.67600 1.000 34.89000 ? 438 TYR A CE1 1 
ATOM   3231 C CE2 . TYR A 1 438 ? 35.60700  -0.59200  76.00200 1.000 34.89000 ? 438 TYR A CE2 1 
ATOM   3232 C CZ  . TYR A 1 438 ? 36.34300  -0.64700  74.83700 1.000 34.89000 ? 438 TYR A CZ  1 
ATOM   3233 O OH  . TYR A 1 438 ? 37.57400  -1.26300  74.83100 1.000 34.89000 ? 438 TYR A OH  1 
ATOM   3234 N N   . VAL A 1 439 ? 30.72300  3.39700   73.46400 1.000 25.60000 ? 439 VAL A N   1 
ATOM   3235 C CA  . VAL A 1 439 ? 29.34100  3.59900   73.04800 1.000 25.60000 ? 439 VAL A CA  1 
ATOM   3236 C C   . VAL A 1 439 ? 29.00800  2.51600   72.03200 1.000 25.60000 ? 439 VAL A C   1 
ATOM   3237 O O   . VAL A 1 439 ? 29.76900  2.29700   71.08400 1.000 25.60000 ? 439 VAL A O   1 
ATOM   3238 C CB  . VAL A 1 439 ? 29.10900  4.99800   72.44700 1.000 25.60000 ? 439 VAL A CB  1 
ATOM   3239 C CG1 . VAL A 1 439 ? 27.67900  5.12700   71.96000 1.000 25.60000 ? 439 VAL A CG1 1 
ATOM   3240 C CG2 . VAL A 1 439 ? 29.41700  6.07600   73.47100 1.000 25.60000 ? 439 VAL A CG2 1 
ATOM   3241 N N   . LEU A 1 440 ? 27.87900  1.83700   72.23000 1.000 21.30000 ? 440 LEU A N   1 
ATOM   3242 C CA  . LEU A 1 440 ? 27.48900  0.70800   71.38900 1.000 21.30000 ? 440 LEU A CA  1 
ATOM   3243 C C   . LEU A 1 440 ? 26.07400  0.93400   70.88000 1.000 21.30000 ? 440 LEU A C   1 
ATOM   3244 O O   . LEU A 1 440 ? 25.11800  0.86400   71.65800 1.000 21.30000 ? 440 LEU A O   1 
ATOM   3245 C CB  . LEU A 1 440 ? 27.56400  -0.60900  72.16200 1.000 21.30000 ? 440 LEU A CB  1 
ATOM   3246 C CG  . LEU A 1 440 ? 28.75800  -0.89400  73.06800 1.000 21.30000 ? 440 LEU A CG  1 
ATOM   3247 C CD1 . LEU A 1 440 ? 28.51500  -2.18800  73.82600 1.000 21.30000 ? 440 LEU A CD1 1 
ATOM   3248 C CD2 . LEU A 1 440 ? 30.03900  -0.97500  72.26100 1.000 21.30000 ? 440 LEU A CD2 1 
ATOM   3249 N N   . TRP A 1 441 ? 25.93700  1.22100   69.59100 1.000 18.19000 ? 441 TRP A N   1 
ATOM   3250 C CA  . TRP A 1 441 ? 24.63000  1.22300   68.95200 1.000 18.19000 ? 441 TRP A CA  1 
ATOM   3251 C C   . TRP A 1 441 ? 24.26100  -0.18900  68.50600 1.000 18.19000 ? 441 TRP A C   1 
ATOM   3252 O O   . TRP A 1 441 ? 25.12400  -0.98800  68.13300 1.000 18.19000 ? 441 TRP A O   1 
ATOM   3253 C CB  . TRP A 1 441 ? 24.61000  2.18500   67.76500 1.000 18.19000 ? 441 TRP A CB  1 
ATOM   3254 C CG  . TRP A 1 441 ? 24.71900  3.62900   68.17100 1.000 18.19000 ? 441 TRP A CG  1 
ATOM   3255 C CD1 . TRP A 1 441 ? 23.69300  4.47000   68.49300 1.000 18.19000 ? 441 TRP A CD1 1 
ATOM   3256 C CD2 . TRP A 1 441 ? 25.92200  4.39700   68.30400 1.000 18.19000 ? 441 TRP A CD2 1 
ATOM   3257 N NE1 . TRP A 1 441 ? 24.18100  5.71400   68.81100 1.000 18.19000 ? 441 TRP A NE1 1 
ATOM   3258 C CE2 . TRP A 1 441 ? 25.54700  5.69600   68.70400 1.000 18.19000 ? 441 TRP A CE2 1 
ATOM   3259 C CE3 . TRP A 1 441 ? 27.27900  4.11400   68.12300 1.000 18.19000 ? 441 TRP A CE3 1 
ATOM   3260 C CZ2 . TRP A 1 441 ? 26.47900  6.70700   68.92400 1.000 18.19000 ? 441 TRP A CZ2 1 
ATOM   3261 C CZ3 . TRP A 1 441 ? 28.20300  5.12000   68.34200 1.000 18.19000 ? 441 TRP A CZ3 1 
ATOM   3262 C CH2 . TRP A 1 441 ? 27.79900  6.40100   68.73700 1.000 18.19000 ? 441 TRP A CH2 1 
ATOM   3263 N N   . PHE A 1 442 ? 22.96300  -0.48400  68.53300 1.000 18.93000 ? 442 PHE A N   1 
ATOM   3264 C CA  . PHE A 1 442 ? 22.44300  -1.81400  68.25000 1.000 18.93000 ? 442 PHE A CA  1 
ATOM   3265 C C   . PHE A 1 442 ? 21.30400  -1.71000  67.24900 1.000 18.93000 ? 442 PHE A C   1 
ATOM   3266 O O   . PHE A 1 442 ? 20.45600  -0.81700  67.35500 1.000 18.93000 ? 442 PHE A O   1 
ATOM   3267 C CB  . PHE A 1 442 ? 21.92100  -2.50000  69.52300 1.000 18.93000 ? 442 PHE A CB  1 
ATOM   3268 C CG  . PHE A 1 442 ? 22.91300  -2.54500  70.65000 1.000 18.93000 ? 442 PHE A CG  1 
ATOM   3269 C CD1 . PHE A 1 442 ? 24.21600  -2.95900  70.43400 1.000 18.93000 ? 442 PHE A CD1 1 
ATOM   3270 C CD2 . PHE A 1 442 ? 22.53700  -2.17600  71.93100 1.000 18.93000 ? 442 PHE A CD2 1 
ATOM   3271 C CE1 . PHE A 1 442 ? 25.12500  -3.00200  71.47600 1.000 18.93000 ? 442 PHE A CE1 1 
ATOM   3272 C CE2 . PHE A 1 442 ? 23.44100  -2.21600  72.97500 1.000 18.93000 ? 442 PHE A CE2 1 
ATOM   3273 C CZ  . PHE A 1 442 ? 24.73600  -2.63000  72.74800 1.000 18.93000 ? 442 PHE A CZ  1 
ATOM   3274 N N   . ARG A 1 443 ? 21.26900  -2.64100  66.29600 1.000 16.95000 ? 443 ARG A N   1 
ATOM   3275 C CA  . ARG A 1 443 ? 20.18600  -2.69100  65.33100 1.000 16.95000 ? 443 ARG A CA  1 
ATOM   3276 C C   . ARG A 1 443 ? 19.61800  -4.10300  65.26100 1.000 16.95000 ? 443 ARG A C   1 
ATOM   3277 O O   . ARG A 1 443 ? 20.37000  -5.08200  65.34200 1.000 16.95000 ? 443 ARG A O   1 
ATOM   3278 C CB  . ARG A 1 443 ? 20.67500  -2.25300  63.94200 1.000 16.95000 ? 443 ARG A CB  1 
ATOM   3279 C CG  . ARG A 1 443 ? 19.82300  -1.17700  63.29100 1.000 16.95000 ? 443 ARG A CG  1 
ATOM   3280 C CD  . ARG A 1 443 ? 20.37300  -0.78300  61.93200 1.000 16.95000 ? 443 ARG A CD  1 
ATOM   3281 N NE  . ARG A 1 443 ? 20.62300  0.65100   61.84600 1.000 16.95000 ? 443 ARG A NE  1 
ATOM   3282 C CZ  . ARG A 1 443 ? 21.09600  1.26800   60.77100 1.000 16.95000 ? 443 ARG A CZ  1 
ATOM   3283 N NH1 . ARG A 1 443 ? 21.38400  0.60400   59.66300 1.000 16.95000 ? 443 ARG A NH1 1 
ATOM   3284 N NH2 . ARG A 1 443 ? 21.28700  2.58300   60.81000 1.000 16.95000 ? 443 ARG A NH2 1 
ATOM   3285 N N   . PRO A 1 444 ? 18.30400  -4.24000  65.10300 1.000 18.23000 ? 444 PRO A N   1 
ATOM   3286 C CA  . PRO A 1 444 ? 17.69500  -5.57200  65.06400 1.000 18.23000 ? 444 PRO A CA  1 
ATOM   3287 C C   . PRO A 1 444 ? 17.99400  -6.29500  63.76100 1.000 18.23000 ? 444 PRO A C   1 
ATOM   3288 O O   . PRO A 1 444 ? 18.35100  -5.69300  62.74600 1.000 18.23000 ? 444 PRO A O   1 
ATOM   3289 C CB  . PRO A 1 444 ? 16.20000  -5.27900  65.20300 1.000 18.23000 ? 444 PRO A CB  1 
ATOM   3290 C CG  . PRO A 1 444 ? 16.04200  -3.95500  64.55700 1.000 18.23000 ? 444 PRO A CG  1 
ATOM   3291 C CD  . PRO A 1 444 ? 17.31400  -3.18500  64.83100 1.000 18.23000 ? 444 PRO A CD  1 
ATOM   3292 N N   . GLU A 1 445 ? 17.84700  -7.61600  63.81100 1.000 20.38000 ? 445 GLU A N   1 
ATOM   3293 C CA  . GLU A 1 445 ? 17.96500  -8.42300  62.60600 1.000 20.38000 ? 445 GLU A CA  1 
ATOM   3294 C C   . GLU A 1 445 ? 16.90500  -8.01500  61.59200 1.000 20.38000 ? 445 GLU A C   1 
ATOM   3295 O O   . GLU A 1 445 ? 15.75400  -7.74300  61.94400 1.000 20.38000 ? 445 GLU A O   1 
ATOM   3296 C CB  . GLU A 1 445 ? 17.81500  -9.90600  62.94400 1.000 20.38000 ? 445 GLU A CB  1 
ATOM   3297 C CG  . GLU A 1 445 ? 18.03200  -10.83700 61.76300 1.000 20.38000 ? 445 GLU A CG  1 
ATOM   3298 C CD  . GLU A 1 445 ? 17.60500  -12.26200 62.05300 1.000 20.38000 ? 445 GLU A CD  1 
ATOM   3299 O OE1 . GLU A 1 445 ? 16.48800  -12.45700 62.57800 1.000 20.38000 ? 445 GLU A OE1 1 
ATOM   3300 O OE2 . GLU A 1 445 ? 18.39100  -13.18800 61.76000 1.000 20.38000 ? 445 GLU A OE2 1 
ATOM   3301 N N   . GLU A 1 446 ? 17.30200  -7.96600  60.32500 1.000 20.19000 ? 446 GLU A N   1 
ATOM   3302 C CA  . GLU A 1 446 ? 16.39300  -7.68300  59.21800 1.000 20.19000 ? 446 GLU A CA  1 
ATOM   3303 C C   . GLU A 1 446 ? 16.44900  -8.88200  58.27900 1.000 20.19000 ? 446 GLU A C   1 
ATOM   3304 O O   . GLU A 1 446 ? 17.36000  -8.98900  57.45300 1.000 20.19000 ? 446 GLU A O   1 
ATOM   3305 C CB  . GLU A 1 446 ? 16.77500  -6.38900  58.50300 1.000 20.19000 ? 446 GLU A CB  1 
ATOM   3306 C CG  . GLU A 1 446 ? 15.70800  -5.85000  57.55600 1.000 20.19000 ? 446 GLU A CG  1 
ATOM   3307 C CD  . GLU A 1 446 ? 14.67800  -4.97700  58.25600 1.000 20.19000 ? 446 GLU A CD  1 
ATOM   3308 O OE1 . GLU A 1 446 ? 14.50400  -5.11800  59.48500 1.000 20.19000 ? 446 GLU A OE1 1 
ATOM   3309 O OE2 . GLU A 1 446 ? 14.04700  -4.14200  57.57300 1.000 20.19000 ? 446 GLU A OE2 1 
ATOM   3310 N N   . VAL A 1 447 ? 15.48600  -9.79100  58.41900 1.000 18.02000 ? 447 VAL A N   1 
ATOM   3311 C CA  . VAL A 1 447 ? 15.44600  -10.97300 57.56700 1.000 18.02000 ? 447 VAL A CA  1 
ATOM   3312 C C   . VAL A 1 447 ? 15.06600  -10.54100 56.15900 1.000 18.02000 ? 447 VAL A C   1 
ATOM   3313 O O   . VAL A 1 447 ? 14.02200  -9.91500  55.94600 1.000 18.02000 ? 447 VAL A O   1 
ATOM   3314 C CB  . VAL A 1 447 ? 14.46100  -12.01200 58.11600 1.000 18.02000 ? 447 VAL A CB  1 
ATOM   3315 C CG1 . VAL A 1 447 ? 14.68300  -13.35600 57.44100 1.000 18.02000 ? 447 VAL A CG1 1 
ATOM   3316 C CG2 . VAL A 1 447 ? 14.59900  -12.12900 59.62600 1.000 18.02000 ? 447 VAL A CG2 1 
ATOM   3317 N N   . GLN A 1 448 ? 15.90900  -10.87700 55.18900 1.000 18.59000 ? 448 GLN A N   1 
ATOM   3318 C CA  . GLN A 1 448 ? 15.70100  -10.47200 53.80600 1.000 18.59000 ? 448 GLN A CA  1 
ATOM   3319 C C   . GLN A 1 448 ? 15.35500  -11.69300 52.96800 1.000 18.59000 ? 448 GLN A C   1 
ATOM   3320 O O   . GLN A 1 448 ? 15.99100  -12.74100 53.09900 1.000 18.59000 ? 448 GLN A O   1 
ATOM   3321 C CB  . GLN A 1 448 ? 16.94100  -9.76300  53.25500 1.000 18.59000 ? 448 GLN A CB  1 
ATOM   3322 C CG  . GLN A 1 448 ? 17.21200  -8.41400  53.91600 1.000 18.59000 ? 448 GLN A CG  1 
ATOM   3323 C CD  . GLN A 1 448 ? 18.69200  -8.14000  54.12600 1.000 18.59000 ? 448 GLN A CD  1 
ATOM   3324 O OE1 . GLN A 1 448 ? 19.53700  -8.59700  53.35700 1.000 18.59000 ? 448 GLN A OE1 1 
ATOM   3325 N NE2 . GLN A 1 448 ? 19.01000  -7.39600  55.18100 1.000 18.59000 ? 448 GLN A NE2 1 
ATOM   3326 N N   . THR A 1 449 ? 14.34600  -11.55900 52.11700 1.000 14.44000 ? 449 THR A N   1 
ATOM   3327 C CA  . THR A 1 449 ? 13.89600  -12.64300 51.25000 1.000 14.44000 ? 449 THR A CA  1 
ATOM   3328 C C   . THR A 1 449 ? 14.17900  -12.21700 49.81300 1.000 14.44000 ? 449 THR A C   1 
ATOM   3329 O O   . THR A 1 449 ? 13.31000  -11.67700 49.12700 1.000 14.44000 ? 449 THR A O   1 
ATOM   3330 C CB  . THR A 1 449 ? 12.42200  -12.94500 51.46700 1.000 14.44000 ? 449 THR A CB  1 
ATOM   3331 O OG1 . THR A 1 449 ? 12.14800  -12.99200 52.87300 1.000 14.44000 ? 449 THR A OG1 1 
ATOM   3332 C CG2 . THR A 1 449 ? 12.06300  -14.28200 50.84300 1.000 14.44000 ? 449 THR A CG2 1 
ATOM   3333 N N   . VAL A 1 450 ? 15.40500  -12.45800 49.36400 1.000 13.50000 ? 450 VAL A N   1 
ATOM   3334 C CA  . VAL A 1 450 ? 15.84100  -12.03300 48.03900 1.000 13.50000 ? 450 VAL A CA  1 
ATOM   3335 C C   . VAL A 1 450 ? 15.40300  -13.07700 47.01900 1.000 13.50000 ? 450 VAL A C   1 
ATOM   3336 O O   . VAL A 1 450 ? 15.85700  -14.22400 47.06300 1.000 13.50000 ? 450 VAL A O   1 
ATOM   3337 C CB  . VAL A 1 450 ? 17.36200  -11.82800 47.99800 1.000 13.50000 ? 450 VAL A CB  1 
ATOM   3338 C CG1 . VAL A 1 450 ? 17.77000  -11.20900 46.67900 1.000 13.50000 ? 450 VAL A CG1 1 
ATOM   3339 C CG2 . VAL A 1 450 ? 17.80900  -10.96100 49.16600 1.000 13.50000 ? 450 VAL A CG2 1 
ATOM   3340 N N   . ASN A 1 451 ? 14.53200  -12.67900 46.09500 1.000 13.42000 ? 451 ASN A N   1 
ATOM   3341 C CA  . ASN A 1 451 ? 13.97100  -13.59500 45.10100 1.000 13.42000 ? 451 ASN A CA  1 
ATOM   3342 C C   . ASN A 1 451 ? 14.78900  -13.50000 43.81900 1.000 13.42000 ? 451 ASN A C   1 
ATOM   3343 O O   . ASN A 1 451 ? 14.64600  -12.55200 43.04500 1.000 13.42000 ? 451 ASN A O   1 
ATOM   3344 C CB  . ASN A 1 451 ? 12.50400  -13.27600 44.84400 1.000 13.42000 ? 451 ASN A CB  1 
ATOM   3345 C CG  . ASN A 1 451 ? 11.64200  -13.47000 46.07200 1.000 13.42000 ? 451 ASN A CG  1 
ATOM   3346 O OD1 . ASN A 1 451 ? 12.13900  -13.46900 47.19900 1.000 13.42000 ? 451 ASN A OD1 1 
ATOM   3347 N ND2 . ASN A 1 451 ? 10.34200  -13.64100 45.86300 1.000 13.42000 ? 451 ASN A ND2 1 
ATOM   3348 N N   . TRP A 1 452 ? 15.65700  -14.48400 43.59600 1.000 14.19000 ? 452 TRP A N   1 
ATOM   3349 C CA  . TRP A 1 452 ? 16.46700  -14.56400 42.39200 1.000 14.19000 ? 452 TRP A CA  1 
ATOM   3350 C C   . TRP A 1 452 ? 15.76400  -15.35600 41.29900 1.000 14.19000 ? 452 TRP A C   1 
ATOM   3351 O O   . TRP A 1 452 ? 14.92500  -16.22100 41.56700 1.000 14.19000 ? 452 TRP A O   1 
ATOM   3352 C CB  . TRP A 1 452 ? 17.81500  -15.21700 42.69800 1.000 14.19000 ? 452 TRP A CB  1 
ATOM   3353 C CG  . TRP A 1 452 ? 18.61000  -14.47800 43.70800 1.000 14.19000 ? 452 TRP A CG  1 
ATOM   3354 C CD1 . TRP A 1 452 ? 18.58300  -14.65100 45.06000 1.000 14.19000 ? 452 TRP A CD1 1 
ATOM   3355 C CD2 . TRP A 1 452 ? 19.55800  -13.43800 43.45400 1.000 14.19000 ? 452 TRP A CD2 1 
ATOM   3356 N NE1 . TRP A 1 452 ? 19.45900  -13.78400 45.66400 1.000 14.19000 ? 452 TRP A NE1 1 
ATOM   3357 C CE2 . TRP A 1 452 ? 20.07000  -13.02700 44.69900 1.000 14.19000 ? 452 TRP A CE2 1 
ATOM   3358 C CE3 . TRP A 1 452 ? 20.02400  -12.81500 42.29200 1.000 14.19000 ? 452 TRP A CE3 1 
ATOM   3359 C CZ2 . TRP A 1 452 ? 21.02600  -12.02000 44.81700 1.000 14.19000 ? 452 TRP A CZ2 1 
ATOM   3360 C CZ3 . TRP A 1 452 ? 20.97300  -11.81500 42.41100 1.000 14.19000 ? 452 TRP A CZ3 1 
ATOM   3361 C CH2 . TRP A 1 452 ? 21.46300  -11.42700 43.66300 1.000 14.19000 ? 452 TRP A CH2 1 
ATOM   3362 N N   . GLY A 1 453 ? 16.12700  -15.05200 40.05500 1.000 16.41000 ? 453 GLY A N   1 
ATOM   3363 C CA  . GLY A 1 453 ? 15.81000  -15.91600 38.93600 1.000 16.41000 ? 453 GLY A CA  1 
ATOM   3364 C C   . GLY A 1 453 ? 16.95600  -16.87400 38.68400 1.000 16.41000 ? 453 GLY A C   1 
ATOM   3365 O O   . GLY A 1 453 ? 17.48700  -16.94500 37.57200 1.000 16.41000 ? 453 GLY A O   1 
ATOM   3366 N N   . GLY A 1 454 ? 17.32400  -17.60900 39.73800 1.000 15.07000 ? 454 GLY A N   1 
ATOM   3367 C CA  . GLY A 1 454 ? 18.49000  -18.50500 39.67400 1.000 15.07000 ? 454 GLY A CA  1 
ATOM   3368 C C   . GLY A 1 454 ? 19.73000  -17.70600 39.98900 1.000 15.07000 ? 454 GLY A C   1 
ATOM   3369 O O   . GLY A 1 454 ? 19.76600  -16.53800 39.59900 1.000 15.07000 ? 454 GLY A O   1 
ATOM   3370 N N   . ASN A 1 455 ? 20.69000  -18.27900 40.70200 1.000 14.48000 ? 455 ASN A N   1 
ATOM   3371 C CA  . ASN A 1 455 ? 21.96700  -17.55800 40.91200 1.000 14.48000 ? 455 ASN A CA  1 
ATOM   3372 C C   . ASN A 1 455 ? 22.99100  -18.52500 41.46800 1.000 14.48000 ? 455 ASN A C   1 
ATOM   3373 O O   . ASN A 1 455 ? 22.59000  -19.38100 42.26500 1.000 14.48000 ? 455 ASN A O   1 
ATOM   3374 C CB  . ASN A 1 455 ? 21.84200  -16.40300 41.89200 1.000 14.48000 ? 455 ASN A CB  1 
ATOM   3375 C CG  . ASN A 1 455 ? 23.12100  -15.61900 42.06500 1.000 14.48000 ? 455 ASN A CG  1 
ATOM   3376 O OD1 . ASN A 1 455 ? 23.93400  -15.54500 41.15400 1.000 14.48000 ? 455 ASN A OD1 1 
ATOM   3377 N ND2 . ASN A 1 455 ? 23.29900  -15.01900 43.22900 1.000 14.48000 ? 455 ASN A ND2 1 
ATOM   3378 N N   . PRO A 1 456 ? 24.24900  -18.53100 40.99900 1.000 30.00000 ? 456 PRO A N   1 
ATOM   3379 C CA  . PRO A 1 456 ? 25.28900  -19.34400 41.61200 1.000 30.00000 ? 456 PRO A CA  1 
ATOM   3380 C C   . PRO A 1 456 ? 26.15500  -18.52700 42.57900 1.000 30.00000 ? 456 PRO A C   1 
ATOM   3381 O O   . PRO A 1 456 ? 27.29800  -18.31400 42.24200 1.000 30.00000 ? 456 PRO A O   1 
ATOM   3382 C CB  . PRO A 1 456 ? 26.15700  -19.76000 40.42200 1.000 30.00000 ? 456 PRO A CB  1 
ATOM   3383 C CG  . PRO A 1 456 ? 25.47400  -19.16100 39.20300 1.000 30.00000 ? 456 PRO A CG  1 
ATOM   3384 C CD  . PRO A 1 456 ? 24.69600  -17.97600 39.73300 1.000 30.00000 ? 456 PRO A CD  1 
ATOM   3385 N N   . GLU A 1 477 ? 14.79200  -20.50600 37.08000 1.000 20.00000 ? 477 GLU A N   1 
ATOM   3386 C CA  . GLU A 1 477 ? 13.64500  -20.69100 37.96200 1.000 20.00000 ? 477 GLU A CA  1 
ATOM   3387 C C   . GLU A 1 477 ? 13.76600  -19.80500 39.20600 1.000 20.00000 ? 477 GLU A C   1 
ATOM   3388 O O   . GLU A 1 477 ? 14.77300  -19.12200 39.39500 1.000 20.00000 ? 477 GLU A O   1 
ATOM   3389 C CB  . GLU A 1 477 ? 13.51300  -22.16300 38.36300 1.000 20.00000 ? 477 GLU A CB  1 
ATOM   3390 C CG  . GLU A 1 477 ? 12.07900  -22.64800 38.52700 1.000 20.00000 ? 477 GLU A CG  1 
ATOM   3391 C CD  . GLU A 1 477 ? 11.99700  -24.10800 38.93600 1.000 20.00000 ? 477 GLU A CD  1 
ATOM   3392 O OE1 . GLU A 1 477 ? 13.02600  -24.66100 39.37800 1.000 20.00000 ? 477 GLU A OE1 1 
ATOM   3393 O OE2 . GLU A 1 477 ? 10.90400  -24.70200 38.81500 1.000 20.00000 ? 477 GLU A OE2 1 
ATOM   3394 N N   . LEU A 1 478 ? 12.72900  -19.81200 40.04000 1.000 15.35000 ? 478 LEU A N   1 
ATOM   3395 C CA  . LEU A 1 478 ? 12.72000  -19.00800 41.25500 1.000 15.35000 ? 478 LEU A CA  1 
ATOM   3396 C C   . LEU A 1 478 ? 13.69500  -19.56400 42.28900 1.000 15.35000 ? 478 LEU A C   1 
ATOM   3397 O O   . LEU A 1 478 ? 13.88700  -20.77700 42.40500 1.000 15.35000 ? 478 LEU A O   1 
ATOM   3398 C CB  . LEU A 1 478 ? 11.30800  -18.95400 41.84000 1.000 15.35000 ? 478 LEU A CB  1 
ATOM   3399 C CG  . LEU A 1 478 ? 11.06700  -18.13400 43.10900 1.000 15.35000 ? 478 LEU A CG  1 
ATOM   3400 C CD1 . LEU A 1 478 ? 11.56500  -16.70700 42.93900 1.000 15.35000 ? 478 LEU A CD1 1 
ATOM   3401 C CD2 . LEU A 1 478 ? 9.58800   -18.14800 43.45700 1.000 15.35000 ? 478 LEU A CD2 1 
ATOM   3402 N N   . TRP A 1 479 ? 14.30900  -18.65700 43.05100 1.000 13.03000 ? 479 TRP A N   1 
ATOM   3403 C CA  . TRP A 1 479 ? 15.23100  -19.03800 44.12100 1.000 13.03000 ? 479 TRP A CA  1 
ATOM   3404 C C   . TRP A 1 479 ? 15.08500  -18.04400 45.26400 1.000 13.03000 ? 479 TRP A C   1 
ATOM   3405 O O   . TRP A 1 479 ? 15.54100  -16.90400 45.15000 1.000 13.03000 ? 479 TRP A O   1 
ATOM   3406 C CB  . TRP A 1 479 ? 16.67400  -19.06400 43.62500 1.000 13.03000 ? 479 TRP A CB  1 
ATOM   3407 C CG  . TRP A 1 479 ? 17.09600  -20.34700 42.99300 1.000 13.03000 ? 479 TRP A CG  1 
ATOM   3408 C CD1 . TRP A 1 479 ? 16.94400  -20.70500 41.68700 1.000 13.03000 ? 479 TRP A CD1 1 
ATOM   3409 C CD2 . TRP A 1 479 ? 17.76200  -21.44100 43.63400 1.000 13.03000 ? 479 TRP A CD2 1 
ATOM   3410 N NE1 . TRP A 1 479 ? 17.46700  -21.95800 41.47500 1.000 13.03000 ? 479 TRP A NE1 1 
ATOM   3411 C CE2 . TRP A 1 479 ? 17.97500  -22.43100 42.65600 1.000 13.03000 ? 479 TRP A CE2 1 
ATOM   3412 C CE3 . TRP A 1 479 ? 18.19500  -21.68100 44.94200 1.000 13.03000 ? 479 TRP A CE3 1 
ATOM   3413 C CZ2 . TRP A 1 479 ? 18.60200  -23.64200 42.94300 1.000 13.03000 ? 479 TRP A CZ2 1 
ATOM   3414 C CZ3 . TRP A 1 479 ? 18.81700  -22.88300 45.22500 1.000 13.03000 ? 479 TRP A CZ3 1 
ATOM   3415 C CH2 . TRP A 1 479 ? 19.01400  -23.84800 44.23000 1.000 13.03000 ? 479 TRP A CH2 1 
ATOM   3416 N N   . LYS A 1 480 ? 14.44300  -18.45700 46.35000 1.000 11.69000 ? 480 LYS A N   1 
ATOM   3417 C CA  . LYS A 1 480 ? 14.46700  -17.64300 47.55600 1.000 11.69000 ? 480 LYS A CA  1 
ATOM   3418 C C   . LYS A 1 480 ? 15.85600  -17.68300 48.18000 1.000 11.69000 ? 480 LYS A C   1 
ATOM   3419 O O   . LYS A 1 480 ? 16.52700  -18.71800 48.17300 1.000 11.69000 ? 480 LYS A O   1 
ATOM   3420 C CB  . LYS A 1 480 ? 13.42400  -18.13400 48.55900 1.000 11.69000 ? 480 LYS A CB  1 
ATOM   3421 C CG  . LYS A 1 480 ? 12.03100  -18.31300 47.97900 1.000 11.69000 ? 480 LYS A CG  1 
ATOM   3422 C CD  . LYS A 1 480 ? 11.52000  -17.03000 47.35300 1.000 11.69000 ? 480 LYS A CD  1 
ATOM   3423 C CE  . LYS A 1 480 ? 10.07500  -17.17400 46.91500 1.000 11.69000 ? 480 LYS A CE  1 
ATOM   3424 N NZ  . LYS A 1 480 ? 9.17400   -17.42700 48.07200 1.000 11.69000 ? 480 LYS A NZ  1 
ATOM   3425 N N   . GLU A 1 481 ? 16.29200  -16.54700 48.71800 1.000 13.09000 ? 481 GLU A N   1 
ATOM   3426 C CA  . GLU A 1 481 ? 17.49800  -16.47900 49.53500 1.000 13.09000 ? 481 GLU A CA  1 
ATOM   3427 C C   . GLU A 1 481 ? 17.12500  -15.80800 50.84500 1.000 13.09000 ? 481 GLU A C   1 
ATOM   3428 O O   . GLU A 1 481 ? 16.68000  -14.65400 50.84700 1.000 13.09000 ? 481 GLU A O   1 
ATOM   3429 C CB  . GLU A 1 481 ? 18.62100  -15.70700 48.83700 1.000 13.09000 ? 481 GLU A CB  1 
ATOM   3430 C CG  . GLU A 1 481 ? 19.92100  -15.69300 49.63200 1.000 13.09000 ? 481 GLU A CG  1 
ATOM   3431 C CD  . GLU A 1 481 ? 20.89800  -14.63700 49.15500 1.000 13.09000 ? 481 GLU A CD  1 
ATOM   3432 O OE1 . GLU A 1 481 ? 20.53000  -13.83400 48.27200 1.000 13.09000 ? 481 GLU A OE1 1 
ATOM   3433 O OE2 . GLU A 1 481 ? 22.03700  -14.60800 49.66800 1.000 13.09000 ? 481 GLU A OE2 1 
ATOM   3434 N N   . ILE A 1 482 ? 17.29000  -16.53300 51.94600 1.000 13.16000 ? 482 ILE A N   1 
ATOM   3435 C CA  . ILE A 1 482 ? 16.87400  -16.07600 53.26500 1.000 13.16000 ? 482 ILE A CA  1 
ATOM   3436 C C   . ILE A 1 482 ? 18.11500  -15.55000 53.97300 1.000 13.16000 ? 482 ILE A C   1 
ATOM   3437 O O   . ILE A 1 482 ? 18.95400  -16.32400 54.44400 1.000 13.16000 ? 482 ILE A O   1 
ATOM   3438 C CB  . ILE A 1 482 ? 16.19000  -17.19100 54.05800 1.000 13.16000 ? 482 ILE A CB  1 
ATOM   3439 C CG1 . ILE A 1 482 ? 15.06500  -17.80800 53.22400 1.000 13.16000 ? 482 ILE A CG1 1 
ATOM   3440 C CG2 . ILE A 1 482 ? 15.64300  -16.65800 55.36800 1.000 13.16000 ? 482 ILE A CG2 1 
ATOM   3441 C CD1 . ILE A 1 482 ? 14.03000  -16.80900 52.74800 1.000 13.16000 ? 482 ILE A CD1 1 
ATOM   3442 N N   . VAL A 1 483 ? 18.24000  -14.22900 54.03800 1.000 16.76000 ? 483 VAL A N   1 
ATOM   3443 C CA  . VAL A 1 483 ? 19.32100  -13.57800 54.76100 1.000 16.76000 ? 483 VAL A CA  1 
ATOM   3444 C C   . VAL A 1 483 ? 18.86400  -13.32700 56.19000 1.000 16.76000 ? 483 VAL A C   1 
ATOM   3445 O O   . VAL A 1 483 ? 17.76200  -12.80800 56.41900 1.000 16.76000 ? 483 VAL A O   1 
ATOM   3446 C CB  . VAL A 1 483 ? 19.73300  -12.26700 54.07500 1.000 16.76000 ? 483 VAL A CB  1 
ATOM   3447 C CG1 . VAL A 1 483 ? 21.05500  -11.77900 54.64200 1.000 16.76000 ? 483 VAL A CG1 1 
ATOM   3448 C CG2 . VAL A 1 483 ? 19.82000  -12.46900 52.57000 1.000 16.76000 ? 483 VAL A CG2 1 
ATOM   3449 N N   . ARG A 1 484 ? 19.72200  -13.67200 57.14600 1.000 19.01000 ? 484 ARG A N   1 
ATOM   3450 C CA  . ARG A 1 484 ? 19.41000  -13.57000 58.56300 1.000 19.01000 ? 484 ARG A CA  1 
ATOM   3451 C C   . ARG A 1 484 ? 20.69900  -13.28200 59.31900 1.000 19.01000 ? 484 ARG A C   1 
ATOM   3452 O O   . ARG A 1 484 ? 21.79900  -13.38000 58.77000 1.000 19.01000 ? 484 ARG A O   1 
ATOM   3453 C CB  . ARG A 1 484 ? 18.72800  -14.84300 59.07500 1.000 19.01000 ? 484 ARG A CB  1 
ATOM   3454 C CG  . ARG A 1 484 ? 19.19200  -16.10800 58.37600 1.000 19.01000 ? 484 ARG A CG  1 
ATOM   3455 C CD  . ARG A 1 484 ? 18.36400  -17.31300 58.79200 1.000 19.01000 ? 484 ARG A CD  1 
ATOM   3456 N NE  . ARG A 1 484 ? 18.66800  -18.48300 57.97700 1.000 19.01000 ? 484 ARG A NE  1 
ATOM   3457 C CZ  . ARG A 1 484 ? 19.67900  -19.31200 58.20100 1.000 19.01000 ? 484 ARG A CZ  1 
ATOM   3458 N NH1 . ARG A 1 484 ? 20.50800  -19.13100 59.21600 1.000 19.01000 ? 484 ARG A NH1 1 
ATOM   3459 N NH2 . ARG A 1 484 ? 19.86400  -20.34600 57.38600 1.000 19.01000 ? 484 ARG A NH2 1 
ATOM   3460 N N   . LEU A 1 485 ? 20.54700  -12.91400 60.59000 1.000 21.18000 ? 485 LEU A N   1 
ATOM   3461 C CA  . LEU A 1 485 ? 21.61500  -12.38300 61.43500 1.000 21.18000 ? 485 LEU A CA  1 
ATOM   3462 C C   . LEU A 1 485 ? 22.16300  -11.06200 60.91000 1.000 21.18000 ? 485 LEU A C   1 
ATOM   3463 O O   . LEU A 1 485 ? 23.18500  -10.57600 61.41000 1.000 21.18000 ? 485 LEU A O   1 
ATOM   3464 C CB  . LEU A 1 485 ? 22.77400  -13.38100 61.60200 1.000 21.18000 ? 485 LEU A CB  1 
ATOM   3465 C CG  . LEU A 1 485 ? 22.51600  -14.87700 61.79700 1.000 21.18000 ? 485 LEU A CG  1 
ATOM   3466 C CD1 . LEU A 1 485 ? 23.83700  -15.63000 61.79500 1.000 21.18000 ? 485 LEU A CD1 1 
ATOM   3467 C CD2 . LEU A 1 485 ? 21.76500  -15.15000 63.07900 1.000 21.18000 ? 485 LEU A CD2 1 
ATOM   3468 N N   . LYS A 1 486 ? 21.50400  -10.46400 59.92000 1.000 19.21000 ? 486 LYS A N   1 
ATOM   3469 C CA  . LYS A 1 486 ? 21.98100  -9.25600  59.26200 1.000 19.21000 ? 486 LYS A CA  1 
ATOM   3470 C C   . LYS A 1 486 ? 20.98400  -8.13400  59.50500 1.000 19.21000 ? 486 LYS A C   1 
ATOM   3471 O O   . LYS A 1 486 ? 19.80600  -8.25500  59.15200 1.000 19.21000 ? 486 LYS A O   1 
ATOM   3472 C CB  . LYS A 1 486 ? 22.17400  -9.49100  57.76200 1.000 19.21000 ? 486 LYS A CB  1 
ATOM   3473 C CG  . LYS A 1 486 ? 23.55300  -9.11400  57.24300 1.000 19.21000 ? 486 LYS A CG  1 
ATOM   3474 C CD  . LYS A 1 486 ? 23.64500  -9.30700  55.73500 1.000 19.21000 ? 486 LYS A CD  1 
ATOM   3475 C CE  . LYS A 1 486 ? 25.02200  -8.93200  55.20300 1.000 19.21000 ? 486 LYS A CE  1 
ATOM   3476 N NZ  . LYS A 1 486 ? 25.07700  -8.98100  53.71400 1.000 19.21000 ? 486 LYS A NZ  1 
ATOM   3477 N N   . SER A 1 487 ? 21.45800  -7.05000  60.10900 1.000 17.56000 ? 487 SER A N   1 
ATOM   3478 C CA  . SER A 1 487 ? 20.64800  -5.86700  60.33100 1.000 17.56000 ? 487 SER A CA  1 
ATOM   3479 C C   . SER A 1 487 ? 20.56100  -5.04000  59.05200 1.000 17.56000 ? 487 SER A C   1 
ATOM   3480 O O   . SER A 1 487 ? 21.21600  -5.32700  58.04600 1.000 17.56000 ? 487 SER A O   1 
ATOM   3481 C CB  . SER A 1 487 ? 21.23300  -5.02500  61.46200 1.000 17.56000 ? 487 SER A CB  1 
ATOM   3482 O OG  . SER A 1 487 ? 22.45900  -4.43700  61.06300 1.000 17.56000 ? 487 SER A OG  1 
ATOM   3483 N N   . LEU A 1 488 ? 19.72900  -4.00700  59.09300 1.000 16.69000 ? 488 LEU A N   1 
ATOM   3484 C CA  . LEU A 1 488 ? 19.71800  -3.04200  58.00600 1.000 16.69000 ? 488 LEU A CA  1 
ATOM   3485 C C   . LEU A 1 488 ? 21.08100  -2.36000  57.94000 1.000 16.69000 ? 488 LEU A C   1 
ATOM   3486 O O   . LEU A 1 488 ? 21.58300  -1.89100  58.97300 1.000 16.69000 ? 488 LEU A O   1 
ATOM   3487 C CB  . LEU A 1 488 ? 18.61200  -2.00800  58.20800 1.000 16.69000 ? 488 LEU A CB  1 
ATOM   3488 C CG  . LEU A 1 488 ? 17.21400  -2.43500  57.76400 1.000 16.69000 ? 488 LEU A CG  1 
ATOM   3489 C CD1 . LEU A 1 488 ? 16.20400  -1.33700  58.04900 1.000 16.69000 ? 488 LEU A CD1 1 
ATOM   3490 C CD2 . LEU A 1 488 ? 17.22100  -2.78700  56.28600 1.000 16.69000 ? 488 LEU A CD2 1 
ATOM   3491 N N   . PRO A 1 489 ? 21.71700  -2.30100  56.77100 1.000 16.65000 ? 489 PRO A N   1 
ATOM   3492 C CA  . PRO A 1 489 ? 23.10600  -1.83000  56.70900 1.000 16.65000 ? 489 PRO A CA  1 
ATOM   3493 C C   . PRO A 1 489 ? 23.23600  -0.37900  57.15100 1.000 16.65000 ? 489 PRO A C   1 
ATOM   3494 O O   . PRO A 1 489 ? 22.35200  0.44700   56.91700 1.000 16.65000 ? 489 PRO A O   1 
ATOM   3495 C CB  . PRO A 1 489 ? 23.46600  -1.99700  55.22800 1.000 16.65000 ? 489 PRO A CB  1 
ATOM   3496 C CG  . PRO A 1 489 ? 22.15200  -1.92200  54.51800 1.000 16.65000 ? 489 PRO A CG  1 
ATOM   3497 C CD  . PRO A 1 489 ? 21.15900  -2.57300  55.43600 1.000 16.65000 ? 489 PRO A CD  1 
ATOM   3498 N N   . TRP A 1 490 ? 24.35300  -0.08000  57.81000 1.000 17.75000 ? 490 TRP A N   1 
ATOM   3499 C CA  . TRP A 1 490 ? 24.64200  1.29000   58.20600 1.000 17.75000 ? 490 TRP A CA  1 
ATOM   3500 C C   . TRP A 1 490 ? 24.93600  2.15000   56.98200 1.000 17.75000 ? 490 TRP A C   1 
ATOM   3501 O O   . TRP A 1 490 ? 25.64900  1.73000   56.06500 1.000 17.75000 ? 490 TRP A O   1 
ATOM   3502 C CB  . TRP A 1 490 ? 25.83100  1.32700   59.16500 1.000 17.75000 ? 490 TRP A CB  1 
ATOM   3503 C CG  . TRP A 1 490 ? 25.69100  0.40100   60.33100 1.000 17.75000 ? 490 TRP A CG  1 
ATOM   3504 C CD1 . TRP A 1 490 ? 26.26100  -0.82900  60.47400 1.000 17.75000 ? 490 TRP A CD1 1 
ATOM   3505 C CD2 . TRP A 1 490 ? 24.92600  0.62900   61.52000 1.000 17.75000 ? 490 TRP A CD2 1 
ATOM   3506 N NE1 . TRP A 1 490 ? 25.90100  -1.38100  61.67900 1.000 17.75000 ? 490 TRP A NE1 1 
ATOM   3507 C CE2 . TRP A 1 490 ? 25.08100  -0.50500  62.34000 1.000 17.75000 ? 490 TRP A CE2 1 
ATOM   3508 C CE3 . TRP A 1 490 ? 24.12600  1.68300   61.97100 1.000 17.75000 ? 490 TRP A CE3 1 
ATOM   3509 C CZ2 . TRP A 1 490 ? 24.46600  -0.61600  63.58400 1.000 17.75000 ? 490 TRP A CZ2 1 
ATOM   3510 C CZ3 . TRP A 1 490 ? 23.51700  1.57200   63.20400 1.000 17.75000 ? 490 TRP A CZ3 1 
ATOM   3511 C CH2 . TRP A 1 490 ? 23.68900  0.43100   63.99600 1.000 17.75000 ? 490 TRP A CH2 1 
ATOM   3512 N N   . LYS A 1 491 ? 24.38800  3.36300   56.97000 1.000 21.62000 ? 491 LYS A N   1 
ATOM   3513 C CA  . LYS A 1 491 ? 24.80700  4.35000   55.98400 1.000 21.62000 ? 491 LYS A CA  1 
ATOM   3514 C C   . LYS A 1 491 ? 26.17700  4.90700   56.35800 1.000 21.62000 ? 491 LYS A C   1 
ATOM   3515 O O   . LYS A 1 491 ? 26.54600  4.97100   57.53400 1.000 21.62000 ? 491 LYS A O   1 
ATOM   3516 C CB  . LYS A 1 491 ? 23.78900  5.48500   55.87700 1.000 21.62000 ? 491 LYS A CB  1 
ATOM   3517 C CG  . LYS A 1 491 ? 22.79400  5.32800   54.73500 1.000 21.62000 ? 491 LYS A CG  1 
ATOM   3518 C CD  . LYS A 1 491 ? 21.58900  4.49400   55.13300 1.000 21.62000 ? 491 LYS A CD  1 
ATOM   3519 C CE  . LYS A 1 491 ? 20.53700  4.50900   54.03100 1.000 21.62000 ? 491 LYS A CE  1 
ATOM   3520 N NZ  . LYS A 1 491 ? 19.27900  3.81700   54.42900 1.000 21.62000 ? 491 LYS A NZ  1 
ATOM   3521 N N   . SER A 1 492 ? 26.94200  5.30300   55.33700 1.000 23.16000 ? 492 SER A N   1 
ATOM   3522 C CA  . SER A 1 492 ? 28.28900  5.80500   55.59200 1.000 23.16000 ? 492 SER A CA  1 
ATOM   3523 C C   . SER A 1 492 ? 28.25900  7.08200   56.42200 1.000 23.16000 ? 492 SER A C   1 
ATOM   3524 O O   . SER A 1 492 ? 29.09100  7.26900   57.32000 1.000 23.16000 ? 492 SER A O   1 
ATOM   3525 C CB  . SER A 1 492 ? 29.01800  6.04100   54.26900 1.000 23.16000 ? 492 SER A CB  1 
ATOM   3526 O OG  . SER A 1 492 ? 29.08300  4.84900   53.50600 1.000 23.16000 ? 492 SER A OG  1 
ATOM   3527 N N   . TYR A 1 493 ? 27.29200  7.96600   56.15600 1.000 24.01000 ? 493 TYR A N   1 
ATOM   3528 C CA  . TYR A 1 493 ? 27.20700  9.19800   56.93300 1.000 24.01000 ? 493 TYR A CA  1 
ATOM   3529 C C   . TYR A 1 493 ? 26.78800  8.92800   58.37200 1.000 24.01000 ? 493 TYR A C   1 
ATOM   3530 O O   . TYR A 1 493 ? 27.17300  9.68000   59.27400 1.000 24.01000 ? 493 TYR A O   1 
ATOM   3531 C CB  . TYR A 1 493 ? 26.25500  10.19200  56.26400 1.000 24.01000 ? 493 TYR A CB  1 
ATOM   3532 C CG  . TYR A 1 493 ? 24.89200  9.64600   55.90500 1.000 24.01000 ? 493 TYR A CG  1 
ATOM   3533 C CD1 . TYR A 1 493 ? 23.87200  9.59500   56.84600 1.000 24.01000 ? 493 TYR A CD1 1 
ATOM   3534 C CD2 . TYR A 1 493 ? 24.61700  9.21000   54.61600 1.000 24.01000 ? 493 TYR A CD2 1 
ATOM   3535 C CE1 . TYR A 1 493 ? 22.62000  9.10700   56.51900 1.000 24.01000 ? 493 TYR A CE1 1 
ATOM   3536 C CE2 . TYR A 1 493 ? 23.36800  8.72300   54.27900 1.000 24.01000 ? 493 TYR A CE2 1 
ATOM   3537 C CZ  . TYR A 1 493 ? 22.37400  8.67400   55.23500 1.000 24.01000 ? 493 TYR A CZ  1 
ATOM   3538 O OH  . TYR A 1 493 ? 21.12900  8.18800   54.90700 1.000 24.01000 ? 493 TYR A OH  1 
ATOM   3539 N N   . GLU A 1 494 ? 26.02800  7.86000   58.61500 1.000 20.45000 ? 494 GLU A N   1 
ATOM   3540 C CA  . GLU A 1 494 ? 25.68500  7.50800   59.98800 1.000 20.45000 ? 494 GLU A CA  1 
ATOM   3541 C C   . GLU A 1 494 ? 26.92600  7.10000   60.77300 1.000 20.45000 ? 494 GLU A C   1 
ATOM   3542 O O   . GLU A 1 494 ? 27.12700  7.54100   61.91100 1.000 20.45000 ? 494 GLU A O   1 
ATOM   3543 C CB  . GLU A 1 494 ? 24.64500  6.38700   60.00000 1.000 20.45000 ? 494 GLU A CB  1 
ATOM   3544 C CG  . GLU A 1 494 ? 23.29100  6.78700   59.43700 1.000 20.45000 ? 494 GLU A CG  1 
ATOM   3545 C CD  . GLU A 1 494 ? 22.36200  5.60100   59.26500 1.000 20.45000 ? 494 GLU A CD  1 
ATOM   3546 O OE1 . GLU A 1 494 ? 22.84200  4.45200   59.35600 1.000 20.45000 ? 494 GLU A OE1 1 
ATOM   3547 O OE2 . GLU A 1 494 ? 21.15200  5.81700   59.03900 1.000 20.45000 ? 494 GLU A OE2 1 
ATOM   3548 N N   . VAL A 1 495 ? 27.78000  6.26600   60.17400 1.000 22.70000 ? 495 VAL A N   1 
ATOM   3549 C CA  . VAL A 1 495 ? 29.01200  5.87600   60.85100 1.000 22.70000 ? 495 VAL A CA  1 
ATOM   3550 C C   . VAL A 1 495 ? 29.95000  7.06600   61.00000 1.000 22.70000 ? 495 VAL A C   1 
ATOM   3551 O O   . VAL A 1 495 ? 30.67500  7.17600   61.99800 1.000 22.70000 ? 495 VAL A O   1 
ATOM   3552 C CB  . VAL A 1 495 ? 29.68700  4.71700   60.09500 1.000 22.70000 ? 495 VAL A CB  1 
ATOM   3553 C CG1 . VAL A 1 495 ? 30.83500  4.14400   60.91500 1.000 22.70000 ? 495 VAL A CG1 1 
ATOM   3554 C CG2 . VAL A 1 495 ? 28.66900  3.63800   59.76500 1.000 22.70000 ? 495 VAL A CG2 1 
ATOM   3555 N N   . ASN A 1 496 ? 29.93700  7.99000   60.03400 1.000 27.02000 ? 496 ASN A N   1 
ATOM   3556 C CA  . ASN A 1 496 ? 30.76100  9.18700   60.16900 1.000 27.02000 ? 496 ASN A CA  1 
ATOM   3557 C C   . ASN A 1 496 ? 30.27800  10.06100  61.31900 1.000 27.02000 ? 496 ASN A C   1 
ATOM   3558 O O   . ASN A 1 496 ? 31.09000  10.58900  62.08800 1.000 27.02000 ? 496 ASN A O   1 
ATOM   3559 C CB  . ASN A 1 496 ? 30.76800  9.97600   58.86000 1.000 27.02000 ? 496 ASN A CB  1 
ATOM   3560 C CG  . ASN A 1 496 ? 31.63500  9.33200   57.79700 1.000 27.02000 ? 496 ASN A CG  1 
ATOM   3561 O OD1 . ASN A 1 496 ? 32.83200  9.60700   57.70800 1.000 27.02000 ? 496 ASN A OD1 1 
ATOM   3562 N ND2 . ASN A 1 496 ? 31.03600  8.47000   56.98500 1.000 27.02000 ? 496 ASN A ND2 1 
ATOM   3563 N N   . ALA A 1 497 ? 28.96000  10.21400  61.46200 1.000 23.84000 ? 497 ALA A N   1 
ATOM   3564 C CA  . ALA A 1 497 ? 28.43200  10.95300  62.60100 1.000 23.84000 ? 497 ALA A CA  1 
ATOM   3565 C C   . ALA A 1 497 ? 28.73300  10.24600  63.91300 1.000 23.84000 ? 497 ALA A C   1 
ATOM   3566 O O   . ALA A 1 497 ? 29.00100  10.90700  64.92200 1.000 23.84000 ? 497 ALA A O   1 
ATOM   3567 C CB  . ALA A 1 497 ? 26.92900  11.16100  62.43500 1.000 23.84000 ? 497 ALA A CB  1 
ATOM   3568 N N   . ALA A 1 498 ? 28.72900  8.91300   63.91400 1.000 25.51000 ? 498 ALA A N   1 
ATOM   3569 C CA  . ALA A 1 498 ? 29.07000  8.18800   65.13100 1.000 25.51000 ? 498 ALA A CA  1 
ATOM   3570 C C   . ALA A 1 498 ? 30.52900  8.40200   65.50800 1.000 25.51000 ? 498 ALA A C   1 
ATOM   3571 O O   . ALA A 1 498 ? 30.85500  8.53200   66.69300 1.000 25.51000 ? 498 ALA A O   1 
ATOM   3572 C CB  . ALA A 1 498 ? 28.77300  6.69800   64.96200 1.000 25.51000 ? 498 ALA A CB  1 
ATOM   3573 N N   . ALA A 1 499 ? 31.42000  8.45100   64.51500 1.000 26.56000 ? 499 ALA A N   1 
ATOM   3574 C CA  . ALA A 1 499 ? 32.82300  8.73300   64.80300 1.000 26.56000 ? 499 ALA A CA  1 
ATOM   3575 C C   . ALA A 1 499 ? 33.01600  10.17300  65.26700 1.000 26.56000 ? 499 ALA A C   1 
ATOM   3576 O O   . ALA A 1 499 ? 33.84500  10.44500  66.14400 1.000 26.56000 ? 499 ALA A O   1 
ATOM   3577 C CB  . ALA A 1 499 ? 33.68100  8.44500   63.57100 1.000 26.56000 ? 499 ALA A CB  1 
ATOM   3578 N N   . GLU A 1 500 ? 32.25600  11.10600  64.68900 1.000 29.66000 ? 500 GLU A N   1 
ATOM   3579 C CA  . GLU A 1 500 ? 32.31400  12.50500  65.10400 1.000 29.66000 ? 500 GLU A CA  1 
ATOM   3580 C C   . GLU A 1 500 ? 31.78100  12.69500  66.51900 1.000 29.66000 ? 500 GLU A C   1 
ATOM   3581 O O   . GLU A 1 500 ? 32.21800  13.60600  67.24100 1.000 29.66000 ? 500 GLU A O   1 
ATOM   3582 C CB  . GLU A 1 500 ? 31.52800  13.35100  64.10100 1.000 29.66000 ? 500 GLU A CB  1 
ATOM   3583 C CG  . GLU A 1 500 ? 31.23300  14.77900  64.51300 1.000 29.66000 ? 500 GLU A CG  1 
ATOM   3584 C CD  . GLU A 1 500 ? 30.42800  15.51300  63.45700 1.000 29.66000 ? 500 GLU A CD  1 
ATOM   3585 O OE1 . GLU A 1 500 ? 30.30800  14.98300  62.33200 1.000 29.66000 ? 500 GLU A OE1 1 
ATOM   3586 O OE2 . GLU A 1 500 ? 29.91200  16.61200  63.74800 1.000 29.66000 ? 500 GLU A OE2 1 
ATOM   3587 N N   . LEU A 1 501 ? 30.84900  11.83500  66.93400 1.000 29.83000 ? 501 LEU A N   1 
ATOM   3588 C CA  . LEU A 1 501 ? 30.29300  11.94500  68.27500 1.000 29.83000 ? 501 LEU A CA  1 
ATOM   3589 C C   . LEU A 1 501 ? 31.34500  11.68100  69.34200 1.000 29.83000 ? 501 LEU A C   1 
ATOM   3590 O O   . LEU A 1 501 ? 31.21400  12.17000  70.46500 1.000 29.83000 ? 501 LEU A O   1 
ATOM   3591 C CB  . LEU A 1 501 ? 29.11700  10.98300  68.44400 1.000 29.83000 ? 501 LEU A CB  1 
ATOM   3592 C CG  . LEU A 1 501 ? 28.24800  11.25800  69.67300 1.000 29.83000 ? 501 LEU A CG  1 
ATOM   3593 C CD1 . LEU A 1 501 ? 27.42200  12.52000  69.47100 1.000 29.83000 ? 501 LEU A CD1 1 
ATOM   3594 C CD2 . LEU A 1 501 ? 27.36100  10.07000  69.99800 1.000 29.83000 ? 501 LEU A CD2 1 
ATOM   3595 N N   . ARG A 1 502 ? 32.39900  10.92900  69.01600 1.000 34.21000 ? 502 ARG A N   1 
ATOM   3596 C CA  . ARG A 1 502 ? 33.46000  10.70000  69.99300 1.000 34.21000 ? 502 ARG A CA  1 
ATOM   3597 C C   . ARG A 1 502 ? 34.15100  12.00700  70.36600 1.000 34.21000 ? 502 ARG A C   1 
ATOM   3598 O O   . ARG A 1 502 ? 34.33300  12.31500  71.55100 1.000 34.21000 ? 502 ARG A O   1 
ATOM   3599 C CB  . ARG A 1 502 ? 34.47100  9.69300   69.44500 1.000 34.21000 ? 502 ARG A CB  1 
ATOM   3600 C CG  . ARG A 1 502 ? 35.60200  9.38200   70.40600 1.000 34.21000 ? 502 ARG A CG  1 
ATOM   3601 C CD  . ARG A 1 502 ? 36.72500  8.63200   69.71600 1.000 34.21000 ? 502 ARG A CD  1 
ATOM   3602 N NE  . ARG A 1 502 ? 37.94200  8.63800   70.51800 1.000 34.21000 ? 502 ARG A NE  1 
ATOM   3603 C CZ  . ARG A 1 502 ? 38.79200  9.65400   70.57800 1.000 34.21000 ? 502 ARG A CZ  1 
ATOM   3604 N NH1 . ARG A 1 502 ? 38.58400  10.77000  69.89700 1.000 34.21000 ? 502 ARG A NH1 1 
ATOM   3605 N NH2 . ARG A 1 502 ? 39.87400  9.55100   71.34400 1.000 34.21000 ? 502 ARG A NH2 1 
ATOM   3606 N N   . GLY A 1 503 ? 34.51700  12.80600  69.36300 1.000 32.90000 ? 503 GLY A N   1 
ATOM   3607 C CA  . GLY A 1 503 ? 35.10700  14.10100  69.65100 1.000 32.90000 ? 503 GLY A CA  1 
ATOM   3608 C C   . GLY A 1 503 ? 34.10500  15.06400  70.25600 1.000 32.90000 ? 503 GLY A C   1 
ATOM   3609 O O   . GLY A 1 503 ? 34.45100  15.86900  71.12700 1.000 32.90000 ? 503 GLY A O   1 
ATOM   3610 N N   . ALA A 1 504 ? 32.84300  14.98300  69.81800 1.000 33.65000 ? 504 ALA A N   1 
ATOM   3611 C CA  . ALA A 1 504 ? 31.81400  15.82800  70.41900 1.000 33.65000 ? 504 ALA A CA  1 
ATOM   3612 C C   . ALA A 1 504 ? 31.61800  15.50800  71.89600 1.000 33.65000 ? 504 ALA A C   1 
ATOM   3613 O O   . ALA A 1 504 ? 31.27500  16.39600  72.68500 1.000 33.65000 ? 504 ALA A O   1 
ATOM   3614 C CB  . ALA A 1 504 ? 30.49700  15.67200  69.66000 1.000 33.65000 ? 504 ALA A CB  1 
ATOM   3615 N N   . ILE A 1 505 ? 31.83300  14.25100  72.28500 1.000 36.20000 ? 505 ILE A N   1 
ATOM   3616 C CA  . ILE A 1 505 ? 31.71700  13.85500  73.68300 1.000 36.20000 ? 505 ILE A CA  1 
ATOM   3617 C C   . ILE A 1 505 ? 32.94800  14.28300  74.46800 1.000 36.20000 ? 505 ILE A C   1 
ATOM   3618 O O   . ILE A 1 505 ? 32.83700  14.78900  75.59100 1.000 36.20000 ? 505 ILE A O   1 
ATOM   3619 C CB  . ILE A 1 505 ? 31.48000  12.33500  73.77700 1.000 36.20000 ? 505 ILE A CB  1 
ATOM   3620 C CG1 . ILE A 1 505 ? 30.04200  11.99200  73.37800 1.000 36.20000 ? 505 ILE A CG1 1 
ATOM   3621 C CG2 . ILE A 1 505 ? 31.79500  11.81900  75.17300 1.000 36.20000 ? 505 ILE A CG2 1 
ATOM   3622 C CD1 . ILE A 1 505 ? 29.79600  10.51100  73.18600 1.000 36.20000 ? 505 ILE A CD1 1 
ATOM   3623 N N   . ILE A 1 506 ? 34.13800  14.09500  73.89200 1.000 35.78000 ? 506 ILE A N   1 
ATOM   3624 C CA  . ILE A 1 506 ? 35.35700  14.48200  74.59400 1.000 35.78000 ? 506 ILE A CA  1 
ATOM   3625 C C   . ILE A 1 506 ? 35.42000  15.99500  74.79100 1.000 35.78000 ? 506 ILE A C   1 
ATOM   3626 O O   . ILE A 1 506 ? 35.99300  16.47500  75.77700 1.000 35.78000 ? 506 ILE A O   1 
ATOM   3627 C CB  . ILE A 1 506 ? 36.59400  13.94800  73.84600 1.000 35.78000 ? 506 ILE A CB  1 
ATOM   3628 C CG1 . ILE A 1 506 ? 36.55400  12.42100  73.78500 1.000 35.78000 ? 506 ILE A CG1 1 
ATOM   3629 C CG2 . ILE A 1 506 ? 37.88000  14.39800  74.52400 1.000 35.78000 ? 506 ILE A CG2 1 
ATOM   3630 C CD1 . ILE A 1 506 ? 37.73900  11.81100  73.07700 1.000 35.78000 ? 506 ILE A CD1 1 
ATOM   3631 N N   . THR A 1 507 ? 34.81100  16.77100  73.88800 1.000 37.04000 ? 507 THR A N   1 
ATOM   3632 C CA  . THR A 1 507 ? 34.93600  18.22500  73.96500 1.000 37.04000 ? 507 THR A CA  1 
ATOM   3633 C C   . THR A 1 507 ? 34.26900  18.78200  75.21900 1.000 37.04000 ? 507 THR A C   1 
ATOM   3634 O O   . THR A 1 507 ? 34.89300  19.52200  75.98900 1.000 37.04000 ? 507 THR A O   1 
ATOM   3635 C CB  . THR A 1 507 ? 34.33700  18.87300  72.71700 1.000 37.04000 ? 507 THR A CB  1 
ATOM   3636 O OG1 . THR A 1 507 ? 35.10800  18.50900  71.56500 1.000 37.04000 ? 507 THR A OG1 1 
ATOM   3637 C CG2 . THR A 1 507 ? 34.32200  20.38800  72.85900 1.000 37.04000 ? 507 THR A CG2 1 
ATOM   3638 N N   . VAL A 1 508 ? 33.06600  18.30800  75.48800 1.000 37.58000 ? 508 VAL A N   1 
ATOM   3639 C CA  . VAL A 1 508 ? 32.44400  18.71800  76.76600 1.000 37.58000 ? 508 VAL A CA  1 
ATOM   3640 C C   . VAL A 1 508 ? 33.15400  17.88300  77.82100 1.000 37.58000 ? 508 VAL A C   1 
ATOM   3641 O O   . VAL A 1 508 ? 32.76200  16.72100  78.00600 1.000 37.58000 ? 508 VAL A O   1 
ATOM   3642 C CB  . VAL A 1 508 ? 30.93000  18.48300  76.75100 1.000 37.58000 ? 508 VAL A CB  1 
ATOM   3643 C CG1 . VAL A 1 508 ? 30.28700  18.84500  78.08000 1.000 37.58000 ? 508 VAL A CG1 1 
ATOM   3644 C CG2 . VAL A 1 508 ? 30.27000  19.23700  75.60800 1.000 37.58000 ? 508 VAL A CG2 1 
ATOM   3645 N N   . VAL A 1 509 ? 34.20200  18.44300  78.42900 1.000 42.85000 ? 509 VAL A N   1 
ATOM   3646 C CA  . VAL A 1 509 ? 34.96000  17.73200  79.49700 1.000 42.85000 ? 509 VAL A CA  1 
ATOM   3647 C C   . VAL A 1 509 ? 34.22200  17.90800  80.82600 1.000 42.85000 ? 509 VAL A C   1 
ATOM   3648 O O   . VAL A 1 509 ? 33.27600  18.71700  80.86100 1.000 42.85000 ? 509 VAL A O   1 
ATOM   3649 C CB  . VAL A 1 509 ? 36.39000  18.28300  79.57900 1.000 42.85000 ? 509 VAL A CB  1 
ATOM   3650 C CG1 . VAL A 1 509 ? 36.99071  18.48326  78.19757 1.000 42.85000 ? 509 VAL A CG1 1 
ATOM   3651 C CG2 . VAL A 1 509 ? 36.43401  19.57895  80.37250 1.000 42.85000 ? 509 VAL A CG2 1 
ATOM   3652 N N   . ASN B 1 16  ? -1.04200  42.51700  46.76300 1.000 48.49000 ? 16  ASN B N   1 
ATOM   3653 C CA  . ASN B 1 16  ? -1.20300  43.57800  45.77500 1.000 48.49000 ? 16  ASN B CA  1 
ATOM   3654 C C   . ASN B 1 16  ? -1.12800  43.00300  44.36400 1.000 48.49000 ? 16  ASN B C   1 
ATOM   3655 O O   . ASN B 1 16  ? -2.04500  42.31400  43.91600 1.000 48.49000 ? 16  ASN B O   1 
ATOM   3656 C CB  . ASN B 1 16  ? -0.13700  44.65900  45.97200 1.000 48.49000 ? 16  ASN B CB  1 
ATOM   3657 C CG  . ASN B 1 16  ? -0.46000  45.94000  45.22800 1.000 48.49000 ? 16  ASN B CG  1 
ATOM   3658 O OD1 . ASN B 1 16  ? -1.61500  46.20400  44.89500 1.000 48.49000 ? 16  ASN B OD1 1 
ATOM   3659 N ND2 . ASN B 1 16  ? 0.56300   46.74500  44.96600 1.000 48.49000 ? 16  ASN B ND2 1 
ATOM   3660 N N   . CYS B 1 17  ? -0.03100  43.30000  43.66200 1.000 43.96000 ? 17  CYS B N   1 
ATOM   3661 C CA  . CYS B 1 17  ? 0.18900   42.70000  42.35000 1.000 43.96000 ? 17  CYS B CA  1 
ATOM   3662 C C   . CYS B 1 17  ? 0.37800   41.19400  42.45300 1.000 43.96000 ? 17  CYS B C   1 
ATOM   3663 O O   . CYS B 1 17  ? 0.08200   40.46400  41.49900 1.000 43.96000 ? 17  CYS B O   1 
ATOM   3664 C CB  . CYS B 1 17  ? 1.39700   43.34500  41.67400 1.000 43.96000 ? 17  CYS B CB  1 
ATOM   3665 S SG  . CYS B 1 17  ? 1.07100   43.90200  39.99200 1.000 43.96000 ? 17  CYS B SG  1 
ATOM   3666 N N   . ASP B 1 18  ? 0.86200   40.71400  43.59900 1.000 41.70000 ? 18  ASP B N   1 
ATOM   3667 C CA  . ASP B 1 18  ? 1.03000   39.28900  43.85000 1.000 41.70000 ? 18  ASP B CA  1 
ATOM   3668 C C   . ASP B 1 18  ? -0.27500  38.59800  44.21400 1.000 41.70000 ? 18  ASP B C   1 
ATOM   3669 O O   . ASP B 1 18  ? -0.29200  37.36900  44.34200 1.000 41.70000 ? 18  ASP B O   1 
ATOM   3670 C CB  . ASP B 1 18  ? 2.05000   39.06800  44.97100 1.000 41.70000 ? 18  ASP B CB  1 
ATOM   3671 C CG  . ASP B 1 18  ? 3.47400   38.97800  44.45900 1.000 41.70000 ? 18  ASP B CG  1 
ATOM   3672 O OD1 . ASP B 1 18  ? 3.69900   38.28200  43.44800 1.000 41.70000 ? 18  ASP B OD1 1 
ATOM   3673 O OD2 . ASP B 1 18  ? 4.36900   39.60000  45.06900 1.000 41.70000 ? 18  ASP B OD2 1 
ATOM   3674 N N   . LYS B 1 19  ? -1.35300  39.35000  44.40000 1.000 46.07000 ? 19  LYS B N   1 
ATOM   3675 C CA  . LYS B 1 19  ? -2.64800  38.80800  44.78800 1.000 46.07000 ? 19  LYS B CA  1 
ATOM   3676 C C   . LYS B 1 19  ? -3.69400  39.06400  43.70700 1.000 46.07000 ? 19  LYS B C   1 
ATOM   3677 O O   . LYS B 1 19  ? -4.84300  39.40200  43.99500 1.000 46.07000 ? 19  LYS B O   1 
ATOM   3678 C CB  . LYS B 1 19  ? -3.09100  39.38800  46.12800 1.000 46.07000 ? 19  LYS B CB  1 
ATOM   3679 C CG  . LYS B 1 19  ? -2.17800  39.01800  47.28600 1.000 46.07000 ? 19  LYS B CG  1 
ATOM   3680 C CD  . LYS B 1 19  ? -2.66800  39.61600  48.59300 1.000 46.07000 ? 19  LYS B CD  1 
ATOM   3681 C CE  . LYS B 1 19  ? -1.80900  39.16200  49.75900 1.000 46.07000 ? 19  LYS B CE  1 
ATOM   3682 N NZ  . LYS B 1 19  ? -1.82300  37.68100  49.90300 1.000 46.07000 ? 19  LYS B NZ  1 
ATOM   3683 N N   . GLU B 1 20  ? -3.29700  38.92000  42.44100 1.000 49.06000 ? 20  GLU B N   1 
ATOM   3684 C CA  . GLU B 1 20  ? -4.19400  39.11900  41.30600 1.000 49.06000 ? 20  GLU B CA  1 
ATOM   3685 C C   . GLU B 1 20  ? -4.51900  37.79000  40.64400 1.000 49.06000 ? 20  GLU B C   1 
ATOM   3686 O O   . GLU B 1 20  ? -3.59800  37.08100  40.21100 1.000 49.06000 ? 20  GLU B O   1 
ATOM   3687 C CB  . GLU B 1 20  ? -3.58600  40.07800  40.28800 1.000 49.06000 ? 20  GLU B CB  1 
ATOM   3688 C CG  . GLU B 1 20  ? -4.50600  40.36200  39.10700 1.000 49.06000 ? 20  GLU B CG  1 
ATOM   3689 C CD  . GLU B 1 20  ? -3.96700  41.43700  38.18700 1.000 49.06000 ? 20  GLU B CD  1 
ATOM   3690 O OE1 . GLU B 1 20  ? -2.94000  42.05800  38.53200 1.000 49.06000 ? 20  GLU B OE1 1 
ATOM   3691 O OE2 . GLU B 1 20  ? -4.57300  41.66100  37.11700 1.000 49.06000 ? 20  GLU B OE2 1 
ATOM   3692 N N   . PRO B 1 21  ? -5.79400  37.40900  40.54300 1.000 48.07000 ? 21  PRO B N   1 
ATOM   3693 C CA  . PRO B 1 21  ? -6.18100  36.17400  39.82600 1.000 48.07000 ? 21  PRO B CA  1 
ATOM   3694 C C   . PRO B 1 21  ? -6.19500  36.36000  38.31000 1.000 48.07000 ? 21  PRO B C   1 
ATOM   3695 O O   . PRO B 1 21  ? -7.22900  36.50900  37.65900 1.000 48.07000 ? 21  PRO B O   1 
ATOM   3696 C CB  . PRO B 1 21  ? -7.57700  35.89100  40.38300 1.000 48.07000 ? 21  PRO B CB  1 
ATOM   3697 C CG  . PRO B 1 21  ? -8.12800  37.24800  40.66400 1.000 48.07000 ? 21  PRO B CG  1 
ATOM   3698 C CD  . PRO B 1 21  ? -6.96400  38.10900  41.10000 1.000 48.07000 ? 21  PRO B CD  1 
ATOM   3699 N N   . ILE B 1 22  ? -4.99700  36.35500  37.72000 1.000 41.99000 ? 22  ILE B N   1 
ATOM   3700 C CA  . ILE B 1 22  ? -4.86900  36.56400  36.28300 1.000 41.99000 ? 22  ILE B CA  1 
ATOM   3701 C C   . ILE B 1 22  ? -5.42200  35.39400  35.48200 1.000 41.99000 ? 22  ILE B C   1 
ATOM   3702 O O   . ILE B 1 22  ? -5.70300  35.54600  34.28700 1.000 41.99000 ? 22  ILE B O   1 
ATOM   3703 C CB  . ILE B 1 22  ? -3.39900  36.81600  35.90300 1.000 41.99000 ? 22  ILE B CB  1 
ATOM   3704 C CG1 . ILE B 1 22  ? -2.54000  35.61200  36.28900 1.000 41.99000 ? 22  ILE B CG1 1 
ATOM   3705 C CG2 . ILE B 1 22  ? -2.88600  38.08100  36.57100 1.000 41.99000 ? 22  ILE B CG2 1 
ATOM   3706 C CD1 . ILE B 1 22  ? -1.13100  35.68700  35.76300 1.000 41.99000 ? 22  ILE B CD1 1 
ATOM   3707 N N   . HIS B 1 23  ? -5.58000  34.22700  36.10300 1.000 41.29000 ? 23  HIS B N   1 
ATOM   3708 C CA  . HIS B 1 23  ? -5.99600  33.03000  35.38400 1.000 41.29000 ? 23  HIS B CA  1 
ATOM   3709 C C   . HIS B 1 23  ? -7.48300  33.00600  35.05600 1.000 41.29000 ? 23  HIS B C   1 
ATOM   3710 O O   . HIS B 1 23  ? -7.91000  32.14800  34.27600 1.000 41.29000 ? 23  HIS B O   1 
ATOM   3711 C CB  . HIS B 1 23  ? -5.62800  31.77600  36.18100 1.000 41.29000 ? 23  HIS B CB  1 
ATOM   3712 C CG  . HIS B 1 23  ? -6.38000  31.62700  37.46700 1.000 41.29000 ? 23  HIS B CG  1 
ATOM   3713 N ND1 . HIS B 1 23  ? -6.86500  32.70200  38.17900 1.000 41.29000 ? 23  HIS B ND1 1 
ATOM   3714 C CD2 . HIS B 1 23  ? -6.72800  30.52300  38.16900 1.000 41.29000 ? 23  HIS B CD2 1 
ATOM   3715 C CE1 . HIS B 1 23  ? -7.47800  32.26800  39.26600 1.000 41.29000 ? 23  HIS B CE1 1 
ATOM   3716 N NE2 . HIS B 1 23  ? -7.41000  30.94900  39.28300 1.000 41.29000 ? 23  HIS B NE2 1 
ATOM   3717 N N   . ILE B 1 24  ? -8.28000  33.90800  35.61900 1.000 42.07000 ? 24  ILE B N   1 
ATOM   3718 C CA  . ILE B 1 24  ? -9.69700  33.96800  35.27400 1.000 42.07000 ? 24  ILE B CA  1 
ATOM   3719 C C   . ILE B 1 24  ? -10.08100 35.40800  34.94700 1.000 42.07000 ? 24  ILE B C   1 
ATOM   3720 O O   . ILE B 1 24  ? -10.86300 36.02400  35.68600 1.000 42.07000 ? 24  ILE B O   1 
ATOM   3721 C CB  . ILE B 1 24  ? -10.55700 33.40100  36.41500 1.000 42.07000 ? 24  ILE B CB  1 
ATOM   3722 C CG1 . ILE B 1 24  ? -10.09300 33.96600  37.76200 1.000 42.07000 ? 24  ILE B CG1 1 
ATOM   3723 C CG2 . ILE B 1 24  ? -10.46900 31.88600  36.44800 1.000 42.07000 ? 24  ILE B CG2 1 
ATOM   3724 C CD1 . ILE B 1 24  ? -10.83900 33.40900  38.95800 1.000 42.07000 ? 24  ILE B CD1 1 
ATOM   3725 N N   . PRO B 1 25  ? -9.56900  35.98400  33.85500 1.000 42.94000 ? 25  PRO B N   1 
ATOM   3726 C CA  . PRO B 1 25  ? -10.03200 37.32200  33.45100 1.000 42.94000 ? 25  PRO B CA  1 
ATOM   3727 C C   . PRO B 1 25  ? -11.51400 37.38800  33.13500 1.000 42.94000 ? 25  PRO B C   1 
ATOM   3728 O O   . PRO B 1 25  ? -12.14000 38.43300  33.34300 1.000 42.94000 ? 25  PRO B O   1 
ATOM   3729 C CB  . PRO B 1 25  ? -9.17500  37.63300  32.22000 1.000 42.94000 ? 25  PRO B CB  1 
ATOM   3730 C CG  . PRO B 1 25  ? -8.83100  36.30100  31.66100 1.000 42.94000 ? 25  PRO B CG  1 
ATOM   3731 C CD  . PRO B 1 25  ? -8.66800  35.39100  32.84900 1.000 42.94000 ? 25  PRO B CD  1 
ATOM   3732 N N   . GLY B 1 26  ? -12.09400 36.30000  32.63100 1.000 42.93000 ? 26  GLY B N   1 
ATOM   3733 C CA  . GLY B 1 26  ? -13.40900 36.34600  32.03700 1.000 42.93000 ? 26  GLY B CA  1 
ATOM   3734 C C   . GLY B 1 26  ? -13.41900 36.78700  30.59100 1.000 42.93000 ? 26  GLY B C   1 
ATOM   3735 O O   . GLY B 1 26  ? -14.49300 36.82600  29.97500 1.000 42.93000 ? 26  GLY B O   1 
ATOM   3736 N N   . PHE B 1 27  ? -12.25600 37.10200  30.02500 1.000 43.26000 ? 27  PHE B N   1 
ATOM   3737 C CA  . PHE B 1 27  ? -12.11600 37.56300  28.65400 1.000 43.26000 ? 27  PHE B CA  1 
ATOM   3738 C C   . PHE B 1 27  ? -11.07000 36.70300  27.95900 1.000 43.26000 ? 27  PHE B C   1 
ATOM   3739 O O   . PHE B 1 27  ? -10.30800 35.97500  28.60000 1.000 43.26000 ? 27  PHE B O   1 
ATOM   3740 C CB  . PHE B 1 27  ? -11.70100 39.04400  28.58800 1.000 43.26000 ? 27  PHE B CB  1 
ATOM   3741 C CG  . PHE B 1 27  ? -12.79400 40.01700  28.95800 1.000 43.26000 ? 27  PHE B CG  1 
ATOM   3742 C CD1 . PHE B 1 27  ? -13.34400 40.02200  30.23000 1.000 43.26000 ? 27  PHE B CD1 1 
ATOM   3743 C CD2 . PHE B 1 27  ? -13.24000 40.95500  28.04000 1.000 43.26000 ? 27  PHE B CD2 1 
ATOM   3744 C CE1 . PHE B 1 27  ? -14.33900 40.92200  30.57000 1.000 43.26000 ? 27  PHE B CE1 1 
ATOM   3745 C CE2 . PHE B 1 27  ? -14.23000 41.86100  28.37500 1.000 43.26000 ? 27  PHE B CE2 1 
ATOM   3746 C CZ  . PHE B 1 27  ? -14.78100 41.84300  29.64100 1.000 43.26000 ? 27  PHE B CZ  1 
ATOM   3747 N N   . VAL B 1 28  ? -11.03200 36.78900  26.62700 1.000 41.26000 ? 28  VAL B N   1 
ATOM   3748 C CA  . VAL B 1 28  ? -10.04300 36.07700  25.82600 1.000 41.26000 ? 28  VAL B CA  1 
ATOM   3749 C C   . VAL B 1 28  ? -9.57200  36.98600  24.70000 1.000 41.26000 ? 28  VAL B C   1 
ATOM   3750 O O   . VAL B 1 28  ? -10.21200 37.98500  24.36500 1.000 41.26000 ? 28  VAL B O   1 
ATOM   3751 C CB  . VAL B 1 28  ? -10.57900 34.75300  25.23300 1.000 41.26000 ? 28  VAL B CB  1 
ATOM   3752 C CG1 . VAL B 1 28  ? -11.00300 33.79400  26.33200 1.000 41.26000 ? 28  VAL B CG1 1 
ATOM   3753 C CG2 . VAL B 1 28  ? -11.72200 35.02400  24.26800 1.000 41.26000 ? 28  VAL B CG2 1 
ATOM   3754 N N   . GLN B 1 29  ? -8.42400  36.63200  24.12800 1.000 37.68000 ? 29  GLN B N   1 
ATOM   3755 C CA  . GLN B 1 29  ? -7.89600  37.39800  23.01400 1.000 37.68000 ? 29  GLN B CA  1 
ATOM   3756 C C   . GLN B 1 29  ? -8.77800  37.20700  21.78300 1.000 37.68000 ? 29  GLN B C   1 
ATOM   3757 O O   . GLN B 1 29  ? -9.17500  36.07800  21.47200 1.000 37.68000 ? 29  GLN B O   1 
ATOM   3758 C CB  . GLN B 1 29  ? -6.45400  36.98700  22.70400 1.000 37.68000 ? 29  GLN B CB  1 
ATOM   3759 C CG  . GLN B 1 29  ? -5.53300  37.06300  23.91200 1.000 37.68000 ? 29  GLN B CG  1 
ATOM   3760 C CD  . GLN B 1 29  ? -4.06200  36.96800  23.54900 1.000 37.68000 ? 29  GLN B CD  1 
ATOM   3761 O OE1 . GLN B 1 29  ? -3.61400  37.54600  22.56000 1.000 37.68000 ? 29  GLN B OE1 1 
ATOM   3762 N NE2 . GLN B 1 29  ? -3.30200  36.23900  24.35700 1.000 37.68000 ? 29  GLN B NE2 1 
ATOM   3763 N N   . PRO B 1 30  ? -9.09800  38.29000  21.07300 1.000 42.73000 ? 30  PRO B N   1 
ATOM   3764 C CA  . PRO B 1 30  ? -10.07700 38.20400  19.97600 1.000 42.73000 ? 30  PRO B CA  1 
ATOM   3765 C C   . PRO B 1 30  ? -9.70300  37.23300  18.87200 1.000 42.73000 ? 30  PRO B C   1 
ATOM   3766 O O   . PRO B 1 30  ? -10.60300 36.64500  18.25700 1.000 42.73000 ? 30  PRO B O   1 
ATOM   3767 C CB  . PRO B 1 30  ? -10.13200 39.64700  19.45600 1.000 42.73000 ? 30  PRO B CB  1 
ATOM   3768 C CG  . PRO B 1 30  ? -8.78800  40.20600  19.79600 1.000 42.73000 ? 30  PRO B CG  1 
ATOM   3769 C CD  . PRO B 1 30  ? -8.41100  39.58900  21.10500 1.000 42.73000 ? 30  PRO B CD  1 
ATOM   3770 N N   . HIS B 1 31  ? -8.41300  37.04100  18.59700 1.000 38.91000 ? 31  HIS B N   1 
ATOM   3771 C CA  . HIS B 1 31  ? -8.01800  36.32200  17.39000 1.000 38.91000 ? 31  HIS B CA  1 
ATOM   3772 C C   . HIS B 1 31  ? -8.45200  34.86100  17.40900 1.000 38.91000 ? 31  HIS B C   1 
ATOM   3773 O O   . HIS B 1 31  ? -8.47600  34.22400  16.35100 1.000 38.91000 ? 31  HIS B O   1 
ATOM   3774 C CB  . HIS B 1 31  ? -6.50600  36.43700  17.16600 1.000 38.91000 ? 31  HIS B CB  1 
ATOM   3775 C CG  . HIS B 1 31  ? -5.68200  35.56400  18.05900 1.000 38.91000 ? 31  HIS B CG  1 
ATOM   3776 N ND1 . HIS B 1 31  ? -5.58700  35.76600  19.41900 1.000 38.91000 ? 31  HIS B ND1 1 
ATOM   3777 C CD2 . HIS B 1 31  ? -4.89500  34.49800  17.78100 1.000 38.91000 ? 31  HIS B CD2 1 
ATOM   3778 C CE1 . HIS B 1 31  ? -4.78700  34.85400  19.94200 1.000 38.91000 ? 31  HIS B CE1 1 
ATOM   3779 N NE2 . HIS B 1 31  ? -4.35400  34.07200  18.96900 1.000 38.91000 ? 31  HIS B NE2 1 
ATOM   3780 N N   . GLY B 1 32  ? -8.78800  34.31200  18.58000 1.000 42.10000 ? 32  GLY B N   1 
ATOM   3781 C CA  . GLY B 1 32  ? -9.36100  32.98900  18.67900 1.000 42.10000 ? 32  GLY B CA  1 
ATOM   3782 C C   . GLY B 1 32  ? -10.77700 33.02200  19.23900 1.000 42.10000 ? 32  GLY B C   1 
ATOM   3783 O O   . GLY B 1 32  ? -11.28000 34.06300  19.67700 1.000 42.10000 ? 32  GLY B O   1 
ATOM   3784 N N   . VAL B 1 33  ? -11.41600 31.85400  19.21500 1.000 44.58000 ? 33  VAL B N   1 
ATOM   3785 C CA  . VAL B 1 33  ? -12.75100 31.65300  19.76700 1.000 44.58000 ? 33  VAL B CA  1 
ATOM   3786 C C   . VAL B 1 33  ? -12.66900 30.56700  20.82700 1.000 44.58000 ? 33  VAL B C   1 
ATOM   3787 O O   . VAL B 1 33  ? -12.19900 29.45900  20.55000 1.000 44.58000 ? 33  VAL B O   1 
ATOM   3788 C CB  . VAL B 1 33  ? -13.77100 31.26700  18.68100 1.000 44.58000 ? 33  VAL B CB  1 
ATOM   3789 C CG1 . VAL B 1 33  ? -14.95700 30.54200  19.30100 1.000 44.58000 ? 33  VAL B CG1 1 
ATOM   3790 C CG2 . VAL B 1 33  ? -14.24600 32.49700  17.94700 1.000 44.58000 ? 33  VAL B CG2 1 
ATOM   3791 N N   . LEU B 1 34  ? -13.12200 30.87900  22.03500 1.000 46.34000 ? 34  LEU B N   1 
ATOM   3792 C CA  . LEU B 1 34  ? -13.15500 29.90200  23.11200 1.000 46.34000 ? 34  LEU B CA  1 
ATOM   3793 C C   . LEU B 1 34  ? -14.55600 29.32200  23.25100 1.000 46.34000 ? 34  LEU B C   1 
ATOM   3794 O O   . LEU B 1 34  ? -15.55400 30.03600  23.11100 1.000 46.34000 ? 34  LEU B O   1 
ATOM   3795 C CB  . LEU B 1 34  ? -12.70500 30.52900  24.43300 1.000 46.34000 ? 34  LEU B CB  1 
ATOM   3796 C CG  . LEU B 1 34  ? -12.19800 29.53800  25.48200 1.000 46.34000 ? 34  LEU B CG  1 
ATOM   3797 C CD1 . LEU B 1 34  ? -11.02700 30.12700  26.24500 1.000 46.34000 ? 34  LEU B CD1 1 
ATOM   3798 C CD2 . LEU B 1 34  ? -13.30900 29.13000  26.43800 1.000 46.34000 ? 34  LEU B CD2 1 
ATOM   3799 N N   . LEU B 1 35  ? -14.62200 28.01900  23.53000 1.000 50.44000 ? 35  LEU B N   1 
ATOM   3800 C CA  . LEU B 1 35  ? -15.88900 27.31900  23.73900 1.000 50.44000 ? 35  LEU B CA  1 
ATOM   3801 C C   . LEU B 1 35  ? -15.72300 26.39300  24.93800 1.000 50.44000 ? 35  LEU B C   1 
ATOM   3802 O O   . LEU B 1 35  ? -15.05500 25.36100  24.83600 1.000 50.44000 ? 35  LEU B O   1 
ATOM   3803 C CB  . LEU B 1 35  ? -16.29500 26.52400  22.49600 1.000 50.44000 ? 35  LEU B CB  1 
ATOM   3804 C CG  . LEU B 1 35  ? -16.32100 27.26200  21.15900 1.000 50.44000 ? 35  LEU B CG  1 
ATOM   3805 C CD1 . LEU B 1 35  ? -16.44600 26.28100  20.00100 1.000 50.44000 ? 35  LEU B CD1 1 
ATOM   3806 C CD2 . LEU B 1 35  ? -17.45400 28.27300  21.13200 1.000 50.44000 ? 35  LEU B CD2 1 
ATOM   3807 N N   . ALA B 1 36  ? -16.31100 26.77000  26.06900 1.000 53.44000 ? 36  ALA B N   1 
ATOM   3808 C CA  . ALA B 1 36  ? -16.30200 25.94100  27.27000 1.000 53.44000 ? 36  ALA B CA  1 
ATOM   3809 C C   . ALA B 1 36  ? -17.54500 25.06100  27.24800 1.000 53.44000 ? 36  ALA B C   1 
ATOM   3810 O O   . ALA B 1 36  ? -18.66200 25.55300  27.45300 1.000 53.44000 ? 36  ALA B O   1 
ATOM   3811 C CB  . ALA B 1 36  ? -16.26200 26.80700  28.52600 1.000 53.44000 ? 36  ALA B CB  1 
ATOM   3812 N N   . ILE B 1 37  ? -17.35800 23.76600  26.99100 1.000 56.35000 ? 37  ILE B N   1 
ATOM   3813 C CA  . ILE B 1 37  ? -18.46500 22.83400  26.82100 1.000 56.35000 ? 37  ILE B CA  1 
ATOM   3814 C C   . ILE B 1 37  ? -18.45200 21.82600  27.96200 1.000 56.35000 ? 37  ILE B C   1 
ATOM   3815 O O   . ILE B 1 37  ? -17.38800 21.39200  28.41400 1.000 56.35000 ? 37  ILE B O   1 
ATOM   3816 C CB  . ILE B 1 37  ? -18.41200 22.12500  25.45300 1.000 56.35000 ? 37  ILE B CB  1 
ATOM   3817 C CG1 . ILE B 1 37  ? -17.19200 21.21100  25.34400 1.000 56.35000 ? 37  ILE B CG1 1 
ATOM   3818 C CG2 . ILE B 1 37  ? -18.38900 23.14400  24.32700 1.000 56.35000 ? 37  ILE B CG2 1 
ATOM   3819 C CD1 . ILE B 1 37  ? -17.12300 20.46100  24.03300 1.000 56.35000 ? 37  ILE B CD1 1 
ATOM   3820 N N   . LYS B 1 38  ? -19.63900 21.46000  28.43200 1.000 62.73000 ? 38  LYS B N   1 
ATOM   3821 C CA  . LYS B 1 38  ? -19.75600 20.52100  29.54000 1.000 62.73000 ? 38  LYS B CA  1 
ATOM   3822 C C   . LYS B 1 38  ? -19.73500 19.09100  29.01200 1.000 62.73000 ? 38  LYS B C   1 
ATOM   3823 O O   . LYS B 1 38  ? -20.52600 18.73400  28.13200 1.000 62.73000 ? 38  LYS B O   1 
ATOM   3824 C CB  . LYS B 1 38  ? -21.03600 20.79800  30.32500 1.000 62.73000 ? 38  LYS B CB  1 
ATOM   3825 C CG  . LYS B 1 38  ? -21.57200 19.61000  31.09600 1.000 62.73000 ? 38  LYS B CG  1 
ATOM   3826 C CD  . LYS B 1 38  ? -22.99700 19.87800  31.55200 1.000 62.73000 ? 38  LYS B CD  1 
ATOM   3827 C CE  . LYS B 1 38  ? -23.84700 20.41800  30.40900 1.000 62.73000 ? 38  LYS B CE  1 
ATOM   3828 N NZ  . LYS B 1 38  ? -25.23400 20.76700  30.82500 1.000 62.73000 ? 38  LYS B NZ  1 
ATOM   3829 N N   . GLU B 1 39  ? -18.81600 18.27800  29.53900 1.000 60.86000 ? 39  GLU B N   1 
ATOM   3830 C CA  . GLU B 1 39  ? -18.71500 16.87200  29.18100 1.000 60.86000 ? 39  GLU B CA  1 
ATOM   3831 C C   . GLU B 1 39  ? -19.80500 16.06100  29.88000 1.000 60.86000 ? 39  GLU B C   1 
ATOM   3832 O O   . GLU B 1 39  ? -20.22100 16.39700  30.99200 1.000 60.86000 ? 39  GLU B O   1 
ATOM   3833 C CB  . GLU B 1 39  ? -17.34100 16.32700  29.56100 1.000 60.86000 ? 39  GLU B CB  1 
ATOM   3834 C CG  . GLU B 1 39  ? -16.65100 15.53900  28.45700 1.000 60.86000 ? 39  GLU B CG  1 
ATOM   3835 C CD  . GLU B 1 39  ? -15.23400 15.15700  28.82400 1.000 60.86000 ? 39  GLU B CD  1 
ATOM   3836 O OE1 . GLU B 1 39  ? -14.71900 15.68800  29.83100 1.000 60.86000 ? 39  GLU B OE1 1 
ATOM   3837 O OE2 . GLU B 1 39  ? -14.63400 14.32800  28.10800 1.000 60.86000 ? 39  GLU B OE2 1 
ATOM   3838 N N   . PRO B 1 40  ? -20.28700 14.97700  29.25000 1.000 63.17000 ? 40  PRO B N   1 
ATOM   3839 C CA  . PRO B 1 40  ? -19.98000 14.50700  27.89300 1.000 63.17000 ? 40  PRO B CA  1 
ATOM   3840 C C   . PRO B 1 40  ? -21.07800 14.82500  26.88100 1.000 63.17000 ? 40  PRO B C   1 
ATOM   3841 O O   . PRO B 1 40  ? -21.13300 14.21900  25.81500 1.000 63.17000 ? 40  PRO B O   1 
ATOM   3842 C CB  . PRO B 1 40  ? -19.82600 12.99900  28.10200 1.000 63.17000 ? 40  PRO B CB  1 
ATOM   3843 C CG  . PRO B 1 40  ? -20.88200 12.69200  29.13500 1.000 63.17000 ? 40  PRO B CG  1 
ATOM   3844 C CD  . PRO B 1 40  ? -20.96200 13.92200  30.02900 1.000 63.17000 ? 40  PRO B CD  1 
ATOM   3845 N N   . GLU B 1 41  ? -21.96700 15.76900  27.18100 1.000 62.67000 ? 41  GLU B N   1 
ATOM   3846 C CA  . GLU B 1 41  ? -23.06700 16.09600  26.28100 1.000 62.67000 ? 41  GLU B CA  1 
ATOM   3847 C C   . GLU B 1 41  ? -22.66400 17.05500  25.16900 1.000 62.67000 ? 41  GLU B C   1 
ATOM   3848 O O   . GLU B 1 41  ? -23.49300 17.34400  24.29900 1.000 62.67000 ? 41  GLU B O   1 
ATOM   3849 C CB  . GLU B 1 41  ? -24.23900 16.69000  27.06900 1.000 62.67000 ? 41  GLU B CB  1 
ATOM   3850 C CG  . GLU B 1 41  ? -24.73200 15.82000  28.21400 1.000 62.67000 ? 41  GLU B CG  1 
ATOM   3851 C CD  . GLU B 1 41  ? -23.99900 16.09200  29.51200 1.000 62.67000 ? 41  GLU B CD  1 
ATOM   3852 O OE1 . GLU B 1 41  ? -23.51500 17.22900  29.69400 1.000 62.67000 ? 41  GLU B OE1 1 
ATOM   3853 O OE2 . GLU B 1 41  ? -23.90300 15.17000  30.34800 1.000 62.67000 ? 41  GLU B OE2 1 
ATOM   3854 N N   . LEU B 1 42  ? -21.42600 17.55600  25.18400 1.000 61.86000 ? 42  LEU B N   1 
ATOM   3855 C CA  . LEU B 1 42  ? -20.95700 18.56600  24.23300 1.000 61.86000 ? 42  LEU B CA  1 
ATOM   3856 C C   . LEU B 1 42  ? -21.82200 19.82200  24.27600 1.000 61.86000 ? 42  LEU B C   1 
ATOM   3857 O O   . LEU B 1 42  ? -22.00500 20.50000  23.26300 1.000 61.86000 ? 42  LEU B O   1 
ATOM   3858 C CB  . LEU B 1 42  ? -20.89500 18.01100  22.80600 1.000 61.86000 ? 42  LEU B CB  1 
ATOM   3859 C CG  . LEU B 1 42  ? -20.05300 16.75200  22.59100 1.000 61.86000 ? 42  LEU B CG  1 
ATOM   3860 C CD1 . LEU B 1 42  ? -19.98300 16.40300  21.11100 1.000 61.86000 ? 42  LEU B CD1 1 
ATOM   3861 C CD2 . LEU B 1 42  ? -18.66100 16.92900  23.17400 1.000 61.86000 ? 42  LEU B CD2 1 
ATOM   3862 N N   . THR B 1 43  ? -22.35300 20.14000  25.45400 1.000 63.20000 ? 43  THR B N   1 
ATOM   3863 C CA  . THR B 1 43  ? -23.20300 21.31000  25.63200 1.000 63.20000 ? 43  THR B CA  1 
ATOM   3864 C C   . THR B 1 43  ? -22.33100 22.54400  25.83500 1.000 63.20000 ? 43  THR B C   1 
ATOM   3865 O O   . THR B 1 43  ? -21.54700 22.60300  26.78700 1.000 63.20000 ? 43  THR B O   1 
ATOM   3866 C CB  . THR B 1 43  ? -24.13100 21.10000  26.82600 1.000 63.20000 ? 43  THR B CB  1 
ATOM   3867 O OG1 . THR B 1 43  ? -24.84400 19.86700  26.66800 1.000 63.20000 ? 43  THR B OG1 1 
ATOM   3868 C CG2 . THR B 1 43  ? -25.12400 22.23400  26.93800 1.000 63.20000 ? 43  THR B CG2 1 
ATOM   3869 N N   . ILE B 1 44  ? -22.48900 23.54300  24.96500 1.000 59.57000 ? 44  ILE B N   1 
ATOM   3870 C CA  . ILE B 1 44  ? -21.61300 24.71100  24.98100 1.000 59.57000 ? 44  ILE B CA  1 
ATOM   3871 C C   . ILE B 1 44  ? -22.05100 25.66500  26.08400 1.000 59.57000 ? 44  ILE B C   1 
ATOM   3872 O O   . ILE B 1 44  ? -22.83300 26.59300  25.84500 1.000 59.57000 ? 44  ILE B O   1 
ATOM   3873 C CB  . ILE B 1 44  ? -21.59800 25.42800  23.62000 1.000 59.57000 ? 44  ILE B CB  1 
ATOM   3874 C CG1 . ILE B 1 44  ? -21.56000 24.42000  22.47400 1.000 59.57000 ? 44  ILE B CG1 1 
ATOM   3875 C CG2 . ILE B 1 44  ? -20.38700 26.32500  23.52200 1.000 59.57000 ? 44  ILE B CG2 1 
ATOM   3876 C CD1 . ILE B 1 44  ? -21.70500 25.06200  21.11400 1.000 59.57000 ? 44  ILE B CD1 1 
ATOM   3877 N N   . LEU B 1 45  ? -21.54900 25.43900  27.30000 1.000 59.30000 ? 45  LEU B N   1 
ATOM   3878 C CA  . LEU B 1 45  ? -21.94400 26.27000  28.43300 1.000 59.30000 ? 45  LEU B CA  1 
ATOM   3879 C C   . LEU B 1 45  ? -21.48200 27.71400  28.28400 1.000 59.30000 ? 45  LEU B C   1 
ATOM   3880 O O   . LEU B 1 45  ? -22.15900 28.62800  28.77100 1.000 59.30000 ? 45  LEU B O   1 
ATOM   3881 C CB  . LEU B 1 45  ? -21.40200 25.67900  29.73300 1.000 59.30000 ? 45  LEU B CB  1 
ATOM   3882 C CG  . LEU B 1 45  ? -22.01100 24.35700  30.19900 1.000 59.30000 ? 45  LEU B CG  1 
ATOM   3883 C CD1 . LEU B 1 45  ? -21.65800 24.09900  31.65400 1.000 59.30000 ? 45  LEU B CD1 1 
ATOM   3884 C CD2 . LEU B 1 45  ? -23.51700 24.35900  30.00200 1.000 59.30000 ? 45  LEU B CD2 1 
ATOM   3885 N N   . GLN B 1 46  ? -20.35100 27.94800  27.61800 1.000 54.54000 ? 46  GLN B N   1 
ATOM   3886 C CA  . GLN B 1 46  ? -19.79600 29.29400  27.53500 1.000 54.54000 ? 46  GLN B CA  1 
ATOM   3887 C C   . GLN B 1 46  ? -19.12100 29.49700  26.18700 1.000 54.54000 ? 46  GLN B C   1 
ATOM   3888 O O   . GLN B 1 46  ? -18.50900 28.57700  25.64000 1.000 54.54000 ? 46  GLN B O   1 
ATOM   3889 C CB  . GLN B 1 46  ? -18.78600 29.55300  28.66300 1.000 54.54000 ? 46  GLN B CB  1 
ATOM   3890 C CG  . GLN B 1 46  ? -19.40100 29.66500  30.04900 1.000 54.54000 ? 46  GLN B CG  1 
ATOM   3891 C CD  . GLN B 1 46  ? -18.37400 29.56400  31.16100 1.000 54.54000 ? 46  GLN B CD  1 
ATOM   3892 O OE1 . GLN B 1 46  ? -17.65800 28.56900  31.27300 1.000 54.54000 ? 46  GLN B OE1 1 
ATOM   3893 N NE2 . GLN B 1 46  ? -18.29800 30.59800  31.99100 1.000 54.54000 ? 46  GLN B NE2 1 
ATOM   3894 N N   . VAL B 1 47  ? -19.21100 30.72500  25.67300 1.000 53.39000 ? 47  VAL B N   1 
ATOM   3895 C CA  . VAL B 1 47  ? -18.56600 31.10700  24.42200 1.000 53.39000 ? 47  VAL B CA  1 
ATOM   3896 C C   . VAL B 1 47  ? -17.94400 32.48400  24.59000 1.000 53.39000 ? 47  VAL B C   1 
ATOM   3897 O O   . VAL B 1 47  ? -18.43100 33.31900  25.35900 1.000 53.39000 ? 47  VAL B O   1 
ATOM   3898 C CB  . VAL B 1 47  ? -19.54200 31.12500  23.22000 1.000 53.39000 ? 47  VAL B CB  1 
ATOM   3899 C CG1 . VAL B 1 47  ? -20.18800 29.77300  23.02100 1.000 53.39000 ? 47  VAL B CG1 1 
ATOM   3900 C CG2 . VAL B 1 47  ? -20.60300 32.20500  23.40300 1.000 53.39000 ? 47  VAL B CG2 1 
ATOM   3901 N N   . SER B 1 48  ? -16.85000 32.71200  23.87100 1.000 51.73000 ? 48  SER B N   1 
ATOM   3902 C CA  . SER B 1 48  ? -16.34300 34.06500  23.70300 1.000 51.73000 ? 48  SER B CA  1 
ATOM   3903 C C   . SER B 1 48  ? -17.34800 34.88600  22.90500 1.000 51.73000 ? 48  SER B C   1 
ATOM   3904 O O   . SER B 1 48  ? -18.00400 34.37300  21.99400 1.000 51.73000 ? 48  SER B O   1 
ATOM   3905 C CB  . SER B 1 48  ? -14.98700 34.03900  23.00100 1.000 51.73000 ? 48  SER B CB  1 
ATOM   3906 O OG  . SER B 1 48  ? -15.04600 33.27600  21.80800 1.000 51.73000 ? 48  SER B OG  1 
ATOM   3907 N N   . ASN B 1 49  ? -17.47400 36.16800  23.25100 1.000 54.74000 ? 49  ASN B N   1 
ATOM   3908 C CA  . ASN B 1 49  ? -18.51100 36.99200  22.63700 1.000 54.74000 ? 49  ASN B CA  1 
ATOM   3909 C C   . ASN B 1 49  ? -18.25600 37.24800  21.15800 1.000 54.74000 ? 49  ASN B C   1 
ATOM   3910 O O   . ASN B 1 49  ? -19.18100 37.65100  20.44500 1.000 54.74000 ? 49  ASN B O   1 
ATOM   3911 C CB  . ASN B 1 49  ? -18.64600 38.32500  23.37800 1.000 54.74000 ? 49  ASN B CB  1 
ATOM   3912 C CG  . ASN B 1 49  ? -17.49300 39.26800  23.10100 1.000 54.74000 ? 49  ASN B CG  1 
ATOM   3913 O OD1 . ASN B 1 49  ? -16.48700 39.25600  23.80500 1.000 54.74000 ? 49  ASN B OD1 1 
ATOM   3914 N ND2 . ASN B 1 49  ? -17.64000 40.10000  22.07500 1.000 54.74000 ? 49  ASN B ND2 1 
ATOM   3915 N N   . ASN B 1 50  ? -17.03400 37.03100  20.68200 1.000 55.94000 ? 50  ASN B N   1 
ATOM   3916 C CA  . ASN B 1 50  ? -16.67500 37.32500  19.30100 1.000 55.94000 ? 50  ASN B CA  1 
ATOM   3917 C C   . ASN B 1 50  ? -17.10000 36.23100  18.32500 1.000 55.94000 ? 50  ASN B C   1 
ATOM   3918 O O   . ASN B 1 50  ? -16.67100 36.26100  17.16700 1.000 55.94000 ? 50  ASN B O   1 
ATOM   3919 C CB  . ASN B 1 50  ? -15.16500 37.56100  19.19100 1.000 55.94000 ? 50  ASN B CB  1 
ATOM   3920 C CG  . ASN B 1 50  ? -14.36100 36.28400  19.34800 1.000 55.94000 ? 50  ASN B CG  1 
ATOM   3921 O OD1 . ASN B 1 50  ? -14.15300 35.79800  20.45900 1.000 55.94000 ? 50  ASN B OD1 1 
ATOM   3922 N ND2 . ASN B 1 50  ? -13.89500 35.73900  18.23000 1.000 55.94000 ? 50  ASN B ND2 1 
ATOM   3923 N N   . THR B 1 51  ? -17.92100 35.27000  18.76200 1.000 62.24000 ? 51  THR B N   1 
ATOM   3924 C CA  . THR B 1 51  ? -18.30400 34.16900  17.88300 1.000 62.24000 ? 51  THR B CA  1 
ATOM   3925 C C   . THR B 1 51  ? -19.06100 34.65200  16.65200 1.000 62.24000 ? 51  THR B C   1 
ATOM   3926 O O   . THR B 1 51  ? -18.91600 34.06900  15.57300 1.000 62.24000 ? 51  THR B O   1 
ATOM   3927 C CB  . THR B 1 51  ? -19.16100 33.15300  18.64400 1.000 62.24000 ? 51  THR B CB  1 
ATOM   3928 O OG1 . THR B 1 51  ? -20.20600 33.83300  19.35100 1.000 62.24000 ? 51  THR B OG1 1 
ATOM   3929 C CG2 . THR B 1 51  ? -18.31700 32.35200  19.62500 1.000 62.24000 ? 51  THR B CG2 1 
ATOM   3930 N N   . TYR B 1 52  ? -19.85300 35.72000  16.78200 1.000 69.30000 ? 52  TYR B N   1 
ATOM   3931 C CA  . TYR B 1 52  ? -20.71700 36.12900  15.67800 1.000 69.30000 ? 52  TYR B CA  1 
ATOM   3932 C C   . TYR B 1 52  ? -19.92700 36.60000  14.46300 1.000 69.30000 ? 52  TYR B C   1 
ATOM   3933 O O   . TYR B 1 52  ? -20.38400 36.42800  13.32700 1.000 69.30000 ? 52  TYR B O   1 
ATOM   3934 C CB  . TYR B 1 52  ? -21.68200 37.22300  16.13700 1.000 69.30000 ? 52  TYR B CB  1 
ATOM   3935 C CG  . TYR B 1 52  ? -22.55900 37.75900  15.02700 1.000 69.30000 ? 52  TYR B CG  1 
ATOM   3936 C CD1 . TYR B 1 52  ? -23.35900 36.90500  14.27600 1.000 69.30000 ? 52  TYR B CD1 1 
ATOM   3937 C CD2 . TYR B 1 52  ? -22.58600 39.11500  14.72900 1.000 69.30000 ? 52  TYR B CD2 1 
ATOM   3938 C CE1 . TYR B 1 52  ? -24.15700 37.38700  13.25500 1.000 69.30000 ? 52  TYR B CE1 1 
ATOM   3939 C CE2 . TYR B 1 52  ? -23.38500 39.60700  13.71200 1.000 69.30000 ? 52  TYR B CE2 1 
ATOM   3940 C CZ  . TYR B 1 52  ? -24.16900 38.73900  12.98000 1.000 69.30000 ? 52  TYR B CZ  1 
ATOM   3941 O OH  . TYR B 1 52  ? -24.96500 39.22300  11.96700 1.000 69.30000 ? 52  TYR B OH  1 
ATOM   3942 N N   . ASN B 1 53  ? -18.74400 37.17900  14.66800 1.000 68.22000 ? 53  ASN B N   1 
ATOM   3943 C CA  . ASN B 1 53  ? -18.00400 37.75000  13.54700 1.000 68.22000 ? 53  ASN B CA  1 
ATOM   3944 C C   . ASN B 1 53  ? -17.22200 36.68200  12.78800 1.000 68.22000 ? 53  ASN B C   1 
ATOM   3945 O O   . ASN B 1 53  ? -17.38900 36.51900  11.57500 1.000 68.22000 ? 53  ASN B O   1 
ATOM   3946 C CB  . ASN B 1 53  ? -17.07000 38.85600  14.04500 1.000 68.22000 ? 53  ASN B CB  1 
ATOM   3947 C CG  . ASN B 1 53  ? -17.82400 40.04500  14.61000 1.000 68.22000 ? 53  ASN B CG  1 
ATOM   3948 O OD1 . ASN B 1 53  ? -18.10400 40.10500  15.80800 1.000 68.22000 ? 53  ASN B OD1 1 
ATOM   3949 N ND2 . ASN B 1 53  ? -18.16100 40.99600  13.74700 1.000 68.22000 ? 53  ASN B ND2 1 
ATOM   3950 N N   . CYS B 1 54  ? -16.36800 35.94200  13.49000 1.000 65.95000 ? 54  CYS B N   1 
ATOM   3951 C CA  . CYS B 1 54  ? -15.50200 34.94500  12.87400 1.000 65.95000 ? 54  CYS B CA  1 
ATOM   3952 C C   . CYS B 1 54  ? -16.14200 33.56600  12.77700 1.000 65.95000 ? 54  CYS B C   1 
ATOM   3953 O O   . CYS B 1 54  ? -15.48400 32.62700  12.31700 1.000 65.95000 ? 54  CYS B O   1 
ATOM   3954 C CB  . CYS B 1 54  ? -14.17500 34.85100  13.63700 1.000 65.95000 ? 54  CYS B CB  1 
ATOM   3955 S SG  . CYS B 1 54  ? -14.32900 34.88500  15.43500 1.000 65.95000 ? 54  CYS B SG  1 
ATOM   3956 N N   . LEU B 1 55  ? -17.39300 33.41100  13.21000 1.000 65.24000 ? 55  LEU B N   1 
ATOM   3957 C CA  . LEU B 1 55  ? -18.08400 32.13100  13.11900 1.000 65.24000 ? 55  LEU B CA  1 
ATOM   3958 C C   . LEU B 1 55  ? -19.43900 32.19700  12.43600 1.000 65.24000 ? 55  LEU B C   1 
ATOM   3959 O O   . LEU B 1 55  ? -19.95300 31.14300  12.04200 1.000 65.24000 ? 55  LEU B O   1 
ATOM   3960 C CB  . LEU B 1 55  ? -18.27800 31.52400  14.51700 1.000 65.24000 ? 55  LEU B CB  1 
ATOM   3961 C CG  . LEU B 1 55  ? -17.02700 31.06900  15.26800 1.000 65.24000 ? 55  LEU B CG  1 
ATOM   3962 C CD1 . LEU B 1 55  ? -17.41200 30.47800  16.61200 1.000 65.24000 ? 55  LEU B CD1 1 
ATOM   3963 C CD2 . LEU B 1 55  ? -16.24200 30.06300  14.44400 1.000 65.24000 ? 55  LEU B CD2 1 
ATOM   3964 N N   . GLY B 1 56  ? -20.03800 33.37500  12.28300 1.000 69.04000 ? 56  GLY B N   1 
ATOM   3965 C CA  . GLY B 1 56  ? -21.37200 33.46100  11.73000 1.000 69.04000 ? 56  GLY B CA  1 
ATOM   3966 C C   . GLY B 1 56  ? -22.46900 33.04700  12.68100 1.000 69.04000 ? 56  GLY B C   1 
ATOM   3967 O O   . GLY B 1 56  ? -23.59700 32.81000  12.23600 1.000 69.04000 ? 56  GLY B O   1 
ATOM   3968 N N   . PHE B 1 57  ? -22.17100 32.94800  13.97500 1.000 71.03000 ? 57  PHE B N   1 
ATOM   3969 C CA  . PHE B 1 57  ? -23.10600 32.43900  14.97200 1.000 71.03000 ? 57  PHE B CA  1 
ATOM   3970 C C   . PHE B 1 57  ? -23.10100 33.37200  16.17400 1.000 71.03000 ? 57  PHE B C   1 
ATOM   3971 O O   . PHE B 1 57  ? -22.05600 33.57200  16.80000 1.000 71.03000 ? 57  PHE B O   1 
ATOM   3972 C CB  . PHE B 1 57  ? -22.72900 31.01700  15.39500 1.000 71.03000 ? 57  PHE B CB  1 
ATOM   3973 C CG  . PHE B 1 57  ? -23.53800 29.94500  14.72100 1.000 71.03000 ? 57  PHE B CG  1 
ATOM   3974 C CD1 . PHE B 1 57  ? -23.39100 29.69300  13.36700 1.000 71.03000 ? 57  PHE B CD1 1 
ATOM   3975 C CD2 . PHE B 1 57  ? -24.43500 29.17500  15.44700 1.000 71.03000 ? 57  PHE B CD2 1 
ATOM   3976 C CE1 . PHE B 1 57  ? -24.13300 28.70400  12.74500 1.000 71.03000 ? 57  PHE B CE1 1 
ATOM   3977 C CE2 . PHE B 1 57  ? -25.17900 28.18500  14.83100 1.000 71.03000 ? 57  PHE B CE2 1 
ATOM   3978 C CZ  . PHE B 1 57  ? -25.02800 27.94800  13.47900 1.000 71.03000 ? 57  PHE B CZ  1 
ATOM   3979 N N   . HIS B 1 58  ? -24.27100 33.91000  16.51200 1.000 71.21000 ? 58  HIS B N   1 
ATOM   3980 C CA  . HIS B 1 58  ? -24.36800 34.86700  17.60000 1.000 71.21000 ? 58  HIS B CA  1 
ATOM   3981 C C   . HIS B 1 58  ? -24.00900 34.20200  18.92900 1.000 71.21000 ? 58  HIS B C   1 
ATOM   3982 O O   . HIS B 1 58  ? -24.19300 32.99200  19.09700 1.000 71.21000 ? 58  HIS B O   1 
ATOM   3983 C CB  . HIS B 1 58  ? -25.77600 35.45100  17.68500 1.000 71.21000 ? 58  HIS B CB  1 
ATOM   3984 C CG  . HIS B 1 58  ? -26.04600 36.54400  16.69800 1.000 71.21000 ? 58  HIS B CG  1 
ATOM   3985 N ND1 . HIS B 1 58  ? -25.55000 37.82100  16.84800 1.000 71.21000 ? 58  HIS B ND1 1 
ATOM   3986 C CD2 . HIS B 1 58  ? -26.78000 36.55600  15.56000 1.000 71.21000 ? 58  HIS B CD2 1 
ATOM   3987 C CE1 . HIS B 1 58  ? -25.95900 38.57100  15.83900 1.000 71.21000 ? 58  HIS B CE1 1 
ATOM   3988 N NE2 . HIS B 1 58  ? -26.70700 37.82800  15.04400 1.000 71.21000 ? 58  HIS B NE2 1 
ATOM   3989 N N   . PRO B 1 59  ? -23.47300 34.96700  19.88400 1.000 68.90000 ? 59  PRO B N   1 
ATOM   3990 C CA  . PRO B 1 59  ? -23.15700 34.38100  21.19700 1.000 68.90000 ? 59  PRO B CA  1 
ATOM   3991 C C   . PRO B 1 59  ? -24.36300 33.75700  21.88000 1.000 68.90000 ? 59  PRO B C   1 
ATOM   3992 O O   . PRO B 1 59  ? -24.20800 32.75300  22.58900 1.000 68.90000 ? 59  PRO B O   1 
ATOM   3993 C CB  . PRO B 1 59  ? -22.61400 35.58000  21.99100 1.000 68.90000 ? 59  PRO B CB  1 
ATOM   3994 C CG  . PRO B 1 59  ? -22.14500 36.54400  20.94800 1.000 68.90000 ? 59  PRO B CG  1 
ATOM   3995 C CD  . PRO B 1 59  ? -23.08400 36.38400  19.79700 1.000 68.90000 ? 59  PRO B CD  1 
ATOM   3996 N N   . GLU B 1 60  ? -25.56000 34.32500  21.70000 1.000 72.35000 ? 60  GLU B N   1 
ATOM   3997 C CA  . GLU B 1 60  ? -26.76200 33.71500  22.25900 1.000 72.35000 ? 60  GLU B CA  1 
ATOM   3998 C C   . GLU B 1 60  ? -27.17000 32.45000  21.51500 1.000 72.35000 ? 60  GLU B C   1 
ATOM   3999 O O   . GLU B 1 60  ? -27.89400 31.62400  22.08000 1.000 72.35000 ? 60  GLU B O   1 
ATOM   4000 C CB  . GLU B 1 60  ? -27.92100 34.71200  22.24900 1.000 72.35000 ? 60  GLU B CB  1 
ATOM   4001 C CG  . GLU B 1 60  ? -27.55800 36.12000  22.69000 1.000 72.35000 ? 60  GLU B CG  1 
ATOM   4002 C CD  . GLU B 1 60  ? -27.11900 36.99300  21.53100 1.000 72.35000 ? 60  GLU B CD  1 
ATOM   4003 O OE1 . GLU B 1 60  ? -27.15400 36.51100  20.38000 1.000 72.35000 ? 60  GLU B OE1 1 
ATOM   4004 O OE2 . GLU B 1 60  ? -26.74200 38.15800  21.77000 1.000 72.35000 ? 60  GLU B OE2 1 
ATOM   4005 N N   . GLU B 1 61  ? -26.72600 32.28100  20.26600 1.000 73.63000 ? 61  GLU B N   1 
ATOM   4006 C CA  . GLU B 1 61  ? -27.09300 31.10000  19.49300 1.000 73.63000 ? 61  GLU B CA  1 
ATOM   4007 C C   . GLU B 1 61  ? -26.49600 29.82200  20.06300 1.000 73.63000 ? 61  GLU B C   1 
ATOM   4008 O O   . GLU B 1 61  ? -27.03300 28.73800  19.80800 1.000 73.63000 ? 61  GLU B O   1 
ATOM   4009 C CB  . GLU B 1 61  ? -26.66200 31.25800  18.03400 1.000 73.63000 ? 61  GLU B CB  1 
ATOM   4010 C CG  . GLU B 1 61  ? -27.43000 32.31600  17.26400 1.000 73.63000 ? 61  GLU B CG  1 
ATOM   4011 C CD  . GLU B 1 61  ? -27.09500 32.31800  15.78400 1.000 73.63000 ? 61  GLU B CD  1 
ATOM   4012 O OE1 . GLU B 1 61  ? -26.75100 31.24300  15.24800 1.000 73.63000 ? 61  GLU B OE1 1 
ATOM   4013 O OE2 . GLU B 1 61  ? -27.17400 33.39500  15.15800 1.000 73.63000 ? 61  GLU B OE2 1 
ATOM   4014 N N   . LEU B 1 62  ? -25.39800 29.91600  20.81900 1.000 66.47000 ? 62  LEU B N   1 
ATOM   4015 C CA  . LEU B 1 62  ? -24.71800 28.74600  21.38000 1.000 66.47000 ? 62  LEU B CA  1 
ATOM   4016 C C   . LEU B 1 62  ? -24.54200 28.97300  22.87900 1.000 66.47000 ? 62  LEU B C   1 
ATOM   4017 O O   . LEU B 1 62  ? -23.44500 29.27600  23.35500 1.000 66.47000 ? 62  LEU B O   1 
ATOM   4018 C CB  . LEU B 1 62  ? -23.38500 28.49300  20.68000 1.000 66.47000 ? 62  LEU B CB  1 
ATOM   4019 C CG  . LEU B 1 62  ? -23.40300 28.60400  19.15600 1.000 66.47000 ? 62  LEU B CG  1 
ATOM   4020 C CD1 . LEU B 1 62  ? -22.87000 29.96000  18.73300 1.000 66.47000 ? 62  LEU B CD1 1 
ATOM   4021 C CD2 . LEU B 1 62  ? -22.61200 27.48100  18.51200 1.000 66.47000 ? 62  LEU B CD2 1 
ATOM   4022 N N   . LEU B 1 63  ? -25.63700 28.83000  23.62200 1.000 65.44000 ? 63  LEU B N   1 
ATOM   4023 C CA  . LEU B 1 63  ? -25.61200 28.87600  25.07900 1.000 65.44000 ? 63  LEU B CA  1 
ATOM   4024 C C   . LEU B 1 63  ? -26.46200 27.72600  25.59200 1.000 65.44000 ? 63  LEU B C   1 
ATOM   4025 O O   . LEU B 1 63  ? -27.66700 27.67800  25.32400 1.000 65.44000 ? 63  LEU B O   1 
ATOM   4026 C CB  . LEU B 1 63  ? -26.12700 30.21900  25.60800 1.000 65.44000 ? 63  LEU B CB  1 
ATOM   4027 C CG  . LEU B 1 63  ? -25.20600 31.42200  25.38800 1.000 65.44000 ? 63  LEU B CG  1 
ATOM   4028 C CD1 . LEU B 1 63  ? -25.87300 32.71300  25.84000 1.000 65.44000 ? 63  LEU B CD1 1 
ATOM   4029 C CD2 . LEU B 1 63  ? -23.88100 31.22200  26.10900 1.000 65.44000 ? 63  LEU B CD2 1 
ATOM   4030 N N   . ASN B 1 64  ? -25.83200 26.80100  26.31500 1.000 63.41000 ? 64  ASN B N   1 
ATOM   4031 C CA  . ASN B 1 64  ? -26.43900 25.53300  26.71600 1.000 63.41000 ? 64  ASN B CA  1 
ATOM   4032 C C   . ASN B 1 64  ? -26.93700 24.73500  25.51600 1.000 63.41000 ? 64  ASN B C   1 
ATOM   4033 O O   . ASN B 1 64  ? -27.84600 23.90900  25.64500 1.000 63.41000 ? 64  ASN B O   1 
ATOM   4034 C CB  . ASN B 1 64  ? -27.57500 25.74200  27.72500 1.000 63.41000 ? 64  ASN B CB  1 
ATOM   4035 C CG  . ASN B 1 64  ? -27.07300 25.83800  29.15600 1.000 63.41000 ? 64  ASN B CG  1 
ATOM   4036 O OD1 . ASN B 1 64  ? -27.06300 24.84900  29.89000 1.000 63.41000 ? 64  ASN B OD1 1 
ATOM   4037 N ND2 . ASN B 1 64  ? -26.65100 27.03200  29.55800 1.000 63.41000 ? 64  ASN B ND2 1 
ATOM   4038 N N   . GLN B 1 65  ? -26.34900 24.97100  24.34700 1.000 68.39000 ? 65  GLN B N   1 
ATOM   4039 C CA  . GLN B 1 65  ? -26.53700 24.31400  23.06800 1.000 68.39000 ? 65  GLN B CA  1 
ATOM   4040 C C   . GLN B 1 65  ? -25.48100 23.23500  22.86400 1.000 68.39000 ? 65  GLN B C   1 
ATOM   4041 O O   . GLN B 1 65  ? -24.35000 23.37200  23.33400 1.000 68.39000 ? 65  GLN B O   1 
ATOM   4042 C CB  . GLN B 1 65  ? -26.44600 25.33100  21.92300 1.000 68.39000 ? 65  GLN B CB  1 
ATOM   4043 C CG  . GLN B 1 65  ? -27.44700 26.46900  22.01800 1.000 68.39000 ? 65  GLN B CG  1 
ATOM   4044 C CD  . GLN B 1 65  ? -28.79000 26.12000  21.41000 1.000 68.39000 ? 65  GLN B CD  1 
ATOM   4045 O OE1 . GLN B 1 65  ? -28.89700 25.20700  20.59100 1.000 68.39000 ? 65  GLN B OE1 1 
ATOM   4046 N NE2 . GLN B 1 65  ? -29.82700 26.84900  21.80900 1.000 68.39000 ? 65  GLN B NE2 1 
ATOM   4047 N N   . PRO B 1 66  ? -25.82000 22.14900  22.17000 1.000 68.67000 ? 66  PRO B N   1 
ATOM   4048 C CA  . PRO B 1 66  ? -24.80100 21.15000  21.82600 1.000 68.67000 ? 66  PRO B CA  1 
ATOM   4049 C C   . PRO B 1 66  ? -23.73000 21.72900  20.91000 1.000 68.67000 ? 66  PRO B C   1 
ATOM   4050 O O   . PRO B 1 66  ? -23.99600 22.59800  20.07600 1.000 68.67000 ? 66  PRO B O   1 
ATOM   4051 C CB  . PRO B 1 66  ? -25.60600 20.05200  21.11900 1.000 68.67000 ? 66  PRO B CB  1 
ATOM   4052 C CG  . PRO B 1 66  ? -27.00600 20.23800  21.59600 1.000 68.67000 ? 66  PRO B CG  1 
ATOM   4053 C CD  . PRO B 1 66  ? -27.17100 21.71700  21.77800 1.000 68.67000 ? 66  PRO B CD  1 
ATOM   4054 N N   . LEU B 1 67  ? -22.49900 21.23300  21.07700 1.000 66.36000 ? 67  LEU B N   1 
ATOM   4055 C CA  . LEU B 1 67  ? -21.42000 21.58100  20.15600 1.000 66.36000 ? 67  LEU B CA  1 
ATOM   4056 C C   . LEU B 1 67  ? -21.70500 21.09800  18.74000 1.000 66.36000 ? 67  LEU B C   1 
ATOM   4057 O O   . LEU B 1 67  ? -21.20300 21.68900  17.77700 1.000 66.36000 ? 67  LEU B O   1 
ATOM   4058 C CB  . LEU B 1 67  ? -20.09600 20.99200  20.65500 1.000 66.36000 ? 67  LEU B CB  1 
ATOM   4059 C CG  . LEU B 1 67  ? -18.88400 21.02600  19.71500 1.000 66.36000 ? 67  LEU B CG  1 
ATOM   4060 C CD1 . LEU B 1 67  ? -18.45100 22.45700  19.41500 1.000 66.36000 ? 67  LEU B CD1 1 
ATOM   4061 C CD2 . LEU B 1 67  ? -17.72600 20.21600  20.27700 1.000 66.36000 ? 67  LEU B CD2 1 
ATOM   4062 N N   . ARG B 1 68  ? -22.52800 20.05900  18.59800 1.000 65.83000 ? 68  ARG B N   1 
ATOM   4063 C CA  . ARG B 1 68  ? -22.81800 19.49100  17.28800 1.000 65.83000 ? 68  ARG B CA  1 
ATOM   4064 C C   . ARG B 1 68  ? -23.48100 20.50200  16.36200 1.000 65.83000 ? 68  ARG B C   1 
ATOM   4065 O O   . ARG B 1 68  ? -23.37900 20.37600  15.13800 1.000 65.83000 ? 68  ARG B O   1 
ATOM   4066 C CB  . ARG B 1 68  ? -23.70300 18.25800  17.45400 1.000 65.83000 ? 68  ARG B CB  1 
ATOM   4067 C CG  . ARG B 1 68  ? -23.30200 17.38800  18.63500 1.000 65.83000 ? 68  ARG B CG  1 
ATOM   4068 C CD  . ARG B 1 68  ? -24.40500 16.42900  19.03700 1.000 65.83000 ? 68  ARG B CD  1 
ATOM   4069 N NE  . ARG B 1 68  ? -25.61500 17.13300  19.44300 1.000 65.83000 ? 68  ARG B NE  1 
ATOM   4070 C CZ  . ARG B 1 68  ? -26.68000 16.54600  19.97000 1.000 65.83000 ? 68  ARG B CZ  1 
ATOM   4071 N NH1 . ARG B 1 68  ? -26.71500 15.24100  20.18200 1.000 65.83000 ? 68  ARG B NH1 1 
ATOM   4072 N NH2 . ARG B 1 68  ? -27.73600 17.28800  20.29300 1.000 65.83000 ? 68  ARG B NH2 1 
ATOM   4073 N N   . LYS B 1 69  ? -24.17800 21.49800  16.92000 1.000 68.62000 ? 69  LYS B N   1 
ATOM   4074 C CA  . LYS B 1 69  ? -24.79400 22.52500  16.08500 1.000 68.62000 ? 69  LYS B CA  1 
ATOM   4075 C C   . LYS B 1 69  ? -23.76200 23.39800  15.38200 1.000 68.62000 ? 69  LYS B C   1 
ATOM   4076 O O   . LYS B 1 69  ? -24.08600 24.01700  14.36400 1.000 68.62000 ? 69  LYS B O   1 
ATOM   4077 C CB  . LYS B 1 69  ? -25.73700 23.40000  16.91600 1.000 68.62000 ? 69  LYS B CB  1 
ATOM   4078 C CG  . LYS B 1 69  ? -25.05100 24.46300  17.76000 1.000 68.62000 ? 69  LYS B CG  1 
ATOM   4079 C CD  . LYS B 1 69  ? -26.06300 25.43100  18.35700 1.000 68.62000 ? 69  LYS B CD  1 
ATOM   4080 C CE  . LYS B 1 69  ? -26.83800 26.16100  17.27100 1.000 68.62000 ? 69  LYS B CE  1 
ATOM   4081 N NZ  . LYS B 1 69  ? -27.78700 27.16300  17.83200 1.000 68.62000 ? 69  LYS B NZ  1 
ATOM   4082 N N   . LEU B 1 70  ? -22.54100 23.48200  15.90800 1.000 67.71000 ? 70  LEU B N   1 
ATOM   4083 C CA  . LEU B 1 70  ? -21.50700 24.30800  15.29900 1.000 67.71000 ? 70  LEU B CA  1 
ATOM   4084 C C   . LEU B 1 70  ? -20.47100 23.50900  14.52100 1.000 67.71000 ? 70  LEU B C   1 
ATOM   4085 O O   . LEU B 1 70  ? -19.91300 24.02800  13.54700 1.000 67.71000 ? 70  LEU B O   1 
ATOM   4086 C CB  . LEU B 1 70  ? -20.80100 25.15000  16.36800 1.000 67.71000 ? 70  LEU B CB  1 
ATOM   4087 C CG  . LEU B 1 70  ? -20.04700 26.38100  15.85600 1.000 67.71000 ? 70  LEU B CG  1 
ATOM   4088 C CD1 . LEU B 1 70  ? -21.00100 27.34700  15.16500 1.000 67.71000 ? 70  LEU B CD1 1 
ATOM   4089 C CD2 . LEU B 1 70  ? -19.29800 27.07500  16.98700 1.000 67.71000 ? 70  LEU B CD2 1 
ATOM   4090 N N   . LEU B 1 71  ? -20.19900 22.27000  14.91700 1.000 65.19000 ? 71  LEU B N   1 
ATOM   4091 C CA  . LEU B 1 71  ? -19.20500 21.43400  14.26100 1.000 65.19000 ? 71  LEU B CA  1 
ATOM   4092 C C   . LEU B 1 71  ? -19.87100 20.31800  13.46600 1.000 65.19000 ? 71  LEU B C   1 
ATOM   4093 O O   . LEU B 1 71  ? -20.92600 19.80100  13.84700 1.000 65.19000 ? 71  LEU B O   1 
ATOM   4094 C CB  . LEU B 1 71  ? -18.23400 20.82900  15.28100 1.000 65.19000 ? 71  LEU B CB  1 
ATOM   4095 C CG  . LEU B 1 71  ? -16.92200 21.58000  15.51900 1.000 65.19000 ? 71  LEU B CG  1 
ATOM   4096 C CD1 . LEU B 1 71  ? -16.09500 20.89200  16.59600 1.000 65.19000 ? 71  LEU B CD1 1 
ATOM   4097 C CD2 . LEU B 1 71  ? -16.13100 21.69200  14.22500 1.000 65.19000 ? 71  LEU B CD2 1 
ATOM   4098 N N   . GLU B 1 72  ? -19.23600 19.95000  12.35600 1.000 62.68000 ? 72  GLU B N   1 
ATOM   4099 C CA  . GLU B 1 72  ? -19.71300 18.84700  11.53500 1.000 62.68000 ? 72  GLU B CA  1 
ATOM   4100 C C   . GLU B 1 72  ? -19.62400 17.53200  12.30200 1.000 62.68000 ? 72  GLU B C   1 
ATOM   4101 O O   . GLU B 1 72  ? -18.71100 17.31500  13.10400 1.000 62.68000 ? 72  GLU B O   1 
ATOM   4102 C CB  . GLU B 1 72  ? -18.90300 18.75500  10.24200 1.000 62.68000 ? 72  GLU B CB  1 
ATOM   4103 C CG  . GLU B 1 72  ? -18.94400 20.01500  9.38700  1.000 62.68000 ? 72  GLU B CG  1 
ATOM   4104 C CD  . GLU B 1 72  ? -20.30500 20.26200  8.75900  1.000 62.68000 ? 72  GLU B CD  1 
ATOM   4105 O OE1 . GLU B 1 72  ? -21.07800 19.29300  8.60500  1.000 62.68000 ? 72  GLU B OE1 1 
ATOM   4106 O OE2 . GLU B 1 72  ? -20.60000 21.42700  8.41800  1.000 62.68000 ? 72  GLU B OE2 1 
ATOM   4107 N N   . SER B 1 73  ? -20.59600 16.65000  12.04900 1.000 57.26000 ? 73  SER B N   1 
ATOM   4108 C CA  . SER B 1 73  ? -20.64500 15.38000  12.76700 1.000 57.26000 ? 73  SER B CA  1 
ATOM   4109 C C   . SER B 1 73  ? -19.43500 14.50700  12.45900 1.000 57.26000 ? 73  SER B C   1 
ATOM   4110 O O   . SER B 1 73  ? -19.03100 13.69300  13.29600 1.000 57.26000 ? 73  SER B O   1 
ATOM   4111 C CB  . SER B 1 73  ? -21.93400 14.63200  12.43000 1.000 57.26000 ? 73  SER B CB  1 
ATOM   4112 O OG  . SER B 1 73  ? -22.02000 13.42400  13.16500 1.000 57.26000 ? 73  SER B OG  1 
ATOM   4113 N N   . GLU B 1 74  ? -18.84900 14.65600  11.26900 1.000 56.27000 ? 74  GLU B N   1 
ATOM   4114 C CA  . GLU B 1 74  ? -17.63100 13.92000  10.94800 1.000 56.27000 ? 74  GLU B CA  1 
ATOM   4115 C C   . GLU B 1 74  ? -16.46900 14.34500  11.83400 1.000 56.27000 ? 74  GLU B C   1 
ATOM   4116 O O   . GLU B 1 74  ? -15.56400 13.54500  12.09700 1.000 56.27000 ? 74  GLU B O   1 
ATOM   4117 C CB  . GLU B 1 74  ? -17.26600 14.12300  9.47800  1.000 56.27000 ? 74  GLU B CB  1 
ATOM   4118 C CG  . GLU B 1 74  ? -18.20400 13.45100  8.49100  1.000 56.27000 ? 74  GLU B CG  1 
ATOM   4119 C CD  . GLU B 1 74  ? -19.48900 14.22500  8.25300  1.000 56.27000 ? 74  GLU B CD  1 
ATOM   4120 O OE1 . GLU B 1 74  ? -20.11600 14.68100  9.23300  1.000 56.27000 ? 74  GLU B OE1 1 
ATOM   4121 O OE2 . GLU B 1 74  ? -19.87200 14.37800  7.07500  1.000 56.27000 ? 74  GLU B OE2 1 
ATOM   4122 N N   . GLN B 1 75  ? -16.47100 15.59500  12.29400 1.000 58.57000 ? 75  GLN B N   1 
ATOM   4123 C CA  . GLN B 1 75  ? -15.38800 16.10100  13.12500 1.000 58.57000 ? 75  GLN B CA  1 
ATOM   4124 C C   . GLN B 1 75  ? -15.62700 15.88400  14.61300 1.000 58.57000 ? 75  GLN B C   1 
ATOM   4125 O O   . GLN B 1 75  ? -14.66100 15.67600  15.35800 1.000 58.57000 ? 75  GLN B O   1 
ATOM   4126 C CB  . GLN B 1 75  ? -15.16600 17.58800  12.83300 1.000 58.57000 ? 75  GLN B CB  1 
ATOM   4127 C CG  . GLN B 1 75  ? -14.63700 17.84100  11.42600 1.000 58.57000 ? 75  GLN B CG  1 
ATOM   4128 C CD  . GLN B 1 75  ? -14.76400 19.28600  10.99100 1.000 58.57000 ? 75  GLN B CD  1 
ATOM   4129 O OE1 . GLN B 1 75  ? -15.64000 20.01400  11.45600 1.000 58.57000 ? 75  GLN B OE1 1 
ATOM   4130 N NE2 . GLN B 1 75  ? -13.88600 19.71000  10.08800 1.000 58.57000 ? 75  GLN B NE2 1 
ATOM   4131 N N   . ILE B 1 76  ? -16.88000 15.92700  15.07400 1.000 56.51000 ? 76  ILE B N   1 
ATOM   4132 C CA  . ILE B 1 76  ? -17.14700 15.59100  16.46800 1.000 56.51000 ? 76  ILE B CA  1 
ATOM   4133 C C   . ILE B 1 76  ? -16.96800 14.10200  16.72500 1.000 56.51000 ? 76  ILE B C   1 
ATOM   4134 O O   . ILE B 1 76  ? -16.78200 13.69500  17.87700 1.000 56.51000 ? 76  ILE B O   1 
ATOM   4135 C CB  . ILE B 1 76  ? -18.55500 16.03600  16.90600 1.000 56.51000 ? 76  ILE B CB  1 
ATOM   4136 C CG1 . ILE B 1 76  ? -19.62500 15.18300  16.22600 1.000 56.51000 ? 76  ILE B CG1 1 
ATOM   4137 C CG2 . ILE B 1 76  ? -18.76800 17.51100  16.61200 1.000 56.51000 ? 76  ILE B CG2 1 
ATOM   4138 C CD1 . ILE B 1 76  ? -20.99300 15.33500  16.83700 1.000 56.51000 ? 76  ILE B CD1 1 
ATOM   4139 N N   . ASP B 1 77  ? -17.03900 13.27000  15.68000 1.000 58.53000 ? 77  ASP B N   1 
ATOM   4140 C CA  . ASP B 1 77  ? -16.74600 11.85200  15.85600 1.000 58.53000 ? 77  ASP B CA  1 
ATOM   4141 C C   . ASP B 1 77  ? -15.29200 11.64300  16.25500 1.000 58.53000 ? 77  ASP B C   1 
ATOM   4142 O O   . ASP B 1 77  ? -14.99100 10.82500  17.13200 1.000 58.53000 ? 77  ASP B O   1 
ATOM   4143 C CB  . ASP B 1 77  ? -17.06200 11.08100  14.57300 1.000 58.53000 ? 77  ASP B CB  1 
ATOM   4144 C CG  . ASP B 1 77  ? -18.55100 10.92500  14.33400 1.000 58.53000 ? 77  ASP B CG  1 
ATOM   4145 O OD1 . ASP B 1 77  ? -19.34500 11.46100  15.13500 1.000 58.53000 ? 77  ASP B OD1 1 
ATOM   4146 O OD2 . ASP B 1 77  ? -18.92800 10.26300  13.34300 1.000 58.53000 ? 77  ASP B OD2 1 
ATOM   4147 N N   . PHE B 1 78  ? -14.37400 12.37700  15.62000 1.000 55.53000 ? 78  PHE B N   1 
ATOM   4148 C CA  . PHE B 1 78  ? -12.98400 12.35300  16.05900 1.000 55.53000 ? 78  PHE B CA  1 
ATOM   4149 C C   . PHE B 1 78  ? -12.82700 12.98300  17.43600 1.000 55.53000 ? 78  PHE B C   1 
ATOM   4150 O O   . PHE B 1 78  ? -11.98300 12.54300  18.22400 1.000 55.53000 ? 78  PHE B O   1 
ATOM   4151 C CB  . PHE B 1 78  ? -12.10500 13.07900  15.04200 1.000 55.53000 ? 78  PHE B CB  1 
ATOM   4152 C CG  . PHE B 1 78  ? -10.63100 12.88600  15.26000 1.000 55.53000 ? 78  PHE B CG  1 
ATOM   4153 C CD1 . PHE B 1 78  ? -10.14700 11.74000  15.86900 1.000 55.53000 ? 78  PHE B CD1 1 
ATOM   4154 C CD2 . PHE B 1 78  ? -9.72700  13.85500  14.85500 1.000 55.53000 ? 78  PHE B CD2 1 
ATOM   4155 C CE1 . PHE B 1 78  ? -8.79000  11.56300  16.06700 1.000 55.53000 ? 78  PHE B CE1 1 
ATOM   4156 C CE2 . PHE B 1 78  ? -8.36900  13.68400  15.05100 1.000 55.53000 ? 78  PHE B CE2 1 
ATOM   4157 C CZ  . PHE B 1 78  ? -7.90000  12.53600  15.65800 1.000 55.53000 ? 78  PHE B CZ  1 
ATOM   4158 N N   . LEU B 1 79  ? -13.63800 13.99800  17.74600 1.000 56.03000 ? 79  LEU B N   1 
ATOM   4159 C CA  . LEU B 1 79  ? -13.51000 14.68400  19.02800 1.000 56.03000 ? 79  LEU B CA  1 
ATOM   4160 C C   . LEU B 1 79  ? -13.84000 13.75700  20.19200 1.000 56.03000 ? 79  LEU B C   1 
ATOM   4161 O O   . LEU B 1 79  ? -13.22800 13.85400  21.26100 1.000 56.03000 ? 79  LEU B O   1 
ATOM   4162 C CB  . LEU B 1 79  ? -14.41100 15.92100  19.04900 1.000 56.03000 ? 79  LEU B CB  1 
ATOM   4163 C CG  . LEU B 1 79  ? -14.38800 16.81800  20.29100 1.000 56.03000 ? 79  LEU B CG  1 
ATOM   4164 C CD1 . LEU B 1 79  ? -14.42600 18.28400  19.88500 1.000 56.03000 ? 79  LEU B CD1 1 
ATOM   4165 C CD2 . LEU B 1 79  ? -15.55300 16.49500  21.21500 1.000 56.03000 ? 79  LEU B CD2 1 
ATOM   4166 N N   . ASN B 1 80  ? -14.80000 12.84800  20.00600 1.000 56.23000 ? 80  ASN B N   1 
ATOM   4167 C CA  . ASN B 1 80  ? -15.09300 11.87900  21.05700 1.000 56.23000 ? 80  ASN B CA  1 
ATOM   4168 C C   . ASN B 1 80  ? -13.93600 10.90300  21.24400 1.000 56.23000 ? 80  ASN B C   1 
ATOM   4169 O O   . ASN B 1 80  ? -13.60800 10.52500  22.37700 1.000 56.23000 ? 80  ASN B O   1 
ATOM   4170 C CB  . ASN B 1 80  ? -16.38500 11.13200  20.73300 1.000 56.23000 ? 80  ASN B CB  1 
ATOM   4171 C CG  . ASN B 1 80  ? -17.57300 12.06200  20.58300 1.000 56.23000 ? 80  ASN B CG  1 
ATOM   4172 O OD1 . ASN B 1 80  ? -17.69000 13.06000  21.29500 1.000 56.23000 ? 80  ASN B OD1 1 
ATOM   4173 N ND2 . ASN B 1 80  ? -18.46000 11.74000  19.65000 1.000 56.23000 ? 80  ASN B ND2 1 
ATOM   4174 N N   . ASP B 1 81  ? -13.29000 10.50600  20.14400 1.000 56.10000 ? 81  ASP B N   1 
ATOM   4175 C CA  . ASP B 1 81  ? -12.12100 9.64000   20.24300 1.000 56.10000 ? 81  ASP B CA  1 
ATOM   4176 C C   . ASP B 1 81  ? -10.95800 10.35500  20.91600 1.000 56.10000 ? 81  ASP B C   1 
ATOM   4177 O O   . ASP B 1 81  ? -10.12700 9.71200   21.56800 1.000 56.10000 ? 81  ASP B O   1 
ATOM   4178 C CB  . ASP B 1 81  ? -11.72200 9.14400   18.85200 1.000 56.10000 ? 81  ASP B CB  1 
ATOM   4179 C CG  . ASP B 1 81  ? -10.57000 8.16000   18.89000 1.000 56.10000 ? 81  ASP B CG  1 
ATOM   4180 O OD1 . ASP B 1 81  ? -10.67300 7.14900   19.61700 1.000 56.10000 ? 81  ASP B OD1 1 
ATOM   4181 O OD2 . ASP B 1 81  ? -9.56600  8.39300   18.18300 1.000 56.10000 ? 81  ASP B OD2 1 
ATOM   4182 N N   . CYS B 1 82  ? -10.88000 11.67900  20.76900 1.000 51.73000 ? 82  CYS B N   1 
ATOM   4183 C CA  . CYS B 1 82  ? -9.88300  12.44500  21.50800 1.000 51.73000 ? 82  CYS B CA  1 
ATOM   4184 C C   . CYS B 1 82  ? -10.23700 12.52800  22.98800 1.000 51.73000 ? 82  CYS B C   1 
ATOM   4185 O O   . CYS B 1 82  ? -9.35600  12.42700  23.85000 1.000 51.73000 ? 82  CYS B O   1 
ATOM   4186 C CB  . CYS B 1 82  ? -9.75500  13.84500  20.91000 1.000 51.73000 ? 82  CYS B CB  1 
ATOM   4187 S SG  . CYS B 1 82  ? -9.41800  13.87300  19.13500 1.000 51.73000 ? 82  CYS B SG  1 
ATOM   4188 N N   . LEU B 1 83  ? -11.52300 12.71200  23.29900 1.000 52.85000 ? 83  LEU B N   1 
ATOM   4189 C CA  . LEU B 1 83  ? -11.96000 12.80600  24.68800 1.000 52.85000 ? 83  LEU B CA  1 
ATOM   4190 C C   . LEU B 1 83  ? -11.83700 11.48500  25.43300 1.000 52.85000 ? 83  LEU B C   1 
ATOM   4191 O O   . LEU B 1 83  ? -11.74900 11.49200  26.66600 1.000 52.85000 ? 83  LEU B O   1 
ATOM   4192 C CB  . LEU B 1 83  ? -13.40400 13.30800  24.76200 1.000 52.85000 ? 83  LEU B CB  1 
ATOM   4193 C CG  . LEU B 1 83  ? -13.60500 14.81900  24.64200 1.000 52.85000 ? 83  LEU B CG  1 
ATOM   4194 C CD1 . LEU B 1 83  ? -15.07300 15.17600  24.80900 1.000 52.85000 ? 83  LEU B CD1 1 
ATOM   4195 C CD2 . LEU B 1 83  ? -12.75200 15.55000  25.66600 1.000 52.85000 ? 83  LEU B CD2 1 
ATOM   4196 N N   . THR B 1 84  ? -11.83800 10.35400  24.72200 1.000 52.09000 ? 84  THR B N   1 
ATOM   4197 C CA  . THR B 1 84  ? -11.63000 9.07000   25.38600 1.000 52.09000 ? 84  THR B CA  1 
ATOM   4198 C C   . THR B 1 84  ? -10.24500 8.96200   26.01100 1.000 52.09000 ? 84  THR B C   1 
ATOM   4199 O O   . THR B 1 84  ? -10.06600 8.19600   26.96300 1.000 52.09000 ? 84  THR B O   1 
ATOM   4200 C CB  . THR B 1 84  ? -11.83200 7.91600   24.40300 1.000 52.09000 ? 84  THR B CB  1 
ATOM   4201 O OG1 . THR B 1 84  ? -10.99800 8.10800   23.25200 1.000 52.09000 ? 84  THR B OG1 1 
ATOM   4202 C CG2 . THR B 1 84  ? -13.28800 7.82500   23.96500 1.000 52.09000 ? 84  THR B CG2 1 
ATOM   4203 N N   . GLN B 1 85  ? -9.27000  9.71000   25.50300 1.000 49.86000 ? 85  GLN B N   1 
ATOM   4204 C CA  . GLN B 1 85  ? -7.89900  9.60500   25.98200 1.000 49.86000 ? 85  GLN B CA  1 
ATOM   4205 C C   . GLN B 1 85  ? -7.75900  10.16000  27.39600 1.000 49.86000 ? 85  GLN B C   1 
ATOM   4206 O O   . GLN B 1 85  ? -8.54700  10.99700  27.84500 1.000 49.86000 ? 85  GLN B O   1 
ATOM   4207 C CB  . GLN B 1 85  ? -6.95000  10.34600  25.03900 1.000 49.86000 ? 85  GLN B CB  1 
ATOM   4208 C CG  . GLN B 1 85  ? -7.12900  9.98900   23.57300 1.000 49.86000 ? 85  GLN B CG  1 
ATOM   4209 C CD  . GLN B 1 85  ? -6.90500  8.51400   23.29800 1.000 49.86000 ? 85  GLN B CD  1 
ATOM   4210 O OE1 . GLN B 1 85  ? -6.06100  7.87600   23.92600 1.000 49.86000 ? 85  GLN B OE1 1 
ATOM   4211 N NE2 . GLN B 1 85  ? -7.66700  7.96300   22.35800 1.000 49.86000 ? 85  GLN B NE2 1 
ATOM   4212 N N   . GLU B 1 86  ? -6.74000  9.66400   28.10700 1.000 44.99000 ? 86  GLU B N   1 
ATOM   4213 C CA  . GLU B 1 86  ? -6.44600  10.16600  29.44700 1.000 44.99000 ? 86  GLU B CA  1 
ATOM   4214 C C   . GLU B 1 86  ? -6.05500  11.64100  29.42600 1.000 44.99000 ? 86  GLU B C   1 
ATOM   4215 O O   . GLU B 1 86  ? -6.35400  12.37600  30.37500 1.000 44.99000 ? 86  GLU B O   1 
ATOM   4216 C CB  . GLU B 1 86  ? -5.33500  9.32200   30.07600 1.000 44.99000 ? 86  GLU B CB  1 
ATOM   4217 C CG  . GLU B 1 86  ? -4.76000  9.88200   31.36300 1.000 44.99000 ? 86  GLU B CG  1 
ATOM   4218 C CD  . GLU B 1 86  ? -3.55000  9.10800   31.83900 1.000 44.99000 ? 86  GLU B CD  1 
ATOM   4219 O OE1 . GLU B 1 86  ? -3.44200  7.90900   31.50400 1.000 44.99000 ? 86  GLU B OE1 1 
ATOM   4220 O OE2 . GLU B 1 86  ? -2.70500  9.70000   32.54100 1.000 44.99000 ? 86  GLU B OE2 1 
ATOM   4221 N N   . ASP B 1 87  ? -5.41000  12.09300  28.35000 1.000 48.25000 ? 87  ASP B N   1 
ATOM   4222 C CA  . ASP B 1 87  ? -5.02900  13.49300  28.18400 1.000 48.25000 ? 87  ASP B CA  1 
ATOM   4223 C C   . ASP B 1 87  ? -5.32100  13.91200  26.75300 1.000 48.25000 ? 87  ASP B C   1 
ATOM   4224 O O   . ASP B 1 87  ? -4.78100  13.32900  25.80800 1.000 48.25000 ? 87  ASP B O   1 
ATOM   4225 C CB  . ASP B 1 87  ? -3.55200  13.71500  28.51500 1.000 48.25000 ? 87  ASP B CB  1 
ATOM   4226 C CG  . ASP B 1 87  ? -3.33300  14.10300  29.96100 1.000 48.25000 ? 87  ASP B CG  1 
ATOM   4227 O OD1 . ASP B 1 87  ? -3.84400  15.16500  30.37500 1.000 48.25000 ? 87  ASP B OD1 1 
ATOM   4228 O OD2 . ASP B 1 87  ? -2.66100  13.34000  30.68500 1.000 48.25000 ? 87  ASP B OD2 1 
ATOM   4229 N N   . ILE B 1 88  ? -6.16800  14.93100  26.60300 1.000 47.20000 ? 88  ILE B N   1 
ATOM   4230 C CA  . ILE B 1 88  ? -6.63900  15.34100  25.28400 1.000 47.20000 ? 88  ILE B CA  1 
ATOM   4231 C C   . ILE B 1 88  ? -5.53600  16.00000  24.46300 1.000 47.20000 ? 88  ILE B C   1 
ATOM   4232 O O   . ILE B 1 88  ? -5.57300  15.96100  23.22500 1.000 47.20000 ? 88  ILE B O   1 
ATOM   4233 C CB  . ILE B 1 88  ? -7.85300  16.27400  25.43700 1.000 47.20000 ? 88  ILE B CB  1 
ATOM   4234 C CG1 . ILE B 1 88  ? -8.78800  15.74200  26.52300 1.000 47.20000 ? 88  ILE B CG1 1 
ATOM   4235 C CG2 . ILE B 1 88  ? -8.59600  16.39100  24.12500 1.000 47.20000 ? 88  ILE B CG2 1 
ATOM   4236 C CD1 . ILE B 1 88  ? -9.80100  16.76000  27.01200 1.000 47.20000 ? 88  ILE B CD1 1 
ATOM   4237 N N   . GLN B 1 89  ? -4.52500  16.58100  25.11800 1.000 47.35000 ? 89  GLN B N   1 
ATOM   4238 C CA  . GLN B 1 89  ? -3.57300  17.43800  24.41500 1.000 47.35000 ? 89  GLN B CA  1 
ATOM   4239 C C   . GLN B 1 89  ? -2.76800  16.68400  23.36600 1.000 47.35000 ? 89  GLN B C   1 
ATOM   4240 O O   . GLN B 1 89  ? -2.15400  17.32000  22.50000 1.000 47.35000 ? 89  GLN B O   1 
ATOM   4241 C CB  . GLN B 1 89  ? -2.61800  18.11400  25.40300 1.000 47.35000 ? 89  GLN B CB  1 
ATOM   4242 C CG  . GLN B 1 89  ? -3.25500  19.20900  26.24500 1.000 47.35000 ? 89  GLN B CG  1 
ATOM   4243 C CD  . GLN B 1 89  ? -3.78600  18.69600  27.57000 1.000 47.35000 ? 89  GLN B CD  1 
ATOM   4244 O OE1 . GLN B 1 89  ? -3.86700  17.48800  27.79300 1.000 47.35000 ? 89  GLN B OE1 1 
ATOM   4245 N NE2 . GLN B 1 89  ? -4.14200  19.61500  28.46200 1.000 47.35000 ? 89  GLN B NE2 1 
ATOM   4246 N N   . ILE B 1 90  ? -2.74000  15.35200  23.43300 1.000 43.39000 ? 90  ILE B N   1 
ATOM   4247 C CA  . ILE B 1 90  ? -2.02000  14.58000  22.42600 1.000 43.39000 ? 90  ILE B CA  1 
ATOM   4248 C C   . ILE B 1 90  ? -2.60000  14.82500  21.04100 1.000 43.39000 ? 90  ILE B C   1 
ATOM   4249 O O   . ILE B 1 90  ? -1.88000  14.76200  20.03700 1.000 43.39000 ? 90  ILE B O   1 
ATOM   4250 C CB  . ILE B 1 90  ? -2.05100  13.08400  22.78500 1.000 43.39000 ? 90  ILE B CB  1 
ATOM   4251 C CG1 . ILE B 1 90  ? -1.96800  12.90000  24.30000 1.000 43.39000 ? 90  ILE B CG1 1 
ATOM   4252 C CG2 . ILE B 1 90  ? -0.91700  12.35100  22.08900 1.000 43.39000 ? 90  ILE B CG2 1 
ATOM   4253 C CD1 . ILE B 1 90  ? -2.22200  11.48100  24.75800 1.000 43.39000 ? 90  ILE B CD1 1 
ATOM   4254 N N   . VAL B 1 91  ? -3.90400  15.11300  20.95600 1.000 45.74000 ? 91  VAL B N   1 
ATOM   4255 C CA  . VAL B 1 91  ? -4.54100  15.31100  19.65600 1.000 45.74000 ? 91  VAL B CA  1 
ATOM   4256 C C   . VAL B 1 91  ? -4.42600  16.73600  19.13000 1.000 45.74000 ? 91  VAL B C   1 
ATOM   4257 O O   . VAL B 1 91  ? -4.78200  16.98400  17.96800 1.000 45.74000 ? 91  VAL B O   1 
ATOM   4258 C CB  . VAL B 1 91  ? -6.02600  14.90800  19.71600 1.000 45.74000 ? 91  VAL B CB  1 
ATOM   4259 C CG1 . VAL B 1 91  ? -6.17600  13.58800  20.45800 1.000 45.74000 ? 91  VAL B CG1 1 
ATOM   4260 C CG2 . VAL B 1 91  ? -6.85200  16.00700  20.36700 1.000 45.74000 ? 91  VAL B CG2 1 
ATOM   4261 N N   . ASN B 1 92  ? -3.95300  17.67800  19.93800 1.000 42.58000 ? 92  ASN B N   1 
ATOM   4262 C CA  . ASN B 1 92  ? -3.81900  19.04700  19.46500 1.000 42.58000 ? 92  ASN B CA  1 
ATOM   4263 C C   . ASN B 1 92  ? -2.66900  19.14600  18.46400 1.000 42.58000 ? 92  ASN B C   1 
ATOM   4264 O O   . ASN B 1 92  ? -1.62400  18.51600  18.65400 1.000 42.58000 ? 92  ASN B O   1 
ATOM   4265 C CB  . ASN B 1 92  ? -3.58400  20.00300  20.63500 1.000 42.58000 ? 92  ASN B CB  1 
ATOM   4266 C CG  . ASN B 1 92  ? -4.78600  20.10300  21.55800 1.000 42.58000 ? 92  ASN B CG  1 
ATOM   4267 O OD1 . ASN B 1 92  ? -5.92600  19.91000  21.13600 1.000 42.58000 ? 92  ASN B OD1 1 
ATOM   4268 N ND2 . ASN B 1 92  ? -4.53500  20.41200  22.82600 1.000 42.58000 ? 92  ASN B ND2 1 
ATOM   4269 N N   . PRO B 1 93  ? -2.82600  19.92900  17.38800 1.000 43.15000 ? 93  PRO B N   1 
ATOM   4270 C CA  . PRO B 1 93  ? -4.00900  20.71100  17.01100 1.000 43.15000 ? 93  PRO B CA  1 
ATOM   4271 C C   . PRO B 1 93  ? -4.97900  19.93000  16.12500 1.000 43.15000 ? 93  PRO B C   1 
ATOM   4272 O O   . PRO B 1 93  ? -4.59200  19.38900  15.09200 1.000 43.15000 ? 93  PRO B O   1 
ATOM   4273 C CB  . PRO B 1 93  ? -3.39100  21.90000  16.27100 1.000 43.15000 ? 93  PRO B CB  1 
ATOM   4274 C CG  . PRO B 1 93  ? -2.20300  21.28900  15.56000 1.000 43.15000 ? 93  PRO B CG  1 
ATOM   4275 C CD  . PRO B 1 93  ? -1.70000  20.17700  16.46800 1.000 43.15000 ? 93  PRO B CD  1 
ATOM   4276 N N   . VAL B 1 94  ? -6.25200  19.84100  16.51100 1.000 46.51000 ? 94  VAL B N   1 
ATOM   4277 C CA  . VAL B 1 94  ? -7.24500  19.21500  15.64900 1.000 46.51000 ? 94  VAL B CA  1 
ATOM   4278 C C   . VAL B 1 94  ? -7.55200  20.14300  14.48000 1.000 46.51000 ? 94  VAL B C   1 
ATOM   4279 O O   . VAL B 1 94  ? -7.44500  21.37000  14.58600 1.000 46.51000 ? 94  VAL B O   1 
ATOM   4280 C CB  . VAL B 1 94  ? -8.51800  18.87600  16.44500 1.000 46.51000 ? 94  VAL B CB  1 
ATOM   4281 C CG1 . VAL B 1 94  ? -9.34900  17.83500  15.70900 1.000 46.51000 ? 94  VAL B CG1 1 
ATOM   4282 C CG2 . VAL B 1 94  ? -8.15700  18.39500  17.84200 1.000 46.51000 ? 94  VAL B CG2 1 
ATOM   4283 N N   . GLU B 1 95  ? -7.92200  19.55900  13.34600 1.000 53.00000 ? 95  GLU B N   1 
ATOM   4284 C CA  . GLU B 1 95  ? -8.25000  20.32700  12.14600 1.000 53.00000 ? 95  GLU B CA  1 
ATOM   4285 C C   . GLU B 1 95  ? -9.76800  20.33800  11.98300 1.000 53.00000 ? 95  GLU B C   1 
ATOM   4286 O O   . GLU B 1 95  ? -10.35000 19.39600  11.43900 1.000 53.00000 ? 95  GLU B O   1 
ATOM   4287 C CB  . GLU B 1 95  ? -7.55900  19.73900  10.92000 1.000 53.00000 ? 95  GLU B CB  1 
ATOM   4288 C CG  . GLU B 1 95  ? -7.44400  20.70400  9.75200  1.000 53.00000 ? 95  GLU B CG  1 
ATOM   4289 C CD  . GLU B 1 95  ? -6.38500  21.76600  9.97600  1.000 53.00000 ? 95  GLU B CD  1 
ATOM   4290 O OE1 . GLU B 1 95  ? -5.42600  21.50100  10.73200 1.000 53.00000 ? 95  GLU B OE1 1 
ATOM   4291 O OE2 . GLU B 1 95  ? -6.51000  22.86500  9.39500  1.000 53.00000 ? 95  GLU B OE2 1 
ATOM   4292 N N   . PHE B 1 96  ? -10.41000 21.40500  12.45300 1.000 53.38000 ? 96  PHE B N   1 
ATOM   4293 C CA  . PHE B 1 96  ? -11.85800 21.52000  12.32900 1.000 53.38000 ? 96  PHE B CA  1 
ATOM   4294 C C   . PHE B 1 96  ? -12.23300 22.34000  11.09800 1.000 53.38000 ? 96  PHE B C   1 
ATOM   4295 O O   . PHE B 1 96  ? -11.55200 23.30600  10.75200 1.000 53.38000 ? 96  PHE B O   1 
ATOM   4296 C CB  . PHE B 1 96  ? -12.46600 22.15000  13.58400 1.000 53.38000 ? 96  PHE B CB  1 
ATOM   4297 C CG  . PHE B 1 96  ? -12.28800 21.32500  14.82800 1.000 53.38000 ? 96  PHE B CG  1 
ATOM   4298 C CD1 . PHE B 1 96  ? -12.95400 20.12000  14.97900 1.000 53.38000 ? 96  PHE B CD1 1 
ATOM   4299 C CD2 . PHE B 1 96  ? -11.46500 21.76300  15.85300 1.000 53.38000 ? 96  PHE B CD2 1 
ATOM   4300 C CE1 . PHE B 1 96  ? -12.79400 19.36200  16.12500 1.000 53.38000 ? 96  PHE B CE1 1 
ATOM   4301 C CE2 . PHE B 1 96  ? -11.30300 21.01100  17.00200 1.000 53.38000 ? 96  PHE B CE2 1 
ATOM   4302 C CZ  . PHE B 1 96  ? -11.96800 19.80900  17.13800 1.000 53.38000 ? 96  PHE B CZ  1 
ATOM   4303 N N   . ILE B 1 106 ? -11.37500 26.10000  7.66500  1.000 48.99000 ? 106 ILE B N   1 
ATOM   4304 C CA  . ILE B 1 106 ? -10.06700 25.64700  8.11900  1.000 48.99000 ? 106 ILE B CA  1 
ATOM   4305 C C   . ILE B 1 106 ? -9.72200  26.32800  9.43700  1.000 48.99000 ? 106 ILE B C   1 
ATOM   4306 O O   . ILE B 1 106 ? -9.44500  27.52700  9.47000  1.000 48.99000 ? 106 ILE B O   1 
ATOM   4307 C CB  . ILE B 1 106 ? -8.98000  25.92000  7.06500  1.000 48.99000 ? 106 ILE B CB  1 
ATOM   4308 C CG1 . ILE B 1 106 ? -9.56000  25.80900  5.65400  1.000 48.99000 ? 106 ILE B CG1 1 
ATOM   4309 C CG2 . ILE B 1 106 ? -7.82700  24.94400  7.22800  1.000 48.99000 ? 106 ILE B CG2 1 
ATOM   4310 C CD1 . ILE B 1 106 ? -8.55800  26.12100  4.56000  1.000 48.99000 ? 106 ILE B CD1 1 
ATOM   4311 N N   . PHE B 1 107 ? -9.73800  25.56300  10.52600 1.000 49.34000 ? 107 PHE B N   1 
ATOM   4312 C CA  . PHE B 1 107 ? -9.45200  26.10300  11.84700 1.000 49.34000 ? 107 PHE B CA  1 
ATOM   4313 C C   . PHE B 1 107 ? -8.63500  25.10000  12.64600 1.000 49.34000 ? 107 PHE B C   1 
ATOM   4314 O O   . PHE B 1 107 ? -8.88800  23.89300  12.58800 1.000 49.34000 ? 107 PHE B O   1 
ATOM   4315 C CB  . PHE B 1 107 ? -10.74300 26.44400  12.60300 1.000 49.34000 ? 107 PHE B CB  1 
ATOM   4316 C CG  . PHE B 1 107 ? -11.55600 27.53100  11.95900 1.000 49.34000 ? 107 PHE B CG  1 
ATOM   4317 C CD1 . PHE B 1 107 ? -12.51100 27.22700  11.00200 1.000 49.34000 ? 107 PHE B CD1 1 
ATOM   4318 C CD2 . PHE B 1 107 ? -11.36400 28.85700  12.31100 1.000 49.34000 ? 107 PHE B CD2 1 
ATOM   4319 C CE1 . PHE B 1 107 ? -13.25900 28.22600  10.40600 1.000 49.34000 ? 107 PHE B CE1 1 
ATOM   4320 C CE2 . PHE B 1 107 ? -12.11000 29.86100  11.72000 1.000 49.34000 ? 107 PHE B CE2 1 
ATOM   4321 C CZ  . PHE B 1 107 ? -13.05900 29.54500  10.76600 1.000 49.34000 ? 107 PHE B CZ  1 
ATOM   4322 N N   . ASP B 1 108 ? -7.65000  25.60500  13.38500 1.000 42.13000 ? 108 ASP B N   1 
ATOM   4323 C CA  . ASP B 1 108 ? -6.89400  24.78300  14.32000 1.000 42.13000 ? 108 ASP B CA  1 
ATOM   4324 C C   . ASP B 1 108 ? -7.55700  24.83500  15.68800 1.000 42.13000 ? 108 ASP B C   1 
ATOM   4325 O O   . ASP B 1 108 ? -7.79500  25.92000  16.23000 1.000 42.13000 ? 108 ASP B O   1 
ATOM   4326 C CB  . ASP B 1 108 ? -5.44200  25.24700  14.41900 1.000 42.13000 ? 108 ASP B CB  1 
ATOM   4327 C CG  . ASP B 1 108 ? -4.60000  24.77900  13.25400 1.000 42.13000 ? 108 ASP B CG  1 
ATOM   4328 O OD1 . ASP B 1 108 ? -5.18200  24.35300  12.23300 1.000 42.13000 ? 108 ASP B OD1 1 
ATOM   4329 O OD2 . ASP B 1 108 ? -3.35700  24.82400  13.36100 1.000 42.13000 ? 108 ASP B OD2 1 
ATOM   4330 N N   . GLY B 1 109 ? -7.84900  23.66500  16.23700 1.000 43.24000 ? 109 GLY B N   1 
ATOM   4331 C CA  . GLY B 1 109 ? -8.51300  23.53900  17.52200 1.000 43.24000 ? 109 GLY B CA  1 
ATOM   4332 C C   . GLY B 1 109 ? -7.56100  22.97700  18.56300 1.000 43.24000 ? 109 GLY B C   1 
ATOM   4333 O O   . GLY B 1 109 ? -6.75000  22.09500  18.26900 1.000 43.24000 ? 109 GLY B O   1 
ATOM   4334 N N   . ILE B 1 110 ? -7.67000  23.50600  19.77400 1.000 41.46000 ? 110 ILE B N   1 
ATOM   4335 C CA  . ILE B 1 110 ? -6.89000  23.07500  20.92300 1.000 41.46000 ? 110 ILE B CA  1 
ATOM   4336 C C   . ILE B 1 110 ? -7.87800  22.64800  21.99400 1.000 41.46000 ? 110 ILE B C   1 
ATOM   4337 O O   . ILE B 1 110 ? -8.74300  23.43700  22.39600 1.000 41.46000 ? 110 ILE B O   1 
ATOM   4338 C CB  . ILE B 1 110 ? -5.96600  24.18900  21.43600 1.000 41.46000 ? 110 ILE B CB  1 
ATOM   4339 C CG1 . ILE B 1 110 ? -5.00900  24.63700  20.32900 1.000 41.46000 ? 110 ILE B CG1 1 
ATOM   4340 C CG2 . ILE B 1 110 ? -5.20500  23.72600  22.66800 1.000 41.46000 ? 110 ILE B CG2 1 
ATOM   4341 C CD1 . ILE B 1 110 ? -4.34400  25.96900  20.60000 1.000 41.46000 ? 110 ILE B CD1 1 
ATOM   4342 N N   . ILE B 1 111 ? -7.76700  21.40000  22.43800 1.000 44.67000 ? 111 ILE B N   1 
ATOM   4343 C CA  . ILE B 1 111 ? -8.67400  20.82600  23.42100 1.000 44.67000 ? 111 ILE B CA  1 
ATOM   4344 C C   . ILE B 1 111 ? -7.88000  20.51400  24.68100 1.000 44.67000 ? 111 ILE B C   1 
ATOM   4345 O O   . ILE B 1 111 ? -6.81600  19.88700  24.61100 1.000 44.67000 ? 111 ILE B O   1 
ATOM   4346 C CB  . ILE B 1 111 ? -9.36700  19.56300  22.88100 1.000 44.67000 ? 111 ILE B CB  1 
ATOM   4347 C CG1 . ILE B 1 111 ? -9.78500  19.77000  21.42300 1.000 44.67000 ? 111 ILE B CG1 1 
ATOM   4348 C CG2 . ILE B 1 111 ? -10.57700 19.22300  23.72700 1.000 44.67000 ? 111 ILE B CG2 1 
ATOM   4349 C CD1 . ILE B 1 111 ? -10.41500 18.54900  20.78700 1.000 44.67000 ? 111 ILE B CD1 1 
ATOM   4350 N N   . HIS B 1 112 ? -8.40000  20.94700  25.82700 1.000 43.19000 ? 112 HIS B N   1 
ATOM   4351 C CA  . HIS B 1 112 ? -7.76300  20.66600  27.11200 1.000 43.19000 ? 112 HIS B CA  1 
ATOM   4352 C C   . HIS B 1 112 ? -8.80700  20.81200  28.20700 1.000 43.19000 ? 112 HIS B C   1 
ATOM   4353 O O   . HIS B 1 112 ? -9.45700  21.85600  28.30900 1.000 43.19000 ? 112 HIS B O   1 
ATOM   4354 C CB  . HIS B 1 112 ? -6.57400  21.60100  27.35400 1.000 43.19000 ? 112 HIS B CB  1 
ATOM   4355 C CG  . HIS B 1 112 ? -6.93200  23.05400  27.34100 1.000 43.19000 ? 112 HIS B CG  1 
ATOM   4356 N ND1 . HIS B 1 112 ? -7.33700  23.72900  28.47100 1.000 43.19000 ? 112 HIS B ND1 1 
ATOM   4357 C CD2 . HIS B 1 112 ? -6.94900  23.96000  26.33500 1.000 43.19000 ? 112 HIS B CD2 1 
ATOM   4358 C CE1 . HIS B 1 112 ? -7.58700  24.98900  28.16300 1.000 43.19000 ? 112 HIS B CE1 1 
ATOM   4359 N NE2 . HIS B 1 112 ? -7.35900  25.15500  26.87300 1.000 43.19000 ? 112 HIS B NE2 1 
ATOM   4360 N N   . ARG B 1 113 ? -8.98300  19.76200  29.00300 1.000 46.63000 ? 113 ARG B N   1 
ATOM   4361 C CA  . ARG B 1 113 ? -9.92200  19.80500  30.11400 1.000 46.63000 ? 113 ARG B CA  1 
ATOM   4362 C C   . ARG B 1 113 ? -9.43400  20.78400  31.17500 1.000 46.63000 ? 113 ARG B C   1 
ATOM   4363 O O   . ARG B 1 113 ? -8.24300  20.83700  31.49000 1.000 46.63000 ? 113 ARG B O   1 
ATOM   4364 C CB  . ARG B 1 113 ? -10.08800 18.40900  30.71000 1.000 46.63000 ? 113 ARG B CB  1 
ATOM   4365 C CG  . ARG B 1 113 ? -11.31200 18.22100  31.58500 1.000 46.63000 ? 113 ARG B CG  1 
ATOM   4366 C CD  . ARG B 1 113 ? -11.24700 16.87600  32.29300 1.000 46.63000 ? 113 ARG B CD  1 
ATOM   4367 N NE  . ARG B 1 113 ? -10.66800 15.84100  31.44300 1.000 46.63000 ? 113 ARG B NE  1 
ATOM   4368 C CZ  . ARG B 1 113 ? -11.37100 15.01300  30.68100 1.000 46.63000 ? 113 ARG B CZ  1 
ATOM   4369 N NH1 . ARG B 1 113 ? -12.69200 15.05800  30.64700 1.000 46.63000 ? 113 ARG B NH1 1 
ATOM   4370 N NH2 . ARG B 1 113 ? -10.73100 14.11800  29.93400 1.000 46.63000 ? 113 ARG B NH2 1 
ATOM   4371 N N   . SER B 1 114 ? -10.36000 21.56200  31.73000 1.000 48.06000 ? 114 SER B N   1 
ATOM   4372 C CA  . SER B 1 114 ? -10.01400 22.51000  32.78500 1.000 48.06000 ? 114 SER B CA  1 
ATOM   4373 C C   . SER B 1 114 ? -11.29100 22.97600  33.46700 1.000 48.06000 ? 114 SER B C   1 
ATOM   4374 O O   . SER B 1 114 ? -12.16300 23.55700  32.81300 1.000 48.06000 ? 114 SER B O   1 
ATOM   4375 C CB  . SER B 1 114 ? -9.23400  23.69700  32.21900 1.000 48.06000 ? 114 SER B CB  1 
ATOM   4376 O OG  . SER B 1 114 ? -10.04700 24.48000  31.36800 1.000 48.06000 ? 114 SER B OG  1 
ATOM   4377 N N   . ASN B 1 115 ? -11.38900 22.73900  34.77600 1.000 52.30000 ? 115 ASN B N   1 
ATOM   4378 C CA  . ASN B 1 115 ? -12.50300 23.20600  35.60100 1.000 52.30000 ? 115 ASN B CA  1 
ATOM   4379 C C   . ASN B 1 115 ? -13.84500 22.68000  35.08700 1.000 52.30000 ? 115 ASN B C   1 
ATOM   4380 O O   . ASN B 1 115 ? -14.74700 23.43600  34.72000 1.000 52.30000 ? 115 ASN B O   1 
ATOM   4381 C CB  . ASN B 1 115 ? -12.50400 24.73600  35.69600 1.000 52.30000 ? 115 ASN B CB  1 
ATOM   4382 C CG  . ASN B 1 115 ? -13.42300 25.25200  36.78900 1.000 52.30000 ? 115 ASN B CG  1 
ATOM   4383 O OD1 . ASN B 1 115 ? -14.49300 25.79500  36.51200 1.000 52.30000 ? 115 ASN B OD1 1 
ATOM   4384 N ND2 . ASN B 1 115 ? -13.01200 25.07600  38.04000 1.000 52.30000 ? 115 ASN B ND2 1 
ATOM   4385 N N   . GLY B 1 116 ? -13.96200 21.35500  35.07300 1.000 53.61000 ? 116 GLY B N   1 
ATOM   4386 C CA  . GLY B 1 116 ? -15.20000 20.71500  34.67200 1.000 53.61000 ? 116 GLY B CA  1 
ATOM   4387 C C   . GLY B 1 116 ? -15.40700 20.71700  33.17300 1.000 53.61000 ? 116 GLY B C   1 
ATOM   4388 O O   . GLY B 1 116 ? -15.20500 19.69500  32.51000 1.000 53.61000 ? 116 GLY B O   1 
ATOM   4389 N N   . VAL B 1 117 ? -15.82900 21.86100  32.63000 1.000 51.97000 ? 117 VAL B N   1 
ATOM   4390 C CA  . VAL B 1 117 ? -16.03300 21.98100  31.19300 1.000 51.97000 ? 117 VAL B CA  1 
ATOM   4391 C C   . VAL B 1 117 ? -14.70400 21.83500  30.46500 1.000 51.97000 ? 117 VAL B C   1 
ATOM   4392 O O   . VAL B 1 117 ? -13.68200 22.40500  30.87100 1.000 51.97000 ? 117 VAL B O   1 
ATOM   4393 C CB  . VAL B 1 117 ? -16.70000 23.32600  30.85800 1.000 51.97000 ? 117 VAL B CB  1 
ATOM   4394 C CG1 . VAL B 1 117 ? -18.14700 23.33000  31.31300 1.000 51.97000 ? 117 VAL B CG1 1 
ATOM   4395 C CG2 . VAL B 1 117 ? -15.94300 24.48200  31.50100 1.000 51.97000 ? 117 VAL B CG2 1 
ATOM   4396 N N   . VAL B 1 118 ? -14.70400 21.05200  29.38900 1.000 48.21000 ? 118 VAL B N   1 
ATOM   4397 C CA  . VAL B 1 118 ? -13.55700 21.02100  28.49300 1.000 48.21000 ? 118 VAL B CA  1 
ATOM   4398 C C   . VAL B 1 118 ? -13.53100 22.30300  27.66900 1.000 48.21000 ? 118 VAL B C   1 
ATOM   4399 O O   . VAL B 1 118 ? -14.58000 22.84700  27.29100 1.000 48.21000 ? 118 VAL B O   1 
ATOM   4400 C CB  . VAL B 1 118 ? -13.60600 19.77000  27.59800 1.000 48.21000 ? 118 VAL B CB  1 
ATOM   4401 C CG1 . VAL B 1 118 ? -12.31500 19.62700  26.81300 1.000 48.21000 ? 118 VAL B CG1 1 
ATOM   4402 C CG2 . VAL B 1 118 ? -13.85200 18.53400  28.44600 1.000 48.21000 ? 118 VAL B CG2 1 
ATOM   4403 N N   . ILE B 1 119 ? -12.32800 22.79600  27.38400 1.000 44.33000 ? 119 ILE B N   1 
ATOM   4404 C CA  . ILE B 1 119 ? -12.14000 24.00900  26.59700 1.000 44.33000 ? 119 ILE B CA  1 
ATOM   4405 C C   . ILE B 1 119 ? -11.77100 23.62100  25.17400 1.000 44.33000 ? 119 ILE B C   1 
ATOM   4406 O O   . ILE B 1 119 ? -10.86800 22.80200  24.95900 1.000 44.33000 ? 119 ILE B O   1 
ATOM   4407 C CB  . ILE B 1 119 ? -11.06000 24.91400  27.21600 1.000 44.33000 ? 119 ILE B CB  1 
ATOM   4408 C CG1 . ILE B 1 119 ? -11.45000 25.30300  28.64000 1.000 44.33000 ? 119 ILE B CG1 1 
ATOM   4409 C CG2 . ILE B 1 119 ? -10.85800 26.16100  26.36900 1.000 44.33000 ? 119 ILE B CG2 1 
ATOM   4410 C CD1 . ILE B 1 119 ? -12.74400 26.06100  28.71700 1.000 44.33000 ? 119 ILE B CD1 1 
ATOM   4411 N N   . LEU B 1 120 ? -12.46200 24.21100  24.20100 1.000 46.43000 ? 120 LEU B N   1 
ATOM   4412 C CA  . LEU B 1 120 ? -12.11700 24.08200  22.78900 1.000 46.43000 ? 120 LEU B CA  1 
ATOM   4413 C C   . LEU B 1 120 ? -11.79100 25.47400  22.27000 1.000 46.43000 ? 120 LEU B C   1 
ATOM   4414 O O   . LEU B 1 120 ? -12.67100 26.33900  22.20100 1.000 46.43000 ? 120 LEU B O   1 
ATOM   4415 C CB  . LEU B 1 120 ? -13.25500 23.44700  21.99100 1.000 46.43000 ? 120 LEU B CB  1 
ATOM   4416 C CG  . LEU B 1 120 ? -13.03500 23.38100  20.47700 1.000 46.43000 ? 120 LEU B CG  1 
ATOM   4417 C CD1 . LEU B 1 120 ? -11.73800 22.65500  20.15500 1.000 46.43000 ? 120 LEU B CD1 1 
ATOM   4418 C CD2 . LEU B 1 120 ? -14.21300 22.71300  19.78400 1.000 46.43000 ? 120 LEU B CD2 1 
ATOM   4419 N N   . GLU B 1 121 ? -10.52700 25.70100  21.93500 1.000 42.32000 ? 121 GLU B N   1 
ATOM   4420 C CA  . GLU B 1 121 ? -10.08000 26.97700  21.39900 1.000 42.32000 ? 121 GLU B CA  1 
ATOM   4421 C C   . GLU B 1 121 ? -9.85300  26.82900  19.90300 1.000 42.32000 ? 121 GLU B C   1 
ATOM   4422 O O   . GLU B 1 121 ? -9.17800  25.89500  19.46700 1.000 42.32000 ? 121 GLU B O   1 
ATOM   4423 C CB  . GLU B 1 121 ? -8.80400  27.44100  22.10000 1.000 42.32000 ? 121 GLU B CB  1 
ATOM   4424 C CG  . GLU B 1 121 ? -8.72600  26.99200  23.55100 1.000 42.32000 ? 121 GLU B CG  1 
ATOM   4425 C CD  . GLU B 1 121 ? -7.75500  27.81100  24.37000 1.000 42.32000 ? 121 GLU B CD  1 
ATOM   4426 O OE1 . GLU B 1 121 ? -7.92100  29.04800  24.42500 1.000 42.32000 ? 121 GLU B OE1 1 
ATOM   4427 O OE2 . GLU B 1 121 ? -6.82600  27.21700  24.95600 1.000 42.32000 ? 121 GLU B OE2 1 
ATOM   4428 N N   . LEU B 1 122 ? -10.41500 27.74200  19.12200 1.000 40.77000 ? 122 LEU B N   1 
ATOM   4429 C CA  . LEU B 1 122 ? -10.30900 27.70300  17.67200 1.000 40.77000 ? 122 LEU B CA  1 
ATOM   4430 C C   . LEU B 1 122 ? -9.55500  28.93000  17.19000 1.000 40.77000 ? 122 LEU B C   1 
ATOM   4431 O O   . LEU B 1 122 ? -9.84200  30.04900  17.62200 1.000 40.77000 ? 122 LEU B O   1 
ATOM   4432 C CB  . LEU B 1 122 ? -11.69300 27.63400  17.02400 1.000 40.77000 ? 122 LEU B CB  1 
ATOM   4433 C CG  . LEU B 1 122 ? -12.39000 26.27900  17.14000 1.000 40.77000 ? 122 LEU B CG  1 
ATOM   4434 C CD1 . LEU B 1 122 ? -13.87300 26.41300  16.84500 1.000 40.77000 ? 122 LEU B CD1 1 
ATOM   4435 C CD2 . LEU B 1 122 ? -11.74400 25.27600  16.19700 1.000 40.77000 ? 122 LEU B CD2 1 
ATOM   4436 N N   . GLU B 1 123 ? -8.60000  28.71400  16.29500 1.000 40.48000 ? 123 GLU B N   1 
ATOM   4437 C CA  . GLU B 1 123 ? -7.83100  29.78900  15.69600 1.000 40.48000 ? 123 GLU B CA  1 
ATOM   4438 C C   . GLU B 1 123 ? -7.81700  29.61200  14.18700 1.000 40.48000 ? 123 GLU B C   1 
ATOM   4439 O O   . GLU B 1 123 ? -7.92200  28.48300  13.69100 1.000 40.48000 ? 123 GLU B O   1 
ATOM   4440 C CB  . GLU B 1 123 ? -6.38800  29.80800  16.22800 1.000 40.48000 ? 123 GLU B CB  1 
ATOM   4441 C CG  . GLU B 1 123 ? -6.24300  30.38200  17.62700 1.000 40.48000 ? 123 GLU B CG  1 
ATOM   4442 C CD  . GLU B 1 123 ? -4.83000  30.24900  18.16400 1.000 40.48000 ? 123 GLU B CD  1 
ATOM   4443 O OE1 . GLU B 1 123 ? -4.24300  29.15500  18.02600 1.000 40.48000 ? 123 GLU B OE1 1 
ATOM   4444 O OE2 . GLU B 1 123 ? -4.30700  31.23900  18.72000 1.000 40.48000 ? 123 GLU B OE2 1 
ATOM   4445 N N   . PRO B 1 124 ? -7.70900  30.70300  13.43000 1.000 40.67000 ? 124 PRO B N   1 
ATOM   4446 C CA  . PRO B 1 124 ? -7.58700  30.56500  11.97700 1.000 40.67000 ? 124 PRO B CA  1 
ATOM   4447 C C   . PRO B 1 124 ? -6.33300  29.78500  11.61800 1.000 40.67000 ? 124 PRO B C   1 
ATOM   4448 O O   . PRO B 1 124 ? -5.29100  29.92100  12.25900 1.000 40.67000 ? 124 PRO B O   1 
ATOM   4449 C CB  . PRO B 1 124 ? -7.52000  32.01800  11.48300 1.000 40.67000 ? 124 PRO B CB  1 
ATOM   4450 C CG  . PRO B 1 124 ? -7.10800  32.81600  12.68400 1.000 40.67000 ? 124 PRO B CG  1 
ATOM   4451 C CD  . PRO B 1 124 ? -7.71900  32.11300  13.85600 1.000 40.67000 ? 124 PRO B CD  1 
ATOM   4452 N N   . ALA B 1 125 ? -6.44300  28.96100  10.58100 1.000 39.97000 ? 125 ALA B N   1 
ATOM   4453 C CA  . ALA B 1 125 ? -5.37000  28.06200  10.18200 1.000 39.97000 ? 125 ALA B CA  1 
ATOM   4454 C C   . ALA B 1 125 ? -4.55600  28.70200  9.06500  1.000 39.97000 ? 125 ALA B C   1 
ATOM   4455 O O   . ALA B 1 125 ? -5.07600  28.94100  7.96900  1.000 39.97000 ? 125 ALA B O   1 
ATOM   4456 C CB  . ALA B 1 125 ? -5.92900  26.71200  9.73600  1.000 39.97000 ? 125 ALA B CB  1 
ATOM   4457 N N   . ILE B 1 126 ? -3.28400  28.97300  9.34200  1.000 37.50000 ? 126 ILE B N   1 
ATOM   4458 C CA  . ILE B 1 126 ? -2.37700  29.50300  8.33500  1.000 37.50000 ? 126 ILE B CA  1 
ATOM   4459 C C   . ILE B 1 126 ? -2.11000  28.43900  7.27800  1.000 37.50000 ? 126 ILE B C   1 
ATOM   4460 O O   . ILE B 1 126 ? -2.19200  27.24200  7.55700  1.000 37.50000 ? 126 ILE B O   1 
ATOM   4461 C CB  . ILE B 1 126 ? -1.06000  29.99500  8.96500  1.000 37.50000 ? 126 ILE B CB  1 
ATOM   4462 C CG1 . ILE B 1 126 ? -1.27200  31.33800  9.67000  1.000 37.50000 ? 126 ILE B CG1 1 
ATOM   4463 C CG2 . ILE B 1 126 ? 0.03500   30.09300  7.91100  1.000 37.50000 ? 126 ILE B CG2 1 
ATOM   4464 C CD1 . ILE B 1 126 ? -0.00400  31.93500  10.25300 1.000 37.50000 ? 126 ILE B CD1 1 
ATOM   4465 N N   . ASN B 1 132 ? 6.23000   21.97000  1.93200  1.000 66.83000 ? 132 ASN B N   1 
ATOM   4466 C CA  . ASN B 1 132 ? 6.18900   23.23500  2.65600  1.000 66.83000 ? 132 ASN B CA  1 
ATOM   4467 C C   . ASN B 1 132 ? 6.59100   23.04300  4.11600  1.000 66.83000 ? 132 ASN B C   1 
ATOM   4468 O O   . ASN B 1 132 ? 6.24800   22.03400  4.73400  1.000 66.83000 ? 132 ASN B O   1 
ATOM   4469 C CB  . ASN B 1 132 ? 4.79400   23.85800  2.56600  1.000 66.83000 ? 132 ASN B CB  1 
ATOM   4470 C CG  . ASN B 1 132 ? 3.71500   22.95400  3.13000  1.000 66.83000 ? 132 ASN B CG  1 
ATOM   4471 O OD1 . ASN B 1 132 ? 3.25000   22.03100  2.46100  1.000 66.83000 ? 132 ASN B OD1 1 
ATOM   4472 N ND2 . ASN B 1 132 ? 3.30900   23.21800  4.36600  1.000 66.83000 ? 132 ASN B ND2 1 
ATOM   4473 N N   . TYR B 1 133 ? 7.32300   24.02100  4.65300  1.000 65.23000 ? 133 TYR B N   1 
ATOM   4474 C CA  . TYR B 1 133 ? 7.80700   23.99900  6.03500  1.000 65.23000 ? 133 TYR B CA  1 
ATOM   4475 C C   . TYR B 1 133 ? 8.65100   22.76100  6.33300  1.000 65.23000 ? 133 TYR B C   1 
ATOM   4476 O O   . TYR B 1 133 ? 8.65000   22.25300  7.45700  1.000 65.23000 ? 133 TYR B O   1 
ATOM   4477 C CB  . TYR B 1 133 ? 6.64700   24.10600  7.03300  1.000 65.23000 ? 133 TYR B CB  1 
ATOM   4478 C CG  . TYR B 1 133 ? 6.11600   25.51200  7.21700  1.000 65.23000 ? 133 TYR B CG  1 
ATOM   4479 C CD1 . TYR B 1 133 ? 5.19700   26.05300  6.32600  1.000 65.23000 ? 133 TYR B CD1 1 
ATOM   4480 C CD2 . TYR B 1 133 ? 6.53100   26.29700  8.28700  1.000 65.23000 ? 133 TYR B CD2 1 
ATOM   4481 C CE1 . TYR B 1 133 ? 4.71000   27.33700  6.49300  1.000 65.23000 ? 133 TYR B CE1 1 
ATOM   4482 C CE2 . TYR B 1 133 ? 6.05000   27.58100  8.46300  1.000 65.23000 ? 133 TYR B CE2 1 
ATOM   4483 C CZ  . TYR B 1 133 ? 5.14000   28.09600  7.56400  1.000 65.23000 ? 133 TYR B CZ  1 
ATOM   4484 O OH  . TYR B 1 133 ? 4.65900   29.37400  7.73700  1.000 65.23000 ? 133 TYR B OH  1 
ATOM   4485 N N   . PHE B 1 134 ? 9.37600   22.25800  5.32900  1.000 63.94000 ? 134 PHE B N   1 
ATOM   4486 C CA  . PHE B 1 134 ? 10.32900  21.17800  5.56900  1.000 63.94000 ? 134 PHE B CA  1 
ATOM   4487 C C   . PHE B 1 134 ? 11.63200  21.70800  6.15600  1.000 63.94000 ? 134 PHE B C   1 
ATOM   4488 O O   . PHE B 1 134 ? 12.19100  21.11100  7.08900  1.000 63.94000 ? 134 PHE B O   1 
ATOM   4489 C CB  . PHE B 1 134 ? 10.59600  20.41900  4.26800  1.000 63.94000 ? 134 PHE B CB  1 
ATOM   4490 C CG  . PHE B 1 134 ? 11.82000  19.55000  4.31200  1.000 63.94000 ? 134 PHE B CG  1 
ATOM   4491 C CD1 . PHE B 1 134 ? 11.81500  18.35700  5.01500  1.000 63.94000 ? 134 PHE B CD1 1 
ATOM   4492 C CD2 . PHE B 1 134 ? 12.97500  19.92400  3.64200  1.000 63.94000 ? 134 PHE B CD2 1 
ATOM   4493 C CE1 . PHE B 1 134 ? 12.94100  17.55500  5.05600  1.000 63.94000 ? 134 PHE B CE1 1 
ATOM   4494 C CE2 . PHE B 1 134 ? 14.10300  19.12600  3.67800  1.000 63.94000 ? 134 PHE B CE2 1 
ATOM   4495 C CZ  . PHE B 1 134 ? 14.08600  17.94000  4.38600  1.000 63.94000 ? 134 PHE B CZ  1 
ATOM   4496 N N   . ARG B 1 135 ? 12.11200  22.84200  5.63400  1.000 59.53000 ? 135 ARG B N   1 
ATOM   4497 C CA  . ARG B 1 135 ? 13.29000  23.47900  6.20800  1.000 59.53000 ? 135 ARG B CA  1 
ATOM   4498 C C   . ARG B 1 135 ? 13.05200  23.84500  7.66100  1.000 59.53000 ? 135 ARG B C   1 
ATOM   4499 O O   . ARG B 1 135 ? 13.97800  23.78600  8.47500  1.000 59.53000 ? 135 ARG B O   1 
ATOM   4500 C CB  . ARG B 1 135 ? 13.65500  24.73400  5.41200  1.000 59.53000 ? 135 ARG B CB  1 
ATOM   4501 C CG  . ARG B 1 135 ? 13.83400  24.51800  3.92100  1.000 59.53000 ? 135 ARG B CG  1 
ATOM   4502 C CD  . ARG B 1 135 ? 15.29700  24.60700  3.52500  1.000 59.53000 ? 135 ARG B CD  1 
ATOM   4503 N NE  . ARG B 1 135 ? 16.10500  23.61000  4.21600  1.000 59.53000 ? 135 ARG B NE  1 
ATOM   4504 C CZ  . ARG B 1 135 ? 16.22500  22.34800  3.82900  1.000 59.53000 ? 135 ARG B CZ  1 
ATOM   4505 N NH1 . ARG B 1 135 ? 15.59600  21.89100  2.75800  1.000 59.53000 ? 135 ARG B NH1 1 
ATOM   4506 N NH2 . ARG B 1 135 ? 16.99200  21.52200  4.53500  1.000 59.53000 ? 135 ARG B NH2 1 
ATOM   4507 N N   . PHE B 1 136 ? 11.80900  24.18400  8.00800  1.000 50.80000 ? 136 PHE B N   1 
ATOM   4508 C CA  . PHE B 1 136 ? 11.48900  24.59000  9.37100  1.000 50.80000 ? 136 PHE B CA  1 
ATOM   4509 C C   . PHE B 1 136 ? 11.72400  23.45100  10.35800 1.000 50.80000 ? 136 PHE B C   1 
ATOM   4510 O O   . PHE B 1 136 ? 12.46000  23.60800  11.33800 1.000 50.80000 ? 136 PHE B O   1 
ATOM   4511 C CB  . PHE B 1 136 ? 10.04100  25.08300  9.42000  1.000 50.80000 ? 136 PHE B CB  1 
ATOM   4512 C CG  . PHE B 1 136 ? 9.41000   25.01000  10.77700 1.000 50.80000 ? 136 PHE B CG  1 
ATOM   4513 C CD1 . PHE B 1 136 ? 9.68900   25.96600  11.73800 1.000 50.80000 ? 136 PHE B CD1 1 
ATOM   4514 C CD2 . PHE B 1 136 ? 8.51500   23.99900  11.08300 1.000 50.80000 ? 136 PHE B CD2 1 
ATOM   4515 C CE1 . PHE B 1 136 ? 9.10000   25.90200  12.98400 1.000 50.80000 ? 136 PHE B CE1 1 
ATOM   4516 C CE2 . PHE B 1 136 ? 7.92300   23.93200  12.32600 1.000 50.80000 ? 136 PHE B CE2 1 
ATOM   4517 C CZ  . PHE B 1 136 ? 8.21800   24.88300  13.27800 1.000 50.80000 ? 136 PHE B CZ  1 
ATOM   4518 N N   . TYR B 1 137 ? 11.12900  22.28200  10.10000 1.000 49.15000 ? 137 TYR B N   1 
ATOM   4519 C CA  . TYR B 1 137 ? 11.34500  21.13800  10.98300 1.000 49.15000 ? 137 TYR B CA  1 
ATOM   4520 C C   . TYR B 1 137 ? 12.78400  20.63500  10.92700 1.000 49.15000 ? 137 TYR B C   1 
ATOM   4521 O O   . TYR B 1 137 ? 13.31200  20.15000  11.94100 1.000 49.15000 ? 137 TYR B O   1 
ATOM   4522 C CB  . TYR B 1 137 ? 10.36900  20.01600  10.63200 1.000 49.15000 ? 137 TYR B CB  1 
ATOM   4523 C CG  . TYR B 1 137 ? 9.00700   20.17300  11.27400 1.000 49.15000 ? 137 TYR B CG  1 
ATOM   4524 C CD1 . TYR B 1 137 ? 8.88600   20.55600  12.60400 1.000 49.15000 ? 137 TYR B CD1 1 
ATOM   4525 C CD2 . TYR B 1 137 ? 7.84400   19.94500  10.55000 1.000 49.15000 ? 137 TYR B CD2 1 
ATOM   4526 C CE1 . TYR B 1 137 ? 7.64400   20.70000  13.19800 1.000 49.15000 ? 137 TYR B CE1 1 
ATOM   4527 C CE2 . TYR B 1 137 ? 6.59700   20.08900  11.13500 1.000 49.15000 ? 137 TYR B CE2 1 
ATOM   4528 C CZ  . TYR B 1 137 ? 6.50400   20.46800  12.45800 1.000 49.15000 ? 137 TYR B CZ  1 
ATOM   4529 O OH  . TYR B 1 137 ? 5.26700   20.61200  13.04400 1.000 49.15000 ? 137 TYR B OH  1 
ATOM   4530 N N   . HIS B 1 138 ? 13.44300  20.75400  9.76900  1.000 49.34000 ? 138 HIS B N   1 
ATOM   4531 C CA  . HIS B 1 138 ? 14.83100  20.31000  9.68800  1.000 49.34000 ? 138 HIS B CA  1 
ATOM   4532 C C   . HIS B 1 138 ? 15.73500  21.16600  10.57100 1.000 49.34000 ? 138 HIS B C   1 
ATOM   4533 O O   . HIS B 1 138 ? 16.56100  20.64100  11.32800 1.000 49.34000 ? 138 HIS B O   1 
ATOM   4534 C CB  . HIS B 1 138 ? 15.31200  20.33000  8.23900  1.000 49.34000 ? 138 HIS B CB  1 
ATOM   4535 C CG  . HIS B 1 138 ? 16.70700  19.81500  8.06600  1.000 49.34000 ? 138 HIS B CG  1 
ATOM   4536 N ND1 . HIS B 1 138 ? 17.71600  20.57100  7.51000  1.000 49.34000 ? 138 HIS B ND1 1 
ATOM   4537 C CD2 . HIS B 1 138 ? 17.26400  18.62300  8.38700  1.000 49.34000 ? 138 HIS B CD2 1 
ATOM   4538 C CE1 . HIS B 1 138 ? 18.83200  19.86400  7.48800  1.000 49.34000 ? 138 HIS B CE1 1 
ATOM   4539 N NE2 . HIS B 1 138 ? 18.58500  18.67900  8.01600  1.000 49.34000 ? 138 HIS B NE2 1 
ATOM   4540 N N   . LEU B 1 139 ? 15.57900  22.49100  10.51500 1.000 45.61000 ? 139 LEU B N   1 
ATOM   4541 C CA  . LEU B 1 139 ? 16.35900  23.33100  11.41500 1.000 45.61000 ? 139 LEU B CA  1 
ATOM   4542 C C   . LEU B 1 139 ? 15.86100  23.24700  12.85300 1.000 45.61000 ? 139 LEU B C   1 
ATOM   4543 O O   . LEU B 1 139 ? 16.62300  23.55800  13.76900 1.000 45.61000 ? 139 LEU B O   1 
ATOM   4544 C CB  . LEU B 1 139 ? 16.39000  24.78500  10.92200 1.000 45.61000 ? 139 LEU B CB  1 
ATOM   4545 C CG  . LEU B 1 139 ? 15.13000  25.58500  10.58600 1.000 45.61000 ? 139 LEU B CG  1 
ATOM   4546 C CD1 . LEU B 1 139 ? 14.49500  26.17000  11.82100 1.000 45.61000 ? 139 LEU B CD1 1 
ATOM   4547 C CD2 . LEU B 1 139 ? 15.44400  26.68100  9.57300  1.000 45.61000 ? 139 LEU B CD2 1 
ATOM   4548 N N   . VAL B 1 140 ? 14.62400  22.79500  13.08100 1.000 41.22000 ? 140 VAL B N   1 
ATOM   4549 C CA  . VAL B 1 140 ? 14.18200  22.52100  14.44900 1.000 41.22000 ? 140 VAL B CA  1 
ATOM   4550 C C   . VAL B 1 140 ? 14.99800  21.38400  15.05200 1.000 41.22000 ? 140 VAL B C   1 
ATOM   4551 O O   . VAL B 1 140 ? 15.54100  21.49900  16.16100 1.000 41.22000 ? 140 VAL B O   1 
ATOM   4552 C CB  . VAL B 1 140 ? 12.67400  22.20500  14.47700 1.000 41.22000 ? 140 VAL B CB  1 
ATOM   4553 C CG1 . VAL B 1 140 ? 12.31500  21.41400  15.72800 1.000 41.22000 ? 140 VAL B CG1 1 
ATOM   4554 C CG2 . VAL B 1 140 ? 11.85900  23.48500  14.41700 1.000 41.22000 ? 140 VAL B CG2 1 
ATOM   4555 N N   . LYS B 1 141 ? 15.09900  20.26300  14.33100 1.000 37.38000 ? 141 LYS B N   1 
ATOM   4556 C CA  . LYS B 1 141 ? 15.91600  19.16900  14.85200 1.000 37.38000 ? 141 LYS B CA  1 
ATOM   4557 C C   . LYS B 1 141 ? 17.39200  19.55300  14.90500 1.000 37.38000 ? 141 LYS B C   1 
ATOM   4558 O O   . LYS B 1 141 ? 18.11200  19.13200  15.82400 1.000 37.38000 ? 141 LYS B O   1 
ATOM   4559 C CB  . LYS B 1 141 ? 15.70800  17.88900  14.03300 1.000 37.38000 ? 141 LYS B CB  1 
ATOM   4560 C CG  . LYS B 1 141 ? 16.25600  17.91600  12.62100 1.000 37.38000 ? 141 LYS B CG  1 
ATOM   4561 C CD  . LYS B 1 141 ? 16.45100  16.50900  12.07200 1.000 37.38000 ? 141 LYS B CD  1 
ATOM   4562 C CE  . LYS B 1 141 ? 15.15400  15.71900  12.07600 1.000 37.38000 ? 141 LYS B CE  1 
ATOM   4563 N NZ  . LYS B 1 141 ? 15.35100  14.34000  11.54900 1.000 37.38000 ? 141 LYS B NZ  1 
ATOM   4564 N N   . LEU B 1 142 ? 17.85400  20.38000  13.96100 1.000 37.14000 ? 142 LEU B N   1 
ATOM   4565 C CA  . LEU B 1 142 ? 19.22600  20.87200  14.03600 1.000 37.14000 ? 142 LEU B CA  1 
ATOM   4566 C C   . LEU B 1 142 ? 19.44100  21.72100  15.28300 1.000 37.14000 ? 142 LEU B C   1 
ATOM   4567 O O   . LEU B 1 142 ? 20.50100  21.65200  15.91400 1.000 37.14000 ? 142 LEU B O   1 
ATOM   4568 C CB  . LEU B 1 142 ? 19.56500  21.67200  12.77800 1.000 37.14000 ? 142 LEU B CB  1 
ATOM   4569 C CG  . LEU B 1 142 ? 19.95500  20.88100  11.52900 1.000 37.14000 ? 142 LEU B CG  1 
ATOM   4570 C CD1 . LEU B 1 142 ? 19.80400  21.74000  10.28500 1.000 37.14000 ? 142 LEU B CD1 1 
ATOM   4571 C CD2 . LEU B 1 142 ? 21.38300  20.36800  11.64900 1.000 37.14000 ? 142 LEU B CD2 1 
ATOM   4572 N N   . ALA B 1 143 ? 18.43700  22.51200  15.66700 1.000 33.46000 ? 143 ALA B N   1 
ATOM   4573 C CA  . ALA B 1 143 ? 18.54100  23.32100  16.87500 1.000 33.46000 ? 143 ALA B CA  1 
ATOM   4574 C C   . ALA B 1 143 ? 18.53800  22.45300  18.12300 1.000 33.46000 ? 143 ALA B C   1 
ATOM   4575 O O   . ALA B 1 143 ? 19.23300  22.75700  19.09800 1.000 33.46000 ? 143 ALA B O   1 
ATOM   4576 C CB  . ALA B 1 143 ? 17.39700  24.33300  16.92500 1.000 33.46000 ? 143 ALA B CB  1 
ATOM   4577 N N   . ILE B 1 144 ? 17.76100  21.36900  18.11100 1.000 29.41000 ? 144 ILE B N   1 
ATOM   4578 C CA  . ILE B 1 144 ? 17.78100  20.44600  19.24500 1.000 29.41000 ? 144 ILE B CA  1 
ATOM   4579 C C   . ILE B 1 144 ? 19.16200  19.81900  19.38500 1.000 29.41000 ? 144 ILE B C   1 
ATOM   4580 O O   . ILE B 1 144 ? 19.69700  19.68000  20.49700 1.000 29.41000 ? 144 ILE B O   1 
ATOM   4581 C CB  . ILE B 1 144 ? 16.68800  19.37500  19.07900 1.000 29.41000 ? 144 ILE B CB  1 
ATOM   4582 C CG1 . ILE B 1 144 ? 15.31800  20.03500  18.93500 1.000 29.41000 ? 144 ILE B CG1 1 
ATOM   4583 C CG2 . ILE B 1 144 ? 16.69400  18.42300  20.25900 1.000 29.41000 ? 144 ILE B CG2 1 
ATOM   4584 C CD1 . ILE B 1 144 ? 14.31500  19.18400  18.20400 1.000 29.41000 ? 144 ILE B CD1 1 
ATOM   4585 N N   . GLY B 1 145 ? 19.78600  19.48500  18.25500 1.000 29.86000 ? 145 GLY B N   1 
ATOM   4586 C CA  . GLY B 1 145 ? 21.12800  18.93300  18.31200 1.000 29.86000 ? 145 GLY B CA  1 
ATOM   4587 C C   . GLY B 1 145 ? 22.15600  19.95500  18.75700 1.000 29.86000 ? 145 GLY B C   1 
ATOM   4588 O O   . GLY B 1 145 ? 23.09800  19.62500  19.48500 1.000 29.86000 ? 145 GLY B O   1 
ATOM   4589 N N   . LYS B 1 146 ? 21.99300  21.20900  18.33000 1.000 28.55000 ? 146 LYS B N   1 
ATOM   4590 C CA  . LYS B 1 146 ? 22.89100  22.26400  18.78800 1.000 28.55000 ? 146 LYS B CA  1 
ATOM   4591 C C   . LYS B 1 146 ? 22.74700  22.49700  20.28500 1.000 28.55000 ? 146 LYS B C   1 
ATOM   4592 O O   . LYS B 1 146 ? 23.73400  22.78600  20.97100 1.000 28.55000 ? 146 LYS B O   1 
ATOM   4593 C CB  . LYS B 1 146 ? 22.61700  23.55700  18.02100 1.000 28.55000 ? 146 LYS B CB  1 
ATOM   4594 C CG  . LYS B 1 146 ? 22.92100  23.49400  16.53500 1.000 28.55000 ? 146 LYS B CG  1 
ATOM   4595 C CD  . LYS B 1 146 ? 22.38800  24.72700  15.82500 1.000 28.55000 ? 146 LYS B CD  1 
ATOM   4596 C CE  . LYS B 1 146 ? 22.57400  24.62200  14.32300 1.000 28.55000 ? 146 LYS B CE  1 
ATOM   4597 N NZ  . LYS B 1 146 ? 22.06200  25.82700  13.61900 1.000 28.55000 ? 146 LYS B NZ  1 
ATOM   4598 N N   . LEU B 1 147 ? 21.52600  22.37200  20.80900 1.000 26.41000 ? 147 LEU B N   1 
ATOM   4599 C CA  . LEU B 1 147 ? 21.33000  22.48800  22.25000 1.000 26.41000 ? 147 LEU B CA  1 
ATOM   4600 C C   . LEU B 1 147 ? 21.98600  21.32900  22.98300 1.000 26.41000 ? 147 LEU B C   1 
ATOM   4601 O O   . LEU B 1 147 ? 22.54000  21.51100  24.07400 1.000 26.41000 ? 147 LEU B O   1 
ATOM   4602 C CB  . LEU B 1 147 ? 19.83900  22.54500  22.58100 1.000 26.41000 ? 147 LEU B CB  1 
ATOM   4603 C CG  . LEU B 1 147 ? 19.08700  23.83200  22.24800 1.000 26.41000 ? 147 LEU B CG  1 
ATOM   4604 C CD1 . LEU B 1 147 ? 17.59300  23.62800  22.43300 1.000 26.41000 ? 147 LEU B CD1 1 
ATOM   4605 C CD2 . LEU B 1 147 ? 19.58800  24.98600  23.10700 1.000 26.41000 ? 147 LEU B CD2 1 
ATOM   4606 N N   . GLN B 1 148 ? 21.94100  20.13100  22.39500 1.000 28.43000 ? 148 GLN B N   1 
ATOM   4607 C CA  . GLN B 1 148 ? 22.56000  18.97100  23.02400 1.000 28.43000 ? 148 GLN B CA  1 
ATOM   4608 C C   . GLN B 1 148 ? 24.08100  18.96900  22.91300 1.000 28.43000 ? 148 GLN B C   1 
ATOM   4609 O O   . GLN B 1 148 ? 24.74000  18.24700  23.67000 1.000 28.43000 ? 148 GLN B O   1 
ATOM   4610 C CB  . GLN B 1 148 ? 21.98400  17.69300  22.41600 1.000 28.43000 ? 148 GLN B CB  1 
ATOM   4611 C CG  . GLN B 1 148 ? 20.52400  17.47000  22.78000 1.000 28.43000 ? 148 GLN B CG  1 
ATOM   4612 C CD  . GLN B 1 148 ? 19.82700  16.50300  21.85000 1.000 28.43000 ? 148 GLN B CD  1 
ATOM   4613 O OE1 . GLN B 1 148 ? 19.69300  16.76300  20.65500 1.000 28.43000 ? 148 GLN B OE1 1 
ATOM   4614 N NE2 . GLN B 1 148 ? 19.37700  15.37800  22.39400 1.000 28.43000 ? 148 GLN B NE2 1 
ATOM   4615 N N   . SER B 1 149 ? 24.65000  19.75600  21.99700 1.000 29.05000 ? 149 SER B N   1 
ATOM   4616 C CA  . SER B 1 149 ? 26.09700  19.84200  21.83200 1.000 29.05000 ? 149 SER B CA  1 
ATOM   4617 C C   . SER B 1 149 ? 26.75800  20.81900  22.79900 1.000 29.05000 ? 149 SER B C   1 
ATOM   4618 O O   . SER B 1 149 ? 27.99100  20.87500  22.85000 1.000 29.05000 ? 149 SER B O   1 
ATOM   4619 C CB  . SER B 1 149 ? 26.43600  20.23800  20.39100 1.000 29.05000 ? 149 SER B CB  1 
ATOM   4620 O OG  . SER B 1 149 ? 25.82200  21.46400  20.03100 1.000 29.05000 ? 149 SER B OG  1 
ATOM   4621 N N   . THR B 1 150 ? 25.97600  21.57700  23.56000 1.000 27.72000 ? 150 THR B N   1 
ATOM   4622 C CA  . THR B 1 150 ? 26.50200  22.59500  24.45700 1.000 27.72000 ? 150 THR B CA  1 
ATOM   4623 C C   . THR B 1 150 ? 27.20000  21.96300  25.65700 1.000 27.72000 ? 150 THR B C   1 
ATOM   4624 O O   . THR B 1 150 ? 26.98300  20.79700  25.99500 1.000 27.72000 ? 150 THR B O   1 
ATOM   4625 C CB  . THR B 1 150 ? 25.37900  23.50300  24.94400 1.000 27.72000 ? 150 THR B CB  1 
ATOM   4626 O OG1 . THR B 1 150 ? 24.39700  22.70800  25.61900 1.000 27.72000 ? 150 THR B OG1 1 
ATOM   4627 C CG2 . THR B 1 150 ? 24.72400  24.20600  23.77200 1.000 27.72000 ? 150 THR B CG2 1 
ATOM   4628 N N   . LYS B 1 151 ? 28.08200  22.74600  26.28700 1.000 29.91000 ? 151 LYS B N   1 
ATOM   4629 C CA  . LYS B 1 151 ? 28.74100  22.32700  27.51600 1.000 29.91000 ? 151 LYS B CA  1 
ATOM   4630 C C   . LYS B 1 151 ? 28.53600  23.26500  28.70000 1.000 29.91000 ? 151 LYS B C   1 
ATOM   4631 O O   . LYS B 1 151 ? 28.69600  22.82000  29.84200 1.000 29.91000 ? 151 LYS B O   1 
ATOM   4632 C CB  . LYS B 1 151 ? 30.24900  22.14900  27.28400 1.000 29.91000 ? 151 LYS B CB  1 
ATOM   4633 C CG  . LYS B 1 151 ? 30.92000  23.32500  26.60200 1.000 29.91000 ? 151 LYS B CG  1 
ATOM   4634 C CD  . LYS B 1 151 ? 32.42500  23.16700  26.63600 1.000 29.91000 ? 151 LYS B CD  1 
ATOM   4635 C CE  . LYS B 1 151 ? 32.91600  23.07500  28.07000 1.000 29.91000 ? 151 LYS B CE  1 
ATOM   4636 N NZ  . LYS B 1 151 ? 34.21800  22.36900  28.17100 1.000 29.91000 ? 151 LYS B NZ  1 
ATOM   4637 N N   . THR B 1 152 ? 28.19400  24.53500  28.47400 1.000 26.48000 ? 152 THR B N   1 
ATOM   4638 C CA  . THR B 1 152 ? 27.94300  25.48200  29.55400 1.000 26.48000 ? 152 THR B CA  1 
ATOM   4639 C C   . THR B 1 152 ? 26.58500  26.14100  29.34900 1.000 26.48000 ? 152 THR B C   1 
ATOM   4640 O O   . THR B 1 152 ? 26.04400  26.16500  28.24100 1.000 26.48000 ? 152 THR B O   1 
ATOM   4641 C CB  . THR B 1 152 ? 29.02900  26.56800  29.64600 1.000 26.48000 ? 152 THR B CB  1 
ATOM   4642 O OG1 . THR B 1 152 ? 28.95000  27.42900  28.50300 1.000 26.48000 ? 152 THR B OG1 1 
ATOM   4643 C CG2 . THR B 1 152 ? 30.41500  25.94300  29.71200 1.000 26.48000 ? 152 THR B CG2 1 
ATOM   4644 N N   . VAL B 1 153 ? 26.03600  26.67400  30.44500 1.000 21.98000 ? 153 VAL B N   1 
ATOM   4645 C CA  . VAL B 1 153 ? 24.70900  27.28400  30.39900 1.000 21.98000 ? 153 VAL B CA  1 
ATOM   4646 C C   . VAL B 1 153 ? 24.68700  28.49300  29.47200 1.000 21.98000 ? 153 VAL B C   1 
ATOM   4647 O O   . VAL B 1 153 ? 23.67700  28.75500  28.80800 1.000 21.98000 ? 153 VAL B O   1 
ATOM   4648 C CB  . VAL B 1 153 ? 24.25200  27.65400  31.82500 1.000 21.98000 ? 153 VAL B CB  1 
ATOM   4649 C CG1 . VAL B 1 153 ? 22.87100  28.29300  31.80300 1.000 21.98000 ? 153 VAL B CG1 1 
ATOM   4650 C CG2 . VAL B 1 153 ? 24.25600  26.42100  32.71600 1.000 21.98000 ? 153 VAL B CG2 1 
ATOM   4651 N N   . THR B 1 154 ? 25.79100  29.24100  29.39700 1.000 22.53000 ? 154 THR B N   1 
ATOM   4652 C CA  . THR B 1 154 ? 25.82400  30.41300  28.52500 1.000 22.53000 ? 154 THR B CA  1 
ATOM   4653 C C   . THR B 1 154 ? 25.71900  30.01600  27.05600 1.000 22.53000 ? 154 THR B C   1 
ATOM   4654 O O   . THR B 1 154 ? 25.06700  30.70900  26.25900 1.000 22.53000 ? 154 THR B O   1 
ATOM   4655 C CB  . THR B 1 154 ? 27.10400  31.21100  28.77500 1.000 22.53000 ? 154 THR B CB  1 
ATOM   4656 O OG1 . THR B 1 154 ? 27.28200  31.40100  30.18400 1.000 22.53000 ? 154 THR B OG1 1 
ATOM   4657 C CG2 . THR B 1 154 ? 27.03000  32.56800  28.09500 1.000 22.53000 ? 154 THR B CG2 1 
ATOM   4658 N N   . GLU B 1 155 ? 26.34300  28.89500  26.68300 1.000 24.33000 ? 155 GLU B N   1 
ATOM   4659 C CA  . GLU B 1 155 ? 26.21600  28.41200  25.31500 1.000 24.33000 ? 155 GLU B CA  1 
ATOM   4660 C C   . GLU B 1 155 ? 24.78700  27.98700  25.02000 1.000 24.33000 ? 155 GLU B C   1 
ATOM   4661 O O   . GLU B 1 155 ? 24.26200  28.27000  23.93700 1.000 24.33000 ? 155 GLU B O   1 
ATOM   4662 C CB  . GLU B 1 155 ? 27.18300  27.25400  25.07400 1.000 24.33000 ? 155 GLU B CB  1 
ATOM   4663 C CG  . GLU B 1 155 ? 28.63300  27.68000  24.92300 1.000 24.33000 ? 155 GLU B CG  1 
ATOM   4664 C CD  . GLU B 1 155 ? 29.60000  26.61700  25.39800 1.000 24.33000 ? 155 GLU B CD  1 
ATOM   4665 O OE1 . GLU B 1 155 ? 29.35300  26.03500  26.47400 1.000 24.33000 ? 155 GLU B OE1 1 
ATOM   4666 O OE2 . GLU B 1 155 ? 30.60100  26.36000  24.69600 1.000 24.33000 ? 155 GLU B OE2 1 
ATOM   4667 N N   . ILE B 1 156 ? 24.12500  27.34700  25.99000 1.000 20.47000 ? 156 ILE B N   1 
ATOM   4668 C CA  . ILE B 1 156 ? 22.72500  26.98500  25.79800 1.000 20.47000 ? 156 ILE B CA  1 
ATOM   4669 C C   . ILE B 1 156 ? 21.88900  28.23900  25.63100 1.000 20.47000 ? 156 ILE B C   1 
ATOM   4670 O O   . ILE B 1 156 ? 20.96300  28.28100  24.81700 1.000 20.47000 ? 156 ILE B O   1 
ATOM   4671 C CB  . ILE B 1 156 ? 22.21000  26.13900  26.97600 1.000 20.47000 ? 156 ILE B CB  1 
ATOM   4672 C CG1 . ILE B 1 156 ? 23.19200  25.02900  27.32700 1.000 20.47000 ? 156 ILE B CG1 1 
ATOM   4673 C CG2 . ILE B 1 156 ? 20.85100  25.54800  26.64600 1.000 20.47000 ? 156 ILE B CG2 1 
ATOM   4674 C CD1 . ILE B 1 156 ? 22.65400  24.07000  28.35700 1.000 20.47000 ? 156 ILE B CD1 1 
ATOM   4675 N N   . SER B 1 157 ? 22.24300  29.29800  26.35700 1.000 17.76000 ? 157 SER B N   1 
ATOM   4676 C CA  . SER B 1 157 ? 21.46900  30.53000  26.29800 1.000 17.76000 ? 157 SER B CA  1 
ATOM   4677 C C   . SER B 1 157 ? 21.57300  31.17300  24.92400 1.000 17.76000 ? 157 SER B C   1 
ATOM   4678 O O   . SER B 1 157 ? 20.55400  31.45900  24.27600 1.000 17.76000 ? 157 SER B O   1 
ATOM   4679 C CB  . SER B 1 157 ? 21.95900  31.48900  27.38100 1.000 17.76000 ? 157 SER B CB  1 
ATOM   4680 O OG  . SER B 1 157 ? 21.98800  30.85100  28.64200 1.000 17.76000 ? 157 SER B OG  1 
ATOM   4681 N N   . GLN B 1 158 ? 22.80400  31.38400  24.45200 1.000 18.47000 ? 158 GLN B N   1 
ATOM   4682 C CA  . GLN B 1 158 ? 22.97400  32.01400  23.14800 1.000 18.47000 ? 158 GLN B CA  1 
ATOM   4683 C C   . GLN B 1 158 ? 22.39700  31.14200  22.04000 1.000 18.47000 ? 158 GLN B C   1 
ATOM   4684 O O   . GLN B 1 158 ? 21.74700  31.64800  21.11500 1.000 18.47000 ? 158 GLN B O   1 
ATOM   4685 C CB  . GLN B 1 158 ? 24.45100  32.31300  22.89000 1.000 18.47000 ? 158 GLN B CB  1 
ATOM   4686 C CG  . GLN B 1 158 ? 24.73100  32.94100  21.52800 1.000 18.47000 ? 158 GLN B CG  1 
ATOM   4687 C CD  . GLN B 1 158 ? 24.00400  34.26200  21.31900 1.000 18.47000 ? 158 GLN B CD  1 
ATOM   4688 O OE1 . GLN B 1 158 ? 22.85600  34.29100  20.87400 1.000 18.47000 ? 158 GLN B OE1 1 
ATOM   4689 N NE2 . GLN B 1 158 ? 24.67800  35.36300  21.63300 1.000 18.47000 ? 158 GLN B NE2 1 
ATOM   4690 N N   . ILE B 1 159 ? 22.56100  29.82000  22.14900 1.000 19.37000 ? 159 ILE B N   1 
ATOM   4691 C CA  . ILE B 1 159 ? 22.07700  28.94500  21.09100 1.000 19.37000 ? 159 ILE B CA  1 
ATOM   4692 C C   . ILE B 1 159 ? 20.55600  28.93300  21.05700 1.000 19.37000 ? 159 ILE B C   1 
ATOM   4693 O O   . ILE B 1 159 ? 19.95200  29.01100  19.98200 1.000 19.37000 ? 159 ILE B O   1 
ATOM   4694 C CB  . ILE B 1 159 ? 22.66100  27.53000  21.25800 1.000 19.37000 ? 159 ILE B CB  1 
ATOM   4695 C CG1 . ILE B 1 159 ? 24.13600  27.52700  20.84900 1.000 19.37000 ? 159 ILE B CG1 1 
ATOM   4696 C CG2 . ILE B 1 159 ? 21.86500  26.51800  20.44400 1.000 19.37000 ? 159 ILE B CG2 1 
ATOM   4697 C CD1 . ILE B 1 159 ? 24.75000  26.15300  20.75100 1.000 19.37000 ? 159 ILE B CD1 1 
ATOM   4698 N N   . ILE B 1 160 ? 19.90600  28.86000  22.22200 1.000 18.01000 ? 160 ILE B N   1 
ATOM   4699 C CA  . ILE B 1 160 ? 18.45200  28.79000  22.21700 1.000 18.01000 ? 160 ILE B CA  1 
ATOM   4700 C C   . ILE B 1 160 ? 17.85200  30.10600  21.74500 1.000 18.01000 ? 160 ILE B C   1 
ATOM   4701 O O   . ILE B 1 160 ? 16.86800  30.10900  20.99600 1.000 18.01000 ? 160 ILE B O   1 
ATOM   4702 C CB  . ILE B 1 160 ? 17.90700  28.36800  23.59600 1.000 18.01000 ? 160 ILE B CB  1 
ATOM   4703 C CG1 . ILE B 1 160 ? 16.42000  28.03700  23.48200 1.000 18.01000 ? 160 ILE B CG1 1 
ATOM   4704 C CG2 . ILE B 1 160 ? 18.09900  29.45700  24.63800 1.000 18.01000 ? 160 ILE B CG2 1 
ATOM   4705 C CD1 . ILE B 1 160 ? 16.09300  27.07000  22.36800 1.000 18.01000 ? 160 ILE B CD1 1 
ATOM   4706 N N   . VAL B 1 161 ? 18.44600  31.24500  22.12200 1.000 17.86000 ? 161 VAL B N   1 
ATOM   4707 C CA  . VAL B 1 161 ? 17.86300  32.50000  21.65600 1.000 17.86000 ? 161 VAL B CA  1 
ATOM   4708 C C   . VAL B 1 161 ? 18.06500  32.65400  20.15300 1.000 17.86000 ? 161 VAL B C   1 
ATOM   4709 O O   . VAL B 1 161 ? 17.13700  33.04300  19.42800 1.000 17.86000 ? 161 VAL B O   1 
ATOM   4710 C CB  . VAL B 1 161 ? 18.41300  33.70500  22.44500 1.000 17.86000 ? 161 VAL B CB  1 
ATOM   4711 C CG1 . VAL B 1 161 ? 18.03600  33.58100  23.90700 1.000 17.86000 ? 161 VAL B CG1 1 
ATOM   4712 C CG2 . VAL B 1 161 ? 19.91200  33.84500  22.28600 1.000 17.86000 ? 161 VAL B CG2 1 
ATOM   4713 N N   . THR B 1 162 ? 19.25000  32.28800  19.64800 1.000 18.86000 ? 162 THR B N   1 
ATOM   4714 C CA  . THR B 1 162 ? 19.48900  32.39200  18.21300 1.000 18.86000 ? 162 THR B CA  1 
ATOM   4715 C C   . THR B 1 162 ? 18.55700  31.47400  17.43300 1.000 18.86000 ? 162 THR B C   1 
ATOM   4716 O O   . THR B 1 162 ? 17.98700  31.87800  16.41200 1.000 18.86000 ? 162 THR B O   1 
ATOM   4717 C CB  . THR B 1 162 ? 20.95000  32.06500  17.90400 1.000 18.86000 ? 162 THR B CB  1 
ATOM   4718 O OG1 . THR B 1 162 ? 21.79000  33.11600  18.39500 1.000 18.86000 ? 162 THR B OG1 1 
ATOM   4719 C CG2 . THR B 1 162 ? 21.16100  31.90700  16.40700 1.000 18.86000 ? 162 THR B CG2 1 
ATOM   4720 N N   . GLU B 1 163 ? 18.34800  30.25100  17.92500 1.000 21.58000 ? 163 GLU B N   1 
ATOM   4721 C CA  . GLU B 1 163 ? 17.52500  29.30300  17.18600 1.000 21.58000 ? 163 GLU B CA  1 
ATOM   4722 C C   . GLU B 1 163 ? 16.05200  29.67700  17.24600 1.000 21.58000 ? 163 GLU B C   1 
ATOM   4723 O O   . GLU B 1 163 ? 15.34000  29.55200  16.24500 1.000 21.58000 ? 163 GLU B O   1 
ATOM   4724 C CB  . GLU B 1 163 ? 17.75000  27.88600  17.71100 1.000 21.58000 ? 163 GLU B CB  1 
ATOM   4725 C CG  . GLU B 1 163 ? 19.17100  27.37500  17.50800 1.000 21.58000 ? 163 GLU B CG  1 
ATOM   4726 C CD  . GLU B 1 163 ? 19.63000  27.44900  16.06400 1.000 21.58000 ? 163 GLU B CD  1 
ATOM   4727 O OE1 . GLU B 1 163 ? 18.80600  27.20300  15.15600 1.000 21.58000 ? 163 GLU B OE1 1 
ATOM   4728 O OE2 . GLU B 1 163 ? 20.82000  27.75600  15.83800 1.000 21.58000 ? 163 GLU B OE2 1 
ATOM   4729 N N   . VAL B 1 164 ? 15.56900  30.14500  18.40000 1.000 20.02000 ? 164 VAL B N   1 
ATOM   4730 C CA  . VAL B 1 164 ? 14.17600  30.57000  18.47300 1.000 20.02000 ? 164 VAL B CA  1 
ATOM   4731 C C   . VAL B 1 164 ? 13.94200  31.78000  17.57700 1.000 20.02000 ? 164 VAL B C   1 
ATOM   4732 O O   . VAL B 1 164 ? 12.88700  31.90000  16.93900 1.000 20.02000 ? 164 VAL B O   1 
ATOM   4733 C CB  . VAL B 1 164 ? 13.77600  30.84700  19.93400 1.000 20.02000 ? 164 VAL B CB  1 
ATOM   4734 C CG1 . VAL B 1 164 ? 12.40200  31.49500  20.00000 1.000 20.02000 ? 164 VAL B CG1 1 
ATOM   4735 C CG2 . VAL B 1 164 ? 13.78100  29.55300  20.73400 1.000 20.02000 ? 164 VAL B CG2 1 
ATOM   4736 N N   . ARG B 1 165 ? 14.93600  32.66900  17.46900 1.000 20.84000 ? 165 ARG B N   1 
ATOM   4737 C CA  . ARG B 1 165 ? 14.77900  33.80800  16.57000 1.000 20.84000 ? 165 ARG B CA  1 
ATOM   4738 C C   . ARG B 1 165 ? 14.78600  33.36800  15.11100 1.000 20.84000 ? 165 ARG B C   1 
ATOM   4739 O O   . ARG B 1 165 ? 13.99300  33.86500  14.30200 1.000 20.84000 ? 165 ARG B O   1 
ATOM   4740 C CB  . ARG B 1 165 ? 15.87600  34.83900  16.83200 1.000 20.84000 ? 165 ARG B CB  1 
ATOM   4741 C CG  . ARG B 1 165 ? 15.92000  35.96700  15.81700 1.000 20.84000 ? 165 ARG B CG  1 
ATOM   4742 C CD  . ARG B 1 165 ? 16.19100  37.30000  16.48700 1.000 20.84000 ? 165 ARG B CD  1 
ATOM   4743 N NE  . ARG B 1 165 ? 16.78100  38.26400  15.56700 1.000 20.84000 ? 165 ARG B NE  1 
ATOM   4744 C CZ  . ARG B 1 165 ? 16.09900  38.96100  14.66900 1.000 20.84000 ? 165 ARG B CZ  1 
ATOM   4745 N NH1 . ARG B 1 165 ? 14.79200  38.81200  14.52600 1.000 20.84000 ? 165 ARG B NH1 1 
ATOM   4746 N NH2 . ARG B 1 165 ? 16.74500  39.82500  13.89200 1.000 20.84000 ? 165 ARG B NH2 1 
ATOM   4747 N N   . ARG B 1 166 ? 15.66400  32.42600  14.75900 1.000 21.67000 ? 166 ARG B N   1 
ATOM   4748 C CA  . ARG B 1 166 ? 15.70900  31.92200  13.39000 1.000 21.67000 ? 166 ARG B CA  1 
ATOM   4749 C C   . ARG B 1 166 ? 14.44000  31.16300  13.03000 1.000 21.67000 ? 166 ARG B C   1 
ATOM   4750 O O   . ARG B 1 166 ? 14.04500  31.13100  11.85900 1.000 21.67000 ? 166 ARG B O   1 
ATOM   4751 C CB  . ARG B 1 166 ? 16.93700  31.02900  13.21300 1.000 21.67000 ? 166 ARG B CB  1 
ATOM   4752 C CG  . ARG B 1 166 ? 17.18100  30.53100  11.80200 1.000 21.67000 ? 166 ARG B CG  1 
ATOM   4753 C CD  . ARG B 1 166 ? 18.40200  29.63000  11.78400 1.000 21.67000 ? 166 ARG B CD  1 
ATOM   4754 N NE  . ARG B 1 166 ? 19.57100  30.30400  12.33800 1.000 21.67000 ? 166 ARG B NE  1 
ATOM   4755 C CZ  . ARG B 1 166 ? 20.61600  29.68200  12.86600 1.000 21.67000 ? 166 ARG B CZ  1 
ATOM   4756 N NH1 . ARG B 1 166 ? 20.66200  28.36300  12.95300 1.000 21.67000 ? 166 ARG B NH1 1 
ATOM   4757 N NH2 . ARG B 1 166 ? 21.63700  30.40100  13.32300 1.000 21.67000 ? 166 ARG B NH2 1 
ATOM   4758 N N   . ILE B 1 167 ? 13.79100  30.55100  14.01800 1.000 23.53000 ? 167 ILE B N   1 
ATOM   4759 C CA  . ILE B 1 167 ? 12.57900  29.78500  13.75400 1.000 23.53000 ? 167 ILE B CA  1 
ATOM   4760 C C   . ILE B 1 167 ? 11.36300  30.69400  13.65100 1.000 23.53000 ? 167 ILE B C   1 
ATOM   4761 O O   . ILE B 1 167 ? 10.48600  30.48100  12.80600 1.000 23.53000 ? 167 ILE B O   1 
ATOM   4762 C CB  . ILE B 1 167 ? 12.40100  28.71700  14.84600 1.000 23.53000 ? 167 ILE B CB  1 
ATOM   4763 C CG1 . ILE B 1 167 ? 13.49600  27.66400  14.71600 1.000 23.53000 ? 167 ILE B CG1 1 
ATOM   4764 C CG2 . ILE B 1 167 ? 11.02400  28.08800  14.77600 1.000 23.53000 ? 167 ILE B CG2 1 
ATOM   4765 C CD1 . ILE B 1 167 ? 13.35300  26.51500  15.65300 1.000 23.53000 ? 167 ILE B CD1 1 
ATOM   4766 N N   . THR B 1 168 ? 11.28400  31.71600  14.50000 1.000 22.90000 ? 168 THR B N   1 
ATOM   4767 C CA  . THR B 1 168 ? 10.07600  32.52500  14.59500 1.000 22.90000 ? 168 THR B CA  1 
ATOM   4768 C C   . THR B 1 168 ? 10.13600  33.82700  13.81300 1.000 22.90000 ? 168 THR B C   1 
ATOM   4769 O O   . THR B 1 168 ? 9.09500   34.30100  13.34800 1.000 22.90000 ? 168 THR B O   1 
ATOM   4770 C CB  . THR B 1 168 ? 9.77600   32.84500  16.05900 1.000 22.90000 ? 168 THR B CB  1 
ATOM   4771 O OG1 . THR B 1 168 ? 10.93600  33.42900  16.66700 1.000 22.90000 ? 168 THR B OG1 1 
ATOM   4772 C CG2 . THR B 1 168 ? 9.39500   31.58700  16.80600 1.000 22.90000 ? 168 THR B CG2 1 
ATOM   4773 N N   . GLY B 1 169 ? 11.31600  34.41600  13.64700 1.000 23.03000 ? 169 GLY B N   1 
ATOM   4774 C CA  . GLY B 1 169 ? 11.40100  35.71600  13.01800 1.000 23.03000 ? 169 GLY B CA  1 
ATOM   4775 C C   . GLY B 1 169 ? 11.05400  36.88900  13.90900 1.000 23.03000 ? 169 GLY B C   1 
ATOM   4776 O O   . GLY B 1 169 ? 10.85300  37.99500  13.39400 1.000 23.03000 ? 169 GLY B O   1 
ATOM   4777 N N   . PHE B 1 170 ? 10.96400  36.68500  15.22200 1.000 22.04000 ? 170 PHE B N   1 
ATOM   4778 C CA  . PHE B 1 170 ? 10.74700  37.79900  16.13600 1.000 22.04000 ? 170 PHE B CA  1 
ATOM   4779 C C   . PHE B 1 170 ? 11.91900  38.76900  16.07400 1.000 22.04000 ? 170 PHE B C   1 
ATOM   4780 O O   . PHE B 1 170 ? 13.07800  38.36000  15.95500 1.000 22.04000 ? 170 PHE B O   1 
ATOM   4781 C CB  . PHE B 1 170 ? 10.56900  37.29100  17.56800 1.000 22.04000 ? 170 PHE B CB  1 
ATOM   4782 C CG  . PHE B 1 170 ? 9.16300   36.89200  17.90400 1.000 22.04000 ? 170 PHE B CG  1 
ATOM   4783 C CD1 . PHE B 1 170 ? 8.27100   37.81700  18.41900 1.000 22.04000 ? 170 PHE B CD1 1 
ATOM   4784 C CD2 . PHE B 1 170 ? 8.73400   35.59300  17.71500 1.000 22.04000 ? 170 PHE B CD2 1 
ATOM   4785 C CE1 . PHE B 1 170 ? 6.97600   37.45200  18.73200 1.000 22.04000 ? 170 PHE B CE1 1 
ATOM   4786 C CE2 . PHE B 1 170 ? 7.44300   35.22000  18.02600 1.000 22.04000 ? 170 PHE B CE2 1 
ATOM   4787 C CZ  . PHE B 1 170 ? 6.56200   36.15100  18.53500 1.000 22.04000 ? 170 PHE B CZ  1 
ATOM   4788 N N   . ASP B 1 171 ? 11.61000  40.06600  16.15600 1.000 23.66000 ? 171 ASP B N   1 
ATOM   4789 C CA  . ASP B 1 171 ? 12.65600  41.08300  16.10200 1.000 23.66000 ? 171 ASP B CA  1 
ATOM   4790 C C   . ASP B 1 171 ? 13.59900  40.98700  17.29300 1.000 23.66000 ? 171 ASP B C   1 
ATOM   4791 O O   . ASP B 1 171 ? 14.77400  41.35800  17.18400 1.000 23.66000 ? 171 ASP B O   1 
ATOM   4792 C CB  . ASP B 1 171 ? 12.03400  42.47800  16.03900 1.000 23.66000 ? 171 ASP B CB  1 
ATOM   4793 C CG  . ASP B 1 171 ? 11.20800  42.69600  14.78900 1.000 23.66000 ? 171 ASP B CG  1 
ATOM   4794 O OD1 . ASP B 1 171 ? 11.51600  42.07100  13.75200 1.000 23.66000 ? 171 ASP B OD1 1 
ATOM   4795 O OD2 . ASP B 1 171 ? 10.24700  43.49300  14.84400 1.000 23.66000 ? 171 ASP B OD2 1 
ATOM   4796 N N   . ARG B 1 172 ? 13.11400  40.48900  18.42900 1.000 19.35000 ? 172 ARG B N   1 
ATOM   4797 C CA  . ARG B 1 172 ? 13.91900  40.39800  19.63700 1.000 19.35000 ? 172 ARG B CA  1 
ATOM   4798 C C   . ARG B 1 172 ? 13.65100  39.06900  20.32500 1.000 19.35000 ? 172 ARG B C   1 
ATOM   4799 O O   . ARG B 1 172 ? 12.50000  38.64300  20.43000 1.000 19.35000 ? 172 ARG B O   1 
ATOM   4800 C CB  . ARG B 1 172 ? 13.60700  41.55700  20.59500 1.000 19.35000 ? 172 ARG B CB  1 
ATOM   4801 C CG  . ARG B 1 172 ? 14.36600  41.50800  21.90900 1.000 19.35000 ? 172 ARG B CG  1 
ATOM   4802 C CD  . ARG B 1 172 ? 13.90300  42.60500  22.85300 1.000 19.35000 ? 172 ARG B CD  1 
ATOM   4803 N NE  . ARG B 1 172 ? 14.02500  43.93100  22.25900 1.000 19.35000 ? 172 ARG B NE  1 
ATOM   4804 C CZ  . ARG B 1 172 ? 15.14100  44.64700  22.24600 1.000 19.35000 ? 172 ARG B CZ  1 
ATOM   4805 N NH1 . ARG B 1 172 ? 16.26400  44.18600  22.77300 1.000 19.35000 ? 172 ARG B NH1 1 
ATOM   4806 N NH2 . ARG B 1 172 ? 15.13000  45.85500  21.69200 1.000 19.35000 ? 172 ARG B NH2 1 
ATOM   4807 N N   . VAL B 1 173 ? 14.71600  38.42200  20.79500 1.000 17.24000 ? 173 VAL B N   1 
ATOM   4808 C CA  . VAL B 1 173 ? 14.61800  37.18400  21.56300 1.000 17.24000 ? 173 VAL B CA  1 
ATOM   4809 C C   . VAL B 1 173 ? 15.67500  37.23900  22.65600 1.000 17.24000 ? 173 VAL B C   1 
ATOM   4810 O O   . VAL B 1 173 ? 16.86800  37.37500  22.36100 1.000 17.24000 ? 173 VAL B O   1 
ATOM   4811 C CB  . VAL B 1 173 ? 14.81000  35.92500  20.69600 1.000 17.24000 ? 173 VAL B CB  1 
ATOM   4812 C CG1 . VAL B 1 173 ? 14.93200  34.69300  21.57600 1.000 17.24000 ? 173 VAL B CG1 1 
ATOM   4813 C CG2 . VAL B 1 173 ? 13.65400  35.75800  19.71900 1.000 17.24000 ? 173 VAL B CG2 1 
ATOM   4814 N N   . MET B 1 174 ? 15.24800  37.13200  23.91100 1.000 13.49000 ? 174 MET B N   1 
ATOM   4815 C CA  . MET B 1 174 ? 16.14800  37.26400  25.04900 1.000 13.49000 ? 174 MET B CA  1 
ATOM   4816 C C   . MET B 1 174 ? 15.94800  36.10600  26.01000 1.000 13.49000 ? 174 MET B C   1 
ATOM   4817 O O   . MET B 1 174 ? 14.81000  35.76800  26.35000 1.000 13.49000 ? 174 MET B O   1 
ATOM   4818 C CB  . MET B 1 174 ? 15.90900  38.57600  25.79800 1.000 13.49000 ? 174 MET B CB  1 
ATOM   4819 C CG  . MET B 1 174 ? 15.86600  39.81600  24.93200 1.000 13.49000 ? 174 MET B CG  1 
ATOM   4820 S SD  . MET B 1 174 ? 15.20400  41.21100  25.85800 1.000 13.49000 ? 174 MET B SD  1 
ATOM   4821 C CE  . MET B 1 174 ? 13.57600  40.58800  26.26800 1.000 13.49000 ? 174 MET B CE  1 
ATOM   4822 N N   . PHE B 1 175 ? 17.04800  35.51700  26.46700 1.000 12.82000 ? 175 PHE B N   1 
ATOM   4823 C CA  . PHE B 1 175 ? 16.98200  34.60000  27.59300 1.000 12.82000 ? 175 PHE B CA  1 
ATOM   4824 C C   . PHE B 1 175 ? 17.05500  35.39900  28.88600 1.000 12.82000 ? 175 PHE B C   1 
ATOM   4825 O O   . PHE B 1 175 ? 17.89000  36.29600  29.03300 1.000 12.82000 ? 175 PHE B O   1 
ATOM   4826 C CB  . PHE B 1 175 ? 18.11400  33.57300  27.53500 1.000 12.82000 ? 175 PHE B CB  1 
ATOM   4827 C CG  . PHE B 1 175 ? 17.77800  32.25700  28.18600 1.000 12.82000 ? 175 PHE B CG  1 
ATOM   4828 C CD1 . PHE B 1 175 ? 16.68500  32.13300  29.02800 1.000 12.82000 ? 175 PHE B CD1 1 
ATOM   4829 C CD2 . PHE B 1 175 ? 18.55600  31.14400  27.94900 1.000 12.82000 ? 175 PHE B CD2 1 
ATOM   4830 C CE1 . PHE B 1 175 ? 16.38600  30.92400  29.62200 1.000 12.82000 ? 175 PHE B CE1 1 
ATOM   4831 C CE2 . PHE B 1 175 ? 18.26200  29.93500  28.53700 1.000 12.82000 ? 175 PHE B CE2 1 
ATOM   4832 C CZ  . PHE B 1 175 ? 17.17400  29.82400  29.37400 1.000 12.82000 ? 175 PHE B CZ  1 
ATOM   4833 N N   . TYR B 1 176 ? 16.19700  35.03900  29.83700 1.000 13.04000 ? 176 TYR B N   1 
ATOM   4834 C CA  . TYR B 1 176 ? 15.90000  35.84400  31.01600 1.000 13.04000 ? 176 TYR B CA  1 
ATOM   4835 C C   . TYR B 1 176 ? 16.01500  34.91600  32.21900 1.000 13.04000 ? 176 TYR B C   1 
ATOM   4836 O O   . TYR B 1 176 ? 15.03100  34.28000  32.60500 1.000 13.04000 ? 176 TYR B O   1 
ATOM   4837 C CB  . TYR B 1 176 ? 14.50300  36.45000  30.86000 1.000 13.04000 ? 176 TYR B CB  1 
ATOM   4838 C CG  . TYR B 1 176 ? 14.04100  37.40000  31.93800 1.000 13.04000 ? 176 TYR B CG  1 
ATOM   4839 C CD1 . TYR B 1 176 ? 14.45400  38.72600  31.94900 1.000 13.04000 ? 176 TYR B CD1 1 
ATOM   4840 C CD2 . TYR B 1 176 ? 13.14800  36.98200  32.91600 1.000 13.04000 ? 176 TYR B CD2 1 
ATOM   4841 C CE1 . TYR B 1 176 ? 14.01500  39.60200  32.92600 1.000 13.04000 ? 176 TYR B CE1 1 
ATOM   4842 C CE2 . TYR B 1 176 ? 12.70300  37.84800  33.89500 1.000 13.04000 ? 176 TYR B CE2 1 
ATOM   4843 C CZ  . TYR B 1 176 ? 13.13500  39.15700  33.89400 1.000 13.04000 ? 176 TYR B CZ  1 
ATOM   4844 O OH  . TYR B 1 176 ? 12.69000  40.01500  34.87500 1.000 13.04000 ? 176 TYR B OH  1 
ATOM   4845 N N   . ARG B 1 177 ? 17.22700  34.78800  32.75700 1.000 13.48000 ? 177 ARG B N   1 
ATOM   4846 C CA  . ARG B 1 177 ? 17.43700  33.94400  33.92700 1.000 13.48000 ? 177 ARG B CA  1 
ATOM   4847 C C   . ARG B 1 177 ? 16.90200  34.63200  35.17600 1.000 13.48000 ? 177 ARG B C   1 
ATOM   4848 O O   . ARG B 1 177 ? 16.96100  35.85700  35.30000 1.000 13.48000 ? 177 ARG B O   1 
ATOM   4849 C CB  . ARG B 1 177 ? 18.92400  33.61400  34.08600 1.000 13.48000 ? 177 ARG B CB  1 
ATOM   4850 C CG  . ARG B 1 177 ? 19.29500  32.93400  35.40300 1.000 13.48000 ? 177 ARG B CG  1 
ATOM   4851 C CD  . ARG B 1 177 ? 20.69600  32.33100  35.36700 1.000 13.48000 ? 177 ARG B CD  1 
ATOM   4852 N NE  . ARG B 1 177 ? 21.70700  33.28000  34.91400 1.000 13.48000 ? 177 ARG B NE  1 
ATOM   4853 C CZ  . ARG B 1 177 ? 22.38500  34.09900  35.70800 1.000 13.48000 ? 177 ARG B CZ  1 
ATOM   4854 N NH1 . ARG B 1 177 ? 22.17800  34.12600  37.01500 1.000 13.48000 ? 177 ARG B NH1 1 
ATOM   4855 N NH2 . ARG B 1 177 ? 23.29500  34.91100  35.17700 1.000 13.48000 ? 177 ARG B NH2 1 
ATOM   4856 N N   . PHE B 1 178 ? 16.36700  33.84300  36.10100 1.000 13.82000 ? 178 PHE B N   1 
ATOM   4857 C CA  . PHE B 1 178 ? 15.87600  34.38700  37.35700 1.000 13.82000 ? 178 PHE B CA  1 
ATOM   4858 C C   . PHE B 1 178 ? 16.94600  34.32600  38.44000 1.000 13.82000 ? 178 PHE B C   1 
ATOM   4859 O O   . PHE B 1 178 ? 17.80800  33.44400  38.44500 1.000 13.82000 ? 178 PHE B O   1 
ATOM   4860 C CB  . PHE B 1 178 ? 14.61900  33.65000  37.81600 1.000 13.82000 ? 178 PHE B CB  1 
ATOM   4861 C CG  . PHE B 1 178 ? 13.39000  34.03000  37.04700 1.000 13.82000 ? 178 PHE B CG  1 
ATOM   4862 C CD1 . PHE B 1 178 ? 12.85500  35.30100  37.16000 1.000 13.82000 ? 178 PHE B CD1 1 
ATOM   4863 C CD2 . PHE B 1 178 ? 12.77400  33.12600  36.20600 1.000 13.82000 ? 178 PHE B CD2 1 
ATOM   4864 C CE1 . PHE B 1 178 ? 11.72700  35.65800  36.45000 1.000 13.82000 ? 178 PHE B CE1 1 
ATOM   4865 C CE2 . PHE B 1 178 ? 11.64600  33.47900  35.49500 1.000 13.82000 ? 178 PHE B CE2 1 
ATOM   4866 C CZ  . PHE B 1 178 ? 11.12200  34.74600  35.61700 1.000 13.82000 ? 178 PHE B CZ  1 
ATOM   4867 N N   . ASP B 1 179 ? 16.88200  35.29000  39.35200 1.000 20.25000 ? 179 ASP B N   1 
ATOM   4868 C CA  . ASP B 1 179 ? 17.75000  35.37700  40.51500 1.000 20.25000 ? 179 ASP B CA  1 
ATOM   4869 C C   . ASP B 1 179 ? 17.17500  34.56500  41.67100 1.000 20.25000 ? 179 ASP B C   1 
ATOM   4870 O O   . ASP B 1 179 ? 15.99700  34.20000  41.68100 1.000 20.25000 ? 179 ASP B O   1 
ATOM   4871 C CB  . ASP B 1 179 ? 17.93100  36.83800  40.93600 1.000 20.25000 ? 179 ASP B CB  1 
ATOM   4872 C CG  . ASP B 1 179 ? 19.12700  37.04400  41.83800 1.000 20.25000 ? 179 ASP B CG  1 
ATOM   4873 O OD1 . ASP B 1 179 ? 19.80600  36.04700  42.16300 1.000 20.25000 ? 179 ASP B OD1 1 
ATOM   4874 O OD2 . ASP B 1 179 ? 19.38900  38.20700  42.21600 1.000 20.25000 ? 179 ASP B OD2 1 
ATOM   4875 N N   . ARG B 1 180 ? 18.03100  34.27200  42.65300 1.000 24.61000 ? 180 ARG B N   1 
ATOM   4876 C CA  . ARG B 1 180 ? 17.53400  33.66900  43.88400 1.000 24.61000 ? 180 ARG B CA  1 
ATOM   4877 C C   . ARG B 1 180 ? 16.57500  34.60900  44.60200 1.000 24.61000 ? 180 ARG B C   1 
ATOM   4878 O O   . ARG B 1 180 ? 15.67200  34.15400  45.31400 1.000 24.61000 ? 180 ARG B O   1 
ATOM   4879 C CB  . ARG B 1 180 ? 18.69700  33.28900  44.79900 1.000 24.61000 ? 180 ARG B CB  1 
ATOM   4880 C CG  . ARG B 1 180 ? 18.40200  32.10200  45.70500 1.000 24.61000 ? 180 ARG B CG  1 
ATOM   4881 C CD  . ARG B 1 180 ? 19.49600  31.90300  46.73900 1.000 24.61000 ? 180 ARG B CD  1 
ATOM   4882 N NE  . ARG B 1 180 ? 20.82200  31.85900  46.13400 1.000 24.61000 ? 180 ARG B NE  1 
ATOM   4883 C CZ  . ARG B 1 180 ? 21.94800  31.69000  46.81300 1.000 24.61000 ? 180 ARG B CZ  1 
ATOM   4884 N NH1 . ARG B 1 180 ? 21.94600  31.53200  48.12600 1.000 24.61000 ? 180 ARG B NH1 1 
ATOM   4885 N NH2 . ARG B 1 180 ? 23.10500  31.68100  46.15700 1.000 24.61000 ? 180 ARG B NH2 1 
ATOM   4886 N N   . ASP B 1 181 ? 16.74600  35.91700  44.41600 1.000 22.87000 ? 181 ASP B N   1 
ATOM   4887 C CA  . ASP B 1 181 ? 15.78600  36.92100  44.85600 1.000 22.87000 ? 181 ASP B CA  1 
ATOM   4888 C C   . ASP B 1 181 ? 14.67300  37.13000  43.84000 1.000 22.87000 ? 181 ASP B C   1 
ATOM   4889 O O   . ASP B 1 181 ? 13.89500  38.08200  43.97100 1.000 22.87000 ? 181 ASP B O   1 
ATOM   4890 C CB  . ASP B 1 181 ? 16.49700  38.24800  45.13500 1.000 22.87000 ? 181 ASP B CB  1 
ATOM   4891 C CG  . ASP B 1 181 ? 17.54700  38.12800  46.22000 1.000 22.87000 ? 181 ASP B CG  1 
ATOM   4892 O OD1 . ASP B 1 181 ? 17.32300  37.36600  47.18400 1.000 22.87000 ? 181 ASP B OD1 1 
ATOM   4893 O OD2 . ASP B 1 181 ? 18.59800  38.79300  46.10600 1.000 22.87000 ? 181 ASP B OD2 1 
ATOM   4894 N N   . TRP B 1 182 ? 14.61300  36.26600  42.82500 1.000 21.35000 ? 182 TRP B N   1 
ATOM   4895 C CA  . TRP B 1 182 ? 13.62800  36.29900  41.74700 1.000 21.35000 ? 182 TRP B CA  1 
ATOM   4896 C C   . TRP B 1 182 ? 13.74400  37.54500  40.87900 1.000 21.35000 ? 182 TRP B C   1 
ATOM   4897 O O   . TRP B 1 182 ? 12.81300  37.87700  40.13900 1.000 21.35000 ? 182 TRP B O   1 
ATOM   4898 C CB  . TRP B 1 182 ? 12.20300  36.15100  42.29000 1.000 21.35000 ? 182 TRP B CB  1 
ATOM   4899 C CG  . TRP B 1 182 ? 11.85100  34.73000  42.58100 1.000 21.35000 ? 182 TRP B CG  1 
ATOM   4900 C CD1 . TRP B 1 182 ? 11.73800  34.14400  43.80700 1.000 21.35000 ? 182 TRP B CD1 1 
ATOM   4901 C CD2 . TRP B 1 182 ? 11.58500  33.70500  41.61900 1.000 21.35000 ? 182 TRP B CD2 1 
ATOM   4902 N NE1 . TRP B 1 182 ? 11.40700  32.81800  43.66800 1.000 21.35000 ? 182 TRP B NE1 1 
ATOM   4903 C CE2 . TRP B 1 182 ? 11.30800  32.52300  42.33400 1.000 21.35000 ? 182 TRP B CE2 1 
ATOM   4904 C CE3 . TRP B 1 182 ? 11.55100  33.67200  40.22200 1.000 21.35000 ? 182 TRP B CE3 1 
ATOM   4905 C CZ2 . TRP B 1 182 ? 10.99900  31.32300  41.69900 1.000 21.35000 ? 182 TRP B CZ2 1 
ATOM   4906 C CZ3 . TRP B 1 182 ? 11.24200  32.48100  39.59300 1.000 21.35000 ? 182 TRP B CZ3 1 
ATOM   4907 C CH2 . TRP B 1 182 ? 10.97100  31.32200  40.33100 1.000 21.35000 ? 182 TRP B CH2 1 
ATOM   4908 N N   . ASN B 1 183 ? 14.87900  38.23300  40.94000 1.000 16.76000 ? 183 ASN B N   1 
ATOM   4909 C CA  . ASN B 1 183 ? 15.18100  39.24400  39.93800 1.000 16.76000 ? 183 ASN B CA  1 
ATOM   4910 C C   . ASN B 1 183 ? 15.45400  38.57200  38.60000 1.000 16.76000 ? 183 ASN B C   1 
ATOM   4911 O O   . ASN B 1 183 ? 16.02500  37.48100  38.53900 1.000 16.76000 ? 183 ASN B O   1 
ATOM   4912 C CB  . ASN B 1 183 ? 16.39200  40.07700  40.35900 1.000 16.76000 ? 183 ASN B CB  1 
ATOM   4913 C CG  . ASN B 1 183 ? 16.16400  40.82900  41.65300 1.000 16.76000 ? 183 ASN B CG  1 
ATOM   4914 O OD1 . ASN B 1 183 ? 15.05700  41.28800  41.93300 1.000 16.76000 ? 183 ASN B OD1 1 
ATOM   4915 N ND2 . ASN B 1 183 ? 17.21700  40.95900  42.45300 1.000 16.76000 ? 183 ASN B ND2 1 
ATOM   4916 N N   . GLY B 1 184 ? 15.02800  39.21500  37.52400 1.000 13.29000 ? 184 GLY B N   1 
ATOM   4917 C CA  . GLY B 1 184 ? 15.41600  38.75300  36.21300 1.000 13.29000 ? 184 GLY B CA  1 
ATOM   4918 C C   . GLY B 1 184 ? 16.78300  39.26600  35.81200 1.000 13.29000 ? 184 GLY B C   1 
ATOM   4919 O O   . GLY B 1 184 ? 17.34700  40.17000  36.42600 1.000 13.29000 ? 184 GLY B O   1 
ATOM   4920 N N   . ILE B 1 185 ? 17.32200  38.67100  34.75300 1.000 11.52000 ? 185 ILE B N   1 
ATOM   4921 C CA  . ILE B 1 185 ? 18.55200  39.16600  34.14700 1.000 11.52000 ? 185 ILE B CA  1 
ATOM   4922 C C   . ILE B 1 185 ? 18.64700  38.61500  32.73300 1.000 11.52000 ? 185 ILE B C   1 
ATOM   4923 O O   . ILE B 1 185 ? 18.50000  37.40700  32.50600 1.000 11.52000 ? 185 ILE B O   1 
ATOM   4924 C CB  . ILE B 1 185 ? 19.79500  38.80400  34.98500 1.000 11.52000 ? 185 ILE B CB  1 
ATOM   4925 C CG1 . ILE B 1 185 ? 21.07600  39.19400  34.24200 1.000 11.52000 ? 185 ILE B CG1 1 
ATOM   4926 C CG2 . ILE B 1 185 ? 19.80900  37.33100  35.34700 1.000 11.52000 ? 185 ILE B CG2 1 
ATOM   4927 C CD1 . ILE B 1 185 ? 22.34100  38.92500  35.02700 1.000 11.52000 ? 185 ILE B CD1 1 
ATOM   4928 N N   . VAL B 1 186 ? 18.89000  39.50200  31.77100 1.000 11.40000 ? 186 VAL B N   1 
ATOM   4929 C CA  . VAL B 1 186 ? 18.98500  39.11700  30.36700 1.000 11.40000 ? 186 VAL B CA  1 
ATOM   4930 C C   . VAL B 1 186 ? 20.35900  38.48400  30.16900 1.000 11.40000 ? 186 VAL B C   1 
ATOM   4931 O O   . VAL B 1 186 ? 21.35900  39.17900  29.99600 1.000 11.40000 ? 186 VAL B O   1 
ATOM   4932 C CB  . VAL B 1 186 ? 18.76600  40.30800  29.43300 1.000 11.40000 ? 186 VAL B CB  1 
ATOM   4933 C CG1 . VAL B 1 186 ? 18.94400  39.88500  27.98500 1.000 11.40000 ? 186 VAL B CG1 1 
ATOM   4934 C CG2 . VAL B 1 186 ? 17.38000  40.89400  29.65000 1.000 11.40000 ? 186 VAL B CG2 1 
ATOM   4935 N N   . ILE B 1 187 ? 20.41100  37.15300  30.21500 1.000 12.46000 ? 187 ILE B N   1 
ATOM   4936 C CA  . ILE B 1 187 ? 21.67500  36.44800  30.04000 1.000 12.46000 ? 187 ILE B CA  1 
ATOM   4937 C C   . ILE B 1 187 ? 22.03000  36.20100  28.57700 1.000 12.46000 ? 187 ILE B C   1 
ATOM   4938 O O   . ILE B 1 187 ? 23.21400  36.02900  28.25800 1.000 12.46000 ? 187 ILE B O   1 
ATOM   4939 C CB  . ILE B 1 187 ? 21.65900  35.10800  30.79200 1.000 12.46000 ? 187 ILE B CB  1 
ATOM   4940 C CG1 . ILE B 1 187 ? 20.53400  34.21300  30.26700 1.000 12.46000 ? 187 ILE B CG1 1 
ATOM   4941 C CG2 . ILE B 1 187 ? 21.50100  35.34700  32.28000 1.000 12.46000 ? 187 ILE B CG2 1 
ATOM   4942 C CD1 . ILE B 1 187 ? 20.50800  32.83700  30.88900 1.000 12.46000 ? 187 ILE B CD1 1 
ATOM   4943 N N   . ALA B 1 188 ? 21.04600  36.18100  27.68300 1.000 13.02000 ? 188 ALA B N   1 
ATOM   4944 C CA  . ALA B 1 188 ? 21.30100  35.99800  26.26300 1.000 13.02000 ? 188 ALA B CA  1 
ATOM   4945 C C   . ALA B 1 188 ? 20.29000  36.81200  25.47700 1.000 13.02000 ? 188 ALA B C   1 
ATOM   4946 O O   . ALA B 1 188 ? 19.16600  37.03700  25.93100 1.000 13.02000 ? 188 ALA B O   1 
ATOM   4947 C CB  . ALA B 1 188 ? 21.21800  34.52800  25.83900 1.000 13.02000 ? 188 ALA B CB  1 
ATOM   4948 N N   . GLU B 1 189 ? 20.69800  37.25200  24.29000 1.000 16.59000 ? 189 GLU B N   1 
ATOM   4949 C CA  . GLU B 1 189 ? 19.83200  38.09600  23.48000 1.000 16.59000 ? 189 GLU B CA  1 
ATOM   4950 C C   . GLU B 1 189 ? 20.19900  37.94600  22.01400 1.000 16.59000 ? 189 GLU B C   1 
ATOM   4951 O O   . GLU B 1 189 ? 21.38200  37.97400  21.66200 1.000 16.59000 ? 189 GLU B O   1 
ATOM   4952 C CB  . GLU B 1 189 ? 19.94900  39.56200  23.91400 1.000 16.59000 ? 189 GLU B CB  1 
ATOM   4953 C CG  . GLU B 1 189 ? 19.00500  40.51500  23.20200 1.000 16.59000 ? 189 GLU B CG  1 
ATOM   4954 C CD  . GLU B 1 189 ? 19.24400  41.96000  23.59100 1.000 16.59000 ? 189 GLU B CD  1 
ATOM   4955 O OE1 . GLU B 1 189 ? 20.37300  42.28200  24.02000 1.000 16.59000 ? 189 GLU B OE1 1 
ATOM   4956 O OE2 . GLU B 1 189 ? 18.30200  42.77200  23.47100 1.000 16.59000 ? 189 GLU B OE2 1 
ATOM   4957 N N   . ASP B 1 190 ? 19.18300  37.78400  21.17000 1.000 19.30000 ? 190 ASP B N   1 
ATOM   4958 C CA  . ASP B 1 190 ? 19.32000  37.89400  19.72200 1.000 19.30000 ? 190 ASP B CA  1 
ATOM   4959 C C   . ASP B 1 190 ? 18.25000  38.87200  19.26300 1.000 19.30000 ? 190 ASP B C   1 
ATOM   4960 O O   . ASP B 1 190 ? 17.05600  38.56300  19.32700 1.000 19.30000 ? 190 ASP B O   1 
ATOM   4961 C CB  . ASP B 1 190 ? 19.17000  36.54000  19.02700 1.000 19.30000 ? 190 ASP B CB  1 
ATOM   4962 C CG  . ASP B 1 190 ? 19.43700  36.61700  17.53100 1.000 19.30000 ? 190 ASP B CG  1 
ATOM   4963 O OD1 . ASP B 1 190 ? 19.98200  37.64300  17.07100 1.000 19.30000 ? 190 ASP B OD1 1 
ATOM   4964 O OD2 . ASP B 1 190 ? 19.09700  35.65200  16.81400 1.000 19.30000 ? 190 ASP B OD2 1 
ATOM   4965 N N   . LYS B 1 191 ? 18.67400  40.04900  18.81400 1.000 20.41000 ? 191 LYS B N   1 
ATOM   4966 C CA  . LYS B 1 191 ? 17.76700  41.14200  18.50900 1.000 20.41000 ? 191 LYS B CA  1 
ATOM   4967 C C   . LYS B 1 191 ? 18.14600  41.77100  17.17600 1.000 20.41000 ? 191 LYS B C   1 
ATOM   4968 O O   . LYS B 1 191 ? 19.16600  41.43800  16.56700 1.000 20.41000 ? 191 LYS B O   1 
ATOM   4969 C CB  . LYS B 1 191 ? 17.77200  42.19400  19.62800 1.000 20.41000 ? 191 LYS B CB  1 
ATOM   4970 C CG  . LYS B 1 191 ? 19.16400  42.61200  20.08600 1.000 20.41000 ? 191 LYS B CG  1 
ATOM   4971 C CD  . LYS B 1 191 ? 19.53500  43.98300  19.55300 1.000 20.41000 ? 191 LYS B CD  1 
ATOM   4972 C CE  . LYS B 1 191 ? 21.01000  44.28100  19.75500 1.000 20.41000 ? 191 LYS B CE  1 
ATOM   4973 N NZ  . LYS B 1 191 ? 21.38700  45.58100  19.13500 1.000 20.41000 ? 191 LYS B NZ  1 
ATOM   4974 N N   . GLN B 1 192 ? 17.29700  42.69100  16.72700 1.000 22.74000 ? 192 GLN B N   1 
ATOM   4975 C CA  . GLN B 1 192 ? 17.50400  43.36500  15.45500 1.000 22.74000 ? 192 GLN B CA  1 
ATOM   4976 C C   . GLN B 1 192 ? 18.74100  44.25500  15.51300 1.000 22.74000 ? 192 GLN B C   1 
ATOM   4977 O O   . GLN B 1 192 ? 19.15100  44.71900  16.58000 1.000 22.74000 ? 192 GLN B O   1 
ATOM   4978 C CB  . GLN B 1 192 ? 16.27600  44.19500  15.08700 1.000 22.74000 ? 192 GLN B CB  1 
ATOM   4979 C CG  . GLN B 1 192 ? 16.09000  44.38900  13.59600 1.000 22.74000 ? 192 GLN B CG  1 
ATOM   4980 C CD  . GLN B 1 192 ? 15.68500  43.11000  12.89500 1.000 22.74000 ? 192 GLN B CD  1 
ATOM   4981 O OE1 . GLN B 1 192 ? 14.92500  42.30700  13.43800 1.000 22.74000 ? 192 GLN B OE1 1 
ATOM   4982 N NE2 . GLN B 1 192 ? 16.19300  42.90900  11.68500 1.000 22.74000 ? 192 GLN B NE2 1 
ATOM   4983 N N   . GLU B 1 193 ? 19.34500  44.48000  14.34300 1.000 27.88000 ? 193 GLU B N   1 
ATOM   4984 C CA  . GLU B 1 193 ? 20.60000  45.22300  14.28800 1.000 27.88000 ? 193 GLU B CA  1 
ATOM   4985 C C   . GLU B 1 193 ? 20.45200  46.62300  14.87100 1.000 27.88000 ? 193 GLU B C   1 
ATOM   4986 O O   . GLU B 1 193 ? 21.35600  47.11600  15.55700 1.000 27.88000 ? 193 GLU B O   1 
ATOM   4987 C CB  . GLU B 1 193 ? 21.08700  45.30700  12.84000 1.000 27.88000 ? 193 GLU B CB  1 
ATOM   4988 C CG  . GLU B 1 193 ? 21.55400  43.99000  12.24400 1.000 27.88000 ? 193 GLU B CG  1 
ATOM   4989 C CD  . GLU B 1 193 ? 23.02000  43.71800  12.51700 1.000 27.88000 ? 193 GLU B CD  1 
ATOM   4990 O OE1 . GLU B 1 193 ? 23.69600  44.60900  13.07200 1.000 27.88000 ? 193 GLU B OE1 1 
ATOM   4991 O OE2 . GLU B 1 193 ? 23.49600  42.61500  12.17400 1.000 27.88000 ? 193 GLU B OE2 1 
ATOM   4992 N N   . HIS B 1 194 ? 19.32000  47.27600  14.61900 1.000 22.11000 ? 194 HIS B N   1 
ATOM   4993 C CA  . HIS B 1 194 ? 19.09000  48.62700  15.11200 1.000 22.11000 ? 194 HIS B CA  1 
ATOM   4994 C C   . HIS B 1 194 ? 18.50200  48.66900  16.51700 1.000 22.11000 ? 194 HIS B C   1 
ATOM   4995 O O   . HIS B 1 194 ? 18.51600  49.73400  17.14400 1.000 22.11000 ? 194 HIS B O   1 
ATOM   4996 C CB  . HIS B 1 194 ? 18.15700  49.37800  14.16000 1.000 22.11000 ? 194 HIS B CB  1 
ATOM   4997 C CG  . HIS B 1 194 ? 16.77900  48.79700  14.09000 1.000 22.11000 ? 194 HIS B CG  1 
ATOM   4998 N ND1 . HIS B 1 194 ? 15.76300  49.19000  14.93300 1.000 22.11000 ? 194 HIS B ND1 1 
ATOM   4999 C CD2 . HIS B 1 194 ? 16.25300  47.84400  13.28500 1.000 22.11000 ? 194 HIS B CD2 1 
ATOM   5000 C CE1 . HIS B 1 194 ? 14.66700  48.51000  14.64600 1.000 22.11000 ? 194 HIS B CE1 1 
ATOM   5001 N NE2 . HIS B 1 194 ? 14.93800  47.68600  13.65000 1.000 22.11000 ? 194 HIS B NE2 1 
ATOM   5002 N N   . LEU B 1 195 ? 17.99700  47.54900  17.02400 1.000 20.74000 ? 195 LEU B N   1 
ATOM   5003 C CA  . LEU B 1 195 ? 17.30000  47.56000  18.29800 1.000 20.74000 ? 195 LEU B CA  1 
ATOM   5004 C C   . LEU B 1 195 ? 18.28100  47.72500  19.45900 1.000 20.74000 ? 195 LEU B C   1 
ATOM   5005 O O   . LEU B 1 195 ? 19.41300  47.23900  19.40100 1.000 20.74000 ? 195 LEU B O   1 
ATOM   5006 C CB  . LEU B 1 195 ? 16.49100  46.28100  18.47900 1.000 20.74000 ? 195 LEU B CB  1 
ATOM   5007 C CG  . LEU B 1 195 ? 15.12800  46.27900  17.78600 1.000 20.74000 ? 195 LEU B CG  1 
ATOM   5008 C CD1 . LEU B 1 195 ? 14.37100  45.00600  18.11500 1.000 20.74000 ? 195 LEU B CD1 1 
ATOM   5009 C CD2 . LEU B 1 195 ? 14.32600  47.50700  18.19000 1.000 20.74000 ? 195 LEU B CD2 1 
ATOM   5010 N N   . PRO B 1 196 ? 17.87100  48.41700  20.52000 1.000 17.99000 ? 196 PRO B N   1 
ATOM   5011 C CA  . PRO B 1 196 ? 18.72100  48.50900  21.71000 1.000 17.99000 ? 196 PRO B CA  1 
ATOM   5012 C C   . PRO B 1 196 ? 18.94100  47.14000  22.33700 1.000 17.99000 ? 196 PRO B C   1 
ATOM   5013 O O   . PRO B 1 196 ? 18.05700  46.28200  22.32800 1.000 17.99000 ? 196 PRO B O   1 
ATOM   5014 C CB  . PRO B 1 196 ? 17.92900  49.43600  22.64200 1.000 17.99000 ? 196 PRO B CB  1 
ATOM   5015 C CG  . PRO B 1 196 ? 16.51000  49.30900  22.18000 1.000 17.99000 ? 196 PRO B CG  1 
ATOM   5016 C CD  . PRO B 1 196 ? 16.59200  49.12800  20.69500 1.000 17.99000 ? 196 PRO B CD  1 
ATOM   5017 N N   . SER B 1 197 ? 20.13800  46.94000  22.88100 1.000 15.81000 ? 197 SER B N   1 
ATOM   5018 C CA  . SER B 1 197 ? 20.48800  45.68900  23.54200 1.000 15.81000 ? 197 SER B CA  1 
ATOM   5019 C C   . SER B 1 197 ? 20.16100  45.79200  25.02700 1.000 15.81000 ? 197 SER B C   1 
ATOM   5020 O O   . SER B 1 197 ? 20.75600  46.60400  25.74400 1.000 15.81000 ? 197 SER B O   1 
ATOM   5021 C CB  . SER B 1 197 ? 21.96600  45.36000  23.33700 1.000 15.81000 ? 197 SER B CB  1 
ATOM   5022 O OG  . SER B 1 197 ? 22.29500  44.11300  23.92400 1.000 15.81000 ? 197 SER B OG  1 
ATOM   5023 N N   . TYR B 1 198 ? 19.22800  44.96400  25.48800 1.000 15.77000 ? 198 TYR B N   1 
ATOM   5024 C CA  . TYR B 1 198 ? 18.86700  44.89600  26.89600 1.000 15.77000 ? 198 TYR B CA  1 
ATOM   5025 C C   . TYR B 1 198 ? 19.72300  43.89700  27.66600 1.000 15.77000 ? 198 TYR B C   1 
ATOM   5026 O O   . TYR B 1 198 ? 19.36500  43.52300  28.78800 1.000 15.77000 ? 198 TYR B O   1 
ATOM   5027 C CB  . TYR B 1 198 ? 17.38500  44.54000  27.04700 1.000 15.77000 ? 198 TYR B CB  1 
ATOM   5028 C CG  . TYR B 1 198 ? 16.45100  45.52100  26.37800 1.000 15.77000 ? 198 TYR B CG  1 
ATOM   5029 C CD1 . TYR B 1 198 ? 16.76900  46.87100  26.30000 1.000 15.77000 ? 198 TYR B CD1 1 
ATOM   5030 C CD2 . TYR B 1 198 ? 15.25300  45.09800  25.82000 1.000 15.77000 ? 198 TYR B CD2 1 
ATOM   5031 C CE1 . TYR B 1 198 ? 15.91800  47.77200  25.68700 1.000 15.77000 ? 198 TYR B CE1 1 
ATOM   5032 C CE2 . TYR B 1 198 ? 14.39500  45.99100  25.20500 1.000 15.77000 ? 198 TYR B CE2 1 
ATOM   5033 C CZ  . TYR B 1 198 ? 14.73300  47.32700  25.14200 1.000 15.77000 ? 198 TYR B CZ  1 
ATOM   5034 O OH  . TYR B 1 198 ? 13.88400  48.22100  24.53100 1.000 15.77000 ? 198 TYR B OH  1 
ATOM   5035 N N   . LEU B 1 199 ? 20.83700  43.46100  27.08300 1.000 13.11000 ? 199 LEU B N   1 
ATOM   5036 C CA  . LEU B 1 199 ? 21.66300  42.42900  27.69100 1.000 13.11000 ? 199 LEU B CA  1 
ATOM   5037 C C   . LEU B 1 199 ? 22.23200  42.89900  29.02400 1.000 13.11000 ? 199 LEU B C   1 
ATOM   5038 O O   . LEU B 1 199 ? 22.57000  44.07400  29.19500 1.000 13.11000 ? 199 LEU B O   1 
ATOM   5039 C CB  . LEU B 1 199 ? 22.79900  42.04700  26.74200 1.000 13.11000 ? 199 LEU B CB  1 
ATOM   5040 C CG  . LEU B 1 199 ? 23.62400  40.81700  27.11400 1.000 13.11000 ? 199 LEU B CG  1 
ATOM   5041 C CD1 . LEU B 1 199 ? 22.75600  39.57200  27.06900 1.000 13.11000 ? 199 LEU B CD1 1 
ATOM   5042 C CD2 . LEU B 1 199 ? 24.81500  40.67900  26.18400 1.000 13.11000 ? 199 LEU B CD2 1 
ATOM   5043 N N   . ASP B 1 200 ? 22.31500  41.96800  29.97400 1.000 13.22000 ? 200 ASP B N   1 
ATOM   5044 C CA  . ASP B 1 200 ? 22.88400  42.13300  31.30900 1.000 13.22000 ? 200 ASP B CA  1 
ATOM   5045 C C   . ASP B 1 200 ? 22.05500  43.04300  32.20400 1.000 13.22000 ? 200 ASP B C   1 
ATOM   5046 O O   . ASP B 1 200 ? 22.45400  43.28700  33.35000 1.000 13.22000 ? 200 ASP B O   1 
ATOM   5047 C CB  . ASP B 1 200 ? 24.32400  42.66500  31.26600 1.000 13.22000 ? 200 ASP B CB  1 
ATOM   5048 C CG  . ASP B 1 200 ? 25.20300  41.88400  30.31300 1.000 13.22000 ? 200 ASP B CG  1 
ATOM   5049 O OD1 . ASP B 1 200 ? 25.26400  40.64200  30.44000 1.000 13.22000 ? 200 ASP B OD1 1 
ATOM   5050 O OD2 . ASP B 1 200 ? 25.81900  42.51100  29.42600 1.000 13.22000 ? 200 ASP B OD2 1 
ATOM   5051 N N   . LEU B 1 201 ? 20.91600  43.54400  31.73700 1.000 11.03000 ? 201 LEU B N   1 
ATOM   5052 C CA  . LEU B 1 201 ? 20.08300  44.41200  32.55700 1.000 11.03000 ? 201 LEU B CA  1 
ATOM   5053 C C   . LEU B 1 201 ? 19.29000  43.56900  33.54600 1.000 11.03000 ? 201 LEU B C   1 
ATOM   5054 O O   . LEU B 1 201 ? 18.46300  42.74500  33.14500 1.000 11.03000 ? 201 LEU B O   1 
ATOM   5055 C CB  . LEU B 1 201 ? 19.14300  45.23900  31.68400 1.000 11.03000 ? 201 LEU B CB  1 
ATOM   5056 C CG  . LEU B 1 201 ? 19.78500  46.24800  30.73200 1.000 11.03000 ? 201 LEU B CG  1 
ATOM   5057 C CD1 . LEU B 1 201 ? 18.71000  47.07500  30.04700 1.000 11.03000 ? 201 LEU B CD1 1 
ATOM   5058 C CD2 . LEU B 1 201 ? 20.77000  47.14400  31.46900 1.000 11.03000 ? 201 LEU B CD2 1 
ATOM   5059 N N   . HIS B 1 202 ? 19.54800  43.76600  34.83400 1.000 11.26000 ? 202 HIS B N   1 
ATOM   5060 C CA  . HIS B 1 202 ? 18.71400  43.15600  35.85500 1.000 11.26000 ? 202 HIS B CA  1 
ATOM   5061 C C   . HIS B 1 202 ? 17.35600  43.84400  35.89300 1.000 11.26000 ? 202 HIS B C   1 
ATOM   5062 O O   . HIS B 1 202 ? 17.23500  45.04300  35.62900 1.000 11.26000 ? 202 HIS B O   1 
ATOM   5063 C CB  . HIS B 1 202 ? 19.38100  43.24200  37.22800 1.000 11.26000 ? 202 HIS B CB  1 
ATOM   5064 C CG  . HIS B 1 202 ? 20.66900  42.48500  37.32700 1.000 11.26000 ? 202 HIS B CG  1 
ATOM   5065 N ND1 . HIS B 1 202 ? 21.73200  42.70900  36.47900 1.000 11.26000 ? 202 HIS B ND1 1 
ATOM   5066 C CD2 . HIS B 1 202 ? 21.06600  41.51300  38.18100 1.000 11.26000 ? 202 HIS B CD2 1 
ATOM   5067 C CE1 . HIS B 1 202 ? 22.72800  41.90400  36.80400 1.000 11.26000 ? 202 HIS B CE1 1 
ATOM   5068 N NE2 . HIS B 1 202 ? 22.35000  41.16800  37.83300 1.000 11.26000 ? 202 HIS B NE2 1 
ATOM   5069 N N   . TYR B 1 203 ? 16.32800  43.07400  36.22300 1.000 12.85000 ? 203 TYR B N   1 
ATOM   5070 C CA  . TYR B 1 203 ? 15.00100  43.64000  36.37600 1.000 12.85000 ? 203 TYR B CA  1 
ATOM   5071 C C   . TYR B 1 203 ? 14.41300  43.21200  37.71100 1.000 12.85000 ? 203 TYR B C   1 
ATOM   5072 O O   . TYR B 1 203 ? 14.69300  42.11100  38.19600 1.000 12.85000 ? 203 TYR B O   1 
ATOM   5073 C CB  . TYR B 1 203 ? 14.07600  43.20400  35.23100 1.000 12.85000 ? 203 TYR B CB  1 
ATOM   5074 C CG  . TYR B 1 203 ? 14.51100  43.72400  33.88000 1.000 12.85000 ? 203 TYR B CG  1 
ATOM   5075 C CD1 . TYR B 1 203 ? 14.17100  45.00400  33.46600 1.000 12.85000 ? 203 TYR B CD1 1 
ATOM   5076 C CD2 . TYR B 1 203 ? 15.26600  42.93800  33.02100 1.000 12.85000 ? 203 TYR B CD2 1 
ATOM   5077 C CE1 . TYR B 1 203 ? 14.56800  45.48700  32.23100 1.000 12.85000 ? 203 TYR B CE1 1 
ATOM   5078 C CE2 . TYR B 1 203 ? 15.66700  43.41200  31.78400 1.000 12.85000 ? 203 TYR B CE2 1 
ATOM   5079 C CZ  . TYR B 1 203 ? 15.31600  44.68700  31.39500 1.000 12.85000 ? 203 TYR B CZ  1 
ATOM   5080 O OH  . TYR B 1 203 ? 15.71100  45.16600  30.16700 1.000 12.85000 ? 203 TYR B OH  1 
ATOM   5081 N N   . PRO B 1 204 ? 13.59800  44.06400  38.32400 1.000 17.12000 ? 204 PRO B N   1 
ATOM   5082 C CA  . PRO B 1 204 ? 13.04200  43.73600  39.64000 1.000 17.12000 ? 204 PRO B CA  1 
ATOM   5083 C C   . PRO B 1 204 ? 12.11700  42.53200  39.58700 1.000 17.12000 ? 204 PRO B C   1 
ATOM   5084 O O   . PRO B 1 204 ? 11.45200  42.27000  38.58200 1.000 17.12000 ? 204 PRO B O   1 
ATOM   5085 C CB  . PRO B 1 204 ? 12.27800  45.00800  40.03000 1.000 17.12000 ? 204 PRO B CB  1 
ATOM   5086 C CG  . PRO B 1 204 ? 11.99500  45.69300  38.73700 1.000 17.12000 ? 204 PRO B CG  1 
ATOM   5087 C CD  . PRO B 1 204 ? 13.17300  45.39600  37.86300 1.000 17.12000 ? 204 PRO B CD  1 
ATOM   5088 N N   . ALA B 1 205 ? 12.09100  41.79000  40.69600 1.000 18.86000 ? 205 ALA B N   1 
ATOM   5089 C CA  . ALA B 1 205 ? 11.16800  40.66900  40.82400 1.000 18.86000 ? 205 ALA B CA  1 
ATOM   5090 C C   . ALA B 1 205 ? 9.71700   41.12100  40.75300 1.000 18.86000 ? 205 ALA B C   1 
ATOM   5091 O O   . ALA B 1 205 ? 8.83900   40.31200  40.43500 1.000 18.86000 ? 205 ALA B O   1 
ATOM   5092 C CB  . ALA B 1 205 ? 11.42000  39.92700  42.13600 1.000 18.86000 ? 205 ALA B CB  1 
ATOM   5093 N N   . SER B 1 206 ? 9.44900   42.39300  41.04700 1.000 22.95000 ? 206 SER B N   1 
ATOM   5094 C CA  . SER B 1 206 ? 8.08800   42.90800  40.99100 1.000 22.95000 ? 206 SER B CA  1 
ATOM   5095 C C   . SER B 1 206 ? 7.50200   42.84900  39.58500 1.000 22.95000 ? 206 SER B C   1 
ATOM   5096 O O   . SER B 1 206 ? 6.27400   42.84200  39.43700 1.000 22.95000 ? 206 SER B O   1 
ATOM   5097 C CB  . SER B 1 206 ? 8.06200   44.34600  41.51300 1.000 22.95000 ? 206 SER B CB  1 
ATOM   5098 O OG  . SER B 1 206 ? 8.75100   44.45300  42.74800 1.000 22.95000 ? 206 SER B OG  1 
ATOM   5099 N N   . ASP B 1 207 ? 8.34700   42.81800  38.54900 1.000 26.09000 ? 207 ASP B N   1 
ATOM   5100 C CA  . ASP B 1 207 ? 7.83600   42.77400  37.18200 1.000 26.09000 ? 207 ASP B CA  1 
ATOM   5101 C C   . ASP B 1 207 ? 7.04400   41.50200  36.90800 1.000 26.09000 ? 207 ASP B C   1 
ATOM   5102 O O   . ASP B 1 207 ? 6.10800   41.51800  36.10100 1.000 26.09000 ? 207 ASP B O   1 
ATOM   5103 C CB  . ASP B 1 207 ? 8.98900   42.89700  36.18500 1.000 26.09000 ? 207 ASP B CB  1 
ATOM   5104 C CG  . ASP B 1 207 ? 9.34000   44.33400  35.87900 1.000 26.09000 ? 207 ASP B CG  1 
ATOM   5105 O OD1 . ASP B 1 207 ? 8.41600   45.11000  35.55500 1.000 26.09000 ? 207 ASP B OD1 1 
ATOM   5106 O OD2 . ASP B 1 207 ? 10.53500  44.68800  35.96800 1.000 26.09000 ? 207 ASP B OD2 1 
ATOM   5107 N N   . ILE B 1 208 ? 7.38800   40.40400  37.56700 1.000 25.86000 ? 208 ILE B N   1 
ATOM   5108 C CA  . ILE B 1 208 ? 6.70300   39.13000  37.40000 1.000 25.86000 ? 208 ILE B CA  1 
ATOM   5109 C C   . ILE B 1 208 ? 6.14800   38.71200  38.75700 1.000 25.86000 ? 208 ILE B C   1 
ATOM   5110 O O   . ILE B 1 208 ? 6.86600   38.15800  39.59000 1.000 25.86000 ? 208 ILE B O   1 
ATOM   5111 C CB  . ILE B 1 208 ? 7.64000   38.05100  36.82500 1.000 25.86000 ? 208 ILE B CB  1 
ATOM   5112 C CG1 . ILE B 1 208 ? 8.38600   38.57300  35.59700 1.000 25.86000 ? 208 ILE B CG1 1 
ATOM   5113 C CG2 . ILE B 1 208 ? 6.85300   36.82000  36.42100 1.000 25.86000 ? 208 ILE B CG2 1 
ATOM   5114 C CD1 . ILE B 1 208 ? 9.79700   39.01500  35.88400 1.000 25.86000 ? 208 ILE B CD1 1 
ATOM   5115 N N   . PRO B 1 209 ? 4.86600   38.96900  39.01500 1.000 30.53000 ? 209 PRO B N   1 
ATOM   5116 C CA  . PRO B 1 209 ? 4.27500   38.58500  40.30100 1.000 30.53000 ? 209 PRO B CA  1 
ATOM   5117 C C   . PRO B 1 209 ? 4.16400   37.07600  40.43200 1.000 30.53000 ? 209 PRO B C   1 
ATOM   5118 O O   . PRO B 1 209 ? 4.20500   36.33300  39.45000 1.000 30.53000 ? 209 PRO B O   1 
ATOM   5119 C CB  . PRO B 1 209 ? 2.88800   39.23800  40.27800 1.000 30.53000 ? 209 PRO B CB  1 
ATOM   5120 C CG  . PRO B 1 209 ? 2.95500   40.28000  39.21000 1.000 30.53000 ? 209 PRO B CG  1 
ATOM   5121 C CD  . PRO B 1 209 ? 3.93200   39.75700  38.19400 1.000 30.53000 ? 209 PRO B CD  1 
ATOM   5122 N N   . THR B 1 210 ? 4.04000   36.63100  41.68200 1.000 32.05000 ? 210 THR B N   1 
ATOM   5123 C CA  . THR B 1 210 ? 3.97900   35.20000  41.97700 1.000 32.05000 ? 210 THR B CA  1 
ATOM   5124 C C   . THR B 1 210 ? 2.91300   34.45100  41.18200 1.000 32.05000 ? 210 THR B C   1 
ATOM   5125 O O   . THR B 1 210 ? 3.23300   33.38500  40.63100 1.000 32.05000 ? 210 THR B O   1 
ATOM   5126 C CB  . THR B 1 210 ? 3.77200   34.99800  43.48700 1.000 32.05000 ? 210 THR B CB  1 
ATOM   5127 O OG1 . THR B 1 210 ? 4.77000   35.72200  44.21700 1.000 32.05000 ? 210 THR B OG1 1 
ATOM   5128 C CG2 . THR B 1 210 ? 3.86300   33.52600  43.85200 1.000 32.05000 ? 210 THR B CG2 1 
ATOM   5129 N N   . PRO B 1 211 ? 1.65100   34.90700  41.09100 1.000 32.83000 ? 211 PRO B N   1 
ATOM   5130 C CA  . PRO B 1 211 ? 0.68600   34.15600  40.26200 1.000 32.83000 ? 211 PRO B CA  1 
ATOM   5131 C C   . PRO B 1 211 ? 1.10200   34.03100  38.80500 1.000 32.83000 ? 211 PRO B C   1 
ATOM   5132 O O   . PRO B 1 211 ? 0.87700   32.98500  38.18300 1.000 32.83000 ? 211 PRO B O   1 
ATOM   5133 C CB  . PRO B 1 211 ? -0.61300  34.96500  40.41100 1.000 32.83000 ? 211 PRO B CB  1 
ATOM   5134 C CG  . PRO B 1 211 ? -0.42300  35.81100  41.61300 1.000 32.83000 ? 211 PRO B CG  1 
ATOM   5135 C CD  . PRO B 1 211 ? 1.03500   36.11600  41.67300 1.000 32.83000 ? 211 PRO B CD  1 
ATOM   5136 N N   . ALA B 1 212 ? 1.73900   35.06700  38.24800 1.000 31.00000 ? 212 ALA B N   1 
ATOM   5137 C CA  . ALA B 1 212 ? 2.23500   34.98300  36.87900 1.000 31.00000 ? 212 ALA B CA  1 
ATOM   5138 C C   . ALA B 1 212 ? 3.38200   33.99200  36.76500 1.000 31.00000 ? 212 ALA B C   1 
ATOM   5139 O O   . ALA B 1 212 ? 3.48300   33.25900  35.77200 1.000 31.00000 ? 212 ALA B O   1 
ATOM   5140 C CB  . ALA B 1 212 ? 2.68400   36.36000  36.39900 1.000 31.00000 ? 212 ALA B CB  1 
ATOM   5141 N N   . ARG B 1 213 ? 4.25600   33.95200  37.77200 1.000 27.83000 ? 213 ARG B N   1 
ATOM   5142 C CA  . ARG B 1 213 ? 5.33300   32.97200  37.76800 1.000 27.83000 ? 213 ARG B CA  1 
ATOM   5143 C C   . ARG B 1 213 ? 4.78000   31.55700  37.82400 1.000 27.83000 ? 213 ARG B C   1 
ATOM   5144 O O   . ARG B 1 213 ? 5.28600   30.65700  37.14600 1.000 27.83000 ? 213 ARG B O   1 
ATOM   5145 C CB  . ARG B 1 213 ? 6.27700   33.22500  38.94300 1.000 27.83000 ? 213 ARG B CB  1 
ATOM   5146 C CG  . ARG B 1 213 ? 7.45600   34.11800  38.61900 1.000 27.83000 ? 213 ARG B CG  1 
ATOM   5147 C CD  . ARG B 1 213 ? 8.23600   34.45800  39.87400 1.000 27.83000 ? 213 ARG B CD  1 
ATOM   5148 N NE  . ARG B 1 213 ? 7.57500   35.47000  40.68900 1.000 27.83000 ? 213 ARG B NE  1 
ATOM   5149 C CZ  . ARG B 1 213 ? 7.85600   35.70300  41.96400 1.000 27.83000 ? 213 ARG B CZ  1 
ATOM   5150 N NH1 . ARG B 1 213 ? 8.75600   34.98400  42.61500 1.000 27.83000 ? 213 ARG B NH1 1 
ATOM   5151 N NH2 . ARG B 1 213 ? 7.21500   36.67600  42.60400 1.000 27.83000 ? 213 ARG B NH2 1 
ATOM   5152 N N   . LYS B 1 214 ? 3.70800   31.35100  38.59200 1.000 33.37000 ? 214 LYS B N   1 
ATOM   5153 C CA  . LYS B 1 214 ? 3.11100   30.02100  38.66800 1.000 33.37000 ? 214 LYS B CA  1 
ATOM   5154 C C   . LYS B 1 214 ? 2.43600   29.64700  37.35500 1.000 33.37000 ? 214 LYS B C   1 
ATOM   5155 O O   . LYS B 1 214 ? 2.54200   28.50200  36.89800 1.000 33.37000 ? 214 LYS B O   1 
ATOM   5156 C CB  . LYS B 1 214 ? 2.10900   29.95400  39.82100 1.000 33.37000 ? 214 LYS B CB  1 
ATOM   5157 C CG  . LYS B 1 214 ? 2.65900   30.39100  41.17200 1.000 33.37000 ? 214 LYS B CG  1 
ATOM   5158 C CD  . LYS B 1 214 ? 3.94900   29.67100  41.53200 1.000 33.37000 ? 214 LYS B CD  1 
ATOM   5159 C CE  . LYS B 1 214 ? 4.45400   30.12300  42.89400 1.000 33.37000 ? 214 LYS B CE  1 
ATOM   5160 N NZ  . LYS B 1 214 ? 5.75800   29.50500  43.25800 1.000 33.37000 ? 214 LYS B NZ  1 
ATOM   5161 N N   . LEU B 1 215 ? 1.74100   30.60100  36.73000 1.000 29.83000 ? 215 LEU B N   1 
ATOM   5162 C CA  . LEU B 1 215 ? 1.10500   30.31100  35.44900 1.000 29.83000 ? 215 LEU B CA  1 
ATOM   5163 C C   . LEU B 1 215 ? 2.14200   30.01600  34.37500 1.000 29.83000 ? 215 LEU B C   1 
ATOM   5164 O O   . LEU B 1 215 ? 1.91000   29.18200  33.49100 1.000 29.83000 ? 215 LEU B O   1 
ATOM   5165 C CB  . LEU B 1 215 ? 0.21500   31.47300  35.01600 1.000 29.83000 ? 215 LEU B CB  1 
ATOM   5166 C CG  . LEU B 1 215 ? -1.27500  31.27800  35.30500 1.000 29.83000 ? 215 LEU B CG  1 
ATOM   5167 C CD1 . LEU B 1 215 ? -2.11400  32.32500  34.58500 1.000 29.83000 ? 215 LEU B CD1 1 
ATOM   5168 C CD2 . LEU B 1 215 ? -1.69800  29.87700  34.90600 1.000 29.83000 ? 215 LEU B CD2 1 
ATOM   5169 N N   . TYR B 1 216 ? 3.29400   30.68800  34.42600 1.000 28.73000 ? 216 TYR B N   1 
ATOM   5170 C CA  . TYR B 1 216 ? 4.35900   30.35100  33.48700 1.000 28.73000 ? 216 TYR B CA  1 
ATOM   5171 C C   . TYR B 1 216 ? 5.02500   29.02800  33.84100 1.000 28.73000 ? 216 TYR B C   1 
ATOM   5172 O O   . TYR B 1 216 ? 5.56300   28.35300  32.95700 1.000 28.73000 ? 216 TYR B O   1 
ATOM   5173 C CB  . TYR B 1 216 ? 5.36900   31.49100  33.41500 1.000 28.73000 ? 216 TYR B CB  1 
ATOM   5174 C CG  . TYR B 1 216 ? 4.88100   32.59700  32.51500 1.000 28.73000 ? 216 TYR B CG  1 
ATOM   5175 C CD1 . TYR B 1 216 ? 4.02200   32.31200  31.46100 1.000 28.73000 ? 216 TYR B CD1 1 
ATOM   5176 C CD2 . TYR B 1 216 ? 5.25500   33.91700  32.72100 1.000 28.73000 ? 216 TYR B CD2 1 
ATOM   5177 C CE1 . TYR B 1 216 ? 3.55900   33.30300  30.63400 1.000 28.73000 ? 216 TYR B CE1 1 
ATOM   5178 C CE2 . TYR B 1 216 ? 4.79400   34.92200  31.89100 1.000 28.73000 ? 216 TYR B CE2 1 
ATOM   5179 C CZ  . TYR B 1 216 ? 3.94500   34.60300  30.84900 1.000 28.73000 ? 216 TYR B CZ  1 
ATOM   5180 O OH  . TYR B 1 216 ? 3.46500   35.57500  30.00800 1.000 28.73000 ? 216 TYR B OH  1 
ATOM   5181 N N   . SER B 1 217 ? 4.99700   28.63800  35.11700 1.000 27.41000 ? 217 SER B N   1 
ATOM   5182 C CA  . SER B 1 217 ? 5.43800   27.30000  35.49300 1.000 27.41000 ? 217 SER B CA  1 
ATOM   5183 C C   . SER B 1 217 ? 4.46900   26.22600  35.02100 1.000 27.41000 ? 217 SER B C   1 
ATOM   5184 O O   . SER B 1 217 ? 4.87300   25.07000  34.85800 1.000 27.41000 ? 217 SER B O   1 
ATOM   5185 C CB  . SER B 1 217 ? 5.62400   27.20900  37.00900 1.000 27.41000 ? 217 SER B CB  1 
ATOM   5186 O OG  . SER B 1 217 ? 6.68800   28.03700  37.44400 1.000 27.41000 ? 217 SER B OG  1 
ATOM   5187 N N   . GLN B 1 218 ? 3.20300   26.58100  34.80300 1.000 30.50000 ? 218 GLN B N   1 
ATOM   5188 C CA  . GLN B 1 218 ? 2.21000   25.63100  34.28300 1.000 30.50000 ? 218 GLN B CA  1 
ATOM   5189 C C   . GLN B 1 218 ? 2.18100   25.67200  32.75700 1.000 30.50000 ? 218 GLN B C   1 
ATOM   5190 O O   . GLN B 1 218 ? 2.56700   24.70400  32.09600 1.000 30.50000 ? 218 GLN B O   1 
ATOM   5191 C CB  . GLN B 1 218 ? 0.83400   25.91900  34.88700 1.000 30.50000 ? 218 GLN B CB  1 
ATOM   5192 C CG  . GLN B 1 218 ? 0.74100   25.60000  36.37500 1.000 30.50000 ? 218 GLN B CG  1 
ATOM   5193 C CD  . GLN B 1 218 ? -0.64400  25.84200  36.94700 1.000 30.50000 ? 218 GLN B CD  1 
ATOM   5194 O OE1 . GLN B 1 218 ? -1.53400  26.34300  36.25900 1.000 30.50000 ? 218 GLN B OE1 1 
ATOM   5195 N NE2 . GLN B 1 218 ? -0.83300  25.48300  38.21200 1.000 30.50000 ? 218 GLN B NE2 1 
ATOM   5196 N N   . ASN B 1 219 ? 1.72300   26.78500  32.18500 1.000 27.79000 ? 219 ASN B N   1 
ATOM   5197 C CA  . ASN B 1 219 ? 1.76400   26.94600  30.73500 1.000 27.79000 ? 219 ASN B CA  1 
ATOM   5198 C C   . ASN B 1 219 ? 3.20100   27.17900  30.28600 1.000 27.79000 ? 219 ASN B C   1 
ATOM   5199 O O   . ASN B 1 219 ? 3.84100   28.14900  30.70300 1.000 27.79000 ? 219 ASN B O   1 
ATOM   5200 C CB  . ASN B 1 219 ? 0.87100   28.10500  30.29800 1.000 27.79000 ? 219 ASN B CB  1 
ATOM   5201 C CG  . ASN B 1 219 ? -0.49500  27.64500  29.82100 1.000 27.79000 ? 219 ASN B CG  1 
ATOM   5202 O OD1 . ASN B 1 219 ? -0.63700  26.56400  29.24800 1.000 27.79000 ? 219 ASN B OD1 1 
ATOM   5203 N ND2 . ASN B 1 219 ? -1.50900  28.47200  30.05000 1.000 27.79000 ? 219 ASN B ND2 1 
ATOM   5204 N N   . TRP B 1 220 ? 3.70800   26.28900  29.43000 1.000 25.69000 ? 220 TRP B N   1 
ATOM   5205 C CA  . TRP B 1 220 ? 5.09000   26.37900  28.97900 1.000 25.69000 ? 220 TRP B CA  1 
ATOM   5206 C C   . TRP B 1 220 ? 5.29300   27.37000  27.84200 1.000 25.69000 ? 220 TRP B C   1 
ATOM   5207 O O   . TRP B 1 220 ? 6.42900   27.79600  27.60700 1.000 25.69000 ? 220 TRP B O   1 
ATOM   5208 C CB  . TRP B 1 220 ? 5.58200   24.99900  28.54700 1.000 25.69000 ? 220 TRP B CB  1 
ATOM   5209 C CG  . TRP B 1 220 ? 6.03400   24.16100  29.69000 1.000 25.69000 ? 220 TRP B CG  1 
ATOM   5210 C CD1 . TRP B 1 220 ? 5.29400   23.77800  30.77000 1.000 25.69000 ? 220 TRP B CD1 1 
ATOM   5211 C CD2 . TRP B 1 220 ? 7.33500   23.59600  29.87300 1.000 25.69000 ? 220 TRP B CD2 1 
ATOM   5212 N NE1 . TRP B 1 220 ? 6.05700   23.01100  31.61700 1.000 25.69000 ? 220 TRP B NE1 1 
ATOM   5213 C CE2 . TRP B 1 220 ? 7.31400   22.88300  31.08700 1.000 25.69000 ? 220 TRP B CE2 1 
ATOM   5214 C CE3 . TRP B 1 220 ? 8.51800   23.62400  29.12600 1.000 25.69000 ? 220 TRP B CE3 1 
ATOM   5215 C CZ2 . TRP B 1 220 ? 8.42900   22.20400  31.57300 1.000 25.69000 ? 220 TRP B CZ2 1 
ATOM   5216 C CZ3 . TRP B 1 220 ? 9.62300   22.95000  29.61100 1.000 25.69000 ? 220 TRP B CZ3 1 
ATOM   5217 C CH2 . TRP B 1 220 ? 9.57100   22.25100  30.82300 1.000 25.69000 ? 220 TRP B CH2 1 
ATOM   5218 N N   . LEU B 1 221 ? 4.23100   27.75800  27.14700 1.000 24.85000 ? 221 LEU B N   1 
ATOM   5219 C CA  . LEU B 1 221 ? 4.35200   28.70000  26.04800 1.000 24.85000 ? 221 LEU B CA  1 
ATOM   5220 C C   . LEU B 1 221 ? 3.20700   29.69300  26.13500 1.000 24.85000 ? 221 LEU B C   1 
ATOM   5221 O O   . LEU B 1 221 ? 2.06600   29.31300  26.41100 1.000 24.85000 ? 221 LEU B O   1 
ATOM   5222 C CB  . LEU B 1 221 ? 4.33300   27.98700  24.69200 1.000 24.85000 ? 221 LEU B CB  1 
ATOM   5223 C CG  . LEU B 1 221 ? 4.74400   28.82600  23.48300 1.000 24.85000 ? 221 LEU B CG  1 
ATOM   5224 C CD1 . LEU B 1 221 ? 6.25600   28.94100  23.39200 1.000 24.85000 ? 221 LEU B CD1 1 
ATOM   5225 C CD2 . LEU B 1 221 ? 4.17600   28.22100  22.22500 1.000 24.85000 ? 221 LEU B CD2 1 
ATOM   5226 N N   . ARG B 1 222 ? 3.51800   30.96300  25.89200 1.000 30.21000 ? 222 ARG B N   1 
ATOM   5227 C CA  . ARG B 1 222 ? 2.53200   32.02400  26.03200 1.000 30.21000 ? 222 ARG B CA  1 
ATOM   5228 C C   . ARG B 1 222 ? 2.68600   33.00300  24.88100 1.000 30.21000 ? 222 ARG B C   1 
ATOM   5229 O O   . ARG B 1 222 ? 3.80600   33.30000  24.45800 1.000 30.21000 ? 222 ARG B O   1 
ATOM   5230 C CB  . ARG B 1 222 ? 2.68400   32.74200  27.37900 1.000 30.21000 ? 222 ARG B CB  1 
ATOM   5231 C CG  . ARG B 1 222 ? 1.76600   33.93800  27.57600 1.000 30.21000 ? 222 ARG B CG  1 
ATOM   5232 C CD  . ARG B 1 222 ? 0.30400   33.55100  27.45700 1.000 30.21000 ? 222 ARG B CD  1 
ATOM   5233 N NE  . ARG B 1 222 ? -0.57100  34.68300  27.73500 1.000 30.21000 ? 222 ARG B NE  1 
ATOM   5234 C CZ  . ARG B 1 222 ? -1.88800  34.67000  27.58000 1.000 30.21000 ? 222 ARG B CZ  1 
ATOM   5235 N NH1 . ARG B 1 222 ? -2.52100  33.59700  27.13500 1.000 30.21000 ? 222 ARG B NH1 1 
ATOM   5236 N NH2 . ARG B 1 222 ? -2.58700  35.76100  27.87600 1.000 30.21000 ? 222 ARG B NH2 1 
ATOM   5237 N N   . LEU B 1 223 ? 1.55900   33.50000  24.37400 1.000 32.44000 ? 223 LEU B N   1 
ATOM   5238 C CA  . LEU B 1 223 ? 1.56600   34.37100  23.20900 1.000 32.44000 ? 223 LEU B CA  1 
ATOM   5239 C C   . LEU B 1 223 ? 0.55100   35.49100  23.35600 1.000 32.44000 ? 223 LEU B C   1 
ATOM   5240 O O   . LEU B 1 223 ? -0.56200  35.28200  23.84600 1.000 32.44000 ? 223 LEU B O   1 
ATOM   5241 C CB  . LEU B 1 223 ? 1.25800   33.59900  21.92300 1.000 32.44000 ? 223 LEU B CB  1 
ATOM   5242 C CG  . LEU B 1 223 ? 2.42100   32.91900  21.20800 1.000 32.44000 ? 223 LEU B CG  1 
ATOM   5243 C CD1 . LEU B 1 223 ? 2.71000   31.55500  21.81000 1.000 32.44000 ? 223 LEU B CD1 1 
ATOM   5244 C CD2 . LEU B 1 223 ? 2.10600   32.80900  19.73400 1.000 32.44000 ? 223 LEU B CD2 1 
ATOM   5245 N N   . ILE B 1 224 ? 0.95400   36.67900  22.92000 1.000 31.67000 ? 224 ILE B N   1 
ATOM   5246 C CA  . ILE B 1 224 ? 0.06600   37.81300  22.69400 1.000 31.67000 ? 224 ILE B CA  1 
ATOM   5247 C C   . ILE B 1 224 ? 0.30800   38.23600  21.25100 1.000 31.67000 ? 224 ILE B C   1 
ATOM   5248 O O   . ILE B 1 224 ? 1.25500   38.99200  20.98100 1.000 31.67000 ? 224 ILE B O   1 
ATOM   5249 C CB  . ILE B 1 224 ? 0.33100   38.95900  23.68100 1.000 31.67000 ? 224 ILE B CB  1 
ATOM   5250 C CG1 . ILE B 1 224 ? 0.53100   38.40900  25.09200 1.000 31.67000 ? 224 ILE B CG1 1 
ATOM   5251 C CG2 . ILE B 1 224 ? -0.82600  39.94300  23.67100 1.000 31.67000 ? 224 ILE B CG2 1 
ATOM   5252 C CD1 . ILE B 1 224 ? 1.08100   39.42400  26.05500 1.000 31.67000 ? 224 ILE B CD1 1 
ATOM   5253 N N   . PRO B 1 225 ? -0.45300  37.69900  20.29300 1.000 32.31000 ? 225 PRO B N   1 
ATOM   5254 C CA  . PRO B 1 225 ? -0.22000  38.04700  18.88200 1.000 32.31000 ? 225 PRO B CA  1 
ATOM   5255 C C   . PRO B 1 225 ? -0.34600  39.52900  18.58200 1.000 32.31000 ? 225 PRO B C   1 
ATOM   5256 O O   . PRO B 1 225 ? 0.34900   40.03200  17.69100 1.000 32.31000 ? 225 PRO B O   1 
ATOM   5257 C CB  . PRO B 1 225 ? -1.28800  37.23100  18.14200 1.000 32.31000 ? 225 PRO B CB  1 
ATOM   5258 C CG  . PRO B 1 225 ? -1.57300  36.08300  19.04800 1.000 32.31000 ? 225 PRO B CG  1 
ATOM   5259 C CD  . PRO B 1 225 ? -1.46000  36.63500  20.43900 1.000 32.31000 ? 225 PRO B CD  1 
ATOM   5260 N N   . ASP B 1 226 ? -1.22600  40.24300  19.28100 1.000 38.21000 ? 226 ASP B N   1 
ATOM   5261 C CA  . ASP B 1 226 ? -1.45200  41.66400  19.03000 1.000 38.21000 ? 226 ASP B CA  1 
ATOM   5262 C C   . ASP B 1 226 ? -1.61900  42.35200  20.37700 1.000 38.21000 ? 226 ASP B C   1 
ATOM   5263 O O   . ASP B 1 226 ? -2.63200  42.15100  21.05100 1.000 38.21000 ? 226 ASP B O   1 
ATOM   5264 C CB  . ASP B 1 226 ? -2.68100  41.87300  18.14500 1.000 38.21000 ? 226 ASP B CB  1 
ATOM   5265 C CG  . ASP B 1 226 ? -2.77500  43.28300  17.58900 1.000 38.21000 ? 226 ASP B CG  1 
ATOM   5266 O OD1 . ASP B 1 226 ? -2.62100  44.25000  18.36300 1.000 38.21000 ? 226 ASP B OD1 1 
ATOM   5267 O OD2 . ASP B 1 226 ? -3.00400  43.41900  16.36800 1.000 38.21000 ? 226 ASP B OD2 1 
ATOM   5268 N N   . ALA B 1 227 ? -0.63300  43.16500  20.76500 1.000 39.65000 ? 227 ALA B N   1 
ATOM   5269 C CA  . ALA B 1 227 ? -0.71200  43.85900  22.04700 1.000 39.65000 ? 227 ALA B CA  1 
ATOM   5270 C C   . ALA B 1 227 ? -1.86000  44.86000  22.08000 1.000 39.65000 ? 227 ALA B C   1 
ATOM   5271 O O   . ALA B 1 227 ? -2.37600  45.17400  23.15900 1.000 39.65000 ? 227 ALA B O   1 
ATOM   5272 C CB  . ALA B 1 227 ? 0.61300   44.55800  22.34900 1.000 39.65000 ? 227 ALA B CB  1 
ATOM   5273 N N   . ASP B 1 228 ? -2.27600  45.36000  20.92000 1.000 41.38000 ? 228 ASP B N   1 
ATOM   5274 C CA  . ASP B 1 228 ? -3.35600  46.33200  20.81800 1.000 41.38000 ? 228 ASP B CA  1 
ATOM   5275 C C   . ASP B 1 228 ? -4.72800  45.67500  20.73000 1.000 41.38000 ? 228 ASP B C   1 
ATOM   5276 O O   . ASP B 1 228 ? -5.69700  46.34200  20.35500 1.000 41.38000 ? 228 ASP B O   1 
ATOM   5277 C CB  . ASP B 1 228 ? -3.13200  47.24200  19.60700 1.000 41.38000 ? 228 ASP B CB  1 
ATOM   5278 C CG  . ASP B 1 228 ? -1.77600  47.92300  19.63200 1.000 41.38000 ? 228 ASP B CG  1 
ATOM   5279 O OD1 . ASP B 1 228 ? -1.34900  48.36000  20.72100 1.000 41.38000 ? 228 ASP B OD1 1 
ATOM   5280 O OD2 . ASP B 1 228 ? -1.13400  48.01400  18.56300 1.000 41.38000 ? 228 ASP B OD2 1 
ATOM   5281 N N   . TYR B 1 229 ? -4.82600  44.38700  21.05200 1.000 40.38000 ? 229 TYR B N   1 
ATOM   5282 C CA  . TYR B 1 229 ? -6.08200  43.66300  20.92300 1.000 40.38000 ? 229 TYR B CA  1 
ATOM   5283 C C   . TYR B 1 229 ? -7.13900  44.20800  21.87700 1.000 40.38000 ? 229 TYR B C   1 
ATOM   5284 O O   . TYR B 1 229 ? -6.83900  44.66900  22.98200 1.000 40.38000 ? 229 TYR B O   1 
ATOM   5285 C CB  . TYR B 1 229 ? -5.87100  42.16900  21.19500 1.000 40.38000 ? 229 TYR B CB  1 
ATOM   5286 C CG  . TYR B 1 229 ? -5.76700  41.78900  22.66600 1.000 40.38000 ? 229 TYR B CG  1 
ATOM   5287 C CD1 . TYR B 1 229 ? -6.90200  41.49500  23.41600 1.000 40.38000 ? 229 TYR B CD1 1 
ATOM   5288 C CD2 . TYR B 1 229 ? -4.53400  41.70700  23.29900 1.000 40.38000 ? 229 TYR B CD2 1 
ATOM   5289 C CE1 . TYR B 1 229 ? -6.81200  41.14700  24.74900 1.000 40.38000 ? 229 TYR B CE1 1 
ATOM   5290 C CE2 . TYR B 1 229 ? -4.43500  41.35600  24.63200 1.000 40.38000 ? 229 TYR B CE2 1 
ATOM   5291 C CZ  . TYR B 1 229 ? -5.57700  41.07800  25.35100 1.000 40.38000 ? 229 TYR B CZ  1 
ATOM   5292 O OH  . TYR B 1 229 ? -5.48600  40.72900  26.67700 1.000 40.38000 ? 229 TYR B OH  1 
ATOM   5293 N N   . GLN B 1 230 ? -8.39100  44.15500  21.43200 1.000 45.91000 ? 230 GLN B N   1 
ATOM   5294 C CA  . GLN B 1 230 ? -9.53300  44.34500  22.31400 1.000 45.91000 ? 230 GLN B CA  1 
ATOM   5295 C C   . GLN B 1 230 ? -9.99000  42.98300  22.82200 1.000 45.91000 ? 230 GLN B C   1 
ATOM   5296 O O   . GLN B 1 230 ? -10.23500 42.07000  22.02700 1.000 45.91000 ? 230 GLN B O   1 
ATOM   5297 C CB  . GLN B 1 230 ? -10.67300 45.05800  21.58700 1.000 45.91000 ? 230 GLN B CB  1 
ATOM   5298 C CG  . GLN B 1 230 ? -11.87400 45.36900  22.46900 1.000 45.91000 ? 230 GLN B CG  1 
ATOM   5299 C CD  . GLN B 1 230 ? -11.57900 46.43400  23.50900 1.000 45.91000 ? 230 GLN B CD  1 
ATOM   5300 O OE1 . GLN B 1 230 ? -10.93400 47.44100  23.21600 1.000 45.91000 ? 230 GLN B OE1 1 
ATOM   5301 N NE2 . GLN B 1 230 ? -12.04800 46.21500  24.73200 1.000 45.91000 ? 230 GLN B NE2 1 
ATOM   5302 N N   . ALA B 1 231 ? -10.10400 42.85200  24.14000 1.000 47.75000 ? 231 ALA B N   1 
ATOM   5303 C CA  . ALA B 1 231 ? -10.42900 41.56600  24.74200 1.000 47.75000 ? 231 ALA B CA  1 
ATOM   5304 C C   . ALA B 1 231 ? -11.84500 41.13200  24.38100 1.000 47.75000 ? 231 ALA B C   1 
ATOM   5305 O O   . ALA B 1 231 ? -12.76000 41.95400  24.27900 1.000 47.75000 ? 231 ALA B O   1 
ATOM   5306 C CB  . ALA B 1 231 ? -10.27000 41.63700  26.26000 1.000 47.75000 ? 231 ALA B CB  1 
ATOM   5307 N N   . ALA B 1 232 ? -12.01900 39.82600  24.18300 1.000 46.82000 ? 232 ALA B N   1 
ATOM   5308 C CA  . ALA B 1 232 ? -13.31800 39.23500  23.87500 1.000 46.82000 ? 232 ALA B CA  1 
ATOM   5309 C C   . ALA B 1 232 ? -13.86400 38.56300  25.13200 1.000 46.82000 ? 232 ALA B C   1 
ATOM   5310 O O   . ALA B 1 232 ? -13.30200 37.57100  25.60700 1.000 46.82000 ? 232 ALA B O   1 
ATOM   5311 C CB  . ALA B 1 232 ? -13.20100 38.23800  22.72500 1.000 46.82000 ? 232 ALA B CB  1 
ATOM   5312 N N   . ALA B 1 233 ? -14.96000 39.10000  25.66300 1.000 49.09000 ? 233 ALA B N   1 
ATOM   5313 C CA  . ALA B 1 233 ? -15.56100 38.55000  26.87000 1.000 49.09000 ? 233 ALA B CA  1 
ATOM   5314 C C   . ALA B 1 233 ? -16.22300 37.20400  26.59300 1.000 49.09000 ? 233 ALA B C   1 
ATOM   5315 O O   . ALA B 1 233 ? -16.69800 36.93400  25.48700 1.000 49.09000 ? 233 ALA B O   1 
ATOM   5316 C CB  . ALA B 1 233 ? -16.59000 39.52000  27.44700 1.000 49.09000 ? 233 ALA B CB  1 
ATOM   5317 N N   . ILE B 1 234 ? -16.24200 36.35300  27.61600 1.000 50.76000 ? 234 ILE B N   1 
ATOM   5318 C CA  . ILE B 1 234 ? -16.93200 35.07000  27.56300 1.000 50.76000 ? 234 ILE B CA  1 
ATOM   5319 C C   . ILE B 1 234 ? -18.27800 35.21400  28.26100 1.000 50.76000 ? 234 ILE B C   1 
ATOM   5320 O O   . ILE B 1 234 ? -18.34500 35.63300  29.42200 1.000 50.76000 ? 234 ILE B O   1 
ATOM   5321 C CB  . ILE B 1 234 ? -16.09300 33.95300  28.20100 1.000 50.76000 ? 234 ILE B CB  1 
ATOM   5322 C CG1 . ILE B 1 234 ? -14.85600 33.66700  27.34900 1.000 50.76000 ? 234 ILE B CG1 1 
ATOM   5323 C CG2 . ILE B 1 234 ? -16.92600 32.69400  28.37800 1.000 50.76000 ? 234 ILE B CG2 1 
ATOM   5324 C CD1 . ILE B 1 234 ? -14.03900 32.49700  27.84400 1.000 50.76000 ? 234 ILE B CD1 1 
ATOM   5325 N N   . VAL B 1 235 ? -19.34300 34.86700  27.55100 1.000 52.73000 ? 235 VAL B N   1 
ATOM   5326 C CA  . VAL B 1 235 ? -20.71700 34.93300  28.04100 1.000 52.73000 ? 235 VAL B CA  1 
ATOM   5327 C C   . VAL B 1 235 ? -21.18900 33.51300  28.33400 1.000 52.73000 ? 235 VAL B C   1 
ATOM   5328 O O   . VAL B 1 235 ? -21.14400 32.65800  27.43900 1.000 52.73000 ? 235 VAL B O   1 
ATOM   5329 C CB  . VAL B 1 235 ? -21.64900 35.62500  27.03100 1.000 52.73000 ? 235 VAL B CB  1 
ATOM   5330 C CG1 . VAL B 1 235 ? -21.53200 37.13400  27.14600 1.000 52.73000 ? 235 VAL B CG1 1 
ATOM   5331 C CG2 . VAL B 1 235 ? -21.33900 35.17500  25.60500 1.000 52.73000 ? 235 VAL B CG2 1 
ATOM   5332 N N   . PRO B 1 236 ? -21.62500 33.20200  29.56200 1.000 52.71000 ? 236 PRO B N   1 
ATOM   5333 C CA  . PRO B 1 236 ? -21.54800 33.99800  30.80200 1.000 52.71000 ? 236 PRO B CA  1 
ATOM   5334 C C   . PRO B 1 236 ? -20.13900 34.04400  31.39000 1.000 52.71000 ? 236 PRO B C   1 
ATOM   5335 O O   . PRO B 1 236 ? -19.31600 33.18300  31.08800 1.000 52.71000 ? 236 PRO B O   1 
ATOM   5336 C CB  . PRO B 1 236 ? -22.53800 33.28100  31.72800 1.000 52.71000 ? 236 PRO B CB  1 
ATOM   5337 C CG  . PRO B 1 236 ? -22.49100 31.85500  31.27700 1.000 52.71000 ? 236 PRO B CG  1 
ATOM   5338 C CD  . PRO B 1 236 ? -22.32300 31.92200  29.78100 1.000 52.71000 ? 236 PRO B CD  1 
ATOM   5339 N N   . THR B 1 237 ? -19.82600 35.03900  32.22500 1.000 54.08000 ? 237 THR B N   1 
ATOM   5340 C CA  . THR B 1 237 ? -18.52900 35.05800  32.89700 1.000 54.08000 ? 237 THR B CA  1 
ATOM   5341 C C   . THR B 1 237 ? -18.38800 33.87500  33.84900 1.000 54.08000 ? 237 THR B C   1 
ATOM   5342 O O   . THR B 1 237 ? -17.40600 33.12700  33.78900 1.000 54.08000 ? 237 THR B O   1 
ATOM   5343 C CB  . THR B 1 237 ? -18.34800 36.37800  33.64900 1.000 54.08000 ? 237 THR B CB  1 
ATOM   5344 O OG1 . THR B 1 237 ? -18.22700 37.45500  32.71000 1.000 54.08000 ? 237 THR B OG1 1 
ATOM   5345 C CG2 . THR B 1 237 ? -17.10500 36.33100  34.52600 1.000 54.08000 ? 237 THR B CG2 1 
ATOM   5346 N N   . ASN B 1 238 ? -19.36600 33.68900  34.73200 1.000 56.87000 ? 238 ASN B N   1 
ATOM   5347 C CA  . ASN B 1 238 ? -19.42000 32.51000  35.58200 1.000 56.87000 ? 238 ASN B CA  1 
ATOM   5348 C C   . ASN B 1 238 ? -19.91700 31.30700  34.78800 1.000 56.87000 ? 238 ASN B C   1 
ATOM   5349 O O   . ASN B 1 238 ? -20.59500 31.44200  33.76600 1.000 56.87000 ? 238 ASN B O   1 
ATOM   5350 C CB  . ASN B 1 238 ? -20.32700 32.75200  36.78900 1.000 56.87000 ? 238 ASN B CB  1 
ATOM   5351 C CG  . ASN B 1 238 ? -19.72500 33.72200  37.78300 1.000 56.87000 ? 238 ASN B CG  1 
ATOM   5352 O OD1 . ASN B 1 238 ? -19.86100 34.93700  37.64300 1.000 56.87000 ? 238 ASN B OD1 1 
ATOM   5353 N ND2 . ASN B 1 238 ? -19.05700 33.18800  38.79900 1.000 56.87000 ? 238 ASN B ND2 1 
ATOM   5354 N N   . ASN B 1 239 ? -19.56000 30.11900  35.26200 1.000 58.04000 ? 239 ASN B N   1 
ATOM   5355 C CA  . ASN B 1 239 ? -20.08900 28.90500  34.65600 1.000 58.04000 ? 239 ASN B CA  1 
ATOM   5356 C C   . ASN B 1 239 ? -21.59800 28.85000  34.88800 1.000 58.04000 ? 239 ASN B C   1 
ATOM   5357 O O   . ASN B 1 239 ? -22.05100 29.01900  36.03000 1.000 58.04000 ? 239 ASN B O   1 
ATOM   5358 C CB  . ASN B 1 239 ? -19.41900 27.66700  35.25100 1.000 58.04000 ? 239 ASN B CB  1 
ATOM   5359 C CG  . ASN B 1 239 ? -19.86200 26.38300  34.57300 1.000 58.04000 ? 239 ASN B CG  1 
ATOM   5360 O OD1 . ASN B 1 239 ? -19.88500 26.29200  33.34500 1.000 58.04000 ? 239 ASN B OD1 1 
ATOM   5361 N ND2 . ASN B 1 239 ? -20.22500 25.38700  35.37200 1.000 58.04000 ? 239 ASN B ND2 1 
ATOM   5362 N N   . PRO B 1 240 ? -22.40200 28.65100  33.84300 1.000 58.51000 ? 240 PRO B N   1 
ATOM   5363 C CA  . PRO B 1 240 ? -23.86400 28.63100  34.03500 1.000 58.51000 ? 240 PRO B CA  1 
ATOM   5364 C C   . PRO B 1 240 ? -24.34600 27.57400  35.01400 1.000 58.51000 ? 240 PRO B C   1 
ATOM   5365 O O   . PRO B 1 240 ? -25.33800 27.80600  35.71600 1.000 58.51000 ? 240 PRO B O   1 
ATOM   5366 C CB  . PRO B 1 240 ? -24.40500 28.38500  32.61900 1.000 58.51000 ? 240 PRO B CB  1 
ATOM   5367 C CG  . PRO B 1 240 ? -23.26000 27.79600  31.86300 1.000 58.51000 ? 240 PRO B CG  1 
ATOM   5368 C CD  . PRO B 1 240 ? -22.02800 28.42100  32.43600 1.000 58.51000 ? 240 PRO B CD  1 
ATOM   5369 N N   . LEU B 1 241 ? -23.68600 26.41800  35.07600 1.000 58.69000 ? 241 LEU B N   1 
ATOM   5370 C CA  . LEU B 1 241 ? -24.16800 25.31800  35.90000 1.000 58.69000 ? 241 LEU B CA  1 
ATOM   5371 C C   . LEU B 1 241 ? -23.58400 25.29300  37.30500 1.000 58.69000 ? 241 LEU B C   1 
ATOM   5372 O O   . LEU B 1 241 ? -24.12900 24.59700  38.17000 1.000 58.69000 ? 241 LEU B O   1 
ATOM   5373 C CB  . LEU B 1 241 ? -23.87100 23.97400  35.22700 1.000 58.69000 ? 241 LEU B CB  1 
ATOM   5374 C CG  . LEU B 1 241 ? -24.56800 23.67400  33.90000 1.000 58.69000 ? 241 LEU B CG  1 
ATOM   5375 C CD1 . LEU B 1 241 ? -24.65300 22.17400  33.70500 1.000 58.69000 ? 241 LEU B CD1 1 
ATOM   5376 C CD2 . LEU B 1 241 ? -25.94800 24.30700  33.84000 1.000 58.69000 ? 241 LEU B CD2 1 
ATOM   5377 N N   . THR B 1 242 ? -22.49500 26.01700  37.56300 1.000 57.96000 ? 242 THR B N   1 
ATOM   5378 C CA  . THR B 1 242 ? -21.85100 25.92100  38.86500 1.000 57.96000 ? 242 THR B CA  1 
ATOM   5379 C C   . THR B 1 242 ? -21.48800 27.25900  39.49500 1.000 57.96000 ? 242 THR B C   1 
ATOM   5380 O O   . THR B 1 242 ? -20.94700 27.25700  40.60500 1.000 57.96000 ? 242 THR B O   1 
ATOM   5381 C CB  . THR B 1 242 ? -20.58200 25.05200  38.77400 1.000 57.96000 ? 242 THR B CB  1 
ATOM   5382 O OG1 . THR B 1 242 ? -19.78000 25.48000  37.66800 1.000 57.96000 ? 242 THR B OG1 1 
ATOM   5383 C CG2 . THR B 1 242 ? -20.94300 23.58000  38.60400 1.000 57.96000 ? 242 THR B CG2 1 
ATOM   5384 N N   . ASP B 1 243 ? -21.77500 28.39000  38.84400 1.000 57.40000 ? 243 ASP B N   1 
ATOM   5385 C CA  . ASP B 1 243 ? -21.41300 29.71200  39.36600 1.000 57.40000 ? 243 ASP B CA  1 
ATOM   5386 C C   . ASP B 1 243 ? -19.91400 29.79500  39.65400 1.000 57.40000 ? 243 ASP B C   1 
ATOM   5387 O O   . ASP B 1 243 ? -19.48700 30.32200  40.68400 1.000 57.40000 ? 243 ASP B O   1 
ATOM   5388 C CB  . ASP B 1 243 ? -22.23200 30.05900  40.61500 1.000 57.40000 ? 243 ASP B CB  1 
ATOM   5389 C CG  . ASP B 1 243 ? -22.13400 31.52900  40.99500 1.000 57.40000 ? 243 ASP B CG  1 
ATOM   5390 O OD1 . ASP B 1 243 ? -21.58900 32.31900  40.19500 1.000 57.40000 ? 243 ASP B OD1 1 
ATOM   5391 O OD2 . ASP B 1 243 ? -22.59900 31.89200  42.09700 1.000 57.40000 ? 243 ASP B OD2 1 
ATOM   5392 N N   . GLU B 1 244 ? -19.10500 29.27100  38.73600 1.000 56.55000 ? 244 GLU B N   1 
ATOM   5393 C CA  . GLU B 1 244 ? -17.66800 29.25800  38.94300 1.000 56.55000 ? 244 GLU B CA  1 
ATOM   5394 C C   . GLU B 1 244 ? -16.95600 29.95000  37.78900 1.000 56.55000 ? 244 GLU B C   1 
ATOM   5395 O O   . GLU B 1 244 ? -17.42200 29.90200  36.64500 1.000 56.55000 ? 244 GLU B O   1 
ATOM   5396 C CB  . GLU B 1 244 ? -17.13600 27.82300  39.07100 1.000 56.55000 ? 244 GLU B CB  1 
ATOM   5397 C CG  . GLU B 1 244 ? -17.76800 27.01300  40.18900 1.000 56.55000 ? 244 GLU B CG  1 
ATOM   5398 C CD  . GLU B 1 244 ? -17.44000 27.55500  41.56600 1.000 56.55000 ? 244 GLU B CD  1 
ATOM   5399 O OE1 . GLU B 1 244 ? -16.39900 28.23100  41.71300 1.000 56.55000 ? 244 GLU B OE1 1 
ATOM   5400 O OE2 . GLU B 1 244 ? -18.22700 27.30400  42.50400 1.000 56.55000 ? 244 GLU B OE2 1 
ATOM   5401 N N   . PRO B 1 245 ? -15.82900 30.60800  38.05900 1.000 52.81000 ? 245 PRO B N   1 
ATOM   5402 C CA  . PRO B 1 245 ? -15.04200 31.19700  36.97300 1.000 52.81000 ? 245 PRO B CA  1 
ATOM   5403 C C   . PRO B 1 245 ? -14.49200 30.12300  36.04800 1.000 52.81000 ? 245 PRO B C   1 
ATOM   5404 O O   . PRO B 1 245 ? -14.17400 29.01000  36.47000 1.000 52.81000 ? 245 PRO B O   1 
ATOM   5405 C CB  . PRO B 1 245 ? -13.91400 31.93200  37.70800 1.000 52.81000 ? 245 PRO B CB  1 
ATOM   5406 C CG  . PRO B 1 245 ? -14.40700 32.10200  39.11400 1.000 52.81000 ? 245 PRO B CG  1 
ATOM   5407 C CD  . PRO B 1 245 ? -15.26000 30.90400  39.38300 1.000 52.81000 ? 245 PRO B CD  1 
ATOM   5408 N N   . LEU B 1 246 ? -14.38400 30.46900  34.76900 1.000 45.69000 ? 246 LEU B N   1 
ATOM   5409 C CA  . LEU B 1 246 ? -13.76800 29.57400  33.80000 1.000 45.69000 ? 246 LEU B CA  1 
ATOM   5410 C C   . LEU B 1 246 ? -12.25600 29.61600  33.97400 1.000 45.69000 ? 246 LEU B C   1 
ATOM   5411 O O   . LEU B 1 246 ? -11.63500 30.66900  33.79500 1.000 45.69000 ? 246 LEU B O   1 
ATOM   5412 C CB  . LEU B 1 246 ? -14.15800 29.96800  32.38000 1.000 45.69000 ? 246 LEU B CB  1 
ATOM   5413 C CG  . LEU B 1 246 ? -13.60800 29.03200  31.30900 1.000 45.69000 ? 246 LEU B CG  1 
ATOM   5414 C CD1 . LEU B 1 246 ? -13.98800 27.60200  31.64100 1.000 45.69000 ? 246 LEU B CD1 1 
ATOM   5415 C CD2 . LEU B 1 246 ? -14.13600 29.43000  29.94700 1.000 45.69000 ? 246 LEU B CD2 1 
ATOM   5416 N N   . ASP B 1 247 ? -11.66000 28.47100  34.29900 1.000 42.12000 ? 247 ASP B N   1 
ATOM   5417 C CA  . ASP B 1 247 ? -10.23300 28.40800  34.61100 1.000 42.12000 ? 247 ASP B CA  1 
ATOM   5418 C C   . ASP B 1 247 ? -9.45900  28.42500  33.30100 1.000 42.12000 ? 247 ASP B C   1 
ATOM   5419 O O   . ASP B 1 247 ? -9.24900  27.39800  32.65400 1.000 42.12000 ? 247 ASP B O   1 
ATOM   5420 C CB  . ASP B 1 247 ? -9.91200  27.17200  35.44100 1.000 42.12000 ? 247 ASP B CB  1 
ATOM   5421 C CG  . ASP B 1 247 ? -8.54800  27.25200  36.10100 1.000 42.12000 ? 247 ASP B CG  1 
ATOM   5422 O OD1 . ASP B 1 247 ? -7.85100  28.26900  35.90600 1.000 42.12000 ? 247 ASP B OD1 1 
ATOM   5423 O OD2 . ASP B 1 247 ? -8.17500  26.29900  36.81900 1.000 42.12000 ? 247 ASP B OD2 1 
ATOM   5424 N N   . LEU B 1 248 ? -9.02300  29.62200  32.91400 1.000 39.75000 ? 248 LEU B N   1 
ATOM   5425 C CA  . LEU B 1 248 ? -8.28100  29.84100  31.68200 1.000 39.75000 ? 248 LEU B CA  1 
ATOM   5426 C C   . LEU B 1 248 ? -6.78400  29.62200  31.85900 1.000 39.75000 ? 248 LEU B C   1 
ATOM   5427 O O   . LEU B 1 248 ? -5.99800  30.04800  31.00400 1.000 39.75000 ? 248 LEU B O   1 
ATOM   5428 C CB  . LEU B 1 248 ? -8.55200  31.25000  31.15100 1.000 39.75000 ? 248 LEU B CB  1 
ATOM   5429 C CG  . LEU B 1 248 ? -10.01500 31.55900  30.82400 1.000 39.75000 ? 248 LEU B CG  1 
ATOM   5430 C CD1 . LEU B 1 248 ? -10.16600 32.97600  30.29100 1.000 39.75000 ? 248 LEU B CD1 1 
ATOM   5431 C CD2 . LEU B 1 248 ? -10.56300 30.54900  29.83000 1.000 39.75000 ? 248 LEU B CD2 1 
ATOM   5432 N N   . SER B 1 249 ? -6.37400  28.98400  32.96000 1.000 35.60000 ? 249 SER B N   1 
ATOM   5433 C CA  . SER B 1 249 ? -4.95200  28.79300  33.22400 1.000 35.60000 ? 249 SER B CA  1 
ATOM   5434 C C   . SER B 1 249 ? -4.29000  27.98000  32.12000 1.000 35.60000 ? 249 SER B C   1 
ATOM   5435 O O   . SER B 1 249 ? -3.12900  28.22200  31.77100 1.000 35.60000 ? 249 SER B O   1 
ATOM   5436 C CB  . SER B 1 249 ? -4.76500  28.10300  34.57500 1.000 35.60000 ? 249 SER B CB  1 
ATOM   5437 O OG  . SER B 1 249 ? -5.60500  28.67200  35.56200 1.000 35.60000 ? 249 SER B OG  1 
ATOM   5438 N N   . GLY B 1 250 ? -5.01500  27.01600  31.55300 1.000 35.71000 ? 250 GLY B N   1 
ATOM   5439 C CA  . GLY B 1 250 ? -4.53900  26.28300  30.40000 1.000 35.71000 ? 250 GLY B CA  1 
ATOM   5440 C C   . GLY B 1 250 ? -4.86400  26.90600  29.06600 1.000 35.71000 ? 250 GLY B C   1 
ATOM   5441 O O   . GLY B 1 250 ? -4.37200  26.43700  28.03500 1.000 35.71000 ? 250 GLY B O   1 
ATOM   5442 N N   . SER B 1 251 ? -5.68700  27.95200  29.05700 1.000 36.28000 ? 251 SER B N   1 
ATOM   5443 C CA  . SER B 1 251 ? -6.10400  28.56700  27.80600 1.000 36.28000 ? 251 SER B CA  1 
ATOM   5444 C C   . SER B 1 251 ? -4.93600  29.26600  27.12400 1.000 36.28000 ? 251 SER B C   1 
ATOM   5445 O O   . SER B 1 251 ? -4.14100  29.95700  27.76800 1.000 36.28000 ? 251 SER B O   1 
ATOM   5446 C CB  . SER B 1 251 ? -7.23500  29.56300  28.06000 1.000 36.28000 ? 251 SER B CB  1 
ATOM   5447 O OG  . SER B 1 251 ? -7.58400  30.25200  26.87200 1.000 36.28000 ? 251 SER B OG  1 
ATOM   5448 N N   . VAL B 1 252 ? -4.83800  29.08400  25.80700 1.000 36.17000 ? 252 VAL B N   1 
ATOM   5449 C CA  . VAL B 1 252 ? -3.86400  29.82900  25.01800 1.000 36.17000 ? 252 VAL B CA  1 
ATOM   5450 C C   . VAL B 1 252 ? -4.39600  31.18300  24.56300 1.000 36.17000 ? 252 VAL B C   1 
ATOM   5451 O O   . VAL B 1 252 ? -3.60400  32.04700  24.16000 1.000 36.17000 ? 252 VAL B O   1 
ATOM   5452 C CB  . VAL B 1 252 ? -3.41400  29.01200  23.79400 1.000 36.17000 ? 252 VAL B CB  1 
ATOM   5453 C CG1 . VAL B 1 252 ? -2.91800  27.63900  24.22700 1.000 36.17000 ? 252 VAL B CG1 1 
ATOM   5454 C CG2 . VAL B 1 252 ? -4.55000  28.88500  22.79000 1.000 36.17000 ? 252 VAL B CG2 1 
ATOM   5455 N N   . LEU B 1 253 ? -5.70900  31.39400  24.61800 1.000 37.55000 ? 253 LEU B N   1 
ATOM   5456 C CA  . LEU B 1 253 ? -6.33100  32.64100  24.20200 1.000 37.55000 ? 253 LEU B CA  1 
ATOM   5457 C C   . LEU B 1 253 ? -6.66400  33.54900  25.37700 1.000 37.55000 ? 253 LEU B C   1 
ATOM   5458 O O   . LEU B 1 253 ? -7.30100  34.58900  25.18000 1.000 37.55000 ? 253 LEU B O   1 
ATOM   5459 C CB  . LEU B 1 253 ? -7.59500  32.34900  23.39300 1.000 37.55000 ? 253 LEU B CB  1 
ATOM   5460 C CG  . LEU B 1 253 ? -7.41600  31.42400  22.18900 1.000 37.55000 ? 253 LEU B CG  1 
ATOM   5461 C CD1 . LEU B 1 253 ? -8.76700  31.05300  21.60600 1.000 37.55000 ? 253 LEU B CD1 1 
ATOM   5462 C CD2 . LEU B 1 253 ? -6.53200  32.07300  21.13600 1.000 37.55000 ? 253 LEU B CD2 1 
ATOM   5463 N N   . ARG B 1 254 ? -6.25000  33.17800  26.58700 1.000 35.56000 ? 254 ARG B N   1 
ATOM   5464 C CA  . ARG B 1 254 ? -6.63600  33.91700  27.78100 1.000 35.56000 ? 254 ARG B CA  1 
ATOM   5465 C C   . ARG B 1 254 ? -6.13800  35.35600  27.72100 1.000 35.56000 ? 254 ARG B C   1 
ATOM   5466 O O   . ARG B 1 254 ? -5.01200  35.62800  27.29400 1.000 35.56000 ? 254 ARG B O   1 
ATOM   5467 C CB  . ARG B 1 254 ? -6.08500  33.21100  29.02100 1.000 35.56000 ? 254 ARG B CB  1 
ATOM   5468 C CG  . ARG B 1 254 ? -6.11800  34.02600  30.29900 1.000 35.56000 ? 254 ARG B CG  1 
ATOM   5469 C CD  . ARG B 1 254 ? -5.41000  33.28000  31.41500 1.000 35.56000 ? 254 ARG B CD  1 
ATOM   5470 N NE  . ARG B 1 254 ? -4.12700  32.74800  30.97000 1.000 35.56000 ? 254 ARG B NE  1 
ATOM   5471 C CZ  . ARG B 1 254 ? -2.96400  33.36600  31.12200 1.000 35.56000 ? 254 ARG B CZ  1 
ATOM   5472 N NH1 . ARG B 1 254 ? -2.87800  34.53900  31.72900 1.000 35.56000 ? 254 ARG B NH1 1 
ATOM   5473 N NH2 . ARG B 1 254 ? -1.85900  32.79200  30.65500 1.000 35.56000 ? 254 ARG B NH2 1 
ATOM   5474 N N   . SER B 1 255 ? -6.99600  36.28200  28.14400 1.000 37.52000 ? 255 SER B N   1 
ATOM   5475 C CA  . SER B 1 255 ? -6.65200  37.69500  28.11800 1.000 37.52000 ? 255 SER B CA  1 
ATOM   5476 C C   . SER B 1 255 ? -5.56600  38.00900  29.14000 1.000 37.52000 ? 255 SER B C   1 
ATOM   5477 O O   . SER B 1 255 ? -5.56000  37.47900  30.25400 1.000 37.52000 ? 255 SER B O   1 
ATOM   5478 C CB  . SER B 1 255 ? -7.89100  38.55000  28.38600 1.000 37.52000 ? 255 SER B CB  1 
ATOM   5479 O OG  . SER B 1 255 ? -7.57100  39.93100  28.33900 1.000 37.52000 ? 255 SER B OG  1 
ATOM   5480 N N   . VAL B 1 256 ? -4.64500  38.87800  28.74700 1.000 38.18000 ? 256 VAL B N   1 
ATOM   5481 C CA  . VAL B 1 256 ? -3.55700  39.31300  29.61200 1.000 38.18000 ? 256 VAL B CA  1 
ATOM   5482 C C   . VAL B 1 256 ? -4.07900  40.31700  30.63100 1.000 38.18000 ? 256 VAL B C   1 
ATOM   5483 O O   . VAL B 1 256 ? -5.08200  41.00300  30.40600 1.000 38.18000 ? 256 VAL B O   1 
ATOM   5484 C CB  . VAL B 1 256 ? -2.41200  39.90700  28.76900 1.000 38.18000 ? 256 VAL B CB  1 
ATOM   5485 C CG1 . VAL B 1 256 ? -1.16300  40.10600  29.61900 1.000 38.18000 ? 256 VAL B CG1 1 
ATOM   5486 C CG2 . VAL B 1 256 ? -2.11800  39.01600  27.57500 1.000 38.18000 ? 256 VAL B CG2 1 
ATOM   5487 N N   . SER B 1 257 ? -3.39900  40.40100  31.77100 1.000 39.59000 ? 257 SER B N   1 
ATOM   5488 C CA  . SER B 1 257 ? -3.72800  41.42600  32.74700 1.000 39.59000 ? 257 SER B CA  1 
ATOM   5489 C C   . SER B 1 257 ? -3.42300  42.81100  32.17100 1.000 39.59000 ? 257 SER B C   1 
ATOM   5490 O O   . SER B 1 257 ? -2.51400  42.96500  31.35100 1.000 39.59000 ? 257 SER B O   1 
ATOM   5491 C CB  . SER B 1 257 ? -2.93000  41.22600  34.03000 1.000 39.59000 ? 257 SER B CB  1 
ATOM   5492 O OG  . SER B 1 257 ? -1.67400  41.86400  33.91600 1.000 39.59000 ? 257 SER B OG  1 
ATOM   5493 N N   . PRO B 1 258 ? -4.18300  43.83400  32.58000 1.000 41.27000 ? 258 PRO B N   1 
ATOM   5494 C CA  . PRO B 1 258 ? -3.97500  45.17600  32.00700 1.000 41.27000 ? 258 PRO B CA  1 
ATOM   5495 C C   . PRO B 1 258 ? -2.57600  45.73800  32.19700 1.000 41.27000 ? 258 PRO B C   1 
ATOM   5496 O O   . PRO B 1 258 ? -2.09300  46.46700  31.32100 1.000 41.27000 ? 258 PRO B O   1 
ATOM   5497 C CB  . PRO B 1 258 ? -5.02600  46.02700  32.73400 1.000 41.27000 ? 258 PRO B CB  1 
ATOM   5498 C CG  . PRO B 1 258 ? -6.06800  45.05000  33.17700 1.000 41.27000 ? 258 PRO B CG  1 
ATOM   5499 C CD  . PRO B 1 258 ? -5.31100  43.80500  33.52500 1.000 41.27000 ? 258 PRO B CD  1 
ATOM   5500 N N   . CYS B 1 259 ? -1.90600  45.42400  33.31100 1.000 41.81000 ? 259 CYS B N   1 
ATOM   5501 C CA  . CYS B 1 259 ? -0.60200  46.02300  33.58100 1.000 41.81000 ? 259 CYS B CA  1 
ATOM   5502 C C   . CYS B 1 259 ? 0.43400   45.58700  32.55700 1.000 41.81000 ? 259 CYS B C   1 
ATOM   5503 O O   . CYS B 1 259 ? 1.26300   46.39300  32.10900 1.000 41.81000 ? 259 CYS B O   1 
ATOM   5504 C CB  . CYS B 1 259 ? -0.14500  45.64300  34.98600 1.000 41.81000 ? 259 CYS B CB  1 
ATOM   5505 S SG  . CYS B 1 259 ? -1.48400  45.63200  36.18800 1.000 41.81000 ? 259 CYS B SG  1 
ATOM   5506 N N   . HIS B 1 260 ? 0.39000   44.31700  32.15900 1.000 37.97000 ? 260 HIS B N   1 
ATOM   5507 C CA  . HIS B 1 260 ? 1.35600   43.83100  31.18600 1.000 37.97000 ? 260 HIS B CA  1 
ATOM   5508 C C   . HIS B 1 260 ? 1.12000   44.45300  29.81800 1.000 37.97000 ? 260 HIS B C   1 
ATOM   5509 O O   . HIS B 1 260 ? 2.07600   44.79100  29.11100 1.000 37.97000 ? 260 HIS B O   1 
ATOM   5510 C CB  . HIS B 1 260 ? 1.29500   42.31000  31.11100 1.000 37.97000 ? 260 HIS B CB  1 
ATOM   5511 C CG  . HIS B 1 260 ? 2.32300   41.71900  30.20400 1.000 37.97000 ? 260 HIS B CG  1 
ATOM   5512 N ND1 . HIS B 1 260 ? 1.99700   41.04000  29.05100 1.000 37.97000 ? 260 HIS B ND1 1 
ATOM   5513 C CD2 . HIS B 1 260 ? 3.67500   41.72600  30.26900 1.000 37.97000 ? 260 HIS B CD2 1 
ATOM   5514 C CE1 . HIS B 1 260 ? 3.10400   40.64300  28.45000 1.000 37.97000 ? 260 HIS B CE1 1 
ATOM   5515 N NE2 . HIS B 1 260 ? 4.13600   41.04800  29.16800 1.000 37.97000 ? 260 HIS B NE2 1 
ATOM   5516 N N   . ILE B 1 261 ? -0.14500  44.62300  29.42800 1.000 41.08000 ? 261 ILE B N   1 
ATOM   5517 C CA  . ILE B 1 261 ? -0.43500  45.28300  28.16000 1.000 41.08000 ? 261 ILE B CA  1 
ATOM   5518 C C   . ILE B 1 261 ? -0.02700  46.75200  28.20900 1.000 41.08000 ? 261 ILE B C   1 
ATOM   5519 O O   . ILE B 1 261 ? 0.43300   47.31000  27.20300 1.000 41.08000 ? 261 ILE B O   1 
ATOM   5520 C CB  . ILE B 1 261 ? -1.92400  45.11300  27.80700 1.000 41.08000 ? 261 ILE B CB  1 
ATOM   5521 C CG1 . ILE B 1 261 ? -2.29600  43.62900  27.77300 1.000 41.08000 ? 261 ILE B CG1 1 
ATOM   5522 C CG2 . ILE B 1 261 ? -2.23600  45.75400  26.46300 1.000 41.08000 ? 261 ILE B CG2 1 
ATOM   5523 C CD1 . ILE B 1 261 ? -1.57800  42.85100  26.69000 1.000 41.08000 ? 261 ILE B CD1 1 
ATOM   5524 N N   . GLU B 1 262 ? -0.15800  47.39800  29.37300 1.000 44.45000 ? 262 GLU B N   1 
ATOM   5525 C CA  . GLU B 1 262 ? 0.29100   48.78200  29.49200 1.000 44.45000 ? 262 GLU B CA  1 
ATOM   5526 C C   . GLU B 1 262 ? 1.80000   48.87900  29.35000 1.000 44.45000 ? 262 GLU B C   1 
ATOM   5527 O O   . GLU B 1 262 ? 2.31600   49.81600  28.73500 1.000 44.45000 ? 262 GLU B O   1 
ATOM   5528 C CB  . GLU B 1 262 ? -0.14900  49.38000  30.82700 1.000 44.45000 ? 262 GLU B CB  1 
ATOM   5529 C CG  . GLU B 1 262 ? 0.47700   50.74300  31.11500 1.000 44.45000 ? 262 GLU B CG  1 
ATOM   5530 C CD  . GLU B 1 262 ? -0.29800  51.54300  32.14000 1.000 44.45000 ? 262 GLU B CD  1 
ATOM   5531 O OE1 . GLU B 1 262 ? -1.27200  51.00100  32.70100 1.000 44.45000 ? 262 GLU B OE1 1 
ATOM   5532 O OE2 . GLU B 1 262 ? 0.06200   52.71500  32.37700 1.000 44.45000 ? 262 GLU B OE2 1 
ATOM   5533 N N   . TYR B 1 263 ? 2.52400   47.90200  29.89100 1.000 41.58000 ? 263 TYR B N   1 
ATOM   5534 C CA  . TYR B 1 263 ? 3.96900   47.86700  29.69600 1.000 41.58000 ? 263 TYR B CA  1 
ATOM   5535 C C   . TYR B 1 263 ? 4.31500   47.61200  28.22900 1.000 41.58000 ? 263 TYR B C   1 
ATOM   5536 O O   . TYR B 1 263 ? 5.23800   48.23200  27.67900 1.000 41.58000 ? 263 TYR B O   1 
ATOM   5537 C CB  . TYR B 1 263 ? 4.54500   46.80000  30.62600 1.000 41.58000 ? 263 TYR B CB  1 
ATOM   5538 C CG  . TYR B 1 263 ? 6.04600   46.69900  30.78400 1.000 41.58000 ? 263 TYR B CG  1 
ATOM   5539 C CD1 . TYR B 1 263 ? 6.91900   47.15100  29.80800 1.000 41.58000 ? 263 TYR B CD1 1 
ATOM   5540 C CD2 . TYR B 1 263 ? 6.58700   46.10700  31.91900 1.000 41.58000 ? 263 TYR B CD2 1 
ATOM   5541 C CE1 . TYR B 1 263 ? 8.27200   47.03900  29.96000 1.000 41.58000 ? 263 TYR B CE1 1 
ATOM   5542 C CE2 . TYR B 1 263 ? 7.94600   45.99000  32.08600 1.000 41.58000 ? 263 TYR B CE2 1 
ATOM   5543 C CZ  . TYR B 1 263 ? 8.79100   46.44400  31.09600 1.000 41.58000 ? 263 TYR B CZ  1 
ATOM   5544 O OH  . TYR B 1 263 ? 10.15800  46.30000  31.23100 1.000 41.58000 ? 263 TYR B OH  1 
ATOM   5545 N N   . LEU B 1 264 ? 3.54800   46.74400  27.56500 1.000 38.77000 ? 264 LEU B N   1 
ATOM   5546 C CA  . LEU B 1 264 ? 3.78900   46.49200  26.14900 1.000 38.77000 ? 264 LEU B CA  1 
ATOM   5547 C C   . LEU B 1 264 ? 3.57800   47.75500  25.32800 1.000 38.77000 ? 264 LEU B C   1 
ATOM   5548 O O   . LEU B 1 264 ? 4.29700   48.00200  24.35400 1.000 38.77000 ? 264 LEU B O   1 
ATOM   5549 C CB  . LEU B 1 264 ? 2.87200   45.37700  25.64900 1.000 38.77000 ? 264 LEU B CB  1 
ATOM   5550 C CG  . LEU B 1 264 ? 3.10100   43.96000  26.17200 1.000 38.77000 ? 264 LEU B CG  1 
ATOM   5551 C CD1 . LEU B 1 264 ? 2.04700   43.02200  25.60800 1.000 38.77000 ? 264 LEU B CD1 1 
ATOM   5552 C CD2 . LEU B 1 264 ? 4.49700   43.47300  25.82200 1.000 38.77000 ? 264 LEU B CD2 1 
ATOM   5553 N N   . HIS B 1 265 ? 2.59600   48.57300  25.70900 1.000 42.55000 ? 265 HIS B N   1 
ATOM   5554 C CA  . HIS B 1 265 ? 2.46300   49.88600  25.08300 1.000 42.55000 ? 265 HIS B CA  1 
ATOM   5555 C C   . HIS B 1 265 ? 3.62700   50.79600  25.46300 1.000 42.55000 ? 265 HIS B C   1 
ATOM   5556 O O   . HIS B 1 265 ? 4.08500   51.60600  24.64700 1.000 42.55000 ? 265 HIS B O   1 
ATOM   5557 C CB  . HIS B 1 265 ? 1.13800   50.53300  25.48100 1.000 42.55000 ? 265 HIS B CB  1 
ATOM   5558 C CG  . HIS B 1 265 ? -0.06800  49.78100  25.01300 1.000 42.55000 ? 265 HIS B CG  1 
ATOM   5559 N ND1 . HIS B 1 265 ? -0.05500  48.95600  23.90900 1.000 42.55000 ? 265 HIS B ND1 1 
ATOM   5560 C CD2 . HIS B 1 265 ? -1.33000  49.73600  25.50200 1.000 42.55000 ? 265 HIS B CD2 1 
ATOM   5561 C CE1 . HIS B 1 265 ? -1.25700  48.43400  23.74000 1.000 42.55000 ? 265 HIS B CE1 1 
ATOM   5562 N NE2 . HIS B 1 265 ? -2.04900  48.89200  24.69300 1.000 42.55000 ? 265 HIS B NE2 1 
ATOM   5563 N N   . ASN B 1 266 ? 4.12800   50.65900  26.69500 1.000 42.98000 ? 266 ASN B N   1 
ATOM   5564 C CA  . ASN B 1 266 ? 5.17300   51.55000  27.18700 1.000 42.98000 ? 266 ASN B CA  1 
ATOM   5565 C C   . ASN B 1 266 ? 6.48700   51.36500  26.44400 1.000 42.98000 ? 266 ASN B C   1 
ATOM   5566 O O   . ASN B 1 266 ? 7.23100   52.33400  26.26000 1.000 42.98000 ? 266 ASN B O   1 
ATOM   5567 C CB  . ASN B 1 266 ? 5.37700   51.34400  28.68900 1.000 42.98000 ? 266 ASN B CB  1 
ATOM   5568 C CG  . ASN B 1 266 ? 4.27400   51.97100  29.51800 1.000 42.98000 ? 266 ASN B CG  1 
ATOM   5569 O OD1 . ASN B 1 266 ? 3.54400   52.84300  29.04700 1.000 42.98000 ? 266 ASN B OD1 1 
ATOM   5570 N ND2 . ASN B 1 266 ? 4.15000   51.53200  30.76500 1.000 42.98000 ? 266 ASN B ND2 1 
ATOM   5571 N N   . MET B 1 267 ? 6.80100   50.14700  26.00100 1.000 41.77000 ? 267 MET B N   1 
ATOM   5572 C CA  . MET B 1 267 ? 8.02100   49.97000  25.21800 1.000 41.77000 ? 267 MET B CA  1 
ATOM   5573 C C   . MET B 1 267 ? 7.75300   49.50500  23.79100 1.000 41.77000 ? 267 MET B C   1 
ATOM   5574 O O   . MET B 1 267 ? 8.69700   49.13500  23.08100 1.000 41.77000 ? 267 MET B O   1 
ATOM   5575 C CB  . MET B 1 267 ? 8.99700   49.02900  25.92500 1.000 41.77000 ? 267 MET B CB  1 
ATOM   5576 C CG  . MET B 1 267 ? 8.65800   47.57000  25.87800 1.000 41.77000 ? 267 MET B CG  1 
ATOM   5577 S SD  . MET B 1 267 ? 10.17700  46.63200  26.13600 1.000 41.77000 ? 267 MET B SD  1 
ATOM   5578 C CE  . MET B 1 267 ? 10.95100  46.75100  24.52100 1.000 41.77000 ? 267 MET B CE  1 
ATOM   5579 N N   . GLY B 1 268 ? 6.49500   49.50400  23.35600 1.000 38.37000 ? 268 GLY B N   1 
ATOM   5580 C CA  . GLY B 1 268 ? 6.16800   49.54000  21.94700 1.000 38.37000 ? 268 GLY B CA  1 
ATOM   5581 C C   . GLY B 1 268 ? 6.23100   48.23000  21.19400 1.000 38.37000 ? 268 GLY B C   1 
ATOM   5582 O O   . GLY B 1 268 ? 6.05300   48.23800  19.96900 1.000 38.37000 ? 268 GLY B O   1 
ATOM   5583 N N   . VAL B 1 269 ? 6.48000   47.11000  21.86400 1.000 36.17000 ? 269 VAL B N   1 
ATOM   5584 C CA  . VAL B 1 269 ? 6.44300   45.81200  21.19700 1.000 36.17000 ? 269 VAL B CA  1 
ATOM   5585 C C   . VAL B 1 269 ? 4.99300   45.34700  21.13200 1.000 36.17000 ? 269 VAL B C   1 
ATOM   5586 O O   . VAL B 1 269 ? 4.33800   45.17400  22.16500 1.000 36.17000 ? 269 VAL B O   1 
ATOM   5587 C CB  . VAL B 1 269 ? 7.33000   44.79100  21.92100 1.000 36.17000 ? 269 VAL B CB  1 
ATOM   5588 C CG1 . VAL B 1 269 ? 6.88500   43.38300  21.59800 1.000 36.17000 ? 269 VAL B CG1 1 
ATOM   5589 C CG2 . VAL B 1 269 ? 8.78700   44.99500  21.52400 1.000 36.17000 ? 269 VAL B CG2 1 
ATOM   5590 N N   . LYS B 1 270 ? 4.48700   45.15400  19.91500 1.000 37.19000 ? 270 LYS B N   1 
ATOM   5591 C CA  . LYS B 1 270 ? 3.07100   44.89600  19.69000 1.000 37.19000 ? 270 LYS B CA  1 
ATOM   5592 C C   . LYS B 1 270 ? 2.73400   43.41600  19.55000 1.000 37.19000 ? 270 LYS B C   1 
ATOM   5593 O O   . LYS B 1 270 ? 1.56300   43.08100  19.34100 1.000 37.19000 ? 270 LYS B O   1 
ATOM   5594 C CB  . LYS B 1 270 ? 2.59200   45.66300  18.45300 1.000 37.19000 ? 270 LYS B CB  1 
ATOM   5595 C CG  . LYS B 1 270 ? 2.85800   47.16300  18.53100 1.000 37.19000 ? 270 LYS B CG  1 
ATOM   5596 C CD  . LYS B 1 270 ? 2.41100   47.73500  19.87400 1.000 37.19000 ? 270 LYS B CD  1 
ATOM   5597 C CE  . LYS B 1 270 ? 2.89600   49.16500  20.06800 1.000 37.19000 ? 270 LYS B CE  1 
ATOM   5598 N NZ  . LYS B 1 270 ? 2.59100   49.67700  21.43400 1.000 37.19000 ? 270 LYS B NZ  1 
ATOM   5599 N N   . ALA B 1 271 ? 3.71900   42.52700  19.65500 1.000 31.54000 ? 271 ALA B N   1 
ATOM   5600 C CA  . ALA B 1 271 ? 3.47200   41.09300  19.62100 1.000 31.54000 ? 271 ALA B CA  1 
ATOM   5601 C C   . ALA B 1 271 ? 4.55700   40.40200  20.43000 1.000 31.54000 ? 271 ALA B C   1 
ATOM   5602 O O   . ALA B 1 271 ? 5.73400   40.75600  20.32200 1.000 31.54000 ? 271 ALA B O   1 
ATOM   5603 C CB  . ALA B 1 271 ? 3.45500   40.55300  18.18700 1.000 31.54000 ? 271 ALA B CB  1 
ATOM   5604 N N   . SER B 1 272 ? 4.16700   39.40200  21.21800 1.000 27.37000 ? 272 SER B N   1 
ATOM   5605 C CA  . SER B 1 272 ? 5.11300   38.77900  22.13300 1.000 27.37000 ? 272 SER B CA  1 
ATOM   5606 C C   . SER B 1 272 ? 4.87000   37.28100  22.23000 1.000 27.37000 ? 272 SER B C   1 
ATOM   5607 O O   . SER B 1 272 ? 3.73600   36.80500  22.13800 1.000 27.37000 ? 272 SER B O   1 
ATOM   5608 C CB  . SER B 1 272 ? 5.03500   39.39700  23.53600 1.000 27.37000 ? 272 SER B CB  1 
ATOM   5609 O OG  . SER B 1 272 ? 3.82900   39.03700  24.18400 1.000 27.37000 ? 272 SER B OG  1 
ATOM   5610 N N   . MET B 1 273 ? 5.96100   36.54600  22.43100 1.000 22.89000 ? 273 MET B N   1 
ATOM   5611 C CA  . MET B 1 273 ? 5.92300   35.12400  22.72800 1.000 22.89000 ? 273 MET B CA  1 
ATOM   5612 C C   . MET B 1 273 ? 6.92700   34.83900  23.83400 1.000 22.89000 ? 273 MET B C   1 
ATOM   5613 O O   . MET B 1 273 ? 7.93600   35.53500  23.97100 1.000 22.89000 ? 273 MET B O   1 
ATOM   5614 C CB  . MET B 1 273 ? 6.23800   34.26400  21.48900 1.000 22.89000 ? 273 MET B CB  1 
ATOM   5615 C CG  . MET B 1 273 ? 6.05800   32.76500  21.71500 1.000 22.89000 ? 273 MET B CG  1 
ATOM   5616 S SD  . MET B 1 273 ? 6.37600   31.72100  20.27800 1.000 22.89000 ? 273 MET B SD  1 
ATOM   5617 C CE  . MET B 1 273 ? 8.16400   31.75500  20.22000 1.000 22.89000 ? 273 MET B CE  1 
ATOM   5618 N N   . SER B 1 274 ? 6.63300   33.82200  24.63800 1.000 23.26000 ? 274 SER B N   1 
ATOM   5619 C CA  . SER B 1 274 ? 7.51600   33.43000  25.72400 1.000 23.26000 ? 274 SER B CA  1 
ATOM   5620 C C   . SER B 1 274 ? 7.50700   31.91900  25.87200 1.000 23.26000 ? 274 SER B C   1 
ATOM   5621 O O   . SER B 1 274 ? 6.45100   31.28200  25.79400 1.000 23.26000 ? 274 SER B O   1 
ATOM   5622 C CB  . SER B 1 274 ? 7.10500   34.08000  27.04800 1.000 23.26000 ? 274 SER B CB  1 
ATOM   5623 O OG  . SER B 1 274 ? 5.89300   33.53400  27.53900 1.000 23.26000 ? 274 SER B OG  1 
ATOM   5624 N N   . ILE B 1 275 ? 8.69400   31.35900  26.09300 1.000 19.24000 ? 275 ILE B N   1 
ATOM   5625 C CA  . ILE B 1 275 ? 8.88500   29.93400  26.33100 1.000 19.24000 ? 275 ILE B CA  1 
ATOM   5626 C C   . ILE B 1 275 ? 9.38900   29.77700  27.75700 1.000 19.24000 ? 275 ILE B C   1 
ATOM   5627 O O   . ILE B 1 275 ? 10.43900  30.32600  28.11100 1.000 19.24000 ? 275 ILE B O   1 
ATOM   5628 C CB  . ILE B 1 275 ? 9.87900   29.32000  25.33300 1.000 19.24000 ? 275 ILE B CB  1 
ATOM   5629 C CG1 . ILE B 1 275 ? 9.68700   29.92400  23.94200 1.000 19.24000 ? 275 ILE B CG1 1 
ATOM   5630 C CG2 . ILE B 1 275 ? 9.72300   27.81000  25.28900 1.000 19.24000 ? 275 ILE B CG2 1 
ATOM   5631 C CD1 . ILE B 1 275 ? 10.72900  29.48500  22.93900 1.000 19.24000 ? 275 ILE B CD1 1 
ATOM   5632 N N   . SER B 1 276 ? 8.64700   29.04300  28.58000 1.000 17.57000 ? 276 SER B N   1 
ATOM   5633 C CA  . SER B 1 276 ? 9.07900   28.83300  29.95600 1.000 17.57000 ? 276 SER B CA  1 
ATOM   5634 C C   . SER B 1 276 ? 10.23900  27.84800  30.00200 1.000 17.57000 ? 276 SER B C   1 
ATOM   5635 O O   . SER B 1 276 ? 10.16200  26.75300  29.43700 1.000 17.57000 ? 276 SER B O   1 
ATOM   5636 C CB  . SER B 1 276 ? 7.92200   28.31500  30.80900 1.000 17.57000 ? 276 SER B CB  1 
ATOM   5637 O OG  . SER B 1 276 ? 6.88300   29.27200  30.89600 1.000 17.57000 ? 276 SER B OG  1 
ATOM   5638 N N   . ILE B 1 277 ? 11.31500  28.23700  30.67700 1.000 14.33000 ? 277 ILE B N   1 
ATOM   5639 C CA  . ILE B 1 277 ? 12.39300  27.32400  31.03300 1.000 14.33000 ? 277 ILE B CA  1 
ATOM   5640 C C   . ILE B 1 277 ? 12.18300  26.91100  32.48100 1.000 14.33000 ? 277 ILE B C   1 
ATOM   5641 O O   . ILE B 1 277 ? 12.03500  27.76500  33.36200 1.000 14.33000 ? 277 ILE B O   1 
ATOM   5642 C CB  . ILE B 1 277 ? 13.77100  27.97500  30.83000 1.000 14.33000 ? 277 ILE B CB  1 
ATOM   5643 C CG1 . ILE B 1 277 ? 13.91100  28.46100  29.38700 1.000 14.33000 ? 277 ILE B CG1 1 
ATOM   5644 C CG2 . ILE B 1 277 ? 14.88100  26.99900  31.18300 1.000 14.33000 ? 277 ILE B CG2 1 
ATOM   5645 C CD1 . ILE B 1 277 ? 13.71100  27.37500  28.35600 1.000 14.33000 ? 277 ILE B CD1 1 
ATOM   5646 N N   . ILE B 1 278 ? 12.17400  25.60700  32.73700 1.000 16.96000 ? 278 ILE B N   1 
ATOM   5647 C CA  . ILE B 1 278 ? 11.75300  25.08200  34.02900 1.000 16.96000 ? 278 ILE B CA  1 
ATOM   5648 C C   . ILE B 1 278 ? 12.77000  24.06500  34.52200 1.000 16.96000 ? 278 ILE B C   1 
ATOM   5649 O O   . ILE B 1 278 ? 13.23200  23.21200  33.75700 1.000 16.96000 ? 278 ILE B O   1 
ATOM   5650 C CB  . ILE B 1 278 ? 10.34600  24.45400  33.94200 1.000 16.96000 ? 278 ILE B CB  1 
ATOM   5651 C CG1 . ILE B 1 278 ? 9.29700   25.54900  33.73900 1.000 16.96000 ? 278 ILE B CG1 1 
ATOM   5652 C CG2 . ILE B 1 278 ? 10.04000  23.63000  35.18200 1.000 16.96000 ? 278 ILE B CG2 1 
ATOM   5653 C CD1 . ILE B 1 278 ? 7.87800   25.04200  33.72200 1.000 16.96000 ? 278 ILE B CD1 1 
ATOM   5654 N N   . LYS B 1 279 ? 13.10900  24.15300  35.80600 1.000 17.24000 ? 279 LYS B N   1 
ATOM   5655 C CA  . LYS B 1 279 ? 13.97600  23.18300  36.45600 1.000 17.24000 ? 279 LYS B CA  1 
ATOM   5656 C C   . LYS B 1 279 ? 13.48000  22.95900  37.87500 1.000 17.24000 ? 279 LYS B C   1 
ATOM   5657 O O   . LYS B 1 279 ? 13.20700  23.92400  38.59600 1.000 17.24000 ? 279 LYS B O   1 
ATOM   5658 C CB  . LYS B 1 279 ? 15.43300  23.65900  36.47200 1.000 17.24000 ? 279 LYS B CB  1 
ATOM   5659 C CG  . LYS B 1 279 ? 16.37000  22.73900  37.23300 1.000 17.24000 ? 279 LYS B CG  1 
ATOM   5660 C CD  . LYS B 1 279 ? 17.80100  23.24500  37.20400 1.000 17.24000 ? 279 LYS B CD  1 
ATOM   5661 C CE  . LYS B 1 279 ? 18.71700  22.33300  38.00800 1.000 17.24000 ? 279 LYS B CE  1 
ATOM   5662 N NZ  . LYS B 1 279 ? 20.13100  22.79600  37.99700 1.000 17.24000 ? 279 LYS B NZ  1 
ATOM   5663 N N   . ASN B 1 280 ? 13.38200  21.68800  38.27000 1.000 20.03000 ? 280 ASN B N   1 
ATOM   5664 C CA  . ASN B 1 280 ? 12.89900  21.30500  39.59800 1.000 20.03000 ? 280 ASN B CA  1 
ATOM   5665 C C   . ASN B 1 280 ? 11.52100  21.90000  39.87400 1.000 20.03000 ? 280 ASN B C   1 
ATOM   5666 O O   . ASN B 1 280 ? 11.22300  22.34600  40.98500 1.000 20.03000 ? 280 ASN B O   1 
ATOM   5667 C CB  . ASN B 1 280 ? 13.89700  21.70900  40.68500 1.000 20.03000 ? 280 ASN B CB  1 
ATOM   5668 C CG  . ASN B 1 280 ? 15.26000  21.07400  40.49100 1.000 20.03000 ? 280 ASN B CG  1 
ATOM   5669 O OD1 . ASN B 1 280 ? 15.36500  19.92400  40.06300 1.000 20.03000 ? 280 ASN B OD1 1 
ATOM   5670 N ND2 . ASN B 1 280 ? 16.31300  21.82300  40.79900 1.000 20.03000 ? 280 ASN B ND2 1 
ATOM   5671 N N   . ASN B 1 281 ? 10.67600  21.91200  38.84200 1.000 21.49000 ? 281 ASN B N   1 
ATOM   5672 C CA  . ASN B 1 281 ? 9.33200   22.48500  38.89300 1.000 21.49000 ? 281 ASN B CA  1 
ATOM   5673 C C   . ASN B 1 281 ? 9.34100   23.95000  39.31200 1.000 21.49000 ? 281 ASN B C   1 
ATOM   5674 O O   . ASN B 1 281 ? 8.35100   24.45100  39.85300 1.000 21.49000 ? 281 ASN B O   1 
ATOM   5675 C CB  . ASN B 1 281 ? 8.41700   21.68000  39.82100 1.000 21.49000 ? 281 ASN B CB  1 
ATOM   5676 C CG  . ASN B 1 281 ? 8.20700   20.26400  39.34000 1.000 21.49000 ? 281 ASN B CG  1 
ATOM   5677 O OD1 . ASN B 1 281 ? 7.23800   19.97300  38.64000 1.000 21.49000 ? 281 ASN B OD1 1 
ATOM   5678 N ND2 . ASN B 1 281 ? 9.12200   19.37400  39.70300 1.000 21.49000 ? 281 ASN B ND2 1 
ATOM   5679 N N   . LYS B 1 282 ? 10.44300  24.65000  39.07200 1.000 18.37000 ? 282 LYS B N   1 
ATOM   5680 C CA  . LYS B 1 282 ? 10.53900  26.07900  39.32600 1.000 18.37000 ? 282 LYS B CA  1 
ATOM   5681 C C   . LYS B 1 282 ? 10.91000  26.77700  38.02600 1.000 18.37000 ? 282 LYS B C   1 
ATOM   5682 O O   . LYS B 1 282 ? 11.66700  26.23500  37.21400 1.000 18.37000 ? 282 LYS B O   1 
ATOM   5683 C CB  . LYS B 1 282 ? 11.57300  26.38500  40.42200 1.000 18.37000 ? 282 LYS B CB  1 
ATOM   5684 C CG  . LYS B 1 282 ? 11.72700  27.86600  40.75000 1.000 18.37000 ? 282 LYS B CG  1 
ATOM   5685 C CD  . LYS B 1 282 ? 12.72000  28.10300  41.88100 1.000 18.37000 ? 282 LYS B CD  1 
ATOM   5686 C CE  . LYS B 1 282 ? 12.20600  27.54700  43.20000 1.000 18.37000 ? 282 LYS B CE  1 
ATOM   5687 N NZ  . LYS B 1 282 ? 13.10000  27.88700  44.34400 1.000 18.37000 ? 282 LYS B NZ  1 
ATOM   5688 N N   . LEU B 1 283 ? 10.37400  27.97600  37.83000 1.000 15.00000 ? 283 LEU B N   1 
ATOM   5689 C CA  . LEU B 1 283 ? 10.63600  28.72900  36.60800 1.000 15.00000 ? 283 LEU B CA  1 
ATOM   5690 C C   . LEU B 1 283 ? 12.07900  29.21300  36.64300 1.000 15.00000 ? 283 LEU B C   1 
ATOM   5691 O O   . LEU B 1 283 ? 12.39300  30.23200  37.25900 1.000 15.00000 ? 283 LEU B O   1 
ATOM   5692 C CB  . LEU B 1 283 ? 9.65900   29.89200  36.47800 1.000 15.00000 ? 283 LEU B CB  1 
ATOM   5693 C CG  . LEU B 1 283 ? 9.59800   30.57300  35.11100 1.000 15.00000 ? 283 LEU B CG  1 
ATOM   5694 C CD1 . LEU B 1 283 ? 9.25200   29.56500  34.03000 1.000 15.00000 ? 283 LEU B CD1 1 
ATOM   5695 C CD2 . LEU B 1 283 ? 8.58900   31.70800  35.12800 1.000 15.00000 ? 283 LEU B CD2 1 
ATOM   5696 N N   . TRP B 1 284 ? 12.97000  28.45600  36.00100 1.000 13.30000 ? 284 TRP B N   1 
ATOM   5697 C CA  . TRP B 1 284 ? 14.37900  28.82100  35.95300 1.000 13.30000 ? 284 TRP B CA  1 
ATOM   5698 C C   . TRP B 1 284 ? 14.62900  30.05900  35.10300 1.000 13.30000 ? 284 TRP B C   1 
ATOM   5699 O O   . TRP B 1 284 ? 15.65500  30.72300  35.28300 1.000 13.30000 ? 284 TRP B O   1 
ATOM   5700 C CB  . TRP B 1 284 ? 15.19800  27.64400  35.41900 1.000 13.30000 ? 284 TRP B CB  1 
ATOM   5701 C CG  . TRP B 1 284 ? 16.67800  27.83000  35.52100 1.000 13.30000 ? 284 TRP B CG  1 
ATOM   5702 C CD1 . TRP B 1 284 ? 17.47900  27.46200  36.56100 1.000 13.30000 ? 284 TRP B CD1 1 
ATOM   5703 C CD2 . TRP B 1 284 ? 17.54200  28.41600  34.53900 1.000 13.30000 ? 284 TRP B CD2 1 
ATOM   5704 N NE1 . TRP B 1 284 ? 18.78500  27.78700  36.29200 1.000 13.30000 ? 284 TRP B NE1 1 
ATOM   5705 C CE2 . TRP B 1 284 ? 18.85000  28.37500  35.05600 1.000 13.30000 ? 284 TRP B CE2 1 
ATOM   5706 C CE3 . TRP B 1 284 ? 17.33400  28.97500  33.27400 1.000 13.30000 ? 284 TRP B CE3 1 
ATOM   5707 C CZ2 . TRP B 1 284 ? 19.94600  28.87000  34.35500 1.000 13.30000 ? 284 TRP B CZ2 1 
ATOM   5708 C CZ3 . TRP B 1 284 ? 18.42400  29.46700  32.58100 1.000 13.30000 ? 284 TRP B CZ3 1 
ATOM   5709 C CH2 . TRP B 1 284 ? 19.71300  29.40900  33.12100 1.000 13.30000 ? 284 TRP B CH2 1 
ATOM   5710 N N   . GLY B 1 285 ? 13.72700  30.37900  34.18400 1.000 12.58000 ? 285 GLY B N   1 
ATOM   5711 C CA  . GLY B 1 285 ? 13.93100  31.52400  33.32000 1.000 12.58000 ? 285 GLY B CA  1 
ATOM   5712 C C   . GLY B 1 285 ? 12.80800  31.64200  32.31700 1.000 12.58000 ? 285 GLY B C   1 
ATOM   5713 O O   . GLY B 1 285 ? 11.82100  30.90300  32.36600 1.000 12.58000 ? 285 GLY B O   1 
ATOM   5714 N N   . LEU B 1 286 ? 12.96700  32.59400  31.40400 1.000 13.76000 ? 286 LEU B N   1 
ATOM   5715 C CA  . LEU B 1 286 ? 11.98200  32.80300  30.35100 1.000 13.76000 ? 286 LEU B CA  1 
ATOM   5716 C C   . LEU B 1 286 ? 12.67700  33.22700  29.06700 1.000 13.76000 ? 286 LEU B C   1 
ATOM   5717 O O   . LEU B 1 286 ? 13.62400  34.01600  29.09600 1.000 13.76000 ? 286 LEU B O   1 
ATOM   5718 C CB  . LEU B 1 286 ? 10.95000  33.85800  30.76100 1.000 13.76000 ? 286 LEU B CB  1 
ATOM   5719 C CG  . LEU B 1 286 ? 9.81800   33.40200  31.68000 1.000 13.76000 ? 286 LEU B CG  1 
ATOM   5720 C CD1 . LEU B 1 286 ? 9.15400   34.59600  32.34200 1.000 13.76000 ? 286 LEU B CD1 1 
ATOM   5721 C CD2 . LEU B 1 286 ? 8.80100   32.59600  30.89100 1.000 13.76000 ? 286 LEU B CD2 1 
ATOM   5722 N N   . ILE B 1 287 ? 12.19700  32.71400  27.94100 1.000 14.99000 ? 287 ILE B N   1 
ATOM   5723 C CA  . ILE B 1 287 ? 12.70300  33.11500  26.63300 1.000 14.99000 ? 287 ILE B CA  1 
ATOM   5724 C C   . ILE B 1 287 ? 11.68600  34.10400  26.07900 1.000 14.99000 ? 287 ILE B C   1 
ATOM   5725 O O   . ILE B 1 287 ? 10.69200  33.72100  25.46000 1.000 14.99000 ? 287 ILE B O   1 
ATOM   5726 C CB  . ILE B 1 287 ? 12.91700  31.92400  25.70300 1.000 14.99000 ? 287 ILE B CB  1 
ATOM   5727 C CG1 . ILE B 1 287 ? 13.80300  30.88200  26.37800 1.000 14.99000 ? 287 ILE B CG1 1 
ATOM   5728 C CG2 . ILE B 1 287 ? 13.57000  32.37500  24.40800 1.000 14.99000 ? 287 ILE B CG2 1 
ATOM   5729 C CD1 . ILE B 1 287 ? 14.01400  29.64900  25.54100 1.000 14.99000 ? 287 ILE B CD1 1 
ATOM   5730 N N   . ALA B 1 288 ? 11.93600  35.39100  26.30600 1.000 16.11000 ? 288 ALA B N   1 
ATOM   5731 C CA  . ALA B 1 288 ? 11.00400  36.42200  25.86900 1.000 16.11000 ? 288 ALA B CA  1 
ATOM   5732 C C   . ALA B 1 288 ? 11.23000  36.75100  24.40000 1.000 16.11000 ? 288 ALA B C   1 
ATOM   5733 O O   . ALA B 1 288 ? 12.35100  37.07100  23.99000 1.000 16.11000 ? 288 ALA B O   1 
ATOM   5734 C CB  . ALA B 1 288 ? 11.15400  37.68000  26.72000 1.000 16.11000 ? 288 ALA B CB  1 
ATOM   5735 N N   . CYS B 1 289 ? 10.16400  36.66000  23.61100 1.000 21.11000 ? 289 CYS B N   1 
ATOM   5736 C CA  . CYS B 1 289 ? 10.16300  37.07700  22.21900 1.000 21.11000 ? 289 CYS B CA  1 
ATOM   5737 C C   . CYS B 1 289 ? 9.35200   38.35700  22.07800 1.000 21.11000 ? 289 CYS B C   1 
ATOM   5738 O O   . CYS B 1 289 ? 8.30600   38.51500  22.71700 1.000 21.11000 ? 289 CYS B O   1 
ATOM   5739 C CB  . CYS B 1 289 ? 9.58700   35.98200  21.31700 1.000 21.11000 ? 289 CYS B CB  1 
ATOM   5740 S SG  . CYS B 1 289 ? 10.44800  34.39200  21.43100 1.000 21.11000 ? 289 CYS B SG  1 
ATOM   5741 N N   . HIS B 1 290 ? 9.83200   39.25900  21.22800 1.000 25.35000 ? 290 HIS B N   1 
ATOM   5742 C CA  . HIS B 1 290 ? 9.23800   40.57300  21.04900 1.000 25.35000 ? 290 HIS B CA  1 
ATOM   5743 C C   . HIS B 1 290 ? 9.25100   40.92300  19.57000 1.000 25.35000 ? 290 HIS B C   1 
ATOM   5744 O O   . HIS B 1 290 ? 10.22700  40.64200  18.86600 1.000 25.35000 ? 290 HIS B O   1 
ATOM   5745 C CB  . HIS B 1 290 ? 9.99600   41.63900  21.85100 1.000 25.35000 ? 290 HIS B CB  1 
ATOM   5746 C CG  . HIS B 1 290 ? 9.80200   41.53400  23.33100 1.000 25.35000 ? 290 HIS B CG  1 
ATOM   5747 N ND1 . HIS B 1 290 ? 10.82300  41.74400  24.23300 1.000 25.35000 ? 290 HIS B ND1 1 
ATOM   5748 C CD2 . HIS B 1 290 ? 8.70300   41.24800  24.06800 1.000 25.35000 ? 290 HIS B CD2 1 
ATOM   5749 C CE1 . HIS B 1 290 ? 10.36400  41.58300  25.46100 1.000 25.35000 ? 290 HIS B CE1 1 
ATOM   5750 N NE2 . HIS B 1 290 ? 9.07900   41.28500  25.38900 1.000 25.35000 ? 290 HIS B NE2 1 
ATOM   5751 N N   . HIS B 1 291 ? 8.17000   41.55200  19.11100 1.000 29.47000 ? 291 HIS B N   1 
ATOM   5752 C CA  . HIS B 1 291 ? 8.01700   41.91600  17.70900 1.000 29.47000 ? 291 HIS B CA  1 
ATOM   5753 C C   . HIS B 1 291 ? 7.43100   43.31500  17.62100 1.000 29.47000 ? 291 HIS B C   1 
ATOM   5754 O O   . HIS B 1 291 ? 6.46000   43.62700  18.31900 1.000 29.47000 ? 291 HIS B O   1 
ATOM   5755 C CB  . HIS B 1 291 ? 7.11200   40.91600  16.97700 1.000 29.47000 ? 291 HIS B CB  1 
ATOM   5756 C CG  . HIS B 1 291 ? 7.48800   40.69400  15.54500 1.000 29.47000 ? 291 HIS B CG  1 
ATOM   5757 N ND1 . HIS B 1 291 ? 6.58000   40.28900  14.59100 1.000 29.47000 ? 291 HIS B ND1 1 
ATOM   5758 C CD2 . HIS B 1 291 ? 8.67700   40.80800  14.90900 1.000 29.47000 ? 291 HIS B CD2 1 
ATOM   5759 C CE1 . HIS B 1 291 ? 7.19300   40.16800  13.42700 1.000 29.47000 ? 291 HIS B CE1 1 
ATOM   5760 N NE2 . HIS B 1 291 ? 8.46500   40.47900  13.59200 1.000 29.47000 ? 291 HIS B NE2 1 
ATOM   5761 N N   . GLN B 1 292 ? 8.02300   44.15600  16.77100 1.000 33.98000 ? 292 GLN B N   1 
ATOM   5762 C CA  . GLN B 1 292 ? 7.47600   45.49200  16.55700 1.000 33.98000 ? 292 GLN B CA  1 
ATOM   5763 C C   . GLN B 1 292 ? 6.14300   45.42000  15.82200 1.000 33.98000 ? 292 GLN B C   1 
ATOM   5764 O O   . GLN B 1 292 ? 5.15300   46.03400  16.23900 1.000 33.98000 ? 292 GLN B O   1 
ATOM   5765 C CB  . GLN B 1 292 ? 8.48100   46.34300  15.77600 1.000 33.98000 ? 292 GLN B CB  1 
ATOM   5766 C CG  . GLN B 1 292 ? 8.09100   47.80500  15.61800 1.000 33.98000 ? 292 GLN B CG  1 
ATOM   5767 C CD  . GLN B 1 292 ? 8.38100   48.62300  16.86100 1.000 33.98000 ? 292 GLN B CD  1 
ATOM   5768 O OE1 . GLN B 1 292 ? 9.05500   48.15900  17.78100 1.000 33.98000 ? 292 GLN B OE1 1 
ATOM   5769 N NE2 . GLN B 1 292 ? 7.87300   49.85100  16.89400 1.000 33.98000 ? 292 GLN B NE2 1 
ATOM   5770 N N   . THR B 1 293 ? 6.10200   44.66900  14.72900 1.000 32.57000 ? 293 THR B N   1 
ATOM   5771 C CA  . THR B 1 293 ? 4.88200   44.40400  13.98900 1.000 32.57000 ? 293 THR B CA  1 
ATOM   5772 C C   . THR B 1 293 ? 4.06100   43.32300  14.68400 1.000 32.57000 ? 293 THR B C   1 
ATOM   5773 O O   . THR B 1 293 ? 4.59500   42.52700  15.46000 1.000 32.57000 ? 293 THR B O   1 
ATOM   5774 C CB  . THR B 1 293 ? 5.21800   43.97300  12.56500 1.000 32.57000 ? 293 THR B CB  1 
ATOM   5775 O OG1 . THR B 1 293 ? 5.80700   42.66700  12.58400 1.000 32.57000 ? 293 THR B OG1 1 
ATOM   5776 C CG2 . THR B 1 293 ? 6.19800   44.95000  11.93200 1.000 32.57000 ? 293 THR B CG2 1 
ATOM   5777 N N   . PRO B 1 294 ? 2.75200   43.28200  14.44000 1.000 31.91000 ? 294 PRO B N   1 
ATOM   5778 C CA  . PRO B 1 294 ? 1.95500   42.15300  14.93300 1.000 31.91000 ? 294 PRO B CA  1 
ATOM   5779 C C   . PRO B 1 294 ? 2.41100   40.84700  14.29600 1.000 31.91000 ? 294 PRO B C   1 
ATOM   5780 O O   . PRO B 1 294 ? 2.81600   40.80400  13.12900 1.000 31.91000 ? 294 PRO B O   1 
ATOM   5781 C CB  . PRO B 1 294 ? 0.52500   42.51200  14.51200 1.000 31.91000 ? 294 PRO B CB  1 
ATOM   5782 C CG  . PRO B 1 294 ? 0.69700   43.46800  13.37200 1.000 31.91000 ? 294 PRO B CG  1 
ATOM   5783 C CD  . PRO B 1 294 ? 1.92300   44.26000  13.71200 1.000 31.91000 ? 294 PRO B CD  1 
ATOM   5784 N N   . LYS B 1 295 ? 2.34600   39.77200  15.07900 1.000 27.82000 ? 295 LYS B N   1 
ATOM   5785 C CA  . LYS B 1 295 ? 2.76800   38.45400  14.62700 1.000 27.82000 ? 295 LYS B CA  1 
ATOM   5786 C C   . LYS B 1 295 ? 1.80700   37.40700  15.16400 1.000 27.82000 ? 295 LYS B C   1 
ATOM   5787 O O   . LYS B 1 295 ? 1.38600   37.47500  16.32000 1.000 27.82000 ? 295 LYS B O   1 
ATOM   5788 C CB  . LYS B 1 295 ? 4.20100   38.14100  15.08200 1.000 27.82000 ? 295 LYS B CB  1 
ATOM   5789 C CG  . LYS B 1 295 ? 4.67200   36.73000  14.76500 1.000 27.82000 ? 295 LYS B CG  1 
ATOM   5790 C CD  . LYS B 1 295 ? 6.14800   36.55800  15.08300 1.000 27.82000 ? 295 LYS B CD  1 
ATOM   5791 C CE  . LYS B 1 295 ? 7.01700   36.77300  13.85500 1.000 27.82000 ? 295 LYS B CE  1 
ATOM   5792 N NZ  . LYS B 1 295 ? 6.83400   35.68500  12.85300 1.000 27.82000 ? 295 LYS B NZ  1 
ATOM   5793 N N   . TYR B 1 296 ? 1.47000   36.43600  14.32000 1.000 32.06000 ? 296 TYR B N   1 
ATOM   5794 C CA  . TYR B 1 296 ? 0.53300   35.36500  14.65300 1.000 32.06000 ? 296 TYR B CA  1 
ATOM   5795 C C   . TYR B 1 296 ? 1.25700   34.03800  14.44900 1.000 32.06000 ? 296 TYR B C   1 
ATOM   5796 O O   . TYR B 1 296 ? 1.22700   33.46500  13.35600 1.000 32.06000 ? 296 TYR B O   1 
ATOM   5797 C CB  . TYR B 1 296 ? -0.73700  35.45800  13.79700 1.000 32.06000 ? 296 TYR B CB  1 
ATOM   5798 C CG  . TYR B 1 296 ? -1.62200  36.63800  14.13500 1.000 32.06000 ? 296 TYR B CG  1 
ATOM   5799 C CD1 . TYR B 1 296 ? -1.29300  37.92100  13.71900 1.000 32.06000 ? 296 TYR B CD1 1 
ATOM   5800 C CD2 . TYR B 1 296 ? -2.79000  36.46500  14.86700 1.000 32.06000 ? 296 TYR B CD2 1 
ATOM   5801 C CE1 . TYR B 1 296 ? -2.09900  39.00000  14.02700 1.000 32.06000 ? 296 TYR B CE1 1 
ATOM   5802 C CE2 . TYR B 1 296 ? -3.60300  37.53600  15.17900 1.000 32.06000 ? 296 TYR B CE2 1 
ATOM   5803 C CZ  . TYR B 1 296 ? -3.25300  38.80200  14.75700 1.000 32.06000 ? 296 TYR B CZ  1 
ATOM   5804 O OH  . TYR B 1 296 ? -4.05800  39.87500  15.06500 1.000 32.06000 ? 296 TYR B OH  1 
ATOM   5805 N N   . VAL B 1 297 ? 1.90500   33.55300  15.50200 1.000 33.03000 ? 297 VAL B N   1 
ATOM   5806 C CA  . VAL B 1 297 ? 2.69300   32.31900  15.39200 1.000 33.03000 ? 297 VAL B CA  1 
ATOM   5807 C C   . VAL B 1 297 ? 1.75100   31.12900  15.24000 1.000 33.03000 ? 297 VAL B C   1 
ATOM   5808 O O   . VAL B 1 297 ? 0.85400   30.93600  16.08000 1.000 33.03000 ? 297 VAL B O   1 
ATOM   5809 C CB  . VAL B 1 297 ? 3.60200   32.15100  16.61400 1.000 33.03000 ? 297 VAL B CB  1 
ATOM   5810 C CG1 . VAL B 1 297 ? 4.56800   30.98800  16.40400 1.000 33.03000 ? 297 VAL B CG1 1 
ATOM   5811 C CG2 . VAL B 1 297 ? 4.36200   33.43800  16.89900 1.000 33.03000 ? 297 VAL B CG2 1 
ATOM   5812 N N   . PRO B 1 298 ? 1.91800   30.31200  14.20500 1.000 36.48000 ? 298 PRO B N   1 
ATOM   5813 C CA  . PRO B 1 298 ? 1.07800   29.12000  14.04600 1.000 36.48000 ? 298 PRO B CA  1 
ATOM   5814 C C   . PRO B 1 298 ? 1.37800   28.07700  15.11000 1.000 36.48000 ? 298 PRO B C   1 
ATOM   5815 O O   . PRO B 1 298 ? 2.44900   28.05600  15.71900 1.000 36.48000 ? 298 PRO B O   1 
ATOM   5816 C CB  . PRO B 1 298 ? 1.44200   28.61000  12.64800 1.000 36.48000 ? 298 PRO B CB  1 
ATOM   5817 C CG  . PRO B 1 298 ? 2.81500   29.13200  12.40600 1.000 36.48000 ? 298 PRO B CG  1 
ATOM   5818 C CD  . PRO B 1 298 ? 2.89300   30.45700  13.10800 1.000 36.48000 ? 298 PRO B CD  1 
ATOM   5819 N N   . TYR B 1 299 ? 0.38900   27.20800  15.34100 1.000 38.40000 ? 299 TYR B N   1 
ATOM   5820 C CA  . TYR B 1 299 ? 0.51600   26.20400  16.39200 1.000 38.40000 ? 299 TYR B CA  1 
ATOM   5821 C C   . TYR B 1 299 ? 1.69100   25.26600  16.14700 1.000 38.40000 ? 299 TYR B C   1 
ATOM   5822 O O   . TYR B 1 299 ? 2.27700   24.75200  17.10300 1.000 38.40000 ? 299 TYR B O   1 
ATOM   5823 C CB  . TYR B 1 299 ? -0.78000  25.39900  16.51700 1.000 38.40000 ? 299 TYR B CB  1 
ATOM   5824 C CG  . TYR B 1 299 ? -0.81900  24.47600  17.72000 1.000 38.40000 ? 299 TYR B CG  1 
ATOM   5825 C CD1 . TYR B 1 299 ? -0.25400  23.20700  17.67000 1.000 38.40000 ? 299 TYR B CD1 1 
ATOM   5826 C CD2 . TYR B 1 299 ? -1.42400  24.87400  18.90500 1.000 38.40000 ? 299 TYR B CD2 1 
ATOM   5827 C CE1 . TYR B 1 299 ? -0.28300  22.36500  18.76500 1.000 38.40000 ? 299 TYR B CE1 1 
ATOM   5828 C CE2 . TYR B 1 299 ? -1.46100  24.03400  20.00600 1.000 38.40000 ? 299 TYR B CE2 1 
ATOM   5829 C CZ  . TYR B 1 299 ? -0.89000  22.78100  19.92900 1.000 38.40000 ? 299 TYR B CZ  1 
ATOM   5830 O OH  . TYR B 1 299 ? -0.92200  21.94100  21.01900 1.000 38.40000 ? 299 TYR B OH  1 
ATOM   5831 N N   . GLU B 1 300 ? 2.05400   25.02700  14.88700 1.000 40.85000 ? 300 GLU B N   1 
ATOM   5832 C CA  . GLU B 1 300 ? 3.18000   24.13800  14.61500 1.000 40.85000 ? 300 GLU B CA  1 
ATOM   5833 C C   . GLU B 1 300 ? 4.49300   24.75600  15.08300 1.000 40.85000 ? 300 GLU B C   1 
ATOM   5834 O O   . GLU B 1 300 ? 5.26600   24.12400  15.81500 1.000 40.85000 ? 300 GLU B O   1 
ATOM   5835 C CB  . GLU B 1 300 ? 3.23400   23.80400  13.12400 1.000 40.85000 ? 300 GLU B CB  1 
ATOM   5836 C CG  . GLU B 1 300 ? 2.23100   22.74100  12.67200 1.000 40.85000 ? 300 GLU B CG  1 
ATOM   5837 C CD  . GLU B 1 300 ? 0.78100   23.20700  12.72000 1.000 40.85000 ? 300 GLU B CD  1 
ATOM   5838 O OE1 . GLU B 1 300 ? 0.53200   24.40500  12.97600 1.000 40.85000 ? 300 GLU B OE1 1 
ATOM   5839 O OE2 . GLU B 1 300 ? -0.11600  22.36700  12.49500 1.000 40.85000 ? 300 GLU B OE2 1 
ATOM   5840 N N   . ILE B 1 301 ? 4.74900   26.00800  14.69400 1.000 36.54000 ? 301 ILE B N   1 
ATOM   5841 C CA  . ILE B 1 301 ? 5.94700   26.69100  15.16900 1.000 36.54000 ? 301 ILE B CA  1 
ATOM   5842 C C   . ILE B 1 301 ? 5.87900   26.90000  16.67500 1.000 36.54000 ? 301 ILE B C   1 
ATOM   5843 O O   . ILE B 1 301 ? 6.90300   26.83800  17.36800 1.000 36.54000 ? 301 ILE B O   1 
ATOM   5844 C CB  . ILE B 1 301 ? 6.13200   28.01900  14.41400 1.000 36.54000 ? 301 ILE B CB  1 
ATOM   5845 C CG1 . ILE B 1 301 ? 6.13300   27.77500  12.90400 1.000 36.54000 ? 301 ILE B CG1 1 
ATOM   5846 C CG2 . ILE B 1 301 ? 7.42100   28.70100  14.83600 1.000 36.54000 ? 301 ILE B CG2 1 
ATOM   5847 C CD1 . ILE B 1 301 ? 6.41800   29.01200  12.08600 1.000 36.54000 ? 301 ILE B CD1 1 
ATOM   5848 N N   . ARG B 1 302 ? 4.67300   27.10700  17.21000 1.000 34.15000 ? 302 ARG B N   1 
ATOM   5849 C CA  . ARG B 1 302 ? 4.51400   27.27500  18.65100 1.000 34.15000 ? 302 ARG B CA  1 
ATOM   5850 C C   . ARG B 1 302 ? 4.93600   26.01800  19.40000 1.000 34.15000 ? 302 ARG B C   1 
ATOM   5851 O O   . ARG B 1 302 ? 5.71800   26.07900  20.35700 1.000 34.15000 ? 302 ARG B O   1 
ATOM   5852 C CB  . ARG B 1 302 ? 3.05900   27.61900  18.96900 1.000 34.15000 ? 302 ARG B CB  1 
ATOM   5853 C CG  . ARG B 1 302 ? 2.73000   29.10000  18.94500 1.000 34.15000 ? 302 ARG B CG  1 
ATOM   5854 C CD  . ARG B 1 302 ? 1.29200   29.33400  19.37900 1.000 34.15000 ? 302 ARG B CD  1 
ATOM   5855 N NE  . ARG B 1 302 ? 0.34300   29.09100  18.30000 1.000 34.15000 ? 302 ARG B NE  1 
ATOM   5856 C CZ  . ARG B 1 302 ? -0.96100  28.93100  18.47400 1.000 34.15000 ? 302 ARG B CZ  1 
ATOM   5857 N NH1 . ARG B 1 302 ? -1.50400  28.94800  19.68100 1.000 34.15000 ? 302 ARG B NH1 1 
ATOM   5858 N NH2 . ARG B 1 302 ? -1.73900  28.74400  17.41200 1.000 34.15000 ? 302 ARG B NH2 1 
ATOM   5859 N N   . HIS B 1 303 ? 4.42200   24.86300  18.97500 1.000 34.51000 ? 303 HIS B N   1 
ATOM   5860 C CA  . HIS B 1 303 ? 4.76700   23.60500  19.62100 1.000 34.51000 ? 303 HIS B CA  1 
ATOM   5861 C C   . HIS B 1 303 ? 6.23400   23.25900  19.42200 1.000 34.51000 ? 303 HIS B C   1 
ATOM   5862 O O   . HIS B 1 303 ? 6.85800   22.67100  20.31400 1.000 34.51000 ? 303 HIS B O   1 
ATOM   5863 C CB  . HIS B 1 303 ? 3.87600   22.48700  19.08200 1.000 34.51000 ? 303 HIS B CB  1 
ATOM   5864 C CG  . HIS B 1 303 ? 3.68600   21.35200  20.03800 1.000 34.51000 ? 303 HIS B CG  1 
ATOM   5865 N ND1 . HIS B 1 303 ? 2.98600   21.48400  21.21800 1.000 34.51000 ? 303 HIS B ND1 1 
ATOM   5866 C CD2 . HIS B 1 303 ? 4.09900   20.06400  19.98700 1.000 34.51000 ? 303 HIS B CD2 1 
ATOM   5867 C CE1 . HIS B 1 303 ? 2.97700   20.32600  21.85300 1.000 34.51000 ? 303 HIS B CE1 1 
ATOM   5868 N NE2 . HIS B 1 303 ? 3.64400   19.44700  21.12700 1.000 34.51000 ? 303 HIS B NE2 1 
ATOM   5869 N N   . ALA B 1 304 ? 6.81100   23.63100  18.27600 1.000 30.79000 ? 304 ALA B N   1 
ATOM   5870 C CA  . ALA B 1 304 ? 8.23600   23.39500  18.08000 1.000 30.79000 ? 304 ALA B CA  1 
ATOM   5871 C C   . ALA B 1 304 ? 9.06600   24.22000  19.05500 1.000 30.79000 ? 304 ALA B C   1 
ATOM   5872 O O   . ALA B 1 304 ? 10.00900  23.70500  19.66700 1.000 30.79000 ? 304 ALA B O   1 
ATOM   5873 C CB  . ALA B 1 304 ? 8.63000   23.70700  16.63700 1.000 30.79000 ? 304 ALA B CB  1 
ATOM   5874 N N   . CYS B 1 305 ? 8.71600   25.49700  19.23300 1.000 27.99000 ? 305 CYS B N   1 
ATOM   5875 C CA  . CYS B 1 305 ? 9.42700   26.31800  20.20600 1.000 27.99000 ? 305 CYS B CA  1 
ATOM   5876 C C   . CYS B 1 305 ? 9.21700   25.81500  21.62800 1.000 27.99000 ? 305 CYS B C   1 
ATOM   5877 O O   . CYS B 1 305 ? 10.13500  25.88800  22.45100 1.000 27.99000 ? 305 CYS B O   1 
ATOM   5878 C CB  . CYS B 1 305 ? 8.98200   27.77400  20.08500 1.000 27.99000 ? 305 CYS B CB  1 
ATOM   5879 S SG  . CYS B 1 305 ? 9.34900   28.51300  18.48400 1.000 27.99000 ? 305 CYS B SG  1 
ATOM   5880 N N   . GLU B 1 306 ? 8.03400   25.28000  21.92900 1.000 28.48000 ? 306 GLU B N   1 
ATOM   5881 C CA  . GLU B 1 306 ? 7.79300   24.74800  23.26700 1.000 28.48000 ? 306 GLU B CA  1 
ATOM   5882 C C   . GLU B 1 306 ? 8.64100   23.50800  23.52900 1.000 28.48000 ? 306 GLU B C   1 
ATOM   5883 O O   . GLU B 1 306 ? 9.20400   23.34600  24.62100 1.000 28.48000 ? 306 GLU B O   1 
ATOM   5884 C CB  . GLU B 1 306 ? 6.30600   24.43900  23.43600 1.000 28.48000 ? 306 GLU B CB  1 
ATOM   5885 C CG  . GLU B 1 306 ? 5.87700   24.13400  24.85700 1.000 28.48000 ? 306 GLU B CG  1 
ATOM   5886 C CD  . GLU B 1 306 ? 4.37000   24.06600  24.99000 1.000 28.48000 ? 306 GLU B CD  1 
ATOM   5887 O OE1 . GLU B 1 306 ? 3.68000   24.16700  23.95400 1.000 28.48000 ? 306 GLU B OE1 1 
ATOM   5888 O OE2 . GLU B 1 306 ? 3.87500   23.91700  26.12700 1.000 28.48000 ? 306 GLU B OE2 1 
ATOM   5889 N N   . PHE B 1 307 ? 8.74900   22.62200  22.53700 1.000 25.87000 ? 307 PHE B N   1 
ATOM   5890 C CA  . PHE B 1 307 ? 9.63800   21.47600  22.68300 1.000 25.87000 ? 307 PHE B CA  1 
ATOM   5891 C C   . PHE B 1 307 ? 11.09600  21.90600  22.78200 1.000 25.87000 ? 307 PHE B C   1 
ATOM   5892 O O   . PHE B 1 307 ? 11.87700  21.29100  23.51800 1.000 25.87000 ? 307 PHE B O   1 
ATOM   5893 C CB  . PHE B 1 307 ? 9.44100   20.51000  21.51600 1.000 25.87000 ? 307 PHE B CB  1 
ATOM   5894 C CG  . PHE B 1 307 ? 10.38600  19.34600  21.52800 1.000 25.87000 ? 307 PHE B CG  1 
ATOM   5895 C CD1 . PHE B 1 307 ? 10.49300  18.53500  22.64500 1.000 25.87000 ? 307 PHE B CD1 1 
ATOM   5896 C CD2 . PHE B 1 307 ? 11.15800  19.05500  20.41800 1.000 25.87000 ? 307 PHE B CD2 1 
ATOM   5897 C CE1 . PHE B 1 307 ? 11.35800  17.46000  22.65800 1.000 25.87000 ? 307 PHE B CE1 1 
ATOM   5898 C CE2 . PHE B 1 307 ? 12.02200  17.98000  20.42600 1.000 25.87000 ? 307 PHE B CE2 1 
ATOM   5899 C CZ  . PHE B 1 307 ? 12.12400  17.18300  21.54600 1.000 25.87000 ? 307 PHE B CZ  1 
ATOM   5900 N N   . LEU B 1 308 ? 11.47700  22.96700  22.06700 1.000 23.06000 ? 308 LEU B N   1 
ATOM   5901 C CA  . LEU B 1 308 ? 12.83200  23.48800  22.20400 1.000 23.06000 ? 308 LEU B CA  1 
ATOM   5902 C C   . LEU B 1 308 ? 13.06500  24.02600  23.60600 1.000 23.06000 ? 308 LEU B C   1 
ATOM   5903 O O   . LEU B 1 308 ? 14.16100  23.88700  24.16000 1.000 23.06000 ? 308 LEU B O   1 
ATOM   5904 C CB  . LEU B 1 308 ? 13.08600  24.58200  21.17500 1.000 23.06000 ? 308 LEU B CB  1 
ATOM   5905 C CG  . LEU B 1 308 ? 13.16000  24.15600  19.71300 1.000 23.06000 ? 308 LEU B CG  1 
ATOM   5906 C CD1 . LEU B 1 308 ? 12.77300  25.32800  18.85200 1.000 23.06000 ? 308 LEU B CD1 1 
ATOM   5907 C CD2 . LEU B 1 308 ? 14.55700  23.67400  19.36500 1.000 23.06000 ? 308 LEU B CD2 1 
ATOM   5908 N N   . GLY B 1 309 ? 12.03400  24.61400  24.21100 1.000 22.27000 ? 309 GLY B N   1 
ATOM   5909 C CA  . GLY B 1 309 ? 12.16900  25.07900  25.58100 1.000 22.27000 ? 309 GLY B CA  1 
ATOM   5910 C C   . GLY B 1 309 ? 12.29600  23.93300  26.56400 1.000 22.27000 ? 309 GLY B C   1 
ATOM   5911 O O   . GLY B 1 309 ? 13.05800  24.01400  27.53100 1.000 22.27000 ? 309 GLY B O   1 
ATOM   5912 N N   . GLN B 1 310 ? 11.58000  22.83600  26.31100 1.000 22.77000 ? 310 GLN B N   1 
ATOM   5913 C CA  . GLN B 1 310 ? 11.74000  21.65000  27.14900 1.000 22.77000 ? 310 GLN B CA  1 
ATOM   5914 C C   . GLN B 1 310 ? 13.15300  21.08500  27.04000 1.000 22.77000 ? 310 GLN B C   1 
ATOM   5915 O O   . GLN B 1 310 ? 13.77400  20.72000  28.05300 1.000 22.77000 ? 310 GLN B O   1 
ATOM   5916 C CB  . GLN B 1 310 ? 10.70900  20.59500  26.74800 1.000 22.77000 ? 310 GLN B CB  1 
ATOM   5917 C CG  . GLN B 1 310 ? 10.75900  19.32500  27.57200 1.000 22.77000 ? 310 GLN B CG  1 
ATOM   5918 C CD  . GLN B 1 310 ? 10.15900  19.50700  28.94900 1.000 22.77000 ? 310 GLN B CD  1 
ATOM   5919 O OE1 . GLN B 1 310 ? 8.95700   19.73700  29.08900 1.000 22.77000 ? 310 GLN B OE1 1 
ATOM   5920 N NE2 . GLN B 1 310 ? 10.99400  19.41100  29.97600 1.000 22.77000 ? 310 GLN B NE2 1 
ATOM   5921 N N   . VAL B 1 311 ? 13.68500  21.02100  25.81700 1.000 20.55000 ? 311 VAL B N   1 
ATOM   5922 C CA  . VAL B 1 311 ? 15.04200  20.51800  25.62300 1.000 20.55000 ? 311 VAL B CA  1 
ATOM   5923 C C   . VAL B 1 311 ? 16.05100  21.44000  26.29500 1.000 20.55000 ? 311 VAL B C   1 
ATOM   5924 O O   . VAL B 1 311 ? 17.01800  20.98100  26.91800 1.000 20.55000 ? 311 VAL B O   1 
ATOM   5925 C CB  . VAL B 1 311 ? 15.33800  20.35200  24.12100 1.000 20.55000 ? 311 VAL B CB  1 
ATOM   5926 C CG1 . VAL B 1 311 ? 16.80100  20.00500  23.89800 1.000 20.55000 ? 311 VAL B CG1 1 
ATOM   5927 C CG2 . VAL B 1 311 ? 14.43800  19.28800  23.51700 1.000 20.55000 ? 311 VAL B CG2 1 
ATOM   5928 N N   . THR B 1 312 ? 15.82700  22.75400  26.20400 1.000 19.44000 ? 312 THR B N   1 
ATOM   5929 C CA  . THR B 1 312 ? 16.71900  23.71000  26.84900 1.000 19.44000 ? 312 THR B CA  1 
ATOM   5930 C C   . THR B 1 312 ? 16.67400  23.57200  28.36200 1.000 19.44000 ? 312 THR B C   1 
ATOM   5931 O O   . THR B 1 312 ? 17.70600  23.67900  29.03300 1.000 19.44000 ? 312 THR B O   1 
ATOM   5932 C CB  . THR B 1 312 ? 16.34100  25.13000  26.43200 1.000 19.44000 ? 312 THR B CB  1 
ATOM   5933 O OG1 . THR B 1 312 ? 16.34800  25.22000  25.00300 1.000 19.44000 ? 312 THR B OG1 1 
ATOM   5934 C CG2 . THR B 1 312 ? 17.32000  26.14100  27.00400 1.000 19.44000 ? 312 THR B CG2 1 
ATOM   5935 N N   . SER B 1 313 ? 15.49100  23.29100  28.91100 1.000 19.20000 ? 313 SER B N   1 
ATOM   5936 C CA  . SER B 1 313 ? 15.36700  23.11600  30.35200 1.000 19.20000 ? 313 SER B CA  1 
ATOM   5937 C C   . SER B 1 313 ? 16.14900  21.89800  30.81700 1.000 19.20000 ? 313 SER B C   1 
ATOM   5938 O O   . SER B 1 313 ? 16.92400  21.96900  31.78200 1.000 19.20000 ? 313 SER B O   1 
ATOM   5939 C CB  . SER B 1 313 ? 13.89200  22.98400  30.73000 1.000 19.20000 ? 313 SER B CB  1 
ATOM   5940 O OG  . SER B 1 313 ? 13.12400  24.04000  30.18000 1.000 19.20000 ? 313 SER B OG  1 
ATOM   5941 N N   . LEU B 1 314 ? 15.97000  20.76800  30.12700 1.000 20.84000 ? 314 LEU B N   1 
ATOM   5942 C CA  . LEU B 1 314 ? 16.69400  19.56600  30.52700 1.000 20.84000 ? 314 LEU B CA  1 
ATOM   5943 C C   . LEU B 1 314 ? 18.19900  19.73500  30.34600 1.000 20.84000 ? 314 LEU B C   1 
ATOM   5944 O O   . LEU B 1 314 ? 18.98700  19.26800  31.18000 1.000 20.84000 ? 314 LEU B O   1 
ATOM   5945 C CB  . LEU B 1 314 ? 16.18100  18.36300  29.73900 1.000 20.84000 ? 314 LEU B CB  1 
ATOM   5946 C CG  . LEU B 1 314 ? 14.71300  18.04100  30.01800 1.000 20.84000 ? 314 LEU B CG  1 
ATOM   5947 C CD1 . LEU B 1 314 ? 14.25300  16.85400  29.19800 1.000 20.84000 ? 314 LEU B CD1 1 
ATOM   5948 C CD2 . LEU B 1 314 ? 14.49900  17.79000  31.50400 1.000 20.84000 ? 314 LEU B CD2 1 
ATOM   5949 N N   . GLU B 1 315 ? 18.61800  20.45300  29.29900 1.000 21.19000 ? 315 GLU B N   1 
ATOM   5950 C CA  . GLU B 1 315 ? 20.04700  20.65200  29.08500 1.000 21.19000 ? 315 GLU B CA  1 
ATOM   5951 C C   . GLU B 1 315 ? 20.65100  21.54600  30.15900 1.000 21.19000 ? 315 GLU B C   1 
ATOM   5952 O O   . GLU B 1 315 ? 21.74000  21.26000  30.66900 1.000 21.19000 ? 315 GLU B O   1 
ATOM   5953 C CB  . GLU B 1 315 ? 20.29600  21.24000  27.69600 1.000 21.19000 ? 315 GLU B CB  1 
ATOM   5954 C CG  . GLU B 1 315 ? 20.29700  20.21000  26.57800 1.000 21.19000 ? 315 GLU B CG  1 
ATOM   5955 C CD  . GLU B 1 315 ? 21.48900  19.27200  26.64600 1.000 21.19000 ? 315 GLU B CD  1 
ATOM   5956 O OE1 . GLU B 1 315 ? 22.51700  19.65400  27.24500 1.000 21.19000 ? 315 GLU B OE1 1 
ATOM   5957 O OE2 . GLU B 1 315 ? 21.39800  18.15300  26.10000 1.000 21.19000 ? 315 GLU B OE2 1 
ATOM   5958 N N   . ILE B 1 316 ? 19.95900  22.62800  30.52000 1.000 19.51000 ? 316 ILE B N   1 
ATOM   5959 C CA  . ILE B 1 316 ? 20.47500  23.51900  31.55200 1.000 19.51000 ? 316 ILE B CA  1 
ATOM   5960 C C   . ILE B 1 316 ? 20.53200  22.80500  32.89500 1.000 19.51000 ? 316 ILE B C   1 
ATOM   5961 O O   . ILE B 1 316 ? 21.48900  22.97500  33.66500 1.000 19.51000 ? 316 ILE B O   1 
ATOM   5962 C CB  . ILE B 1 316 ? 19.62000  24.79700  31.61600 1.000 19.51000 ? 316 ILE B CB  1 
ATOM   5963 C CG1 . ILE B 1 316 ? 19.89600  25.67500  30.39600 1.000 19.51000 ? 316 ILE B CG1 1 
ATOM   5964 C CG2 . ILE B 1 316 ? 19.88000  25.56400  32.90200 1.000 19.51000 ? 316 ILE B CG2 1 
ATOM   5965 C CD1 . ILE B 1 316 ? 19.00600  26.88500  30.30800 1.000 19.51000 ? 316 ILE B CD1 1 
ATOM   5966 N N   . ALA B 1 317 ? 19.53600  21.96100  33.18100 1.000 20.31000 ? 317 ALA B N   1 
ATOM   5967 C CA  . ALA B 1 317 ? 19.57000  21.20800  34.42900 1.000 20.31000 ? 317 ALA B CA  1 
ATOM   5968 C C   . ALA B 1 317 ? 20.74800  20.24400  34.45000 1.000 20.31000 ? 317 ALA B C   1 
ATOM   5969 O O   . ALA B 1 317 ? 21.45100  20.13100  35.46400 1.000 20.31000 ? 317 ALA B O   1 
ATOM   5970 C CB  . ALA B 1 317 ? 18.25300  20.45900  34.62700 1.000 20.31000 ? 317 ALA B CB  1 
ATOM   5971 N N   . THR B 1 318 ? 21.01000  19.57600  33.32100 1.000 22.44000 ? 318 THR B N   1 
ATOM   5972 C CA  . THR B 1 318 ? 22.13800  18.65300  33.26400 1.000 22.44000 ? 318 THR B CA  1 
ATOM   5973 C C   . THR B 1 318 ? 23.46200  19.38600  33.44800 1.000 22.44000 ? 318 THR B C   1 
ATOM   5974 O O   . THR B 1 318 ? 24.33400  18.92900  34.20000 1.000 22.44000 ? 318 THR B O   1 
ATOM   5975 C CB  . THR B 1 318 ? 22.13000  17.89600  31.93600 1.000 22.44000 ? 318 THR B CB  1 
ATOM   5976 O OG1 . THR B 1 318 ? 20.95000  17.08800  31.85100 1.000 22.44000 ? 318 THR B OG1 1 
ATOM   5977 C CG2 . THR B 1 318 ? 23.35900  17.00600  31.82000 1.000 22.44000 ? 318 THR B CG2 1 
ATOM   5978 N N   . LYS B 1 319 ? 23.61700  20.54300  32.79800 1.000 23.64000 ? 319 LYS B N   1 
ATOM   5979 C CA  . LYS B 1 319 ? 24.87300  21.27600  32.91400 1.000 23.64000 ? 319 LYS B CA  1 
ATOM   5980 C C   . LYS B 1 319 ? 25.09900  21.74500  34.34300 1.000 23.64000 ? 319 LYS B C   1 
ATOM   5981 O O   . LYS B 1 319 ? 26.19400  21.58100  34.89600 1.000 23.64000 ? 319 LYS B O   1 
ATOM   5982 C CB  . LYS B 1 319 ? 24.89300  22.47300  31.96300 1.000 23.64000 ? 319 LYS B CB  1 
ATOM   5983 C CG  . LYS B 1 319 ? 24.62300  22.15000  30.51400 1.000 23.64000 ? 319 LYS B CG  1 
ATOM   5984 C CD  . LYS B 1 319 ? 25.59700  21.15000  29.94100 1.000 23.64000 ? 319 LYS B CD  1 
ATOM   5985 C CE  . LYS B 1 319 ? 25.20900  20.82200  28.51400 1.000 23.64000 ? 319 LYS B CE  1 
ATOM   5986 N NZ  . LYS B 1 319 ? 26.10400  19.80600  27.90000 1.000 23.64000 ? 319 LYS B NZ  1 
ATOM   5987 N N   . GLU B 1 320 ? 24.06700  22.32400  34.96700 1.000 22.97000 ? 320 GLU B N   1 
ATOM   5988 C CA  . GLU B 1 320 ? 24.24800  22.84500  36.31700 1.000 22.97000 ? 320 GLU B CA  1 
ATOM   5989 C C   . GLU B 1 320 ? 24.51800  21.72600  37.31300 1.000 22.97000 ? 320 GLU B C   1 
ATOM   5990 O O   . GLU B 1 320 ? 25.36100  21.87400  38.20900 1.000 22.97000 ? 320 GLU B O   1 
ATOM   5991 C CB  . GLU B 1 320 ? 23.02500  23.65800  36.73900 1.000 22.97000 ? 320 GLU B CB  1 
ATOM   5992 C CG  . GLU B 1 320 ? 22.85000  24.95800  35.97500 1.000 22.97000 ? 320 GLU B CG  1 
ATOM   5993 C CD  . GLU B 1 320 ? 21.77600  25.84400  36.57200 1.000 22.97000 ? 320 GLU B CD  1 
ATOM   5994 O OE1 . GLU B 1 320 ? 21.02800  25.36700  37.45200 1.000 22.97000 ? 320 GLU B OE1 1 
ATOM   5995 O OE2 . GLU B 1 320 ? 21.68400  27.02100  36.16400 1.000 22.97000 ? 320 GLU B OE2 1 
ATOM   5996 N N   . ASP B 1 321 ? 23.84500  20.58100  37.15200 1.000 26.74000 ? 321 ASP B N   1 
ATOM   5997 C CA  . ASP B 1 321 ? 24.06900  19.48200  38.08400 1.000 26.74000 ? 321 ASP B CA  1 
ATOM   5998 C C   . ASP B 1 321 ? 25.46300  18.89000  37.91900 1.000 26.74000 ? 321 ASP B C   1 
ATOM   5999 O O   . ASP B 1 321 ? 26.13300  18.58400  38.91400 1.000 26.74000 ? 321 ASP B O   1 
ATOM   6000 C CB  . ASP B 1 321 ? 22.99100  18.41400  37.89900 1.000 26.74000 ? 321 ASP B CB  1 
ATOM   6001 C CG  . ASP B 1 321 ? 21.59700  18.93500  38.20800 1.000 26.74000 ? 321 ASP B CG  1 
ATOM   6002 O OD1 . ASP B 1 321 ? 21.47500  19.85700  39.04300 1.000 26.74000 ? 321 ASP B OD1 1 
ATOM   6003 O OD2 . ASP B 1 321 ? 20.62300  18.42500  37.61400 1.000 26.74000 ? 321 ASP B OD2 1 
ATOM   6004 N N   . ASN B 1 322 ? 25.93400  18.73800  36.67600 1.000 30.78000 ? 322 ASN B N   1 
ATOM   6005 C CA  . ASN B 1 322 ? 27.28400  18.22000  36.47800 1.000 30.78000 ? 322 ASN B CA  1 
ATOM   6006 C C   . ASN B 1 322 ? 28.34100  19.19900  36.98000 1.000 30.78000 ? 322 ASN B C   1 
ATOM   6007 O O   . ASN B 1 322 ? 29.37100  18.78000  37.52400 1.000 30.78000 ? 322 ASN B O   1 
ATOM   6008 C CB  . ASN B 1 322 ? 27.51200  17.88500  35.00500 1.000 30.78000 ? 322 ASN B CB  1 
ATOM   6009 C CG  . ASN B 1 322 ? 27.24700  16.42300  34.69300 1.000 30.78000 ? 322 ASN B CG  1 
ATOM   6010 O OD1 . ASN B 1 322 ? 28.16400  15.60100  34.69000 1.000 30.78000 ? 322 ASN B OD1 1 
ATOM   6011 N ND2 . ASN B 1 322 ? 25.98700  16.09100  34.43500 1.000 30.78000 ? 322 ASN B ND2 1 
ATOM   6012 N N   . GLU B 1 323 ? 28.10100  20.50500  36.83300 1.000 31.61000 ? 323 GLU B N   1 
ATOM   6013 C CA  . GLU B 1 323 ? 29.06600  21.47300  37.34500 1.000 31.61000 ? 323 GLU B CA  1 
ATOM   6014 C C   . GLU B 1 323 ? 29.11700  21.44500  38.86800 1.000 31.61000 ? 323 GLU B C   1 
ATOM   6015 O O   . GLU B 1 323 ? 30.20500  21.50600  39.46200 1.000 31.61000 ? 323 GLU B O   1 
ATOM   6016 C CB  . GLU B 1 323 ? 28.72500  22.87600  36.83800 1.000 31.61000 ? 323 GLU B CB  1 
ATOM   6017 C CG  . GLU B 1 323 ? 28.93900  23.06800  35.34000 1.000 31.61000 ? 323 GLU B CG  1 
ATOM   6018 C CD  . GLU B 1 323 ? 28.27500  24.32500  34.80700 1.000 31.61000 ? 323 GLU B CD  1 
ATOM   6019 O OE1 . GLU B 1 323 ? 27.70900  25.08900  35.61800 1.000 31.61000 ? 323 GLU B OE1 1 
ATOM   6020 O OE2 . GLU B 1 323 ? 28.31400  24.54800  33.57700 1.000 31.61000 ? 323 GLU B OE2 1 
ATOM   6021 N N   . ASP B 1 324 ? 27.95400  21.32600  39.51800 1.000 32.92000 ? 324 ASP B N   1 
ATOM   6022 C CA  . ASP B 1 324 ? 27.94700  21.21400  40.97300 1.000 32.92000 ? 324 ASP B CA  1 
ATOM   6023 C C   . ASP B 1 324 ? 28.63100  19.93200  41.42700 1.000 32.92000 ? 324 ASP B C   1 
ATOM   6024 O O   . ASP B 1 324 ? 29.35700  19.93000  42.42700 1.000 32.92000 ? 324 ASP B O   1 
ATOM   6025 C CB  . ASP B 1 324 ? 26.51500  21.27100  41.50400 1.000 32.92000 ? 324 ASP B CB  1 
ATOM   6026 C CG  . ASP B 1 324 ? 26.10500  22.66600  41.92400 1.000 32.92000 ? 324 ASP B CG  1 
ATOM   6027 O OD1 . ASP B 1 324 ? 26.97100  23.56700  41.93100 1.000 32.92000 ? 324 ASP B OD1 1 
ATOM   6028 O OD2 . ASP B 1 324 ? 24.91400  22.86200  42.24800 1.000 32.92000 ? 324 ASP B OD2 1 
ATOM   6029 N N   . SER B 1 325 ? 28.44600  18.84000  40.68000 1.000 33.56000 ? 325 SER B N   1 
ATOM   6030 C CA  . SER B 1 325 ? 29.09900  17.59000  41.04900 1.000 33.56000 ? 325 SER B CA  1 
ATOM   6031 C C   . SER B 1 325 ? 30.61200  17.69200  40.90100 1.000 33.56000 ? 325 SER B C   1 
ATOM   6032 O O   . SER B 1 325 ? 31.35800  17.19100  41.75000 1.000 33.56000 ? 325 SER B O   1 
ATOM   6033 C CB  . SER B 1 325 ? 28.55000  16.44000  40.20500 1.000 33.56000 ? 325 SER B CB  1 
ATOM   6034 O OG  . SER B 1 325 ? 27.16700  16.24400  40.44700 1.000 33.56000 ? 325 SER B OG  1 
ATOM   6035 N N   . GLU B 1 326 ? 31.08400  18.37200  39.85200 1.000 37.37000 ? 326 GLU B N   1 
ATOM   6036 C CA  . GLU B 1 326 ? 32.52400  18.52800  39.66700 1.000 37.37000 ? 326 GLU B CA  1 
ATOM   6037 C C   . GLU B 1 326 ? 33.13000  19.37500  40.77700 1.000 37.37000 ? 326 GLU B C   1 
ATOM   6038 O O   . GLU B 1 326 ? 34.17200  19.02000  41.34900 1.000 37.37000 ? 326 GLU B O   1 
ATOM   6039 C CB  . GLU B 1 326 ? 32.82300  19.15300  38.30300 1.000 37.37000 ? 326 GLU B CB  1 
ATOM   6040 C CG  . GLU B 1 326 ? 32.61700  18.22900  37.11600 1.000 37.37000 ? 326 GLU B CG  1 
ATOM   6041 C CD  . GLU B 1 326 ? 33.20900  18.79300  35.83700 1.000 37.37000 ? 326 GLU B CD  1 
ATOM   6042 O OE1 . GLU B 1 326 ? 33.96400  19.78600  35.91600 1.000 37.37000 ? 326 GLU B OE1 1 
ATOM   6043 O OE2 . GLU B 1 326 ? 32.92100  18.24400  34.75300 1.000 37.37000 ? 326 GLU B OE2 1 
ATOM   6044 N N   . SER B 1 327 ? 32.48800  20.50300  41.09700 1.000 36.38000 ? 327 SER B N   1 
ATOM   6045 C CA  . SER B 1 327 ? 33.01900  21.35800  42.15400 1.000 36.38000 ? 327 SER B CA  1 
ATOM   6046 C C   . SER B 1 327 ? 32.99100  20.64600  43.50100 1.000 36.38000 ? 327 SER B C   1 
ATOM   6047 O O   . SER B 1 327 ? 33.94000  20.75300  44.29000 1.000 36.38000 ? 327 SER B O   1 
ATOM   6048 C CB  . SER B 1 327 ? 32.23600  22.66900  42.21400 1.000 36.38000 ? 327 SER B CB  1 
ATOM   6049 O OG  . SER B 1 327 ? 30.84500  22.43400  42.34900 1.000 36.38000 ? 327 SER B OG  1 
ATOM   6050 N N   . LYS B 1 328 ? 31.93800  19.86600  43.76000 1.000 35.57000 ? 328 LYS B N   1 
ATOM   6051 C CA  . LYS B 1 328 ? 31.85600  19.14100  45.02200 1.000 35.57000 ? 328 LYS B CA  1 
ATOM   6052 C C   . LYS B 1 328 ? 32.92700  18.06100  45.11000 1.000 35.57000 ? 328 LYS B C   1 
ATOM   6053 O O   . LYS B 1 328 ? 33.54500  17.87700  46.16500 1.000 35.57000 ? 328 LYS B O   1 
ATOM   6054 C CB  . LYS B 1 328 ? 30.46000  18.53900  45.17700 1.000 35.57000 ? 328 LYS B CB  1 
ATOM   6055 C CG  . LYS B 1 328 ? 29.99400  18.37600  46.61200 1.000 35.57000 ? 328 LYS B CG  1 
ATOM   6056 C CD  . LYS B 1 328 ? 28.50600  18.07000  46.65500 1.000 35.57000 ? 328 LYS B CD  1 
ATOM   6057 C CE  . LYS B 1 328 ? 27.71000  19.13500  45.91600 1.000 35.57000 ? 328 LYS B CE  1 
ATOM   6058 N NZ  . LYS B 1 328 ? 26.25900  18.80900  45.85300 1.000 35.57000 ? 328 LYS B NZ  1 
ATOM   6059 N N   . ILE B 1 329 ? 33.19100  17.36200  44.00300 1.000 36.21000 ? 329 ILE B N   1 
ATOM   6060 C CA  . ILE B 1 329 ? 34.19500  16.30400  44.03200 1.000 36.21000 ? 329 ILE B CA  1 
ATOM   6061 C C   . ILE B 1 329 ? 35.58600  16.88700  44.24300 1.000 36.21000 ? 329 ILE B C   1 
ATOM   6062 O O   . ILE B 1 329 ? 36.37700  16.36500  45.04100 1.000 36.21000 ? 329 ILE B O   1 
ATOM   6063 C CB  . ILE B 1 329 ? 34.11800  15.46100  42.74500 1.000 36.21000 ? 329 ILE B CB  1 
ATOM   6064 C CG1 . ILE B 1 329 ? 32.89200  14.54500  42.78100 1.000 36.21000 ? 329 ILE B CG1 1 
ATOM   6065 C CG2 . ILE B 1 329 ? 35.39200  14.64900  42.55300 1.000 36.21000 ? 329 ILE B CG2 1 
ATOM   6066 C CD1 . ILE B 1 329 ? 32.75900  13.65300  41.56300 1.000 36.21000 ? 329 ILE B CD1 1 
ATOM   6067 N N   . GLU B 1 330 ? 35.91400  17.97900  43.54400 1.000 36.69000 ? 330 GLU B N   1 
ATOM   6068 C CA  . GLU B 1 330 ? 37.23300  18.56800  43.76000 1.000 36.69000 ? 330 GLU B CA  1 
ATOM   6069 C C   . GLU B 1 330 ? 37.36900  19.15700  45.16100 1.000 36.69000 ? 330 GLU B C   1 
ATOM   6070 O O   . GLU B 1 330 ? 38.46000  19.10700  45.74500 1.000 36.69000 ? 330 GLU B O   1 
ATOM   6071 C CB  . GLU B 1 330 ? 37.54600  19.61400  42.68700 1.000 36.69000 ? 330 GLU B CB  1 
ATOM   6072 C CG  . GLU B 1 330 ? 36.53900  20.73100  42.53700 1.000 36.69000 ? 330 GLU B CG  1 
ATOM   6073 C CD  . GLU B 1 330 ? 36.74100  21.50600  41.24800 1.000 36.69000 ? 330 GLU B CD  1 
ATOM   6074 O OE1 . GLU B 1 330 ? 37.80100  21.32700  40.61200 1.000 36.69000 ? 330 GLU B OE1 1 
ATOM   6075 O OE2 . GLU B 1 330 ? 35.84200  22.28400  40.86600 1.000 36.69000 ? 330 GLU B OE2 1 
ATOM   6076 N N   . ILE B 1 331 ? 36.28300  19.68700  45.73500 1.000 35.09000 ? 331 ILE B N   1 
ATOM   6077 C CA  . ILE B 1 331 ? 36.37700  20.20600  47.09600 1.000 35.09000 ? 331 ILE B CA  1 
ATOM   6078 C C   . ILE B 1 331 ? 36.58000  19.06800  48.09600 1.000 35.09000 ? 331 ILE B C   1 
ATOM   6079 O O   . ILE B 1 331 ? 37.34800  19.19900  49.06000 1.000 35.09000 ? 331 ILE B O   1 
ATOM   6080 C CB  . ILE B 1 331 ? 35.14400  21.07500  47.42100 1.000 35.09000 ? 331 ILE B CB  1 
ATOM   6081 C CG1 . ILE B 1 331 ? 35.53200  22.23600  48.33200 1.000 35.09000 ? 331 ILE B CG1 1 
ATOM   6082 C CG2 . ILE B 1 331 ? 34.02300  20.27700  48.07100 1.000 35.09000 ? 331 ILE B CG2 1 
ATOM   6083 C CD1 . ILE B 1 331 ? 34.38500  23.17200  48.61700 1.000 35.09000 ? 331 ILE B CD1 1 
ATOM   6084 N N   . LYS B 1 332 ? 35.93600  17.91700  47.86300 1.000 34.24000 ? 332 LYS B N   1 
ATOM   6085 C CA  . LYS B 1 332 ? 36.16700  16.77700  48.74600 1.000 34.24000 ? 332 LYS B CA  1 
ATOM   6086 C C   . LYS B 1 332 ? 37.58900  16.25200  48.59900 1.000 34.24000 ? 332 LYS B C   1 
ATOM   6087 O O   . LYS B 1 332 ? 38.20400  15.82100  49.58200 1.000 34.24000 ? 332 LYS B O   1 
ATOM   6088 C CB  . LYS B 1 332 ? 35.15600  15.66200  48.47200 1.000 34.24000 ? 332 LYS B CB  1 
ATOM   6089 C CG  . LYS B 1 332 ? 33.69100  16.06800  48.59100 1.000 34.24000 ? 332 LYS B CG  1 
ATOM   6090 C CD  . LYS B 1 332 ? 33.43700  17.01400  49.75500 1.000 34.24000 ? 332 LYS B CD  1 
ATOM   6091 C CE  . LYS B 1 332 ? 32.03500  17.60500  49.67500 1.000 34.24000 ? 332 LYS B CE  1 
ATOM   6092 N NZ  . LYS B 1 332 ? 31.84800  18.75200  50.60800 1.000 34.24000 ? 332 LYS B NZ  1 
ATOM   6093 N N   . SER B 1 333 ? 38.13600  16.29400  47.38100 1.000 34.64000 ? 333 SER B N   1 
ATOM   6094 C CA  . SER B 1 333 ? 39.51800  15.86500  47.18900 1.000 34.64000 ? 333 SER B CA  1 
ATOM   6095 C C   . SER B 1 333 ? 40.48800  16.79800  47.90100 1.000 34.64000 ? 333 SER B C   1 
ATOM   6096 O O   . SER B 1 333 ? 41.47800  16.34400  48.49300 1.000 34.64000 ? 333 SER B O   1 
ATOM   6097 C CB  . SER B 1 333 ? 39.84000  15.79300  45.69700 1.000 34.64000 ? 333 SER B CB  1 
ATOM   6098 O OG  . SER B 1 333 ? 41.23200  15.62900  45.48500 1.000 34.64000 ? 333 SER B OG  1 
ATOM   6099 N N   . VAL B 1 334 ? 40.20700  18.10300  47.87700 1.000 34.60000 ? 334 VAL B N   1 
ATOM   6100 C CA  . VAL B 1 334 ? 41.05600  19.04800  48.59600 1.000 34.60000 ? 334 VAL B CA  1 
ATOM   6101 C C   . VAL B 1 334 ? 40.98200  18.79000  50.09400 1.000 34.60000 ? 334 VAL B C   1 
ATOM   6102 O O   . VAL B 1 334 ? 42.00100  18.82400  50.79800 1.000 34.60000 ? 334 VAL B O   1 
ATOM   6103 C CB  . VAL B 1 334 ? 40.65900  20.49500  48.24900 1.000 34.60000 ? 334 VAL B CB  1 
ATOM   6104 C CG1 . VAL B 1 334 ? 41.28200  21.47000  49.23700 1.000 34.60000 ? 334 VAL B CG1 1 
ATOM   6105 C CG2 . VAL B 1 334 ? 41.08000  20.83300  46.82800 1.000 34.60000 ? 334 VAL B CG2 1 
ATOM   6106 N N   . LEU B 1 335 ? 39.78300  18.49000  50.60200 1.000 32.76000 ? 335 LEU B N   1 
ATOM   6107 C CA  . LEU B 1 335 ? 39.66700  18.20000  52.02800 1.000 32.76000 ? 335 LEU B CA  1 
ATOM   6108 C C   . LEU B 1 335 ? 40.40500  16.91800  52.39800 1.000 32.76000 ? 335 LEU B C   1 
ATOM   6109 O O   . LEU B 1 335 ? 41.04200  16.84600  53.45500 1.000 32.76000 ? 335 LEU B O   1 
ATOM   6110 C CB  . LEU B 1 335 ? 38.19900  18.10100  52.43600 1.000 32.76000 ? 335 LEU B CB  1 
ATOM   6111 C CG  . LEU B 1 335 ? 37.97900  17.65700  53.88500 1.000 32.76000 ? 335 LEU B CG  1 
ATOM   6112 C CD1 . LEU B 1 335 ? 38.55400  18.67300  54.86400 1.000 32.76000 ? 335 LEU B CD1 1 
ATOM   6113 C CD2 . LEU B 1 335 ? 36.51100  17.41300  54.15700 1.000 32.76000 ? 335 LEU B CD2 1 
ATOM   6114 N N   . ALA B 1 336 ? 40.35000  15.90300  51.53300 1.000 33.54000 ? 336 ALA B N   1 
ATOM   6115 C CA  . ALA B 1 336 ? 41.04700  14.65700  51.83600 1.000 33.54000 ? 336 ALA B CA  1 
ATOM   6116 C C   . ALA B 1 336 ? 42.55600  14.85800  51.82900 1.000 33.54000 ? 336 ALA B C   1 
ATOM   6117 O O   . ALA B 1 336 ? 43.26600  14.31700  52.68800 1.000 33.54000 ? 336 ALA B O   1 
ATOM   6118 C CB  . ALA B 1 336 ? 40.64200  13.57100  50.84100 1.000 33.54000 ? 336 ALA B CB  1 
ATOM   6119 N N   . LYS B 1 337 ? 43.06200  15.65900  50.88700 1.000 36.17000 ? 337 LYS B N   1 
ATOM   6120 C CA  . LYS B 1 337 ? 44.49000  15.95900  50.88000 1.000 36.17000 ? 337 LYS B CA  1 
ATOM   6121 C C   . LYS B 1 337 ? 44.89100  16.74900  52.12100 1.000 36.17000 ? 337 LYS B C   1 
ATOM   6122 O O   . LYS B 1 337 ? 45.96600  16.52200  52.69000 1.000 36.17000 ? 337 LYS B O   1 
ATOM   6123 C CB  . LYS B 1 337 ? 44.85600  16.72800  49.61100 1.000 36.17000 ? 337 LYS B CB  1 
ATOM   6124 C CG  . LYS B 1 337 ? 45.70500  15.94700  48.62100 1.000 36.17000 ? 337 LYS B CG  1 
ATOM   6125 C CD  . LYS B 1 337 ? 45.74300  16.65500  47.27700 1.000 36.17000 ? 337 LYS B CD  1 
ATOM   6126 C CE  . LYS B 1 337 ? 46.88800  16.16700  46.40600 1.000 36.17000 ? 337 LYS B CE  1 
ATOM   6127 N NZ  . LYS B 1 337 ? 46.98300  16.96200  45.14800 1.000 36.17000 ? 337 LYS B NZ  1 
ATOM   6128 N N   . LEU B 1 338 ? 44.02500  17.66000  52.57700 1.000 34.93000 ? 338 LEU B N   1 
ATOM   6129 C CA  . LEU B 1 338 ? 44.34000  18.41900  53.78400 1.000 34.93000 ? 338 LEU B CA  1 
ATOM   6130 C C   . LEU B 1 338 ? 44.35600  17.52500  55.01800 1.000 34.93000 ? 338 LEU B C   1 
ATOM   6131 O O   . LEU B 1 338 ? 45.20700  17.69200  55.90100 1.000 34.93000 ? 338 LEU B O   1 
ATOM   6132 C CB  . LEU B 1 338 ? 43.34300  19.56400  53.96200 1.000 34.93000 ? 338 LEU B CB  1 
ATOM   6133 C CG  . LEU B 1 338 ? 43.77400  20.94500  53.45900 1.000 34.93000 ? 338 LEU B CG  1 
ATOM   6134 C CD1 . LEU B 1 338 ? 44.12400  20.91700  51.98000 1.000 34.93000 ? 338 LEU B CD1 1 
ATOM   6135 C CD2 . LEU B 1 338 ? 42.68600  21.97100  53.73500 1.000 34.93000 ? 338 LEU B CD2 1 
ATOM   6136 N N   . VAL B 1 339 ? 43.43200  16.56500  55.09700 1.000 36.63000 ? 339 VAL B N   1 
ATOM   6137 C CA  . VAL B 1 339 ? 43.42800  15.65200  56.23700 1.000 36.63000 ? 339 VAL B CA  1 
ATOM   6138 C C   . VAL B 1 339 ? 44.66500  14.76400  56.21300 1.000 36.63000 ? 339 VAL B C   1 
ATOM   6139 O O   . VAL B 1 339 ? 45.27500  14.49200  57.25700 1.000 36.63000 ? 339 VAL B O   1 
ATOM   6140 C CB  . VAL B 1 339 ? 42.13300  14.82000  56.26000 1.000 36.63000 ? 339 VAL B CB  1 
ATOM   6141 C CG1 . VAL B 1 339 ? 42.15600  13.83200  57.41800 1.000 36.63000 ? 339 VAL B CG1 1 
ATOM   6142 C CG2 . VAL B 1 339 ? 40.92400  15.72800  56.36600 1.000 36.63000 ? 339 VAL B CG2 1 
ATOM   6143 N N   . GLU B 1 340 ? 45.06800  14.31400  55.02000 1.000 38.11000 ? 340 GLU B N   1 
ATOM   6144 C CA  . GLU B 1 340 ? 46.28400  13.51600  54.91400 1.000 38.11000 ? 340 GLU B CA  1 
ATOM   6145 C C   . GLU B 1 340 ? 47.51800  14.32400  55.29500 1.000 38.11000 ? 340 GLU B C   1 
ATOM   6146 O O   . GLU B 1 340 ? 48.46900  13.77300  55.86100 1.000 38.11000 ? 340 GLU B O   1 
ATOM   6147 C CB  . GLU B 1 340 ? 46.42500  12.96600  53.49500 1.000 38.11000 ? 340 GLU B CB  1 
ATOM   6148 C CG  . GLU B 1 340 ? 47.51900  11.92500  53.33400 1.000 38.11000 ? 340 GLU B CG  1 
ATOM   6149 C CD  . GLU B 1 340 ? 47.70300  11.49300  51.89200 1.000 38.11000 ? 340 GLU B CD  1 
ATOM   6150 O OE1 . GLU B 1 340 ? 47.53400  12.34100  50.99100 1.000 38.11000 ? 340 GLU B OE1 1 
ATOM   6151 O OE2 . GLU B 1 340 ? 48.01300  10.30500  51.66000 1.000 38.11000 ? 340 GLU B OE2 1 
ATOM   6152 N N   . TYR B 1 341 ? 47.51900  15.62700  54.99700 1.000 37.91000 ? 341 TYR B N   1 
ATOM   6153 C CA  . TYR B 1 341 ? 48.63000  16.47400  55.41900 1.000 37.91000 ? 341 TYR B CA  1 
ATOM   6154 C C   . TYR B 1 341 ? 48.63700  16.66300  56.93100 1.000 37.91000 ? 341 TYR B C   1 
ATOM   6155 O O   . TYR B 1 341 ? 49.70400  16.67500  57.55600 1.000 37.91000 ? 341 TYR B O   1 
ATOM   6156 C CB  . TYR B 1 341 ? 48.55900  17.82900  54.71700 1.000 37.91000 ? 341 TYR B CB  1 
ATOM   6157 C CG  . TYR B 1 341 ? 48.69900  17.76500  53.21400 1.000 37.91000 ? 341 TYR B CG  1 
ATOM   6158 C CD1 . TYR B 1 341 ? 49.26200  16.65800  52.59300 1.000 37.91000 ? 341 TYR B CD1 1 
ATOM   6159 C CD2 . TYR B 1 341 ? 48.26900  18.81500  52.41400 1.000 37.91000 ? 341 TYR B CD2 1 
ATOM   6160 C CE1 . TYR B 1 341 ? 49.39100  16.59700  51.22000 1.000 37.91000 ? 341 TYR B CE1 1 
ATOM   6161 C CE2 . TYR B 1 341 ? 48.39500  18.76400  51.04000 1.000 37.91000 ? 341 TYR B CE2 1 
ATOM   6162 C CZ  . TYR B 1 341 ? 48.95600  17.65300  50.44800 1.000 37.91000 ? 341 TYR B CZ  1 
ATOM   6163 O OH  . TYR B 1 341 ? 49.08400  17.59500  49.08000 1.000 37.91000 ? 341 TYR B OH  1 
ATOM   6164 N N   . MET B 1 342 ? 47.45500  16.81900  57.53400 1.000 39.75000 ? 342 MET B N   1 
ATOM   6165 C CA  . MET B 1 342 ? 47.38600  16.97000  58.98400 1.000 39.75000 ? 342 MET B CA  1 
ATOM   6166 C C   . MET B 1 342 ? 47.81000  15.69700  59.70200 1.000 39.75000 ? 342 MET B C   1 
ATOM   6167 O O   . MET B 1 342 ? 48.36000  15.76400  60.80700 1.000 39.75000 ? 342 MET B O   1 
ATOM   6168 C CB  . MET B 1 342 ? 45.97400  17.36300  59.41300 1.000 39.75000 ? 342 MET B CB  1 
ATOM   6169 C CG  . MET B 1 342 ? 45.52400  18.72100  58.91900 1.000 39.75000 ? 342 MET B CG  1 
ATOM   6170 S SD  . MET B 1 342 ? 43.94700  19.20500  59.64000 1.000 39.75000 ? 342 MET B SD  1 
ATOM   6171 C CE  . MET B 1 342 ? 42.91200  17.82100  59.17000 1.000 39.75000 ? 342 MET B CE  1 
ATOM   6172 N N   . SER B 1 343 ? 47.56700  14.53500  59.09700 1.000 40.77000 ? 343 SER B N   1 
ATOM   6173 C CA  . SER B 1 343 ? 47.99100  13.27900  59.69800 1.000 40.77000 ? 343 SER B CA  1 
ATOM   6174 C C   . SER B 1 343 ? 49.44900  12.94300  59.41200 1.000 40.77000 ? 343 SER B C   1 
ATOM   6175 O O   . SER B 1 343 ? 49.96600  11.97500  59.98000 1.000 40.77000 ? 343 SER B O   1 
ATOM   6176 C CB  . SER B 1 343 ? 47.09100  12.13800  59.21700 1.000 40.77000 ? 343 SER B CB  1 
ATOM   6177 O OG  . SER B 1 343 ? 45.74400  12.35800  59.60300 1.000 40.77000 ? 343 SER B OG  1 
ATOM   6178 N N   . ALA B 1 344 ? 50.12200  13.71100  58.55800 1.000 42.36000 ? 344 ALA B N   1 
ATOM   6179 C CA  . ALA B 1 344 ? 51.49800  13.44300  58.15900 1.000 42.36000 ? 344 ALA B CA  1 
ATOM   6180 C C   . ALA B 1 344 ? 52.40300  14.63700  58.44400 1.000 42.36000 ? 344 ALA B C   1 
ATOM   6181 O O   . ALA B 1 344 ? 53.32800  14.93400  57.68400 1.000 42.36000 ? 344 ALA B O   1 
ATOM   6182 C CB  . ALA B 1 344 ? 51.57000  13.05500  56.68400 1.000 42.36000 ? 344 ALA B CB  1 
ATOM   6183 N N   . GLU B 1 345 ? 52.14800  15.33500  59.54800 1.000 42.43000 ? 345 GLU B N   1 
ATOM   6184 C CA  . GLU B 1 345 ? 52.96700  16.47000  59.94600 1.000 42.43000 ? 345 GLU B CA  1 
ATOM   6185 C C   . GLU B 1 345 ? 52.90000  16.60900  61.45900 1.000 42.43000 ? 345 GLU B C   1 
ATOM   6186 O O   . GLU B 1 345 ? 51.91800  16.20300  62.08700 1.000 42.43000 ? 345 GLU B O   1 
ATOM   6187 C CB  . GLU B 1 345 ? 52.50800  17.76400  59.26200 1.000 42.43000 ? 345 GLU B CB  1 
ATOM   6188 C CG  . GLU B 1 345 ? 53.57000  18.85400  59.18300 1.000 42.43000 ? 345 GLU B CG  1 
ATOM   6189 C CD  . GLU B 1 345 ? 54.52800  18.66700  58.01800 1.000 42.43000 ? 345 GLU B CD  1 
ATOM   6190 O OE1 . GLU B 1 345 ? 54.48900  17.59900  57.37000 1.000 42.43000 ? 345 GLU B OE1 1 
ATOM   6191 O OE2 . GLU B 1 345 ? 55.31900  19.59500  57.74500 1.000 42.43000 ? 345 GLU B OE2 1 
ATOM   6192 N N   . LYS B 1 346 ? 53.95700  17.18100  62.04100 1.000 44.23000 ? 346 LYS B N   1 
ATOM   6193 C CA  . LYS B 1 346 ? 54.03200  17.28300  63.49700 1.000 44.23000 ? 346 LYS B CA  1 
ATOM   6194 C C   . LYS B 1 346 ? 52.93300  18.18700  64.04200 1.000 44.23000 ? 346 LYS B C   1 
ATOM   6195 O O   . LYS B 1 346 ? 52.25800  17.84600  65.02000 1.000 44.23000 ? 346 LYS B O   1 
ATOM   6196 C CB  . LYS B 1 346 ? 55.41600  17.78800  63.91600 1.000 44.23000 ? 346 LYS B CB  1 
ATOM   6197 C CG  . LYS B 1 346 ? 55.92600  18.98800  63.12700 1.000 44.23000 ? 346 LYS B CG  1 
ATOM   6198 C CD  . LYS B 1 346 ? 55.79100  20.28300  63.91400 1.000 44.23000 ? 346 LYS B CD  1 
ATOM   6199 C CE  . LYS B 1 346 ? 56.33700  21.46200  63.12500 1.000 44.23000 ? 346 LYS B CE  1 
ATOM   6200 N NZ  . LYS B 1 346 ? 56.19300  22.74700  63.86400 1.000 44.23000 ? 346 LYS B NZ  1 
ATOM   6201 N N   . SER B 1 347 ? 52.72100  19.33300  63.40600 1.000 43.94000 ? 347 SER B N   1 
ATOM   6202 C CA  . SER B 1 347 ? 51.61300  20.21800  63.72700 1.000 43.94000 ? 347 SER B CA  1 
ATOM   6203 C C   . SER B 1 347 ? 50.71400  20.30700  62.50600 1.000 43.94000 ? 347 SER B C   1 
ATOM   6204 O O   . SER B 1 347 ? 51.19500  20.54900  61.39400 1.000 43.94000 ? 347 SER B O   1 
ATOM   6205 C CB  . SER B 1 347 ? 52.10800  21.60700  64.13900 1.000 43.94000 ? 347 SER B CB  1 
ATOM   6206 O OG  . SER B 1 347 ? 52.85100  22.21500  63.09800 1.000 43.94000 ? 347 SER B OG  1 
ATOM   6207 N N   . PHE B 1 348 ? 49.41200  20.10500  62.71400 1.000 41.13000 ? 348 PHE B N   1 
ATOM   6208 C CA  . PHE B 1 348 ? 48.48500  20.10400  61.59100 1.000 41.13000 ? 348 PHE B CA  1 
ATOM   6209 C C   . PHE B 1 348 ? 48.42300  21.45700  60.89800 1.000 41.13000 ? 348 PHE B C   1 
ATOM   6210 O O   . PHE B 1 348 ? 48.05100  21.52100  59.72200 1.000 41.13000 ? 348 PHE B O   1 
ATOM   6211 C CB  . PHE B 1 348 ? 47.09000  19.68100  62.05900 1.000 41.13000 ? 348 PHE B CB  1 
ATOM   6212 C CG  . PHE B 1 348 ? 46.44500  20.65000  63.00800 1.000 41.13000 ? 348 PHE B CG  1 
ATOM   6213 C CD1 . PHE B 1 348 ? 46.71300  20.59700  64.36600 1.000 41.13000 ? 348 PHE B CD1 1 
ATOM   6214 C CD2 . PHE B 1 348 ? 45.55700  21.60600  62.54400 1.000 41.13000 ? 348 PHE B CD2 1 
ATOM   6215 C CE1 . PHE B 1 348 ? 46.11600  21.48700  65.24100 1.000 41.13000 ? 348 PHE B CE1 1 
ATOM   6216 C CE2 . PHE B 1 348 ? 44.95700  22.49600  63.41300 1.000 41.13000 ? 348 PHE B CE2 1 
ATOM   6217 C CZ  . PHE B 1 348 ? 45.23600  22.43600  64.76300 1.000 41.13000 ? 348 PHE B CZ  1 
ATOM   6218 N N   . ILE B 1 349 ? 48.76100  22.54000  61.60400 1.000 40.92000 ? 349 ILE B N   1 
ATOM   6219 C CA  . ILE B 1 349 ? 48.75700  23.86200  60.98100 1.000 40.92000 ? 349 ILE B CA  1 
ATOM   6220 C C   . ILE B 1 349 ? 49.78500  23.92500  59.85900 1.000 40.92000 ? 349 ILE B C   1 
ATOM   6221 O O   . ILE B 1 349 ? 49.56000  24.56000  58.82000 1.000 40.92000 ? 349 ILE B O   1 
ATOM   6222 C CB  . ILE B 1 349 ? 49.01700  24.94400  62.04400 1.000 40.92000 ? 349 ILE B CB  1 
ATOM   6223 C CG1 . ILE B 1 349 ? 48.04800  24.77500  63.21400 1.000 40.92000 ? 349 ILE B CG1 1 
ATOM   6224 C CG2 . ILE B 1 349 ? 48.88600  26.33000  61.44100 1.000 40.92000 ? 349 ILE B CG2 1 
ATOM   6225 C CD1 . ILE B 1 349 ? 48.23600  25.79600  64.31100 1.000 40.92000 ? 349 ILE B CD1 1 
ATOM   6226 N N   . ASP B 1 350 ? 50.92700  23.26000  60.04600 1.000 41.47000 ? 350 ASP B N   1 
ATOM   6227 C CA  . ASP B 1 350 ? 51.95200  23.23400  59.00800 1.000 41.47000 ? 350 ASP B CA  1 
ATOM   6228 C C   . ASP B 1 350 ? 51.53700  22.38400  57.81100 1.000 41.47000 ? 350 ASP B C   1 
ATOM   6229 O O   . ASP B 1 350 ? 51.98200  22.64400  56.68700 1.000 41.47000 ? 350 ASP B O   1 
ATOM   6230 C CB  . ASP B 1 350 ? 53.26900  22.73900  59.60000 1.000 41.47000 ? 350 ASP B CB  1 
ATOM   6231 C CG  . ASP B 1 350 ? 53.85500  23.71500  60.60800 1.000 41.47000 ? 350 ASP B CG  1 
ATOM   6232 O OD1 . ASP B 1 350 ? 53.16200  24.68900  60.97100 1.000 41.47000 ? 350 ASP B OD1 1 
ATOM   6233 O OD2 . ASP B 1 350 ? 55.01100  23.51300  61.03200 1.000 41.47000 ? 350 ASP B OD2 1 
ATOM   6234 N N   . GLY B 1 351 ? 50.69700  21.36600  58.02100 1.000 39.35000 ? 351 GLY B N   1 
ATOM   6235 C CA  . GLY B 1 351 ? 50.15900  20.63000  56.89200 1.000 39.35000 ? 351 GLY B CA  1 
ATOM   6236 C C   . GLY B 1 351 ? 49.00300  21.32000  56.20500 1.000 39.35000 ? 351 GLY B C   1 
ATOM   6237 O O   . GLY B 1 351 ? 48.74000  21.05000  55.02900 1.000 39.35000 ? 351 GLY B O   1 
ATOM   6238 N N   . LEU B 1 352 ? 48.31500  22.21400  56.91400 1.000 38.31000 ? 352 LEU B N   1 
ATOM   6239 C CA  . LEU B 1 352 ? 47.22000  22.96000  56.30900 1.000 38.31000 ? 352 LEU B CA  1 
ATOM   6240 C C   . LEU B 1 352 ? 47.72200  24.17700  55.54500 1.000 38.31000 ? 352 LEU B C   1 
ATOM   6241 O O   . LEU B 1 352 ? 47.14500  24.54700  54.51900 1.000 38.31000 ? 352 LEU B O   1 
ATOM   6242 C CB  . LEU B 1 352 ? 46.22100  23.39000  57.38400 1.000 38.31000 ? 352 LEU B CB  1 
ATOM   6243 C CG  . LEU B 1 352 ? 45.38900  22.28500  58.03100 1.000 38.31000 ? 352 LEU B CG  1 
ATOM   6244 C CD1 . LEU B 1 352 ? 44.57800  22.85100  59.18200 1.000 38.31000 ? 352 LEU B CD1 1 
ATOM   6245 C CD2 . LEU B 1 352 ? 44.48200  21.62800  57.00400 1.000 38.31000 ? 352 LEU B CD2 1 
ATOM   6246 N N   . ILE B 1 353 ? 48.79100  24.81000  56.02300 1.000 39.93000 ? 353 ILE B N   1 
ATOM   6247 C CA  . ILE B 1 353 ? 49.24700  26.06600  55.43900 1.000 39.93000 ? 353 ILE B CA  1 
ATOM   6248 C C   . ILE B 1 353 ? 50.36800  25.81800  54.43800 1.000 39.93000 ? 353 ILE B C   1 
ATOM   6249 O O   . ILE B 1 353 ? 50.23300  26.13500  53.25100 1.000 39.93000 ? 353 ILE B O   1 
ATOM   6250 C CB  . ILE B 1 353 ? 49.69900  27.05000  56.53500 1.000 39.93000 ? 353 ILE B CB  1 
ATOM   6251 C CG1 . ILE B 1 353 ? 48.52900  27.39800  57.45900 1.000 39.93000 ? 353 ILE B CG1 1 
ATOM   6252 C CG2 . ILE B 1 353 ? 50.28500  28.30800  55.91300 1.000 39.93000 ? 353 ILE B CG2 1 
ATOM   6253 C CD1 . ILE B 1 353 ? 48.86000  28.45100  58.49800 1.000 39.93000 ? 353 ILE B CD1 1 
ATOM   6254 N N   . ASN B 1 354 ? 51.48400  25.25700  54.91300 1.000 41.29000 ? 354 ASN B N   1 
ATOM   6255 C CA  . ASN B 1 354 ? 52.68500  25.17200  54.08500 1.000 41.29000 ? 354 ASN B CA  1 
ATOM   6256 C C   . ASN B 1 354 ? 52.48700  24.26300  52.87500 1.000 41.29000 ? 354 ASN B C   1 
ATOM   6257 O O   . ASN B 1 354 ? 53.01200  24.54500  51.79100 1.000 41.29000 ? 354 ASN B O   1 
ATOM   6258 C CB  . ASN B 1 354 ? 53.86300  24.68300  54.92900 1.000 41.29000 ? 354 ASN B CB  1 
ATOM   6259 C CG  . ASN B 1 354 ? 54.07800  25.52400  56.17500 1.000 41.29000 ? 354 ASN B CG  1 
ATOM   6260 O OD1 . ASN B 1 354 ? 53.70400  26.69600  56.22200 1.000 41.29000 ? 354 ASN B OD1 1 
ATOM   6261 N ND2 . ASN B 1 354 ? 54.68900  24.92600  57.19200 1.000 41.29000 ? 354 ASN B ND2 1 
ATOM   6262 N N   . LYS B 1 355 ? 51.73500  23.17700  53.03300 1.000 38.53000 ? 355 LYS B N   1 
ATOM   6263 C CA  . LYS B 1 355 ? 51.56200  22.21700  51.95400 1.000 38.53000 ? 355 LYS B CA  1 
ATOM   6264 C C   . LYS B 1 355 ? 50.57100  22.73800  50.91600 1.000 38.53000 ? 355 LYS B C   1 
ATOM   6265 O O   . LYS B 1 355 ? 49.70800  23.57000  51.20400 1.000 38.53000 ? 355 LYS B O   1 
ATOM   6266 C CB  . LYS B 1 355 ? 51.08800  20.86900  52.50000 1.000 38.53000 ? 355 LYS B CB  1 
ATOM   6267 C CG  . LYS B 1 355 ? 51.93100  20.31600  53.64000 1.000 38.53000 ? 355 LYS B CG  1 
ATOM   6268 C CD  . LYS B 1 355 ? 53.30100  19.85000  53.17100 1.000 38.53000 ? 355 LYS B CD  1 
ATOM   6269 C CE  . LYS B 1 355 ? 54.07600  19.21400  54.31700 1.000 38.53000 ? 355 LYS B CE  1 
ATOM   6270 N NZ  . LYS B 1 355 ? 55.40400  18.69500  53.88700 1.000 38.53000 ? 355 LYS B NZ  1 
ATOM   6271 N N   . GLN B 1 356 ? 50.71400  22.24000  49.68900 1.000 39.77000 ? 356 GLN B N   1 
ATOM   6272 C CA  . GLN B 1 356 ? 49.79600  22.54200  48.60300 1.000 39.77000 ? 356 GLN B CA  1 
ATOM   6273 C C   . GLN B 1 356 ? 49.14300  21.25700  48.11100 1.000 39.77000 ? 356 GLN B C   1 
ATOM   6274 O O   . GLN B 1 356 ? 49.85200  20.28200  47.82700 1.000 39.77000 ? 356 GLN B O   1 
ATOM   6275 C CB  . GLN B 1 356 ? 50.51600  23.24300  47.43900 1.000 39.77000 ? 356 GLN B CB  1 
ATOM   6276 C CG  . GLN B 1 356 ? 51.37400  24.43000  47.85200 1.000 39.77000 ? 356 GLN B CG  1 
ATOM   6277 C CD  . GLN B 1 356 ? 50.57400  25.54000  48.51100 1.000 39.77000 ? 356 GLN B CD  1 
ATOM   6278 O OE1 . GLN B 1 356 ? 49.37400  25.68400  48.27600 1.000 39.77000 ? 356 GLN B OE1 1 
ATOM   6279 N NE2 . GLN B 1 356 ? 51.24100  26.33300  49.34300 1.000 39.77000 ? 356 GLN B NE2 1 
ATOM   6280 N N   . PRO B 1 357 ? 47.80500  21.20600  47.98700 1.000 37.32000 ? 357 PRO B N   1 
ATOM   6281 C CA  . PRO B 1 357 ? 46.81000  22.25500  48.27400 1.000 37.32000 ? 357 PRO B CA  1 
ATOM   6282 C C   . PRO B 1 357 ? 46.77300  22.66900  49.74000 1.000 37.32000 ? 357 PRO B C   1 
ATOM   6283 O O   . PRO B 1 357 ? 46.96800  21.84300  50.63100 1.000 37.32000 ? 357 PRO B O   1 
ATOM   6284 C CB  . PRO B 1 357 ? 45.48900  21.60700  47.84000 1.000 37.32000 ? 357 PRO B CB  1 
ATOM   6285 C CG  . PRO B 1 357 ? 45.71800  20.14300  48.04200 1.000 37.32000 ? 357 PRO B CG  1 
ATOM   6286 C CD  . PRO B 1 357 ? 47.15100  19.93200  47.63300 1.000 37.32000 ? 357 PRO B CD  1 
ATOM   6287 N N   . ASN B 1 358 ? 46.52800  23.94000  50.02600 1.000 36.08000 ? 358 ASN B N   1 
ATOM   6288 C CA  . ASN B 1 358 ? 46.50600  24.42400  51.39500 1.000 36.08000 ? 358 ASN B CA  1 
ATOM   6289 C C   . ASN B 1 358 ? 45.06800  24.66400  51.84300 1.000 36.08000 ? 358 ASN B C   1 
ATOM   6290 O O   . ASN B 1 358 ? 44.10800  24.26400  51.17900 1.000 36.08000 ? 358 ASN B O   1 
ATOM   6291 C CB  . ASN B 1 358 ? 47.37100  25.68400  51.53300 1.000 36.08000 ? 358 ASN B CB  1 
ATOM   6292 C CG  . ASN B 1 358 ? 46.91000  26.82500  50.64100 1.000 36.08000 ? 358 ASN B CG  1 
ATOM   6293 O OD1 . ASN B 1 358 ? 45.84900  26.76600  50.02300 1.000 36.08000 ? 358 ASN B OD1 1 
ATOM   6294 N ND2 . ASN B 1 358 ? 47.71500  27.88000  50.57800 1.000 36.08000 ? 358 ASN B ND2 1 
ATOM   6295 N N   . ILE B 1 359 ? 44.92500  25.32600  52.99200 1.000 33.95000 ? 359 ILE B N   1 
ATOM   6296 C CA  . ILE B 1 359 ? 43.60900  25.61400  53.54100 1.000 33.95000 ? 359 ILE B CA  1 
ATOM   6297 C C   . ILE B 1 359 ? 42.82100  26.58300  52.66300 1.000 33.95000 ? 359 ILE B C   1 
ATOM   6298 O O   . ILE B 1 359 ? 41.58500  26.58300  52.70600 1.000 33.95000 ? 359 ILE B O   1 
ATOM   6299 C CB  . ILE B 1 359 ? 43.77400  26.13800  54.98100 1.000 33.95000 ? 359 ILE B CB  1 
ATOM   6300 C CG1 . ILE B 1 359 ? 42.48900  25.95700  55.77900 1.000 33.95000 ? 359 ILE B CG1 1 
ATOM   6301 C CG2 . ILE B 1 359 ? 44.20300  27.59700  54.98500 1.000 33.95000 ? 359 ILE B CG2 1 
ATOM   6302 C CD1 . ILE B 1 359 ? 42.65300  26.27200  57.23600 1.000 33.95000 ? 359 ILE B CD1 1 
ATOM   6303 N N   . LEU B 1 360 ? 43.50400  27.41300  51.86500 1.000 34.35000 ? 360 LEU B N   1 
ATOM   6304 C CA  . LEU B 1 360 ? 42.80700  28.31100  50.94800 1.000 34.35000 ? 360 LEU B CA  1 
ATOM   6305 C C   . LEU B 1 360 ? 42.05400  27.55200  49.86400 1.000 34.35000 ? 360 LEU B C   1 
ATOM   6306 O O   . LEU B 1 360 ? 41.01200  28.02100  49.39400 1.000 34.35000 ? 360 LEU B O   1 
ATOM   6307 C CB  . LEU B 1 360 ? 43.79800  29.27900  50.30300 1.000 34.35000 ? 360 LEU B CB  1 
ATOM   6308 C CG  . LEU B 1 360 ? 44.49000  30.26100  51.24300 1.000 34.35000 ? 360 LEU B CG  1 
ATOM   6309 C CD1 . LEU B 1 360 ? 45.39300  31.20100  50.46600 1.000 34.35000 ? 360 LEU B CD1 1 
ATOM   6310 C CD2 . LEU B 1 360 ? 43.44700  31.03300  52.01600 1.000 34.35000 ? 360 LEU B CD2 1 
ATOM   6311 N N   . ASN B 1 361 ? 42.55900  26.38500  49.45800 1.000 34.92000 ? 361 ASN B N   1 
ATOM   6312 C CA  . ASN B 1 361 ? 41.90600  25.61000  48.41000 1.000 34.92000 ? 361 ASN B CA  1 
ATOM   6313 C C   . ASN B 1 361 ? 40.55300  25.07100  48.84700 1.000 34.92000 ? 361 ASN B C   1 
ATOM   6314 O O   . ASN B 1 361 ? 39.73200  24.72100  47.99300 1.000 34.92000 ? 361 ASN B O   1 
ATOM   6315 C CB  . ASN B 1 361 ? 42.80300  24.45100  47.97200 1.000 34.92000 ? 361 ASN B CB  1 
ATOM   6316 C CG  . ASN B 1 361 ? 44.08400  24.91700  47.31200 1.000 34.92000 ? 361 ASN B CG  1 
ATOM   6317 O OD1 . ASN B 1 361 ? 45.10300  25.10400  47.97400 1.000 34.92000 ? 361 ASN B OD1 1 
ATOM   6318 N ND2 . ASN B 1 361 ? 44.03900  25.10300  45.99800 1.000 34.92000 ? 361 ASN B ND2 1 
ATOM   6319 N N   . LEU B 1 362 ? 40.30800  24.98600  50.15400 1.000 31.59000 ? 362 LEU B N   1 
ATOM   6320 C CA  . LEU B 1 362 ? 39.10800  24.31600  50.63800 1.000 31.59000 ? 362 LEU B CA  1 
ATOM   6321 C C   . LEU B 1 362 ? 37.85300  25.14200  50.37100 1.000 31.59000 ? 362 LEU B C   1 
ATOM   6322 O O   . LEU B 1 362 ? 36.83500  24.60700  49.92200 1.000 31.59000 ? 362 LEU B O   1 
ATOM   6323 C CB  . LEU B 1 362 ? 39.25400  24.01300  52.12700 1.000 31.59000 ? 362 LEU B CB  1 
ATOM   6324 C CG  . LEU B 1 362 ? 38.40700  22.85700  52.64800 1.000 31.59000 ? 362 LEU B CG  1 
ATOM   6325 C CD1 . LEU B 1 362 ? 38.42700  21.70300  51.66200 1.000 31.59000 ? 362 LEU B CD1 1 
ATOM   6326 C CD2 . LEU B 1 362 ? 38.93900  22.41100  53.98600 1.000 31.59000 ? 362 LEU B CD2 1 
ATOM   6327 N N   . VAL B 1 363 ? 37.89900  26.44700  50.64200 1.000 30.11000 ? 363 VAL B N   1 
ATOM   6328 C CA  . VAL B 1 363 ? 36.72400  27.29500  50.49700 1.000 30.11000 ? 363 VAL B CA  1 
ATOM   6329 C C   . VAL B 1 363 ? 36.91400  28.37300  49.43400 1.000 30.11000 ? 363 VAL B C   1 
ATOM   6330 O O   . VAL B 1 363 ? 36.09200  29.28600  49.33400 1.000 30.11000 ? 363 VAL B O   1 
ATOM   6331 C CB  . VAL B 1 363 ? 36.31700  27.92300  51.84500 1.000 30.11000 ? 363 VAL B CB  1 
ATOM   6332 C CG1 . VAL B 1 363 ? 36.33500  26.87700  52.95100 1.000 30.11000 ? 363 VAL B CG1 1 
ATOM   6333 C CG2 . VAL B 1 363 ? 37.22500  29.08500  52.18800 1.000 30.11000 ? 363 VAL B CG2 1 
ATOM   6334 N N   . ASN B 1 364 ? 37.97500  28.27800  48.62800 1.000 31.31000 ? 364 ASN B N   1 
ATOM   6335 C CA  . ASN B 1 364 ? 38.28200  29.26800  47.59100 1.000 31.31000 ? 364 ASN B CA  1 
ATOM   6336 C C   . ASN B 1 364 ? 38.47000  30.66600  48.18200 1.000 31.31000 ? 364 ASN B C   1 
ATOM   6337 O O   . ASN B 1 364 ? 37.96100  31.65600  47.65400 1.000 31.31000 ? 364 ASN B O   1 
ATOM   6338 C CB  . ASN B 1 364 ? 37.20900  29.28700  46.49900 1.000 31.31000 ? 364 ASN B CB  1 
ATOM   6339 C CG  . ASN B 1 364 ? 37.01500  27.93300  45.84800 1.000 31.31000 ? 364 ASN B CG  1 
ATOM   6340 O OD1 . ASN B 1 364 ? 37.32200  26.89800  46.43800 1.000 31.31000 ? 364 ASN B OD1 1 
ATOM   6341 N ND2 . ASN B 1 364 ? 36.49800  27.93400  44.62500 1.000 31.31000 ? 364 ASN B ND2 1 
ATOM   6342 N N   . ALA B 1 365 ? 39.18600  30.74400  49.30000 1.000 32.90000 ? 365 ALA B N   1 
ATOM   6343 C CA  . ALA B 1 365 ? 39.56500  32.00900  49.91200 1.000 32.90000 ? 365 ALA B CA  1 
ATOM   6344 C C   . ALA B 1 365 ? 40.94900  32.44500  49.44000 1.000 32.90000 ? 365 ALA B C   1 
ATOM   6345 O O   . ALA B 1 365 ? 41.75300  31.64100  48.96100 1.000 32.90000 ? 365 ALA B O   1 
ATOM   6346 C CB  . ALA B 1 365 ? 39.54500  31.90300  51.43800 1.000 32.90000 ? 365 ALA B CB  1 
ATOM   6347 N N   . GLN B 1 366 ? 41.21600  33.74200  49.57100 1.000 35.75000 ? 366 GLN B N   1 
ATOM   6348 C CA  . GLN B 1 366 ? 42.52000  34.30200  49.24700 1.000 35.75000 ? 366 GLN B CA  1 
ATOM   6349 C C   . GLN B 1 366 ? 43.34500  34.63400  50.48200 1.000 35.75000 ? 366 GLN B C   1 
ATOM   6350 O O   . GLN B 1 366 ? 44.50500  35.03700  50.34700 1.000 35.75000 ? 366 GLN B O   1 
ATOM   6351 C CB  . GLN B 1 366 ? 42.35700  35.55000  48.37800 1.000 35.75000 ? 366 GLN B CB  1 
ATOM   6352 C CG  . GLN B 1 366 ? 41.03100  35.61900  47.63800 1.000 35.75000 ? 366 GLN B CG  1 
ATOM   6353 C CD  . GLN B 1 366 ? 40.82300  34.49600  46.63600 1.000 35.75000 ? 366 GLN B CD  1 
ATOM   6354 O OE1 . GLN B 1 366 ? 41.77500  33.86600  46.17900 1.000 35.75000 ? 366 GLN B OE1 1 
ATOM   6355 N NE2 . GLN B 1 366 ? 39.56500  34.24200  46.28900 1.000 35.75000 ? 366 GLN B NE2 1 
ATOM   6356 N N   . GLY B 1 367 ? 42.77800  34.47600  51.67500 1.000 36.84000 ? 367 GLY B N   1 
ATOM   6357 C CA  . GLY B 1 367 ? 43.53800  34.67000  52.89500 1.000 36.84000 ? 367 GLY B CA  1 
ATOM   6358 C C   . GLY B 1 367 ? 43.05600  33.71800  53.96600 1.000 36.84000 ? 367 GLY B C   1 
ATOM   6359 O O   . GLY B 1 367 ? 41.92300  33.23600  53.93000 1.000 36.84000 ? 367 GLY B O   1 
ATOM   6360 N N   . ALA B 1 368 ? 43.93100  33.45700  54.93200 1.000 39.79000 ? 368 ALA B N   1 
ATOM   6361 C CA  . ALA B 1 368 ? 43.58400  32.55200  56.01400 1.000 39.79000 ? 368 ALA B CA  1 
ATOM   6362 C C   . ALA B 1 368 ? 44.38600  32.90400  57.25600 1.000 39.79000 ? 368 ALA B C   1 
ATOM   6363 O O   . ALA B 1 368 ? 45.50000  33.42800  57.17100 1.000 39.79000 ? 368 ALA B O   1 
ATOM   6364 C CB  . ALA B 1 368 ? 43.82900  31.09200  55.62400 1.000 39.79000 ? 368 ALA B CB  1 
ATOM   6365 N N   . ALA B 1 369 ? 43.80500  32.59200  58.41000 1.000 45.44000 ? 369 ALA B N   1 
ATOM   6366 C CA  . ALA B 1 369 ? 44.44400  32.85200  59.69700 1.000 45.44000 ? 369 ALA B CA  1 
ATOM   6367 C C   . ALA B 1 369 ? 43.97100  31.79200  60.68100 1.000 45.44000 ? 369 ALA B C   1 
ATOM   6368 O O   . ALA B 1 369 ? 42.78900  31.75600  61.03500 1.000 45.44000 ? 369 ALA B O   1 
ATOM   6369 C CB  . ALA B 1 369 ? 44.11800  34.25500  60.20000 1.000 45.44000 ? 369 ALA B CB  1 
ATOM   6370 N N   . ILE B 1 370 ? 44.88400  30.92900  61.11100 1.000 47.47000 ? 370 ILE B N   1 
ATOM   6371 C CA  . ILE B 1 370 ? 44.59600  29.91600  62.12000 1.000 47.47000 ? 370 ILE B CA  1 
ATOM   6372 C C   . ILE B 1 370 ? 45.04100  30.46900  63.46700 1.000 47.47000 ? 370 ILE B C   1 
ATOM   6373 O O   . ILE B 1 370 ? 46.23800  30.65700  63.70400 1.000 47.47000 ? 370 ILE B O   1 
ATOM   6374 C CB  . ILE B 1 370 ? 45.28800  28.58300  61.80500 1.000 47.47000 ? 370 ILE B CB  1 
ATOM   6375 C CG1 . ILE B 1 370 ? 44.80100  28.02900  60.46500 1.000 47.47000 ? 370 ILE B CG1 1 
ATOM   6376 C CG2 . ILE B 1 370 ? 45.03600  27.57700  62.91700 1.000 47.47000 ? 370 ILE B CG2 1 
ATOM   6377 C CD1 . ILE B 1 370 ? 45.39000  26.67700  60.11500 1.000 47.47000 ? 370 ILE B CD1 1 
ATOM   6378 N N   . CYS B 1 371 ? 44.08200  30.74900  64.34200 1.000 51.84000 ? 371 CYS B N   1 
ATOM   6379 C CA  . CYS B 1 371 ? 44.37200  31.24800  65.68000 1.000 51.84000 ? 371 CYS B CA  1 
ATOM   6380 C C   . CYS B 1 371 ? 44.39000  30.10400  66.68500 1.000 51.84000 ? 371 CYS B C   1 
ATOM   6381 O O   . CYS B 1 371 ? 43.36300  29.46900  66.91900 1.000 51.84000 ? 371 CYS B O   1 
ATOM   6382 C CB  . CYS B 1 371 ? 43.33800  32.29500  66.09900 1.000 51.84000 ? 371 CYS B CB  1 
ATOM   6383 S SG  . CYS B 1 371 ? 43.27600  32.62300  67.87800 1.000 51.84000 ? 371 CYS B SG  1 
ATOM   6384 N N   . GLU B 1 375 ? 46.89500  32.28700  69.69300 1.000 55.25000 ? 375 GLU B N   1 
ATOM   6385 C CA  . GLU B 1 375 ? 47.98800  32.55200  68.76400 1.000 55.25000 ? 375 GLU B CA  1 
ATOM   6386 C C   . GLU B 1 375 ? 47.47900  32.93600  67.38000 1.000 55.25000 ? 375 GLU B C   1 
ATOM   6387 O O   . GLU B 1 375 ? 46.31800  33.31000  67.22200 1.000 55.25000 ? 375 GLU B O   1 
ATOM   6388 C CB  . GLU B 1 375 ? 48.90500  31.33800  68.65400 1.000 55.25000 ? 375 GLU B CB  1 
ATOM   6389 C CG  . GLU B 1 375 ? 49.77900  31.11900  69.87000 1.000 55.25000 ? 375 GLU B CG  1 
ATOM   6390 C CD  . GLU B 1 375 ? 51.14100  30.57800  69.49900 1.000 55.25000 ? 375 GLU B CD  1 
ATOM   6391 O OE1 . GLU B 1 375 ? 51.51600  30.69000  68.31300 1.000 55.25000 ? 375 GLU B OE1 1 
ATOM   6392 O OE2 . GLU B 1 375 ? 51.83400  30.04100  70.38800 1.000 55.25000 ? 375 GLU B OE2 1 
ATOM   6393 N N   . LEU B 1 376 ? 48.35400  32.85000  66.37800 1.000 55.48000 ? 376 LEU B N   1 
ATOM   6394 C CA  . LEU B 1 376 ? 47.97400  33.23300  65.02600 1.000 55.48000 ? 376 LEU B CA  1 
ATOM   6395 C C   . LEU B 1 376 ? 48.96800  32.66300  64.02200 1.000 55.48000 ? 376 LEU B C   1 
ATOM   6396 O O   . LEU B 1 376 ? 50.16600  32.56400  64.29800 1.000 55.48000 ? 376 LEU B O   1 
ATOM   6397 C CB  . LEU B 1 376 ? 47.90000  34.75600  64.89400 1.000 55.48000 ? 376 LEU B CB  1 
ATOM   6398 C CG  . LEU B 1 376 ? 46.84800  35.32200  63.94200 1.000 55.48000 ? 376 LEU B CG  1 
ATOM   6399 C CD1 . LEU B 1 376 ? 45.49400  34.67800  64.18700 1.000 55.48000 ? 376 LEU B CD1 1 
ATOM   6400 C CD2 . LEU B 1 376 ? 46.76100  36.82300  64.12300 1.000 55.48000 ? 376 LEU B CD2 1 
ATOM   6401 N N   . TYR B 1 377 ? 48.44300  32.29200  62.85400 1.000 53.69000 ? 377 TYR B N   1 
ATOM   6402 C CA  . TYR B 1 377 ? 49.25600  31.84000  61.72500 1.000 53.69000 ? 377 TYR B CA  1 
ATOM   6403 C C   . TYR B 1 377 ? 48.56700  32.30900  60.45000 1.000 53.69000 ? 377 TYR B C   1 
ATOM   6404 O O   . TYR B 1 377 ? 47.47400  31.83300  60.13000 1.000 53.69000 ? 377 TYR B O   1 
ATOM   6405 C CB  . TYR B 1 377 ? 49.42500  30.32200  61.72800 1.000 53.69000 ? 377 TYR B CB  1 
ATOM   6406 C CG  . TYR B 1 377 ? 50.15100  29.77400  62.93600 1.000 53.69000 ? 377 TYR B CG  1 
ATOM   6407 C CD1 . TYR B 1 377 ? 51.53900  29.75800  62.98800 1.000 53.69000 ? 377 TYR B CD1 1 
ATOM   6408 C CD2 . TYR B 1 377 ? 49.44800  29.26400  64.02200 1.000 53.69000 ? 377 TYR B CD2 1 
ATOM   6409 C CE1 . TYR B 1 377 ? 52.20800  29.25400  64.09000 1.000 53.69000 ? 377 TYR B CE1 1 
ATOM   6410 C CE2 . TYR B 1 377 ? 50.10800  28.75900  65.12800 1.000 53.69000 ? 377 TYR B CE2 1 
ATOM   6411 C CZ  . TYR B 1 377 ? 51.48700  28.75600  65.15600 1.000 53.69000 ? 377 TYR B CZ  1 
ATOM   6412 O OH  . TYR B 1 377 ? 52.14600  28.25300  66.25500 1.000 53.69000 ? 377 TYR B OH  1 
ATOM   6413 N N   . LEU B 1 378 ? 49.19000  33.25300  59.75000 1.000 48.19000 ? 378 LEU B N   1 
ATOM   6414 C CA  . LEU B 1 378 ? 48.63900  33.86300  58.54800 1.000 48.19000 ? 378 LEU B CA  1 
ATOM   6415 C C   . LEU B 1 378 ? 49.04700  33.08900  57.29500 1.000 48.19000 ? 378 LEU B C   1 
ATOM   6416 O O   . LEU B 1 378 ? 50.06100  32.38700  57.26900 1.000 48.19000 ? 378 LEU B O   1 
ATOM   6417 C CB  . LEU B 1 378 ? 49.08900  35.32300  58.43200 1.000 48.19000 ? 378 LEU B CB  1 
ATOM   6418 C CG  . LEU B 1 378 ? 48.31900  36.40100  59.20800 1.000 48.19000 ? 378 LEU B CG  1 
ATOM   6419 C CD1 . LEU B 1 378 ? 48.24400  36.10500  60.69800 1.000 48.19000 ? 378 LEU B CD1 1 
ATOM   6420 C CD2 . LEU B 1 378 ? 48.94900  37.76700  58.97900 1.000 48.19000 ? 378 LEU B CD2 1 
ATOM   6421 N N   . LEU B 1 379 ? 48.23400  33.23000  56.24800 1.000 40.67000 ? 379 LEU B N   1 
ATOM   6422 C CA  . LEU B 1 379 ? 48.50900  32.59300  54.96200 1.000 40.67000 ? 379 LEU B CA  1 
ATOM   6423 C C   . LEU B 1 379 ? 47.83500  33.39000  53.85600 1.000 40.67000 ? 379 LEU B C   1 
ATOM   6424 O O   . LEU B 1 379 ? 46.60700  33.51200  53.84200 1.000 40.67000 ? 379 LEU B O   1 
ATOM   6425 C CB  . LEU B 1 379 ? 48.01500  31.14300  54.95300 1.000 40.67000 ? 379 LEU B CB  1 
ATOM   6426 C CG  . LEU B 1 379 ? 47.88600  30.46000  53.58800 1.000 40.67000 ? 379 LEU B CG  1 
ATOM   6427 C CD1 . LEU B 1 379 ? 49.22800  30.40500  52.87600 1.000 40.67000 ? 379 LEU B CD1 1 
ATOM   6428 C CD2 . LEU B 1 379 ? 47.29900  29.06400  53.73600 1.000 40.67000 ? 379 LEU B CD2 1 
ATOM   6429 N N   . GLY B 1 380 ? 48.62900  33.90800  52.91900 1.000 42.38000 ? 380 GLY B N   1 
ATOM   6430 C CA  . GLY B 1 380 ? 48.07700  34.64300  51.79500 1.000 42.38000 ? 380 GLY B CA  1 
ATOM   6431 C C   . GLY B 1 380 ? 47.69000  36.07100  52.14200 1.000 42.38000 ? 380 GLY B C   1 
ATOM   6432 O O   . GLY B 1 380 ? 48.09600  36.63800  53.16300 1.000 42.38000 ? 380 GLY B O   1 
ATOM   6433 N N   . ASN B 1 381 ? 46.88700  36.66300  51.25800 1.000 45.36000 ? 381 ASN B N   1 
ATOM   6434 C CA  . ASN B 1 381 ? 46.45300  38.04600  51.42200 1.000 45.36000 ? 381 ASN B CA  1 
ATOM   6435 C C   . ASN B 1 381 ? 45.46700  38.16100  52.57700 1.000 45.36000 ? 381 ASN B C   1 
ATOM   6436 O O   . ASN B 1 381 ? 44.26300  37.94700  52.40100 1.000 45.36000 ? 381 ASN B O   1 
ATOM   6437 C CB  . ASN B 1 381 ? 45.82300  38.56900  50.12900 1.000 45.36000 ? 381 ASN B CB  1 
ATOM   6438 C CG  . ASN B 1 381 ? 46.71700  38.36400  48.92300 1.000 45.36000 ? 381 ASN B CG  1 
ATOM   6439 O OD1 . ASN B 1 381 ? 47.93800  38.49100  49.01200 1.000 45.36000 ? 381 ASN B OD1 1 
ATOM   6440 N ND2 . ASN B 1 381 ? 46.11100  38.03800  47.78700 1.000 45.36000 ? 381 ASN B ND2 1 
ATOM   6441 N N   . THR B 1 382 ? 45.96800  38.51000  53.75400 1.000 44.80000 ? 382 THR B N   1 
ATOM   6442 C CA  . THR B 1 382 ? 45.19900  38.55900  54.98400 1.000 44.80000 ? 382 THR B CA  1 
ATOM   6443 C C   . THR B 1 382 ? 45.32800  39.93200  55.62500 1.000 44.80000 ? 382 THR B C   1 
ATOM   6444 O O   . THR B 1 382 ? 46.31100  40.64700  55.39200 1.000 44.80000 ? 382 THR B O   1 
ATOM   6445 C CB  . THR B 1 382 ? 45.68200  37.49600  55.98300 1.000 44.80000 ? 382 THR B CB  1 
ATOM   6446 O OG1 . THR B 1 382 ? 46.98600  37.84900  56.45600 1.000 44.80000 ? 382 THR B OG1 1 
ATOM   6447 C CG2 . THR B 1 382 ? 45.74800  36.13900  55.33000 1.000 44.80000 ? 382 THR B CG2 1 
ATOM   6448 N N   . PRO B 1 383 ? 44.35100  40.34000  56.43500 1.000 47.17000 ? 383 PRO B N   1 
ATOM   6449 C CA  . PRO B 1 383 ? 44.52600  41.56900  57.21200 1.000 47.17000 ? 383 PRO B CA  1 
ATOM   6450 C C   . PRO B 1 383 ? 45.71100  41.43400  58.15400 1.000 47.17000 ? 383 PRO B C   1 
ATOM   6451 O O   . PRO B 1 383 ? 45.98900  40.36000  58.69300 1.000 47.17000 ? 383 PRO B O   1 
ATOM   6452 C CB  . PRO B 1 383 ? 43.20600  41.70100  57.98200 1.000 47.17000 ? 383 PRO B CB  1 
ATOM   6453 C CG  . PRO B 1 383 ? 42.62600  40.32600  57.98600 1.000 47.17000 ? 383 PRO B CG  1 
ATOM   6454 C CD  . PRO B 1 383 ? 43.03900  39.71900  56.68200 1.000 47.17000 ? 383 PRO B CD  1 
ATOM   6455 N N   . GLU B 1 384 ? 46.41100  42.54600  58.34300 1.000 59.98000 ? 384 GLU B N   1 
ATOM   6456 C CA  . GLU B 1 384 ? 47.64500  42.55800  59.11100 1.000 59.98000 ? 384 GLU B CA  1 
ATOM   6457 C C   . GLU B 1 384 ? 47.36800  42.28900  60.58600 1.000 59.98000 ? 384 GLU B C   1 
ATOM   6458 O O   . GLU B 1 384 ? 46.23800  42.41100  61.06800 1.000 59.98000 ? 384 GLU B O   1 
ATOM   6459 C CB  . GLU B 1 384 ? 48.36600  43.89400  58.94300 1.000 59.98000 ? 384 GLU B CB  1 
ATOM   6460 C CG  . GLU B 1 384 ? 47.57700  45.09200  59.44300 1.000 59.98000 ? 384 GLU B CG  1 
ATOM   6461 C CD  . GLU B 1 384 ? 48.23800  46.40900  59.08800 1.000 59.98000 ? 384 GLU B CD  1 
ATOM   6462 O OE1 . GLU B 1 384 ? 49.09500  46.41800  58.18000 1.000 59.98000 ? 384 GLU B OE1 1 
ATOM   6463 O OE2 . GLU B 1 384 ? 47.90200  47.43400  59.71900 1.000 59.98000 ? 384 GLU B OE2 1 
ATOM   6464 N N   . LYS B 1 385 ? 48.41400  41.86900  61.29400 1.000 59.97000 ? 385 LYS B N   1 
ATOM   6465 C CA  . LYS B 1 385 ? 48.29900  41.60900  62.72100 1.000 59.97000 ? 385 LYS B CA  1 
ATOM   6466 C C   . LYS B 1 385 ? 47.80500  42.85400  63.45000 1.000 59.97000 ? 385 LYS B C   1 
ATOM   6467 O O   . LYS B 1 385 ? 48.10200  43.98700  63.05500 1.000 59.97000 ? 385 LYS B O   1 
ATOM   6468 C CB  . LYS B 1 385 ? 49.64500  41.15900  63.29200 1.000 59.97000 ? 385 LYS B CB  1 
ATOM   6469 C CG  . LYS B 1 385 ? 50.03300  39.73300  62.93200 1.000 59.97000 ? 385 LYS B CG  1 
ATOM   6470 C CD  . LYS B 1 385 ? 51.52100  39.50100  63.15300 1.000 59.97000 ? 385 LYS B CD  1 
ATOM   6471 C CE  . LYS B 1 385 ? 51.86100  38.02000  63.20100 1.000 59.97000 ? 385 LYS B CE  1 
ATOM   6472 N NZ  . LYS B 1 385 ? 51.35000  37.37600  64.44400 1.000 59.97000 ? 385 LYS B NZ  1 
ATOM   6473 N N   . GLN B 1 386 ? 47.01600  42.61800  64.50400 1.000 57.32000 ? 386 GLN B N   1 
ATOM   6474 C CA  . GLN B 1 386 ? 46.25700  43.60800  65.26900 1.000 57.32000 ? 386 GLN B CA  1 
ATOM   6475 C C   . GLN B 1 386 ? 44.94400  43.94200  64.56600 1.000 57.32000 ? 386 GLN B C   1 
ATOM   6476 O O   . GLN B 1 386 ? 43.93800  44.19900  65.23300 1.000 57.32000 ? 386 GLN B O   1 
ATOM   6477 C CB  . GLN B 1 386 ? 47.07300  44.87900  65.54300 1.000 57.32000 ? 386 GLN B CB  1 
ATOM   6478 C CG  . GLN B 1 386 ? 46.36800  45.91200  66.41600 1.000 57.32000 ? 386 GLN B CG  1 
ATOM   6479 C CD  . GLN B 1 386 ? 46.06100  45.40000  67.81300 1.000 57.32000 ? 386 GLN B CD  1 
ATOM   6480 O OE1 . GLN B 1 386 ? 45.08000  44.68600  68.02600 1.000 57.32000 ? 386 GLN B OE1 1 
ATOM   6481 N NE2 . GLN B 1 386 ? 46.89900  45.76900  68.77500 1.000 57.32000 ? 386 GLN B NE2 1 
ATOM   6482 N N   . ASP B 1 387 ? 44.92500  43.94400  63.23100 1.000 56.78000 ? 387 ASP B N   1 
ATOM   6483 C CA  . ASP B 1 387 ? 43.63900  43.97000  62.53900 1.000 56.78000 ? 387 ASP B CA  1 
ATOM   6484 C C   . ASP B 1 387 ? 42.93300  42.62700  62.67700 1.000 56.78000 ? 387 ASP B C   1 
ATOM   6485 O O   . ASP B 1 387 ? 41.76000  42.56200  63.06400 1.000 56.78000 ? 387 ASP B O   1 
ATOM   6486 C CB  . ASP B 1 387 ? 43.82600  44.32500  61.06200 1.000 56.78000 ? 387 ASP B CB  1 
ATOM   6487 C CG  . ASP B 1 387 ? 44.30800  45.74500  60.85600 1.000 56.78000 ? 387 ASP B CG  1 
ATOM   6488 O OD1 . ASP B 1 387 ? 44.49300  46.46800  61.85800 1.000 56.78000 ? 387 ASP B OD1 1 
ATOM   6489 O OD2 . ASP B 1 387 ? 44.49700  46.14000  59.68600 1.000 56.78000 ? 387 ASP B OD2 1 
ATOM   6490 N N   . ILE B 1 388 ? 43.64700  41.53900  62.37600 1.000 55.22000 ? 388 ILE B N   1 
ATOM   6491 C CA  . ILE B 1 388 ? 43.10500  40.20200  62.58900 1.000 55.22000 ? 388 ILE B CA  1 
ATOM   6492 C C   . ILE B 1 388 ? 42.89900  39.93700  64.07600 1.000 55.22000 ? 388 ILE B C   1 
ATOM   6493 O O   . ILE B 1 388 ? 41.98100  39.20200  64.46200 1.000 55.22000 ? 388 ILE B O   1 
ATOM   6494 C CB  . ILE B 1 388 ? 44.03200  39.16300  61.92600 1.000 55.22000 ? 388 ILE B CB  1 
ATOM   6495 C CG1 . ILE B 1 388 ? 43.67600  37.73900  62.35400 1.000 55.22000 ? 388 ILE B CG1 1 
ATOM   6496 C CG2 . ILE B 1 388 ? 45.48000  39.47800  62.22300 1.000 55.22000 ? 388 ILE B CG2 1 
ATOM   6497 C CD1 . ILE B 1 388 ? 42.37100  37.25400  61.79300 1.000 55.22000 ? 388 ILE B CD1 1 
ATOM   6498 N N   . GLN B 1 389 ? 43.71600  40.54700  64.93800 1.000 58.35000 ? 389 GLN B N   1 
ATOM   6499 C CA  . GLN B 1 389 ? 43.48900  40.40900  66.37300 1.000 58.35000 ? 389 GLN B CA  1 
ATOM   6500 C C   . GLN B 1 389 ? 42.19000  41.08500  66.79600 1.000 58.35000 ? 389 GLN B C   1 
ATOM   6501 O O   . GLN B 1 389 ? 41.43200  40.53500  67.60300 1.000 58.35000 ? 389 GLN B O   1 
ATOM   6502 C CB  . GLN B 1 389 ? 44.67300  40.98400  67.15000 1.000 58.35000 ? 389 GLN B CB  1 
ATOM   6503 C CG  . GLN B 1 389 ? 45.99200  40.26400  66.90700 1.000 58.35000 ? 389 GLN B CG  1 
ATOM   6504 C CD  . GLN B 1 389 ? 46.06800  38.92200  67.61000 1.000 58.35000 ? 389 GLN B CD  1 
ATOM   6505 O OE1 . GLN B 1 389 ? 45.21300  38.58700  68.43100 1.000 58.35000 ? 389 GLN B OE1 1 
ATOM   6506 N NE2 . GLN B 1 389 ? 47.09700  38.14600  67.29200 1.000 58.35000 ? 389 GLN B NE2 1 
ATOM   6507 N N   . ASN B 1 390 ? 41.90400  42.27200  66.25300 1.000 56.02000 ? 390 ASN B N   1 
ATOM   6508 C CA  . ASN B 1 390 ? 40.62200  42.90600  66.54200 1.000 56.02000 ? 390 ASN B CA  1 
ATOM   6509 C C   . ASN B 1 390 ? 39.46300  42.12000  65.94600 1.000 56.02000 ? 390 ASN B C   1 
ATOM   6510 O O   . ASN B 1 390 ? 38.37000  42.09000  66.52700 1.000 56.02000 ? 390 ASN B O   1 
ATOM   6511 C CB  . ASN B 1 390 ? 40.61000  44.34300  66.02200 1.000 56.02000 ? 390 ASN B CB  1 
ATOM   6512 C CG  . ASN B 1 390 ? 41.62200  45.22100  66.72400 1.000 56.02000 ? 390 ASN B CG  1 
ATOM   6513 O OD1 . ASN B 1 390 ? 42.09800  44.89200  67.81100 1.000 56.02000 ? 390 ASN B OD1 1 
ATOM   6514 N ND2 . ASN B 1 390 ? 41.96100  46.34600  66.10500 1.000 56.02000 ? 390 ASN B ND2 1 
ATOM   6515 N N   . LEU B 1 391 ? 39.67900  41.47600  64.79700 1.000 52.81000 ? 391 LEU B N   1 
ATOM   6516 C CA  . LEU B 1 391 ? 38.63300  40.63300  64.22800 1.000 52.81000 ? 391 LEU B CA  1 
ATOM   6517 C C   . LEU B 1 391 ? 38.35000  39.43300  65.12300 1.000 52.81000 ? 391 LEU B C   1 
ATOM   6518 O O   . LEU B 1 391 ? 37.18700  39.07100  65.33400 1.000 52.81000 ? 391 LEU B O   1 
ATOM   6519 C CB  . LEU B 1 391 ? 39.03400  40.18200  62.82400 1.000 52.81000 ? 391 LEU B CB  1 
ATOM   6520 C CG  . LEU B 1 391 ? 38.14400  39.15100  62.12700 1.000 52.81000 ? 391 LEU B CG  1 
ATOM   6521 C CD1 . LEU B 1 391 ? 36.70000  39.62500  62.06400 1.000 52.81000 ? 391 LEU B CD1 1 
ATOM   6522 C CD2 . LEU B 1 391 ? 38.67300  38.85600  60.73300 1.000 52.81000 ? 391 LEU B CD2 1 
ATOM   6523 N N   . LEU B 1 392 ? 39.39800  38.82300  65.68300 1.000 54.46000 ? 392 LEU B N   1 
ATOM   6524 C CA  . LEU B 1 392 ? 39.19800  37.73400  66.63400 1.000 54.46000 ? 392 LEU B CA  1 
ATOM   6525 C C   . LEU B 1 392 ? 38.54300  38.22500  67.91700 1.000 54.46000 ? 392 LEU B C   1 
ATOM   6526 O O   . LEU B 1 392 ? 37.75400  37.49500  68.53000 1.000 54.46000 ? 392 LEU B O   1 
ATOM   6527 C CB  . LEU B 1 392 ? 40.53300  37.05800  66.94800 1.000 54.46000 ? 392 LEU B CB  1 
ATOM   6528 C CG  . LEU B 1 392 ? 41.17700  36.25800  65.81700 1.000 54.46000 ? 392 LEU B CG  1 
ATOM   6529 C CD1 . LEU B 1 392 ? 42.59400  35.86100  66.19100 1.000 54.46000 ? 392 LEU B CD1 1 
ATOM   6530 C CD2 . LEU B 1 392 ? 40.34000  35.03000  65.49800 1.000 54.46000 ? 392 LEU B CD2 1 
ATOM   6531 N N   . LEU B 1 393 ? 38.83700  39.46200  68.32300 1.000 57.02000 ? 393 LEU B N   1 
ATOM   6532 C CA  . LEU B 1 393 ? 38.18400  40.03500  69.49500 1.000 57.02000 ? 393 LEU B CA  1 
ATOM   6533 C C   . LEU B 1 393 ? 36.68700  40.18500  69.25900 1.000 57.02000 ? 393 LEU B C   1 
ATOM   6534 O O   . LEU B 1 393 ? 35.86800  39.76800  70.08800 1.000 57.02000 ? 393 LEU B O   1 
ATOM   6535 C CB  . LEU B 1 393 ? 38.82300  41.38500  69.83400 1.000 57.02000 ? 393 LEU B CB  1 
ATOM   6536 C CG  . LEU B 1 393 ? 38.12900  42.32700  70.82300 1.000 57.02000 ? 393 LEU B CG  1 
ATOM   6537 C CD1 . LEU B 1 393 ? 39.15900  43.01200  71.70500 1.000 57.02000 ? 393 LEU B CD1 1 
ATOM   6538 C CD2 . LEU B 1 393 ? 37.28800  43.37100  70.09500 1.000 57.02000 ? 393 LEU B CD2 1 
ATOM   6539 N N   . TRP B 1 394 ? 36.31300  40.76300  68.11500 1.000 54.16000 ? 394 TRP B N   1 
ATOM   6540 C CA  . TRP B 1 394 ? 34.89700  40.89800  67.78900 1.000 54.16000 ? 394 TRP B CA  1 
ATOM   6541 C C   . TRP B 1 394 ? 34.23500  39.53900  67.61100 1.000 54.16000 ? 394 TRP B C   1 
ATOM   6542 O O   . TRP B 1 394 ? 33.05700  39.37600  67.94700 1.000 54.16000 ? 394 TRP B O   1 
ATOM   6543 C CB  . TRP B 1 394 ? 34.71800  41.74300  66.52700 1.000 54.16000 ? 394 TRP B CB  1 
ATOM   6544 C CG  . TRP B 1 394 ? 33.27800  41.94800  66.14500 1.000 54.16000 ? 394 TRP B CG  1 
ATOM   6545 C CD1 . TRP B 1 394 ? 32.47700  42.99400  66.50100 1.000 54.16000 ? 394 TRP B CD1 1 
ATOM   6546 C CD2 . TRP B 1 394 ? 32.46900  41.08100  65.33800 1.000 54.16000 ? 394 TRP B CD2 1 
ATOM   6547 N NE1 . TRP B 1 394 ? 31.22100  42.83400  65.96600 1.000 54.16000 ? 394 TRP B NE1 1 
ATOM   6548 C CE2 . TRP B 1 394 ? 31.19100  41.66700  65.24700 1.000 54.16000 ? 394 TRP B CE2 1 
ATOM   6549 C CE3 . TRP B 1 394 ? 32.70200  39.86700  64.68300 1.000 54.16000 ? 394 TRP B CE3 1 
ATOM   6550 C CZ2 . TRP B 1 394 ? 30.15000  41.08100  64.52900 1.000 54.16000 ? 394 TRP B CZ2 1 
ATOM   6551 C CZ3 . TRP B 1 394 ? 31.66700  39.28700  63.97100 1.000 54.16000 ? 394 TRP B CZ3 1 
ATOM   6552 C CH2 . TRP B 1 394 ? 30.40800  39.89500  63.90000 1.000 54.16000 ? 394 TRP B CH2 1 
ATOM   6553 N N   . ILE B 1 395 ? 34.97500  38.55200  67.10400 1.000 55.16000 ? 395 ILE B N   1 
ATOM   6554 C CA  . ILE B 1 395 ? 34.41300  37.22000  66.90700 1.000 55.16000 ? 395 ILE B CA  1 
ATOM   6555 C C   . ILE B 1 395 ? 34.10800  36.56600  68.24900 1.000 55.16000 ? 395 ILE B C   1 
ATOM   6556 O O   . ILE B 1 395 ? 33.01200  36.03800  68.46500 1.000 55.16000 ? 395 ILE B O   1 
ATOM   6557 C CB  . ILE B 1 395 ? 35.37000  36.36300  66.05700 1.000 55.16000 ? 395 ILE B CB  1 
ATOM   6558 C CG1 . ILE B 1 395 ? 35.17300  36.66000  64.56800 1.000 55.16000 ? 395 ILE B CG1 1 
ATOM   6559 C CG2 . ILE B 1 395 ? 35.19400  34.88000  66.35500 1.000 55.16000 ? 395 ILE B CG2 1 
ATOM   6560 C CD1 . ILE B 1 395 ? 36.16100  35.95100  63.66700 1.000 55.16000 ? 395 ILE B CD1 1 
ATOM   6561 N N   . HIS B 1 396 ? 35.07000  36.59900  69.17400 1.000 58.45000 ? 396 HIS B N   1 
ATOM   6562 C CA  . HIS B 1 396 ? 34.83200  36.03100  70.49700 1.000 58.45000 ? 396 HIS B CA  1 
ATOM   6563 C C   . HIS B 1 396 ? 33.75500  36.79500  71.25400 1.000 58.45000 ? 396 HIS B C   1 
ATOM   6564 O O   . HIS B 1 396 ? 33.00700  36.19800  72.03900 1.000 58.45000 ? 396 HIS B O   1 
ATOM   6565 C CB  . HIS B 1 396 ? 36.12900  36.00700  71.30500 1.000 58.45000 ? 396 HIS B CB  1 
ATOM   6566 C CG  . HIS B 1 396 ? 35.94500  35.57500  72.72600 1.000 58.45000 ? 396 HIS B CG  1 
ATOM   6567 N ND1 . HIS B 1 396 ? 35.24000  34.44200  73.07400 1.000 58.45000 ? 396 HIS B ND1 1 
ATOM   6568 C CD2 . HIS B 1 396 ? 36.36900  36.12500  73.88800 1.000 58.45000 ? 396 HIS B CD2 1 
ATOM   6569 C CE1 . HIS B 1 396 ? 35.24000  34.31200  74.38800 1.000 58.45000 ? 396 HIS B CE1 1 
ATOM   6570 N NE2 . HIS B 1 396 ? 35.91900  35.32000  74.90700 1.000 58.45000 ? 396 HIS B NE2 1 
ATOM   6571 N N   . ASN B 1 397 ? 33.65300  38.10900  71.03700 1.000 58.15000 ? 397 ASN B N   1 
ATOM   6572 C CA  . ASN B 1 397 ? 32.67400  38.90200  71.77200 1.000 58.15000 ? 397 ASN B CA  1 
ATOM   6573 C C   . ASN B 1 397 ? 31.26900  38.78700  71.19400 1.000 58.15000 ? 397 ASN B C   1 
ATOM   6574 O O   . ASN B 1 397 ? 30.29000  38.97100  71.92600 1.000 58.15000 ? 397 ASN B O   1 
ATOM   6575 C CB  . ASN B 1 397 ? 33.10800  40.36900  71.79700 1.000 58.15000 ? 397 ASN B CB  1 
ATOM   6576 C CG  . ASN B 1 397 ? 32.21800  41.22600  72.67700 1.000 58.15000 ? 397 ASN B CG  1 
ATOM   6577 O OD1 . ASN B 1 397 ? 31.63200  40.74300  73.64600 1.000 58.15000 ? 397 ASN B OD1 1 
ATOM   6578 N ND2 . ASN B 1 397 ? 32.11200  42.50700  72.34300 1.000 58.15000 ? 397 ASN B ND2 1 
ATOM   6579 N N   . ASN B 1 398 ? 31.13700  38.47500  69.90600 1.000 56.36000 ? 398 ASN B N   1 
ATOM   6580 C CA  . ASN B 1 398 ? 29.84600  38.57400  69.23500 1.000 56.36000 ? 398 ASN B CA  1 
ATOM   6581 C C   . ASN B 1 398 ? 29.38500  37.26900  68.61000 1.000 56.36000 ? 398 ASN B C   1 
ATOM   6582 O O   . ASN B 1 398 ? 28.26800  36.82000  68.89400 1.000 56.36000 ? 398 ASN B O   1 
ATOM   6583 C CB  . ASN B 1 398 ? 29.89900  39.67500  68.16500 1.000 56.36000 ? 398 ASN B CB  1 
ATOM   6584 C CG  . ASN B 1 398 ? 30.14500  41.04700  68.75500 1.000 56.36000 ? 398 ASN B CG  1 
ATOM   6585 O OD1 . ASN B 1 398 ? 29.20700  41.80000  69.01600 1.000 56.36000 ? 398 ASN B OD1 1 
ATOM   6586 N ND2 . ASN B 1 398 ? 31.41200  41.37700  68.97500 1.000 56.36000 ? 398 ASN B ND2 1 
ATOM   6587 N N   . ILE B 1 399 ? 30.19900  36.65100  67.74900 1.000 54.71000 ? 399 ILE B N   1 
ATOM   6588 C CA  . ILE B 1 399 ? 29.73700  35.46900  67.03300 1.000 54.71000 ? 399 ILE B CA  1 
ATOM   6589 C C   . ILE B 1 399 ? 29.48200  34.33900  68.02400 1.000 54.71000 ? 399 ILE B C   1 
ATOM   6590 O O   . ILE B 1 399 ? 30.17900  34.19800  69.03900 1.000 54.71000 ? 399 ILE B O   1 
ATOM   6591 C CB  . ILE B 1 399 ? 30.73700  35.07000  65.93300 1.000 54.71000 ? 399 ILE B CB  1 
ATOM   6592 C CG1 . ILE B 1 399 ? 30.00700  34.35100  64.80100 1.000 54.71000 ? 399 ILE B CG1 1 
ATOM   6593 C CG2 . ILE B 1 399 ? 31.82100  34.16300  66.46500 1.000 54.71000 ? 399 ILE B CG2 1 
ATOM   6594 C CD1 . ILE B 1 399 ? 29.00700  35.21900  64.07700 1.000 54.71000 ? 399 ILE B CD1 1 
ATOM   6595 N N   . ASP B 1 400 ? 28.44400  33.55200  67.75200 1.000 57.18000 ? 400 ASP B N   1 
ATOM   6596 C CA  . ASP B 1 400 ? 27.93800  32.56400  68.70000 1.000 57.18000 ? 400 ASP B CA  1 
ATOM   6597 C C   . ASP B 1 400 ? 27.52600  31.29500  67.96000 1.000 57.18000 ? 400 ASP B C   1 
ATOM   6598 O O   . ASP B 1 400 ? 26.45000  30.73800  68.17900 1.000 57.18000 ? 400 ASP B O   1 
ATOM   6599 C CB  . ASP B 1 400 ? 26.77100  33.14700  69.49700 1.000 57.18000 ? 400 ASP B CB  1 
ATOM   6600 C CG  . ASP B 1 400 ? 26.63800  32.53300  70.87600 1.000 57.18000 ? 400 ASP B CG  1 
ATOM   6601 O OD1 . ASP B 1 400 ? 27.07900  31.38000  71.06300 1.000 57.18000 ? 400 ASP B OD1 1 
ATOM   6602 O OD2 . ASP B 1 400 ? 26.09000  33.20700  71.77500 1.000 57.18000 ? 400 ASP B OD2 1 
ATOM   6603 N N   . GLU B 1 401 ? 28.39300  30.82700  67.06400 1.000 50.01000 ? 401 GLU B N   1 
ATOM   6604 C CA  . GLU B 1 401 ? 28.13200  29.64200  66.25900 1.000 50.01000 ? 401 GLU B CA  1 
ATOM   6605 C C   . GLU B 1 401 ? 29.43700  28.88900  66.04700 1.000 50.01000 ? 401 GLU B C   1 
ATOM   6606 O O   . GLU B 1 401 ? 30.52800  29.44400  66.19300 1.000 50.01000 ? 401 GLU B O   1 
ATOM   6607 C CB  . GLU B 1 401 ? 27.52100  29.99300  64.89400 1.000 50.01000 ? 401 GLU B CB  1 
ATOM   6608 C CG  . GLU B 1 401 ? 26.26300  30.84400  64.94300 1.000 50.01000 ? 401 GLU B CG  1 
ATOM   6609 C CD  . GLU B 1 401 ? 26.04000  31.61400  63.65600 1.000 50.01000 ? 401 GLU B CD  1 
ATOM   6610 O OE1 . GLU B 1 401 ? 26.73300  31.32600  62.65700 1.000 50.01000 ? 401 GLU B OE1 1 
ATOM   6611 O OE2 . GLU B 1 401 ? 25.17600  32.51500  63.64400 1.000 50.01000 ? 401 GLU B OE2 1 
ATOM   6612 N N   . ASP B 1 402 ? 29.31400  27.59700  65.72900 1.000 42.87000 ? 402 ASP B N   1 
ATOM   6613 C CA  . ASP B 1 402 ? 30.49600  26.81700  65.37500 1.000 42.87000 ? 402 ASP B CA  1 
ATOM   6614 C C   . ASP B 1 402 ? 31.11400  27.29100  64.06500 1.000 42.87000 ? 402 ASP B C   1 
ATOM   6615 O O   . ASP B 1 402 ? 32.33800  27.22600  63.89700 1.000 42.87000 ? 402 ASP B O   1 
ATOM   6616 C CB  . ASP B 1 402 ? 30.14100  25.33200  65.29300 1.000 42.87000 ? 402 ASP B CB  1 
ATOM   6617 C CG  . ASP B 1 402 ? 30.74800  24.52500  66.42700 1.000 42.87000 ? 402 ASP B CG  1 
ATOM   6618 O OD1 . ASP B 1 402 ? 31.27400  25.13400  67.38300 1.000 42.87000 ? 402 ASP B OD1 1 
ATOM   6619 O OD2 . ASP B 1 402 ? 30.70400  23.27700  66.35500 1.000 42.87000 ? 402 ASP B OD2 1 
ATOM   6620 N N   . ILE B 1 403 ? 30.29600  27.78300  63.14000 1.000 39.48000 ? 403 ILE B N   1 
ATOM   6621 C CA  . ILE B 1 403 ? 30.77100  28.26800  61.85100 1.000 39.48000 ? 403 ILE B CA  1 
ATOM   6622 C C   . ILE B 1 403 ? 29.93200  29.47400  61.45500 1.000 39.48000 ? 403 ILE B C   1 
ATOM   6623 O O   . ILE B 1 403 ? 28.71500  29.50000  61.66500 1.000 39.48000 ? 403 ILE B O   1 
ATOM   6624 C CB  . ILE B 1 403 ? 30.72300  27.16400  60.77100 1.000 39.48000 ? 403 ILE B CB  1 
ATOM   6625 C CG1 . ILE B 1 403 ? 31.37100  27.65300  59.47400 1.000 39.48000 ? 403 ILE B CG1 1 
ATOM   6626 C CG2 . ILE B 1 403 ? 29.29200  26.68700  60.53200 1.000 39.48000 ? 403 ILE B CG2 1 
ATOM   6627 C CD1 . ILE B 1 403 ? 31.70700  26.54100  58.51300 1.000 39.48000 ? 403 ILE B CD1 1 
ATOM   6628 N N   . PHE B 1 404 ? 30.59300  30.47800  60.88700 1.000 37.22000 ? 404 PHE B N   1 
ATOM   6629 C CA  . PHE B 1 404 ? 29.94900  31.72500  60.51000 1.000 37.22000 ? 404 PHE B CA  1 
ATOM   6630 C C   . PHE B 1 404 ? 30.57500  32.21000  59.21500 1.000 37.22000 ? 404 PHE B C   1 
ATOM   6631 O O   . PHE B 1 404 ? 31.75200  31.96300  58.95600 1.000 37.22000 ? 404 PHE B O   1 
ATOM   6632 C CB  . PHE B 1 404 ? 30.09300  32.77400  61.62400 1.000 37.22000 ? 404 PHE B CB  1 
ATOM   6633 C CG  . PHE B 1 404 ? 30.11800  34.19600  61.13500 1.000 37.22000 ? 404 PHE B CG  1 
ATOM   6634 C CD1 . PHE B 1 404 ? 28.95100  34.83400  60.75100 1.000 37.22000 ? 404 PHE B CD1 1 
ATOM   6635 C CD2 . PHE B 1 404 ? 31.31000  34.90200  61.08300 1.000 37.22000 ? 404 PHE B CD2 1 
ATOM   6636 C CE1 . PHE B 1 404 ? 28.97400  36.14300  60.31000 1.000 37.22000 ? 404 PHE B CE1 1 
ATOM   6637 C CE2 . PHE B 1 404 ? 31.33800  36.21100  60.64300 1.000 37.22000 ? 404 PHE B CE2 1 
ATOM   6638 C CZ  . PHE B 1 404 ? 30.16900  36.83200  60.25700 1.000 37.22000 ? 404 PHE B CZ  1 
ATOM   6639 N N   . TYR B 1 405 ? 29.78000  32.88500  58.39200 1.000 33.23000 ? 405 TYR B N   1 
ATOM   6640 C CA  . TYR B 1 405 ? 30.30500  33.36800  57.12500 1.000 33.23000 ? 405 TYR B CA  1 
ATOM   6641 C C   . TYR B 1 405 ? 29.46100  34.53600  56.64700 1.000 33.23000 ? 405 TYR B C   1 
ATOM   6642 O O   . TYR B 1 405 ? 28.26000  34.60800  56.91900 1.000 33.23000 ? 405 TYR B O   1 
ATOM   6643 C CB  . TYR B 1 405 ? 30.33300  32.25700  56.06800 1.000 33.23000 ? 405 TYR B CB  1 
ATOM   6644 C CG  . TYR B 1 405 ? 28.97000  31.78500  55.61300 1.000 33.23000 ? 405 TYR B CG  1 
ATOM   6645 C CD1 . TYR B 1 405 ? 28.13100  31.08300  56.47000 1.000 33.23000 ? 405 TYR B CD1 1 
ATOM   6646 C CD2 . TYR B 1 405 ? 28.52900  32.02500  54.31800 1.000 33.23000 ? 405 TYR B CD2 1 
ATOM   6647 C CE1 . TYR B 1 405 ? 26.88700  30.64700  56.05600 1.000 33.23000 ? 405 TYR B CE1 1 
ATOM   6648 C CE2 . TYR B 1 405 ? 27.28600  31.59100  53.89400 1.000 33.23000 ? 405 TYR B CE2 1 
ATOM   6649 C CZ  . TYR B 1 405 ? 26.46900  30.90200  54.76600 1.000 33.23000 ? 405 TYR B CZ  1 
ATOM   6650 O OH  . TYR B 1 405 ? 25.23100  30.46800  54.34700 1.000 33.23000 ? 405 TYR B OH  1 
ATOM   6651 N N   . THR B 1 406 ? 30.11300  35.44900  55.93400 1.000 31.53000 ? 406 THR B N   1 
ATOM   6652 C CA  . THR B 1 406 ? 29.41600  36.56700  55.31700 1.000 31.53000 ? 406 THR B CA  1 
ATOM   6653 C C   . THR B 1 406 ? 30.25100  37.08600  54.15700 1.000 31.53000 ? 406 THR B C   1 
ATOM   6654 O O   . THR B 1 406 ? 31.48200  37.10500  54.22900 1.000 31.53000 ? 406 THR B O   1 
ATOM   6655 C CB  . THR B 1 406 ? 29.14000  37.68800  56.33200 1.000 31.53000 ? 406 THR B CB  1 
ATOM   6656 O OG1 . THR B 1 406 ? 28.49700  38.78800  55.67600 1.000 31.53000 ? 406 THR B OG1 1 
ATOM   6657 C CG2 . THR B 1 406 ? 30.43200  38.16800  56.98100 1.000 31.53000 ? 406 THR B CG2 1 
ATOM   6658 N N   . ASP B 1 407 ? 29.57400  37.49600  53.08500 1.000 30.10000 ? 407 ASP B N   1 
ATOM   6659 C CA  . ASP B 1 407 ? 30.25400  38.10600  51.95000 1.000 30.10000 ? 407 ASP B CA  1 
ATOM   6660 C C   . ASP B 1 407 ? 30.54700  39.58600  52.16300 1.000 30.10000 ? 407 ASP B C   1 
ATOM   6661 O O   . ASP B 1 407 ? 31.25000  40.18500  51.34300 1.000 30.10000 ? 407 ASP B O   1 
ATOM   6662 C CB  . ASP B 1 407 ? 29.42800  37.91700  50.67400 1.000 30.10000 ? 407 ASP B CB  1 
ATOM   6663 C CG  . ASP B 1 407 ? 27.99400  38.38800  50.83000 1.000 30.10000 ? 407 ASP B CG  1 
ATOM   6664 O OD1 . ASP B 1 407 ? 27.46400  38.32400  51.96000 1.000 30.10000 ? 407 ASP B OD1 1 
ATOM   6665 O OD2 . ASP B 1 407 ? 27.39600  38.82000  49.82200 1.000 30.10000 ? 407 ASP B OD2 1 
ATOM   6666 N N   . SER B 1 408 ? 30.02400  40.18400  53.23800 1.000 33.52000 ? 408 SER B N   1 
ATOM   6667 C CA  . SER B 1 408 ? 30.26200  41.59200  53.57400 1.000 33.52000 ? 408 SER B CA  1 
ATOM   6668 C C   . SER B 1 408 ? 30.50000  41.67000  55.08200 1.000 33.52000 ? 408 SER B C   1 
ATOM   6669 O O   . SER B 1 408 ? 29.57200  41.92200  55.85500 1.000 33.52000 ? 408 SER B O   1 
ATOM   6670 C CB  . SER B 1 408 ? 29.09600  42.47000  53.14400 1.000 33.52000 ? 408 SER B CB  1 
ATOM   6671 O OG  . SER B 1 408 ? 29.31600  43.82000  53.51800 1.000 33.52000 ? 408 SER B OG  1 
ATOM   6672 N N   . LEU B 1 409 ? 31.74900  41.43800  55.49300 1.000 38.55000 ? 409 LEU B N   1 
ATOM   6673 C CA  . LEU B 1 409 ? 32.08100  41.49200  56.91200 1.000 38.55000 ? 409 LEU B CA  1 
ATOM   6674 C C   . LEU B 1 409 ? 31.91000  42.89400  57.48400 1.000 38.55000 ? 409 LEU B C   1 
ATOM   6675 O O   . LEU B 1 409 ? 31.56300  43.04300  58.66100 1.000 38.55000 ? 409 LEU B O   1 
ATOM   6676 C CB  . LEU B 1 409 ? 33.51500  41.00400  57.12900 1.000 38.55000 ? 409 LEU B CB  1 
ATOM   6677 C CG  . LEU B 1 409 ? 34.07600  41.08700  58.55000 1.000 38.55000 ? 409 LEU B CG  1 
ATOM   6678 C CD1 . LEU B 1 409 ? 33.24700  40.24000  59.50500 1.000 38.55000 ? 409 LEU B CD1 1 
ATOM   6679 C CD2 . LEU B 1 409 ? 35.53900  40.67000  58.58100 1.000 38.55000 ? 409 LEU B CD2 1 
ATOM   6680 N N   . SER B 1 410 ? 32.13600  43.92800  56.66900 1.000 40.93000 ? 410 SER B N   1 
ATOM   6681 C CA  . SER B 1 410 ? 32.14000  45.29300  57.18500 1.000 40.93000 ? 410 SER B CA  1 
ATOM   6682 C C   . SER B 1 410 ? 30.76200  45.74000  57.66200 1.000 40.93000 ? 410 SER B C   1 
ATOM   6683 O O   . SER B 1 410 ? 30.66900  46.56200  58.58100 1.000 40.93000 ? 410 SER B O   1 
ATOM   6684 C CB  . SER B 1 410 ? 32.66900  46.25200  56.12000 1.000 40.93000 ? 410 SER B CB  1 
ATOM   6685 O OG  . SER B 1 410 ? 31.87800  46.19600  54.94700 1.000 40.93000 ? 410 SER B OG  1 
ATOM   6686 N N   . GLN B 1 411 ? 29.68800  45.22500  57.06400 1.000 39.89000 ? 411 GLN B N   1 
ATOM   6687 C CA  . GLN B 1 411 ? 28.35800  45.68600  57.44300 1.000 39.89000 ? 411 GLN B CA  1 
ATOM   6688 C C   . GLN B 1 411 ? 27.85600  45.06700  58.74100 1.000 39.89000 ? 411 GLN B C   1 
ATOM   6689 O O   . GLN B 1 411 ? 26.86100  45.54900  59.29200 1.000 39.89000 ? 411 GLN B O   1 
ATOM   6690 C CB  . GLN B 1 411 ? 27.35700  45.42000  56.31500 1.000 39.89000 ? 411 GLN B CB  1 
ATOM   6691 C CG  . GLN B 1 411 ? 27.11900  43.95900  55.99400 1.000 39.89000 ? 411 GLN B CG  1 
ATOM   6692 C CD  . GLN B 1 411 ? 26.11300  43.77400  54.87300 1.000 39.89000 ? 411 GLN B CD  1 
ATOM   6693 O OE1 . GLN B 1 411 ? 25.49900  44.73600  54.41000 1.000 39.89000 ? 411 GLN B OE1 1 
ATOM   6694 N NE2 . GLN B 1 411 ? 25.93900  42.53400  54.43000 1.000 39.89000 ? 411 GLN B NE2 1 
ATOM   6695 N N   . VAL B 1 412 ? 28.50300  44.01200  59.23600 1.000 42.75000 ? 412 VAL B N   1 
ATOM   6696 C CA  . VAL B 1 412 ? 28.25100  43.49200  60.57500 1.000 42.75000 ? 412 VAL B CA  1 
ATOM   6697 C C   . VAL B 1 412 ? 29.38200  43.81400  61.53500 1.000 42.75000 ? 412 VAL B C   1 
ATOM   6698 O O   . VAL B 1 412 ? 29.28200  43.49300  62.72800 1.000 42.75000 ? 412 VAL B O   1 
ATOM   6699 C CB  . VAL B 1 412 ? 27.98700  41.97400  60.54900 1.000 42.75000 ? 412 VAL B CB  1 
ATOM   6700 C CG1 . VAL B 1 412 ? 26.89500  41.64400  59.54200 1.000 42.75000 ? 412 VAL B CG1 1 
ATOM   6701 C CG2 . VAL B 1 412 ? 29.26800  41.21300  60.23200 1.000 42.75000 ? 412 VAL B CG2 1 
ATOM   6702 N N   . TYR B 1 413 ? 30.45100  44.44200  61.05300 1.000 46.56000 ? 413 TYR B N   1 
ATOM   6703 C CA  . TYR B 1 413 ? 31.64000  44.77000  61.82700 1.000 46.56000 ? 413 TYR B CA  1 
ATOM   6704 C C   . TYR B 1 413 ? 32.34300  45.93400  61.14000 1.000 46.56000 ? 413 TYR B C   1 
ATOM   6705 O O   . TYR B 1 413 ? 33.18300  45.71800  60.25400 1.000 46.56000 ? 413 TYR B O   1 
ATOM   6706 C CB  . TYR B 1 413 ? 32.54900  43.54600  61.95300 1.000 46.56000 ? 413 TYR B CB  1 
ATOM   6707 C CG  . TYR B 1 413 ? 33.88100  43.79600  62.62900 1.000 46.56000 ? 413 TYR B CG  1 
ATOM   6708 C CD1 . TYR B 1 413 ? 33.95400  44.41900  63.86800 1.000 46.56000 ? 413 TYR B CD1 1 
ATOM   6709 C CD2 . TYR B 1 413 ? 35.06600  43.37900  62.03500 1.000 46.56000 ? 413 TYR B CD2 1 
ATOM   6710 C CE1 . TYR B 1 413 ? 35.17400  44.63600  64.48800 1.000 46.56000 ? 413 TYR B CE1 1 
ATOM   6711 C CE2 . TYR B 1 413 ? 36.28800  43.59100  62.64600 1.000 46.56000 ? 413 TYR B CE2 1 
ATOM   6712 C CZ  . TYR B 1 413 ? 36.33600  44.21800  63.87200 1.000 46.56000 ? 413 TYR B CZ  1 
ATOM   6713 O OH  . TYR B 1 413 ? 37.55300  44.42900  64.47900 1.000 46.56000 ? 413 TYR B OH  1 
ATOM   6714 N N   . PRO B 1 414 ? 32.02200  47.17400  61.51800 1.000 46.05000 ? 414 PRO B N   1 
ATOM   6715 C CA  . PRO B 1 414 ? 32.48000  48.33600  60.73300 1.000 46.05000 ? 414 PRO B CA  1 
ATOM   6716 C C   . PRO B 1 414 ? 33.98900  48.44100  60.59700 1.000 46.05000 ? 414 PRO B C   1 
ATOM   6717 O O   . PRO B 1 414 ? 34.47100  48.94600  59.57300 1.000 46.05000 ? 414 PRO B O   1 
ATOM   6718 C CB  . PRO B 1 414 ? 31.89600  49.52700  61.50600 1.000 46.05000 ? 414 PRO B CB  1 
ATOM   6719 C CG  . PRO B 1 414 ? 30.71000  48.96300  62.21800 1.000 46.05000 ? 414 PRO B CG  1 
ATOM   6720 C CD  . PRO B 1 414 ? 31.10200  47.56400  62.59900 1.000 46.05000 ? 414 PRO B CD  1 
ATOM   6721 N N   . GLU B 1 415 ? 34.74700  47.97900  61.59300 1.000 45.28000 ? 415 GLU B N   1 
ATOM   6722 C CA  . GLU B 1 415 ? 36.20100  48.08500  61.53600 1.000 45.28000 ? 415 GLU B CA  1 
ATOM   6723 C C   . GLU B 1 415 ? 36.76300  47.40700  60.29200 1.000 45.28000 ? 415 GLU B C   1 
ATOM   6724 O O   . GLU B 1 415 ? 37.77700  47.85300  59.74200 1.000 45.28000 ? 415 GLU B O   1 
ATOM   6725 C CB  . GLU B 1 415 ? 36.81100  47.46900  62.79800 1.000 45.28000 ? 415 GLU B CB  1 
ATOM   6726 C CG  . GLU B 1 415 ? 38.30700  47.67000  62.95600 1.000 45.28000 ? 415 GLU B CG  1 
ATOM   6727 C CD  . GLU B 1 415 ? 38.64900  48.84300  63.85500 1.000 45.28000 ? 415 GLU B CD  1 
ATOM   6728 O OE1 . GLU B 1 415 ? 37.71500  49.52500  64.32700 1.000 45.28000 ? 415 GLU B OE1 1 
ATOM   6729 O OE2 . GLU B 1 415 ? 39.85300  49.07900  64.09300 1.000 45.28000 ? 415 GLU B OE2 1 
ATOM   6730 N N   . ALA B 1 416 ? 36.07100  46.38100  59.78900 1.000 44.40000 ? 416 ALA B N   1 
ATOM   6731 C CA  . ALA B 1 416 ? 36.53800  45.65700  58.61400 1.000 44.40000 ? 416 ALA B CA  1 
ATOM   6732 C C   . ALA B 1 416 ? 36.64900  46.55700  57.39300 1.000 44.40000 ? 416 ALA B C   1 
ATOM   6733 O O   . ALA B 1 416 ? 37.37500  46.21300  56.45000 1.000 44.40000 ? 416 ALA B O   1 
ATOM   6734 C CB  . ALA B 1 416 ? 35.61300  44.47900  58.31600 1.000 44.40000 ? 416 ALA B CB  1 
ATOM   6735 N N   . GLU B 1 417 ? 35.95700  47.70000  57.38900 1.000 43.93000 ? 417 GLU B N   1 
ATOM   6736 C CA  . GLU B 1 417 ? 36.07800  48.62800  56.26900 1.000 43.93000 ? 417 GLU B CA  1 
ATOM   6737 C C   . GLU B 1 417 ? 37.52200  49.05500  56.04800 1.000 43.93000 ? 417 GLU B C   1 
ATOM   6738 O O   . GLU B 1 417 ? 37.91300  49.34400  54.91100 1.000 43.93000 ? 417 GLU B O   1 
ATOM   6739 C CB  . GLU B 1 417 ? 35.21600  49.87100  56.50200 1.000 43.93000 ? 417 GLU B CB  1 
ATOM   6740 C CG  . GLU B 1 417 ? 33.72500  49.67300  56.31100 1.000 43.93000 ? 417 GLU B CG  1 
ATOM   6741 C CD  . GLU B 1 417 ? 33.06300  50.87700  55.66400 1.000 43.93000 ? 417 GLU B CD  1 
ATOM   6742 O OE1 . GLU B 1 417 ? 33.68300  51.48200  54.76200 1.000 43.93000 ? 417 GLU B OE1 1 
ATOM   6743 O OE2 . GLU B 1 417 ? 31.92700  51.22300  56.05500 1.000 43.93000 ? 417 GLU B OE2 1 
ATOM   6744 N N   . LYS B 1 418 ? 38.33000  49.10900  57.11300 1.000 46.33000 ? 418 LYS B N   1 
ATOM   6745 C CA  . LYS B 1 418 ? 39.72200  49.50800  56.92800 1.000 46.33000 ? 418 LYS B CA  1 
ATOM   6746 C C   . LYS B 1 418 ? 40.50600  48.47500  56.12600 1.000 46.33000 ? 418 LYS B C   1 
ATOM   6747 O O   . LYS B 1 418 ? 41.46900  48.83300  55.43900 1.000 46.33000 ? 418 LYS B O   1 
ATOM   6748 C CB  . LYS B 1 418 ? 40.39000  49.76400  58.28000 1.000 46.33000 ? 418 LYS B CB  1 
ATOM   6749 C CG  . LYS B 1 418 ? 40.75700  48.51700  59.05600 1.000 46.33000 ? 418 LYS B CG  1 
ATOM   6750 C CD  . LYS B 1 418 ? 41.23000  48.86100  60.45700 1.000 46.33000 ? 418 LYS B CD  1 
ATOM   6751 C CE  . LYS B 1 418 ? 41.46700  47.60500  61.27600 1.000 46.33000 ? 418 LYS B CE  1 
ATOM   6752 N NZ  . LYS B 1 418 ? 41.80400  47.91700  62.69200 1.000 46.33000 ? 418 LYS B NZ  1 
ATOM   6753 N N   . PHE B 1 419 ? 40.10900  47.20000  56.18300 1.000 44.77000 ? 419 PHE B N   1 
ATOM   6754 C CA  . PHE B 1 419 ? 40.79200  46.14800  55.43700 1.000 44.77000 ? 419 PHE B CA  1 
ATOM   6755 C C   . PHE B 1 419 ? 39.83700  45.40300  54.51000 1.000 44.77000 ? 419 PHE B C   1 
ATOM   6756 O O   . PHE B 1 419 ? 40.01200  44.21000  54.25500 1.000 44.77000 ? 419 PHE B O   1 
ATOM   6757 C CB  . PHE B 1 419 ? 41.51200  45.17500  56.37400 1.000 44.77000 ? 419 PHE B CB  1 
ATOM   6758 C CG  . PHE B 1 419 ? 40.63500  44.56200  57.43600 1.000 44.77000 ? 419 PHE B CG  1 
ATOM   6759 C CD1 . PHE B 1 419 ? 39.85200  43.45100  57.16200 1.000 44.77000 ? 419 PHE B CD1 1 
ATOM   6760 C CD2 . PHE B 1 419 ? 40.62900  45.07200  58.72300 1.000 44.77000 ? 419 PHE B CD2 1 
ATOM   6761 C CE1 . PHE B 1 419 ? 39.06000  42.88200  58.14100 1.000 44.77000 ? 419 PHE B CE1 1 
ATOM   6762 C CE2 . PHE B 1 419 ? 39.84000  44.50600  59.70800 1.000 44.77000 ? 419 PHE B CE2 1 
ATOM   6763 C CZ  . PHE B 1 419 ? 39.05700  43.40800  59.41600 1.000 44.77000 ? 419 PHE B CZ  1 
ATOM   6764 N N   . LYS B 1 420 ? 38.83400  46.10400  53.98000 1.000 40.39000 ? 420 LYS B N   1 
ATOM   6765 C CA  . LYS B 1 420 ? 37.92400  45.48700  53.02400 1.000 40.39000 ? 420 LYS B CA  1 
ATOM   6766 C C   . LYS B 1 420 ? 38.64200  45.05200  51.75500 1.000 40.39000 ? 420 LYS B C   1 
ATOM   6767 O O   . LYS B 1 420 ? 38.15500  44.15900  51.05400 1.000 40.39000 ? 420 LYS B O   1 
ATOM   6768 C CB  . LYS B 1 420 ? 36.79500  46.45500  52.66900 1.000 40.39000 ? 420 LYS B CB  1 
ATOM   6769 C CG  . LYS B 1 420 ? 37.20000  47.53700  51.67400 1.000 40.39000 ? 420 LYS B CG  1 
ATOM   6770 C CD  . LYS B 1 420 ? 36.10600  48.57500  51.50900 1.000 40.39000 ? 420 LYS B CD  1 
ATOM   6771 C CE  . LYS B 1 420 ? 36.38700  49.52100  50.35400 1.000 40.39000 ? 420 LYS B CE  1 
ATOM   6772 N NZ  . LYS B 1 420 ? 35.31500  50.54800  50.21300 1.000 40.39000 ? 420 LYS B NZ  1 
ATOM   6773 N N   . ASP B 1 421 ? 39.78100  45.67200  51.44100 1.000 41.03000 ? 421 ASP B N   1 
ATOM   6774 C CA  . ASP B 1 421 ? 40.50300  45.33700  50.22000 1.000 41.03000 ? 421 ASP B CA  1 
ATOM   6775 C C   . ASP B 1 421 ? 41.03100  43.90800  50.24300 1.000 41.03000 ? 421 ASP B C   1 
ATOM   6776 O O   . ASP B 1 421 ? 41.20100  43.29600  49.18200 1.000 41.03000 ? 421 ASP B O   1 
ATOM   6777 C CB  . ASP B 1 421 ? 41.64800  46.32600  50.01400 1.000 41.03000 ? 421 ASP B CB  1 
ATOM   6778 C CG  . ASP B 1 421 ? 41.25600  47.74600  50.37300 1.000 41.03000 ? 421 ASP B CG  1 
ATOM   6779 O OD1 . ASP B 1 421 ? 40.14000  48.16800  50.00100 1.000 41.03000 ? 421 ASP B OD1 1 
ATOM   6780 O OD2 . ASP B 1 421 ? 42.05900  48.43400  51.03800 1.000 41.03000 ? 421 ASP B OD2 1 
ATOM   6781 N N   . VAL B 1 422 ? 41.29700  43.36400  51.42800 1.000 40.05000 ? 422 VAL B N   1 
ATOM   6782 C CA  . VAL B 1 422 ? 41.79500  42.00000  51.54900 1.000 40.05000 ? 422 VAL B CA  1 
ATOM   6783 C C   . VAL B 1 422 ? 40.82500  41.06900  52.26000 1.000 40.05000 ? 422 VAL B C   1 
ATOM   6784 O O   . VAL B 1 422 ? 40.91900  39.84400  52.07600 1.000 40.05000 ? 422 VAL B O   1 
ATOM   6785 C CB  . VAL B 1 422 ? 43.16500  41.97000  52.25900 1.000 40.05000 ? 422 VAL B CB  1 
ATOM   6786 C CG1 . VAL B 1 422 ? 44.17700  42.80600  51.49200 1.000 40.05000 ? 422 VAL B CG1 1 
ATOM   6787 C CG2 . VAL B 1 422 ? 43.03200  42.46300  53.69200 1.000 40.05000 ? 422 VAL B CG2 1 
ATOM   6788 N N   . ALA B 1 423 ? 39.88300  41.58500  53.06500 1.000 36.89000 ? 423 ALA B N   1 
ATOM   6789 C CA  . ALA B 1 423 ? 38.97500  40.75000  53.83800 1.000 36.89000 ? 423 ALA B CA  1 
ATOM   6790 C C   . ALA B 1 423 ? 37.59700  41.41500  53.90200 1.000 36.89000 ? 423 ALA B C   1 
ATOM   6791 O O   . ALA B 1 423 ? 37.17800  41.96400  54.92100 1.000 36.89000 ? 423 ALA B O   1 
ATOM   6792 C CB  . ALA B 1 423 ? 39.52700  40.48100  55.23900 1.000 36.89000 ? 423 ALA B CB  1 
ATOM   6793 N N   . SER B 1 424 ? 36.87500  41.37700  52.78500 1.000 33.75000 ? 424 SER B N   1 
ATOM   6794 C CA  . SER B 1 424 ? 35.46600  41.74900  52.79600 1.000 33.75000 ? 424 SER B CA  1 
ATOM   6795 C C   . SER B 1 424 ? 34.56100  40.56400  53.08800 1.000 33.75000 ? 424 SER B C   1 
ATOM   6796 O O   . SER B 1 424 ? 33.51400  40.73500  53.72400 1.000 33.75000 ? 424 SER B O   1 
ATOM   6797 C CB  . SER B 1 424 ? 35.06300  42.38500  51.46300 1.000 33.75000 ? 424 SER B CB  1 
ATOM   6798 O OG  . SER B 1 424 ? 35.63000  43.67600  51.33100 1.000 33.75000 ? 424 SER B OG  1 
ATOM   6799 N N   . GLY B 1 425 ? 34.94300  39.37400  52.64000 1.000 32.65000 ? 425 GLY B N   1 
ATOM   6800 C CA  . GLY B 1 425 ? 34.21600  38.14700  52.93200 1.000 32.65000 ? 425 GLY B CA  1 
ATOM   6801 C C   . GLY B 1 425 ? 34.98900  37.33100  53.95200 1.000 32.65000 ? 425 GLY B C   1 
ATOM   6802 O O   . GLY B 1 425 ? 36.21300  37.20500  53.86000 1.000 32.65000 ? 425 GLY B O   1 
ATOM   6803 N N   . LEU B 1 426 ? 34.26500  36.77500  54.91800 1.000 32.68000 ? 426 LEU B N   1 
ATOM   6804 C CA  . LEU B 1 426 ? 34.88900  36.08100  56.03200 1.000 32.68000 ? 426 LEU B CA  1 
ATOM   6805 C C   . LEU B 1 426 ? 34.16400  34.77600  56.32000 1.000 32.68000 ? 426 LEU B C   1 
ATOM   6806 O O   . LEU B 1 426 ? 32.93600  34.69500  56.20500 1.000 32.68000 ? 426 LEU B O   1 
ATOM   6807 C CB  . LEU B 1 426 ? 34.89600  36.95400  57.29700 1.000 32.68000 ? 426 LEU B CB  1 
ATOM   6808 C CG  . LEU B 1 426 ? 35.45200  36.31900  58.57600 1.000 32.68000 ? 426 LEU B CG  1 
ATOM   6809 C CD1 . LEU B 1 426 ? 36.96700  36.21500  58.52500 1.000 32.68000 ? 426 LEU B CD1 1 
ATOM   6810 C CD2 . LEU B 1 426 ? 35.00300  37.07900  59.81400 1.000 32.68000 ? 426 LEU B CD2 1 
ATOM   6811 N N   . ILE B 1 427 ? 34.94200  33.75900  56.68400 1.000 30.93000 ? 427 ILE B N   1 
ATOM   6812 C CA  . ILE B 1 427 ? 34.43700  32.52900  57.28100 1.000 30.93000 ? 427 ILE B CA  1 
ATOM   6813 C C   . ILE B 1 427 ? 35.16800  32.34000  58.60200 1.000 30.93000 ? 427 ILE B C   1 
ATOM   6814 O O   . ILE B 1 427 ? 36.38100  32.09600  58.61800 1.000 30.93000 ? 427 ILE B O   1 
ATOM   6815 C CB  . ILE B 1 427 ? 34.63100  31.30500  56.37700 1.000 30.93000 ? 427 ILE B CB  1 
ATOM   6816 C CG1 . ILE B 1 427 ? 33.74800  31.39600  55.13500 1.000 30.93000 ? 427 ILE B CG1 1 
ATOM   6817 C CG2 . ILE B 1 427 ? 34.31000  30.03200  57.14500 1.000 30.93000 ? 427 ILE B CG2 1 
ATOM   6818 C CD1 . ILE B 1 427 ? 33.69300  30.10300  54.34800 1.000 30.93000 ? 427 ILE B CD1 1 
ATOM   6819 N N   . ALA B 1 428 ? 34.43700  32.45800  59.70500 1.000 36.10000 ? 428 ALA B N   1 
ATOM   6820 C CA  . ALA B 1 428 ? 34.95600  32.18700  61.03700 1.000 36.10000 ? 428 ALA B CA  1 
ATOM   6821 C C   . ALA B 1 428 ? 34.62200  30.75100  61.41800 1.000 36.10000 ? 428 ALA B C   1 
ATOM   6822 O O   . ALA B 1 428 ? 33.44300  30.38900  61.51700 1.000 36.10000 ? 428 ALA B O   1 
ATOM   6823 C CB  . ALA B 1 428 ? 34.37300  33.16400  62.05700 1.000 36.10000 ? 428 ALA B CB  1 
ATOM   6824 N N   . LEU B 1 429 ? 35.65700  29.94000  61.63200 1.000 37.68000 ? 429 LEU B N   1 
ATOM   6825 C CA  . LEU B 1 429 ? 35.51100  28.54000  62.01600 1.000 37.68000 ? 429 LEU B CA  1 
ATOM   6826 C C   . LEU B 1 429 ? 35.88300  28.40700  63.48800 1.000 37.68000 ? 429 LEU B C   1 
ATOM   6827 O O   . LEU B 1 429 ? 37.06000  28.51500  63.84800 1.000 37.68000 ? 429 LEU B O   1 
ATOM   6828 C CB  . LEU B 1 429 ? 36.38200  27.64100  61.14200 1.000 37.68000 ? 429 LEU B CB  1 
ATOM   6829 C CG  . LEU B 1 429 ? 36.15800  26.13700  61.27900 1.000 37.68000 ? 429 LEU B CG  1 
ATOM   6830 C CD1 . LEU B 1 429 ? 34.74700  25.77900  60.84400 1.000 37.68000 ? 429 LEU B CD1 1 
ATOM   6831 C CD2 . LEU B 1 429 ? 37.19000  25.37100  60.46800 1.000 37.68000 ? 429 LEU B CD2 1 
ATOM   6832 N N   . SER B 1 430 ? 34.88200  28.17100  64.33300 1.000 43.08000 ? 430 SER B N   1 
ATOM   6833 C CA  . SER B 1 430 ? 35.08300  28.07800  65.77900 1.000 43.08000 ? 430 SER B CA  1 
ATOM   6834 C C   . SER B 1 430 ? 35.45400  26.64400  66.13300 1.000 43.08000 ? 430 SER B C   1 
ATOM   6835 O O   . SER B 1 430 ? 34.60300  25.82800  66.49200 1.000 43.08000 ? 430 SER B O   1 
ATOM   6836 C CB  . SER B 1 430 ? 33.83600  28.53600  66.52500 1.000 43.08000 ? 430 SER B CB  1 
ATOM   6837 O OG  . SER B 1 430 ? 33.51500  29.88000  66.21000 1.000 43.08000 ? 430 SER B OG  1 
ATOM   6838 N N   . ILE B 1 431 ? 36.74700  26.32700  66.02000 1.000 43.82000 ? 431 ILE B N   1 
ATOM   6839 C CA  . ILE B 1 431 ? 37.22400  25.01000  66.43400 1.000 43.82000 ? 431 ILE B CA  1 
ATOM   6840 C C   . ILE B 1 431 ? 37.05200  24.82700  67.93700 1.000 43.82000 ? 431 ILE B C   1 
ATOM   6841 O O   . ILE B 1 431 ? 36.71000  23.73600  68.41100 1.000 43.82000 ? 431 ILE B O   1 
ATOM   6842 C CB  . ILE B 1 431 ? 38.69100  24.82200  66.00500 1.000 43.82000 ? 431 ILE B CB  1 
ATOM   6843 C CG1 . ILE B 1 431 ? 38.78300  24.58900  64.49700 1.000 43.82000 ? 431 ILE B CG1 1 
ATOM   6844 C CG2 . ILE B 1 431 ? 39.34600  23.67700  66.76700 1.000 43.82000 ? 431 ILE B CG2 1 
ATOM   6845 C CD1 . ILE B 1 431 ? 40.18900  24.35300  64.01700 1.000 43.82000 ? 431 ILE B CD1 1 
ATOM   6846 N N   . SER B 1 432 ? 37.24100  25.89900  68.70600 1.000 48.00000 ? 432 SER B N   1 
ATOM   6847 C CA  . SER B 1 432 ? 37.10200  25.84000  70.16000 1.000 48.00000 ? 432 SER B CA  1 
ATOM   6848 C C   . SER B 1 432 ? 36.73700  27.24600  70.62800 1.000 48.00000 ? 432 SER B C   1 
ATOM   6849 O O   . SER B 1 432 ? 37.61200  28.10800  70.76400 1.000 48.00000 ? 432 SER B O   1 
ATOM   6850 C CB  . SER B 1 432 ? 38.37700  25.33800  70.82400 1.000 48.00000 ? 432 SER B CB  1 
ATOM   6851 O OG  . SER B 1 432 ? 38.15600  25.06300  72.19600 1.000 48.00000 ? 432 SER B OG  1 
ATOM   6852 N N   . LYS B 1 433 ? 35.43900  27.46400  70.85400 1.000 50.67000 ? 433 LYS B N   1 
ATOM   6853 C CA  . LYS B 1 433 ? 34.94600  28.78900  71.21400 1.000 50.67000 ? 433 LYS B CA  1 
ATOM   6854 C C   . LYS B 1 433 ? 35.47800  29.25400  72.56200 1.000 50.67000 ? 433 LYS B C   1 
ATOM   6855 O O   . LYS B 1 433 ? 35.66800  30.45900  72.77000 1.000 50.67000 ? 433 LYS B O   1 
ATOM   6856 C CB  . LYS B 1 433 ? 33.41800  28.78000  71.22600 1.000 50.67000 ? 433 LYS B CB  1 
ATOM   6857 C CG  . LYS B 1 433 ? 32.78200  29.39300  69.99800 1.000 50.67000 ? 433 LYS B CG  1 
ATOM   6858 C CD  . LYS B 1 433 ? 32.81700  30.90500  70.08500 1.000 50.67000 ? 433 LYS B CD  1 
ATOM   6859 C CE  . LYS B 1 433 ? 32.33000  31.53800  68.80200 1.000 50.67000 ? 433 LYS B CE  1 
ATOM   6860 N NZ  . LYS B 1 433 ? 30.95700  31.09300  68.44800 1.000 50.67000 ? 433 LYS B NZ  1 
ATOM   6861 N N   . THR B 1 434 ? 35.72600  28.32600  73.48700 1.000 52.61000 ? 434 THR B N   1 
ATOM   6862 C CA  . THR B 1 434 ? 36.09800  28.71300  74.84400 1.000 52.61000 ? 434 THR B CA  1 
ATOM   6863 C C   . THR B 1 434 ? 37.54700  29.18300  74.92600 1.000 52.61000 ? 434 THR B C   1 
ATOM   6864 O O   . THR B 1 434 ? 37.82100  30.28400  75.41600 1.000 52.61000 ? 434 THR B O   1 
ATOM   6865 C CB  . THR B 1 434 ? 35.86000  27.54500  75.80100 1.000 52.61000 ? 434 THR B CB  1 
ATOM   6866 O OG1 . THR B 1 434 ? 36.66400  26.42700  75.40300 1.000 52.61000 ? 434 THR B OG1 1 
ATOM   6867 C CG2 . THR B 1 434 ? 34.39400  27.13500  75.78400 1.000 52.61000 ? 434 THR B CG2 1 
ATOM   6868 N N   . GLN B 1 435 ? 38.48400  28.37200  74.43800 1.000 56.18000 ? 435 GLN B N   1 
ATOM   6869 C CA  . GLN B 1 435 ? 39.90100  28.71200  74.47400 1.000 56.18000 ? 435 GLN B CA  1 
ATOM   6870 C C   . GLN B 1 435 ? 40.35400  29.46300  73.23000 1.000 56.18000 ? 435 GLN B C   1 
ATOM   6871 O O   . GLN B 1 435 ? 41.55800  29.68400  73.06100 1.000 56.18000 ? 435 GLN B O   1 
ATOM   6872 C CB  . GLN B 1 435 ? 40.75000  27.45200  74.67100 1.000 56.18000 ? 435 GLN B CB  1 
ATOM   6873 C CG  . GLN B 1 435 ? 40.64500  26.42900  73.56000 1.000 56.18000 ? 435 GLN B CG  1 
ATOM   6874 C CD  . GLN B 1 435 ? 41.39200  25.15000  73.88400 1.000 56.18000 ? 435 GLN B CD  1 
ATOM   6875 O OE1 . GLN B 1 435 ? 42.23000  25.11800  74.78500 1.000 56.18000 ? 435 GLN B OE1 1 
ATOM   6876 N NE2 . GLN B 1 435 ? 41.08600  24.08500  73.15200 1.000 56.18000 ? 435 GLN B NE2 1 
ATOM   6877 N N   . ASN B 1 436 ? 39.41900  29.84000  72.35700 1.000 53.62000 ? 436 ASN B N   1 
ATOM   6878 C CA  . ASN B 1 436 ? 39.68900  30.67300  71.18700 1.000 53.62000 ? 436 ASN B CA  1 
ATOM   6879 C C   . ASN B 1 436 ? 40.66400  29.99500  70.22200 1.000 53.62000 ? 436 ASN B C   1 
ATOM   6880 O O   . ASN B 1 436 ? 41.73100  30.51800  69.89400 1.000 53.62000 ? 436 ASN B O   1 
ATOM   6881 C CB  . ASN B 1 436 ? 40.19800  32.05600  71.60800 1.000 53.62000 ? 436 ASN B CB  1 
ATOM   6882 C CG  . ASN B 1 436 ? 39.11100  32.91000  72.22700 1.000 53.62000 ? 436 ASN B CG  1 
ATOM   6883 O OD1 . ASN B 1 436 ? 38.49000  33.72900  71.55000 1.000 53.62000 ? 436 ASN B OD1 1 
ATOM   6884 N ND2 . ASN B 1 436 ? 38.86900  32.71800  73.51900 1.000 53.62000 ? 436 ASN B ND2 1 
ATOM   6885 N N   . LYS B 1 437 ? 40.27600  28.80200  69.77900 1.000 50.74000 ? 437 LYS B N   1 
ATOM   6886 C CA  . LYS B 1 437 ? 40.90900  28.14700  68.63900 1.000 50.74000 ? 437 LYS B CA  1 
ATOM   6887 C C   . LYS B 1 437 ? 40.01500  28.38200  67.42700 1.000 50.74000 ? 437 LYS B C   1 
ATOM   6888 O O   . LYS B 1 437 ? 38.89600  27.86300  67.36400 1.000 50.74000 ? 437 LYS B O   1 
ATOM   6889 C CB  . LYS B 1 437 ? 41.12100  26.65800  68.89900 1.000 50.74000 ? 437 LYS B CB  1 
ATOM   6890 C CG  . LYS B 1 437 ? 42.21500  26.35600  69.91300 1.000 50.74000 ? 437 LYS B CG  1 
ATOM   6891 C CD  . LYS B 1 437 ? 42.41600  24.85800  70.07900 1.000 50.74000 ? 437 LYS B CD  1 
ATOM   6892 C CE  . LYS B 1 437 ? 43.57900  24.55400  71.00900 1.000 50.74000 ? 437 LYS B CE  1 
ATOM   6893 N NZ  . LYS B 1 437 ? 43.74600  23.09100  71.22700 1.000 50.74000 ? 437 LYS B NZ  1 
ATOM   6894 N N   . TYR B 1 438 ? 40.50900  29.16300  66.46900 1.000 47.30000 ? 438 TYR B N   1 
ATOM   6895 C CA  . TYR B 1 438 ? 39.70900  29.61100  65.33900 1.000 47.30000 ? 438 TYR B CA  1 
ATOM   6896 C C   . TYR B 1 438 ? 40.44800  29.37500  64.03100 1.000 47.30000 ? 438 TYR B C   1 
ATOM   6897 O O   . TYR B 1 438 ? 41.67200  29.24200  63.99500 1.000 47.30000 ? 438 TYR B O   1 
ATOM   6898 C CB  . TYR B 1 438 ? 39.35600  31.10300  65.44300 1.000 47.30000 ? 438 TYR B CB  1 
ATOM   6899 C CG  . TYR B 1 438 ? 38.33200  31.44100  66.49900 1.000 47.30000 ? 438 TYR B CG  1 
ATOM   6900 C CD1 . TYR B 1 438 ? 37.03400  30.95800  66.41400 1.000 47.30000 ? 438 TYR B CD1 1 
ATOM   6901 C CD2 . TYR B 1 438 ? 38.65700  32.26500  67.56700 1.000 47.30000 ? 438 TYR B CD2 1 
ATOM   6902 C CE1 . TYR B 1 438 ? 36.09200  31.27200  67.37400 1.000 47.30000 ? 438 TYR B CE1 1 
ATOM   6903 C CE2 . TYR B 1 438 ? 37.72200  32.58500  68.53000 1.000 47.30000 ? 438 TYR B CE2 1 
ATOM   6904 C CZ  . TYR B 1 438 ? 36.44200  32.08600  68.42900 1.000 47.30000 ? 438 TYR B CZ  1 
ATOM   6905 O OH  . TYR B 1 438 ? 35.51100  32.40600  69.38900 1.000 47.30000 ? 438 TYR B OH  1 
ATOM   6906 N N   . VAL B 1 439 ? 39.67700  29.33200  62.94800 1.000 39.36000 ? 439 VAL B N   1 
ATOM   6907 C CA  . VAL B 1 439 ? 40.20600  29.34800  61.59000 1.000 39.36000 ? 439 VAL B CA  1 
ATOM   6908 C C   . VAL B 1 439 ? 39.38500  30.35400  60.79800 1.000 39.36000 ? 439 VAL B C   1 
ATOM   6909 O O   . VAL B 1 439 ? 38.15800  30.22400  60.71100 1.000 39.36000 ? 439 VAL B O   1 
ATOM   6910 C CB  . VAL B 1 439 ? 40.15200  27.96400  60.92400 1.000 39.36000 ? 439 VAL B CB  1 
ATOM   6911 C CG1 . VAL B 1 439 ? 40.60800  28.07000  59.48700 1.000 39.36000 ? 439 VAL B CG1 1 
ATOM   6912 C CG2 . VAL B 1 439 ? 41.01400  26.97200  61.68000 1.000 39.36000 ? 439 VAL B CG2 1 
ATOM   6913 N N   . LEU B 1 440 ? 40.04800  31.36000  60.23700 1.000 38.07000 ? 440 LEU B N   1 
ATOM   6914 C CA  . LEU B 1 440 ? 39.37700  32.40700  59.48300 1.000 38.07000 ? 440 LEU B CA  1 
ATOM   6915 C C   . LEU B 1 440 ? 39.83000  32.37600  58.03200 1.000 38.07000 ? 440 LEU B C   1 
ATOM   6916 O O   . LEU B 1 440 ? 41.02200  32.23000  57.74800 1.000 38.07000 ? 440 LEU B O   1 
ATOM   6917 C CB  . LEU B 1 440 ? 39.65400  33.79200  60.08100 1.000 38.07000 ? 440 LEU B CB  1 
ATOM   6918 C CG  . LEU B 1 440 ? 39.42200  33.99200  61.58100 1.000 38.07000 ? 440 LEU B CG  1 
ATOM   6919 C CD1 . LEU B 1 440 ? 39.34900  35.47000  61.90600 1.000 38.07000 ? 440 LEU B CD1 1 
ATOM   6920 C CD2 . LEU B 1 440 ? 38.16800  33.28600  62.06200 1.000 38.07000 ? 440 LEU B CD2 1 
ATOM   6921 N N   . TRP B 1 441 ? 38.87200  32.51300  57.12100 1.000 32.72000 ? 441 TRP B N   1 
ATOM   6922 C CA  . TRP B 1 441 ? 39.13500  32.68300  55.70100 1.000 32.72000 ? 441 TRP B CA  1 
ATOM   6923 C C   . TRP B 1 441 ? 38.76700  34.10100  55.27800 1.000 32.72000 ? 441 TRP B C   1 
ATOM   6924 O O   . TRP B 1 441 ? 37.88200  34.73000  55.86400 1.000 32.72000 ? 441 TRP B O   1 
ATOM   6925 C CB  . TRP B 1 441 ? 38.35300  31.66600  54.86700 1.000 32.72000 ? 441 TRP B CB  1 
ATOM   6926 C CG  . TRP B 1 441 ? 38.90800  30.27100  54.91400 1.000 32.72000 ? 441 TRP B CG  1 
ATOM   6927 C CD1 . TRP B 1 441 ? 39.85500  29.73800  54.08600 1.000 32.72000 ? 441 TRP B CD1 1 
ATOM   6928 C CD2 . TRP B 1 441 ? 38.53800  29.22600  55.82300 1.000 32.72000 ? 441 TRP B CD2 1 
ATOM   6929 N NE1 . TRP B 1 441 ? 40.09500  28.42900  54.42300 1.000 32.72000 ? 441 TRP B NE1 1 
ATOM   6930 C CE2 . TRP B 1 441 ? 39.30200  28.09100  55.48800 1.000 32.72000 ? 441 TRP B CE2 1 
ATOM   6931 C CE3 . TRP B 1 441 ? 37.63800  29.14200  56.88900 1.000 32.72000 ? 441 TRP B CE3 1 
ATOM   6932 C CZ2 . TRP B 1 441 ? 39.19200  26.88700  56.18100 1.000 32.72000 ? 441 TRP B CZ2 1 
ATOM   6933 C CZ3 . TRP B 1 441 ? 37.53100  27.94400  57.57600 1.000 32.72000 ? 441 TRP B CZ3 1 
ATOM   6934 C CH2 . TRP B 1 441 ? 38.30300  26.83400  57.21800 1.000 32.72000 ? 441 TRP B CH2 1 
ATOM   6935 N N   . PHE B 1 442 ? 39.45000  34.59800  54.24900 1.000 35.88000 ? 442 PHE B N   1 
ATOM   6936 C CA  . PHE B 1 442 ? 39.30800  35.98200  53.82100 1.000 35.88000 ? 442 PHE B CA  1 
ATOM   6937 C C   . PHE B 1 442 ? 39.21000  36.05500  52.30500 1.000 35.88000 ? 442 PHE B C   1 
ATOM   6938 O O   . PHE B 1 442 ? 39.96200  35.38100  51.59100 1.000 35.88000 ? 442 PHE B O   1 
ATOM   6939 C CB  . PHE B 1 442 ? 40.49600  36.84300  54.28300 1.000 35.88000 ? 442 PHE B CB  1 
ATOM   6940 C CG  . PHE B 1 442 ? 40.82100  36.71000  55.74600 1.000 35.88000 ? 442 PHE B CG  1 
ATOM   6941 C CD1 . PHE B 1 442 ? 40.01400  37.29700  56.70700 1.000 35.88000 ? 442 PHE B CD1 1 
ATOM   6942 C CD2 . PHE B 1 442 ? 41.94800  36.01600  56.15700 1.000 35.88000 ? 442 PHE B CD2 1 
ATOM   6943 C CE1 . PHE B 1 442 ? 40.31800  37.18400  58.05200 1.000 35.88000 ? 442 PHE B CE1 1 
ATOM   6944 C CE2 . PHE B 1 442 ? 42.25700  35.89800  57.50000 1.000 35.88000 ? 442 PHE B CE2 1 
ATOM   6945 C CZ  . PHE B 1 442 ? 41.43900  36.48300  58.44800 1.000 35.88000 ? 442 PHE B CZ  1 
ATOM   6946 N N   . ARG B 1 443 ? 38.29900  36.90700  51.82700 1.000 32.11000 ? 443 ARG B N   1 
ATOM   6947 C CA  . ARG B 1 443 ? 38.13000  37.22800  50.42100 1.000 32.11000 ? 443 ARG B CA  1 
ATOM   6948 C C   . ARG B 1 443 ? 38.16500  38.73800  50.23200 1.000 32.11000 ? 443 ARG B C   1 
ATOM   6949 O O   . ARG B 1 443 ? 37.64800  39.48600  51.07200 1.000 32.11000 ? 443 ARG B O   1 
ATOM   6950 C CB  . ARG B 1 443 ? 36.80000  36.67900  49.87900 1.000 32.11000 ? 443 ARG B CB  1 
ATOM   6951 C CG  . ARG B 1 443 ? 36.78800  35.19000  49.57800 1.000 32.11000 ? 443 ARG B CG  1 
ATOM   6952 C CD  . ARG B 1 443 ? 35.41800  34.76600  49.06700 1.000 32.11000 ? 443 ARG B CD  1 
ATOM   6953 N NE  . ARG B 1 443 ? 35.39400  33.38800  48.58800 1.000 32.11000 ? 443 ARG B NE  1 
ATOM   6954 C CZ  . ARG B 1 443 ? 34.30500  32.76800  48.15400 1.000 32.11000 ? 443 ARG B CZ  1 
ATOM   6955 N NH1 . ARG B 1 443 ? 33.12400  33.36600  48.14800 1.000 32.11000 ? 443 ARG B NH1 1 
ATOM   6956 N NH2 . ARG B 1 443 ? 34.40200  31.51600  47.71600 1.000 32.11000 ? 443 ARG B NH2 1 
ATOM   6957 N N   . PRO B 1 444 ? 38.75500  39.21300  49.13900 1.000 33.94000 ? 444 PRO B N   1 
ATOM   6958 C CA  . PRO B 1 444 ? 38.76200  40.64900  48.85700 1.000 33.94000 ? 444 PRO B CA  1 
ATOM   6959 C C   . PRO B 1 444 ? 37.39300  41.13600  48.41800 1.000 33.94000 ? 444 PRO B C   1 
ATOM   6960 O O   . PRO B 1 444 ? 36.54700  40.37100  47.95000 1.000 33.94000 ? 444 PRO B O   1 
ATOM   6961 C CB  . PRO B 1 444 ? 39.78100  40.77500  47.72500 1.000 33.94000 ? 444 PRO B CB  1 
ATOM   6962 C CG  . PRO B 1 444 ? 39.62500  39.49600  46.97900 1.000 33.94000 ? 444 PRO B CG  1 
ATOM   6963 C CD  . PRO B 1 444 ? 39.27700  38.43800  48.00300 1.000 33.94000 ? 444 PRO B CD  1 
ATOM   6964 N N   . GLU B 1 445 ? 37.18500  42.43900  48.57400 1.000 32.71000 ? 445 GLU B N   1 
ATOM   6965 C CA  . GLU B 1 445 ? 36.01200  43.06800  47.98900 1.000 32.71000 ? 445 GLU B CA  1 
ATOM   6966 C C   . GLU B 1 445 ? 36.03700  42.90900  46.47400 1.000 32.71000 ? 445 GLU B C   1 
ATOM   6967 O O   . GLU B 1 445 ? 37.07400  43.09500  45.83100 1.000 32.71000 ? 445 GLU B O   1 
ATOM   6968 C CB  . GLU B 1 445 ? 35.97300  44.55100  48.35500 1.000 32.71000 ? 445 GLU B CB  1 
ATOM   6969 C CG  . GLU B 1 445 ? 34.76300  45.29800  47.82400 1.000 32.71000 ? 445 GLU B CG  1 
ATOM   6970 C CD  . GLU B 1 445 ? 34.95700  46.79900  47.85400 1.000 32.71000 ? 445 GLU B CD  1 
ATOM   6971 O OE1 . GLU B 1 445 ? 35.82500  47.30300  47.10900 1.000 32.71000 ? 445 GLU B OE1 1 
ATOM   6972 O OE2 . GLU B 1 445 ? 34.25400  47.47400  48.63200 1.000 32.71000 ? 445 GLU B OE2 1 
ATOM   6973 N N   . GLU B 1 446 ? 34.88800  42.55500  45.90500 1.000 30.26000 ? 446 GLU B N   1 
ATOM   6974 C CA  . GLU B 1 446 ? 34.68500  42.56200  44.46000 1.000 30.26000 ? 446 GLU B CA  1 
ATOM   6975 C C   . GLU B 1 446 ? 33.57000  43.55300  44.15900 1.000 30.26000 ? 446 GLU B C   1 
ATOM   6976 O O   . GLU B 1 446 ? 32.39400  43.26400  44.40800 1.000 30.26000 ? 446 GLU B O   1 
ATOM   6977 C CB  . GLU B 1 446 ? 34.34400  41.17200  43.92600 1.000 30.26000 ? 446 GLU B CB  1 
ATOM   6978 C CG  . GLU B 1 446 ? 33.84500  41.19500  42.48700 1.000 30.26000 ? 446 GLU B CG  1 
ATOM   6979 C CD  . GLU B 1 446 ? 33.92100  39.84400  41.81200 1.000 30.26000 ? 446 GLU B CD  1 
ATOM   6980 O OE1 . GLU B 1 446 ? 34.87500  39.09000  42.09600 1.000 30.26000 ? 446 GLU B OE1 1 
ATOM   6981 O OE2 . GLU B 1 446 ? 33.02600  39.53700  40.99500 1.000 30.26000 ? 446 GLU B OE2 1 
ATOM   6982 N N   . VAL B 1 447 ? 33.94200  44.73100  43.65700 1.000 25.88000 ? 447 VAL B N   1 
ATOM   6983 C CA  . VAL B 1 447 ? 32.94800  45.74500  43.33200 1.000 25.88000 ? 447 VAL B CA  1 
ATOM   6984 C C   . VAL B 1 447 ? 32.10500  45.26300  42.16100 1.000 25.88000 ? 447 VAL B C   1 
ATOM   6985 O O   . VAL B 1 447 ? 32.63400  44.86200  41.11600 1.000 25.88000 ? 447 VAL B O   1 
ATOM   6986 C CB  . VAL B 1 447 ? 33.63000  47.08400  43.01600 1.000 25.88000 ? 447 VAL B CB  1 
ATOM   6987 C CG1 . VAL B 1 447 ? 32.62100  48.22100  43.08200 1.000 25.88000 ? 447 VAL B CG1 1 
ATOM   6988 C CG2 . VAL B 1 447 ? 34.79000  47.32500  43.97100 1.000 25.88000 ? 447 VAL B CG2 1 
ATOM   6989 N N   . GLN B 1 448 ? 30.78700  45.32500  42.32100 1.000 23.17000 ? 448 GLN B N   1 
ATOM   6990 C CA  . GLN B 1 448 ? 29.85200  44.92600  41.28200 1.000 23.17000 ? 448 GLN B CA  1 
ATOM   6991 C C   . GLN B 1 448 ? 29.11900  46.15200  40.75600 1.000 23.17000 ? 448 GLN B C   1 
ATOM   6992 O O   . GLN B 1 448 ? 28.85500  47.10400  41.49500 1.000 23.17000 ? 448 GLN B O   1 
ATOM   6993 C CB  . GLN B 1 448 ? 28.85200  43.88800  41.80700 1.000 23.17000 ? 448 GLN B CB  1 
ATOM   6994 C CG  . GLN B 1 448 ? 29.47500  42.52700  42.11000 1.000 23.17000 ? 448 GLN B CG  1 
ATOM   6995 C CD  . GLN B 1 448 ? 29.16500  42.03000  43.51300 1.000 23.17000 ? 448 GLN B CD  1 
ATOM   6996 O OE1 . GLN B 1 448 ? 28.11200  42.33400  44.07500 1.000 23.17000 ? 448 GLN B OE1 1 
ATOM   6997 N NE2 . GLN B 1 448 ? 30.08800  41.26500  44.08700 1.000 23.17000 ? 448 GLN B NE2 1 
ATOM   6998 N N   . THR B 1 449 ? 28.80000  46.12800  39.46700 1.000 14.88000 ? 449 THR B N   1 
ATOM   6999 C CA  . THR B 1 449 ? 28.09400  47.22200  38.81000 1.000 14.88000 ? 449 THR B CA  1 
ATOM   7000 C C   . THR B 1 449 ? 26.81400  46.63600  38.22800 1.000 14.88000 ? 449 THR B C   1 
ATOM   7001 O O   . THR B 1 449 ? 26.77800  46.22700  37.06500 1.000 14.88000 ? 449 THR B O   1 
ATOM   7002 C CB  . THR B 1 449 ? 28.95800  47.87500  37.73800 1.000 14.88000 ? 449 THR B CB  1 
ATOM   7003 O OG1 . THR B 1 449 ? 30.23600  48.20800  38.29500 1.000 14.88000 ? 449 THR B OG1 1 
ATOM   7004 C CG2 . THR B 1 449 ? 28.29300  49.14100  37.22200 1.000 14.88000 ? 449 THR B CG2 1 
ATOM   7005 N N   . VAL B 1 450 ? 25.76300  46.58900  39.04100 1.000 12.42000 ? 450 VAL B N   1 
ATOM   7006 C CA  . VAL B 1 450 ? 24.50900  45.97400  38.62400 1.000 12.42000 ? 450 VAL B CA  1 
ATOM   7007 C C   . VAL B 1 450 ? 23.74200  46.99300  37.78600 1.000 12.42000 ? 450 VAL B C   1 
ATOM   7008 O O   . VAL B 1 450 ? 23.22600  47.98100  38.31100 1.000 12.42000 ? 450 VAL B O   1 
ATOM   7009 C CB  . VAL B 1 450 ? 23.68400  45.50700  39.82700 1.000 12.42000 ? 450 VAL B CB  1 
ATOM   7010 C CG1 . VAL B 1 450 ? 22.66400  44.46900  39.39400 1.000 12.42000 ? 450 VAL B CG1 1 
ATOM   7011 C CG2 . VAL B 1 450 ? 24.59500  44.95200  40.91000 1.000 12.42000 ? 450 VAL B CG2 1 
ATOM   7012 N N   . ASN B 1 451 ? 23.67700  46.75900  36.47900 1.000 11.21000 ? 451 ASN B N   1 
ATOM   7013 C CA  . ASN B 1 451 ? 22.97000  47.65400  35.56600 1.000 11.21000 ? 451 ASN B CA  1 
ATOM   7014 C C   . ASN B 1 451 ? 21.49900  47.26700  35.56200 1.000 11.21000 ? 451 ASN B C   1 
ATOM   7015 O O   . ASN B 1 451 ? 21.10600  46.27700  34.94200 1.000 11.21000 ? 451 ASN B O   1 
ATOM   7016 C CB  . ASN B 1 451 ? 23.57000  47.57600  34.16800 1.000 11.21000 ? 451 ASN B CB  1 
ATOM   7017 C CG  . ASN B 1 451 ? 24.91700  48.26200  34.07500 1.000 11.21000 ? 451 ASN B CG  1 
ATOM   7018 O OD1 . ASN B 1 451 ? 25.03900  49.33300  33.48200 1.000 11.21000 ? 451 ASN B OD1 1 
ATOM   7019 N ND2 . ASN B 1 451 ? 25.93700  47.65200  34.66900 1.000 11.21000 ? 451 ASN B ND2 1 
ATOM   7020 N N   . TRP B 1 452 ? 20.68100  48.03700  36.27300 1.000 10.94000 ? 452 TRP B N   1 
ATOM   7021 C CA  . TRP B 1 452 ? 19.26100  47.74300  36.39600 1.000 10.94000 ? 452 TRP B CA  1 
ATOM   7022 C C   . TRP B 1 452 ? 18.45600  48.37900  35.27100 1.000 10.94000 ? 452 TRP B C   1 
ATOM   7023 O O   . TRP B 1 452 ? 18.76900  49.47900  34.80800 1.000 10.94000 ? 452 TRP B O   1 
ATOM   7024 C CB  . TRP B 1 452 ? 18.73700  48.22800  37.74600 1.000 10.94000 ? 452 TRP B CB  1 
ATOM   7025 C CG  . TRP B 1 452 ? 19.13300  47.33300  38.86600 1.000 10.94000 ? 452 TRP B CG  1 
ATOM   7026 C CD1 . TRP B 1 452 ? 20.30100  47.36400  39.57200 1.000 10.94000 ? 452 TRP B CD1 1 
ATOM   7027 C CD2 . TRP B 1 452 ? 18.36600  46.25300  39.40400 1.000 10.94000 ? 452 TRP B CD2 1 
ATOM   7028 N NE1 . TRP B 1 452 ? 20.30300  46.37300  40.52300 1.000 10.94000 ? 452 TRP B NE1 1 
ATOM   7029 C CE2 . TRP B 1 452 ? 19.12700  45.67500  40.44000 1.000 10.94000 ? 452 TRP B CE2 1 
ATOM   7030 C CE3 . TRP B 1 452 ? 17.10700  45.71800  39.11300 1.000 10.94000 ? 452 TRP B CE3 1 
ATOM   7031 C CZ2 . TRP B 1 452 ? 18.67100  44.59200  41.18500 1.000 10.94000 ? 452 TRP B CZ2 1 
ATOM   7032 C CZ3 . TRP B 1 452 ? 16.65600  44.64300  39.85400 1.000 10.94000 ? 452 TRP B CZ3 1 
ATOM   7033 C CH2 . TRP B 1 452 ? 17.43600  44.09100  40.87800 1.000 10.94000 ? 452 TRP B CH2 1 
ATOM   7034 N N   . GLY B 1 453 ? 17.41200  47.67200  34.83800 1.000 10.51000 ? 453 GLY B N   1 
ATOM   7035 C CA  . GLY B 1 453 ? 16.40000  48.25500  33.98100 1.000 10.51000 ? 453 GLY B CA  1 
ATOM   7036 C C   . GLY B 1 453 ? 15.33100  49.03100  34.71400 1.000 10.51000 ? 453 GLY B C   1 
ATOM   7037 O O   . GLY B 1 453 ? 14.49800  49.67500  34.07000 1.000 10.51000 ? 453 GLY B O   1 
ATOM   7038 N N   . GLY B 1 454 ? 15.33900  48.98300  36.04000 1.000 12.03000 ? 454 GLY B N   1 
ATOM   7039 C CA  . GLY B 1 454 ? 14.37900  49.72500  36.83800 1.000 12.03000 ? 454 GLY B CA  1 
ATOM   7040 C C   . GLY B 1 454 ? 14.65600  49.50900  38.31000 1.000 12.03000 ? 454 GLY B C   1 
ATOM   7041 O O   . GLY B 1 454 ? 15.43000  48.62800  38.70100 1.000 12.03000 ? 454 GLY B O   1 
ATOM   7042 N N   . ASN B 1 455 ? 14.00100  50.32900  39.12700 1.000 10.82000 ? 455 ASN B N   1 
ATOM   7043 C CA  . ASN B 1 455 ? 14.18200  50.27000  40.57400 1.000 10.82000 ? 455 ASN B CA  1 
ATOM   7044 C C   . ASN B 1 455 ? 13.53200  49.02200  41.16100 1.000 10.82000 ? 455 ASN B C   1 
ATOM   7045 O O   . ASN B 1 455 ? 14.14600  48.30600  41.95100 1.000 10.82000 ? 455 ASN B O   1 
ATOM   7046 C CB  . ASN B 1 455 ? 13.60900  51.52500  41.24000 1.000 10.82000 ? 455 ASN B CB  1 
ATOM   7047 C CG  . ASN B 1 455 ? 14.69100  52.48500  41.71000 1.000 10.82000 ? 455 ASN B CG  1 
ATOM   7048 O OD1 . ASN B 1 455 ? 15.75500  52.06600  42.16700 1.000 10.82000 ? 455 ASN B OD1 1 
ATOM   7049 N ND2 . ASN B 1 455 ? 14.41800  53.78200  41.60500 1.000 10.82000 ? 455 ASN B ND2 1 
ATOM   7050 N N   . GLU B 1 477 ? 14.32600  53.01900  32.84100 1.000 15.21000 ? 477 GLU B N   1 
ATOM   7051 C CA  . GLU B 1 477 ? 15.55700  52.99600  32.05900 1.000 15.21000 ? 477 GLU B CA  1 
ATOM   7052 C C   . GLU B 1 477 ? 16.73200  52.53800  32.91500 1.000 15.21000 ? 477 GLU B C   1 
ATOM   7053 O O   . GLU B 1 477 ? 16.54500  51.81800  33.89600 1.000 15.21000 ? 477 GLU B O   1 
ATOM   7054 C CB  . GLU B 1 477 ? 15.83900  54.37400  31.45800 1.000 15.21000 ? 477 GLU B CB  1 
ATOM   7055 C CG  . GLU B 1 477 ? 14.70500  54.93600  30.60300 1.000 15.21000 ? 477 GLU B CG  1 
ATOM   7056 C CD  . GLU B 1 477 ? 14.60200  54.28600  29.23000 1.000 15.21000 ? 477 GLU B CD  1 
ATOM   7057 O OE1 . GLU B 1 477 ? 14.45400  53.04800  29.15400 1.000 15.21000 ? 477 GLU B OE1 1 
ATOM   7058 O OE2 . GLU B 1 477 ? 14.67000  55.02200  28.22200 1.000 15.21000 ? 477 GLU B OE2 1 
ATOM   7059 N N   . LEU B 1 478 ? 17.93900  52.95400  32.53700 1.000 12.61000 ? 478 LEU B N   1 
ATOM   7060 C CA  . LEU B 1 478 ? 19.14000  52.49500  33.22100 1.000 12.61000 ? 478 LEU B CA  1 
ATOM   7061 C C   . LEU B 1 478 ? 19.16800  52.98700  34.66400 1.000 12.61000 ? 478 LEU B C   1 
ATOM   7062 O O   . LEU B 1 478 ? 18.75400  54.10900  34.96800 1.000 12.61000 ? 478 LEU B O   1 
ATOM   7063 C CB  . LEU B 1 478 ? 20.39000  52.96500  32.47800 1.000 12.61000 ? 478 LEU B CB  1 
ATOM   7064 C CG  . LEU B 1 478 ? 21.67100  52.19500  32.80500 1.000 12.61000 ? 478 LEU B CG  1 
ATOM   7065 C CD1 . LEU B 1 478 ? 21.44500  50.70400  32.62200 1.000 12.61000 ? 478 LEU B CD1 1 
ATOM   7066 C CD2 . LEU B 1 478 ? 22.82200  52.66900  31.93600 1.000 12.61000 ? 478 LEU B CD2 1 
ATOM   7067 N N   . TRP B 1 479 ? 19.66900  52.13600  35.55000 1.000 11.25000 ? 479 TRP B N   1 
ATOM   7068 C CA  . TRP B 1 479 ? 19.75200  52.41100  36.97600 1.000 11.25000 ? 479 TRP B CA  1 
ATOM   7069 C C   . TRP B 1 479 ? 20.99400  51.72100  37.53300 1.000 11.25000 ? 479 TRP B C   1 
ATOM   7070 O O   . TRP B 1 479 ? 20.91600  50.81200  38.35500 1.000 11.25000 ? 479 TRP B O   1 
ATOM   7071 C CB  . TRP B 1 479 ? 18.49100  51.93000  37.69100 1.000 11.25000 ? 479 TRP B CB  1 
ATOM   7072 C CG  . TRP B 1 479 ? 17.50000  52.99400  38.00000 1.000 11.25000 ? 479 TRP B CG  1 
ATOM   7073 C CD1 . TRP B 1 479 ? 16.26300  53.14600  37.44900 1.000 11.25000 ? 479 TRP B CD1 1 
ATOM   7074 C CD2 . TRP B 1 479 ? 17.65100  54.05500  38.94900 1.000 11.25000 ? 479 TRP B CD2 1 
ATOM   7075 N NE1 . TRP B 1 479 ? 15.63400  54.23800  37.99300 1.000 11.25000 ? 479 TRP B NE1 1 
ATOM   7076 C CE2 . TRP B 1 479 ? 16.46700  54.81400  38.91700 1.000 11.25000 ? 479 TRP B CE2 1 
ATOM   7077 C CE3 . TRP B 1 479 ? 18.67500  54.43700  39.82100 1.000 11.25000 ? 479 TRP B CE3 1 
ATOM   7078 C CZ2 . TRP B 1 479 ? 16.27700  55.93500  39.72100 1.000 11.25000 ? 479 TRP B CZ2 1 
ATOM   7079 C CZ3 . TRP B 1 479 ? 18.48400  55.55000  40.62000 1.000 11.25000 ? 479 TRP B CZ3 1 
ATOM   7080 C CH2 . TRP B 1 479 ? 17.29500  56.28500  40.56400 1.000 11.25000 ? 479 TRP B CH2 1 
ATOM   7081 N N   . LYS B 1 480 ? 22.17400  52.13300  37.07400 1.000 11.05000 ? 480 LYS B N   1 
ATOM   7082 C CA  . LYS B 1 480 ? 23.39300  51.46200  37.50100 1.000 11.05000 ? 480 LYS B CA  1 
ATOM   7083 C C   . LYS B 1 480 ? 23.55400  51.58200  39.01100 1.000 11.05000 ? 480 LYS B C   1 
ATOM   7084 O O   . LYS B 1 480 ? 23.45600  52.67700  39.57300 1.000 11.05000 ? 480 LYS B O   1 
ATOM   7085 C CB  . LYS B 1 480 ? 24.60200  52.06300  36.78400 1.000 11.05000 ? 480 LYS B CB  1 
ATOM   7086 C CG  . LYS B 1 480 ? 24.51400  51.98400  35.26600 1.000 11.05000 ? 480 LYS B CG  1 
ATOM   7087 C CD  . LYS B 1 480 ? 25.60600  52.80000  34.59600 1.000 11.05000 ? 480 LYS B CD  1 
ATOM   7088 C CE  . LYS B 1 480 ? 26.98800  52.33800  35.02100 1.000 11.05000 ? 480 LYS B CE  1 
ATOM   7089 N NZ  . LYS B 1 480 ? 28.05600  53.19700  34.43800 1.000 11.05000 ? 480 LYS B NZ  1 
ATOM   7090 N N   . GLU B 1 481 ? 23.83800  50.45800  39.66300 1.000 13.50000 ? 481 GLU B N   1 
ATOM   7091 C CA  . GLU B 1 481 ? 23.95000  50.38700  41.11300 1.000 13.50000 ? 481 GLU B CA  1 
ATOM   7092 C C   . GLU B 1 481 ? 25.31900  49.82600  41.45100 1.000 13.50000 ? 481 GLU B C   1 
ATOM   7093 O O   . GLU B 1 481 ? 25.64200  48.69600  41.06700 1.000 13.50000 ? 481 GLU B O   1 
ATOM   7094 C CB  . GLU B 1 481 ? 22.85200  49.50900  41.71800 1.000 13.50000 ? 481 GLU B CB  1 
ATOM   7095 C CG  . GLU B 1 481 ? 23.05500  49.20400  43.19800 1.000 13.50000 ? 481 GLU B CG  1 
ATOM   7096 C CD  . GLU B 1 481 ? 22.37900  47.91300  43.63200 1.000 13.50000 ? 481 GLU B CD  1 
ATOM   7097 O OE1 . GLU B 1 481 ? 21.97400  47.12700  42.75100 1.000 13.50000 ? 481 GLU B OE1 1 
ATOM   7098 O OE2 . GLU B 1 481 ? 22.25400  47.68100  44.85400 1.000 13.50000 ? 481 GLU B OE2 1 
ATOM   7099 N N   . ILE B 1 482 ? 26.12500  50.61800  42.14100 1.000 16.53000 ? 482 ILE B N   1 
ATOM   7100 C CA  . ILE B 1 482 ? 27.45200  50.19000  42.55000 1.000 16.53000 ? 482 ILE B CA  1 
ATOM   7101 C C   . ILE B 1 482 ? 27.33400  49.46500  43.88100 1.000 16.53000 ? 482 ILE B C   1 
ATOM   7102 O O   . ILE B 1 482 ? 26.75000  49.99000  44.83600 1.000 16.53000 ? 482 ILE B O   1 
ATOM   7103 C CB  . ILE B 1 482 ? 28.40900  51.38700  42.64900 1.000 16.53000 ? 482 ILE B CB  1 
ATOM   7104 C CG1 . ILE B 1 482 ? 28.30300  52.25100  41.38900 1.000 16.53000 ? 482 ILE B CG1 1 
ATOM   7105 C CG2 . ILE B 1 482 ? 29.83400  50.90700  42.84800 1.000 16.53000 ? 482 ILE B CG2 1 
ATOM   7106 C CD1 . ILE B 1 482 ? 28.58200  51.50200  40.09700 1.000 16.53000 ? 482 ILE B CD1 1 
ATOM   7107 N N   . VAL B 1 483 ? 27.88900  48.25900  43.94500 1.000 21.55000 ? 483 VAL B N   1 
ATOM   7108 C CA  . VAL B 1 483 ? 27.88900  47.44400  45.15100 1.000 21.55000 ? 483 VAL B CA  1 
ATOM   7109 C C   . VAL B 1 483 ? 29.33500  47.24600  45.57100 1.000 21.55000 ? 483 VAL B C   1 
ATOM   7110 O O   . VAL B 1 483 ? 30.14400  46.70400  44.80500 1.000 21.55000 ? 483 VAL B O   1 
ATOM   7111 C CB  . VAL B 1 483 ? 27.18700  46.09400  44.93400 1.000 21.55000 ? 483 VAL B CB  1 
ATOM   7112 C CG1 . VAL B 1 483 ? 27.51700  45.14000  46.06900 1.000 21.55000 ? 483 VAL B CG1 1 
ATOM   7113 C CG2 . VAL B 1 483 ? 25.68400  46.29400  44.82800 1.000 21.55000 ? 483 VAL B CG2 1 
ATOM   7114 N N   . ARG B 1 484 ? 29.66000  47.69400  46.78000 1.000 28.56000 ? 484 ARG B N   1 
ATOM   7115 C CA  . ARG B 1 484 ? 30.99700  47.53000  47.33000 1.000 28.56000 ? 484 ARG B CA  1 
ATOM   7116 C C   . ARG B 1 484 ? 30.89800  46.98600  48.74800 1.000 28.56000 ? 484 ARG B C   1 
ATOM   7117 O O   . ARG B 1 484 ? 29.80300  46.64700  49.20800 1.000 28.56000 ? 484 ARG B O   1 
ATOM   7118 C CB  . ARG B 1 484 ? 31.76100  48.85400  47.30200 1.000 28.56000 ? 484 ARG B CB  1 
ATOM   7119 C CG  . ARG B 1 484 ? 31.05600  50.00700  47.99500 1.000 28.56000 ? 484 ARG B CG  1 
ATOM   7120 C CD  . ARG B 1 484 ? 31.97100  51.21900  48.09300 1.000 28.56000 ? 484 ARG B CD  1 
ATOM   7121 N NE  . ARG B 1 484 ? 32.62800  51.50600  46.82300 1.000 28.56000 ? 484 ARG B NE  1 
ATOM   7122 C CZ  . ARG B 1 484 ? 32.15700  52.33900  45.90400 1.000 28.56000 ? 484 ARG B CZ  1 
ATOM   7123 N NH1 . ARG B 1 484 ? 31.02600  53.00000  46.08500 1.000 28.56000 ? 484 ARG B NH1 1 
ATOM   7124 N NH2 . ARG B 1 484 ? 32.84000  52.51200  44.77600 1.000 28.56000 ? 484 ARG B NH2 1 
ATOM   7125 N N   . LEU B 1 485 ? 32.03500  46.89000  49.43900 1.000 32.35000 ? 485 LEU B N   1 
ATOM   7126 C CA  . LEU B 1 485 ? 32.12300  46.30700  50.77700 1.000 32.35000 ? 485 LEU B CA  1 
ATOM   7127 C C   . LEU B 1 485 ? 31.62100  44.87000  50.81200 1.000 32.35000 ? 485 LEU B C   1 
ATOM   7128 O O   . LEU B 1 485 ? 31.25100  44.36700  51.87600 1.000 32.35000 ? 485 LEU B O   1 
ATOM   7129 C CB  . LEU B 1 485 ? 31.34600  47.14500  51.80300 1.000 32.35000 ? 485 LEU B CB  1 
ATOM   7130 C CG  . LEU B 1 485 ? 31.76000  48.59100  52.05900 1.000 32.35000 ? 485 LEU B CG  1 
ATOM   7131 C CD1 . LEU B 1 485 ? 30.61000  49.36000  52.68500 1.000 32.35000 ? 485 LEU B CD1 1 
ATOM   7132 C CD2 . LEU B 1 485 ? 32.96200  48.62100  52.97100 1.000 32.35000 ? 485 LEU B CD2 1 
ATOM   7133 N N   . LYS B 1 486 ? 31.62400  44.18400  49.67100 1.000 27.98000 ? 486 LYS B N   1 
ATOM   7134 C CA  . LYS B 1 486 ? 31.03100  42.85700  49.56100 1.000 27.98000 ? 486 LYS B CA  1 
ATOM   7135 C C   . LYS B 1 486 ? 31.89500  42.00600  48.64700 1.000 27.98000 ? 486 LYS B C   1 
ATOM   7136 O O   . LYS B 1 486 ? 32.15200  42.38800  47.50100 1.000 27.98000 ? 486 LYS B O   1 
ATOM   7137 C CB  . LYS B 1 486 ? 29.59600  42.93400  49.02700 1.000 27.98000 ? 486 LYS B CB  1 
ATOM   7138 C CG  . LYS B 1 486 ? 28.97800  41.57900  48.72300 1.000 27.98000 ? 486 LYS B CG  1 
ATOM   7139 C CD  . LYS B 1 486 ? 27.60600  41.71100  48.07500 1.000 27.98000 ? 486 LYS B CD  1 
ATOM   7140 C CE  . LYS B 1 486 ? 26.57600  42.26200  49.04800 1.000 27.98000 ? 486 LYS B CE  1 
ATOM   7141 N NZ  . LYS B 1 486 ? 25.19700  42.19800  48.48600 1.000 27.98000 ? 486 LYS B NZ  1 
ATOM   7142 N N   . SER B 1 487 ? 32.33300  40.85600  49.15100 1.000 28.57000 ? 487 SER B N   1 
ATOM   7143 C CA  . SER B 1 487 ? 33.14400  39.93000  48.37900 1.000 28.57000 ? 487 SER B CA  1 
ATOM   7144 C C   . SER B 1 487 ? 32.25100  39.05200  47.50700 1.000 28.57000 ? 487 SER B C   1 
ATOM   7145 O O   . SER B 1 487 ? 31.02900  39.21400  47.45400 1.000 28.57000 ? 487 SER B O   1 
ATOM   7146 C CB  . SER B 1 487 ? 33.99700  39.07000  49.30500 1.000 28.57000 ? 487 SER B CB  1 
ATOM   7147 O OG  . SER B 1 487 ? 33.20600  38.06500  49.91400 1.000 28.57000 ? 487 SER B OG  1 
ATOM   7148 N N   . LEU B 1 488 ? 32.87100  38.10500  46.81200 1.000 26.90000 ? 488 LEU B N   1 
ATOM   7149 C CA  . LEU B 1 488 ? 32.10000  37.12500  46.07000 1.000 26.90000 ? 488 LEU B CA  1 
ATOM   7150 C C   . LEU B 1 488 ? 31.31900  36.24400  47.04000 1.000 26.90000 ? 488 LEU B C   1 
ATOM   7151 O O   . LEU B 1 488 ? 31.81800  35.92100  48.12300 1.000 26.90000 ? 488 LEU B O   1 
ATOM   7152 C CB  . LEU B 1 488 ? 33.01200  36.26300  45.20100 1.000 26.90000 ? 488 LEU B CB  1 
ATOM   7153 C CG  . LEU B 1 488 ? 33.38700  36.84800  43.84200 1.000 26.90000 ? 488 LEU B CG  1 
ATOM   7154 C CD1 . LEU B 1 488 ? 34.32100  35.91200  43.09400 1.000 26.90000 ? 488 LEU B CD1 1 
ATOM   7155 C CD2 . LEU B 1 488 ? 32.13400  37.12100  43.02900 1.000 26.90000 ? 488 LEU B CD2 1 
ATOM   7156 N N   . PRO B 1 489 ? 30.09100  35.85900  46.69500 1.000 27.51000 ? 489 PRO B N   1 
ATOM   7157 C CA  . PRO B 1 489 ? 29.28100  35.06700  47.62900 1.000 27.51000 ? 489 PRO B CA  1 
ATOM   7158 C C   . PRO B 1 489 ? 29.93400  33.72400  47.91900 1.000 27.51000 ? 489 PRO B C   1 
ATOM   7159 O O   . PRO B 1 489 ? 30.56700  33.11900  47.05400 1.000 27.51000 ? 489 PRO B O   1 
ATOM   7160 C CB  . PRO B 1 489 ? 27.94800  34.90000  46.89000 1.000 27.51000 ? 489 PRO B CB  1 
ATOM   7161 C CG  . PRO B 1 489 ? 27.93600  35.99000  45.85400 1.000 27.51000 ? 489 PRO B CG  1 
ATOM   7162 C CD  . PRO B 1 489 ? 29.36400  36.17500  45.45600 1.000 27.51000 ? 489 PRO B CD  1 
ATOM   7163 N N   . TRP B 1 490 ? 29.77600  33.26200  49.15700 1.000 27.76000 ? 490 TRP B N   1 
ATOM   7164 C CA  . TRP B 1 490 ? 30.29100  31.95500  49.54500 1.000 27.76000 ? 490 TRP B CA  1 
ATOM   7165 C C   . TRP B 1 490 ? 29.36800  30.87200  49.00200 1.000 27.76000 ? 490 TRP B C   1 
ATOM   7166 O O   . TRP B 1 490 ? 28.16000  30.89500  49.26100 1.000 27.76000 ? 490 TRP B O   1 
ATOM   7167 C CB  . TRP B 1 490 ? 30.40100  31.84800  51.06600 1.000 27.76000 ? 490 TRP B CB  1 
ATOM   7168 C CG  . TRP B 1 490 ? 31.35200  32.82200  51.68500 1.000 27.76000 ? 490 TRP B CG  1 
ATOM   7169 C CD1 . TRP B 1 490 ? 31.03600  33.99000  52.31600 1.000 27.76000 ? 490 TRP B CD1 1 
ATOM   7170 C CD2 . TRP B 1 490 ? 32.77800  32.71100  51.73700 1.000 27.76000 ? 490 TRP B CD2 1 
ATOM   7171 N NE1 . TRP B 1 490 ? 32.17700  34.61300  52.75700 1.000 27.76000 ? 490 TRP B NE1 1 
ATOM   7172 C CE2 . TRP B 1 490 ? 33.26100  33.84800  52.41400 1.000 27.76000 ? 490 TRP B CE2 1 
ATOM   7173 C CE3 . TRP B 1 490 ? 33.69400  31.76100  51.27600 1.000 27.76000 ? 490 TRP B CE3 1 
ATOM   7174 C CZ2 . TRP B 1 490 ? 34.61800  34.06100  52.64100 1.000 27.76000 ? 490 TRP B CZ2 1 
ATOM   7175 C CZ3 . TRP B 1 490 ? 35.04100  31.97300  51.50300 1.000 27.76000 ? 490 TRP B CZ3 1 
ATOM   7176 C CH2 . TRP B 1 490 ? 35.49000  33.11400  52.18000 1.000 27.76000 ? 490 TRP B CH2 1 
ATOM   7177 N N   . LYS B 1 491 ? 29.92800  29.93000  48.24700 1.000 28.20000 ? 491 LYS B N   1 
ATOM   7178 C CA  . LYS B 1 491 ? 29.15900  28.76500  47.83500 1.000 28.20000 ? 491 LYS B CA  1 
ATOM   7179 C C   . LYS B 1 491 ? 28.93000  27.83600  49.02300 1.000 28.20000 ? 491 LYS B C   1 
ATOM   7180 O O   . LYS B 1 491 ? 29.76400  27.72900  49.92600 1.000 28.20000 ? 491 LYS B O   1 
ATOM   7181 C CB  . LYS B 1 491 ? 29.86500  28.02300  46.70000 1.000 28.20000 ? 491 LYS B CB  1 
ATOM   7182 C CG  . LYS B 1 491 ? 29.67200  28.65800  45.32900 1.000 28.20000 ? 491 LYS B CG  1 
ATOM   7183 C CD  . LYS B 1 491 ? 28.21000  29.01900  45.09900 1.000 28.20000 ? 491 LYS B CD  1 
ATOM   7184 C CE  . LYS B 1 491 ? 27.80900  28.86700  43.63900 1.000 28.20000 ? 491 LYS B CE  1 
ATOM   7185 N NZ  . LYS B 1 491 ? 27.72700  27.43600  43.22900 1.000 28.20000 ? 491 LYS B NZ  1 
ATOM   7186 N N   . SER B 1 492 ? 27.77300  27.16600  49.02100 1.000 27.97000 ? 492 SER B N   1 
ATOM   7187 C CA  . SER B 1 492 ? 27.38000  26.37200  50.18300 1.000 27.97000 ? 492 SER B CA  1 
ATOM   7188 C C   . SER B 1 492 ? 28.34400  25.21700  50.43100 1.000 27.97000 ? 492 SER B C   1 
ATOM   7189 O O   . SER B 1 492 ? 28.63700  24.88000  51.58600 1.000 27.97000 ? 492 SER B O   1 
ATOM   7190 C CB  . SER B 1 492 ? 25.95500  25.84800  49.99900 1.000 27.97000 ? 492 SER B CB  1 
ATOM   7191 O OG  . SER B 1 492 ? 25.85400  25.02600  48.84800 1.000 27.97000 ? 492 SER B OG  1 
ATOM   7192 N N   . TYR B 1 493 ? 28.86800  24.61000  49.36200 1.000 29.65000 ? 493 TYR B N   1 
ATOM   7193 C CA  . TYR B 1 493 ? 29.80700  23.51300  49.55900 1.000 29.65000 ? 493 TYR B CA  1 
ATOM   7194 C C   . TYR B 1 493 ? 31.13000  23.99000  50.14100 1.000 29.65000 ? 493 TYR B C   1 
ATOM   7195 O O   . TYR B 1 493 ? 31.81300  23.20700  50.80500 1.000 29.65000 ? 493 TYR B O   1 
ATOM   7196 C CB  . TYR B 1 493 ? 30.03200  22.73700  48.25500 1.000 29.65000 ? 493 TYR B CB  1 
ATOM   7197 C CG  . TYR B 1 493 ? 30.27800  23.56200  47.01000 1.000 29.65000 ? 493 TYR B CG  1 
ATOM   7198 C CD1 . TYR B 1 493 ? 31.54000  24.06900  46.72400 1.000 29.65000 ? 493 TYR B CD1 1 
ATOM   7199 C CD2 . TYR B 1 493 ? 29.25600  23.79700  46.09800 1.000 29.65000 ? 493 TYR B CD2 1 
ATOM   7200 C CE1 . TYR B 1 493 ? 31.77200  24.81000  45.57700 1.000 29.65000 ? 493 TYR B CE1 1 
ATOM   7201 C CE2 . TYR B 1 493 ? 29.47700  24.53600  44.94800 1.000 29.65000 ? 493 TYR B CE2 1 
ATOM   7202 C CZ  . TYR B 1 493 ? 30.73700  25.03900  44.69300 1.000 29.65000 ? 493 TYR B CZ  1 
ATOM   7203 O OH  . TYR B 1 493 ? 30.96100  25.77500  43.55000 1.000 29.65000 ? 493 TYR B OH  1 
ATOM   7204 N N   . GLU B 1 494 ? 31.49300  25.25800  49.94300 1.000 28.90000 ? 494 GLU B N   1 
ATOM   7205 C CA  . GLU B 1 494 ? 32.69700  25.77700  50.58500 1.000 28.90000 ? 494 GLU B CA  1 
ATOM   7206 C C   . GLU B 1 494 ? 32.52000  25.87700  52.09800 1.000 28.90000 ? 494 GLU B C   1 
ATOM   7207 O O   . GLU B 1 494 ? 33.42000  25.50300  52.86200 1.000 28.90000 ? 494 GLU B O   1 
ATOM   7208 C CB  . GLU B 1 494 ? 33.06000  27.13200  49.98000 1.000 28.90000 ? 494 GLU B CB  1 
ATOM   7209 C CG  . GLU B 1 494 ? 33.29600  27.07600  48.47400 1.000 28.90000 ? 494 GLU B CG  1 
ATOM   7210 C CD  . GLU B 1 494 ? 33.25800  28.44200  47.81500 1.000 28.90000 ? 494 GLU B CD  1 
ATOM   7211 O OE1 . GLU B 1 494 ? 33.25100  29.45600  48.54200 1.000 28.90000 ? 494 GLU B OE1 1 
ATOM   7212 O OE2 . GLU B 1 494 ? 33.22900  28.50000  46.56700 1.000 28.90000 ? 494 GLU B OE2 1 
ATOM   7213 N N   . VAL B 1 495 ? 31.36100  26.36100  52.55400 1.000 29.66000 ? 495 VAL B N   1 
ATOM   7214 C CA  . VAL B 1 495 ? 31.08600  26.39200  53.98800 1.000 29.66000 ? 495 VAL B CA  1 
ATOM   7215 C C   . VAL B 1 495 ? 30.99300  24.97500  54.54700 1.000 29.66000 ? 495 VAL B C   1 
ATOM   7216 O O   . VAL B 1 495 ? 31.42800  24.70100  55.67800 1.000 29.66000 ? 495 VAL B O   1 
ATOM   7217 C CB  . VAL B 1 495 ? 29.80300  27.20000  54.25700 1.000 29.66000 ? 495 VAL B CB  1 
ATOM   7218 C CG1 . VAL B 1 495 ? 29.51500  27.28200  55.74700 1.000 29.66000 ? 495 VAL B CG1 1 
ATOM   7219 C CG2 . VAL B 1 495 ? 29.92300  28.59100  53.65400 1.000 29.66000 ? 495 VAL B CG2 1 
ATOM   7220 N N   . ASN B 1 496 ? 30.45200  24.04400  53.75400 1.000 31.12000 ? 496 ASN B N   1 
ATOM   7221 C CA  . ASN B 1 496 ? 30.42500  22.65000  54.18400 1.000 31.12000 ? 496 ASN B CA  1 
ATOM   7222 C C   . ASN B 1 496 ? 31.83400  22.10100  54.33800 1.000 31.12000 ? 496 ASN B C   1 
ATOM   7223 O O   . ASN B 1 496 ? 32.12900  21.38400  55.30200 1.000 31.12000 ? 496 ASN B O   1 
ATOM   7224 C CB  . ASN B 1 496 ? 29.63600  21.80500  53.18500 1.000 31.12000 ? 496 ASN B CB  1 
ATOM   7225 C CG  . ASN B 1 496 ? 28.14300  22.01000  53.30100 1.000 31.12000 ? 496 ASN B CG  1 
ATOM   7226 O OD1 . ASN B 1 496 ? 27.62500  22.26600  54.38800 1.000 31.12000 ? 496 ASN B OD1 1 
ATOM   7227 N ND2 . ASN B 1 496 ? 27.44000  21.89500  52.18100 1.000 31.12000 ? 496 ASN B ND2 1 
ATOM   7228 N N   . ALA B 1 497 ? 32.72200  22.43800  53.40200 1.000 30.31000 ? 497 ALA B N   1 
ATOM   7229 C CA  . ALA B 1 497 ? 34.10800  22.00700  53.50700 1.000 30.31000 ? 497 ALA B CA  1 
ATOM   7230 C C   . ALA B 1 497 ? 34.79400  22.62900  54.71200 1.000 30.31000 ? 497 ALA B C   1 
ATOM   7231 O O   . ALA B 1 497 ? 35.63300  21.98300  55.34200 1.000 30.31000 ? 497 ALA B O   1 
ATOM   7232 C CB  . ALA B 1 497 ? 34.86100  22.35200  52.22300 1.000 30.31000 ? 497 ALA B CB  1 
ATOM   7233 N N   . ALA B 1 498 ? 34.43200  23.86200  55.06900 1.000 30.82000 ? 498 ALA B N   1 
ATOM   7234 C CA  . ALA B 1 498 ? 35.02200  24.47100  56.25900 1.000 30.82000 ? 498 ALA B CA  1 
ATOM   7235 C C   . ALA B 1 498 ? 34.58000  23.74900  57.52900 1.000 30.82000 ? 498 ALA B C   1 
ATOM   7236 O O   . ALA B 1 498 ? 35.40000  23.47800  58.41900 1.000 30.82000 ? 498 ALA B O   1 
ATOM   7237 C CB  . ALA B 1 498 ? 34.66000  25.95500  56.32500 1.000 30.82000 ? 498 ALA B CB  1 
ATOM   7238 N N   . ALA B 1 499 ? 33.29300  23.40400  57.62400 1.000 32.59000 ? 499 ALA B N   1 
ATOM   7239 C CA  . ALA B 1 499 ? 32.83000  22.68000  58.80800 1.000 32.59000 ? 499 ALA B CA  1 
ATOM   7240 C C   . ALA B 1 499 ? 33.43100  21.27700  58.87600 1.000 32.59000 ? 499 ALA B C   1 
ATOM   7241 O O   . ALA B 1 499 ? 33.82300  20.80400  59.95600 1.000 32.59000 ? 499 ALA B O   1 
ATOM   7242 C CB  . ALA B 1 499 ? 31.30400  22.61600  58.82300 1.000 32.59000 ? 499 ALA B CB  1 
ATOM   7243 N N   . GLU B 1 500 ? 33.53500  20.60200  57.72800 1.000 33.62000 ? 500 GLU B N   1 
ATOM   7244 C CA  . GLU B 1 500 ? 34.18200  19.29600  57.70700 1.000 33.62000 ? 500 GLU B CA  1 
ATOM   7245 C C   . GLU B 1 500 ? 35.66000  19.40500  58.05700 1.000 33.62000 ? 500 GLU B C   1 
ATOM   7246 O O   . GLU B 1 500 ? 36.21900  18.48900  58.67100 1.000 33.62000 ? 500 GLU B O   1 
ATOM   7247 C CB  . GLU B 1 500 ? 33.99700  18.63900  56.33900 1.000 33.62000 ? 500 GLU B CB  1 
ATOM   7248 C CG  . GLU B 1 500 ? 32.54600  18.34500  55.98500 1.000 33.62000 ? 500 GLU B CG  1 
ATOM   7249 C CD  . GLU B 1 500 ? 32.37500  17.84100  54.56200 1.000 33.62000 ? 500 GLU B CD  1 
ATOM   7250 O OE1 . GLU B 1 500 ? 33.33500  17.26400  54.01100 1.000 33.62000 ? 500 GLU B OE1 1 
ATOM   7251 O OE2 . GLU B 1 500 ? 31.27900  18.02700  53.99200 1.000 33.62000 ? 500 GLU B OE2 1 
ATOM   7252 N N   . LEU B 1 501 ? 36.30700  20.51300  57.68400 1.000 32.54000 ? 501 LEU B N   1 
ATOM   7253 C CA  . LEU B 1 501 ? 37.68500  20.72800  58.10400 1.000 32.54000 ? 501 LEU B CA  1 
ATOM   7254 C C   . LEU B 1 501 ? 37.77400  20.89900  59.60900 1.000 32.54000 ? 501 LEU B C   1 
ATOM   7255 O O   . LEU B 1 501 ? 38.71900  20.41100  60.23300 1.000 32.54000 ? 501 LEU B O   1 
ATOM   7256 C CB  . LEU B 1 501 ? 38.27300  21.94900  57.40200 1.000 32.54000 ? 501 LEU B CB  1 
ATOM   7257 C CG  . LEU B 1 501 ? 39.73500  22.24600  57.74400 1.000 32.54000 ? 501 LEU B CG  1 
ATOM   7258 C CD1 . LEU B 1 501 ? 40.65900  21.18100  57.16800 1.000 32.54000 ? 501 LEU B CD1 1 
ATOM   7259 C CD2 . LEU B 1 501 ? 40.13000  23.62600  57.25800 1.000 32.54000 ? 501 LEU B CD2 1 
ATOM   7260 N N   . ARG B 1 502 ? 36.78800  21.56500  60.21500 1.000 34.72000 ? 502 ARG B N   1 
ATOM   7261 C CA  . ARG B 1 502 ? 36.78600  21.67000  61.67200 1.000 34.72000 ? 502 ARG B CA  1 
ATOM   7262 C C   . ARG B 1 502 ? 36.68300  20.29500  62.31600 1.000 34.72000 ? 502 ARG B C   1 
ATOM   7263 O O   . ARG B 1 502 ? 37.41400  19.98100  63.26800 1.000 34.72000 ? 502 ARG B O   1 
ATOM   7264 C CB  . ARG B 1 502 ? 35.63300  22.55000  62.15100 1.000 34.72000 ? 502 ARG B CB  1 
ATOM   7265 C CG  . ARG B 1 502 ? 35.47000  22.54400  63.66500 1.000 34.72000 ? 502 ARG B CG  1 
ATOM   7266 C CD  . ARG B 1 502 ? 34.20500  23.25300  64.11100 1.000 34.72000 ? 502 ARG B CD  1 
ATOM   7267 N NE  . ARG B 1 502 ? 34.19300  23.46200  65.55400 1.000 34.72000 ? 502 ARG B NE  1 
ATOM   7268 C CZ  . ARG B 1 502 ? 33.71200  22.59500  66.43400 1.000 34.72000 ? 502 ARG B CZ  1 
ATOM   7269 N NH1 . ARG B 1 502 ? 33.18000  21.44600  66.05300 1.000 34.72000 ? 502 ARG B NH1 1 
ATOM   7270 N NH2 . ARG B 1 502 ? 33.76600  22.88900  67.73000 1.000 34.72000 ? 502 ARG B NH2 1 
ATOM   7271 N N   . GLY B 1 503 ? 35.80600  19.44500  61.78000 1.000 33.25000 ? 503 GLY B N   1 
ATOM   7272 C CA  . GLY B 1 503 ? 35.65000  18.12000  62.35900 1.000 33.25000 ? 503 GLY B CA  1 
ATOM   7273 C C   . GLY B 1 503 ? 36.88700  17.25700  62.18500 1.000 33.25000 ? 503 GLY B C   1 
ATOM   7274 O O   . GLY B 1 503 ? 37.32000  16.57500  63.12200 1.000 33.25000 ? 503 GLY B O   1 
ATOM   7275 N N   . ALA B 1 504 ? 37.49700  17.30300  60.99600 1.000 32.99000 ? 504 ALA B N   1 
ATOM   7276 C CA  . ALA B 1 504 ? 38.72000  16.54300  60.76900 1.000 32.99000 ? 504 ALA B CA  1 
ATOM   7277 C C   . ALA B 1 504 ? 39.87800  17.07300  61.60200 1.000 32.99000 ? 504 ALA B C   1 
ATOM   7278 O O   . ALA B 1 504 ? 40.72100  16.29100  62.06000 1.000 32.99000 ? 504 ALA B O   1 
ATOM   7279 C CB  . ALA B 1 504 ? 39.08100  16.56900  59.28500 1.000 32.99000 ? 504 ALA B CB  1 
ATOM   7280 N N   . ILE B 1 505 ? 39.92400  18.38700  61.83400 1.000 33.92000 ? 505 ILE B N   1 
ATOM   7281 C CA  . ILE B 1 505 ? 40.96400  18.94300  62.68600 1.000 33.92000 ? 505 ILE B CA  1 
ATOM   7282 C C   . ILE B 1 505 ? 40.80300  18.43500  64.10700 1.000 33.92000 ? 505 ILE B C   1 
ATOM   7283 O O   . ILE B 1 505 ? 41.77900  18.03000  64.74400 1.000 33.92000 ? 505 ILE B O   1 
ATOM   7284 C CB  . ILE B 1 505 ? 40.94200  20.48200  62.63300 1.000 33.92000 ? 505 ILE B CB  1 
ATOM   7285 C CG1 . ILE B 1 505 ? 41.56300  20.99000  61.33200 1.000 33.92000 ? 505 ILE B CG1 1 
ATOM   7286 C CG2 . ILE B 1 505 ? 41.67300  21.07000  63.82900 1.000 33.92000 ? 505 ILE B CG2 1 
ATOM   7287 C CD1 . ILE B 1 505 ? 41.56900  22.49500  61.20200 1.000 33.92000 ? 505 ILE B CD1 1 
ATOM   7288 N N   . ILE B 1 506 ? 39.57100  18.42900  64.62300 1.000 33.07000 ? 506 ILE B N   1 
ATOM   7289 C CA  . ILE B 1 506 ? 39.36700  17.93600  65.98300 1.000 33.07000 ? 506 ILE B CA  1 
ATOM   7290 C C   . ILE B 1 506 ? 39.69600  16.44900  66.07400 1.000 33.07000 ? 506 ILE B C   1 
ATOM   7291 O O   . ILE B 1 506 ? 40.26000  15.98500  67.07500 1.000 33.07000 ? 506 ILE B O   1 
ATOM   7292 C CB  . ILE B 1 506 ? 37.93400  18.23900  66.45600 1.000 33.07000 ? 506 ILE B CB  1 
ATOM   7293 C CG1 . ILE B 1 506 ? 37.73400  19.75200  66.57300 1.000 33.07000 ? 506 ILE B CG1 1 
ATOM   7294 C CG2 . ILE B 1 506 ? 37.65400  17.57100  67.79500 1.000 33.07000 ? 506 ILE B CG2 1 
ATOM   7295 C CD1 . ILE B 1 506 ? 36.39700  20.15600  67.15500 1.000 33.07000 ? 506 ILE B CD1 1 
ATOM   7296 N N   . THR B 1 507 ? 39.40700  15.68500  65.01500 1.000 34.24000 ? 507 THR B N   1 
ATOM   7297 C CA  . THR B 1 507 ? 39.71800  14.25700  65.04400 1.000 34.24000 ? 507 THR B CA  1 
ATOM   7298 C C   . THR B 1 507 ? 41.22500  14.01800  65.06900 1.000 34.24000 ? 507 THR B C   1 
ATOM   7299 O O   . THR B 1 507 ? 41.72900  13.24200  65.89200 1.000 34.24000 ? 507 THR B O   1 
ATOM   7300 C CB  . THR B 1 507 ? 39.08300  13.55300  63.84300 1.000 34.24000 ? 507 THR B CB  1 
ATOM   7301 O OG1 . THR B 1 507 ? 37.65800  13.52300  64.00200 1.000 34.24000 ? 507 THR B OG1 1 
ATOM   7302 C CG2 . THR B 1 507 ? 39.60300  12.13100  63.72300 1.000 34.24000 ? 507 THR B CG2 1 
ATOM   7303 N N   . VAL B 1 508 ? 41.96500  14.68100  64.17500 1.000 35.98000 ? 508 VAL B N   1 
ATOM   7304 C CA  . VAL B 1 508 ? 43.41400  14.50400  64.15800 1.000 35.98000 ? 508 VAL B CA  1 
ATOM   7305 C C   . VAL B 1 508 ? 44.05400  15.07400  65.42300 1.000 35.98000 ? 508 VAL B C   1 
ATOM   7306 O O   . VAL B 1 508 ? 45.09600  14.58000  65.87400 1.000 35.98000 ? 508 VAL B O   1 
ATOM   7307 C CB  . VAL B 1 508 ? 44.01300  15.12500  62.88000 1.000 35.98000 ? 508 VAL B CB  1 
ATOM   7308 C CG1 . VAL B 1 508 ? 45.51800  14.89500  62.82000 1.000 35.98000 ? 508 VAL B CG1 1 
ATOM   7309 C CG2 . VAL B 1 508 ? 43.34500  14.53500  61.64600 1.000 35.98000 ? 508 VAL B CG2 1 
ATOM   7310 N N   . VAL B 1 509 ? 43.44600  16.09800  66.02900 1.000 36.69000 ? 509 VAL B N   1 
ATOM   7311 C CA  . VAL B 1 509 ? 43.97700  16.65000  67.27100 1.000 36.69000 ? 509 VAL B CA  1 
ATOM   7312 C C   . VAL B 1 509 ? 43.79500  15.66500  68.41800 1.000 36.69000 ? 509 VAL B C   1 
ATOM   7313 O O   . VAL B 1 509 ? 44.70100  15.47200  69.23800 1.000 36.69000 ? 509 VAL B O   1 
ATOM   7314 C CB  . VAL B 1 509 ? 43.31500  18.00700  67.57400 1.000 36.69000 ? 509 VAL B CB  1 
ATOM   7315 C CG1 . VAL B 1 509 ? 43.36900  18.31600  69.06400 1.000 36.69000 ? 509 VAL B CG1 1 
ATOM   7316 C CG2 . VAL B 1 509 ? 43.99300  19.11400  66.78400 1.000 36.69000 ? 509 VAL B CG2 1 
ATOM   7317 N N   . LEU B 1 510 ? 42.63500  15.00800  68.48400 1.000 37.59000 ? 510 LEU B N   1 
ATOM   7318 C CA  . LEU B 1 510 ? 42.42600  14.00100  69.51600 1.000 37.59000 ? 510 LEU B CA  1 
ATOM   7319 C C   . LEU B 1 510 ? 43.17100  12.70700  69.22200 1.000 37.59000 ? 510 LEU B C   1 
ATOM   7320 O O   . LEU B 1 510 ? 43.30200  11.86900  70.12200 1.000 37.59000 ? 510 LEU B O   1 
ATOM   7321 C CB  . LEU B 1 510 ? 40.93200  13.73000  69.69400 1.000 37.59000 ? 510 LEU B CB  1 
ATOM   7322 C CG  . LEU B 1 510 ? 40.17200  14.91800  70.29100 1.000 37.59000 ? 510 LEU B CG  1 
ATOM   7323 C CD1 . LEU B 1 510 ? 38.75200  14.53000  70.67100 1.000 37.59000 ? 510 LEU B CD1 1 
ATOM   7324 C CD2 . LEU B 1 510 ? 40.92000  15.49200  71.49000 1.000 37.59000 ? 510 LEU B CD2 1 
ATOM   7325 N N   . ARG B 1 511 ? 43.65500  12.52400  67.99100 1.000 42.79000 ? 511 ARG B N   1 
ATOM   7326 C CA  . ARG B 1 511 ? 44.62200  11.46200  67.73500 1.000 42.79000 ? 511 ARG B CA  1 
ATOM   7327 C C   . ARG B 1 511 ? 45.89700  11.67500  68.54200 1.000 42.79000 ? 511 ARG B C   1 
ATOM   7328 O O   . ARG B 1 511 ? 46.57600  10.70600  68.90300 1.000 42.79000 ? 511 ARG B O   1 
ATOM   7329 C CB  . ARG B 1 511 ? 44.93300  11.39400  66.23800 1.000 42.79000 ? 511 ARG B CB  1 
ATOM   7330 C CG  . ARG B 1 511 ? 45.96100  10.34700  65.83900 1.000 42.79000 ? 511 ARG B CG  1 
ATOM   7331 C CD  . ARG B 1 511 ? 45.47100  8.93600   66.12100 1.000 42.79000 ? 511 ARG B CD  1 
ATOM   7332 N NE  . ARG B 1 511 ? 44.11300  8.72000   65.63800 1.000 42.79000 ? 511 ARG B NE  1 
ATOM   7333 C CZ  . ARG B 1 511 ? 43.06100  8.52500   66.42200 1.000 42.79000 ? 511 ARG B CZ  1 
ATOM   7334 N NH1 . ARG B 1 511 ? 43.18000  8.47600   67.73800 1.000 42.79000 ? 511 ARG B NH1 1 
ATOM   7335 N NH2 . ARG B 1 511 ? 41.86100  8.37000   65.87000 1.000 42.79000 ? 511 ARG B NH2 1 
ATOM   7336 N N   . LYS B 1 512 ? 46.22900  12.92800  68.84300 1.000 42.59000 ? 512 LYS B N   1 
ATOM   7337 C CA  . LYS B 1 512 ? 47.38400  13.25500  69.67100 1.000 42.59000 ? 512 LYS B CA  1 
ATOM   7338 C C   . LYS B 1 512 ? 47.03800  13.13400  71.15300 1.000 42.59000 ? 512 LYS B C   1 
ATOM   7339 O O   . LYS B 1 512 ? 47.62400  12.32800  71.87600 1.000 42.59000 ? 512 LYS B O   1 
ATOM   7340 C CB  . LYS B 1 512 ? 47.88100  14.66900  69.36100 1.000 42.59000 ? 512 LYS B CB  1 
ATOM   7341 C CG  . LYS B 1 512 ? 48.11100  14.94300  67.88200 1.000 42.59000 ? 512 LYS B CG  1 
ATOM   7342 C CD  . LYS B 1 512 ? 49.37300  14.26500  67.37300 1.000 42.59000 ? 512 LYS B CD  1 
ATOM   7343 C CE  . LYS B 1 512 ? 50.61800  14.88500  67.98700 1.000 42.59000 ? 512 LYS B CE  1 
ATOM   7344 N NZ  . LYS B 1 512 ? 51.86700  14.30500  67.42100 1.000 42.59000 ? 512 LYS B NZ  1 
HETATM 7345 C CHA . BLR C 2 .   ? 21.17500  -9.12300  27.86500 1.000 33.73000 ? 601 BLR A CHA 1 
HETATM 7346 N NA  . BLR C 2 .   ? 20.46400  -10.40900 29.97400 1.000 33.73000 ? 601 BLR A NA  1 
HETATM 7347 C C1A . BLR C 2 .   ? 20.35400  -9.37200  29.10000 1.000 33.73000 ? 601 BLR A C1A 1 
HETATM 7348 C C2A . BLR C 2 .   ? 19.31100  -8.56000  29.51500 1.000 33.73000 ? 601 BLR A C2A 1 
HETATM 7349 C C3A . BLR C 2 .   ? 18.77300  -9.12000  30.68200 1.000 33.73000 ? 601 BLR A C3A 1 
HETATM 7350 C C4A . BLR C 2 .   ? 19.50900  -10.27600 30.96700 1.000 33.73000 ? 601 BLR A C4A 1 
HETATM 7351 C CMA . BLR C 2 .   ? 17.62900  -8.52700  31.44000 1.000 33.73000 ? 601 BLR A CMA 1 
HETATM 7352 C CAA . BLR C 2 .   ? 18.81500  -7.32100  28.84300 1.000 33.73000 ? 601 BLR A CAA 1 
HETATM 7353 C CBA . BLR C 2 .   ? 17.62200  -7.68200  27.96300 1.000 33.73000 ? 601 BLR A CBA 1 
HETATM 7354 C CGA . BLR C 2 .   ? 17.12500  -6.62400  26.96800 1.000 33.73000 ? 601 BLR A CGA 1 
HETATM 7355 O O1A . BLR C 2 .   ? 16.31400  -7.03800  26.11300 1.000 33.73000 ? 601 BLR A O1A 1 
HETATM 7356 O O2A . BLR C 2 .   ? 17.55800  -5.46200  27.08100 1.000 33.73000 ? 601 BLR A O2A 1 
HETATM 7357 C CHB . BLR C 2 .   ? 19.23600  -11.11600 32.09300 1.000 33.73000 ? 601 BLR A CHB 1 
HETATM 7358 N NB  . BLR C 2 .   ? 16.79700  -11.52100 32.05700 0.000 33.73000 ? 601 BLR A NB  1 
HETATM 7359 C C1B . BLR C 2 .   ? 18.09600  -11.74200 32.49100 0.000 33.73000 ? 601 BLR A C1B 1 
HETATM 7360 C C2B . BLR C 2 .   ? 18.01300  -12.81900 33.46600 0.000 33.73000 ? 601 BLR A C2B 1 
HETATM 7361 C C3B . BLR C 2 .   ? 16.70500  -13.19300 33.58800 0.000 33.73000 ? 601 BLR A C3B 1 
HETATM 7362 C C4B . BLR C 2 .   ? 15.90900  -12.35500 32.66200 0.000 33.73000 ? 601 BLR A C4B 1 
HETATM 7363 C CMB . BLR C 2 .   ? 19.19100  -13.37500 34.18600 0.000 33.73000 ? 601 BLR A CMB 1 
HETATM 7364 O OB  . BLR C 2 .   ? 14.70100  -12.36000 32.46400 0.000 33.73000 ? 601 BLR A OB  1 
HETATM 7365 C CAB . BLR C 2 .   ? 16.17400  -14.22800 34.45100 0.000 33.73000 ? 601 BLR A CAB 1 
HETATM 7366 C CBB . BLR C 2 .   ? 14.89000  -14.55200 34.64400 0.000 33.73000 ? 601 BLR A CBB 1 
HETATM 7367 N NC  . BLR C 2 .   ? 24.39400  -13.19200 29.85300 1.000 33.73000 ? 601 BLR A NC  1 
HETATM 7368 C C1C . BLR C 2 .   ? 24.64200  -14.37500 30.50400 1.000 33.73000 ? 601 BLR A C1C 1 
HETATM 7369 C C2C . BLR C 2 .   ? 25.76600  -15.01700 29.80100 1.000 33.73000 ? 601 BLR A C2C 1 
HETATM 7370 C C3C . BLR C 2 .   ? 26.12900  -14.20200 28.77600 1.000 33.73000 ? 601 BLR A C3C 1 
HETATM 7371 C C4C . BLR C 2 .   ? 25.26600  -13.02100 28.78600 1.000 33.73000 ? 601 BLR A C4C 1 
HETATM 7372 C CMC . BLR C 2 .   ? 26.31000  -16.33000 30.24000 1.000 33.73000 ? 601 BLR A CMC 1 
HETATM 7373 O OC  . BLR C 2 .   ? 24.03200  -14.78600 31.47600 1.000 33.73000 ? 601 BLR A OC  1 
HETATM 7374 C CAC . BLR C 2 .   ? 27.18500  -14.40500 27.79300 1.000 33.73000 ? 601 BLR A CAC 1 
HETATM 7375 C CBC . BLR C 2 .   ? 28.48100  -14.55500 28.08500 1.000 33.73000 ? 601 BLR A CBC 1 
HETATM 7376 C CHD . BLR C 2 .   ? 25.32300  -11.98100 27.92500 1.000 33.73000 ? 601 BLR A CHD 1 
HETATM 7377 N ND  . BLR C 2 .   ? 23.11700  -10.77600 28.11300 1.000 33.73000 ? 601 BLR A ND  1 
HETATM 7378 C C1D . BLR C 2 .   ? 24.40700  -10.92000 27.63200 1.000 33.73000 ? 601 BLR A C1D 1 
HETATM 7379 C C2D . BLR C 2 .   ? 24.65300  -9.84400  26.79100 1.000 33.73000 ? 601 BLR A C2D 1 
HETATM 7380 C C3D . BLR C 2 .   ? 23.49200  -9.04700  26.78000 1.000 33.73000 ? 601 BLR A C3D 1 
HETATM 7381 C C4D . BLR C 2 .   ? 22.56000  -9.63900  27.60700 1.000 33.73000 ? 601 BLR A C4D 1 
HETATM 7382 C CMD . BLR C 2 .   ? 25.90100  -9.55100  26.03100 1.000 33.73000 ? 601 BLR A CMD 1 
HETATM 7383 C CAD . BLR C 2 .   ? 23.28700  -7.78500  26.00900 1.000 33.73000 ? 601 BLR A CAD 1 
HETATM 7384 C CBD . BLR C 2 .   ? 22.88200  -8.06800  24.54800 1.000 33.73000 ? 601 BLR A CBD 1 
HETATM 7385 C CGD . BLR C 2 .   ? 22.31500  -6.86800  23.78800 1.000 33.73000 ? 601 BLR A CGD 1 
HETATM 7386 O O1D . BLR C 2 .   ? 22.65800  -6.80500  22.56000 1.000 33.73000 ? 601 BLR A O1D 1 
HETATM 7387 O O2D . BLR C 2 .   ? 21.58900  -6.05600  24.36300 1.000 33.73000 ? 601 BLR A O2D 1 
HETATM 7388 C CHA . BLR D 2 .   ? 5.15600   39.50700  33.33000 1.000 39.36000 ? 601 BLR B CHA 1 
HETATM 7389 N NA  . BLR D 2 .   ? 6.43500   41.51600  32.40300 1.000 39.36000 ? 601 BLR B NA  1 
HETATM 7390 C C1A . BLR D 2 .   ? 6.02500   40.22000  32.33700 1.000 39.36000 ? 601 BLR B C1A 1 
HETATM 7391 C C2A . BLR D 2 .   ? 6.58400   39.64000  31.21900 1.000 39.36000 ? 601 BLR B C2A 1 
HETATM 7392 C C3A . BLR D 2 .   ? 7.33600   40.62100  30.57400 1.000 39.36000 ? 601 BLR B C3A 1 
HETATM 7393 C C4A . BLR D 2 .   ? 7.24700   41.81000  31.31900 1.000 39.36000 ? 601 BLR B C4A 1 
HETATM 7394 C CMA . BLR D 2 .   ? 8.06300   40.30100  29.31300 1.000 39.36000 ? 601 BLR B CMA 1 
HETATM 7395 C CAA . BLR D 2 .   ? 6.41800   38.23600  30.73400 1.000 39.36000 ? 601 BLR B CAA 1 
HETATM 7396 C CBA . BLR D 2 .   ? 5.10300   38.08500  29.98500 1.000 39.36000 ? 601 BLR B CBA 1 
HETATM 7397 C CGA . BLR D 2 .   ? 5.22100   37.48200  28.57800 1.000 39.36000 ? 601 BLR B CGA 1 
HETATM 7398 O O1A . BLR D 2 .   ? 4.73300   38.15200  27.64400 1.000 39.36000 ? 601 BLR B O1A 1 
HETATM 7399 O O2A . BLR D 2 .   ? 5.79200   36.38300  28.48100 1.000 39.36000 ? 601 BLR B O2A 1 
HETATM 7400 C CHB . BLR D 2 .   ? 7.89500   43.04300  30.97900 1.000 39.36000 ? 601 BLR B CHB 1 
HETATM 7401 N NB  . BLR D 2 .   ? 8.13300   43.28100  28.52000 0.000 39.36000 ? 601 BLR B NB  1 
HETATM 7402 C C1B . BLR D 2 .   ? 8.48900   43.51900  29.84900 0.000 39.36000 ? 601 BLR B C1B 1 
HETATM 7403 C C2B . BLR D 2 .   ? 9.67400   44.38000  29.80900 0.000 39.36000 ? 601 BLR B C2B 1 
HETATM 7404 C C3B . BLR D 2 .   ? 9.95700   44.62000  28.50400 0.000 39.36000 ? 601 BLR B C3B 1 
HETATM 7405 C C4B . BLR D 2 .   ? 8.97000   43.90900  27.64200 0.000 39.36000 ? 601 BLR B C4B 1 
HETATM 7406 C CMB . BLR D 2 .   ? 10.44200  44.97800  30.95200 0.000 39.36000 ? 601 BLR B CMB 1 
HETATM 7407 O OB  . BLR D 2 .   ? 8.88700   43.87200  26.41300 0.000 39.36000 ? 601 BLR B OB  1 
HETATM 7408 C CAB . BLR D 2 .   ? 11.05500  45.46200  28.08800 0.000 39.36000 ? 601 BLR B CAB 1 
HETATM 7409 C CBB . BLR D 2 .   ? 10.95900  46.73900  27.71600 0.000 39.36000 ? 601 BLR B CBB 1 
HETATM 7410 N NC  . BLR D 2 .   ? 3.99200   44.67200  35.38200 1.000 39.36000 ? 601 BLR B NC  1 
HETATM 7411 C C1C . BLR D 2 .   ? 4.35100   45.87500  35.93800 1.000 39.36000 ? 601 BLR B C1C 1 
HETATM 7412 C C2C . BLR D 2 .   ? 3.61000   45.98500  37.21200 1.000 39.36000 ? 601 BLR B C2C 1 
HETATM 7413 C C3C . BLR D 2 .   ? 2.85700   44.86700  37.35100 1.000 39.36000 ? 601 BLR B C3C 1 
HETATM 7414 C C4C . BLR D 2 .   ? 3.08400   44.00600  36.19700 1.000 39.36000 ? 601 BLR B C4C 1 
HETATM 7415 C CMC . BLR D 2 .   ? 3.73000   47.15700  38.11600 1.000 39.36000 ? 601 BLR B CMC 1 
HETATM 7416 O OC  . BLR D 2 .   ? 5.13600   46.66500  35.43900 1.000 39.36000 ? 601 BLR B OC  1 
HETATM 7417 C CAC . BLR D 2 .   ? 1.95600   44.50300  38.43900 1.000 39.36000 ? 601 BLR B CAC 1 
HETATM 7418 C CBC . BLR D 2 .   ? 0.79400   45.09500  38.72000 1.000 39.36000 ? 601 BLR B CBC 1 
HETATM 7419 C CHD . BLR D 2 .   ? 2.49300   42.81100  36.00100 1.000 39.36000 ? 601 BLR B CHD 1 
HETATM 7420 N ND  . BLR D 2 .   ? 4.08200   41.36500  34.68800 1.000 39.36000 ? 601 BLR B ND  1 
HETATM 7421 C C1D . BLR D 2 .   ? 2.85000   41.65200  35.24200 1.000 39.36000 ? 601 BLR B C1D 1 
HETATM 7422 C C2D . BLR D 2 .   ? 2.00800   40.59200  34.93000 1.000 39.36000 ? 601 BLR B C2D 1 
HETATM 7423 C C3D . BLR D 2 .   ? 2.74700   39.66700  34.17600 1.000 39.36000 ? 601 BLR B C3D 1 
HETATM 7424 C C4D . BLR D 2 .   ? 4.02000   40.16900  34.03800 1.000 39.36000 ? 601 BLR B C4D 1 
HETATM 7425 C CMD . BLR D 2 .   ? 0.57800   40.39900  35.29000 1.000 39.36000 ? 601 BLR B CMD 1 
HETATM 7426 C CAD . BLR D 2 .   ? 2.26700   38.36800  33.61900 1.000 39.36000 ? 601 BLR B CAD 1 
HETATM 7427 C CBD . BLR D 2 .   ? 1.37400   38.47400  32.36700 1.000 39.36000 ? 601 BLR B CBD 1 
HETATM 7428 C CGD . BLR D 2 .   ? 0.72500   37.14800  31.95600 1.000 39.36000 ? 601 BLR B CGD 1 
HETATM 7429 O O1D . BLR D 2 .   ? -0.43300  36.93600  32.45100 1.000 39.36000 ? 601 BLR B O1D 1 
HETATM 7430 O O2D . BLR D 2 .   ? 1.31500   36.37800  31.19700 1.000 39.36000 ? 601 BLR B O2D 1 
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